{"protein": "MTKRLTPQEKLSRKPASRACTFCHQKHLQCSNERPCKNCVKRNIADQCQDITRKRVKYLTGANSKAVAAATTPEATTTTPKRKQKRSVKGSPSISFPSSSISPINTSTFDTNGHPNGHPNDLLRQSLEASQAGQAQAPSLLEIQGPFPQMQTLQPTHTVASETSSSYSQVQPQHHPESSVPPSAPPESVDQLQQLMMHDSAYFNTNNVALNPTNVLEADPFDGHTNTMLNTTTDVLNKLLNDHYEIDNILQPPDDALLVDQQQSSSEATGTSASKAVPMGPSHSNTHFSSNYLNEEYLMLGDILLQSKPTSPSPSNTSASEYNMLSPSYTQNIDFDNIHLSKRKVVQKLKDSRPFISLGFPKDSSLSLDNLNNMAHQTDNLLDNNVSSRGNNNTSNQKLQSAIASKTSKTNPIINFATKYSTEYVSPLSTHQIYQTVSDIYSKDVLNYEYPNSYHALTHFLKTRFSGNNLPHEEKARKRQNLLVILKLIASYRPTFISAHKSLLKPQDLLFLEMSFQRCLIDYEKLSQLNSSPTIIWRRTGEIVSITDDLLSLLGYKLLDILSKRTFIMEIMYDDESIVKYFQLFKSVAVGNLHSSINTKVKLIKNGGAVPGGGTSNGKYNYNNNYNHNYSHNNNNNNNSNNSNNNGMSTGAGNSGDGDGLENNVGTNSYIEFCSVWTVKRDLFDIPMLIIGQFLPILPAGDGVRMY", "text": "FUNCTION: Transcription factor which regulates nonfermentable carbon utilization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ERT1/acuK family."}
{"protein": "MAVHNLKDLLAEGVSGRGVLVRSDLNVPLDSDGEQGRITDPGRITASVPTLSALVEAGAKVVVAAHLGRPKNGPDPALSLAPVAAALGEQLGRHVQLASDVVGTDALARAEGLTDGDVLLLENIRFDARETSKDDAERLALARQLAELVGPTGAFVSDGFGVVHRKQASVYDVATLLPHYAGTLVAEEIAVLEQLTGSTKRPYAVVLGGSKVSDKLGVIESLATKADSIVIGGGMCFTFLAAQGFSVGKSLLETEMVDTCRRLLDTYVDVLRLPVDIVAADRFAADAAPQTVPADAIPDDLMGLDIGPGSVKRFTALLSNAETIFWNGPMGVFEFPAFAAGTKGLAEAIAAATGKGAFSVVGGGDSAAAVRALGIPESGFSHISTGGGASLEYLEGKALPGIEVLGRPQPTGGAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MLKNINPTQTQAWKALTAHFESAQDMDLKELFAQDAARFDKYSARFGSDILVDYSKNLINEETLKHLFALANETELKSAIEAMFSGEAINKTEDRAVLHTALRNRSNTPVMVGGEDVMPAVNAVLEKIKSFTERVIGGEWKGYTGKAITDIVNIGIGGSDLGPYMVTEALAPYKNHLNLHFVSNVDGTHIVETLKKVDPETTLFLIASKTFTTQETMTNAHSARDWFLATAGDQAHVAKHFAALSTNAPAVSEFGIDTDNMFEFWDWVGGRYSLWSAIGLSIALAVGYDNFIELLDGAHEMDNHFVSTDLESNIPVILALIGIWYNNFHGAESEAILPYDQYMHRFAAYFQQGNMESNGKYVDREGNAVTYQTGPIIWGEPGTNGQHAFYQLIHQGTKLIPCDFIAPAISHNPASDHHQKLMSNFFAQTEALAFGKSAETVKAEFAKAGKSEEEMASLVPFKVFEGNRPTNSILVKQITPRTLGNLIAMYEHKIFVQGVIWNIFSFDQWGVELGKQLANQILPELADESEINSHDSSTNGLINAFKAFKA", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MTQITLLTPDDWHLHFRDGDMLKETVPATARLFQRAIVMPNLLPPVTDAKMVIEYRERILAARPEGSDFEPLMTLFLTNDTTEQDIIDAKAAGVVAAKLYPAGATTNSDAAVKALDALFPIFEKMAEVGMLLLVHGEVTESHIDIFDREALFIERNLRRIVDAFPTLKVVFEHITTKEAADFVMSASDNVAATITPQHLLLNRNDLLVGGVRPHNFCLPVLKRNIHQEALRAAIATGSSKFFLGTDSAPHEKHRKESACGCAGCYSAWSALELYAQVFDDLGIIDKLEGFASIHGPDFYGLPRNTSTVTLVKEKWTVPSEIILPNGNPIVPFFAGEEVSWKVKS", "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": "MKLCATFLLVLVTLPLVTGEKSSERSLSGAILRGVRRTCSRRGHRCIRDSQCCGGMCCQGNRCFVAIRRCFHLPF", "text": "FUNCTION: Both natural (L-Leu form) and synthetic (D-Leu from) peptides equally cause sensitivity to touch and body tremor. Neither L-Leu form nor D-Leu form is active on nerve-muscle preparation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I1 superfamily."}
{"protein": "MTWNPHANRFKTFLLLVGMSALIVFVGSLFGRSIMALAVLFAVGMNVYVYFNSDKLALKAMHAQPVSELQAPVMYRIVRELSNAAHQPMPRLYISDTANPNAFATGRNPRNSAVCCTTGILQILNERELRAVLGHELSHVYNRDILISCVAGAMASVITALANIALFAGMFGGNREGTNPFALLLVSFLGPIAATVVRLAVSRSREYQADQSGAELTGDPLALASALRKISGGVEAAPLPPQPQLADQAHLMIASPFRSGEKIGKLFSTHPPMADRIRRLEEMAGRGPGLY", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
{"protein": "VLSPEDKNNVKAAWSKVGGQAGDYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVGEALTTAVNHMDDLPGALSTLSDLHAYKLRVDPVNFKLLSHCLLVTLACHNPGEFTPAVHASLDKFLASVSTVLTSKYR", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
{"protein": "MVKTQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADATLLTDRAAMLGLPLTLRPYSPNSPAQPQTTGTLTLLPVALRESVTAGQLAIENGHYVVETLARACDGCLNGEFAALITGPVHKGVINDAGIPFTGHTEFFEERSQAKKVVMMLATEELRVALATTHLPLRDIADAITPALLHEVIAILHHDLRTKFGIAEPRILVCGLNPHAGEGGHMGTEEIDTIIPVLDELRAQGMKLNGPLPADTLFQPKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTALELAGRGEADVGSFITALNLAIKMIVNTQ", "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": "MLAIRLSRGGSRKRPFYHVVATDSRNARDSNFIERLGFFNPQARGQEEELRLDLERIEYWQSQGGQISDRVKSLIKQYKKSANK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MTETPLLSVRGLAKHYQTRSATLKILDNVSFDIARGEVVGLVGESGSGKTTIGRSVLRLIEPTAGQIMFDGADVATLSAREMRRQRRRMQYIFQDPFASLSPRMTIGEILMEGLNIQGIGTKAERLERARKALEQVELPPDTINRYAHEFSGGQRQRIGIARALTLEPDFIVADEPVSALDVSIQAQVVNLLRDLQQRLGLTMLFISHDLAVVEYICDRVIVLYLGRIMEIASSEDLYARPQHPYTRALLSAIPSPDPDARTERQILRGDIPSPANPPSGCVFRTRCPMAIDACATTVPQLREVRPGHFKACIRDNI", "text": "FUNCTION: Probably part of an ABC transporter complex that could be involved in peptide import. Probably 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": "MRSAKLKFEKRRSRIRHKISKTSNRVRLSIFKSGRHIYAQIIDDSKSITIAAASTLDEKIKKLKKSHCNIENAIKVGEEIAKKADSAGIKDVVFDRGGYKYHGVVKALADAAREKIKF", "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": "MTQVVNVVGAGLAGSEAAYQLAQRGVKVNLIEMRPVKQTPAHHTDKFAELVCSNSLRGNALTNAVGVLKEEMRQLDSLIISAADKARVPAGGALAVDRHDFAGYVTETLKNHPNITVLNEEINSIPEGYTIIATGPLTTDKLANEIVEATGKDQLYFYDAAAPIIEKDSIDMNKVYLKSRYDKGEAAYLNCPMTEDEFNTFYDALMEAEVAPVNEFEKEKYFEGCMPFEVMAERGRKTLLFGPMKPVGLEDPKTGERPYAVVQLRQDDAAGTLYNIVGFQTHLKWGAQKDVIRLIPGLENVEIVRYGVMHRNTFINSPDVLTETYELKGREELYFAGQMTGVEGYVESAASGLVAGINVAHKMLNKGEVIFPRETMIGSMAYYISHAKNEKNFQPMNANFGLLTTLEKKVKDKKLRYEKLADRALTYLDNYKQTL", "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": "MRSKPRIALIAHDRKKDDIVAFAGRHRDFLAQCDLLATGTTGGRIAAETGLPVARMLSGPWGGDLQIGAQLAEGRVTAVVFLRDPMTPQPHEPDINALVRACDVHNVPCATNLATAELVVVELARICFEEDQAAADDAAP", "text": "FUNCTION: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. SIMILARITY: Belongs to the methylglyoxal synthase family."}
{"protein": "MVNFSRKRPAVSSLFSQQQAIEQSLNWQALQPDLVIQDFPLEPVNFWALQPNATQGIDLFLRHPTRSLLMMKVGEPVEYAELLQNFISQNHHKVRSIFGVNYVIEQGDSFSFPHVYTEPAKSLDDNFASQGEALSALYCDQFQLFGSFRIHPRSQDIQLVPGLVHKANGGVLILSAATLLSQFDLWGRLKQILQTQTFDWYSAHPFKNLPCDIPSYALNLKVIVLGNRTELATLAELEENLYSFADYAEIESYISVAEVEEQKTWAGYVQQMAQEQNIELDFLALNKLYQLLVRESENRFLINASPLKLKEILQDASTFTEKTALSAVDFEGIFQQKLAQYGFLKEQTYADILNEQVYVETQGEIVGQINGLSVIEYPGTPVCFGEPSRISCIVQFGDGEVIDVERKNELAGNIHGKGMMIAQACLSNILDLPSQLPFSASLVFEQSYGEIDGDSASLAIFCVLVSALADLPLPQHIAITGSIDQFGLVHSVGGVNDKIEGFFTICQRRGLTGKQGVIIPMTTIQQLSLSDDVKSAVKNGEFFIYPVEDIYQACELLFGRDLLDENKDYTEKTESLSRLIQRRIEGRADSERKSFWHFFRS", "text": "SIMILARITY: Belongs to the peptidase S16 family."}
{"protein": "MLKPLSQLVCALPLVVAASSYADDSAALKDKLAKLDNLKANFSQQVTDVNNKVIQQGTGTFALAVPNQFYWHLTQPDESLIVADGRDVWIYNPFAEEVSVLDFNQAINASPIALLVHRDDATWQAYQVKRQDDCYQITPKAVDASVTGVEVCFKDEQLEVMKLTDQQGNLSVFNLSAQAPLKDADASLFQFTVPEGVDIDDQRLKALD", "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": "MKCCRIMFVLLGLWFVFGLSVPGGRTEAASLRANDAPIVLLHGFTGWGREEMFGFKYWGGVRGDIEQWLNDNGYRTYTLAVGPLSSNWDRACEAYAQLVGGTVDYGAAHAAKHGHARFGRTYPGLLPELKRGGRIHIIAHSQGGQTARMLVSLLENGSQEEREYAKAHNVSLSPLFEGGHHFVLSVTTIATPHDGTTLVNMVDFTDRFFDLQKAVLEAAAVASNVPYTSQVYDFKLDQWGLRRQPGESFDHYFERLKRSPVWTSTDTARYDLSVSGAEKLNQWVQASPNTYYLSFSTERTYRGALTGNHYPELGMNAFSAVVCAPFLGSYRNPTLGIDDRWLENDGIVNTVSMNGPKRGSSDRIVPYDGTLKKGVWNDMGTYNVDHLEIIGVDPNPSFDIRAFYLRLAEQLASLRP", "text": "FUNCTION: Triacylglycerol hydrolase that shows hydrolysis preference towards some of the natural oils such as olive, sunflower and corn oils. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily."}
{"protein": "MSITVHIQYAVPKASVPLQADFLRWVKAALVNQSKAGEITIRVASESEAAQLNWRYRHKEGATNILSFPFEVPSCVSLDVPLLGDLVICAPVVAREALEQTKKEQAHWAHLVVHGVLHLLGFDHQQEVEAQQMESLEVTILESLGYPDPYESV", "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": "LTAVLKADAYGXGIGL", "text": "SIMILARITY: Belongs to the alanine racemase family."}
{"protein": "MKGMRSNIPRALNAGAQIACVDNTGAKVVEIISVKKYRGVKNRMPCAGIGDMCVVSVKKGTPEMRKQVLLAVVVRQKQEFRRPDGLHVSFEDNAMVITDEEGIPKGTDIKGPVAREVAERFPKIGTTASIIV", "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": "MVSIAFYGGIPGGISTPITQQSEKSKCEENTIFQPYCYNNNSKNSMAESKEARDQEMNLKEESKEEKRRNDWWKIGMFLLCLAGTTGGILWWYEGLPQQHYIGLVAIGGRLNGSGQSNAIECWGSFPGCRPFQNYFSYETNRSMHMDNDTATLLEAYHREITFIYKSSCTDSDHCQEYQCKQVNLNSSDPSNSVRVEDVTNTTEYWGFKWLECNQTENFKTILVPENEMVKINDNDTWIPKGCNETWARVKRCPIDILYGIHPIRLSVQPPFFLVQEKGTADTSRIGNCGPTIFLGVLEDNKGVVRGNGTACKVSDLNINRKDYTGIYQVPIFYTCNFTNITSCNNESIISVIMYETNQVQYLLCNNNNNSNNYNCVVQSFGVIGQAHLELPRPNKRIRNQSFNQYNCSINNKTELETWKLVNTSGITPLPISSEANTGLIRHKRDFGISAIVAAIVAATAIAASATMSYVALTEVNKIMEVQNHTFEVENSTLNGMDLIEQQIKILYAMILQTHADVQLLKEKQQVEETFNLIGCIERTHVFCHTGHPWNMSWGHLNESTQWDDWVSKMEDLNQEILTTLHGARNNLAQSMITFNTPDSIAQFGKDLWSHIGNWIPGLGASIIKYIVMFLLIYLLLTSSPKILRALWKVTSGAGSSGSRYLKKKFYHKHASREDTWDQAQHNIHLAGVTGGSGNKYCKQKYSRNDWNGESEEYNRRPKSWVKSIETFGESYISEKTKGEISQPGAAINEHKNGSGGNNPHQGSLDLEIRSEGGNIYDCCIKAQEGTLAIPCCGFPLWLFWGLVIIVGRIAGYGLRGFAVIIRICIRGLNLIFEIIRKMLDYIGRALNPGTSHVSMPQYV", "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": "MAAMKTTPGLVNFFIFNSTYGPREGEEHEKIILYIPTEEDIDRKIKTIGLCEALVKFTETFAPDKPCESLHTQKSRQIFYQPEPDFWMIMTISIPFSEKIAKDGKNTIEYHYDDVLDNVLDAVLKQSYKMFKLFNGPFNYLSETYGREALKKRSEYFFLSYLQTLNFSSFDLLDIFAGIQFLPLDKNTFLKIQSFVNLIEHTFSQIKYTAFLYSDKLVWSGLEQEDMRILYKYLVTSLFPATIDSELADRSSQGYVVIQPKSHHGRFVTGPPDLKDIPTPRKPPRIFVNTDTEQEELLLICYKALDATICLLVSAPFPTLDFFKKLDMFIGPQLTTLANVICEQSSKKSLSSDQQYRYIYFNHMNLAQKSTIHSKKASVAGVSPEIMRLLGDISADFNSFQEDGETYVKTMSDCWVVGRKSDQREFFVILNQKSANLIEINEEVKKLSSCHFNNIFFMD", "text": "SIMILARITY: Belongs to the CCZ1 family."}
{"protein": "MEALVYTFLLIGTLGIIFFAIFFREPPRMVK", "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": "MRHRYSGRRLNRTSAHRKAMFRNMAVSLIEHEMINTTLPKAKEFRRVAEPLITLAKEDSVANRRLVFSRLRDRKAVTKLFNELGPRYQARPGGYLRILKRGFRAGDNAPMAIVELLERPLPDSQEE", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MITNTAAYQFAPIHDPQQLADSVLERAQQRALKGSVLVAEEGINLFLAGDAEQIASFYAWLHADARFAQMRVKYSHSAEQPFARLKVKVKPEIISFRRDDASPLQGRAPSVAPAVLRKWMQQGHDDHGRPLVLLDTRNAQEVAYGTFQGALTLPIDKFTELPEALQPHRAALADATVVSFCTGGIRCEKAALWMHAEGMDNVLQLEGGILGYFEDVGGEGYDGRCFVFDERVALDAELRPLVDGAACADAGKI", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family."}
{"protein": "MNSFRGAFLIWAVATWAETDTSWGATDEPGFQNCKNALKLPVLPVLPGGGWDNLRNVDTGRVMELAYSHCRTTEDGQYIVPDEIFTIPQKQSNLEMNSKILESWVNYQSSTSNSINMELSLFSKVNGKFSLEFQRIKTLQVKDQAVTTQVQVRNLVYTVKINPDAELSLGFKKALMDISEQLENNQTRMATYLAELLVLNYGTHVITSVDAGAALIQEDHIRSSFLQDSQSSRSAVTASAGITFLNIVNFKFEENYTSQNTFTKSYLSNRTNSRVQSFGGLPFYPGITLQAWQQGVSNHLVAMDRAGLPLYFFINPERLPDLPGPLVRKLSKTVEAAVRRYYAVNTYPGCTDLSSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQFSGNEVVQLCQNLEQKNPLTGSVSCPSGYSPVQLLTQTHEEGYNHLECSRKCTLYIFCKTVCEDVFRVARAEFRAFWCAASGQVSENSGLLFGGLFSGKSINPLTNAQSCPAGYFQLKLFENLKVCASLDYELGYRFSIPFGGFFSCAAGNPLVDSATSKDLGAPSLRKCPGGFSQHLALISDGCQVSYCVKAGLFTGGSLPPVRLPPYTRPPLMSQVATNTVLVTNHETASSWIKDPQTHQWRLGEPLELRRAMRVVHGDGEGLSGGAAAGLTLGVTIALAGVVALAIYGARKSRKKGYQALQDEKQSLAAGAAVNGDALDQEQAQNPA", "text": "FUNCTION: Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (By similarity). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (By similarity). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (By similarity). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (By similarity). Required for the antibacterial activity of reactive oxygen species and nitric oxide (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I membrane protein Note=Bacterial infection induces translocation of the cytoplasmic vesicles to bacterium-containing phagocytic vesicles and fusing of the vesicles. SIMILARITY: Belongs to the MPEG1 family."}
{"protein": "MDLPSHHSRLLRQLDEQRRRNLFCDCHIMIDGHTFRAHRNVLYASSGYFKMLLSQSSGNVGQPTTATFDVFSADTFTAILDFMYSGKLNLSGQNVIEIMSAASYLQMTEVIGVCKMFIKSSLDINEKDRDGFLDISDKETGQQTGQCGLYSTGWGMGRYHCNQPEGDIAAYLETSSCTPYGFCSRTDEHPSSQNSISTATMKMLDRHNRIPQIPSSTCSPEEHLRECRILESDDTGCHIEVELPQGEETEAFLNCQTVVQPRSRRRHSLNRATKADEVYAKIMGIKGCLGEDNLPSLHFKCPFCTHTVKRKADLKRHLLCHTGERPYPCQACGKRFTRLEHVRSHYRTIHEAGKPICRWCKRHVTEDSGQVVQEGTRRFRLCNKCVAEVGVGSFPNEVDDDEPTIILSGDEDKEPTWNFHDGIQTSDPEIIEDVSSDVVIHKVDDSDDEIKPIIC", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTTLDSNNNTGGVITYIGSSGSSPNRTSPESLYSDSSNGSFQSLTQGCPTYFPPSPTGSLTQDPARSFGSIPPSLGDDGSPSSSSSSSSSSSSSFYNGSPPGGLQVALEDSNRVSPSKSTSNITKLNGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKRCLKNENCSIVRINRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLAEMQSAMNLANNQLSSQCPLETPPTQHPTPGPMGPSPPPAPAPSPLVGFSQFPQQLTPPRSPSPEPTVEDVISQVARAHREIFTYAHDKLGTSPGNFNANHASGNRPATTPHRWESQGCPPANDNIMAAQRHNEALNSLRQASSSYPPPWPPGAAHHSCHQPNSNGHRLCPTHVYPAPEGEAPVNSPRQGNSKNILLACPMNMYPHGRSGRTVQEIWEDFSMSFTPAVREVVEFAKHIPGFRDLSQHDQVTLLKAGTFEVLMVRFASLFNVKDQTVMFLSRTTYSLQELGAMGMGDLLNAMFDFSEKLNSLALTEEELGLFTAVVLVSADRSGMENSASVEQLQETLLRALRALVLKNRPSETSRFTKLLLKLPDLRTLNNMHSEKLLSFRVDAQ", "text": "FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC1 and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha- cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose- induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner (By similarity). Represses the transcription of CYP2B10, CYP4A10 and CYP4A14 (By similarity). Represses the transcription of CES2 (By similarity). Represses and regulates the circadian expression of TSHB in a NCOR1-dependent manner (By similarity). Negatively regulates the protein stability of NR3C1 and influences the time-dependent subcellular distribution of NR3C1, thereby affecting its transcriptional regulatory activity (By similarity). Plays a critical role in the circadian control of neutrophilic inflammation in the lung; under resting, non-stress conditions, acts as a rhythmic repressor to limit inflammatory activity whereas in the presence of inflammatory triggers undergoes ubiquitin-mediated degradation thereby relieving inhibition of the inflammatory response (By similarity). Plays a key role in the circadian regulation of microglial activation and neuroinflammation; suppresses microglial activation through the NF- kappaB pathway in the central nervous system (By similarity). Plays a role in the regulation of the diurnal rhythms of lipid and protein metabolism in the skeletal muscle via transcriptional repression of genes controlling lipid and amino acid metabolism in the muscle (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, dendrite Cell projection, dendritic spine Note=Localizes to the cytoplasm, dendrites and dendritic spine in the presence of OPHN1. Localizes predominantly to the nucleus at ZT8 whereas it is cytoplasmic at ZT20. Phosphorylation by CSNK1E enhances its cytoplasmic localization. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MKRKLLTTSIALSLAMLATPSYSVDFSGYFRSGVGVSNHGKQQTADKSYVGRLGNEDDTYGEIQLGQQLYNENGKTFYFDSMISMFSNSSNDNETTKNDDAEFGLRQLNLQAKGFVPGLPDATVWAGKRYYQRHDLHIIDTKYWNISGAGAGIENVKAGEGAFSFAWIRADAENMDVDCGNSLNSQECSSREDTYNDLNINYLDARYAGWKPWDGAWTEFGISYAMPNEADTQKNIFLAEGQKFDPKNSMMITGELSHYFSGLKSNQKLVLQYADKGLAHNMVDQGGGWYDVWSINDSAKGYRVIQAGDLPITDHISLSHVLTYGKADEISRWRDSTELLSAVGRGQYAWTKNQKTYLEAGTYQKKDSWKAGTETKYSGQKYTLAHAFSADIPMLTRPELRFFVSYLDGGNENRNRFNDDRSNTVNFGIQAEAWW", "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": "MANYFNTLNLRQQLAQLGKCRFMQRAEFADGCDVLKGKKVVIVGCGAQGLNQGLNMRDSGLDISYTLRKAAITEKRASWQKATDNGFAVGTYEELIPTADLVLNLTPDKQHSDVVKTVMPLMKQGAALGYSHGFNVVEEGQQIRADITVVMVAPKCPGTEVREEYKRGFGVPTLLAVHPENDPKGVGMAIAKAWASATGGDRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCYDKLVAEGTDPAYAGKLIQFGWETITEALKQGGISLMMDRLSNPAKLRAFELSEQLRTLMRPLFEKHMDDIIAGEFSRGMMADWAEDDAKLFGWREETGKSAFENALAFAGKIAEQEYFDNGVVMVAMVKAGVELAFETMVASGIYEESAYYESLHELPLIANTVARKRLYEMNVVISDTAEYGNYLFANAAVPLLREHFMPTLKAGDLGASKAEGQNVDNLALLAANEATRNHPIEKIGQVLRGYMKDMKRIAVGG", "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": "MNKSEQLFEQAQKIIPGGVNSPVRAFNGVGGTPCFIKRAQGAYIYDADDKAYIDYVGSWGPMILGHNHPAILEAVITTAKNGLSFGAPTEIEITMAEKVRELVPSMESLRMVSSGTEATMSAIRLARGYTGRDKILKFEGCYHGHADALLVKAGSGALTLGVPNSPGIPEDFAKHTLTVSYNNIDEVKEIFAKYADEIACIIVEPVAGNMNCIPPVEGFLEGLRDVCDQYSSVLIFDEVMTGFRVALGGAQAHYNIKPDLTTLGKVIGGGMPVGAFGGKQEIMDYIAPVGPVYQAGTLSGNPIAMAAGLASLTELAQGNKHQQLSSATEKLAMGLKAAAERNGVSLSVNYVGAMFGFFFTEDKNPITTYEQATQCDGEMFKRFFHLMLDEGVYLAPSSYETGFLSTSHTDDIIEKTLVAADKCFAQL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
{"protein": "MEKVLVFGHKNPDTDAICSAIAYAELKKELGMNAEPVRLGEISGETQFALDYFKVEGPRFVETVASEVDNVILVDHNERQQSANDIESVRVLEVIDHHRIANFETSDPIYYRCEPVGCTATILNKMYKENGVTIRKEVAGLMLSAIISDSLLFKSPTCTEQDVAAARELAQIAGVDADNYGLEMLKAGADLSGKTMEQLISLDAKEFQMGNAKVEIAQVNAVDTNDVLVHQAELEKVISAVVEEKGLDLFLFVVTDILTNDSVGLAIGKAANVVEKAYNVSLENNTATLKGVVSRKKQIVPVLTEAFQA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase class C family."}
{"protein": "MTQLASSYDPSSFESRLYAQWESAGHFKPSGSGEPYTVLLPPPNVTGTLHMGHAFQQTLMDALVRYHRMRGYDTLWQVGTDHAGIATEMVVSRNLALEGKGETRDTLGREGFIAKVWEWKAQSGDTIERQMRRLGTSSDWSRSTFTMDPQPSAAVTEAFVRWYEQGLIYRGQRLVNWDPVLKTAISDLEVENVEEDGFLWSIRYPLADGVTYEHVEHDADGVETLRETRDYLVVATTRPETMLGDTAVMVHPDDARYATLHAAQIVLPLTGRLVPVITDDYVDRAFGTGVVKVTPAHDFNDYQVGVRHDLPLINLFTVTAAINDNAPERYRGLDRYDARKLVLSELEDLGLLVETKPHKLQVPRGDRTGQVIEPYLTDQWFVKMDALAKRGLELVESGQVKFVPPNWINTYRHWMENIQDWCISRQLWWGHRIPAWFDEAGKCYVGHDEAQVRATHGLGAEVALHQDSDVLETWFSSQLWPFSTLGWPDAQAMDERGFARYLPSSVLVTGFDIIFFWVARMIMATDSFTGQVPFRDVYITGLIRDAQGQKMSKSKGNVLDPLDIIDGISIEDLVAKRTSGLMQPRMAEKIEKATRKEFPDGIIAHGADALRFTIAALATHGRDIKFDLGRAEGYKNFCNKLWNATRFALMNTEGAQFSGVPQPQTETERWILARLDAVAAEAQAHYANYRFDLLAQTLYEFAWNAFCDWFVELAKPALNGAVQDAADSTRHTLLYVLEALLRLLHPLTPFVTEELWQQVAPRLGITGDTISLQAFPQRGDVDTSGYAGAEADIEWLKAMVSALRRVRSELNVPPSKQVRLWLQAGSSDDRARVARFASQLAFLLKLEAIDWLAAGQEAPPAAAAIVGELTLLVPLEGLVDMDAERTRLDKEIKRVENEIGKCNGKLGNATFVQNAPAAVVEQERARLNDWTTQLTGLREQRAKL", "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": "MHRYRTHTCEQLRPENVGETVRLSGWVHRKRDHGNLLFVDLRDHYGLTQVVCDVSSAVFKTLEAVRAESVVSVTGTVVARTAETANAKLPTGAIEVKAQTVEVLSQSEVLPMQVAGDQEYPEDMRLTYRFLDLRREDVHANMVLRSKVISSLRRRMTDQGFLEYQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQFKQMLMVSGFDRYFQVAPCFRDEDSRADRSPGEFYQLDFEMSFVTQEDVFAAIEPVLVGVFEEFGGDRAVTPAPFPRIPYDEAMLKFGSDKPDLRNPLRNADVTEHFADGGFGLFSKQIALGSVVRAIPAPGAAGRPRGWYDKLNEWARESGAGGLGYVVFEEAGPKGPIAKNLEPERVEAIRQALDLKAGDSVFFACDKPLKAAKFSGLVRERICDDLGLRETGVFRFCWTVDFPMYEMNEETGQIEFSHNPFSMPQGEMEALETMDPLAIKAYQYDIVCNGIELSSGAIRNHLPEIMYKAFEIAGYPKEEVEARFGGMLRAFKFGAPPHGGSAPGIDRIVMLLADEPNIREVILFPMNGQAQDLLMQAPNTVSDKQLKELHIKLDLPKKALKVDKGEAAGDKAE", "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": "MKGCLATMDKELWIERANDSLVKHFYEQQSDIEQREGFESKLTFGTAGIRGKFGLGEGRLNKFTIEKLALGLARYLNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVYLPDTYKTTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEEVGDPLQIDIPISKQNTSYIKPFPKSVTDDYMKHIQNMIGYIPKSDLQVVFTSLHGTSVPIVPELLKSLNFNQFNLVDAQCKPDPNFSSVQSANPEDHRAFDQAVELANKSHADLLISTDPDADRLGIAERDAHGHITYFNGNQIGALLLNYRIQQTSQLRHRLMIQSIVSSELTKSLARYNNVKYKEVLTGFKFIAQEIRQLDDHQNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASELKLYGKTLKDELEQIYQTVGRHEDTLFSHTLEGLEGKKKIESIMTHFRSNPPQEIQGLKVKAIEDYLTSEVYHLDKDTTSQINSSKSNVIRVLFDEGFIALRPSGTEPKIKLYVSLKCPDFDDVAQKINAMIFS", "text": "FUNCTION: Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in the S.aureus membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA) (By similarity). SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MPRKKPFSVKQKKKQLQDKRERKRGLQDGLRSSSNSRSGSRERREEQTDTSDGESVTHHIRRLNQQPSQGLGPRGYDPNRYRLHFERDSREEVERRKRAAREQVLQPVSAEVLELDIREVYQPGSVLDFPRRPPWSYEMSKEQLMSQEERSFQEYLGKIHGAYSSEKLSYFEHNLETWRQLWRVLEMSDIVLLITDIRHPVVNFPPALYEYVTGELGLALVLVLNKVDLAPPALVVAWKHYFHQHYPQLHVVLFTSFPRDPRTPQDPSSVLKKSRRRGRGWTRALGPEQLLRACEAITVGKVDLSSWREKIARDVAGATWGNGSGEEEEEEDGPAVLVEQQTDSAMEPTGPTRERYKDGVVTIGCVGFPNVGKSSLINGLVGRKVVSVSRTPGHTRYFQTYFLTPSVKLCDCPGLIFPSLLPRQLQVLAGIYPIAQIQEPYTAVGYLASRIPVQALLHLRHPEAEDPSAEHPWCAWDICEAWAEKRGYKTAKAARNDVYRAANSLLRLAVDGRLSLCFHPPGYSEQKGTWESHPETTELVVLQGRVGPAGDEEEEEEEELSSSCEEEGEEDRDADEEGEGDEDTPTSAPGSSLAGRNPYALLGEDEC", "text": "FUNCTION: Possible regulatory or functional link with the histocompatibility cluster. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family."}
{"protein": "MYAVFQSGGKQHRVSEGQTLRLEKLDVETGATVEFDNVLMIANGEEITVGAPLVAGGKVTAEVVQHGRGDKVKIVKFRRRKHSRKQQGHRQWFTEVKITGISA", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MKGLIARFIAGFALLLWAWDMVFPWQQLMQAEENRYNQIQQRKILRVGMVNHPLSYFIGAEGTAGIEYELAKSFANYLDVRLDIKTFDNSEQLFSALKDNKVDIAAAGLLYQPELSKQFQIGSAYYSASWQVVYKKGSNRPYKLSELEGDLIIPAGSAVLPILQRLKEDNPKLSWQTTNQFTQEELLLQVAEGKIPYTVGISVDISAAQHIRPNIAVGFDLTDEAPVLWYLPNSSYSELQAAVLDFMNHANETGLISRIEEKYFNHLAHFDYVDIQSYLKAIKLVLPKYQSLFEKYRGDLEWQMLAAIAYQESHWDPNATSPTGVRGMMMLTRDTAERMKITDRTSAEQSIRAGSEYLHMLMRQIPETVPKEDRIWYGLAAYNMGFGHLLDVRRLTRQLGGNPDNWLDVKKNLPLLAEKRHYSGLKYGYARGFEAFQYVENIRRYYSSIINHQRVEEQQIQNNEEQPSVPQEISKESDSTLKE", "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": "MFNKFNTKPLWEVSKTLSSVAQGFEPADMVIINSRLINVCTREVIENTDVAVSCGRIALVGDAKHCIGENTEVIDAKGQYIAPGFLDGHIHVESSMLSVSEYARSVVPHGTVGIYMDPHEICNVLGLNGVRYMIEDGKGTPLKNMVTTPSCVPAVPGFEDTGAAVGPEDVRETMKWDEIVGLGEMMNFPGILYSTDHAHGVVGETLKASKTVTGHYSLPETGKGLNGYIASGVRCCHESTRAEDALAKMRLGMYAMFREGSAWHDLKEVSKAITENKVDSRFAVLISDDTHPHTLLKDGHLDHIIKRAIEEGIEPLTAIQMVTINCAQCFQMDHELGSITPGKCADIVFIEDLKDVKITKVIIDGNLVAKGGLLTTSIAKYDYPEDAMNSMHIKNKITPDSFNIMAPNKEKITARVIEIIPERVGTYERHIELKVKDDKVQCDPNKDVLKAVVFERHHETGKAGYGFVKGFGIKRGAMAATVAHDAHNLLVIGTNDEDMALAANTLIECGGGMVAVQDGKVLGLVPLPIAGLMSNKPLEEMAEMVEKLDSAWKEIGCDIVSPFMTMALIPLACLPELRLTNRGLVDCNKFEFVSLFVEE", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family."}
{"protein": "MTQKIIIFDTTLRDGEQSLKMSLSVKKKLKIAFALEKLGVDVIEAGFPISSPGDFESVKKISERIKDAKICSLARCIDGDIDIAAKAMKKANSFRIHIFLGTSALHVQSKLKKTFDQIIDMMVSSVKRAQKYTDDVEFSCEDAGRTSLDDLCRIIELAIDLGVKTINIPDTVGYTIPYEFSNIISSIYKKVPNIDKAIISVHCHDDLGMAVANSISAIQVGARQIEGTITGVGERAGNAALEEILMAIKIRKDILNFKTNIKYQEIYSTCRVISSICNIPVPVNKAIIGSNAFSHSSGIHQDGILKDKKTYEIIVPESIGFVSQPLNLTSRSGRAAVKYRMKKIGYKDSDYNIDILYSRFLKLADKKGRVSDSDLKQLVCFNNKLKNLKD", "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": "MDNCLAAAALNGVDRRSLQRSARLALEVLERAKRRAVDWHALERPKGCMGVLAREAPHLEKQPAAGPQRVLPGEREERPPTLSASFRTMAEFMDYTSSQCGKYYSSVPEEGGATHVYRYHRGESKLHMCLDIGNGQRKDRKKTSLGPGGSYQISEHAPEASQPAENISKDLYIEVYPGTYSVTVGSNDLTKKTHVVAVDSGQSVDLVFPV", "text": "FUNCTION: Enhances NF-kappa-B transcriptional activity by regulating the nuclear localization of the NF-kappa-B subunit RELA and promoting the phosphorylation of RELA by PRKACA. Regulates the effect of the cAMP-dependent protein kinase signaling pathway on the NF-kappa-B activation cascade. SUBCELLULAR LOCATION: Nucleus Note=Locates to punctate spots."}
{"protein": "MSVDTQQAPPEPTDEELAGLDAHWRAANYLAVGQIYLMANPLLTDPLRPEHVKPRLLGHWGTSPGLNLVHTHLNRVIKARDLDALCVWGPGHGGPAVLANAWLEGSYTETYPDITRDAAGMARLFKQFSFPGGVPSHVAPETPGSIHEGGELGYALSHAYGAAFDHPDLVVACVIGDGEAETGPLATSWHSNKFLDPVHDGAVLPILHLNGYKIANPTVLARLPETELDELLRGYGHDPVHVTGDDPAAVHRATARAMDTALDRIAAIQRAAREEGATGRPRWPMIVLRTPKGWTGPAEVDGLPVENTWRAHQVPLSAVRTNPEHLAQLERWLRSYRPEELFDDAGAPRPAVLAAIPEGPRRLGATPYANGGLLLRELPVPPLEKYAVPVGEPGASTHEPTRVLGDLLRDVMAATTDRRDFRLVGPDETASNRLQAVYAATGKAWQERTLPVDEDLDRHGRVMEILSEHTCQGWLEGYLLTGRHGLFSCYEAFVHIVDSMVNQHVKWLRVTRRLPWRAPIASLNYLLTSHVWRQDHNGFSHQEPGFVDHILNKSPEAVRVYLPPDANTLLSVADHALRSRDYVNVIVAGKQPCFDWLTMDQAKAHCARGAGIWDWAGTEDGSREPDVVLACAGDVPTLEILAAAQLIRHHLPELAVRVVNVVDIARLLPSGEHPHGMSDFEYDGLFTADKPVIFAYHGYPWLIHRLAYRRTGHAHLHVRGYKEIGTTTTPFDMVVGNDLDRYRLVMDVIDRVPGLAVRAAAVRQRMEDARQRHHDWIREHGVDLPEVADWTWEAPR", "text": "SIMILARITY: Belongs to the XFP family."}
{"protein": "MYSAPSACTCLCLHFLLLCFQVQVLAAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQAELQKPFKYTTVTKRSRRIRPTHPG", "text": "FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heparin-binding growth factors family."}
{"protein": "MSLSKMSMSGMSGMGMGSSSNSSAATCRMSMLWNWYIHDSCFLAKSWHINTGNKFAGSIIGIFFFAVAIEGLSLVQRMFDRWIVAHSNGKTLSGPLRIFFPSSTVHVTVWQQLIRAAMYSSFYLSATILMLIVMSFNGYAILFGFVGAWIGFFLFASDTYGTPSTGTGCCESR", "text": "FUNCTION: Required for high affinity copper (probably reduced Cu I) transport into the cell. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily."}
{"protein": "MTTMLKGIAASSGVAVAKAYLLVQPDLSFETKTIADTANEEARLDAALATSQSELQLIKDKAVTTLGEEAASVFDAHMMVLADPDMTAQIKAVINDKKVNAESALKEVTDMFIGIFEGMTDNAYMQERAADIKDVTKRVLAHLLGVKLPSPALIDEEVIIVAEDLTPSDTAQLDKKFVKAFVTNIGGRTSHSAIMARTLEIPAVLGTNNITELVSEGQLLAVSGLTGEVILDPSTEQQSEFHKAGEAYAAQKAEWAALKDAETVTADGRHYELAANIGTPKDVEGVNDNGAEAIGLYRTEFLYMDAQDFPTEDDQYEAYKAVLEGMNGKPVVVRTMDIGGDKTLPYFDLPKEMNPFLGWRALRISLSTAGDGMFRTQLRALLRASVHGQLRIMFPMVALVTEFRAAKKIYDEEKAKLIAEGVPVADGIEVGIMIEIPAAAMLADQFAKEVDFFSIGTNDLIQYTMAADRMNEQVSYLYQPYNPSILRLINNVIKAAHAEGKWAGMCGEMAGDQTAVPLLMGMGLDEFSMSATSVLQTRSLMKRLDSKKMEELSSKALSECATMEEVIALVEEYTK", "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": "MIQTESRLEVADNTGAREVMCIKVLGGSKRRYASIGDIIKVSVKEATPRGRVKKGEIYNAVVVRTAKGVRRQDGSLIKFDGNAAVLLNNKLEPIGTRIFGPVTRELRSERFMKIVSLAPEVL", "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": "MCVQTRMLVAVAVVLVVLAVLSDPVSAGYRKPPFNGSIFGKRAGGDSLYEPGKALASACQVAVEACAAWFPGPEKK", "text": "FUNCTION: GYRKPPFNGSIF-amide may be involved in olfaction and contraction of hindgut. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
{"protein": "MSAPDTVSPLDLRFSAAELAERRDRIQSFIRDTVAAAGAERCVLGLSGGIDSTTVAHLTVDELGADALHGLVMPGAVSRDQNMSDAERVAEDLGIEYDVVEIDPFVTQLTDVFPDAAGDEVAVGNARARTRAVINYFVANHGDGVVLGTGNRAEAMTGYYTKYGDQAVDCNPIGNLYKMQVRQLARDLGVPEDLVTKAPTAELWADQTDAGELGVDYDTIDAVLAVHVDGGLPASATATHLDIDPSVVETVRDLYGASKHKRAMPPAP", "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": "MWTVQNRESLGLLSFPVMVAMVCCAHSSNEPSNMSYVKETVDRLLKGYDIRLRPDFGGPPVDVGMRIDVASIDMVSEVNMDYTLTMYFQQSWKDKRLSYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWNGGEGAVTGVNKIELPQFSIVDYKMVSKKVEFTTGAYPRLSLSFRLKRNIGYFILQTYMPSTLITILSWVSFWINYDASAARVALGITTVLTMTTISTHLRETLPKIPYVKAIDIYLMGCFVFVFLALLEYAFVNYIFFGKGPQKKGASKQDQSANEKNKLEMNKVQVDAHGNILLSTLEIRNETSGSEVLTGVSDPKATMYSYDSASIQYRKPLSSREGFGRGLDRHGVPGKGRIRRRASQLKVKIPDLTDVNSIDKWSRMFFPITFSLFNVVYWLYYVH", "text": "FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated 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. GABRB1 sub- subfamily."}
{"protein": "MKTLGEFIVEKQHEFSQATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGAENVQGEVQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPEKGKTYSINEGNYIKFPNGVKKYIKFCQEEDSSTSRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPQGKLRLLYECNPMAFLAEQAGGKASDGKERILDIIPESLHQRRSFFVGNRHMVEDVERFIREYPDA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
{"protein": "MPDFSIENEISKSINKKNCIIVGVDEVGYGSLAGPVVSAASFFLRHDNEIIYNIKDSKKLTPKKRIEVYNTITSIVKWSIGFADVYEIDQHNILNATHLAMQRALNGLNCDIDYVIVDGNKVPDLPWNRKAIVDGDNISVSIAAASIIAKVTRDKLMETLHTQYPEYQWNKNKGYGTKHHLESLYKYGKTIHHRNTFAPLPGITKLYSK", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MKYQVLLYYKYTTIEDPEAFAKEHLAFCKSLNLKGRILVATEGINGTLSGTVEETEKYMEAMQADERFKDTFFKIDPAEEMAFRKMFVRPRSELVALNLEEDVDPLETTGKYLEPAEFKEALLDEDTVVIDARNDYEYDLGHFRGAVRPDIRSFRELPQWIRENKEKFMDKKIVTYCTGGIRCEKFSGWLLKEGFEDVAQLHGGIANYGKNPETRGELWDGKMYVFDDRISVEINHVDKKVIGKDWFDGTPCERYINCANPECNRQILTSEENEHKHLGGCSLECSQHPANRYVKKHNLTEAEVAERLALLEAVEV", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family."}
{"protein": "MSFSRRPKVTKSDIVDQISLNIRNNNLKLEKKYIRLVIDAFFEELKSNLCSNNVIEFRSFGTFEVRKRRGRLNARNPQTGEYVKVLDHHVAYFRPGKDLKERVWGIKG", "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": "MAPTGQVAKKGSKKAVKPPRASGGKKRHRKRKESYGIYIYKVLKQVHPDTGVSSRAMTIMNSFVNDIFERIAGEASRLTQYNKKSTISSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTTAK", "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": "MLKYKGLEGKNVLVVGLAKSGYEAAKLLHHLGANVTVNDGGDLSKDPHAKDLEKMGLKVIGGHHPLSLLDSNPIIVKNPGIPYSVPLISEAEKRGLRILTEVELSYLISEAPIIAVTGTNGKTTVTSLIGDMFDKSRQTGLLSGNIGYVASKVAQEAKPEDYLITELSSFQLLGIEQYRPHIAIITNIYSAHLDYHGTLEEYRNAKRRIYKNQTEDDFLICNYNQRHLIETDGLKSKVYYFSTSQEVDGIYVKDGYIMLNGLRLIHKDDIVLPGEHNLENILAAVLAAVLGGVSIDAVIATLTSFSGIKHRLQYIGSNKTNKYYNDSKATNTLATQFALNSFNQPIIWLCGGLDRGNGFDELIPYMKNVRVMITFGETQDKLTKLGESQGKYVIRATDVKDAVDKVQNVIEPNDVVLLSPACASWDQYNTFEERGDIFIESFRAHLPSK", "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": "MEGMNMGSSMNMDAMSSASKTVASSMASMSMDAMSSASKTILSSMSSMSMEAMSSASKTLASTMSSMASMSMGSSSMSGMSMSMSSTPTSSASAQTTSDSSMSGMSGMSSSDNSSSSGMDMDMSMGMNYYLTPTYKNYPVLFHHLHANNSGKAFGIFLLFVVAAFVYKLLLFVSWCLEVHWFKKWDKQNKYSTLPSANSKDEGKHYDTENNFEIQGLPKLPNLLSDIFVPSLMDLFHDIIRAFLVFTSTMIIYMLMLATMSFVLTYVFAVITGLALSEVFFNRCKIAMLKRWDIQREIQKAKSCPGFGNCQCGRHPEPSPDPIAVADTTSGSDQSTRLEKNNESKVAISENNQKKTPTQEEGCNCATDSGKNQANIERDILENSKLQEQSGNMDQNLLPAEKFTHN", "text": "FUNCTION: High-affinity copper transporter of plasma membrane that mediates copper uptake under low copper conditions (PubMed:8293472, PubMed:7929270, PubMed:8756349, PubMed:12391279). Copper transport through the high affinity system requiring CTRl supplies the iron transport multicopper ferroxidase FET3 with copper, which in turn is required for ferrous iron uptake (PubMed:8293472). The energy for translocation is unlikely to be directly derived from ATP hydrolysis and the exact mechanism driving the transmembrane transport of copper has still to be determined (PubMed:7929270). Binds 4 copper ions via its C-terminal cystein-rich domain and is able to deliver Cu(I) directly to both the chaperone ATX1 and to an N-terminal domain of the CCC2 protein (PubMed:15012137). Also able to mediate the uptake of the anticancer drug cisplatin (PubMed:12391279, PubMed:12370430, PubMed:14511662). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MKIPLRFLLISLVPTLSMSNLLGAATTEELSASNSFDGTTSTTSFSSKTSSATDGTNYVFKDSVVIENVPKTGETQSTSCFKNDAAAGDLNFLGGGFSFTFSNIDATTASGAAIGSEAANKTVTLSGFSALSFLKSPASTVTNGLGAINVKGNLSLLDNDKVLIQDNFSTGDGGAINCAGSLKIANNKSLSFIGNSSSTRGGAIHTKNLTLSSGGETLFQGNTAPTAAGKGGAIAIADSGTLSISGDSGDIIFEGNTIGATGTVSHSAIDLGTSAKITALRAAQGHTIYFYDPITVTGSTSVADALNINSPDTGDNKEYTGTIVFSGEKLTEAEAKDEKNRTSKLLQNVAFKNGTVVLKGDVVLSANGFSQDANSKLIMDLGTSLVANTESIELTNLEINIDSLRNGKKIKLSAATAQKDIRIDRPVVLAISDESFYQNGFLNEDHSYDGILELDAGKDIVISADSRSIDAVQSPYGYQGKWTINWSTDDKKATVSWAKQSFNPTAEQEAPLVPNLLWGSFIDVRSFQNFIELGTEGAPYEKRFWVAGISNVLHRSGRENQRKFRHVSGGAVVGASTRMPGGDTLSLGFAQLFARDKDYFMNTNFAKTYAGSLRLQHDASLYSVVSILLGEGGLREILLPYVSKTLPCSFYGQLSYGHTDHRMKTESLPPPPPTLSTDHTSWGGYVWAGELGTRVAVENTSGRGFFQEYTPFVKVQAVYARQDSFVELGAISRDFSDSHLYNLAIPLGIKLEKRFAEQYYHVVAMYSPDVCRSNPKCTTTLLSNQGSWKTKGSNLARQAGIVQASGFRSLGAAAELFGNFGFEWRGSSRSYNVDAGSKIKF", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Cell outer membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the PMP outer membrane protein family."}
{"protein": "MVVSPSTMAAVRASGAVPNAEFLLAADGIRKEFPGVVALDDVQFHLKRGTVHALMGENGAGKSTLMKILAGIYQPDNGEIRLKGAPIRLDSPLDALENGIAMIHQELNLMAYMTVAENIWIRREPKNRLGFIDHGEMYRRTETLLERLGIDLDPETRVGELSVASRQMVEIAKAVSYNSDVLIMDEPTSALTEREVEHLFRIIRDLRERGIGIVYITHKMNELFEIADEFSVFRDGKYIGTHASTDVTRDDIIRMMVGREITQMFPKEEVPIGDVVLSVKNLNLDGVFHDVSFDVRAGEILGVAGLVGSGRSNVAETVFGVTPASSGTISIDGKPVSIDSPTTAISHRMAFLTEDRKDTGCLLILNILENMQIAVLQDKYVANGFVQENALSEACEEMCRKLRVKTPHLYERIENLSGGNQQKVLIGRWMLTKPRILILDEPTRGIDVGAKAEIHKLVCEMARQGVAVIMISSEMPEVLGMSDRVMVMHEGRVTGFLARSEATQVKVMDLASR", "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": "MKLIASNKKAYFDYEILETLEAGLALLGSEVKALRQTRVNLKDNFVKIIKGEAFLFGVHISYLDTIHAYYKPNERRERKLLLHKKQLLKWQIEASKERLSIVGLKLYFNQRNRAKIQIALVKGKRLHDKRQSLKEKALNKEILADLKHHFKG", "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 (Probable). 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 (PubMed:19043582). 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": "MSEEFQESDIIFSDQSKISTSSRYTKLYNSRNDEKKGTRRHETAEKTSPVRIPTNNFRCLEWDTTEEEDDKTPPHVIIERRMKEQIAFSACTLKGRDLSRHRNSVLRMTGFLEA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the senescence regulator S40 family."}
{"protein": "MKKLTKTNLKYKKQSLKIGDLVEIIAGNDKKKQGTVKAIIKSQEKVIVEGINQRFKHIKPQRSNETGKINQFEAPIHRSNVKKINN", "text": "FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "MSFSVDVLANIAIELQRGIGHQDRFQRLITTLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRRFALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPGQESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDVFSDEELRLIAALAAGALSNALLIEQLESQNMLPGDAAPFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLISGETGTGKELVAKAIHEASPRAVNPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRSLRVDVRVLAATNRDLREEVLAGRFRADLFHRLSVFPLSVPPLRERGDDVILLAGYFCEQCRLRLGLSRVVLSAGARNLLQHYNFPGNVRELEHAIHRAVVLARATRSGDEVILEAQHFAFPDVTLPPPEAAAVPVVKQNLREATEAFQRETIRQALAQNHHNWAACARMLETDVANLHRLAKRLGLKD", "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": "MMFLFVSLFMFIFKWQRLIFILISLEFMMLSLFLKFSYVLGEMMFFYFMCFSVISSILGMVVMVGNMKFFGSDNCIF", "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": "MSNASLVTAFILTGLPHAPGLDALLFGIFLVVYVLTVLGNLLILLVIRVDSHLHTPMYYFLTNLSFIDMWFSTVTVPKMLMTLVSPSGRAISFHSCVAQLYFFHFLGSTECFLYTVMSYDRYLAISYPLRYTSMMSGSRCALLATGTWLSGSLHSAVQTILTFHLPYCGPNQIQHYFCDAPPILKLACADTSANVMVIFVDIGIVASGCFVLIVLSYVSIVCSILRIRTSDGRRRAFQTCASHCIVVLCFFVPCVVIYLRPGSMDAMDGVVAIFYTVLTPLLNPVVYTLRNKEVKKAVLKLRDKVAHPQRK", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MLVYLAEYLTRFHTGFNVFSYVTFRAILGLLTALVFSLWFGPKLIERLQLLQIGQVVRNDGPESHFSKRGTPTMGGLLILAAIFISVLLWGDLGSRYVWVMLFVLGSFGLIGFIDDYRKVVRKDTKGLIARWKYILQSLAALLIAFFLYATAANPGETQLVVPFFKDVMPQLGAVFIVLAYFTIVGSSNAVNLTDGLDGLAIMPTVMVAAAFALIAYLSGHAQFANYLHIPHLPGSGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLSLGAALGTIAVLVRQEILLVIMGGVFVMETLSVILQVGSYKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISIFLVLLGLATLKLR", "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": "MSLPQWCPPHSTLKRNPTTGEDVYCICKRPDYGELMVGCDGCDDWFHFTCLHIPEQFKDLVFSFYCPYCQAGITGKNKDAIINGEGSLPKTLWKRKCRISDCYKPCLQDSKYCSEEHGREFVNDIWSRLKTDEDRAVVKKMVEQTGHIDKFKKFGQLDFIDNNIVVKTDDEKEIFDQIVVRDMTLKTLEDDLQEVQEISLPLFKKKLELLEVYLGWLDNVYTEMRKLDDDAASHVECGKEDSKGTKRKKKKNSSRSRARKNICGYCSTYERIPCSVEEFVRDFGSNEEATKIHEVCTKWKCNRHLDWVSTNQEQYLQQIDSLESMQERLQHLIQARKKQLNIQYYEEILRRGL", "text": "FUNCTION: The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MATQNGGPTQNAAPSLNVLAQYIKDFSFENPNAPRSLAAPPSQPDVNIQIHVNARPGGNGEFEVELKIDGGASIEGNTLFAFELVYAGVFRILNVPEESLQPVALIECPRLLFPFARQIIADAVRNGGFPPLMIDPVDFAALFQQRMQQEGQRIQA", "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": "MTAPLWPNKNEKNHTVKRALSTDMTSNILSSTNASSNEENSRSSSAANVRSGTGANTLTNGGSTRKRLACTNCRNRRKKCDLGFPCGNCSRLELVCNVNDEDLRKKRYTNKYVKSLESHIAQLETNLKNLVQKIYPDDEQILNRMMVGDVLSALPDSSQVSINYTDQTPSLPIPATRGTFIIENDKVSQPLSSFNQQTEPSTLNSGIFNTQKQNFEESLDDQLLLRRSLTPQGEKKKKPLVKGSLYPEGPVSYKRKHPVKSDSLLPVSSLTAATDPSTFSDGITAGNSVLVNGELKKRISDLKTTVIVRGLNDDNPNSINNDPRILKSLSNFYKWLYPGYFIFVHRESFLYGFFNHSKNNYEDSSYCSVELIYAMCAVGSRLTPDLQEYSEVYYQRSKKTLLQLVFDEQSTARITTVQALFCLAFYELGKGNNQLGWYFSGLAIRVGYDMGFQLDPKVWYVDDNNLQLTQSELEIRSRIYWGCYIADHFICLMLGRTSTLSVSNSTMPESDELPEVNGTEEFRFIGRHVLQISLPLKNLIILSRLVQIFTSKIFIESEDIARKLKYLNTFNSQVYNWRQSLPEFLQWSKTLIENDDVSTDPTISYFWYCYYIVRLTFNKPFIEDSQESETVVIEIIDDLKTLLDNFGKKFGNYTKGNLYQLYSCLLAINCLKKLKEIRSSEQDSWNAQLDFFNHIFYTQLYPAYDLPKKLQEDTELETEQENQMLNQVGNINYTHDFSLSHEIDDLIRELFGVGTPQKL", "text": "FUNCTION: TY1 element enhancer binding protein. Binds to the DNA sequence 5'-TCGGTGGTATTATTCCGA-3'. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MHELSMAQGIINAVIDTAESNNATEVTEVGIEIGRLAMINPEQLRFMLSVLVENTIVEDADIKIEEIPVEINCPECGFKGVAELDDKDHYAPIVECPKCGNKRISILNGKDCVVKNIVIEKPDDD", "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": "MLFSGKYQLESQENFEAFRKAIGLPDELIQKGKDIKSISEIEENGDDFKVTITTGSKVIVNTFTVGKEAELETLTGEKAKGVVHRDGNKLKVSLKGIESVTELVDGNTIANTMTLGNIGYKRISKRV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MAGHSKWHNIQHRKGAQDAKRGKIFTKLIKEIVISAKIGGGRIENNHSLKIIIDKALAVNMRRNTIENAVKRGNGDFDGNNYEKIRYEGYSLGGTAIMVDCLSDNRNRTISDIRHAFLKHGGNLGRDGSVSYLFTKQGFISFDTGNENQIMEIALDEGAQDIITNDDDSIDVITTPEDFFTIKDVLTTSGLEPSHAEVTMEPASRVELNLSDAEKFMKLIDHLEDLDETKKIYHNADISDKVMVRL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family."}
{"protein": "MAGQYWRAAGITYLQYANICGTHVRNCLKEPFRAAAKNREGFISNTVMYQNGKESSTIILNSELLQKELLVKKN", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase epsilon family."}
{"protein": "MKFAVIVFPGSNCDVDMFHAIKDELGEEVDYVWHDRENLDEYDAILLPGGFSYGDYLRCGAISRFANAMKAVQKAAEQGKPILGVCNGFQILVESGLLPGALMRNENLKFMCRTVQLRVENNETMFTSQYEKNEVINIPIAHGEGNYYCDEATLKQLEENNQIAFRYVENPNGSVSDIAGIVNEKGNVLGMMPHPERAVDELLGGAEGLKVFQSILKQWRETYVVNA", "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": "MDKRHDPSRRIIAPTGTKLSCKSWLTEAPMRMLMNNLHPDVAERPEDLVVYGGIGRAARDWECYDKIVEVLQRLEDDETLLVQSGKPVGVFKTHSNAPRVIIANSNLVPHWANWEHFNELDKKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVAMAKQHFGGSSKGKWILTGGLGGMGGAQPLAGTMAGYSVLTCEVDETRIDFRLRTRYVDKKATTLDEALAMIDEANASGKPVSVGLLANAADVFAELVERGITPDVVTDQTSAHDPLNGYLPQGWTLEQAAQMRKTDEAAVVKAAKQSMAVQVKAMLALQAAGSATTDYGNNIRQMAFEEGVENAFDFPGFVPAYVRPLFCEGIGPFRWAALSGDPEDIYKTDAKVKELIPDNPHLHNWLDMARERIAFQGLPSRICWVGLKDRARLALAFNEMVNNGELSAPVVIGRDHLDSGSVASPNRETESMLDGSDAVSDWPLMNALLNTASGATWVSLHHGGGVGMGFSQHSGVVIVADGTDDAAARLGRVLWNDPATGVMRHADAGYDIAKDCAKEQGLDLPMLEK", "text": "FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5- propionate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urocanase family."}
{"protein": "MALDIKICGLKTPEAVAAALDGGATHIGFIFFPKSPRHITPDAAARLRAAATGRAVAVAVTVDADDEALDEIVKTVRPDMLQLHGGETPERVRFLKERYNLPVMKAFSIREAGDLEAIAPYRGIADRFLFDAKPPKGSELPGGNGISFDWNLLAALDADIDYMLSGGLNADNIAEALLKTGAPGIDISSGVECAPGEKDVRLIENFFQAVADANAQPFARRA", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MSGRPQAVPTVQVDNAEVIVTEWRFAPGAETGRHRHGHDYVVVPLTDGTLLLETPEGDRHAPLVAGQAYFRKAGVEHNVINASAHEVVFVETEIK", "text": "FUNCTION: Involved in the degradation of beta-alanine."}
{"protein": "MTNDFHHITVLLHETVDMLDIKPDGIYVDATLGGAGHSEYLLSQLGPDGHLYAFDQDQKAIDNAHIRLKKYVDTGQVTFIKDNFRNLSSNLKALGVSEINGICYDLGVSSPQLDERERGFSYKQDAPLDMRMNREQSLTAYDVVNTYSYHDLVRIFFKYGEDKFSKQIARKIEQVRAEKPISTTTELAEIIKSSKSAKELKKKGHPAKQIFQAIRIEVNDELGAADESIQQAMDLLAVDGRISVITFHSLEDRLTKQLFKEASTVEVPKGLPFIPDDLQPKMELVNRKPILPSQEELEANNRAHSAKLRVARRIR", "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": "MDNKTYEISSAEWEFMNIIWMKKYASANNIIEEIQMQKDWSPKTIRTLITRLYKKGFIDRKKDNKIFQYYSLVEESDIKYKTSKNFINKVYKGGFNSLVLNFVEKEDLSQDEIEELRNILNKK", "text": "FUNCTION: Transcriptional repressor that constitutively blocks the transcription of the gene for the penicillin-binding protein MecA. Binds DNA as a dimer (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BlaI transcriptional regulatory family."}
{"protein": "METDCNPMELSSMSGFEEGSELNGFEGTDMKDMRLEAEAVVNDVLFAVNNMFVSKSLRCADDVAYINVETKERNRYCLELTEAGLKVVGYDFDQVDDHLQTPYHETVYSLLDTLSPAYREAFGNALLQRLEALKRDGQS", "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": "MSNSHTLFEAAQAHIPGGVNSPVRAFKGVGGDPVFFESAKGAYLTDADGKQYIDYVASWGPAILGHTHPDVIKAVQTQAEKGLSFGAPTEIETTMADMVCDLIPSMDMVRMVSSGTEATMTAIRLARGYTGRDKIVKFEGCYHGHSDSLLVKAGSGALTLGVPSSPGVPACLAQETLTLTHNDSEEVKKVFSEIGDQIACIIVEPVAGNMNCIPPEDGFLETLREVCDESGAVLIFDEVMCGFRVGLTGAQGRYNITPDLTTFGKVIGGGMPVGAFGGKKEVMQHIAPLGPVYQAGTLSGNPIAMTAGLKTLELISKPGFFEELEAKTTKLVNGLQKAADEAGIAFTTNQVGAMFGFFFSEEKDIRRFSQVAKGNMEQFKAFYHGMLDEGIYLAPSAFEAGFVSSAHTDQDIDDTIAAAKKVMATL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
{"protein": "MAAGKEIRTKIKSVENTRKITKAMEMVAASKMRKAQDRMKAARPYAEKIARVATHLAYAHPEYKHPFVIARDDVKRVGLIIVTSDKGLCGGLNTNAFRVVVNQMKQWEAAGVGIDVTAIGNKGLGFMQRLGANVVSQLTGVGDTPHMDKLIGPVKIMLDAYLEGRIDALYLVYNRFINTMKQEPTLTQLLPLAKMESTEEASLKTHWDYIYEPDAKPVVDAMLMRYIESLVYQGVAENIASEQSARMVAMKAASDNAKNVIGELKLVYNKTRQAAITKELSEIVAGAAAV", "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": "FLNALKNFAKTAGKRLKSLLN", "text": "FUNCTION: Has antibacterial activity against E.coli HP101BA (MIC=6.4 uM), K.pneumoniae PTCC1388 (MIC=7.3 uM), M.luteus PTCC1625 (MIC=4.7 uM) and S.aureus PTCC1431 (MIC=5.3 uM). Has no or very limited (<3%) hemolytic activity at concentrations of 15 ug/ml and 60 ug/ml, respectively. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MSATKLTRREQRARAQHFIDTLEGTAFPNSKRIYLTGTHSGVRVPMREIQLSPTLIGGSKEQPQFEENEAIPVYDTSGPYGDPQIAINVQQGLAKLRQPWIDARGDTEELTVRSSDYTKARLADDGLDELRFSGVLTPKRAKAGRRVTQLHYARQGIITPEMEFIAIRENMGRERIRSEVLRHQHPGMSFGARLPENITAEFVRDEVAAGRAIIPANINHPESEPMIIGRNFLVKVNANIGNSAVTSSIEEEVEKLVWSMRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGIAEDLTWEAFRDTLLEQAEQGVDYFTIHAGVLLRYVPMTAKRLTGIVSRGGSIMAKWCLSHHQENFLYQHFREICEICAAYDVSLSLGDGLRPGSIQDANDEAQFAELHTLGELTKIAWEYDVQVMIEGPGHVPMQMIRRNMTEELEHCHEAPFYTLGPLTTDIAPGYDHFTSGIGASMIGWFGCAMLCYVTPKEHLGLPNKEDVKQGLITYKIAAHAADLAKGHPGAQIRDNAMSKARFEFRWEDQFNLALDPFTARAYHDETLPQESGKVAHFCSMCGPKFCSMKISQEVRDYAATQTIEMGMADMSENFRARGGEIYLRKEEA", "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": "MVGGELVLAALVILLALLLTLVLSHFLPLLLNPKAPKGSFGWPLLGETLRFLSPHASNTLGSFLEDHCSRYGRVFKSHLFCTPTIVSCDQELNHFILQNEERLFQCSYPRPIHGILGKSSMLVVLGEDHKRLRNLALALVTSTKLKPSYLGDIEKIALHIVGSWHGKSKDKGMVNVIAFCEEARKFAFSVIVKQVLGLSPEEPVTAMILEDFLAFMKGLISFPLYIPGTPYAKAVQARARISSTVKGIIEERRNAGSSNKGDFLDVLLSSNELSDEEKVSFVLDSLLGGYETTSLLISMVVYFLGQSAQDLELVKREHEGIRSKKEKDEFLSSEDYKKMEYTQHVINEALRCGNIVKFVHRKALKDVRYKEYLIPSGWKVLPVFSAVHLNPLLHGNAQQFQPCRWEGASQGTSKKFTPFGGGPRLCPGSELAKVEAAFFLHHLVLNYRWRIDGDDIPMAYPYVEFQRGLPIEIEPLCSES", "text": "FUNCTION: Involved in brassinosteroid biosynthesis (PubMed:15705958, PubMed:16369540). May catalyze a C6-oxidation step and may be involved to supply 6-deoxotyphasterol and typhasterol (PubMed:15705958). Involved in internode elongation and seed development (PubMed:15705958). Catalyzes the conversion of campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) (PubMed:16369540). FUNCTION: Involved in brassinosteroid biosynthesis (By similarity). Involved in internode elongation and seed development (By similarity). Catalyzes the conversion of campesterol (CR) to (22S)-22- hydroxycampesterol (22-OHCR, 22-hydroxyCR) (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MISNINALKYKKVLLKVSGEALMGDKQFGHEYEVIKKISSDIKEVIDLGVEVAIVVGGGNIYRGINAALVGMDRASADYIGMLATVINALTLQNVMESLDIYTRVLSAIPMMSVCEPYIRRKAKRHMEKKRVVIFAGGTGNPFCTTDSAAVLRAIEMNCDMLLKATQVDGVYDADPKKNPDAKKYCTINYKDVITNNLQVMDTAAIAVARENKLPIRIFSIKEQGNFARVIQDKGEYTTIEESVV", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MVESQKAMPQPKMGRIRRIHFVGIGGVGMCGIAEVLLNLGYEVSGSDLKASPVTERLESFGAEIFVGHRAENAATADVLVVSSAINPANPEVATALERRIPVVPRAEMLAELMRYRHGVAVAGTHGKTTTTSLLASVFAAGGLDPTFVIGGRLTAAGTNAQLGTSRYLIAEADESDASFLHLQPMVAVVTNIDADHMATYEGDFNKLKKTFVEFLHNLPFYGLAVMCLDDPVVREILPQVKRPTVTYGFSEEADIRAINVRQQGMQTHFTVLRRDCEPLEVSVNMPGNHNVLNALATIAIATDEGITDEAIIQGLSGFQGVGRRFQVYGELPVEGGSVMLVDDYGHHPTEVAAVIKAVRGGWPSRRLVIVYQPHRYSRTRDLYDDFVQVLGDANVLLLMEVYPAGEEPIPGADSRQLCHSIRQRGKLDPIYIERGAELAPLVKPLLRAGDILICQGAGDVGGLAPQLMKSPLFAGAKQEKSK", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family."}
{"protein": "MTAKRIIACLDVKNGRVVKGVNFLNLKDKGDPVELASRYEEEGADEIVFLDITATIEGRKALLEVVKNTASVLSIPLTVGGGIRTIEDVSRILGNGADKVSINTAAVENKKIITEASEQFGAQAIVVAIDVKRVNNSFIVFTRSGTYNTGIDAIQWAKEVEKLGAGEILLTSIDKDGTREGYDIELTKEVNNSVNIPVIASGGAGKMEHFYEVLKVADAALAAGVFHDGVIKIPELKRFLLEKGIEVRV", "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": "MPYSIPLLRPNPADPVPFYRLPHLIHTYSHLPTRAISHDDASMAYYSPAPIGCNLTEGFERRIEREDEEEHLDGLVESLEWLITRGRKGERKGGIITWRGMLTRLITMPYETRDPWEMTAIALDGSVYLELWDPPEEKAKRKREQSAWEKQGYMGYAYESFSTIPQEGRPGNGPEGWGGDVNTNVQWANVVRSAIGEIPLCIAGEVDCVKAEPGSPNPGLSGCMELKTNKVIQHPGHEAMFHKKLLKHWAQSWLLGIPEVVVGFRDDDGILRSQTTFDTAKIPYLVEVLNKPSWSPNRCLQSLHSVCSFLTKNVLPTDPLVTYPHIRGNRQAVKEAGELPPAVVWRLAFDPKKGCELHAVGEVGVVDGRWGGMLKEEYVRWRMGLE", "text": "FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DXO/Dom3Z family."}
{"protein": "MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI", "text": "FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:11012666, PubMed:12534281, PubMed:12662155, PubMed:15039077, PubMed:15664838, PubMed:20536396, PubMed:29382749). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:32796818). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:34019797, PubMed:33731929, PubMed:33731932). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP8, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily."}
{"protein": "MARAIMLQGTGSDVGKTVLVAGLCRLAANRGLTVRPFKPQNMSNNAAVADDGGEIGRAQWLQSLAARTPSSVHMNPVLLKPQSENGSQIIVQGRVFGQAKGRDYQRLKPQLLGAVLASFEKVADGADLVIVEGAGSPAEINLRAGDIANMGFATQAGVPVVLVGDIDRGGVIASLVGTHAILADADRAMISGYIINKFRGDVSLFDNGIRAIEGFTGWPCFGVVPWLSGAARLPAEDSVVLERLAKGGGGALKIAVPVLPRIANFDDLDPLRAEPDVELVFIRSGERLPADASLVVLPGSKSTISDLADLRAAGWDRDLFAHVRRGGRVIGICGGYQMLGRTVHDPLGLEGGTLETPGLALLDVETEMAPEKTVRNSHARSTEYDAPLAGYQIHLGMTRGPDCGRPSAIVDGVPDGALSANGLIMGTYLHGLFASDAYRTRLLQSFGLSGERRNYRESVDKALDEIAGELERYLDPRWLAGLVG", "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": "MASSSPVTPGLMSVVFGIVPVIVAWLYSEYLHYAKYSVSAKTRHSDVNLVEIAKDFVKEDDKALLIEDGGGLQSASPRAKGPTTHSPLIRFVLLDESFLVENRLTLRAIIEFAVLMVYFYICDRTDVFNSSKKSYNRDLFLFLYFLLIIVSAITSFTIHTDKSPFSGKAIMYLNRHQTEEWKGWMQVLFLMYHYFAAAEYYNAIRVFIACYVWMTGFGNFSYYYIRKDFSLARFAQMMWRLNFLVIFSCIVLNNSYMLYYICPMHTLFTLMVYGALGIMSKYNEMGSVIAAKFFACFVVVIIVWEIPGVFEWIWSPFTLLMGYNDPAKPQLPLLHEWHFRSGLDRYIWIIGMLYAYYHPTVESWMDKLEEAEMKFRVAIKTSVALIALTVGYFWYEYIYKMDKLTYNKYHPYTSWIPITVYICLRNITQSFRGYSLTLLAWLGKITLETYISQFHIWLRSGVPDGQPKLLLSLVPDYPLLNFMLTTSIYVAISYRLFELTNTLKTAFIPTKDDKRLVYNTISALIICTCLYFFSFILITIPQKLV", "text": "FUNCTION: Probable O-acetyltransferase involved in the acetylation of cell wall polymers (both pectic and nonpectic polysaccharides) and of xylan during secondary wall biosynthesis. Catalyzes the O-acetylation of xyloglucan. FUNCTION: Seems required for infection by the necrotrophic fungal pathogen Botrytis cinerea. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily."}
{"protein": "MRPLTIIGPTGTGKSDLAIEIADRLSGKIAVEIVNADAYQLYRGMDIGTGKVPLAQRRGIPHHQLDVLDVTETATVAGYQRSAAADIEAIASRGALPLLVGGSMLYVQSLLDDWAFPAKDPAIRARWERRLAQVGPARLHAELVRRDPAAAAVIPLNDARRTVRALEVVEITGRPYAASAPRIGSPRWDSAIIGLDCETKVLDERLAARTKAMFDRGLIEEVISLLPCGLARGVTASRALGYAQVMEALKAGADTQALDSARQQTCLATRRYVRRQRSWFRRDRRVRWLDATVSTAAHRTAIIEAVLGAWRRAS", "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": "MSGQENHDHGRISSTPAAASEPSKAAAHSSDYAPYPKLDPTDVTPPPPQPIPTGAAATTMPAESNPYVSPSPAPRNTMDSVKDTLGKWGKMAADATKKAEDLAGNFWQHLKTGPSVADAAVSRIAQGTKILAEGGYEKVFKQTFDCLPDEKLLKTYACYLSTSAGPVLGVMYLSTHKLAFSSDNPLSYKEGEQTLWSYYKVVLPANQLKAVNPSTSRVNTSDKYIQVISIDNHEFWFMGFVTYESAVKSLQEAVQSHGP", "text": "SIMILARITY: Belongs to the GEM family."}
{"protein": "MTTHRLVMVRHGESLWNQENRFCGWFDAELSEKGAEEAKRGATAIKDAKIEFDICYTSVLKRAIRTLWTILDVTDQMWVPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDTPPPPMDEKHNYYTSISKDRRYAGLKPEELPTCESLKDTIARALPFWNEEIAPKIKAGQRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELDQNLKPTKPMRFLGDEETVRKAMEAVAAQGKAK", "text": "FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
{"protein": "MNVAINGFGRIGRLVLRASAKNPLINIVAINDPFVSTTYMEYMLEYDTVHGKFDGSLSHDETHIFVNGKPIRVFNEMNPENIKWGEEQVQYVVESTGAFTTLEKASTHLKNGVEKVVISAPSSDAPMFVMGVNHELYEKNMHVVSNASCTTNCLAPLAKVVNDKFGIKEGLMTTVHAVTATQKTVDGPSKKDWRGGRGACFNIIPSSTGAAKAVGKVIPSLNGKLTGMSFRVPTADVSVVDLTARLVNPASYDEIKAAIKSASENEMKGILGYTEKAVVSSDFIGDSHSSIFDAEAGIALTDDFVKLVSWYDNEWGYSSRVLDLIEHMVKNE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MAADESVFLRAKDRSYKGLTEDEQKEWSGPFYFIQAADPQLGLMKAWRIGDCDSGGDEWDEEVQLTKQAVQAINKLQPKPRFIVLCGDLVHAMPGSPFREQQIKDLKDALRGTDPHIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDDYFSFWVGGVLCLVLNSQFFFDSSGCPELMEAHEVWLENRLQMAVQTPSRHVLVFQHIPLFLRTPDEEDDYFNLQRGIREHLIQRFKRAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGCQLGDDTHGVRVVVVTENNIIHRYHSLDQLSERGMDEDLKKLLL", "text": "FUNCTION: Protein phosphatase involved in the dephosphorylation of AKT kinase family. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallophosphoesterase superfamily. CPPED1 family."}
{"protein": "MDTTPDNSEKKKTSSVREATFSINESFGGRLLTEEEDVFEQNAWDHVEWDDEHLALAKKCIEEQKLYPVTEKDAYMTHPERYWDQFYGKNEGKFFMNRRWIAQEFPELLDLLKEDAGEKSILEIGCGAGNTIWPILKENKNSNLKIFAVDYSEKAIDVVKQNPLYDAKFCSASVWDLAGSDLLRSIEEASIDAITLIFCFSALSPDQWQQAIENLYRLLKPGGLILFRDYGRLDLTQLRAKKNRILSENFYIRGDGTRVYYMTNEELVDVFGKNFKIIQNGVDKRLIVNRKKRVKMYRCWLQAKFQK", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) (PubMed:27354703). Does not catalyze N(3)- methylcytidine modification of tRNA(Ser) (PubMed:27354703). SIMILARITY: Belongs to the methyltransferase superfamily. METL family."}
{"protein": "MSAIARAAARVRQQNTTPLQRPLLLQRKPVLTHTLALHASPLKPSLATSITSPNFQQSFQRRWASASATAEEGAKEEVWPQRKLPELTETDKLRLRRQRNVGISAHIDSGKTTLTERVLYYTGRIRDIHEVRGRDAVGAKMDSMELEREKGITIQSAATFADWVAPKPPTELKEGETVGNTDKQKFAINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVSGVQSQTITVDRQMRRYNVPRLAFINKMDRAGSNPFRVIGQLRGKLKMNAAAVQVPIGSESDFAGVVDIVRMKAIYNEGVKGNQIVETDEIPESVRALAEEKRAELIEQLSEADETLCDLFLDEAPITPTDIAQALQRATTSLRFTPVFMGSAIKNTGVQPLLDGVCAYLPNPSEVQNQAMDATLPAHAPTIPLVPATDAPLVGLAFKLEEGRYGQLTYMRVYQGELKRGSMIYNARTGKRVKVPRLVRMHADEMEDVDAVVAGEICAMFGVECSSGDTFTDGSSTYTMTSMFVPEPVISLSIRPEGNETPNFSRALNRFQKEDPTFRVHVDSESQETIISGMGELHLDIYVERMKREYNVACVTGKPRVAFRETITEAAKFNYTHKKQSGGSGQFGRVIGSIEPMETDPDTGKDTAFENRIIGGNIPNQFIPAIQKGFQEALDRGLITGHPITGCKFVLDDGSAHAVDSNELAFRLAAIGAFREAFNKARPVVLEPVMTVEIVAPIEFQGNVIGAINQRKGTIVDTEVRDDEFTLTAEVALNDMFGYSSQLRGMTQGKGEFSMEYKNHQPVLPNIQKEMAEAFRKKQLSK", "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": "MTLDSYNIFNDEYLFNMPLSPLPKVLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAMGAIDALGMGIPTCVSSLPLQQTYDASLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSYQAGHIMAGSVNGGGVNNFTNVLAAVSSSRGSASVGSSNANTSNTPARRGGGRRPNRSTNMTPEEEQKRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRRDSMRKEFEALTNSKKQLEYLLATHRSTCQKIRSDMLSVATCNGLIAPAGLLSAGSSGSGASSHHNHNSNDSSNGTITGMDATLNSTGRSNSPLDLKPAANIDSLLLHIKDEPLDGAIDSGSSLDRFPVTSNGSSINNINSIGNNMNSPTLNALNKVPKERPNTLAFQRPLGQMHLSMANNKAGGPTQIQGVPIQTPSTGTFNLVSLMDGGTGLTPVSGPLVPNSSSTNKHPLELPTPTAEPSKLVSL", "text": "FUNCTION: Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Fos subfamily."}
{"protein": "MAPPNTIDAGLTQRHISTSAAPTSAKPAFERNYQLPEFTIKEIRECIPAHCFERSGLRGLCHVAIDLTWASLLFLAATQIDKFENPLIRYLAWPAYWIMQGIVCTGIWVLAHECGHQSFSTSKTLNNTVGWILHSMLLVPYHSWRISHSKHHKATGHMTKDQVFVPKTRSQVGLPPKENAAAAVQEEDMSVHLDEEAPIVTLFWMVIQFLFGWPAYLIMNASGQDYGRWTSHFHTYSPIFEPRNFFDIIISDLGVLAALGALIYASMQLSLLTVTKYYIVPYLFVNFWLVLITFLQHTDPKLPHYREGAWNFQRGALCTVDRSFGKFLDHMFHGIVHTHVAHHLFSQMPFYHAEEATYHLKKLLGEYYVYDPSPIVVAVWRSFRECRFVEDHGDVVFFKK", "text": "FUNCTION: Catalyzes the desaturation of oleic acid (Delta(9)-18:1) to linoleic acid (Delta(9), Delta(12)-18:2). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
{"protein": "MQMGDHQMMGNQRYYRTYVQKVMPAQAGGAVSQNATYVQTAGIRTVHHDGNGQQRIVQLPPGVRQIQQNGVGPAYVRQVPGGQPMQVNFGHPGTIAGRNVAVGVQMRPVQGHNVQQGYQRQQVANQIQQQNRAVFMAQNQQGQQQISYAQAQHRQQQQNQQQHHQQPQHFNHPSQQNQMIMQHRQPQMHHNQQHQMVQPQMTRHQMAQHHAQQPHPQIYVPRDMNLAVPLREPSPEPIPVKIEVPDVPPEGTSAANEEPMPDDGDIDIQIRNVVCNYTLPLHIDLRKLAMNTHNVTYEREKGVMMKQKRSPGCYIKVYSSGKVYIVGCRSEADCKRAARSIARHVQRVMGKTKERVSIRNYRVNNVLATCRLPFGIKIEEVAAKYPSESTYEPELSVGLVWRSVTPKATLRIHTTGSITVTGAQSEADVLEVLSKIYPIVLEFRCLERAKGNVAAQKKRKRKAPVNRGPPIKRERFDDSNYRNSGVINNQVYFSDEDEDLYDELDLEE", "text": "FUNCTION: May be a general transcription factor (PubMed:11030350, PubMed:11030349). Plays an essential role for RNA polymerase II/ama-1 transcription in early embryos whereby it activates a subset of RNA polymerase II promoters and facilitates the reestablishment of transcription after mitosis (PubMed:14726532). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBP family."}
{"protein": "MSGLFVSFEGVDGVGKTTQVERLRAYLEAQGRTVVVTREPGGTVLGKAIRQLLLHGVDGGAVDIAPRAEALLFAADRAQHVAETIRPALERGEVVITDRYLDSSLAYQAGGRELTPEEIRSLSMWATNNLLPDRTYLLDMDPALSHNRLEHAEDRMESAGSDFQSRTRQAFLDLAAAEPNRFHVIDASQSIEQVWSAIEADIQTLLRDNVADVDTVMARSGASTGAVTMGGVR", "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": "MEKITLTRPDDWHLHLRDGEALKAVLPDTVRQFARAIVMPNLKPPVRTVAEAAAYHDRILAAIPPGRTFEPLMTLYLTDNTSPAEIQAAKESGFVKAVKYYPAGATTNSDLGVTDIRKCDAVFEAMQTVDLPLLLHGEVTDHRVDVFDREKVFIETYLRPLKERFPQLRIVLEHITTKDAVEFVLASDEKVAATITPQHLLFNRNSIFQGGIRPHFYCLPILKRETHREALLEAATSGNPKFFLGTDSAPHGRDRKESDCGCAGCYSALHALELYATVFEAADALDKLEGFASFYGPDFYQLPRNTEKITLTKTPWQIPDALPFPESSLVPLWAGQELSWKFAPVA", "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": "MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILEYVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGRRMRGLFF", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Note=(Microbial infection) The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily."}
{"protein": "MQSAMFLTVHHDCGPMDKSAGTGPKSEEKREKMKRTLLKDWKTRLSYFLQNSSSPGKPKTGKKSKPQTFIKPSPEEAQLWAEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCRKPPQITTEPHAT", "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 (By similarity). It is involved in the negative regulation of the angiotensin-activated signaling pathway (By similarity). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (By similarity). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (By similarity). SUBCELLULAR LOCATION: Cell membrane Cytoplasm Nucleus, nucleolus."}
{"protein": "MAAGSGSGTPPGTPPPTLLTDLATGLWKTQTLTAAIETGLFEALAAGDADAPETAQRLGIGKRPAEILLTACTALGLLEQRDGRYRNTAVAAHYLVPGLPDYFGGYVQMVARYTAPGWLRATEAVRTDAPTKPVPDPDRNMFEEGNRPESFWEGLFTFSTLTARQLAASVDLSGVRRIMDVGGGAGATLIELCRQHPHLSGTVVDLPHVCALAGERIAAAGMTGRIDTAAADFFADPLPSGHDAVLLSMILHDWDESQNRKILASCLDALPSGGTVLISELLVDDDKSGPVDAALMSMNMLVGTWGRNYTGAEYTDWLRDAGCSEVRTVRFASPGANGVVAGVKA", "text": "FUNCTION: O-methyltransferase that mediates the formation of 3-methoxy- 5-methyl-1-naphthoate from 3-hydroxy-5-methyl-1-naphthoate in the biosynthesis of the antitumor antibiotic azinomycin B. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MAASTPLLSRGTLIKQGAEAKVYALPSLFPEPTTYHPGSSSSFSAASPTPVILKHRFTKTYRHPTLDASLTSQRLTFEARALARAAKAGVTVPKVVWVDEKAGVIGMERIEGWSVREILGGGAEGEVEVIEEQEIEEDVENKAEDSAVREEPEGPESEGLKALKNLGVTQEHLMRSIGAALARLHKTMIIHGDLTTSNMMVRLTPGGSGPYEIVLIDFGLSSQAQFPENYAVDLYVLERAFASTHPRSEKLYAGVLETYAEGLGEKKWKPIQIKLKDVRRRGRKRDMTG", "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": "MKLDRYDLKILEILSRDGRITKSKLAEAINLSVSPCWERVRRLEKAGVIEGYGARLNTDVLVKRTPVWVQIELKAHNAESFARFEALVHDTPEVTECVAVGGGVDYLVKFEATTIDTYQRLIDEWLVSDVGIERYFTYIVTKTVKRPSASISIDDLAT", "text": "FUNCTION: Acts as a transcriptional regulator. It binds DNA specifically to a fragment from the doeA promoter region. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSSTECYGAPPHNYYQDWPTTHSYYPSVPSSYSPLNHHPADIWAAHPSNYIMGNGHVSPPATASGLSPPASRSSNSSAELPTGVTASQHNTYKWMHTKRSQRPAAPKKKVIDENGTNRTNFTTHQLTELEKEFHTAKYVNRTRRTEIASNLKLQEAQVKIWFQNRRMKEKKREKEKAFLARNTWESNSPTSSCSGEDVKNFK", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQPRGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLAGHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQFYELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTFEEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFSREEIYQLNSDKIIESNKVKASL", "text": "FUNCTION: Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (PubMed:7649182, PubMed:10655068, PubMed:11060359). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2- (4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (PubMed:7649182, PubMed:10655068, PubMed:11060359). SUBCELLULAR LOCATION: Peroxisome Mitochondrion. SIMILARITY: Belongs to the CoA-transferase III family."}
{"protein": "MTTTTIQFNALLLDIEGTITSISFVKDELFPYAFENVGNYLEEHYDNPATQIIVEDLRHIADQQAENDVAVVRIREPRKECIEDVTKNVRHWIKRDKKLTPMKALQGLIWEEAYQRGDVKGHVYPDVLPVLKIVENRKIPIYIYSSGSVHAQKLLFANSIEGDMTKILYGYFDTNIGLKGESNSYTKISERIKIPPSEILFLTDVEAEAAAAKKAGLQTKLVVRPGNAGLTQEAINAYGTIESLEEIL", "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": "MIPYRSRTSTHGRNMAGARGLWRATGMTDSDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEAAGGVAKEFNTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMVNAHCADAMVCISNCDKITPGMMMAAMRLDIPVVFVSGGPMEAGKVNIDGELRAVDLIDAMIEAANPDRTDAEVDEFEKNACPTCGSCSGMFTANSMNCLAEALGLALPGNGSTLATHADREALFRRAGRRIVELTKAYYEGGDTGVSARGIATKAAFENAITLDIAMGGSTNTILHLLAMAREGEVDFTLADIDRLSRVTPCLCKVAPAVQNVHMEDVHRAGGIFGILGELGRAGKLDTSVRTIHEDTMAEALSKWDIAVTNNPEVQELFLAAPGGVRTTQAFSQARRYKDLDTDREKGVIRSAKHAFSKDGGLAVLFGNIAEMGCVVKTAGVDDSILKFSGPAVICESQEEACERILKKRVKAGDVVIIRYEGPRGGPGMQEMLYPTSYLKAMQLGKECALITDGRFSGGTSGLSIGHVSPEAAEGGAIGLLHEGDIIEIDIPNRTINAKVSAEEFAKRRAEMDAKGAAAWKPVEERPRKVSRALKVYAAHVGNASLGAVRLDP", "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": "MHCPFCRHPDSRVIDSRETDEGQAIRRRRSCPECGRRFTTVETAVLAVVKRSGVTEPFSREKVISGVRRACQGRQVDDDALNLLAQQVEDTVRAAGSPEVPSHEVGLAILGPLRDLDEVAYLRFASVYRSFESADDFEREIQALREHRGVATPG", "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": "MAPTRLQLGVRAAYSGFSSLAGFSIFFVWTVVYRQPGTAAMGGLAGVLALWVLVTHVMYMQDYWRTWLRGLRGFFFVGALFSAVSFSAFCTFLTLAITQHQSFKDPNSYYLSCVWSFISFKWAFLLSLYAHRYRADFADISILSDF", "text": "FUNCTION: Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment. 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). 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": "MAIGKRLKKVREGIDRTKLYPIAEAIKMVKERAVSKFDETIEIAFNLGVDPRHADQMVRGVVSLPNGTGRTLRVGVFARGAKADEARAAGADVVGAEDLVEKVQGGTIEFDRCIATPDMMPLVGRLGKVLGPRGMMPNPKIGTVTMDVAGAVAGAKGGNVEFRVEKAGIVQAGIGKASFSEEKLVENIKALTDAVSKAKPAGAKGTYIQRVAVSSTMGPGVKVEPGTILG", "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": "MSNTTVEQFAAELKRPVEDLLKQLKEAGVSKNSGSDSLTLDDKQLLNAYLTKKNGSNSSTISIRRTKTEVSTVDGVKVETRKRGRTVKIPSAEELAAQVKAAQTQAAPVRPEQTAEDAAKARAEAAARAEARAKAEAEAAKLKAAKAGNKAKPAAQKPTEAKAETAPVAAETKPAEESKAEKAQADKMPSEKPAEPKEKAAKPKHERNGKGKDAKKPAKPAAPAVPQPVVSAEEQAQRDEEARRAAALRAHQEALLKEKQERQARREAMKQQAEQQAKAAQEAKTGRQRPAKPAEKPQAAAPAVENKPVNPAKAKKEDRRNRDDEGQGRNAKGKGGKGGRDRNNARNGDDERVRGGKKGKKLKLEPNQHAFQAPTEPVVHEVLVPETITVADLAHKMAVKGVEVVKALMKMGMMVTINQSIDQDTALIVVEELGHIGKPAAADDPEAFLDEGAEAVEAEALPRPPVVTVMGHVDHGKTSLLDYIRRTKVVQGEAGGITQHIGAYHVETPRGVITFLDTPGHEAFTAMRARGAKATDIVILVVAADDGVMPQTIEAIAHAKAAGVPMVVAVNKIDKEAANPERIRQELTAHEVVPDEWGGDVQFIDVSAKKGLNIDALLEAVLLEAEVLELTAPVDAPAKGIIVEARLDKGRGAVATLLVQSGTLKKGDMLLAGTAFGKIRAMVDENGKSITEAGPSIPVEILGLSDVPNAGEDAMVLADEKKAREIALFRQGKYRDVRLAKQQAAKLENMFNNMGETQAQSLSVIIKADVQGSYEALAGSLKKLSTDEVKVNVLHSGVGGITESDVNLAIASGAFIIGFNVRADASSRKLAENENVEIRYYNIIYDAINDVKAAMSGMLSPEEKEQVTGTVEIRQVISVSKVGNIAGCMVTDGVVKRDSHVRLIRNNVVIHTGELASLKRYKDDVKEVRMGFECGLMLKGYNEIMEGDQLECFDIVEVARSL", "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": "MSQADMTCSARQRVFQEALRKGNTKELHSLLQNMTNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADTRLANRDGWSALHIAAFGGHQDIVLYLITRAKYSSSAL", "text": "FUNCTION: Regulates independently canonical Wnt and Notch signaling by modulating LEF1 and Notch protein turnover. Stabilizes LEF1, a pivotal transcription factor in the Wnt signaling cascade, by blocking its ubiquitination. Involved in angiogenesis; involved in intersegmental vessel patterning during development. SIMILARITY: Belongs to the NRARP family."}
{"protein": "MFSKNKHNTKFIVIACVIVVLILILFCFDFQNIQEIIETINQLTNNQNPSKNTASEMSGMRRKIIFFIFNFFGKIILASFIISFLLHIKKNAQIKRLKNKLSLWSKLSFHVSQIGEEVLNELPIGIVLIDISSQEIQWLNPYASFILKNPEINSPLTQINENMAQLISTSDTIPKTIITLKNQKFECFYKKDLSVFYLFDATEKEQIKHLFLQKTLAIAMIAFDNLAESLIRYDLSEQSQIQGEYLSALSDYIEPYESYLKQLIDDRFLLLLNRQNLDKMLENKFSILDTIRNISHKYQLKVTLSMGIACWNLSYEKLATYSQNAIELAQKRGGDQVVVNIENEKIKYFGAKIASLSKQSKVHARINAQNLVDILKKNPHCFIMGHTHTDLDALGSVIAFYKIAATIHPENNNYIILDEEKLDKSLIPVYHQLIKTESKKTLNIITTQQASKMIKDNSLIAVLDTQTKDMLNSPELLSLTPNIVVVDHHRATEEIIPSIFSYVESSASSTVELLVEVMGFLEKEVHITAFEASIMYAGILIDTNAFIYRTSSRTFEVASKLKDLGADAIEVKSWLRKDFDKVLEINKLISEMEIFMDRFAIIQSSEIYENRSFLAQVAESVLNIQNVDAAFMIAKIADNKIAISARSYNEINVQTIMEQMEGGGHLNSAATQLEGTNIKTVTDTLKHFLKLEYEKGEKNMEIILLTDISNKGKKHEIIKVNNGYGNFLIQNKKALLADKANLAVIKQTQILEQEQKRNHELLMQKLKQEIDDKKITLDIQLGPKGKIYGKITLKQISEEFLKVHNITLDRKKISLESEIIAIGIYPVDVFLTDQIKATFFLNVTERKSK", "text": "FUNCTION: Binds to the 23S rRNA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MATINQLVRKPRKDKMKKSNVPALEACPQRRGVCTRVYTTTPKKPNSALRKVARVRLTNGYEVSSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGSLDCAGVDGRKQGRSKYGAKRPKG", "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": "MSKVKIELFTSPMCPHCPAAKRVVEEVANEMPDAVEVEYINVMENPQKAMEYGIMAVPTIVINGDVEFIGAPTKEALVEAIKKRL", "text": "FUNCTION: Acts to maintain redox homeostasis; functions as a protein disulfide reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family."}
{"protein": "MRGSGPRGAGRRRTQGRGGGGDTPRVPASLAGCYSAPLKGPLWTCLLLCAALRTLLASPSNEVNLLDSRTVLGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDENGRNIKDNQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHLAVFPDTITGADSSQLLEVSGSCVNHSVTDDPPKMHCSAEGEWLVPIGKCMCKAGYEEKNGTCQVCRPGFFKASPHSQTCSKCPPHSYTHEEASTSCVCEKDYFRRESDPPTMACTRPPSAPRNAISNVNETSVFLEWIPPADTGGGKDVSYYILCKKCNSHAGVCEECGGHVRYLPQQIGLKNTSVMMADPLAHTNYTFEIEAVNGVSDLSPGTRQYVSVNVTTNQAAPSPVTNVKKGKIAKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETTITAEGLKPASVYVFQIRARTAAGYGVFSRRFEFETTPVFGASNDQSQIPIIGVSVTVGVILLAVMIGFLLSGSCCECGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPTQAVHEFGKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVATKTLKVGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGMLRGIAAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLPSPMDCPAALYQLMLDCWQKDRNSRPKFDDIVNMLDKLIRNPSSLKTLVNASSRVSTLLAEHGSLGSGAYRSVGEWLEATKMGRYTEIFMENGYSSMDAVAQVTLE", "text": "FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI- anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino- hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Cell projection, dendrite. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily."}
{"protein": "MSELTTVARPYARAAFEFAVDSNKIEAWSEMLFFTAEVVNNPTMVKILTSDKTAQELAELFLNVCEDQLDENGQNFIKIMAENGRLRFLPRVAQLFAALEDEHKKQVDVNVVSAYGLSKKQLDELSKSLEKRLARKVNLHCSIDKTLIAGMVVTVGDLVIDSSAKGQLGRLSNTLQS", "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": "MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENELCVICARKLTYVSLTPCHHKTCHICGFRQRALYNKKSCLICRTENEEVMFTDRIDGDISDKYNFCEKNEKYGINFTSEEVATETLNLLKFFCPLSKDEQVCDFGSFKKYNEHLKSEHNRMICLICATHKHAFPCELEIFTQNQLRNHQTKGNSEGFKGHPMCAFCSGKRFYSDDELYIHMRNQHEKCHICDKMNPASPQYFKDYNQLFDHFKHSHYVCTVQTCLDNKFVVFKDELELQAHILQEHGNILKGKPKFFQSELSTFISAPSRVIRERDDYDLPSISSLPGSSSGSRTDVRSASSPEESRLRLAERAKYYLENSKEDFNKFSSYNEDYSKGRLSAEKLLESYKLLFTKPNADVYLLIHNLAETFPKNSSKYNNLNAIYEQREQTLARQTSLPSLSSDSSLSMSIGRGHWGGTNDGGSAGAALGVRNIKNLPTLKSPSASYDPFATTVKKNTLRPVQNIKRTTPQSVSYRTSTNTVAFSPTYLESKKGSSSTSLNNSKDKLKSLNLPQLPPPKPKVQIPGLNRPQIADPKQWGKKSSTQDTNVHDNLRELNTTSGGNKKKGKQKQLLFHIGV", "text": "FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, leading to degradation of nascent peptide chains (PubMed:28757607, PubMed:28223409, PubMed:30609991, PubMed:31819057, PubMed:31532761, PubMed:32615089, PubMed:32203490, PubMed:33338396, PubMed:36627279). HEL2 is activated when ribosomes are stalled within an mRNA following translation of prematurely polyadenylated mRNAs (PubMed:28757607). Acts as a ribosome collision sensor: specifically recognizes and binds collided ribosome and ubiquitinates the 40S ribosomal proteins RPS20/uS10 and RPS3/uS3 (PubMed:30609991, PubMed:31819057, PubMed:32615089, PubMed:32203490). Catalyzes 'Lys-63'-linked polyubiquitination of RPS20/uS10, promoting recruitment of the RQT (ribosome quality control trigger) complex, which drives the disassembly of stalled ribosomes, followed by degradation of nascent peptides (PubMed:30609991, PubMed:31819057, PubMed:36627279). HEL2 also acts as an activator of the No-Go decay (NGD) pathway by mediating polyubiquitination of monoubiquitinated RPS3/uS3 and RPS7/es7: RPS3/uS3 and RPS7/es7 are first monoubiquitinated by MAG2 and MOT2/NOT4, respectively, and HEL2 mediates formation of 'Lys-63'-linked polyubiquitin chains on monoubiquitin, leading to activation of the NGD pathway in a CUE2- mediated endonucleolytic cleavage (PubMed:28943311, PubMed:30893611, PubMed:30609991, PubMed:30718516). Polyubiquitination of RPS3/uS3 also triggers degradation of non-functional 18S rRNA (PubMed:30893611, PubMed:30718516). The RQC pathway and the integrated stress response (ISR) antagonize each other: HEL2 prevents the activation of GCN2, while GCN2 suppresses RQC activation (PubMed:32615089, PubMed:33338396). The RQC pathway functions as a preventive quality control in the secretory pathway: HEL2 binds preferentially to the pre- engaged secretory ribosome-nascent chain complexes and prevents mistargeting of secretory proteins into mitochondria (PubMed:33761353). Independently of its role in RQC, also involved in the polyubiquitination and proteasomal-degradation of excess histone proteins (PubMed:22570702). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ZNF598/HEL2 family."}
{"protein": "MSASLARGMLHKMGGSCCPHHAPTTNPFRMAKLHGNNKSTDYAFEMVCSTLRFGKGVTLEIGYDVRNLGAKKTLLITDKNVQNTIAFKNAEQALKMVNIEYEIFDDVLIEPSEKSMQKAIAFAKSKPFDSFIAVGGGSVIDTTKAAALYASNPEADFLDFVGPPFGKSLQPKNPMLPLIAVPTTAGTGSETTAAAIMDLPEHKCKTGIRLRCIKPYLAVVDPLNVMSMPRNVAIYSGFDVLCHALESYTALPYDQRSPRPARPEVRPVYQGSNPISDVWSREALRIIGQYFRRSVFDPSDEEARTEMLKASSFAGIGFGNAGVHLCHGLSYPISSQAKGCVAHDYPQDKNLIPHGLSVMTTAVADFEFTTAACPDRHLVAAQTLGADIPNNADNEYISRTLCDQLRGFMKDFGVPNGLKGMGFEYSDIDHLTEAASHSVPNIVISPKSTDRDIISKLYEKSLTVY", "text": "FUNCTION: Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2- KG as hydrogen acceptor, resulting in the formation of D-2-HG. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily."}
{"protein": "MAVRKLKPTTPGQRHKIIGTFEEITASVPEKSLVYGKKSSGGRNNEGKMTMRYIGGGHRKVIRIVDFKRNKDGVPAVVKTIEYDPNRSARIALLYYADGEKRYIIAPNGLQVGATLMSGETAAPEIGNTLPLQNIPVGTVIHNIELRPGQGAALVRSAGNFAQLTSREGKYCVIKLPSGEVRQILSTCKATIGSVGNSDHGLERSGKAGRSRWQGRRPRNRGVVMNPVDHPMGGGEGRSSGGHPRSRKGLYAKGLKTRAPKKQSSKYIIERRKK", "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": "MAANDTIADMLTRIRNANLARHQTTQVPATKMTRSIAKVLREEGFIAEIEEAEEGVKHNLVISLKYKGKNRQPLITALKRVSKPGLRVYSNRKELPRVLGGIGIAIISTSSGIMTDREARRQNLGGEVLCYVW", "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": "MANVVVVGAQWGDEGKGKIVDWLSEQADVVVRFQGGHNAGHTLVVGEAVYKLSLLPSGVVRPNTLGVIGNGVVLDPYALASEIDRLAGQGVTVSRENLRVADNATLILSLHRELDALREDGAPGTKIGTTKRGIGPAYEDKVGRRAIRLMDLAEPETLPPKIERLLAHHNALRRGFGLEEISEQTILDELTGIAERVLPYQDTVWRLLDDARRGGKRILFEGAQGALLDVDHGTYPFVTSSNTVAGQAATGSGLGPRAIGYVLGIAKAYTTRVGEGPFPTELHDEIGQRIGERGHEFGTVTGRKRRCGWFDACLVRQTVKTSGIDGIALTKLDVLDGFDEIRVCTAYDIDGQRFDHLPASQAAQQRAVPVYETIPGWSGTTAGARSWADLPAQAIKYVRRIEELIGAPVALLSTSPERDDTILMHNPFED", "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": "MLGRTLREVSAALKQGQVTPTELCKNCLSLIKKTKYLNAYITVSEEVALKQAEESEKRYKQGQSLGDLDGIPVAVKDNFSTTGIETTCASNMLKGYVPPYNATVVQKLLDQGALLMGKTNLDEFAMGSGSTDGVFGPVRNPWTYSKQYRERSRQDAGDDSHWLITGGSSGGSAAAVAAFTCFAALGSDTGGSTRNPAAHCGIVGFKPSYGLVSRHGLIPLVNSMDVPGILTRCVDDTAIVLGTLAGHDPKDSTTVRNPAQPASVPGGMDVSRLCIGIPKEYLVPELSSEVRSLWSQAADLFESEGAKVIEVSLPHTCYSIVCYHVLCTSEVASNMARFDGLQYGHRSGVDVSTEAMYAATRQEGFNDVVRGRILSGNFFLLKENYENYFVKAQKVRRLIVKDFVDVFESGVDVLLTPTTLTEAVPYLEFIKEDNRTRSAQDDIFTQAVNMAGLPAVSVPVALSNQGLPIGLQLIGRAFCDQQLLTVAKWFEKQVQFPVIQLQGLMDDGSLVLENGKLTSASLTQR", "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": "MTIFDNYEVWFVIGSQHLYGPKTLRQVTQHAEHVVKALNTEAKLPCKLVLKPLGTSPDEITAICRDANYDDRCAGLVVWLHTFSPAKMWINGLSILNKPLLQFHTQFNAALPWDSIDMDFMNLNQTAHGGREFGFIGARMRQQHAVVTGHWQDKEAHTRISAWMRQAVSKQDIRQLKVCRFGDNMREVAVTDGDKVAAQIKFGFSVNTWAVGDLVQVVNSISDGDINALIDEYESSYTLTPATRIHGDKRQNVREAARIELGIKRFLEQGGFHAFTTTFEDLHGLKQLPGLAVQRLMQQGYGFAGEGDWKTAALLRIMKVMSTGLQGGTSFMEDYTYHFEKGNDLVLGSHMLEVCPSIAVEEKPLLDVQHLGIGGKEDPARLIFNTQTGSAIVASLIDLGDRYRLLVNCIDTVKTPHDLPKLPVANALWKAQPDLPTASEAWILAGGAHHTVFSHALDLNDMRQFAEMHDIEIAVIDNDTHLPGFKDALRWNDMYYSLKH", "text": "FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. SIMILARITY: Belongs to the arabinose isomerase family."}
{"protein": "MNDQSCVRIMTEWDIVAARQLGRNVAKELGFGTVDQARITTAISELARNIYLYAGKGQIGIEQVADRGKKGLKIIAEDQGPGIPDIRKVMEDGFSTSGGLGAGLPGVKRLMDEFSLNSVAGEGTEIQAIKWLR", "text": "FUNCTION: Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity of the RsbU phosphatase may be stimulated by a long-lived interaction with RsbT and the serine kinase function of RsbT is not required to directly modify RsbU. Also phosphorylates RsbR thanks to its threonine kinase activity, preventing it to phosphorylate RsbT."}
{"protein": "MASGKEIKGKIGSIKNTQKITSAMEMVAASKMKKAQERMASGRPYAQNMLKVIGHIANGNLEYRHPYLEEREVKRVGYIVISTDRGLCGGLNTNEFKLVTQDVKKWREQGVEVDFAALGSKACSFFNRFGGKLLAAESGLGDKPSVSDVVGVVRVMLKAYDEGQIDRVFLVFNDFVNTMTQKPVINQLLPLPKSEDEEYQHRWDYIYEPDPKEILEALMVRYIESQVYQGVVENAASEQAARMVAMKAATDNAGNLIDELQLVYNKARQAAITQEISEIVSGAAAV", "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": "MSTAETPQQPQQQQKLRWGIAWIYSSSNNTIITITDLTGAETVARVSGGMVVRADKDKPSPWAAMQAAYKAAQLALARGINAVHIKVRGPGGYGMKVPGPGASAAIRALARSGLVIGRIEDVTPIPHDTIRPPSGRKGRRV", "text": "FUNCTION: Located on the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MLNILGKRYLFFAISLAMIIPGLIVMAIFGLPLSIDFKGGSLLEVEFASKTLPAPAEVVALYNDLGITDAQVTTTGNNTLLVRSSFIDDDVRAKVVQEMNSRFNDTVTVLRFDSVGPTIGKEVAGRATLAVSIAALAVIIYITWAFRGVHNAFRYGVCAIIAMIHDVLVVISLVSIGGVLFGWQVDALFLTALLSVIGFSVQDKVVVFDRIRENSQIYRKLDFEKLANHSIVQTLQRSINTQLMTVEYMLLAIALFGGITLREFAIILLVGLFMGTYSSIFIAAPSLVIWESGEWRNWFKRGAKPASA", "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": "MNSSSNEKNKDLNRKNFSSKTDSSNNKAVVLLSGGLDSTTCLYQAIADGKEIQALSFDYGQRHKIELSYAKKVTRKLGIPHTIQKLKPELFLGSSLTQKSLHVPKNSLRKEEIPNTYVPGRNILFLSFAVSLAEGTGSDSIYIGVNSMDYSGYPDCRPEFIKMFEMAIQLGTKKGSQGPSIKILTPLQNLSKKEIVLLGNQLKVPFHLTFSCYDPKNGKACGKCDACLLRKKGFQETGVSEK", "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": "MKKLYLKTHGCQMNEYDSAKMADVLKFSHGLELTEDPAVADVFLLNTCSVREKAQTKVFSELGRWRPFKEKRPHVVIGVGGCVASQEGETILKQAPFVDIVFGPQTLHRLPDLLDSVIQKRKSVVDITFPEIEKFDRLPQPRAEGPSAFVSIMEGCSKYCTFCVVPYTRGEEISRPFDDVIAEVASLCEQGVREITLLGQNVNDYRGLMHDGQVADLALLIHYLAAMDNIERIRFTTSHPSAFSENLIDAYAEEPKLANHLHLPVQSGSDRILAAMKRNYTVLEYKSKIRKLRAVRPDISLSSDFIIGFPGETDADFEATMNLIHDMGFDHSFSFIYSPRPGTPAAQLPDDVPMAVKKERLAILQNRINAKAAEISQSMVGTQQRILVTGPSKKYPDQLSGRTENNRVVNFNGDTPLIGQMVTIKIKEARPYSLWGEIC", "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": "MSSRYRVEYQLKAHRKDAFIEWIKGLLAVPFVLHSVTERDNAQEKYRRVFEDVETLINEKITVDSDESLTRAAGVSRLDKLVPTIGTFFTPLPLTEAFLRQNARRAISERAYVSPSFNDIRHILNTAQIVQLARAGELSLVTFDGDVTLYEDGASLAAEDKVIGRLLRLLGAGMHVGIVTAAGYDDAENYERRLFGLLRRLERADLPNEAKRRLCVMGGESNFLFRCYERDGRAGFERVPESVWMSAELHQWNQQDINATLDLAEVMLRALREKLRLPAETQIIRKVRAVGIVPGQRFDPELGREIRVPLLRETLEEIVLTVQGRLENFPPAQRVQFSCFDGGSDVWCDIGGKDLGVAFLQRFYSPERPIRPEQSLHVGDQFAPVGSANDFKARLAGCTAWISSPQETVALLDDLLAELEAQKNM", "text": "FUNCTION: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation. SIMILARITY: Belongs to the ISN1 family."}
{"protein": "MSLSPYELEQEWQPRTYVGRLVKEGRIRSLSEIFEKNLPILEPEIVDYLIGPELKSETVDVRLVQKMTDAGRINRFRVVVVIGNENGFVGVGQGKARQLAVAIEKAIRNAKLNIIPVRRGCGSWECLCSEPHSVPFTVRGKSGSVEVILKPAPRGTGLVAGDAAKVVLRLAGIRDVWSFTKGDTRTTINFVKATYNALKQTYKFVTPLDWART", "text": "FUNCTION: With S4 and S12 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
{"protein": "MLNILLTLVFSLIGLVIGYAVISARLKKAKETAELTLLNAEQDAVNARSKAEMDAEHIKKTAERESKAYKKELLIEAKEEARKYREEIEKEFKSERQELKQMDARLTERAASLDRKDENLSSKEQLLDSKEQSLSDKSRHIDERELQVKQLEVKKAEELEKIASLSQEQARGIILSETEKNLAHDIANRIKEAEREIKDRTDKTAKDLLAQAMQRLAGDYVAEQTITTVHLPDDSMKGRIIGREGRNIRTLESLTGIDIIIDDTPEVVVLSGFDPIRREIARMTLEALIQDGRIHPARIEELVEKNRLEMDNRIREYGEAAAFEIGAPNLHPDLIKLMGRLQFRTSYGQNVLRHSVEVGKLAGLLASELGENVDLARRAGFLHDIGKAIDREVEGSHVEIGTEFARKYKENPVVINTIASHHGDVEAQSVIAVLVAAADALSSARPGARNESMENYIKRLRDLEEIATSFDGVQNSYALQAGREIRIMVQPEKLSDDDVTILAHKVREKIENNLDYPGNIKVTVIRELRAIDYAK", "text": "FUNCTION: Endoribonuclease that initiates mRNA decay. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RNase Y family."}
{"protein": "MVSIRPDEISAILKQQIEDYDKSVSVSNVGSVLTVGDGIARVYGLQQAMAGELLEFEDGTEGIALNLEDDNVGAVLMGEGLGIQEGSTVKATGKIASVPVGEAMLGRVVNSLGRAIDGKGEIATSETRLIESMAPGIIQRKSVHEPMQTGITAIDAMIPVGRGQRELIIGDRQTGKTAIAIDTILNQKDQDMICVYVAVGQKAASVANVVEVLRERGALDYSVIVAANASEPAALQYLAPYTGASIAEYFMYKGKATLVIYDDLSKQAAAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDAMGKGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSSDLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFAELAAFSQFASDLDASTQQQLERGKRLRELLKQPQFSPLILAEQVAIVYAGVKGLIDAVPVDKVVDFSRELREYLKSNKPEFITEIQEKKLMSPEAEAILKDAISEVVSTLVASAA", "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": "MSLADSVLAVNNDLPIRTDSPVHSGKVRSVYWLTDADSRRLIKTKGYNVPEDTPLAIMVISDRISAFDCIFHGEGGLKGIPGKGAALNAISNHWFKLFAENGLADSHILDIPHPFVWIVQKARPIKVEAICRQYITGSMWRAYSKGERVFCGITLPEGLEKDQKLPDLLITPSTKGILTGIPGVPAQDDVNISRSDIEANYQAFGFEKLEDIDLYEKLLKDGFKVISKALADIDQVFVDTKFEFGYVTDKDGNSKLIYMDEVGTPDSSRIWDGAAYRDGKILENSKEGFRQFLLNHFPDPDVLLNKDRMPEREALARDNDLPLEAMMQVSRTYTGVAEKVTGAAIPLPANPKADIIKILREEYDLIL", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MTLGAATANDPIDSTLASPSRDEQRRQANQAAFSRDLEFLSSLANPYYLNHLALSGALSSPSFKRYLKYLDYFRHPKYVKYLHYPQALHFLDLLQNEEEFRLACRDPAFAGEVMAKQIGHWATWRDPENAAGQEQDEAGEQGEARETTGGQTA", "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": "QTCASRCPRPCNAGLCCSIYGYCGSGNAYCGAGNCRCQCRG", "text": "FUNCTION: Has antifungal activity against P.infestans, A.lycopersici, V.dahliae, G.zeae, A.nicotianae, F.moniliforme, F.oxysporum and C.gossypii."}
{"protein": "MIPTIAILSGGFSCEREISLMSGKAVKKALDSLSYNAIEIDVDSNIAEKLKKINPGLAFIALHGPYGEDGCIQGLLEILGIKYTHSGVMASAVAINKVMSKHIFRSLNIDTPKGYVISREDVLKNNIKIDYPYVLKPINEGSSIGVYIIFSHEDYLELKNNSSTIMEKMIVEEYIPGIELHTAVLLDEAIGTIEVRPKNKFYDYEAKYTDGFAEHIFPAKIPDNIYKMTLEHALKIHQFLGCKTISRSDFRYNPKNNTLKMLEINTHPGFTELSLVPEIAKLAKGINFNELVKIIIEDSLQHKNIRDLSHVEQYY", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MSENAQLNGLCDRFRGFYPVVIDVETAGFNAKTDALLEIAAITLKMDEHGWLMPDETLHFHVEPFEGANLQPEALAFNGINPHDPQRGAVSEYDALHAIFKMVRKGMKESDCSRAIMVAHNATFDHSFTMTAAERAGLKRNPFHPFVTFDTAALSGLALGQTVLSKACIAAGMPFDGAQAHSALYDTEQTAQLFCEIVNRWKRLGGWPLPVATPE", "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": "MMKNPIIGRVWKFGDDIDTDVIIPGKYLRTKDMQIFAAHAMEGIAPEFTKKAKPGDIIVAGENFGCGSSREQAPLAIKHAGIACVVAKSFARIFFRNAINVGLPLMEADIECQEGDEIEVDLLKGEVRVPGKGVFVGNKLPDFLLDILTDGGLVSHRKKAQNEQKE", "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 LeuD family. LeuD type 2 subfamily."}
{"protein": "MALRTLASKKVLSFPFGGAGRPLAAAASARGVTTVTLPDLSYDFGALEPAISGEIMRLHHQKHHATYVANYNKALEQLETAVSKGDASAVVQLQAAIKFNGGGHVNHSIFWKNLKPISEGGGEPPHGKLGWAIDEDFGSFEALVKKMNAEGAALQGSGWVWLALDKEAKKVSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA", "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": "MRFCLVFIRLAAFVILSGGATSTTTDNDDTRLLQTSNIETAAVANVLHVMQSSESSKRLLRLNDQADISGHDEERSSLIEKGWKKLRKLIKKVWKYVKKPFKKTAKIIKKPFKSRTKNIHIVYYKSRF", "text": "FUNCTION: Secreted effector that suppresses pattern-triggered immunity (PTI) in plant host. SUBCELLULAR LOCATION: Secreted Host cell membrane Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MKKFLLKPKKSLGQNFILSSEITKRIVVLAGNLEDFNVIEIGPGYGALTKEILAHNPKSLLAIEKDSNLVKCHDQLLNEHQGKFRIVEADALYVVEEELIERPVKVIANLPYNISLALFLKWLNKIKLFTTFTLMFQKEVADRIIARPNSKDYGSLSVLSQLLCDIRREFDIEPKEFFPRPKVYSSVITVKPLPTQRFAVNLEALTKLTRAVFAQRRKMLRNSLQNVTNRTETALENAKLSGNERPKNLTVEQFCLLANNM", "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": "MLVPPDMLVAQTRMIYQMNRYCAERVQARMFKTSTAIREICKIVQDILKEVELQEPRFISSLVECNGRFEGVEVISPNEFEIVLYLNQMGVFNFVDDGTLPGCAVLKLSDGRKRSMSLWVEFITASGYLSSRKIRSRFQTLVAQACDKSMYRDMVKIIGDTTEVKLRIRERYVVQITPAFKCSGIWPRSAAHWPMPHIPWPHPNIVAEVKTEGFDLLSKDSAAMQNKNNNAASMEGDAWVLSFYEAENRLLQGGCRRRCLSMLKTLRDRHLELPGSPISAYHLKNLLLYECEKHPRDYEWDESCIADRINGIFLQLISCLQYRRCPHYFLPSLDMFKGKSPSALEQAAKQVWRLTREMLTNANAFEKL", "text": "SIMILARITY: Belongs to the mab-21 family."}
{"protein": "MKVGIIMGSKSDWPTMKLAAEMLDRFNVPYETKVVSAHRTPQLLADYATQAKDRGIKVIIAGAGGAAHLPGMAAAFTSVPVLGVPVQSRALKGMDSLLSIVQMPKGIAVGTLAIGEAGAANAGILAAQIIGTSNEEVMAAVEAFRKEQTEMVLENPDPSED", "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": "MSRRNPCKFEIRGHCLNGKRCHFSHNYFEWPPHALLVRQNFMLNRILKSMDKSIDTLSEISGAAELDRTEEYALGVVGVLESYIGSINNITKQSACVAMSKLLTELNSDDIKKLRDNEELNSPKIRVYNTVISYIESNRKNNKQTIHLLKRLPADVLKKTIKNTLDIHKSITINNPKESTVSDTNDHAKNNDTT", "text": "FUNCTION: Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription (PubMed:19386701, PubMed:22675274). Transcription anti-terminator that enhances readthrough of intergenic junctions during viral transcription (PubMed:10364337, PubMed:27194388, PubMed:8552680, PubMed:9420254). Preferentially binds to poly(A)-rich sequences (PubMed:24434552). Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (PubMed:18579594). Also, can activate host NF-kappa-B through association with host RELA (PubMed:15629770). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus Note=Localizes in cytoplasmic inclusion bodies substructures called inclusion bodies associated granules (IBAGs) (PubMed:22675274, PubMed:28916773, PubMed:29489893, PubMed:31649314). Forms a layer between the matrix and nucleocapsid (PubMed:23776214, PubMed:24760890). SIMILARITY: Belongs to the pneumoviridae M2-1 protein family."}
{"protein": "MTLQEQIMKALHVQPVIDPKVEIRKRIDFLKDYLKTTGAKGFVLGISGGQDSTLAGRLAQLAVAEVRNEGGNATFISVRLPYKVQKDEDDAQLALQFIQADQSVAFDIASTVDAFSNQYENLLDESLTDFNKGNVKARIRMVTQYAIGGQQGLLVIGTDHAAEAVTGFFTKFGDGGADLLPLTGLTKRQGRDLLQELGADERLYLKMPTADLLDEKPGQADETELGITYDQLDDYLEGKSVPADVAEKIEKRYKVSEHKRQVPASMFDDWWK", "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": "MEANASVDMFSKVLENQLLQTTKLVEEHLDSEIQKLDQMDEDELERLKEKRLEALKKAQQQKQEWLSKGHGEYREIPSERDFFQEDKESKKVVCHFYRDSTFRCKILDRHLVILSKKHLETKFLKLNVEKAPFLCERLRIKVIPTLALVKDGKTQDFVVGFSDLGNTDDFTTETLEWRLGCSDILNYSGNLMEPPFQSQKKFGTNFTKLEKKTIRGKKYDSDSDDD", "text": "FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Midbody Note=Co-localizes with beta-tubulin in the centrosome."}
{"protein": "MSQAVETRTRIKSERYESGVIPYAKMGYWDPEYSIKETDILALFRCTPQPGVDPVEAAAALAGESSTATWTVVWTDLLTACDLYRAKAYRVDPVPSAADTYFCYIAYDIDLFEEGSLANLTASIIGNIFGFKAVKALRLEDMRMPYALLKTYQGPATGLIVERERLDKFGRPLLGATVKPKLGLSGKNYGRVVFEGLKGGLDFLKDDENINSQPFMRYRERFLYSMEGVNHAAAVSGEVKGHYLNATAATMEDMYERAEFAKDLGSVIVMIDLVIGYTAIQSMAIWARKTDMILHLHRAGNSTYSRQKSHGMNFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYNTLLEFKSDINLPQGLFFAQDWASLRKCVPVASGGIHCGQMHQLINYLGDDVVLQFGGGTIGHPDGIQAGATANRVALECMVIARNEGRDYISEGPQILRDAAKTCGPLQTALDLWKDITFNYASTDTADFVETPTANR", "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": "MPTYNQLVRFERKSKVRKTKSPALEANPFKSGVCLVVKTVTPKKPNSALRKVATVRLSNKRTVNVYIPGEKHSVKEHDRVLVRGGQVPDLPGVKYHVVLGAYDIAGVKGRKQGRSRYGAPRKQVVATKK", "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": "MAKSIPSAGLRLRLRLRRNARRRSRKSTRKIPKGVIHVQASFHNTIVTVTDVRGRVISWSSAGTCGFKSTRKGTPFAAQTAAGDAIRPVVDQGMQRAEVRIKGPGLGRDAALRAIRRSGIRLSCIRDVTPLPHNGCRPPKKRRV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED", "text": "FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue (PubMed:30661771). This is the first 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 synthase family."}
{"protein": "MGPVVPVEAFRSAGKISALGAKKGYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAILPDVPEEHRELLRSQGCIVKEIEPIYPPANQIQFAMAYYVINYSKLRIWNFEEYSKMVYLDADIQVYENIDHLLDTPDGYFYAVMDCFCEKTWSHSRQFSIGYCQQCPNKVTWPAQMGSPPPLYFNAGMFVFEPSKTTYQTLLHTLRITPPTPFAEQDFLNMFFEPIYKPIPLVYNLVLAMLWRHPENVELEKVQVVHYCAAGSKPWRYTGQEANMDREDIKMLVKKWWDVYNDESLDFKAEDSIAGEETFSMPSFIASLPEPAVSYIPAPSAA", "text": "FUNCTION: Major galactinol synthase mainly involved in the biosynthesis of storage raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyltransferase 8 family. Galactosyltransferase subfamily."}
{"protein": "MSHAIDELQAIIADLKTELETEPKSSVGVASNSRLARDRIDRMSAEVVDSNPYSRLMALQRMNIVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELDNMNRLFFTPDQAGLSKVAAAAATLSFINPDVEIETHNYNITTVENFDRFLDTISQGGRIAGQPVDLVLSCVDNFEARMAINAACNERNLNWFESGVSENAVSGHIQFIRPGDTACFACAPPLVVAENIDEKTLKREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSDYLGYNALSDFFPKMTLKPNPQCDDRNCIVRQKEFQARPKPVVIEEKAVSEEPLHATNEWGIELVAEDAPQSNPTPAETPVMGEGLRLAYEAPEKSSETSEETVTAATADETSLEDLMAQMKSM", "text": "FUNCTION: E1-like enzyme which activates UFM1. SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5 subfamily."}
{"protein": "MVDPQFASNFYFDQRLNIDAVKLLPGEYFVTTREMVLSTVLGSCVSACIYDQQSRIGGMNHFMLPSSENSSGFPIECARFGGYAMGILIRELLKNGARKQNLVAKVFGGGNVQPAMVTSAIGSQNARFVKKYLAEYEIPILAGDLEGFYPRKLHFFPKSGRVLLKKLHVSHNDTIAKREKHYSRLLLSTVKPGI", "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": "MAIDQATVRKIASLARIAISDAEAAAMEGELNGILGWVEQLGEVDVSGVEPMTAVIPNTLRLRDDVVDADPLTGGNRRDDILANAPAAMHGFFGVPKVIE", "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": "MSHGTYYECEPRGGQQPLEFSGGRAGPGELGDMCEHEASIDLSAYIESGEEQLLSDLFAVKPAPEARGLKGPGTPAFPHYLPPDPRPFAYPPHTFGPDRKALGPGIYSSPGSYDPRAVAVKEEPRGPEGSRAASRGSYNPLQYQVAHCGQTAMHLPPTLAAPGQPLRVLKAPLATAAPPCSPLLKAPSPAGPLHKGKKAVNKDSLEYRLRRERNNIAVRKSRDKAKRRILETQQKVLEYMAENERLRSRVEQLTQELDTLRNLFRQIPEAANLIKGVGGCS", "text": "FUNCTION: Transcriptional activator (PubMed:26019275). C/EBP are DNA- binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation (PubMed:10359588). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. C/EBP subfamily."}
{"protein": "MGVTELGKLIGKEVRREVKLESLSGKCIALDAYNALYQFLASIRQPDGTPLMDRAGRITSHLSGLFYRTINLLEAGIRPVYVFDGKPPEFKLAEIEERRKTREKAMEEVLRAIKEGRREDVAKYAKRAVFITSEMVDEAKRLLSYMGVPWVQAPSEGEAQAAYMARKGHCWAVGSQDYDSLLFGSPKLVRNLAVSPKRKIGEEVIELTPEIIELDAVLRALRLKNREQLIDLAILLGTDYNPDGVPGVGPQKALKLIWEFGSLEKLLETVLKGAYFPIDPLEIKKFFLNPPVTDQYATEVRDPDEAALKDFLIREHDFSEERVSKALERLRKARGKLKTSSLDSFF", "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": "MRILGIETSCDETAASVVLRDEEGRGRILGDVVLSQLEEHSAYGGVVPEIAARAHVEALDALIEEALLRAGVTLRDIDAVAATSGPGLIGGLIVGLMTGKAIARATGKPLYAVNHLEGHALTARLTDGLSFPYLMLLVSGGHTQLILVKGVGEYERWGTTIDDALGEAFDKTAKLLGLPYPGGPAVERAAQAGNAERFDFPRPLVGDARLDFSFSGLKTAVRQAAQSLGPVTDQDIADVCASFQRAISRTLRDRVGRGLKRFRADFASVDQPALVVAGGVAANQTLRRTLQSLCDEHGFRFIAPPLQLCTDNAAMIAWAGAERLAAGLPADGLDAAPRSRWPLDSEAKALIGSGRRGAKA", "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": "MKGYEVNFDGLVGPTHHYAGLSFGNEASTKNRNNLSNPKLAAKQGLLKMKALADMGMKQGVLAPHERPHVPMLRRLGFTGDDISVVAQAMRYSPELLSSLSSASPMWTANAATVSPSADSQDERVHFTAANLNNKFHRSIEAETTSQVLQAIFKNERHFVHHEALPQVALFGDEGAANHNRLGGDYAKRGIQVFVYGQQHLNNGLPGPKRYPARQTREASEAIARLHRLDDAHTVFVQQNPDVIDQGVFHNDVIAVSNQQVLFHHQHAFLNQDQAFAEIRQKMASIGEDFISIEVPENRVTVDDAVATYLFNSQILTRPDGGMTIVVPEESRQNAAVWSYLNDMIQMGTPIDAIQVYDLRESMRNGGGPACLRLRVALNETELNAVNPKVLMNDQLFMTLNQWVDKHYRDRLAQEDLADPHLLMESRMALDELTKILGLGSVYPFQK", "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": "MIITQTSHCYMTSLGILFLINILPGTTGQGESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALEMKKKTPAAPAKKTSTTFNIVGTTYPINLAKDTEFSTISKGAAPSASSTPTIIASPKATYVQDSPTETKTYNSVSKVDKISRIIFPVLFAIFNLVYWATYVNRESAIKGMIRKQ", "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": "MTTANVEQKVKNIIADQLGVGEDEIKITSSFIEDLGADSLDIVELVMAMEEEFEVEIPDEEAENIKTVQDAVNYITTHKK", "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": "MMKGISSVSQSINYNPYIEFNRPQLQISTVNPNPAQSRFSRPRSLRVLSLSADPSANRNPKSAVDAHAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSVLKLLKFSI", "text": "FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (By similarity) (PubMed:27601466). Can also use xylose and fructose as carbohydrate substrates with a low efficiency (PubMed:27601466). Can use GTP, and, to a lower extent, CTP and UTP as alternative phosphoryl donors (PubMed:27601466). SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid. SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily."}
{"protein": "MFKKFDEKENVSNCIQLKTSVIKGIKNQLIDQFPVIEPWLNQIMPKKDPVKIVRCHEHIEILTVNGELLFFRQREGIFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYPAAVDTVVAIMAEGKQHALCVGVMKMSADDIEKVNKGIGIENIHYLNDGLWHMKTYK", "text": "FUNCTION: Plays a role as translation enhancer and involved in cell cycle regulation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MCTS1 family."}
{"protein": "MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGIFFPEKVSVIGNGMVVNPKSLVEELDYLHQEGVATDNLRISDRAHIILPYHIKLDQLQEASKGDNKIGTTNKGIGPAYMDKAARVGIRIADLLDKDIFAERLKANLAEKNRLFEKMYESSPVAFDTIFDEYYAYGQKIKDYVTDTSVILNKALDKGRRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDQTGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNCIDVLSGLDIVKICVAYDLDGKRIDHYPASLEQLKRCKPIYEELPGWSEDITGVRSLEDLPENARNYVRRVSELVGVRISTFSVGPDRDQTNILESVWGL", "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": "MNNEWLNAYVLHRRPYRETSYIVDFFSLEEGRISAVAKGVKNSKSDKKSLLQPFQHLRLQLSGKSDLKNLRHVESVAPSISLTGTALFCAMYVNELTNRIMPQGLASDGVYSAYEAALLALRDEADIEVTLRQLEFALLDEMGLLPDFTSDVEYEMPIEENGRYHFQLDAGFIQIPDDVVGARGIPGTALLSLSQGEFTPLSKKVAKVLCRDLLKPLIGDKPLKSRELFMTKPR", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family."}
{"protein": "MSDIDQRLREDVHLLGELLGETIRQQHGEAFLQKIEDIRHSAKADRRGEGEQLSSTLGDLAEEDLLPVARAFNQFLNLANIAEQYQLIHRRDTDQPEPFEARVLPELLARLKAAGHGNDALARQLARLDIQLVLTAHPTEVARRTLIQKYDAIAAQLAAQDHRDLIPAERQQVRERLRRLIAEAWHTEEIRRTRPTPVDEAKWGFAVIEHSLWQAVPNHLRKVDKALFEATGLRLPLESAPVRFASWMGGDRDGNPNVTAAVTREVLLLARWMAADLFLRDIDYLAAELSMQQASGALREQVGDSAEPYRALLKQLRDRLRATRAWAHASLAGPQPASAAVLVDNRDLIAPLELCYQSLHACGMGVIADGPLLDSLRRAVTFGLFLVRLDVRQDAARHRDALSEITDYLGLGRYADWDEERRIEFLQHELKNRRPLLPAHFKPAAETAEVLATCREIAAAPAASLGSYVISMAGAASDVLAVQLLLKEAGLTRPMRVVPLFETLADLDNAGPVMERLLGLPGYRAGLHGPQEVMIGYSDSAKDAGTTAAAWAQYRAQENLVRICREHQVELLLFHGRGGTVGRGGGPAHAAILSQPPGSVGGRFRTTEQGEMIRFKFGLPGIAEQNLNLYLAAVLEATLLPPPPPEPAWRALMDQLAADGVKAYRGVVRDNPEFVEYFRQSTPEQELGRLPLGSRPAKRRAGGIESLRAIPWIFGWTQTRLMLPAWLGWETALSNALARGQADLLAQMREQWPFFRTRIDMLEMVLAKADAQIAEAYDQRLVQPRLLPLGAHLRDLLSQSCQVVLGLTGQQVLLAHSPETLEFIRLRNTYLDPLHRLQAELLARSRSREAALDSPLEQALLVTVAGIAAGLRNTG", "text": "FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SIMILARITY: Belongs to the PEPCase type 1 family."}
{"protein": "MAVAFNRDKPHCNIGTIGHVDHGKTSLATAITIVSSELSGGAVKVKNYDEIDSAPEERARGITIQTAHVEFISKKRHYALVDCPGHVDYIKNMITGASQTDGLILVVSGVDGVMPQTREHVLLAKQVGVPSIIVCINKIDQADPELLELIEMEVRELLTKYDFPGDTVPIIRCSALKAINGDSDAKKGILELMDSIDDYIPQPTRVLDQPFLMPIEDVFSILGRGTVVTGRIERGVIKVGDEVEIVGLRSTQKTICTGVEMFKKELDQGQAGDNVGILLRGIKREDVERGQVLAKPGTITPHCSFEAEVYVLTKEEGGRHTPFFQNYRPQFYCRTTDVTGEIALLSGKEMVMPGDHATLSVNLVAPIAMDQGLSFAIREGGKTIGAGKVSKIIK", "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": "MLPESFFLHDDVLHLAKELLGHILITKISGKITSGFIVETEAYRGPDDKACHAYNYRKTKRNSPMYSRGGIAYIYRCYGMHSLFNVVTAKQDLPHAVLIRAILPYEGEDIMIQRRQWQNKPKHLLTNGPGKVCQALNLTLEHNTHALTSPHLHISKEKASGRITQTPRIGIDYAEECKDLPWRFLLNIKD", "text": "SIMILARITY: Belongs to the DNA glycosylase MPG family."}
{"protein": "MSSAKPINVYSIPELNQALDEALPSVFARLNYERSYALLDAKLYIGYSIAVVAGLSFFLDKKFERDQIVTYQKLLVGAYFVLSLLFWYFSRFIEKGTVYVGKRRGTKEEIYVKTKFEKNEPLYLVELVQKKKGENSKKELKAKLEVNKVFNESGYLQNDAYFKWFSEQHNVLDTKKNE", "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:8910564, PubMed:10921929). Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (PubMed:8910564, PubMed:10921929). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPCS2 family."}
{"protein": "MASPRLGTFCCPTRDAATQLVLSFQPRAFHALCLGSGGLRLALGLLQLLPGRRPAGPGSPATSPPASVRILRAAAACDLLGCLGMVIRSTVWLGFPNFVDSVSDMNHTEIWPAAFCVGSAMWIQLLYSACFWWLFCYAVDAYLVIRRSAGLSTILLYHIMAWGLATLLCVEGAAMLYYPSVSRCERGLDHAIPHYVTMYLPLLLVLVANPILFQKTVTAVASLLKGRQGIYTENERRMGAVIKIRFFKIMLVLIICWLSNIINESLLFYLEMQTDINGGSLKPVRTAAKTTWFIMGILNPAQGFLLSLAFYGWTGCSLGFQSPRKEIQWESLTTSAAEGAHPSPLMPHENPASGKVSQVGGQTSDEALSMLSEGSDASTIEIHTASESCNKNEGDPALPTHGDL", "text": "FUNCTION: Receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, stimulates Ca(2+) influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalizes beta arrestin at the plasma membrane; this ligand-dependent signaling occurs through a G(q)-mediated pathway in melanocytic cells. Its activity is mediated by G proteins which activate the phosphoinositide signaling pathway. Also plays a role as an intracellular G protein-coupled receptor involved in melanosome biogenesis, organization and transport. SUBCELLULAR LOCATION: Melanosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Note=Distributed throughout the endo-melanosomal system but most of endogenous protein is localized in unpigmented stage II melanosomes. Its expression on the apical cell membrane is sensitive to tyrosine (PubMed:18828673). SIMILARITY: Belongs to the G-protein coupled receptor OA family."}
{"protein": "MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQLEATKNSKGTGSGGKTTSGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMDTVELLQAKVGALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQSKVHQLYETIQRWSPIAASLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMIACSLKDNATLLTQVQTTMCENLSTIEGNFANIDERMKKLGK", "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. May play a role in synapse formation during brain development (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": "MTYSPGNPGYPQAQPAGSYGGVTPSFAHADEGASKLPMYLNIAVAVLGLAAYFASFGPMFTLSTELGGGDGAVSGDTGLPVGVALLAALLAGVALVPKAKSHVTVVAVLGVLGVFLMVSATFNKPSAYSTGWALWVVLAFIVFQAVAAVLALLVETGAITAPAPRPKFDPYGQYGRYGQYGQYGVQPGGYYGQQGAQQAAGLQSPGPQQSPQPPGYGSQYGGYSSSPSQSGSGYTAQPPAQPPAQSGSQQSHQGPSTPPTGFPSFSPPPPVSAGTGSQAGSAPVNYSNPSGGEQSSSPGGAPV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.paratuberculosis 34 kDa antigenic protein."}
{"protein": "MFDVEPIIADHKDVIHDVVFDYYGRRMATCSSDQTVKIWDEDGQGKWNVTSSWKAHSGSIWRVSWAHPEFGQVVATCSFDRTASVWEEVIGEKVSSTNTPTRRWVRRTTLVDSRTSVTDVEFAPKYLGLLLATASADGIIRIYEAPDIMNLSQWPVQHEISNKLPLSCLSWNTSTYMVTQLLAAGSDEAATPTGKVFLFAYSENSRKCVKIDTVNDITDPVTDVAFAPNAGRTFHMLAVASKDLYIVNLRGVTDATDISKLDIQTIKFSEHNCPVWRVCWNMLATMLISTGDDGCVRLWRMNYNRQWRCAAVLKAEGSGPTYEPAPPTPTLATTASATAKFYKKGTIGNQVPWH", "text": "FUNCTION: An essential component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823, PubMed:23723238). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823, PubMed:23723238, PubMed:25512509). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation growth under nutrient replete conditions and growth during female oocyte development (PubMed:21521741, PubMed:25512509, PubMed:23723238, PubMed:27166823). This component is required for activating TORC1 specifically in germline cells to promote cell growth and maintain the oocyte fate, probably influences the organization and/or function of microtubules within ovarian cysts, and promotes accumulation of another GATOR2 complex member mio in germline and somatic tissues (PubMed:27166823, PubMed:23723238, PubMed:25512509, PubMed:21521741). GATOR1 and GATOR2 act at different stages of oogenesis to regulate TORC1 in order to control meiotic entry and promote oocyte growth and development (PubMed:25512509). After exactly four mitotic cyst divisions, the GATOR1 complex members (Iml1, Nprl2 and Nprl3) down-regulate TORC1 to slow cellular metabolism and promote the mitotic/meiotic transition (PubMed:25512509). At later stages of oogenesis, the mio and Nup44A components of the GATOR2 complex inhibit GATOR1 and thus activate TORC1 to promote meiotic progression, and drive oocyte growth and development (PubMed:21521741, PubMed:25512509). In addition to its role in the regulation of the TORC1 complex, functions independently of TORC1 to prevent the inappropriate accumulation of autolysosomes in germline tissues (PubMed:27166823). FUNCTION: Probable component of the nuclear pore complex (NPC) (By similarity). Involved in maintaining the localization of another nucleoporin Mtor to the nuclear envelope of early meiotic female germline cells (PubMed:21521741). It is not involved in recruiting the nucleoporins Mtor, Nup107, Nup153 and FG-containing nucleoporins to the NPC (PubMed:21521741). SUBCELLULAR LOCATION: Nucleus envelope Lysosome Note=Enriched on the nuclear envelope of nurse cells, oocytes and syncytial embryos (PubMed:21521741). In egg chambers detected in lysosomes and autolysosomes of both fed and starved females (PubMed:25512509). SIMILARITY: Belongs to the WD repeat SEC13 family."}
{"protein": "MTDNINKESTTTTTTIDHTTNLLIDKHVEYIVKLGSKKDSFEYWVTEHIRMNGMYWGLSSLYLLKSLDKLDKNEVIQWLLSCQKSNGGFGGNTSHDDHLLSTLSAVQILIQYDALDKIDINSVVDYVVKLQREDGSFVGDQWGEVDTRFSYAAIMCLSLLKSLDKINCEKAVEYILSCQNFDGGFGSIPGAESHAGQIFTCVGALSILNEINKIDIDKLGWWLSERQLPNGGLNGRPEKSSDVCYSWWVLSALSAIDRLHWIDNDKLKSYILKCQDNETGGIADKPGDIPDVFHTFFGICGLSLMGYFKDQIESIDPVYALGTKTLQKLGLNLPWNKNL", "text": "FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal. SIMILARITY: Belongs to the protein prenyltransferase subunit beta family."}
{"protein": "MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELVDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSPEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV", "text": "FUNCTION: Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially degrades benzylamine and phenylethylamine. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the flavin monoamine oxidase family."}
{"protein": "MSKDDCIEFEGTVSETLPNTTFRIKLENGHEVTAHISGRMRKNYIRILTGDRVKIEMTAYDLTKGRIIYRMK", "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": "MTNPKKIEMVNDFQQQFAKKMNELGFTYSNIDLYQQAFSHSSFINDFNMDRLAHNERLEFLGDAVLELTVSRYLFDKHPDLPEGNLTKMRATIVCEPSLVIFANKIELNQLILLGKGEEKTGGRTRPSLVSDAFEAFVGALYLDQGLDVVWQFAEKVIFPYVEDDELVGVVDFKTQFQEYVHSQNRGDVTYRLIKEEGPAHHRLFTSEVILENEAVATGQGKTKKESEQKAAESAYSKLKSNNNL", "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": "MAAPGTPPPLAPETAGADSGGGSGEHRQLPELIRLKRNGGHLSEADIRNFVHALMDGRAQDTQIGAMLMAIRLQGMDLEETSVLTQALAESGQQLEWPKAWHQQLVDKHSTGGVGDKVSLVLAPALAACGCKVPMISGRSLGHTGGTLDKLESIPGFSVTQSPEQMLQILEEVGCCIVGQSEKLVPADGILYAARDVTATVDSVPLITASILSKKAVEGLSTLVVDVKFGGAAVFPDQEKARELAKMLVRVGMGLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGAGPPDLRDLVIRLGGAILWLSGQAETQDQGAARVAAALDDGSALHRFQLMLSAQGVDPGLARALCSGSPTQRRQLLPHARKQEELLSPADGIVECVRALPLACVLHELGAGRSRAGQPIRPGVGAELLVDVGQWLSRGTPWLRVHLDGPALSSQQRRTLLGALVLSDRAPFKAPSPFAELVLPPTTP", "text": "FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity). SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family."}
{"protein": "MAHSIEELAITTIRTLSIDAIEKAKSGHPGMPMGAAPMAYTLWTKFMNHNPANPNWFNRDRFVLSAGHGSMLLYSLLHLSGYDVSMDDLKQFRQWGSKTPGHPEYGHTPGVEATTGPLGQGIAMAVGMAMAERHLAATYNRDGFEIINHYTYAICGDGDLMEGVASEAASLAGHLKLGRLIVLYDSNDISLDGELNLSFSENVAQRFQAYGWQYLRVEDGNNIEEIAKALEEARADLSRPTLIEVKTTIGYGAPNKAGTSGVHGAPLGAQEAKLTKEAYRWTFAEDFYVPEEVYAHFRATVQEPGAKKEAKWNEQLAAYEQAHPELAAQLKRAIEGKLPDGWEASLPVYEAGKSLATRSSSGEVINAIAKAVPQLFGGSADLASSNKTLIKGGGNFLPDSYEGRNVWFGVREFAMGAALNGMALHGGLKVFGGTFFVFSDYLRPAIRLAALMGLPVIYVLTHDSIAVGEDGPTHEPIEHLASLRAMPNLSVIRPADANETAAAWRLALESTDKPTALVLTRQDVPTLAATAELAYEGVKKGAYVVSPAKNGAPEALLLATGSEVGLAVKAQEALAAEGIHVSVISMPSWDRFEAQPKSYRDEVLPPAVTKRLAIEMGASLGWERYVGAEGDILAIDRFGASAPGEKIMAEYGFTVDNVVRRTKALLGK", "text": "FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, likely via a covalent intermediate with the cofactor thiamine pyrophosphate. Can use L-erythrulose as donor and D-ribose-5-phosphate as acceptor substrates, forming glycolaldehyde and D-sedoheptulose-7-phosphate. For synthetic purposes, is able to use hydroxypyruvate (HPA) as donor substrate, making the reaction irreversible due to the release of carbon dioxide, and various aldehydes as acceptor substrates, which leads to the corresponding ketoses. Thus, using hydroxypyruvate as donor and three different aldehydes as acceptors, i.e. glycolaldehyde, D-glyceraldehyde and butyraldehyde, the enzyme stereoselectively forms the corresponding products L-erythrulose, D-xylulose and (3S)-1,3-dihydroxyhexan-2-one, respectively. SIMILARITY: Belongs to the transketolase family."}
{"protein": "MQSRRPVMLVILDGWGWREDPADNAVLQAKTPTFDALWTNGPHAFLRTSGKSVGLPNGQMGNSEVGHLNIGAGRVVMQDLPRISDAIANGEIERAPGLVAFIDKLKASGGTCHLMGLVSPGGVHSLQDHACALAKILAKAGVKTVLHAFTDGRDTPPKSAVDDIVRLRAELPPNVPIATVSGRYYAMDRDNRWERVSKAYGVIADADGPRFADANAVIADGYAAGVNDEFIVPAVIGDYQGMRDGDGVLCFNFRADRVREILAALLDSAFAGFPRKQVKQIAAAAGMTQYSTALDALMGTIFPPQSLVNGLGQVVADAGLHQLRMAETEKYPHVTYFLNGGEEVPYPGEDRIMVPSPKVATYDLQPEMSAPELGDKAVAAIESGKYDLIVLNFANPDMVGHTGSLPAAIKAVETVDTQLGHIVAAIRKAGGALLVTADHGNCEMMRDPETGGPHTAHTTNPVPVLLVGDNGPLADGQLSDLAPTLLKLMELPQPAEMTGKSLIG", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family."}
{"protein": "MINKINFVKMHGLGNDFVIVHKRDLATVCNLSQLAKNMADRHTGIGCDQCIIYEEYNNVYTMIIYNIDGSNAKLCGNATRCLAKLIYLDTGKKDITIMVGKKKLLCNVEAANKISVNVGNVSFNETWMPSRDRIWAFAERYMLDLKETMCVDIGNPHLIIFSKLEPQDQKIIGQKLQAKELFVDGVNVNFAEVKDNKIYLSVWERGAGLTLACGSGACGSFAAGLKLGFVHSPSTVVFKYGNLIMQEEDGNIIMQGEATFVMRGEYYCEK", "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": "MKTIEIDCDSGFCFGVMSAIQRAEKELITNDELYCLGDIVHNSQEVVRLQKKGLKIINHEELGRIYNKKVLFRAHGEPPSTYEVANQNSIHIIDATCPVVLQLQKKIQKIYQSFANTKSQIVLFGRSKHAEVSALVGQTNGNAIVIESKNDIQQIDFAKNIYLFSQTTMFVDDFKEIVKEIENKIIHPIIFSSFNTICHQMVNRINHIRKFAVQHNLLLFVAGDNSSNGTILFNECRRANLNTYLISDEKDIQSEWFNGIKSVGICGATSTPKWLMEKIALSLIPFH", "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": "MKSYYFESNEPVSVQQLNNINVLYYPMPMPDYQEKLDQICQERGYKNRDEVKLNENTENLDAKLKIFFEEHLHDDEEIRFILEGSGFFDVRDANDQWIRIRVEKGDLIIVPANMYHRFTLTETKQIHACRLFTDAPKWVPINRHQQ", "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": "MFEQNLTSEALTVTTVTSQDQITQKPLRDSVKASLKNYLAQLNGQEVSELYELVLAEVEQPLLDTIMQYTRGNQTRAATMMGINRGTLRKKLKKYGMN", "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": "MSLLSVMPATTAQQSRAEQVAHHFHWPLVAVEALCPTPLLLWVGPTGLALKSADGKHQHPITAQLQGGSIGLAGPDSWVRGQPLARAVGIKGQHTPTVVDATAGLGGDGWLMARMGCSMHWAERVPLMGLLLQEGLEQAHQDAQRAEVARRVTLHQADAIQLLQNMQEPPQVVYLDPMFPHEGKGSLPRKAMVQLRQLAGEDQDLPQLFELAMATAEQRVVLKRPLKAPLLTRAKPNFQLKGRSTRFDVYATG", "text": "FUNCTION: Specifically methylates the guanosine in position 1516 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family."}
{"protein": "MNPENYLYLSVLLFTIGAAGVLLRRNAIVVFMCIELMLNAANLAFVTFARMHGNLDGQIFAFFTMVVAAAEVVVGLAIIMIIFRSRRSVSVDDADLLKY", "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": "MALLETRTEPMVLNMGPHHPSMHGVLRLIVTLDGENVIDCEPVIGYLHRGMEKIAENRSNVMFVPYVSRWDYAAGMFNEAITVNAPEKLANIPVPKRASYIRVIMLELNRIANHLLWLGPFLADVGAQTPFFYIFRERELIYDLWEAATGQRLINNNYFRIGGVAADLPYGWLEKCIDFCDYFQAKVDEYERLITDNPIFRRRVEGIGVISREEALNWSLSGPMLRGSGVKWDLRRVDHYECYDDFDWDVITAEEGDCFARYRVRVQEMRESLKIIRQACAGIPGGPYENLEARRMAEGKKSEWYGPDYQYVSKKVAPTFKIPAGEHYVRLESGKGELGVFIQGADDICPWRFKIRAPDFNNLQILPQLLQGVKVADIMAILGSIDVIMGSVDR", "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": "MATLFIADLHLCAEEPAITAGFLRFLAGEARKADALYILGDLFEAWIGDDDPNPLHRQMAAAIKAVSDSGVPCYFIHGNRDFLLGKRFARESGMTLLPEEKVLELYGRRVLIMHGDTLCTDDAGYQAFRAKVHKPWLQTLFLALPLFVRKRIAARMRANSKEANSSKSLAIMDVNQNAVVSAMEKHQVQWLIHGHTHRPAVHELIANQQTAFRVVLGAWHTEGSMVKVTADDVELIHFPF", "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": "MTKLESLLHASTGLSLISGYLMYNRRYLLSFDKKREGETTQSISVIIPARNEEKRLPKLLKSLSQQSMRVECIVMDDDSNDRTAEIAREMGAKVYNVTYDNNGNTWIGKSYACYLGASYTVSDILIFMDADVELNNEHALEAIIQSYARQQYRGLMSIQPYHVVYKPYEHLSAMFNLMTVVGTNSFSTLSKSKGESLAFGPVTVMNKSDYILTQGHKNAASHIIEGFSLGKAFQRCQLPVTRFEGQGFVSFRMYEAGFKTMIEGWTKHLAVGASSTQPHIMMLIILWMVGCITSFSGLALSLFMKTLSFKRMALSYSLYTLQFIRLHRRVGRFSILFLAINSILFLVFILVYINSYRHIHYTKQVKWKGRQFSIK", "text": "FUNCTION: Catalyzes the glycosylation of 4,4'-diaponeurosporenoate, i.e. the esterification of glucose at the C1'' position with the carboxyl group of 4,4'-diaponeurosporenic acid, to form glycosyl-4,4'- diaponeurosporenoate. This is a step in the biosynthesis of staphyloxanthin, an orange pigment present in most staphylococci strains (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. CrtQ subfamily."}
{"protein": "MKTLELALPPSPPSLVPSFNYNSTARSVGNDVRTNFDVQLFLRKPKHQKSEPVVVIQQPQIQPQNPSSRCSTSDILRLMDSLSLPGNEDIYSCLAKESARENDQRGAHELQVHIMKSSIRPTITFINRLLLMHVSCGRLDITRQMFDRMPHRDFHSWAIVFLGCIEMGDYEDAAFLFVSMLKHSQKGAFKIPSWILGCVLKACAMIRDFELGKQVHALCHKLGFIDEEDSYLSGSLIRFYGEFRCLEDANLVLHQLSNANTVAWAAKVTNDYREGEFQEVIRDFIEMGNHGIKKNVSVFSNVLKACSWVSDGGRSGQQVHANAIKLGFESDCLIRCRLIEMYGKYGKVKDAEKVFKSSKDETSVSCWNAMVASYMQNGIYIEAIKLLYQMKATGIKAHDTLLNEAHLQM", "text": "SIMILARITY: Belongs to the PPR family. PCMP-A subfamily."}
{"protein": "MFITSPLEQFELNNYFGFYLFNYHFDFSNFGFYLGLSALIAISLAIINLTPYGSGAKIVPQKFGIAMEAIYFTMLNLVENQIHSSKTVSGQSYFPFIWSLFVLILFSNLLRLIPYGYATTAQLIFTLGLSISILIGATILGLQQHKAKVFGLFLPSGTPTPLIPLLVLIEFVSYIARGLSLGIRLGANIIAGHLTMSILGGLIFTFMGLNLITFIIGFLPITVLVAISLLEFGIAFIQAYVFAILTCGFINDSLNLH", "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": "MSDSTASSINKGLAAADPAIAALIEKEQQRQETHLELIASENFASRAVMDAQGSVLTNKYAEGLPSKRYYGGCEHVDAIEELAIERAKELFGAAWANVQPHSGAQANFAVFLALLQPGDTIMGLDLSHGGHLTHGSPVNVSGKWFNVVQYGVDRETQRLDMEAIRQLALEHKPKLIVCGFSAYPRTIDFAAFRAIADEVGAFLLADMAHIAGLVAAGVHPSPVPHCDVVTTTTHKTLRGPRGGLILCRDADFAKKFDKAVFPGSQGGPLEHVIAAKAVAFGEALQPAFKTYSQHVVANAAALAERLIARGIDVVSGGTDNHVVLLDLRSVGMTGKVADLLVSDVHITANKNTVPFDPESPFVTSGLRLGTAALTTRGFDAGAFREVADVIADRLLNPEDDAVQQQCLRRVEALCQRFPLYAAARQPALA", "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": "MTSSVHELSDNNESHAKKERPDSQTRPQVPSGRSSESIDTNSVYSEPMAHGLYPYPDPYYRSVFAQQAYLPHPYPGVQLQLMGMQQPGVPLQCDAVEEPVFVNAKQYHGILRRRQSRAKLEARNRAIKAKKPYMHESRHLHAIRRPRGCGGRFLNAKKENGDHKEEEEATSDENTSEASSSLRSEKLAMATSGPNGRS", "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": "MRAKGFTLIELAIVIVIIGILVAIAVPRFVDLTDQANQANVDATAAAVRSAYAIATVQAKGIPTCDQVFANPEGGSTSGSTWTSSDNSTTVSCNASADTFTISRGGKTRTLNLTVN", "text": "FUNCTION: Plays an essential role in forming the main structure of the narrow T4P pili that participates in twitching motility. 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": "MALEKLTPAAGSTHATKRIGRGQGSGNGKTAGKGNKGQRARKGYNEKRGFEGGQQPLQRRLPKVGFASKFEKPYVINVEKIAAIKELAEISIATIASVHKISKSVTKIKLIGASAKALASKIKDENVSVSGTK", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MPIKKIISRSNSGIHHSTVIDYKKLLTTNKNKPEKSLLVTLKKHGGRNNQGKITVRHQGGRNKRKYRIIDFKRTHYDNIEATVKSIEYDPNRSCFVSLITYANGAKSYIISPDGIKVGDKILASEHPIDIKPGFSMPLAFIPEGTQVHNIELHPKGGGQIARSAGSYARILGQDETGKYVILQLLSGETRKFLKECRATVGVVSNLDHNLVVIGKAGRNRHRGIRPTVRGSAMNPNDHPHGGGEGRSPVGRDAPRTPWGKRHMGVKTRNMKKASTNLIIRNRKGEQY", "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": "MARPMGKLPSNTRKCAQCAMAEALLEIAGQTINQKDLGRSGRMTRTDNDTWDLASSVGATATMIATARALASRAENPLINDPFAEPLVRAVGIDLFTRLASGELRLEDIGDHATGGRWMIDNIAIRTKFYDDFFGDATTAGIRQVVILAAGLDTRAYRLPWPPGTVVYEIDQPAVIKFKTRALANLNAEPNAERHAVAVDLRNDWPTALKNAGFDPARPTAFSAEGLLSYLPPQGQDRLLDAITALSAPDSRLATQSPLVLDLAEEDEKKMRMKSAAEAWRERGFDLDLTELIYFDQRNDVADYLAGSGWQVTTSTGKELFAAQGLPPFEDDHITRFADRRYISAVLK", "text": "FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. SIMILARITY: Belongs to the UPF0677 family."}
{"protein": "MDAALLLNVEGVKKTILHGGTGELPNFITGSRVIFHFRTMKCDEERTVIDDSRQVGQPMHIIIGNMFKLEVWEILLTSMRVHEVAEFWCDTIHTGVYPILSRSLRQMAQGKDPTEWHVHTCGLANMFAYHTLGYEDLDELQKEPQPLVFVIELLQVDAPSDYQRETWNLSNHEKMKAVPVLHGEGNRLFKLGRYEEASSKYQEAIICLRNLQTKEKPWEVQWLKLEKMINTLILNYCQCLLKKEEYYEVLEHTSDILRHHPGIVKAYYVRARAHAEVWNEAEAKADLQKVLELEPSMQKAVRRELRLLENRMAEKQEEERLRCRNMLSQGATQPPAEPPTEPPAQSSTEPPAEPPTAPSAELSAGPPAEPATEPPPSPGHSLQH", "text": "FUNCTION: May be important in protein trafficking and/or protein folding and stabilization. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MASLGRQVPEWHRLMALSWACLARQTCHFRKEKKMSPSLFCKLTTVPSRGNFQEFSSVRPKKYMQEPEHRTRLVPCLHEEQRTCMGSESLELERAISSLQDMGFAEAHIDSLLNIQPSVHPQQLLDIISELLLLGLNPEPVFMALKKNPQLLKLSATQMKRRSSYLRKLGLGEGKLKRVLSVCPKVFTMRQQDIDNIVKVLKEKCLFTVQHITDILHRCPAVLQEDPSELEYKFQYAYFRMGLTHLDIVRTDFLQYSIAKVKQRHIYLERLGRYQTPDKKGQTQIPNPSLKNILRVSEAEFLARTACSSAEEFEVFKKLLDQEEEESESHMSEEEEEEEEEEEEELP", "text": "FUNCTION: Regulator of mitochondrial ribosome biogenesis and translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S and targets NSUN4 RNA methyltransferase to the mitochondrial large ribosomal subunit (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mTERF family."}
{"protein": "MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDGALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKKACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPISPPATRVLETSPLQPQIAPHREELGPTHQA", "text": "FUNCTION: Has abundant triacylglycerol lipase activity."}
{"protein": "MENRKNFFHLHLISDSTGETLISAGRAAAVQFPHSNPIEHVYPLVRNRRQADAVLQSIDKEPGIVLYTIVDPELADFIDRRCIEIGVPSVNVLEPVIGTFQAYLGPLARRRVGAQHVMNADYFARIEALNYTMDHDDGQMAEDYDQADVVLVGISRTSKTPTSIYLANRGIKTANIPIVPDSPLPESLFAAKGPLIVGLIATSDRISQVRGHRELGTVSGFDPSDYTDRASIAEELKYARSLCARHNWPVIDVTRRSIEETAAAIIALRAKPR", "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": "MTTLNRSELLFVYDAQDCNPNGNPIGDNRPRRDPDTGQGIITDVRLKRYLRDQLQDDGFDIYVKKTEGRSHTRTKLIKDVLGGVDDADDLEDLGDVAEAFLDAATDVRYFGSTLSFEASDKDEDEAFRDALNSSLPNNYQGPVQFLPSKSLNEVEENEEYDSLTSVISTGEGNRQGGFDLDDKRIKYGIFPFWGLVDNNGAESTNLSQADVERLDTLCWRALKNQTTSRSKLGQEPRLYVRVEYEEGNYHVGGLQNLLELGDDSSESLRSVKDVVVDVTELVETLERVADRIDTLHVVGDGRLELDIGDETIRADEFWSHLSEAGHDVHEIDVLNERDLA", "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). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein helps process or stabilize pre-crRNA into individual crRNA units, in vivo Cas6 and Cas7 are also required for optimal crRNA processing and/or stability (PubMed:24459147). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSKNPLGTLVVRIWKAKNLPNKALVGKQSPYCVCRVGEVVKRTQTDKRSGQEPSWNAVLEFNIPSESYHIMKITVFHEGFRKHPHLIGDTVLSFEKAMKEELQSEWYELKNEFQFAGELSVQFKFIPTDPLYFDRASSKPVLQFPYSSVAALTPVPKKPSKPSKPRKKVPVSHPLPPTPPSREEHVSVPRESSLFTYEDDPLPSFPSPYMVDDYYTQDVFVSDNVNDYSYGVQNPTNPRLSVEDYDANHSSLPPVPPPHLILPTASSSQIFH", "text": "FUNCTION: Involved in the ingression of the plasma membrane during cytokinesis, leading to the separation of the daughter cells. Unlike its S.cerevisiae ortholog INN1, it does not play an essential role, probably because the actinomyosin ring is connected to the cell cortex by many more proteins. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes at the barrier septum and the cell tip. SIMILARITY: Belongs to the INN1/fic1 family."}
{"protein": "MSALIARQAPSAAERLADLAVQALVDEADLSPKPGLVDRRGSGAHSDLHLGLMHASAQSLWPAFAAMADAARSEGRVSQALRETLGQLGRDGEAEMLRVTAGVNTHRGAIWALGLLSAAAMLESGASAGGIAASAAALARLDDPAAPHNPDSHGARVCRRYGVLGAREQAQHGFPAVIEHGLPQLLASRRAGAGEQNARLDALLAIMSSLTDTCVLHRAGLEGLTRMQAGARAVLEAGGCASLAGRRRLRALEGEMLSLRASPGGAADLLAATLFLDRLTPAASAPIGSY", "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": "MALVSVAPLVSMRRSLFSSPYELKSIDKTIPNLVMCRKRMLGRPSIRVSSTASVSNDDGVRRRVGDYRYNHWDEDLIDSLATSYEAPSYLKRADTLVEAIKDRFNSMGVDDGERMSPLTDLYQRLWMVDSVERLGIDRHFQNEIKSALDYVFRYFASSYWKEKGIGRGRQSAVTDLNSTALGLRTLRLHGYPVSSDVLENFKDHNGQFTCSGIQTEGEIRGVLNLFRASLIAFPGEKVMEEAEIFSTMYLKHALQKIAVSSLSQEIEYLLEYGWHTNPPRLEARMYMEVFPQDTIYEQKLVELAKVEFNIFHSLQKRELQSLTRWWKHYGFPQLSFTRHIHVEYYTFGSCIATDPKQSAFRLCFAKMSYFVTVLDDIYDTYGTMEELELFTAAIKRWDPSVVDCLPEYMKGVYMAVYDTVNEMAKEAEKVQGRDTLNYVRQAWELYIDAYMPEAKWISSGYLPTFQEYLDNSKISFGTRITILQPILTLGEPLPHEILQEIDFPAKFNDLISVILRLKGDTRCYKADRARGEEASSVSCYMKDNAGLTEEDAIHRINAMVHNLLKELNWELLKPDCNVPISCKKAAFDICRIFHHGYKYRDGYGDATIETKNLVKRTVLEPVPL", "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 (-)-beta-phellandrene (PubMed:23679205). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
{"protein": "MSQARPATLRVAVLGAGSWGTALAAAASRRHPTVLWARDGAQAQAMAARHENTRYLPGVALPHALQVSADLAQALAHLAHDPAHALIILGVPVAGMTPLCTELAARLPALGLQAVPLVWTCKGFEEQTARLPHETVQAALGAMPGLAAGVLSGPSFAREVAQGLPVALTVASGSSAVRDAVTTALHGAAVRIYASTDVVGVEVGGALKNVIAVACGICDGLALGTNARAALITRGLAEMARFGAALGAQQETFAGLTGLGDLVLTATGELSRNRRVGLEIGAGRKLADILASGMTAEGVRCARAARDRARALNIELPITEAVCAVLFEGLSPMTAVSALLAREARPESPTP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MKKKHVAVLMGGFSSERPVSLSSGNSCADALEAEGYRVSRVDVSRDVSRVLSELKPDVAFNALHGPFGEDGTVQGVLEYLGIPYTHSGVLASALAMDKDLAKTVAKSAGIPVASSRVMNRFEIGDKHPMEPPYVVKPVAEGSSFGVVIVREGQSHPPQVLGSAEWGYGERVMVERYIPGRELTCAVMGDRVLGVCEIVPVGHSFYDYDSKYAPGGSRHVCPAEISPNIYQKIERLALKAHQAIGCRGVSRSDFRYDDRLPGEEGIVWLEINTQPGMTPTSLVPDIAAQAGIGFGALLSWMVEDASCPR", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSIYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD", "text": "FUNCTION: Important for virulence. 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": "MDDVTPDELEAVSVLLRLPNPVFFDQEEEEEDEEEEYDEESVCEDDLEVKSCMQTNENKGKKRKVAEQLMDSDVKDNQYRLMLGKEPVKKMMDALGKTEKLGTKGLNVSVYGPNGENHKMVLKIWIKGTPVLTSGWKNFVKSYKLEKHVDFLTIWMFRHKKTREICFAIDSTRFPVKGTLSKRILQEVFKNP", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDQRTIEKFEKESAEMGKGSFKYAWVLDNLKAERERGITIDISLWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADVAILIVAAGTGEFEAGISKNGQTREHILLSYTLGVKQMIVGVNKMDAIQYKQERYEEIKKEISAFLKKTGYNPDKIPFVPISGFQGDNMIEPSTNMPWYKGPTLIGALDSVTPPERPVDKPLRLPLQDVYKISGIGTVPVGRVETGILKPGTIVQFAPSGVSSECKSIEMHHTALAQAIPGDNVGFNVRNLTVKDIKRGNVASDAKNQPAVGCEDFTAQVIVMNHPGQIRKGYTPVLDCHTSHIACKFEELLSKIDRRTGKSMEGGEPEYIKNGDSALVKIVPTKPLCVEEFAKFPPLGRFAVRDMKQTVAVGVVKAVTPRAANASAAGKKK", "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": "MQKKSIIIPALDLIDGNVVRLHQGDYAKQTTYSDNPIEQFASYLAQGAEQLHLVDLTGAKDPAKRQTALIGKIIAETNCQIQVGGGIRTEQDVADLLAVGANRVVIGSTAVKDRAMVKGWFEKYGAEKFVLALDVNIDASGQKIIAISGWQEASGVSLEELIEDYQVVGLQHVLCTDISRDGTLAGSNVNLYREICAKYPKIHFQSSGGIGSLDDIKALKGTGVSGVIVGRALLEGKFNVAEAIECWQNG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "LLVPLVTFHLILGMGTLDHGGALTERRSADATALKPEPVLLQKSDARSTDDNDKDRLTQMKRILKKRGNKARGEEEHSKYQECLREIRVNNVQQEC", "text": "FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin has the highest potency for the NR2B/GRIN2B subunit, followed by NR2A/GRIN2A, NR2C/GRIN2C, and NR2D/GRIN2D subunits. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin B superfamily."}
{"protein": "MARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIDTAPGQHGARKPRLSDYGSQLREKQKVRRIYGILERQFRNYYKEANRLKGNTGENLLVLLEGRLDNVVYRMGFAATRAEARQLVSHKAIVVNGRVVNIPSFQVSVNDVVAVREKSKKQARIKASLELAEQRERPTWLEVEAAKMEGVFKRVPERSDLSADINEHLIVELYSK", "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": "MKDFTTYLSTAPVLAAVWFGFLAGLLIEINRFFPDALSFSFV", "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": "MAKKITAYIKLQVKAAQANPSPPVGPALGQHGVNIMEFCKAFNARTQGIEPGLPTPVIITVYSDRSFTFETKSTPASVLLKKAAGLTSGSAHPNTVKVGTVTRAQLEDIAKAKNADLTAADMEAAVRTIAGSARSMGLNVEGV", "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": "MTIQSTANHQDGYLPAILCLHGAGTNATIFNLQARTIVRCLKHKFRFIFVNAPFESLPGPGVIPTFAEIRPYLRWHCDENAIQEFDVSPELVDNERRLVRSMISDKIEQEATGPSLGIVGVMAFSQGTRVATGLCLDPEFGSSIQFAIIIAGTFPALSLENPVSDSETTNLFSGINGNKHEQLQIPSVHVQGTMDPWGPESARLLKECWSADLAMVVKFHGAHQVPTSKKDAQAVAQAVLSCWDSAQT", "text": "FUNCTION: Thioesterase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells (PubMed:22252016, PubMed:27983606). The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016, PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme (PubMed:27983606). The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism (PubMed:27983606). SIMILARITY: Belongs to the LovG family."}
{"protein": "MKNTADITVLGAGSYGTALAISLASNGHRTLLWGHDPEHIENLKRDRANEAFLPGITLPDLLVPEADLATALAASNNVLVVVPSHVFGLVLEQAKPLLREDSRIVWATKGLEPETGRLLQEVAREVLGDKYPLAVLSGPTFAKELAAGMPTAISVAGTDESFTQDLVELLHSSNRLRVYANDDFTGLQLGGAVKNVIAISAGMSDGIGFGANARTALITRGLVELTRLGEAIGAQASTFMGMAGLGDLVLTCTDNQSRNRRFGLALGKGQGVEEAQVEIGQVVEGYRNTKEVYTLAKRLGVEMPITEQVYKVLYQGGTPHEAAKSLLAREKKSETEDSE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MTKFKLLLAGSLVAIVSMGLLASNINEREKERVALNKTAHSQGIEGKAMSEEWARYYPRQFDSWKKTKESDNITDMLKEKPALVVAWAGYPFSKDYNAPRGHYYALQDNINTLRTGAPVDGKTGPLPSACWTCKSPDVPRIIEQDGELEYFTGKWAKYGDEIVNTIGCYNCHDDKSAELKSKVPYLDRGLSAAGFKTFAESTHQEKRSLVCAQCHVEYYFKKTEWKDDKGVDKTAMVVTLPWSKGISTEQMEAYYDEINFADWTHGISKTPMLKAQHPDWELYKTGIHGQKGVSCADCHMPYTQEGAVKYSDHKVGNPLDNMDKSCMNCHRESEQKLKDIVKQKFERKEFLQDIAFDNIGKAHLETGKAMELGATDAELKEIRTHIRHAQWRADMAIAGHGSFFHAPEEVLRLLASGNEEAQKARIKLVKVLAKYGAIDYVAPDFETKEKAQKLAKVDMEAFIAEKLKFKQTLEQEWKKQAIAKGRLNPESLKGVDEKSSYYDKTKK", "text": "FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine, and even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the cytochrome c-552 family."}
{"protein": "MGQCVTKCKNPSSTLGSKNGDRDPSSKSHSRRGASHREEQVPPCGKPAGDILVNGTKKAEAATEACQLPTSSGDAGRESKTNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREVEGRGALSSGPEGLCPEEQT", "text": "FUNCTION: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation. SUBCELLULAR LOCATION: Cell membrane Cytoplasm Nucleus Cytoplasm, perinuclear region Note=After UVC treatment, the protein enters to the nucleus gradually. Cell membrane localization is essential for CUL3 neddylation."}
{"protein": "MAPKKPNKKNVIQRRPSAEKRILTAQKRELINHSFKSKVKTIVKKFEASLKLDDTQATLSNLQSVYSVVDKAVKRGIFKDNKAARIKSKATLKVNARAS", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
{"protein": "MPSFDVVSKTDLAEVDNALAGITREVAQRFDFKGSKCSVERKDQMITVLADDDSKLKTMHELLSVHFTRRKVDPKALDYKTVEKASGNTVRQEVRIKDGVETVLAKRLVKEIKDAKLKVQVAIQGDELRVTGKKRDDLQEAIALLRKLDVDQPLQYINFRD", "text": "SIMILARITY: Belongs to the UPF0234 family."}
{"protein": "MNKYKPVPKLSSQSPVHHTNLRIPPSGRPFKKEDFLNLISKDSLESDSESLPQEAKSWSDIKDQIQDKDMEPDSLEEDSPSETEEAVNRKAAHNTNREDLSAHDAGVNHSQHQVEDKYSDLRYDPNWKNKREEGQPLAGEALPGSADSSSENLPLAPLYPSREPSMGLSAGKGKEKKSPQSEASLLGSEFLSPKYERSTRQNGFFSELSDSDQEEKSSGLSQYLKSSSSHNDVFLPGSRGPRRRKSKQYFVEKNKLTLGLPMPKTDSYLQLHNKKRGETRLEQISYPVRDTDKMTVQNDKEVENTFMDPEDKWHQRAKQLKNYQEHLSQYEDTKSGNVPRGQSSDAANGQQPSRRTAKARVRKQRKHQKGLKSLGTKELVVSQNNQNNPFQQPQNQRQTADASAKHELAAQTNASNPNLQDARTLTHNPKVTSDSFVSPKQALDRALYKNSISGLNANKRRGHRREEERILYQPQPIYVFSDTHLQDFNELPHRHESPSQRAPQSDHHMNTHRSTKTKKPAKQPQAETKYKNIEMLWKFHSSSDMEPASASPDSRLAQIMEQHQQALMQLAEVQPSEGSLASIILPPILSRVESESQLNSERSHRHQVKMARSNSEGYLLQLERGKRHRKRSSTKSSKLKGYQKRDVKLGGLGPDFASVRDKMQMLMQQKEYAQQVKDYNMKALSILSKPQTSKTESKSAISRKKALDYAKTIPKPKPPNLPDQTAKKTKNSRHSEKEGGLPEISLLEILQSRHEREKQAVAAFKVLHIV", "text": "FUNCTION: Required for the normal development of cilia in brain ependymal cells lining the ventricular surfaces."}
{"protein": "MPKPGVFNFVNKATWDARNALGSLPKETARKNYVDLVSSLSSSSEAPSQGKRGADEKARESKDILVTSEDGITKITFNRPTKKNAISFQMYLDIMHALKNASTDNSVITVFTGTGDYYSSGNDLKNLINDAGEIQDVVATSTKILREFVNCFIDFPKPLVAVVNGPAVGIAVTILALFDAVFASDRATFHTPFSQLSQIPEACSTYMFPKIMGPTKAAEMLLFGKKLTAREAWAQGLVTEVFPESTFETEVWTRLKTYSKLSPNVMRISKELIRKHEKQKLYTVNAEECAAALERMPREEYAKALRNFLFRKAKAKL", "text": "FUNCTION: Catalyzes the isomerization of trans-3-nonenoyl-CoA into trans-2-nonenoyl-CoA (PubMed:24344334). May also have activity towards other enoyl-CoA species (Probable). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MPSYLRNLVWATLAAGLVSAAPTPSRVSDLTKKSSSTCTFSSAASASASKSSCSTIVLSNIEVPAGKTLDLTDLKDGTKVIFEGTTTFGYKEWSGPLIKISGSDITVEAADGAVINADGSRWWDGEGTNGGKTKPKFFYAHSLDDSTISGLNIKNTPVQAFSIQSDNLIIDGVTIDNSDGDENGGHNTDGFDISESTGVTIRNAVVKNQDDCIAINSGQNIYFTGGTCSGGHGLSIGSVGGRDDNTVKNVTITDSTVTDSANGVRIKTVYDATGSVSDVTFSDITVSGITDYGIVIEQDYENGSPTGTPTSGVPITDLTVKGITGSVESDAVEVYILCGDDACSDWTWSGVDITSGQTSSKCENVPSGASC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
{"protein": "MSVNPLIAKITESQLRNDIPDFRAGDSVRVHARIVEGSRERIQIFEGVVIKRRGEGISETYTVRKISNGIGVERTFPLHTPRVDKIEVTRHGRVRRAKLYYLRALHGKAARIPERRRG", "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": "MPKLEMMLLVLLILPLPYFDAAGGQAVQGDGHGDGMDRYLQRDDREARITCQPRGRSKWGRCCLTQMCGNYCCYKHGCRCVYHSWRGHGCSC", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Component 4b which seems to correspond to this toxin blocks both neuronal and muscular subtypes: human alpha-7/CHRNA7 (IC(50)=125 nM), human alpha-3-beta-2 (CHRNA3-CHRNB2) (IC(50)=282 nM), human alpha-4- beta-2 (CHRNA4-CHRNB2) (IC(50)=697 nM), mouse adult muscular subtype alpha-1-beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) (IC(50)=351 nM), and mouse fetal muscular subtype alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHRND) (IC(50)=447 nM). It shows different dissociation rates towards the different subtypes, with a very slow rate towards alpha-7 subtype (almost irreversible), followed by the adult muscular subtype, the fetal muscular subtype, alpha-3-beta-2 and alpha-4-beta-2 (almost entirely reversible within a few minutes of washing). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin D superfamily."}
{"protein": "MDQNRSPNGRDCREPPSPSSTARPGLVVIAGPTATGKSRQALLLAQRLGSPLLNADSRQVYREFDIGTAKPTPAERALWPHELIDFVDPRHTYTVAEFQQAAQARIAAAHRQGQTPILVGGTGLYIQSITAGLGIPAVPPQPQLRAQLETWPPEIRYAWLQQLDPVAAGQIHPHDEVRTLRALEIIYTTGKPASYLRQAHPPDYPILLLGLHCPMPRLEQRIARRTAEMLAAGWIEEVKTLRQRYGPDLPLLQTLGYAEIGAYLEGRIPAAELQPLIVRRTRQFAKRQMTWFRAMPGIQWLDCEAEDLPEQIWKRVTAWMAAQTSAGTTPAVAARPPADP", "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": "MKLSQRVQAIKPSPTLAVTAKAARLKAEGKNIIGLGAGEPDFDTPLHIKDAAITAIRNGFTKYTAVGGTASLKQAIISKFKRENSLEFMPGEILVSSGGKQSFFNLVLATIDPGDEVIIPAPYWVSYPDIVLIAEGKPVFIDTGIEEKFKISPDQLEKAITPRTRMFVVNSPSNPSGSVYSLEELQALGAVLRKYPDILIATDDMYEHILLSGDGFVNILNACPDLKARTVVLNGVSKAYAMTGWRIGYCGGPAAIITAMENIQSQSTSNPNSIAQVAAEAALNGDQSCMVPMIEAFRERNQFLTNALNSIAGIHCLLSEGAFYAFVDVRQAISRLNTQQILQNSSDIAFCNYVLEKAEVAAVPGSAFGCEGYMRLSFATSMDNLQEAVKRIASLLS", "text": "FUNCTION: Catalyzes the reversible conversion of aspartate and 2- oxoglutarate to glutamate and oxaloacetate (PubMed:24302739). Can also transaminate prephenate in the presence of glutamate, with lower efficiency (PubMed:24302739). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MIYISPKLVVALPVKELKDLNRIELLINDVDLVELRLDYLSKFDVDILDLFSKYKEKLIITLRDKDEGGVNYIDPAFKANFVRRMEREKFMYDIEARFALRYQVNVKDKIVSIHYFDNLPEFTEVKEIFDKFDEAYLRKIAVIAKRGYRELLMRVLDNYDNAVVMPMGVNGVERIAFSLLGSKLIYAHAGEETAKGQLHYKDVRRILNQLSTIMSSPST", "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": "MADSKELAEQREETRLIIEELLEDGSDPDALYAIEHHISCENFETLEKAAVEVFKLGYEVTEPEEIEIESGEILVCFDAVSESGLNAELIDAQVEQLMNLAEKMGVYYDGWGTYFEDPDAEYDDEDGENEDDESESDKSSRLH", "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": "MTKLTVKALSEEIGTPVDRLLQQFSDAGINKKDGDSVTESEKQSLLVHLKKEHGSVDDSASPTRLTLQRKTRSTLSVAGSGGKSKDVQVEVRKKRTYVKASALEEEKKAEQLKAEAEEQAKRDAEEAAVRELEQKAQREAEEQAKREAEAEAKAKREAEEKAKRAEADKAKKEMTKKNEQAKKEAEELKARQELEATRKAEAEAAKLVEEARKLAEENEARWKEEEQKKSAAEKDADYHVTTSSHAREAEDAADRKEEQQPRRRKKKAKPAEAAAPRGGRNQRGGRNKKAQVNKPTSMQHGFDKSATVAKQDVAIGETIVVSELASKMSVKATEVIKVMMKMGAMATINQVIDQETAQLVAEEMGHKVILRKENELEEAVLSDRDNSAEAEGRAPVVTIMGHVDHGKTSTLDYIRRAHVADAEAGGITQHIGAYHVETDNGMITFLDTPGHAAFTAMRARGAQATDIVVLVVAADDGVMPQTIEAIQHAKAAGVPLIVAVNKIDKEDANPDNVKNELAQYDVIPEEWGGENMFVHISAKQGTNIDGLLEAILLQSEVLELTAVREGMASGVVVESRLDKGRGPVATVLVQSGTLNKGDIVLCGQEYGRVRAMRDENGKEIESAGPSIPVEILGLSGVPASGDEATVVRDERKAREVANYRQGKFRDVKLARQQKAKLENMFSNMTAGEVAELNVVLKADVQGSVEAIADSLRKLSTDEVKVNIVGSGVGGITETDAVLAAASNAIILGFNVRADATARRTIENENLDLRYYSIIYQLIDEVKAAMGGMLAPEFKQEIIGLAQVRDVFKSPKLGAIAGCMVTEGTIKRSNPIRVLRDNVVIYEGELESLRRFKDDVAEVKNGYECGIGVKNYNDVRVGDQIEVFEIVEIKRTLD", "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": "MLNQLDNLTERVRGSNKLVDRWLHVRKHLLVAYYNLVGIKPGKESYMRLNEKALDDFCQSLVDYLSAGHFSIYERILHKLEGNGQLARAAKIWPQLEANTQQIMDDYDSSLETAIDHDNYLEFQQVLSDIGEALEARFVLEDKLILLVLDAARVKYPA", "text": "FUNCTION: Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rsd/AlgQ family."}
{"protein": "FGVLAVTSR", "text": "SUBCELLULAR LOCATION: Secreted, cell wall."}
{"protein": "MSTIKPSPSNNNLKVRSRPRRKSSIGKIDLGDTVPSLGTMFETKESKTAAKRRMQRLSEATKNDSDLVKKIWFSFREISYRHAWIAPLMILIAVYSAYFTSGNTTKTNVLHRFVAVSYQIGDTNAYGKGINDLCFVFYYMIFFTFLREFLMDVVIRPFAIRLHVTSKHRIKRIMEQMYAIFYTGVSGPFGIYCMYHSDLWFFNTKAMYRTYPDFTNPFLFKVFYLGQAAFWAQQACILVLQLEKPRKDHNELTFHHIVTLLLIWSSYVFHFTKMGLPIYITMDVSDFLLSFSKTLNYLDSGLAFFSFAIFVVAWIYLRHYINLKILWSVLTQFRTEGNYVLNFATQQYKCWISLPIVFVLIGALQLVNLYWLFLIFRVLYRILWRGILKDDRSDSESDEESDESSTTPTDSTPTKKDI", "text": "FUNCTION: Component of the ceramide synthase complex that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward hexacosanoyl-CoA (C26:0-CoA) (PubMed:15692566, PubMed:11694577). N-acylates sphinganine and phytosphingosine bases to form dihydroceramides and phytoceramides, respectively (PubMed:15692566, PubMed:11694577). Redundant with LAG1. Facilitates ER-to-Golgi transport of GPI-anchored proteins. FUNCTION: Component of the ceramide synthase complex required for C26- CoA-dependent ceramide synthesis. Redundant with LAG1. Facilitates ER- to-Golgi transport of GPI-anchored proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sphingosine N-acyltransferase family."}
{"protein": "FFECTLECDIKKEGKPCKPKGCKCNDKDNKDHKKCSGGWRCKLKLCLKF", "text": "FUNCTION: Is toxic to mice but not to insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 04 (lasiotoxin) subfamily."}
{"protein": "MARLLLVCLGGALGSGARYLTSAWALRAFGPDFPRGTLLVNVSGSFLLAGIMTASLQSEAFPPDLRLFLAAGVMGGFTTYSSFNYETLALLEQGRLAAAAGYLLATVLGCLAAAVAATLLVRWLAG", "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": "MRVRNRKGAGEMLAENAHIVVENPADFKGSWSERFGNDHPIHIEVGCGKGAFITGMAALHPEINYIAIDMQLSVLSYALDKAIEADLPNVQMMLVDGAALSEYFADGEIDQVYLNFSDPWPKGRHEKRRLTYKSFLATYEKILRPEGEIHFKTDNRGLFEYSLVSLANYGMELKKVWLDLHQDEEFAPQNVMTEYEQKFSQKGQVIYRLEAKFLPKK", "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": "MPLIMEDGINVDDLFGEPGSLELGLSPSTTSPRGLAQRLDEMRLIGCCQKIAWSKLGCIAYISQDGLRVNVRHLQCRPSDGKWVLSEETPLLPVTDAHGGHTLVHLCWNEPGVELAVADSSGRVSIYSISIALNSIAGHRQAAFDPDDDGAQIVGMMWLNTQRTVHSFYQAAKVQGRWAYSPFRRRPIGPFHPVNKAGLVCVTRSGIIRLLYQNPDGRWAEISAELKNTGYSDRLLTHAALVSTQGGILIATHSACQKLCLYRVHIAWTPTQYDPGQQKPPVPWPVPSFRFLHCKVESQCDVRGTNRHAGDNAPGLPSFTNSLYCLTGLDIVLPALDNPAGSTANPWVVAIYSAPLHVTQDHPQQQGPASVFVRWQLDTGPLTLHPKFDDVPSKKNNAQVKPKLELRRLDDVYSDKYAISIDQIEYGNVLAITYDDGSVVFYDPKTMAVVNGVDDANTVTSLAQAGFHHPPEPSGLHISFSPNACAAVMLDGEGQTHLRLTEHSYGAEGGLHDENKYSAAIAALTLAFCRGCGSDVNTDDILLILVRQLTPEAQATFINEAYRALPINCNFTVEQDKLMNHPYIPRCLSIQAALGFKNKYTPRSFASSIPWAVLQLRHASVLYAFFFQYNKGGTTEPHDPDVLRMVLGNTKWALDFSFYVLNELFDLADDFESLSGDQEAFTQKLKSTSSLPLIILLSSMSRAFLRFICRGLRGIYAGYATAAPLSGDARVYYAEIYQTLESAPIRIDAYEKFLAGVDSAVRHAYHGAGFGDAERPGPEKELLVNARVPPVLVPAVSTILRQTVPALKTEIDRITIYMGDYSWLGLSNDRRTEMYRRSRDVDIIKKIPCRPTASALPETNANANANQNGKSSTQVQQRRRRCVRCCEVSSDTHPPRSLLSFRMIVKLGLLRACVCGGMWTLEPSVYSSAQPSGAPVGQATGRTPALVAAGLAGSS", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 16 family."}
{"protein": "MKPTFPAIVTTAEMQAIEGAMFNGGLPIPALMEKVGQRLSHYLQAHFPTSQYPRVAVLAGPGHNGGDALVVARELWHRGYQVKLWQPFERLKPLTADHARYARFLGLPFVERVEALQEVDVIVDGLFGFGLERELTGELAHAIDEINTWPQPRVSIDVPSGLHSDTGAVLGTAIRADRTLCLGLWKRGLLVEEAQPWVGQGVLIPFDIPSVVIETALASAPRRYCLDDSCWQALPLSRSPITHKYQQGQLLLIGGSGQFGGSILLSALAARCTGVGMLVVAVPQSLKSLVLSRVPDAIVVGCPETPRGAIARLPEGLELGKFSAIACGPGLTPEAVSVVATVLRAETSLVLDADALNILATLSPWPLPSGTILTPHYGEFRRLFPDLVGTAGDRLDQVIAAARWSNAIVLLKGARTAIASARGDLWINPHSTPALARGGSGDVLTGLIGGLLAQQEALRATYGGVWWHAQAALEAEQQATSLGVYPEQLIAHLLPTLRRALAARV", "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": "MSAKNKSNNKTLAENRKARHDYFIEESMEAGIQLVGTEVKSIRAGKSNLKDSYGEIINGEIFIRNMHISPYEKGNIFNRDPLRDRKLLLHKKEIARLLGYTAQQGYTIVPLSLYLKNGRVKVNLAVAKGKKNYDKRDSMLEKAAKRDIERQMKERFR", "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": "MTLPSNNSTSPVFEFFLICFPSFQSWQHWLSLPLSLLFLLAMGANATLLITIYLEASLHQPLYYLLSLLSLLDIVLCLTVIPKVLAIFWFDLRSISFPACFLQVFIMNSFLTMESCTFMIMAYDRYVAICKPLQYSSIITDQFVARAAIFVVARNGLLTMPIPILSSRLRYCAGHIIKNCICTNVSVSKLSCDDITLNQSYQFVIGWTLLGSDLILIVLSYFFILKTVLRIKGEGDMAKALGTCGSHFILILFFTTVLLVLVITNLARKRIPPDVPILLNILHHLIPPALNPIVYGVRTKEIKQGIQNLLRRL", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MARGPKKHLKRVAAPKHWMLDKLTGVFAPRPSTGPHKLRECLPLIVFLRNRLKYALTGDEVKKICMQRFIKIDGKVRVDVTYPAGFMDVISIEKTGEHFRLVYDTKGRFAVHRITVEEAKYKLCKVRKITVGVKGIPHLVTHDARTIRYPDPVIKVNDTVQIDLGTGKIINFIKFDTGNLCMVIGGANLGRVGVITNRERHPGSFDVVHVKDANGNSFATRISNIFVIGNGNKPWISLPRGKGIRLTVAEERDKRLATKQSSG", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
{"protein": "MSLGLLCCVAFSLLWAGPMNAGVTQTPKFHVLKTGQSMTLLCAQDMNHEYMYRYRQDPGKGLRLIYYSVAAALTDKGEVPNGYNVSRSNTEDFPLKLESAAPSQTSVYFCASSY", "text": "FUNCTION: Probable non-functional open reading frame (ORF) of V region of the variable domain of T cell receptor (TR) beta chain (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive T cell receptor (TR) chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane."}
{"protein": "MDIIPAIDLLGGRCVRLYQGDYNQAEVFDTDPVGMARRWLSQGATRLHLVDLDGAKTGEPVNQAAMAAIVQDLAIPVQVGGGVRSRQRVVELLDLGVDRVILGTVAIEQPQLVEALCAEFPGRILIGIDARDGKVATRGWLETSTVQATDLARTVEKAGAAGIIYTDIHRDGTLQGPNLEALRQLASEVNLPIIASGGVSSIADLLNLFVLSTSGVTGVIIGKALYSGDITLTDAIRAVGQGRWQDVPPDLGFSTFA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MIIKKIKMDVCPLDVYEQIRGENTFLLESAEGVPKVARYSILGKAEGKVIFKNGKLKVESFTEFGDKAKDLEGKYECPLDALREVRNEYLKYIDISNIEPIPRFKGGLVGYLSYDIIRYWIDLSNINPKPINDLKFPDAEFFIVKDFISFDLKEKVINLIAEDDEGIRELERIIKNAKIGNNDNKEEKTTENKDLKIKSNMSKEEFIEAVKKAKEYIFAGDIFQVVLSRRIEIDLDNLDHLKIYKKVREINPSPYMYYLDFGDRKIIGSSPEILVRTDYKDNKRLVITRPIAGTIRRGKTEEEDKELEKKLLSDEKERAEHVMLVDLARNDIGKISKFGTVEVTDFMIIEKYSHVQHIVSNVVGELKDNYDSFLAVKATFPAGTLSGAPKVRAMEIIEELEKTWRGPYGGGVGYFGWDDLMDLAITIRTFVISKNKGYIQVGAGIVADSIPENEWEETERKGMANVKTIESLLK", "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": "MKLILLGAPGAGKGTQATFICQKFGIPQISTGDMLRAAVKAGTPLGLEAKKVMDSGGLVSDDIIIGLVKERITQPDCANGFLFDGFPRTIPQADAMKAAGVKLDLVLEIDVPDEAIIERMSGRRVHVASGRTYHVKFNPPKVAGVDDVTGEPLIQRDDDKEATVLKRLQVYQSQTRPLVDYYAAWAATGDAAAPKYRKIAGTGSVDEITTRALAALA", "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": "MNVRTIADLGPDERAAFFDRDAGVDAVRDDVRDIVSQVHEEGDVALRRFAEEFDDVSVGNIDITDAAERAYEEIDDDVREAIEDAAANIRAFHERQVPEDWRDDFEGRELGRRFRPLDSAGVYAPGGTAAYPSSALMGVIPAKVAGVEHVAVATPPAEEVNPVTLAAIHVAGADAVYQVGGAQAIAALAYGTETVSATDIVVGPGNRWVTAAKAEVRGDVAIDFLAGPSEVMVVADGDADPELVAADLIAQAEHDENASVVAVTDDADLAEQVVDAVDEQADGREREAVIRAALDNDTSGVLLARSMSEAVLFAEEYAAEHLSIQAADDESLLERIPSAGSVFLGPYSPVAAGDYATGTNHVLPTGGNARVTGGLSVDTFVRSTTVQRLSEDSLGDIADTITTLAEAEGLDAHAESVRKRFE", "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": "MNFPIERVRADFPLLSRQVNGQPLVYLDSAASAQKPQAVIDKELHFYRDGYAAVHRGIHSLSAEAIQQMEAVRTQVADFIHAASAEEIIFVRGTTEAINLVANSYGRHFLAAGDSIIITEMEHHANIVPWQMLAQDLGVEIRVWPLTATGELEITALAALIDDTTRLLAVTQVSNVLGTVNPIKDIVAQAKAAGLVVLVDGAQAVMHQPVDVQALGCDFYVFSGHKLYGPSGIGILYGKSALLQQMPPWEGGGAMIKTVSLTQGTTFADAPWRFEAGSPNTAGIMGLGAAIDYVTELGLLPIQQYEQSLMHYALAQLSQIKSLTLYGPTERAGVIAFNLGQHHAYDVGSFLDQYGIAIRTGHHCAMPLMAFYQVPSMCRASLALYNTREDVDRLVAGLQRIEKLLG", "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": "MKMSFRWYGKKDPVTLEEIKAIPGMQGIVTAVYDVPVGQAWPLENILELKKMVEEAGLEITVIESIPVHEDIKQGKPNRDALIENYKTSIRNVGAAGIPVVCYNFMPVFDWTRSDLHHPLPDGSTSLAFLKSDLAGVDPVADDLNLPGWDSSYSKEEMKAIIENYRQNISEEDLWANLEYFIKAILPTAEEAGVKMAIHPDDPPYGIFGLPRIITGQEAVERFLNLYDSEHNGITMCVGSYASDPKNDVLAMTEYALKRNRINFMHTRNVTAGAWGFQETAHLSQAGDIDMNAVVKLLVDYDWQGSLRPDHGRRIWGDQTKTPGYGLYDRALGATYFNGLYEANMRAAGKTPDFGIKAKTVGTKEG", "text": "FUNCTION: Catalyzes the dehydration of D-mannonate. SIMILARITY: Belongs to the mannonate dehydratase family."}
{"protein": "MTEQEKTSAVVEETREAVDTTSQPVATEKKSKNNTALILSAVAIAIALAAGIGLYGWGKQQAVNQTATSDALANQLTALQKAQESQKAELEGIIKQQAAQLKQANRQQETLAKQLDEVQQKVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITVRRAITDDIASLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDGEELSSSISEWRINLQKSWQNFMDNFITIRRRDDTAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEETYRQALENVSTWVRAYYDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQAMLEKLMQTRVRNLLAQPAAGTTEAKPAPAPQADTPAAAPQGE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein."}
{"protein": "MSDFSQTVPELVAWARKNDFALTLPTERLAFLLAIATLNGERLDGEMSEGDLVDVFRHVSKTFEQTHETVAQRANNAINDLVKQRLLNRFTSELAEGNAIYRLTPLGISISDYYIRQREFSTLRLSMQLSIVAQELRAAGDAAEEGGDEFHWHRNVFAPLKYSVAEIFDSIDLTQRLMDEAA", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, nucleoid Note=Restricted to the nucleoid region. SIMILARITY: Belongs to the MukF family."}
{"protein": "MSDVDADEARKMAERERKKEEVRKRLEEASRMKKAKKGFLTPERKKKLRKLLMMKAAEDLKQQQMLKEQERQRILQERIIPLPDLDNEDDLEAVYDEIRERLIDLESENYDVSYIVRQKDFEINELTIAVNDLRGKFVKPTLKKVSKTEGKFDKLKKKEATKVDFRAQLKVVDKNEFALDEEDTEKKEKAAWAK", "text": "FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to muscle actomyosin ATPase activity. SIMILARITY: Belongs to the troponin I family."}
{"protein": "MFLRSVNRAVTRSILTTPKPAVVKSSWRVFTVANSKRCFTPAAIMRNQETQRVGDILQSELKIEKETLPESTSLDSFNDFLNKYKFSLVETPGKNEAEIVRRTESGETVHVFFDVAQIANLPYNNAMDENTEQNEDGINEDDFDALSDNFANVNVVISKESASEPAVSFELLMNLQEGSFYVDSATPYPSVDAALNQSAEAEITRELVYHGPPFSNLDEELQESLEAYLESRGVNEELASFISAYSEFKENNEYISWLEKMKKFFH", "text": "FUNCTION: Not known. Binds to the sorting sequence of cytochrome b2. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the MAM33 family."}
{"protein": "MNIRPLHDRVIVERQEVESKSAGGIVLTGSAAEKSTRGVVLAVGKGRILENGTVQPLDVKVGDTVIFAESYGTKTEKIDGKEVLIMSENDIMAIVD", "text": "FUNCTION: Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GroES chaperonin family. SIMILARITY: Belongs to the GroES chaperonin family."}
{"protein": "MPKIIEAVYENGVFKPLQKVDLKEGEKIRLRIEEGIADVIKEFSRKVDQDVLEEFLRERR", "text": "FUNCTION: Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. SIMILARITY: Belongs to the UPF0165 family."}
{"protein": "MARVKRGNVARKRRNKILRLARGFQGSNGSLFRTANQRVMKALCNAYRDRRRRKRDFRRLWIARINAAARINGVSYSRLIGDLKKADVRINRKMLAQLAVMDPKSFTSVVTSAKS", "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": "MNWHFPFFILTTVTLSSVYSQLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTALAQTDLKEPLKALGITEMFEPSKANFAKITRSESLHVSHILQKAKIEVSEDGTKAAVVTTAILIARSSPPWFIVDRPFLFCIRHNPTGAILFLGQVNKP", "text": "FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the serpin family."}
{"protein": "MKYNIVLKFEVEGIVDKPDVIGAIFGQTENLFGEEFDLRELQDKGRLGRIYVNINTSKNKTEGEIIIPSNLDRIETALIAAMVENVDKVGPYNARFKLVEIQDIREEKIKKIIDRAKEILGTWTKEKTLDIKEVIYEISSAVKTGEIIEYGPDRLPAGPDVDKDPELIIVEGRADVINLLRYGYKNVIAIEGATGKIPQTIIDLAKQKKTVIAFLDGDHGGDLILKELLANNVKIDYVARAPTGKEVEELTGKEINKSLANMMTVAQYMKKQQEAQQALKEALAPESQPPIVVSKPTTPEQIKEITIKIPQHIIEEIKKLPGTLEGIMFDENWNPIERIQVRDIVQRLENLTDNQNISYIIFDGVITQRLLDLASAKNIKLLVGARIGGISKRPKNVEILTMTDLFTS", "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": "MNEILNTKDINAIGEFFIETWGCQMNEEDSEKLSGMLKKEGYIRTEERENADVIIFNTCCVRENAELKVYGNLGILKGLKSKNPNLIIAVTGCMMQQKGMAETIKKKFPFVDIIIGTHNLHNFPNYLNEVKKKDTSILKIQEKEDSIIENMPIDRKNSMKAFVTIMYGCNNFCTYCIVPYVRGRERSRTPENIEDEIKKLISEGYKEITLLGQNVNSYGKDLEPKVTFADLLERVNTIDGLERVRFMTSHPKDLTDDVIEAIAKCDKLCEQIHLPVQSGSSEILKKMNRHYDREKYLDVVSKIKKLIPNVALSTDIIVGFPGETEKDFEETLSLVKEVEYDSAFTFLYSIRKGTPAAKFEDQVPEDVKHKRFNRLVEVVNEISAKKNKAYEGKIEEVLVEGTSKNDENKLMGRTRTGKLVNFIGDKDSIGKLVNVKIIKANSFSLTGEEI", "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": "MVRAWRILQEETDDPRDALYSDESVSLEQLAQVGVEYFKFDADTFEQNDDYLKLKNNRGYSYSDTISVSRATLPDFDAKIKSFFEEHLHTDDEIRFILDGSGYFDVRDLDGRQLRDCWIRIECVKGDLLVLPSGIYHRFTLDKKDYIKALRLFIGVPVWTPHNRPADSMKERLDYVSKYLTATT", "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": "MKVFAIAAVAALTAVAVAGPVRPSGDKYLIELGPGKTQWVTKDQKHKMRAAGQTFIDITNEIGTNFVATKPVAANYPKNIAHSSMVSSMIANLSKENLMRDLQAMSEFNNRYYESQTGVESANWLMEQVKKVIDESGAQGAKVEKIDNQFNQFNIIATIPGSSESTVIVGAHQDSINQEDPMGGRAPGADDNGSGSVVVLEALRGVLGSKAFRAANNTNTLEFHWYAGEEGGLLGSQTVFSKYKSDGRQVKAMLNQDLAGFKGQGQEQFGLITDNTNQELNQFCKMIVEKYASIPIVDTECGYACSDHASADRNGFPASMVAETAFEDSNPHIHSADDTVEYLDFDHMLEHAKVALGFMTELGMASNL", "text": "FUNCTION: Probable extracellular aminopeptidase which contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily."}
{"protein": "MKFAIFVNTTREKALELARELTAWLDARSIDYVFDPQSAKALGCGKWEEKADLSQHCDAFVALGGDGTLLLASHYSRSKPVVGINVGDLGFLTEFSPDEMWVAMDHLVSGNYSIHTRSQLEATLESGESLTSLNDVIFEKGSAARRLPAFTILLDDEMLGSYRADGIIIATSTGSTAYSMSAGGPIIAPKSNVFVITPICPHMLTVRPIVISDDKTIKISVDSQSGEFPLKMDGIQKKLLAPGEVVTVKKSPHHINLVANEKRNYCEILRKKLLWSHEHPTGE", "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": "MTNIRKSHPLAKIINESFIDLPAPSNISAWWNFGSLLGVCLILQILTGLFLAMHYTADTMTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGMYYGSYTFSETWNIGILLLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIISALAAVHLLFLHETGSNNPSGVVSDSDKIPFHPYYTIKDILGLLLLILTLMLLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILAIIPLLHTSKQRSMMFRPLSQCLFWFLVADLLTLTWIGGQPVEHPFITIGQLASIFYFSILLILMPIFGTIENRLLKW", "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": "MAVQMEYEKDVKVPALDGKKIAVIGYGSQGHAHSQNLRDTGHDVIIGVRPGKSFDKAKEDGFDTYTVAEATKLADVIMILAPDEIQQELYEAEIAPNLEAGNAVGFAHGFNIHFEFIKVPADVDVFMCAPKGPGHLVRRTFEEGFGVPALYAVYQDATGNAKDIAMDWCKGIGAARVGLLETTYKEETEEDLFGEQAVLCGGLTALIETGFEVLTEAGYAPELAYFEVLHEMKLIVDLIYEGGFKKMRQSISNTAEFGDYVSGPRVITEQVKENMKAVLTDIQNGKFANDFVNDYKAGRPKLTAYREEAANLEIEKVGAELRKAMPFVGQNDDDAFKIYN", "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": "MQTLARLFGQSPFAPLQAHLEMVVSCVEYMLPIFTALRDGRYEELLEMAKLVSDKEYQADCIKNDMRNHLPAGLFMPISRAGILEIISIQDSIADTAEDVAILLTIRRLNFYPSMETLFFRFLEKNLEAFELTMTLLHEFNQLLESSFGGRKADKARLLVGRVAKSEHESDVLQRELMQIFFSDDFIIPEKEFYLWLQVIRRTAGISDSSEKLAHRINMTLEEK", "text": "SIMILARITY: Belongs to the UPF0111 family."}
{"protein": "MNIQDMILTLQKHWSSQGCVLMQAYDVEKGAGTMSPYTFLRSIGPEPWKVAYVEPSRRPADGRYGENPNRLYQHHQFQVIIKPSPDNIQELYLDSLRALGIDPLEHDIRFVEDNWENPSLGCAGLGWEVWLDGMEITQFTYFQQVGGLECKPVSVEITYGIERLASYIQDKENVFDLEWTSGFTVKDLFMMAEYEHSVYTFETSDVDMLFQLFSTYEKEAIKQMDNGLVHPAYDYVLKCSHTFNLLDAKGAISVTERTGYIARVRNLARKVAKTYYEEREKLGFPMLKGEGSSHE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MSEEKPTVRTEEDDRYEDDAGDLDLGQIGSRVWLVKIPKFLMDKWNSIPEDDAANLGCVRVKNDEIQLLLQNSPENADVPKIYNLRVMNKFVRNSYVFRESETSSSMKSTALVGTVAHECNVSPVINDDYRRVMQKRALAASAPKRKVQMIDDRGGSLLAPGTLGSRSRSTTSFIRNVKPRTGEGLKNSRIPRNELLDILFKCFEDYEYWTLKGLREYVKQPEVYLKEVLDSIAILNKRGPYALKYSLKPEYKGTMDAASVELRNQQASQSESSSIDHTGKNTSPDNPGTNAEEDEDDDGVEMIDVV", "text": "FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIF beta subunit family."}
{"protein": "MFKKKMLAASLSVGLIAPLASPIQESRANTNIENIGDGAEVIKRTEDVSSKKWGVTQNVQFDFVKDKKYNKDALIVKMQGFINSRTSFSDVKGRGYELTKRLIWPFQYNIGLTTKDPNVSLINSITLPKTKIETTDVGQTLGYNIGGNFQSAPSIGGNGSFNYSKTISYTQKSYVSEVDKQNSKSVKWGVKANKFVTPDGKKFAHDRYLFVQSPNGPTGSAREYFAPDNQLPPLVQSGFNPSFITTLSHEKGSKLIRVNLKFSYGRNLDITYATLFPRTGIYAERKHNAFVNRNFVVRYKVNWKTHEIKVKGHN", "text": "FUNCTION: Part of a bi-component leucotoxin that acts by forming pores in the membrane of the target cells. LukE-LukD is as effective as the Panton-Valentine leucocidin (PVL) for inducing dermonecrosis when injected in the rabbit skin, but not hemolytic and poorly leucotoxic on human blood cells compared to other leucotoxins expressed by S.aureus. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the aerolysin family."}
{"protein": "MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGVETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITDALKDKIKRAATTTDSDVVITEVGGTVGDIESLPFLEALRQMKADVGSDNVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEEPAGQGIKNKLAQFCDVAPEAVIESLDVEHIYQVPLNMQAQGMDQIVCDHLKLNAPAADMTEWSAMVDKVLNLKKTTKIALVGKYVELHDAYLSVVEALKHSGLANDTAIDIDWVNANDLTAENVASRLADADGIIVPGGFGQRGTEGKIQAIRYARENDVPMLGVCLGMQLTCIEFARHVLHLDGANSAELDPETQYPIIDIMRDQIDIEDMGGTLRLGLYPCKLKPGSKAAAAYGNQEVVQRRHRHRYEFNTKFREQFEAEGFVFSGVSPDNRLMEVVELPDKKFFVAAQYHPEYHSRPNHAEELYSAFVTAAVENAK", "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": "MFHGIKGCMIPMYWWLLGDLDLNGVRNSASSYSGGVNLSKLAVGLDLSEPASSKWSSTTSVKFEVPGHYLLQTLYMCVRLTMTDGRYQRSGRISYNMQNSLLCSGNTHDSMVVLKQESRFAKATDQGLSHFSMQIEQGIPVVSNWLIFNRFKFVASKGVRFGPAFPLASLTGGSIVGDMTPYQAFAIGGLGSVRGYGEVAVGSGRSCLVANTELANKMTEGTIFLDCGTDLGSSRLVPVSSLYLLRTRTIKKLLRHENDKAVAELVSGNPSLRQGKPGFGYGFGYGLRFKSPLGHLQVDYAMNAFNQKTLYFGITNLASST", "text": "FUNCTION: May play a role during plastid development. SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane. SIMILARITY: Belongs to the OEP80 (TC 1.B.33.2) family."}
{"protein": "MASLCLSLHQTLTNPLSAPRCRPLSLSFPGSSTFSIRPSSRRATALTTRASYTPTPATERVISIASYALPFFNSLQYGRFLFAQYPRLGLLFEPIFPILNLYRSVPYASFVAFFGLYLGVVRNTSFSRYVRFNAMQAVTLDVLLAVPVLLTRILDPGQGGGFGMKAMMWGHTGVFVFSFMCFVYGVVSSLLGKTPYIPFVADAAGRQL", "text": "FUNCTION: May be involved in protein precursor import into chloroplasts. Not redundant with TIC20-I, TIC20-IV or TIC20-V. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tic20 family."}
{"protein": "MKKHHLRHALLVLSAAILLAVSCSFSAASASASPPASEKKIAVWEAAILGVVEGITEYLPISSTGHLILASHALGMTQFSETRGPLGTLMVKNDAMDSYNIVIQLGAILAVLGLYRKRVKQMLKGLSGALAVLVSRRSVTALGDSERQGLKLLGLLLLAFLPAAVFGKLFHEVIETYLFGPLPVVYALVAGGVLMIGVEYFFWLKDRNRLRISDVNSMFYRQALFIGMMQVVSMWPGTSRSMITMIAGLIVGLDMIAAAEFSFLLALPTLGAATLYSGYKNWHALDDSAGMLALAVGLAVSWLTAVIAVKALVRWLTHHGLIPFGVYRILLAGVLLIYFWQWR", "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": "MTNIRKTHPLLKIINSSFVDLPAPSSLSSWWNFGSLLGVCLGVQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWLLRYLHANGASMFFICLYLHVGRGLYYGSYTYSETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFAFHFLLPFIVAALVMVHLLFLHETGSNNPTGIPSDPDMIPFHPYYTIKDILGFLVMLTALSALVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVASILILAIIPILHTSKQRSMMFRPLSQYLFWLLVATLFTLTWIGGQPVEHPYIIIGQTASILYFLIILVFMPTISIMENYLLKW", "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": "MKVSSHAMVPTHEIIPREEIPLLLEKYNIKLQQLPKLLDTDPLVLEVEAAPGDVLKITRMSPTAGESTYYRLVIATSL", "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": "MWLCPLALTLILMAASGAACEVKDVCVGSPGIPGTPGSHGLPGRDGRDGVKGDPGPPGPMGPPGETPCPPGNNGLPGAPGVPGERGEKGEAGERGPPGLPAHLDEELQATLHDFRHQILQTRGALSLQGSIMTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF", "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. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film. SIMILARITY: Belongs to the SFTPA family."}
{"protein": "MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRALSTPELYAGDGDLRVRVSTDKEKRTLTISDNGIGMSRDEVIDNLGTIAKSGTKSFLESMGSDQVKDSQLIGQFGVGFYSAFIVADKVTVRTRAAGANADQGVYWESAGEGDYTIADITKDDRGTEITLHLREGEDEFLDDWRVRSVISKYSDHIALPVEIESQTESEEEGGESTVSWEKINKAQALWTRSKSEVSDDEYNEFYKHISHDFTDPLSWSHNRVEGKQEYTSLLYIPAHAPWDMWNRDHKHGLKLYVQRVFIMDDAEQFMPNYLRFVRGLIDSNDLPLNVSREILQDSRVTQNLRNALTKRVLQMLDKLAKDDAEKYQTFWQQFGLVLKEGPAEDGSNREAIAKLLRFATTQSDSSAQTVSLEDYVSRMVEGQDKIYYITADSYAAAKSSPHLELFRKKGIEVLLLSERIDEWMMSYLTEFDGKSFQSVSKADDTLDKLADEENDAQKEAQKALEPFVERVKTLLGERVKDVRFTYRLTDTPAIVVTDADEMSTQMAKLFAAAGQQAPEVKYIFELNPEHALIKRAADVSDEAEFGEWVELLLDQALLAERGTLDDPNLFIRRMNQLLSA", "text": "FUNCTION: Molecular chaperone. Has ATPase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "MKDELNKVVIYTDGACSGNPGPGGWAAVLLFDDNEKTICGNDSDTTNNRMELTAVIEALKLLKVAYNVDLYTDSVYVKDGITLWIRKWKVNGWKTANKMPVKNLELWLELDSLANFHKVTWYWVRAHVGDLYNQKADMLARSQIVR", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase H family."}
{"protein": "MLQSTARTASKLVQPVAGVLAVRSKHTLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKGNLKEAIALQPALKFNGGGHINHSIFWTNLAKDGGEPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKILKIATCANQDPLEGMVPLFGIDVWEHAYYLQYKNVRPDYVHAIWKIANWKNISERFANARQ", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MSFKKAQSHFFLKNPERVRSLQKLSKKIGIKFSKVEYYNTAFIHSSYKNENQEILEDNERLEFLGDSVLGLVAARSLFRKYPKANEGELSRIKSRIVSTPILNSISEKLELSEYLLLGKGEKNSLGKGRRKLSANLFESLVGAIYLDQGFEIAEKFILRHLSEFVENPEKEESVRDYKTQLQEYSQKHFKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRIRKKT", "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": "MIAYVEGRLAEVAGNACVVVTDGGVGYEVFVPGHTLARLPDKGGRVSFFISTEVREDALELYGFATWDERQTFIVLTSISKVGAKTGLAILSQFRPDDLRRLVVEDDVLALTRVSGIGKKTAQHIFLELKYKLKVEDLPAAAPLVTGGAPGGVFRDALAGLANLGYGEEEASHVLKDVLHGEPDLDVGGALRAALRALARGR", "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": "MKNKLLARVARLGGLSSALLLAGCELDVLDPKGPVGEGVKTLIATSTVAMLIVVIPTILETLLFAWQYRQSNTSAEYLPKWCHSNKIEVTIWGVPSLIILFLAVITYQTCHSLDPYKPLEAEANTKPLHVEVVALDWKWLFIYPEQGIATVNQLAIPVNTPIDFNITSDSVMNSFFIPRLGSMIYAMAGMQTQLHLLASEPGDYLGESANYSGRGFSDMKFHTLAVSGDEFNAWVEKVKSSSEQLDSQTYPKLAAPSENPVEYFAHVEPGMFNTIVAKYNNGMVMDKSTGKMIQVQQSAMSDMNMKE", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
{"protein": "MTEQAEDALPIRFTDAAASKVKTLLEEEENDALKLRVYVTGGGCSGFQYGFTFDEKINEGDYTVEKQGVQLVVDPMSLQYLVGGEVDYTSGLEGSRFFVKNPNATTTCGCGASFSV", "text": "FUNCTION: Required for insertion of 4Fe-4S clusters for at least IspG. SIMILARITY: Belongs to the HesB/IscA family."}
{"protein": "MELISKALEAVRRYPLCDSCLGRLFALMGYGIENRERGQAIKTILHMAAVSDYRKGKDVTADLIALAKCHLPTRRFLAGVGIRVDEERCYICGDLMEGVEKYAEMAVEQLRGLDFVSFAVGSTLPEELLEKEAEVVKSLLVTTGESVKHEVNRRIGKELLRRLSDKRVDKLRPNVVVNVDLVSGQVKVVRNPILIGGRYLKLGRKIAQAKRFGNVRTTLLEKLAYLRDTFGGEDHVIHVSGREDSDARMLGSGRPLVVEVKQPLRYTAQVAPFRDKDVIFLPVGFTDRNEVRRLKEKAKTDIKLYRVLVLSESPLKQDDLSKLSALSGATVTQYTPRRIKRLHPRKKRVRMVYDVAWRLVSPHVFELYIRCQGGLYVKEFVHGDGGRTAPNVAELLNTRLEVLELDVLYIE", "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": "MASKIRRDDEVIILAGKDKGKTGKVTKVLVEDGKVFVEGINLIKKHTKPVPQLQQPGGIVEKEAPLQVSNVAIVNSATGKADRVGFRIEDGKKVRFFKSNNELI", "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": "MATSRTAPTRAPSLRSSPALEASPSRTKASVGALVILAVVALCVYLMDQITKALVVSNLSEGQQVAVLGQLLQLHFVKNPGAAFSIGSGSTWIFSLVGVGVLGFVIWYAPRIRSTAWAILFGLLLGGLLGNLTDRLFREPGFGVGHVIDFLQIPLLTAIFNLADVAIVFSMGLFLLLTLRGIGLDGRRQRDEGAGVSSASPAGDESAADKPENLSA", "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": "MPPPHRNHNFRPENVLKRAEDLIAVDKREAALETLYEFITSKRIRYLQVEDLEPIALLLMELAVDLRKGKLAKDALHQYKKNVQMSENGLESVQVVVKRFVDLAEKKLNDAQAKADIKIDQDEDEDLETSQTPESILMSAVSNTDTADRTERELVTPWLRFLWEAFRAVLDILRNNSKTEVTYSTIVNQAFQFCFRFNRKAEFRRLCELLRAHIQTVTTQPKTAGTTNAIDLSDSETIQRYLDQRFSQLNISVKLELWQESFRSVDDVHTLITASKKTPKPVMMANYYENLARIFAVSDNGLFHAAAWNKFFNLYSQSPNATDDELSHYASILVLSTLSIPQRSSNSNETVVDDHRAKNAKLSSLLNLSHVPTRDSLLKSIVSRQILSFVDPCVKKLFDVLGENNFHPLTIKKEIAALFKEIEADKDYKHYIKTLTEVVSVRIFQQVSQVYETVKLDFLVSLGIFEGTEYTLSALEVENLIAIATKEGHLALTIDHESGVVTFKSSPFEDSLSDSLTSRLQISPAELVRSQLQKFAYTLSKTVDTIDPENARRLEASREAAVKRAVAGISEEQEEIANRVKVMDERKRVIDVAKRKQDEEAARLKSERLSAEQKAEQERMLAEQERRSLEKLEREKHLIREREKRKIAEEINAKGIIKIDLDNLENLDTDKLRIMQIEQLNKDKKNLEEKLRALSKKTDHTERAFRRYELQYLEKDAEAQIEQEAKNYELVKANKIAKAKKDFEEAHALKERFTRLVPDYSEFKSEINAKNKDKLKQLQAEAKAQLERAKQERIEQIKRERIEELAQRKREQIQAEQEEARRRQKEEELAKLKEEIRLQREKDAEMLKRRQNVEAEVASRKAAITPAAPAEAKPMTYAEKLKLKRQQAGRS", "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": "MKYDNLLDRFIKYVKVNTRSDPDSETTPSTESQEAFALTILKPEMEAIGLQDVHYNPVNGYLIGTLPANNPTLTRKIGFIAHMDTADFNAENVNPQIIDNYQGGDITLGSSNYKLDPKAFPNLNNYIGQTLITTDGTTLLGADDKSGIAEIMTAIEFLTSQPQIEHCDIKVAFGPDEEIGVGADKFEVADFEVDFAYTMDGGPLGELQYETFSAAALEVTFLGRNVHPGTAKDQMINALELAIDFHEKLPAKERPEYTDGYQGFYHLTGLTGTVEEARASYIIRDFEEASFEARKVKVENIAQSMNAQLGTKRVLVELNDQYYNMKKVIEKDMTAIELAKEVMEELAIKPVIEPIRGGTDGSKISFMGIPTPNIFAGGENMHGRFEFVSLQTMERAVDVIIGLVCKA", "text": "FUNCTION: Cleaves the N-terminal amino acid of tripeptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20B family."}
{"protein": "MEERCESTESPQGQGRKNTKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLHGNKVIEHPCNEENPGKFLFDVVPGGERDRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGGGIFGQKLEDTVRYEKRYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVVPYAKYEDFLSCATLLSKEEEAGVKELMKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSAQNLATVFGPNILRPKVEDPLTIMEGTVVVQQLMSVMISKHDRLFPKDTEPQSKPQDGPNSNNNDGHKKATMGQLQNKENNNTKESPVRRCSWDKPESPQRSSVDNGSPTALSGSKTNSPRNSIHKLDISRSPPLMVKKNPAFNKGSGIVTNGSFSSSNAEGVEKPQTTPNGSLQARRTSSLKSSGTKMGTHSVQNGTVRMGILNTDTLGNSLNGRSMSWLPNGYVTLRDNKQKEPAGESGQHNRLSTYDNVHQQFSSMSLDDKHSVDSATWSTSSCEISLPENSNSCRSSTTTCPEQDFYVGNFEDPVLDGPPQDDLSHPGDYENKSDRRSVGGRSSRATSSSDNSETFVGNTSSNHSALHSLVSSLKQEMTKQKIEYESRIKSLEQRNLTLETEMLSLHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQFFSTFGDLTVEPRRSERGNTIWIQ", "text": "FUNCTION: Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell junction, adherens junction Cell junction, focal adhesion Cell projection Note=Localizes to actin stress fibers. In migrating cells, localizes to membrane lamellae and protusions (By similarity)."}
{"protein": "MTHPNELPLSPLSALQFYATAPYPCSYLDGRIARSQVATPSHLINSDVYTDLVKAGFRRSGVFTYRPYCDGCRACVPVRVPVDRFEPNRTQRRVWKKHGELIATVAPLHYDEEHYALYMRYQSARHAGGGMDRDSRDQYEQFLLQSRINSRLVEFREPPREWPEQPERPDAPGILRMISMIDILGDGLSSVYTFFEPGLPHTSFGTYNIYWQIEQARSLKLPYVYLGYWIRESPKMAYKANFHPLEGLIDGAWRVLDPTGLDLPPVDLAIHGKRPPFKP", "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": "MCPPQAQAEVGSAMTEKTEMVCTSSPAPAPPSKPASPGPLPAEEVDHRNTCNPWLPPGVPVINLGHTRPTGAAMPTTELSAFRPSLLQLAALGTAPPTLALHYHPHPFLNSVYIGPAGPFSIFPNSRLKRRPSHGELDLVDGHQPQKVARRVFTNSRERWRQQHVNGAFAELRKLLPTHPPDRKLSKNEVLRLAMKYIGFLVRLLRDQAAVLASGPSAPGSRKPPAHRGVEGNARCGAGHRVEAARSQPVLPGDCDGDPNGSVRPIKMEQTALSPEVR", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNAFLHAISFFTRIPVPWLRPSEEAWRKSVNWYPAVGLVIGLLLWGVHQAGLVLFSPWIAAILTLIAWVYVTGGLHMDGWMDLADGLGSSRPREQILAIMKDSRVGAMGVLAAIMLLLIKAGAVAELAHPGWGSFLIVAPVAARTHVLLSIKLWPYLSADKGIGKGISSGLSVSSIIVSYIIVFAAGWYLGGLQVMTAIFLSLLFALWFSRSVAKKLGGLNGDCYGAVIESSEAVVLLVLVGSWWL", "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": "MLGIWTLLPLVLTSVVRLLSKCVNAQVTDISSKGFELRKIVTTIETQNLEGLHHEGQFCRNPCPPGERKARDCTVNEDEPDCVPCQEGKEYTDKGHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSAVCEHCDPCTKCEHGIIEECTLTSNTKCKEEDSRSDLPWLCLLLLLIPPIVYVVIKKACRKHRKENQGPHESTTLNPETAINLSDVDLSKYITTIAGAMTLSQVKDFVRKNGVSEAKIDEIKNDNVQDTAEQKVQLLRNWYQLHGKKDACDTLIKGLKTADLCTLAEKIHAVILKDITSDTENSNFRNEIQSLV", "text": "FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen- stimulated suicide of mature T-cells, or both (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane raft."}
{"protein": "MTTPAHVAIIMDGNGRWAKARGMPRLAGHRAGVEALRKTVRAAPDLGISFLTVYAFSSENWSRPKAEVSDLMGLLKLFIRRDLAELHQSGVRVRIIGDRAGLQADIRGLLEEAESLTARNESLTLVIAFNYGGRDEIVRTARKLASAAARGEIDAESITADSFAGGLDTQGIPDPELVIRTSGELRLSNFLLWQAAYSELVFLPCYWPDFSREHLAEALREFAGRERRFGGLGQQDVASRPAAG", "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": "MGYVRTGILMAVMTALFLGVGALIGGQSGAIIALVIAAGMNLFTFWNSDRAVLSMHGAHEVDPRAAPDLYNMVRGLADRAGMPMPKLYLIETDQPNAFATGRNPENAAVAVTRGLLRALTPEEVAGVVAHELAHIRNRDTLLMTVTATFAGAISMLANFAFFFGGSSNEEGERPMGLVGTLALMFLAPLAAGLVQMAISRSREYEADRIGAEICGRPLWLASALGKIEGLAQRIDNVRAERNPATAHMFIVNPLHAMGHDRLFATHPNTANRIAALRAMAEGAPQASRIPRVAARRGPWS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
{"protein": "MKIAQELRAGNVVMIGKDPMVVQKAEFSKSGRNASVVKMKLKNLLTGAGMESVYRADDKFDTVTLDRKECTYSYFADPLYVFMDSDYNQYEVEGDNLGDALNYLDDGMPVEVVFYEGKAISVEMPTTVIREVEYTEPAVRGDTSGKVMKPARIKPTGFELPVAAFVEIGDMIEIDTRTNEFKRRAN", "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": "MRTHMTANRKIYISDVTLRDGSHAIRHQYSVNDARRIAQALDEARVDSIEVAHGDGLQGSSFNYGFGAHTDLEWIHAVASVVKHAKIATLLLPGIGTVHDLKAAYDAGVRVVRVATHCTEADISRQHIECARELGMEAVGFLMMSHMTTAEVLAGQAKLMESYGATCCYVVDSGGALSMQDVRDRFRALKDVLKPETHTGMHAHHNLSLGVANSIVAVESGCDRVDASLAGMGAGAGNAPLEVFIAAAERMGWNHGTDLYKLMDAADDIVRPLQDRPVRVDRETLALGYAGVYSSFLRHSETAAAKYGLKTVDILVELGKRRMVGGQEDMIVDVALDLLRQRRSGAAAV", "text": "SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family."}
{"protein": "MALPKFELLSLADNTVGWGPLASSSSADEPVPFQQFNKADRIGRVADWIGVDRFYRRGNERYNERVYGSAANAGSQFDYIHGMDEHNFQLVDTSKPMARNPQRNFRVRQMHLRKMMQKENEKREMVNQSTNLRMKRSIAKEQQRAFKMWQRRGGNARQGQRGQGGRFGGDRPKERLPSVQVRPEWVVLEEMNLSAFSKLALPNIPGGDDIGDHQYGSLQYYDKTIDRVSVKNSIPLQRCAGVFYNVTTTEDPVIQELAQGGAGNVFGTDIILATLMTAPRSVYSWDIVAYRVGDKLFFDKRNTRDILNPVETLTVSETSAEPPSFDGNGINNAKDLATEAFYINQNFRRQVVKRNDAGFTFKNARAPFEDEETGESGTAYKYRKWNLGNGVDGKPVELVCRTELDGVIHGLGNETQTLTIKAFNEWDSTQSGGVDWRTKLDVQKGAVMATEIKNNSAKVAKWTLQALLAGSDTMKLGYVSRNNARSTQNHSILLTQYVKPTEFASNIALNMDNCWGILRCVIDSCMKQKPGKYLLMKDPQSPVIRLYSLPEGTFESERESSDEENSDDDQ", "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": "MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALTQQATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALVAKLA", "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": "MNDNPVRNFAINFGPQHPAAHGVLRLVLELDGEVVERVDPHIGLLHRGTEKLMEARTYLQNVPYFDRLDYVAPMNQEHAFCLAIEKLLGIEVPRRGQLLRVLWCEIGRILSHLLNVTTQAMDVGALTPPLWGFEEREKLMVFYERASGARMHANYFRPGGVHIDCPQQLIDDIGAWCDPFLKVCDDLNDLFIENRIFKQRNVDIGVISLEDCWRWGFSGVMVRGSGAAWDLRKAQPYECYEEMDFDIPVGRHGDNYDRQVIRMEEMRQSTKIMKQCVEKLSQASGKGPVATPQHKVVPPSRAEMKRSMEALIHHFKLYTEGFHVPAGEVYCGVEAPKGEFGVYLVSDGTDKPYRCKIRAPGFAHLSAMDFLCRKSMLADVSAILGSLDIVFGEVDR", "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": "MNKTIEYQKEFLKENNQLLNIPIKKNILKEILQNDEQDTIITNCITKEVSINLDLIKNPKVLYSIYIMVVEYLKSINIT", "text": "SIMILARITY: Belongs to the asfivirus D79L family."}
{"protein": "MIRFEIHGDNLTITDAIRNYIEDKIGKLERYFNDVPNAVAHVKVKTYQNSTTKIEVTIPLKNVTLRAEERHDDLYAGIDLVTSKLERQVRKYKTRVNRKHKTHGEPEAFVAEVQEAPPENVDDVNAEPTNDSEIEIIRSKQFSLKPMDSEEAVLQMELLGHDFYIFTDRETDGTSIVYKRKDGKYGLIETTE", "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": "MSTITSYFGFLLAASTITPALLIGLSKIRLI", "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": "MAQIHHCVTLLLILCCSGLCGAIQWLGLTVNGSRVAWNESGHCRLLDGLVPEQSQLCKRNLELMQSVVNAAKQAKLTCQMTFSDMRWNCSSVENAPNFTPDLSKGTRESAFVYALASATLSHTIARACASGELPTCSCGATPAEVPGTGFRWGGCGDNLHYGLNMGSAFVDAPMKSSKSGGTQATKMINLHNNAVGRQVLMDSLETKCKCHGVSGSCSVKTCWKGLQDLPHIANELKSKYLGATKVIHRQTGTRRQLVPRELDIRPVRESELVYLVSSPDYCAKNPKLGSYGTQDRVCNKTSVGSDSCNLMCCGRGYNAYTETIVERCQCKYYYCCYVVCKKCERTVERYVCK", "text": "FUNCTION: Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally initiates dorsal/ventral axis formation by a canonical route, which signals via lrp6. In a complex with wnt5a, activates the canonical and non-canonical processes involved in axis formation. In the non- canonical pathway, acts through fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate convergent extension movements during gastrulation. Interactions with the secreted Wnt antagonist sfrp5 to coordinate foregut development, acting via a non-canonical wnt pathway whereby sfrp5 restricts wnt11b activity to prevent inappropriate foregut formation. Mediates cardiogenesis via non-canonical Wnt signaling involving JNK-activation and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MFSLPLNCSPDHIRRGSCWGRPQDLKIAAPAWNSKCHPGAGAAMARQHARTLWYDRPRYVFMEFCVEDSTDVHVLIEDHRIVFSCKNADGVELYNEIEFYAKVNSKPVWLSVDFDNWRDWEGDEEMELAHVEHYAELLKKVSTKRPPPAMDDLDDDSDSADDATSN", "text": "SIMILARITY: Belongs to the p23/wos2 family."}
{"protein": "MFKNAFQSGFLSVLYSIGSKPLEIWDKQVSNGHIKRITDADIQSSVLEIMGQNVSTTYITCPADPNKTLGIKLPFLVLIIKNLNKYFSFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDSGWNQIQFNLSDFTRRAYGTNYIETLRVQVHANCRIRRIYFSDRLYSEEELPAEFKLFLPIQKS", "text": "FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility (PubMed:24259666, PubMed:24574454). Involved in the control of flagellar beating in an asymmetric and planar waveform (PubMed:24259666, PubMed:24574454). Stabilizes outer doublet microtubules (DMTs) of the axoneme and may work as a scaffold for intratubular proteins, such as tektin and PACRG, to produce the beak structures in DMT1, 5 and 6 (PubMed:24259666, PubMed:24574454). Not essential for flagellar assembly (PubMed:24574454). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes predominantly along the length of all nine axonemal outer doublet microtubules (DMTs). Localizes to the inner junction (IJ) between A- and B-tubules of the DMTs. Associates to the basal bodies in a microtubule-dependent manner. Enters into the flagella through diffusion. SIMILARITY: Belongs to the CFAP20 family."}
{"protein": "MARGLGAPHWVAVGLLTWAALGLLVAGHGGHGDLHEDLHEDFHGHSHRRSHEDFHHGHSYAHGHGHTHESIWHGHTHGHEHGHAHEDLHHGHSHGQSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHPLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHTHGHTQGSHGHGTQKYPSKEKQSSEEEEKEANGSRKRKGGSTRLKDGPLRPQNSEEEKTGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAIGALAGTACALLTEGGAVGSEVAGGTGSGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVVMMVLIAHLE", "text": "FUNCTION: Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling (By similarity). Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle (By similarity). Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. KE4/Catsup subfamily."}
{"protein": "MTKKKNKKVTKSERGEANRRLAENRLARHQYEILETLETGIELVGTEVKSIRAGNTNLRDGFCLIREGELQLHNVHISPLNNAGNFFNHDPLRTRKLLAHRKEINKLEIQVARKGLTLIPLSIHLKGSWIKIIIGVGKGRKLHDKREDDKRKQANRDMKSALARYR", "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": "MKLILTADVENLGVAGDIVEVKDGYGRNLLLPRGLAIVATRGAEKQIEGIKRAQEAREIRDLDHAREVKAQLEALEGVSVAVRTSEKGKLFGSVKAEDVAAAVKKAGGPNLDKRSIELPKSLVKATGAYKVNVKLHSDIAATVNFEVVAA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MAISAQAVKELRERTGAGMMDCKRALEETAGDMEKAIDLLRERGVAKAAKKSGRIAAEGLTATAVAGNVAAVVEVNCETDFVGKNPEFQTLVKDIAEHVVSQRPASVEEALEQPFKGAGETLGHVINEKIATIGENISFRRFALSEKTDNGVFGAYLHMGGRIGVLVTLEGTQDETLARDLGMHAAASNPRFANREEVSADEIEREREVLKNQALAEGKPANIVEKMVEGRLSKFFEEYVLVEQPFVKDTDKKVAVLLKEAGATLKGFARFQVGEGIEKKQEDFAAEVMAQVNKQ", "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": "MNGMCWIASYPKAGGHWLRCMLTSYVTGEPVETWPGIQAGVPHLEGLLRDGEAPSADPDEQVLLATHFTADRPVLRFYRESTAKVVCLIRNPRDAMLSLMRMKGIPPEDVEACRKIAETFIADEGFSSVRIWAGEGSWPENIRSWTDSVHESFPNAAVLAVRYEDLRKDPEGELWKVVDFLELGGRDGVADAVANCTLERMREMEERSKLLGLETTGLMTRGGKQLPFVGKGGQRKSLKFMGDDIEKAYADLLHGETDFAHYARLYGYAE", "text": "FUNCTION: Catalyzes the sulfonation of desulfo-A47934, the final step of A47934 biosynthesis. Has also weak activity in vitro with teicoplanin aglycone and teicoplanin. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MDVLHRLAEILEQRKTEAPDKSYAASLYAKGLDTILKKIGEEATETVIAAKDGEPGKIVYEMADLWFHCCVLLAQQGLGPDDVLRELGRRFGMSGLEEKASRKLG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MSKLMLIGTNYWYPSKFGCTIFRKVRFQSTLKCTSTARTQPIDPSAKTIRHLQFVKEIPFETGIDIQEKFVRAHLDIKQLQSKIKREMTNLQKEHNAEIQLNFHEQMILDNINQMKPNPIVLTFQFEPTYTGGKRVKKQITDEQIARYEGFIPSKQKYNKKPKFVQAERGGQVTFHGPGQIVAYIILDLKTFQNLPAKCLVSTIDNAAMNALKVVPKFQGSDEPLNLITQKTNDTGVWVSNQEKIASIGIHVRRSVTSHGICINVDPDLSYMNSFTMCGLSEKKATSIREQVPDSSTSVNDVAVAFVNQLAKLLGITTVERIQLDDLPIYTD", "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: Mitochondrion. SIMILARITY: Belongs to the LipB family."}
{"protein": "MKKLFFFVLIGSSILGFTREVPPSILLKPILNPYHMTGLFFPKVNLLGDTHNLTDYHLDNLKCILACLQRTPYEGAAFTVTDYLGFSDTQKDGIFCFKNLTPESGGVIGSPTQNTPTIKIHNTIGPVLFENNTCHRLWTQTDPENEGNKAREGGAIHAGDVYISNNQNLVGFIKNFAYVQGGAISANTFAYKENKSSFLCLNNSCIQTKTGGKGGAIYVSTSCSFENNNKDLLFIQNSGCAGGAIFSPTCSLIGNQGDIVFYSNHGFKNVDNATNESGDGGAIKVTTRLDITNNGSQIFFSDNISRNFGGAIHAPCLHLVGNGPTYFTNNIANHTGGAIYITGTETSKISADHHAIIFDNNISANATNADGSSSNTNPPHRNAITMDNSAGGIELGAGKSQNLIFYDPIQVTNAGVTVDFNKDASQTGCVVFSGATVLSADISQANLQTKTPATLTLSHGLLCIEDRAQLTVNNFTQTGGIVALGNGAVLSSYQHSTTDATQTPPTTTTTDASVTLNHIGLNLPSILKDGAEMPLLWVEPISTTQGNTTTYTSDTAASFSLNGATLSLIDEDGNSPYENTDLSRALYAQPMLAISEASDNQLQSESMDFSKVNVPHYGWQGLWTWGWAKTENPTTTPPATITDPKKANQFHRTLLLTWLPAGYIPSPKHKSPLIANTLWGNILFATENLKNSSGQELLDRPFWGITGGGLGMMVYQEPRKDHPGFHMHTSGYSAGMITGNTHTFSLRFSQSYTKLNERYAKNYVSSKNYSCQGEMLLSLQEGLMLTKLIGLYSYGNHNSHHFYTQGEDLSSQGEFHSQTFGGAVFFDLPLKPFGRTHILTAPFLGAIGMYSKLSSFTEVGAYPRTFITETPLINVLIPIGVKGSFMNATHRPQAWTVELAYQPVLYRQEPSISTQLLAGKGMWFGHGSPASRHALAYKISQKTQLLRFATLQLQYHGYYSSSTFCNYLNGEVSLRF", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Cell outer membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the PMP outer membrane protein family."}
{"protein": "MPFTYHRTIHFQDTDAAGVVYFANILSICHEGYEASLRTSGISLKEFFTNPNMAFPIVHASVDFLRPLFCGDQVIISLVPQKIGAEKFEINYEIYLADVLVAKAVTRHVCIDANTRSKQELSTEIIQWLDGYRKETEEVERRKAREVV", "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": "MLEKEEIVSPNLEELKSHYHSIITLLGEDAGREGLLKTPERVAKAMLSLTKGYHMDPHEVLRSAKFQEEYSQMVIVKDIDFFSLCEHHMLPFYGKAHVAYIPNGYITGLSKIARVVDIFSHRLQVQERMTLQIKDCIQETLNPLGVMVVVEAKHMCMQMRGVEKQNSITTTSDFTGAFNQAKTREEFMNLIQHGRV", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I family."}
{"protein": "MNIKKLSLCIFFATTQVHAFTQWGAGGITPMGHEWLTRTSALEVLNAEHKTSVDPNDPRNTWTSGLAKNIDISTADDEVAKIKSHTNDNSLYAPRSDAVYSAIVGQRWVDLGGMNVANNLISQTGPDCFDAVSQEPADIQQDHFMRRYDDNGQQGGVKSAQRGQERFITHFINAAMATNKRIVVWDGGGSSAKTDVDYNYFLFGRAVHLFQDSFSPEHVVRSPSDNYEKVRQVKAYICTEGAEQHAHSTGAVLDYTSGDVIWKVGTKTDTGWGGYKASNMKPVALVAMEASKDLWAAFMRTMSVDINEREKYARNEAQVLIDKWMSFDKDEMEHWYDNENNRDNTYVKVDGDTGKGKLQKECMSGLSAKNRYGATIKPKTQKELVDVLDDSRRYCLFNIEAEPGYADANDPYLNIPFNWRWKSNSWLVPNASWQQKQLDRDTGKIIKIKEFTNNQELTVDSIENNYSIVTGAKKPLSLVRVPGDGGKSFYLRSKDNPYLFFSYSDKKNGRIKLWHSPNQAEFEILPGNNIFNLKNTYWNQYVWYDKNSKGAYLTEKGSPDNASSKWIISEEN", "text": "FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined."}
{"protein": "MSLEERVMELESRMAFQDDTIQALNDVLVKQRREFDHLQQQMAAMIKRQEEMGSQFDTFEEEAPPPHY", "text": "SIMILARITY: Belongs to the SlyX family."}
{"protein": "MDLNTILIILGILALIGLVAHGIWSNRREKSQYFDNENAFHRNPQSTGRPSAQASQPMTPNFAQPAKETEQIRQTYQEPQVRQMSSSPEQQTRPTAQAMPENRAEFNPNTVQPEQQPLDFNAAENIKITLPNTETRAGGAEPIRYEYHAEEERSAPLEQTFNQPVYTEDRAVPDMQVSLRQPAPESPISQPTLQQPVNDAPAYQHSQPAPAEPTDFIMLYVVAPENRQFHGPSLAQALDNLGFIFGQGNIYHRHLDLTVASPAIFSVANINQPGTFNPHGMQDFSTVGVALFMQLPVAGNPRANLKMMIQAAKNLASQLGGFVLTEQQEEFDVMAEAAYLARV", "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": "MDSNHQSNYKLSKTEKKFLRKQIKAKHTLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKELRPQALPPGLMVVEEIISSEEEKMLLESVDWTEDTDNQNSQKSLKHRRVKHFGYEFHYENNNVDKDKPLSGGLPDICESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSLGSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQASESLKSGIITSDVGDLTLSKRGLRTSFTFRKVRQTPCNCSYPLVCDSQRKETPPSFPESDKEASRLEQEYVHQVYEEIAGHFSSTRHTPWPHIVEFLKALPSGSIVADIGCGNGKYLGINKELYMIGCDRSQNLVDICRERQFQAFVCDALAVPVRSGSCDACISIAVIHHFATAERRVAALQEIVRLLRPGGKALIYVWAMEQEYNKQKSKYLRGNRNSQGKKEEMNSDTSVQRSLVEQMRDMGSRDSASSVPRINDSQEGGCNSRQVSNSKLPVHVNRTSFYSQDVLVPWHLKGNPDKGKPVEPFGPIGSQDPSPVFHRYYHVFREGELEGACRTVSDVRILQSYYDQGNWCVILQKA", "text": "FUNCTION: Catalyzes the methylation of 5-carboxymethyl uridine to 5- methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain (PubMed:20123966, PubMed:20308323, PubMed:31079898). Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA (PubMed:20123966, PubMed:20308323). Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys)(PubMed:20308323). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)- methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly) (PubMed:21285950). Required for normal survival after DNA damage (PubMed:20308323). May inhibit apoptosis and promote cell survival and angiogenesis (PubMed:19293182). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. SIMILARITY: Belongs to the alkB family."}
{"protein": "MESVLNNEKAIVVFSGGQDSTTCLFYAKKHFKEVELVTFNYGQRHDTEIEVAKQIAQDQGMKHHVLDMSLLSQLTPNALTQHDMEITNNEDGIPNTFVPARNLLFLSFAGALAYQIGAKHIITGVCETDFSGYPDCRDSFIKSMNVTLSLAMDKDFVIHTPLMWLNKAETWKLSDELEVLDYIRTKTLTCYNGIIGDGCGECPACHLRQRGLNQYLESKGAL", "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": "MLFEIIYIVSSLFYIVSIIYTLMRIKHINTVAKKEEIRKEIIEYMRSDEVTNIIVKALNESDINKKLNAIVLALCTHVQELKKSKLCEG", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass type II membrane protein."}
{"protein": "MKNKGKIIQILGPIVDVKFNENQLPKLLNALTIEFEKTKITLEVAQHIGNDVVRTIAMSSTEGLVRNLEVIDTEAPISVPVGKNVLSHMFNVIGENIDNQSIDPNTEKWSIHRKAPSYEEQTATSEILETGIKVIDLLVPYVKGGKIGLFGGAGVGKTVLVQELINNIAVHHGGLSVFAGVGERTREGNDLYYEMKASGVLDKTALVFGQMNEPPGARMRVALSGLTMAEYFRDELNQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTRKGSITSIQAVYVPADDLTDPAPATTFIHLDAQTVLDRNIASLGIYPAIDPLASASRMLSADIVGEEHYKIAREVQRILQKFKELQDIIAILGMDELSDEDKNIVYRARKIRNFLSQPFHVAEKFSGIKGTFVKLSDTLRSFRDILDGKYDDLDESAFLYVGTIEEAKQKHLKNYKGDHVEK", "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": "MINLNGVQFSYNTFTFELDLQIPAQQKVAIIGASGAGKSTLLNLIAGFALPQQGEIWLNGENHSQTQPYERPVSILFQENNLFTHLTVAENMALGLKPSLKLTALEQQRVQQVASAVGLQGFLNQLPTQLSGGQKQRVALARCLLRDKPILLLDEPFSALDPDLRAEMLHLLLQLCDEKKLTLLIVTHQVNELQQKMDRMIRFEHGRMSESTILKDNFNEKQTAL", "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": "MLLAEVAATSDAVAATRSRLAKRAAIADLLRRAPADDVEIVVAYVAGELRQRRTGLGWRSLRDLPGPAEDPSLEVADVDATFAAMADLAGPGSATARAAAAAELFAAATEREQALLRGLVSGELRQGALDALVLDAVADAAGVPAPEVRRAAMFAGATGPVARAALAAAGPAEAVAALSGFMLTVGRAVRPMLAQSAPDVAAAFAKLPGGDVAVSVDVKLDGIRIQVHKAGDEVRVFTRSLDDITGRVPEIVEAVRALPAGALVLDGEALAVDAGGRPRPFQETASRSATRDADVAAAMTLTPFFFDCLHADGRDLVDAPLRERLEVLDAVAGPHVVTRLTTSDPAAAEEFFAAAVRDGQEGVVVKATDTPYEAGRRGAGWIKVKPRHTLDLVVLAVEWGSGRRRGWLSNIHLGARDPAGGFVMLGKTFKGMTDEMLAWQTERFLELETSRDEWAVHLRPEQVVEIAFDGLQRSTRYPGGLALRFARVLRYRDDKTAAEADTIDTVRTLAGL", "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": "MDSLALAPQVYSRKDKSLGVLVANFLTLYNRPDVDLFGLDDAAAKLGVERRRIYDVVNILESIGLVARSGKNQYSWKGFGAVPRALSELKEEGMKEKFAIVPFVAKSEMVVYEKEGEESFMLSPDDQEFSPSPRPDNRKERTLWLLAQNFVKLFLCSDDDLVTFDSATKALLNESQDMNMRKKVRRLYDIANVFSSMKLIEKTHVPETKKPAYRWLGSKTIFENRFIDGSASLCDRNVPKKRAFGTELTNVNAKRNKSGCSKEDSKRNGNQNTSIVIKQEQCDDVKPDVKNFASGSSTPAGTSESNDMGNNIRPRGRLGVIEALSTLYQPSYCNPELLGLFAHYNETFRSYQEEFGREK", "text": "FUNCTION: Inhibitor of E2F-dependent regulation of gene expression. Binds specifically the E2 recognition site as a monomer without interacting with DP proteins. May be up-regulating E2FA and down- regulating repressors of cell cycle progression. Promotes cell proliferation and represses cell elongation. Regulated by proteolysis via a ubiquitin-proteasome pathway. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family."}
{"protein": "MKIFVGNVDGADTTPEELAALFAPYGTVMSCAVMKQFAFVHMRENAGALRAIEALHGHELRPGRALVVEMSRPRPLNTWKIFVGNVSAACTSQELRSLFERRGRVIECDVVKDYAFVHMEKEADAKAAIAQLNGKEVKGKRINVELSTKGQKKGPGLAVQSGDKTKKPGAGDTAFPGTGGFSATFDYQQAFGNSTGGFDGQARQPTPPFFGRDRSPLRRSPPRASYVAPLTAQPATYRAQPSVSLGAAYRAQPSASLGVGYRTQPMTAQAASYRAQPSVSLGAPYRGQLASPSSQSAAASSLGPYGGAQPSASALSSYGGQAAAASSLNSYGAQGSSLASYGNQPSSYGAQAASSYGVRAAASSYNTQGAASSLGSYGAQAASYGAQSAASSLAYGAQAASYNAQPSASYNAQSAPYAAQQAASYSSQPAAYVAQPATAAAYASQPAAYAAQATTPMAGSYGAQPVVQTQLNSYGAQASMGLSGSYGAQSAAAATGSYGAAAAYGAQPSATLAAPHRTQSSASLAASYAAQQHPQAAASYRGQPGNAYDGAGQPSAAYLSMSQGAVANANSTPPPYERTRLSPPRASYDDPYKKAVAMSKRYGSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHSDYARYSGSYNDYLRAAQMHSGYQRRM", "text": "FUNCTION: May function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CENPJ complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CENPJ. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Cytoplasm Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Cytoplasmic localization is crucial for its function in suppressing the formation of aberrant centriolar protein complexes."}
{"protein": "MITLLNLLLAEIAGFITYQHFTASPLRYFIPYPAELLLFAIPLVGLAVRRPFSFYYYSVLIFFNISPILARSETFEGIIDTLNAIDALYNTGTSAIAESLKVAFIGHSTSVDGLLAVTWLYILAEVFQGNWESIKGAKTGGVEIERAYLVYLPAFFFALLVYFLYPFLMSEIDFGLERIVAAVLGIAAFFAGVYLLSRGVEEEDINSGG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MPFVVVSGLSGSGKSTALRALEDAGFFITDNLPPELWGAMYDLSKARGLTRVAVSTDARTRDFLSALDDSYIRLSRREEDLHTLYLEANSEVLLKRYNFTRREHPLGETLMVDFARERELLAPLRAIADTVIDTTDLSATDLAERVLRLFRLEHDFHLRLLSFGFKHAPPRDADLVLDVRSLPNPHYDPVLRPRTGLEREVAQYVFQNQAGEDFYANLRDFVRTSAERARDTGRHGYTVAIGCTGGQHRSVAVASRLAADLRDLNVDITDHRDMKAGTRE", "text": "FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family."}
{"protein": "MGKMRVRFPTLVLVLGIVFLMAVSIGIAYGEKDVLKSHERPEEREQEEWQPRRQRPQSRREEREQEQEQGSPSYPRRQSGYERRQYHERSEQREEREQEQQQGSPSYSRRQRNPYHFSSQRFQTLYKNRNGKIRVLERFDQRTNRLENLQNYRIVEFQSKPNTLILPKHSDADYVLVVLNGRATITIVNPDRRQAYNLEYGDALRIPAGSTSYILNPDDNQKLRVVKLAIPINNPGYFYDFYPSSTKDQQSYFSGFSRNTLEATFNTRYEEIQRIILGNEDEQEYEEQRRGQEQSDQDEGVIVIVSKKQIQKLTKHAQSSSGKDKPSDSGPFNLRSNEPIYSNKYGNFYEITPDRNPQVQDLNISLTYIKINEGALLLPHYNSKAIYVVVVDEGEGNYELVGIRDQQRQQDEQEEKEEEVIRYSARLSEGDIFVIPAGYPISINASSNLRLLGFGINADENQRNFLAGSKDNVIRQLDRAVNELTFPGSAEDIERLIKNQQQSYFANGQPQQQQQQQSEKEGRRGRRGSSLPF", "text": "FUNCTION: [Blad]: Has a lectin-like activity. FUNCTION: Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling. SIMILARITY: Belongs to the 7S seed storage protein family."}
{"protein": "MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPNSGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKISGPQYRLEKQSEPNVAVDLESTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTSQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ", "text": "FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasmic vesicle Nucleus. SIMILARITY: Belongs to the SIN1 family."}
{"protein": "MTKSLSEQLFETAEGLLPGGVNSPVRAFRAVGGVPRFIDRAEGSRIYDIDGREYIDYVGSWGPMILGHSHPQVVEAIRKAVERGTSYGAPTPGEIALARTIIEAFPSMEMIRMVSSGTEAVMSAIRLARGFTGRDKILKFEGCYHGHGDSLLVKAGSGVATLGIPGSPGVPACLAELTITVPFNSNEAFRKAVDRHGKELACVIVEPVAANMGVVNPRPGFLETLRELTRKAGIVLIFDEVITGFRLAYGGFQKLCRLEPDLTCLGKIIGGGLPVGAFGGKRTIMDFLAPNGPVYQAGTLSGNPLAMSAGLATLETLRSRRDDYAALDRRTADLCAAMGKLFRTAELPVRINRAGSLFTVFFTDSDVFDYETASHCNLERYARFFKGMLDRGVYLAPSAFEAAFVSFAHSDEDLEKTLQACAETIKTLGGNP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
{"protein": "MSDSKEPRLQQLGLLEEEQLRGVGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSLSQGQSKQDAIYQNLTQLKAAVSELSEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVDGLPDRSKQQEIYQELTQLKAAVDGLPDRSKQQEIYQELIQLKAAVERLCRPCPWEWTFFQGNCYFMSNSQRNWHNSITACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNHEGTWQWVDGSPLLPSFKQYWNKGEPNNIGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSGDEERLLSPAPTTPNPPPE", "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": "METQAKLRFSRVSPQKARLVADQIRGLPVDDALRTLEYSPRKAAEIVRKVLESAVANAEHNDGADVDELRVARIFVDEGPTMKRIQPRAKGRANRILKRTSHITVAVAED", "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": "MHVTLVEINVKEDKVEQFVEVFRANHQGSLLEPGNLRFDVLQDESIPTRFYIYEAYVDEAAVAAHKKTPHYLRCVEELEGLMTGPRKKTTFIGLMP", "text": "FUNCTION: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5- phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5- phosphonooxypentane-2,4-dione (P-HPD). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LsrG family."}
{"protein": "MVRFESTDSLMLARQLPNKTVALILAGGRGSRLKDLTATRAKPAVHFGGKFRIIDFALSNCLNSGVRRIGVITQYQSHTLVQHIQRGWSFLNEEMNEFVDLLPAQQRLSTEQWYKGTADAVCQNLDIIRRYDAEYIVILAGDHIYKMDYSRMLLDHVEKGAECTVACIPVPISEGSEFGIMEVTADYQITAFYEKPANPPPIPGDPSNALASMGIYIFNADYLFKLLEEDNNTPGSSHDFGKDIIPQLTARKVVWAHPFDLSCVTSNAELPPYWRDVGTLDAYWRANLDLASVTPELDMYDRAWPIRTHMEPLPPAKFVQDRSGSHGMTMNSLVSGGCIVSGSVVVHSVLFPRVRVNSFCTIDSSLLLPDVHVGRSCRLRRCIIDRACHIPEGMVIGENADEDSARFYRSEGGGGVSDSGYAGKVRGKIEPLGFLFVRLDLLIRLSLLIRLNLFIRMNLLIILTLFFKLASIQASH", "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": "MRLFRSREVVGIAADALDFALEASAETHPNEYMGLLRGEEARRVGVDRDGYVVTDVLIIPGTVSDPYSATVRNDLVPNDFHAVGSIHSHPNGVLRPSDADLDTFGSGRVHIIIGSPYGPDDWEAFDQSGEVRDLDVLDADLSDPESFFDFTQDDIDAELDR", "text": "FUNCTION: Probable metalloprotease. Does not hydrolyze SAMP1- and SAMP2-protein conjugates, diglycine-AMC, Ub-AMC, hemoglobin, cytochrome c, carbonic anhydrase, creatinine phosphokinase, beta-amylase and bovine serum albumin. SIMILARITY: Belongs to the peptidase M67B family."}
{"protein": "MPRRREVPKREILPDPKFGNVELSKFMNVIMEGGKKAIAERIIYGALEQIEKKNPGKDPVEAFTMAINNVKPMVEVKSRRVGGSNYQVPVEVRPVRRLALSMRWIKEAARKRGEKSMALRLANELMEATEGRGGAMKKRDEVHRMAEANKAFSHFRF", "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": "MERLVLTLCTLPLAVASAGCATTPARNLSCYQCFKVSSWTECPPTWCSPLDQVCISNEVVVSFKWSVRVLLSKRCAPRCPNDNMKFEWSPAPMVQGVITRRCCSWALCNRALTPQEGRWALRGGLLLQVGLSLLRALL", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor."}
{"protein": "MTAESQQSPTRATAAGAGLQQTSGFTMPVVKVEKDPAPEASMSNGGSEVDDTHKGRRRKRPLQKGKPPYSYIALIAMSIANSADRKLTLGGIYKFITERFPFYRDNSKKWQNSIRHNLTLNDCFIKIPREPGRPGKGNYWALDPNAEDMFDSGSFLRRRKRFKRTDLTTYPAYIHDTSMFSPLQVARATYPNTVYPNMTMSPNYSQQIAPHSSVYYPSSSPAFSSAQPRVFSINTLIGHSGSEHAQPPNRSISPEVNSTSSSSCNYGGSAYSSQAGSGTMLPRSTNPVPYSYSVPNSHLQMNQSTYTHSNAQLFGSASRLPMPTSPPMNSDTVDFYGRMSPGQYTSLATYNSNGQLGGTNAYLRHATYSGNMERFVPAV", "text": "FUNCTION: Transcription factor that binds consensus sites on a variety of gene promoters and activate their transcription. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAVPRQRAAGGLCGDGHHRFWLGPGGGALLAGSGRCRGGGLVILLDVPASMLHGGLNFRQVRWRAIGAILPGMAVGALIGLWLMGQLDKRWPLFLLGLYITWVGWRTLRHGQQAARALPGWTHHAGSGLVGVLEVMFATAGPMVIALLQRRLREVAEIRATVPVVMVVAASIAIAVLFGAGQIDRAHTFERWLVALPIAFMGVVLGNRLARHIPPPAMRRAMAVLLIASGLSLTQHLWR", "text": "FUNCTION: Involved in the uptake of p-toluenesulphonate (TSA). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family."}
{"protein": "MRHRKSGRQLNRSSTHLNSMLKNMACSLFTHEVIKTTLSKAKELRRIVEPIITLSKIDTVSRRRLVFSRIRDNAIVAKLFKKLGPCFFSRLGGYTRILKCGFRSGDKAPMAYIELVDRVKNNKKNEILKK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MSGGSRIQLLSPRLANQIAAGEVVERPASVAKELLENSLDSGARRIEVEVEQGGVKLLRVRDNGGGIAPDDLPLALARHATSKIRELEDLEGVLSLGFRGEALASISSVARLTLTSRTADAGEAWQVETEGRDMTPRVQPAAHPVGTSVEVRDLFFNTPARRKFLKAEKTEFDHLQEVIRRLALARFDVGFHLRHNGKTIFSLHEATDEMARARRVGTICGPGFLEQALPIDVERNGLRLWGWVGLPTFSRSQADLQYFFVNGRAVRDKLVAHAVRQAYRDVLFNGRHPTFVLFLECDPTGVDVNVHPTKHEVRFREGRMVHDFLYGTLHRALADVRPEDQLAAPAAASEIVRPSGQQVGEFGPQGEMRLASPVLEQPQAEPRQSFTPGSGAGSGYQYQYTPRPSQPLPVAETQAVYREFYAPLDGTAPASLPESQGDIPPLGYALAQLKGIYILAENAVGLVLVDMHAAHERIMYERLKVAMASEGLSGQPLLVPESLALSQREADCAEEHAQWFQRLGFELQRLGPETVAIRQIPALLKQAEANRLVQDVLADLMEYGTSDRIQAHLNELLGTMACHGAVRANRRLAIPEMNALLRDMENTERSGQCNHGRPTWTQMGLDDLDKLFLRGR", "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": "MRIEFEVTHPFHPWRGQRFVLSTRKQNWGEDRVMFYDADGRLRSLLASWTDVAAPDVFIQIAAGRSFVRPDDLATLAALIEQIERSHGG", "text": "SIMILARITY: To Rhizobium NGR234A y4oN."}
{"protein": "MNFSTYFENLSVPNNISGNITFPISEDCALPLPMIFTLALAYGAVIILGLSGNLALIIIILKQKEMRNVTNILIVNLSFSDLLATIMCLPFTLIYTLMDHWIFGEVMCKLNEYIQCVSVTVSIFSLVLIAIERHQLIINPRGWRPNNRHACFGITVIWGFAMACSTPLMMYSVLTDEPFKNISLDSYIGKYVCLEDFPEDKFRLSYTTLLFILQYLGPLCFIFVCYTKIFLRLKRRNNMMDKIRDNKYRSSETKRINIMLLSIVVGFALCWLPFFIFNLVFDWNHEAVATCNHNLLFLICHLTAMISTCVNPIFYGFLNKNFQRDLQFFFNFCDFRSREDDYETIAMSTMHTDVSKTSLKQASPIA", "text": "FUNCTION: Receptor for neuropeptide Y and peptide YY. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MVMTDPIADMLTRIRNANMVRHEKLEVPASKMKREIAEILKREGFIRDVEYIEDNKQGILRIFLKYGPNNERVITGLKRISKPGLRVYVKAHEVPRVLNGLGIAILSTSQGILTDKEARQKGTGGEVIAYVW", "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": "MSVKGVEMPEMTWDLDVGNKWRRRKVLSRIHRFWECRLRVWWLSDAGVRETDPPRPRRRPTWMTAVFHVICAVLLTLMIMAIGALIAYLRYYHQDSWRDMLHDLFCGCHYPEKCRRHHERQRSRRRAMDVPDPELGDPARRPLNGAMYYGSGCRFDTVEMVDETRPAPPALSSPETGDDSNDDAVAGGGAGGVTSSATRTTSSNALLPEWMDAVHVAVQAAVQATVQVSGPRENAVSPAT", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HHV-5 UL136 protein family."}
{"protein": "MYIQILGSAAGGGFPQWNCNCVNCAGFRDGSLRAQARTQSSIALSDDGVNWVLCNASPDIRAQLQGFAPMQPGRALRDTGISAIVLMDSQIDHTTGLLSLREGCPHQVWCTDMVHEDLSTGFPLFEMLKHWNGGLNWNRIELQGSFVIPACPNLRFTPFPLRSAAPPYSPHRFDPHPGDNIGLLVEDTRTGGKLFYAPGLGKVDEALAEKMRDADCLLVDGTMWDDDEMQRRGVGTRTGREMGHLAQNGPGGMLDVLEGFPEQRKVLIHINNTNPILDEDSPERAELVRRNVEVAFDGMSIEL", "text": "FUNCTION: May be involved in the transport of PQQ or its precursor to the periplasm. SIMILARITY: Belongs to the PqqB family."}
{"protein": "MKLTLWTYEGPPHVGAMRVATGMTGLHYVLHAPQGDTYADLLFTMIERRGKRPPVSYTTFQARDLGSDTAEVFQQACRDAYERFQPQAIMVGASCTAELIQDDTGGLADALSLPVPVVHLELPSYQRKENFGADESFLQICRKLAKPTERTAQVSCNILGPTALGFRHRDDVTEITQLLNAMGIAVNVVAPMGSSPADIARLGAAHFNVLLYPETAESAARWAEKTLKQPYTKVVPIGVGATRDFIAEVAKLAGVEPKADESRLRQPWWSASVDSTYLTGKRVFLFGDATHVIAAARIARDEVGFEVVGMGCYNREYARPLRAAAKDYGLEALITDDYLEVEEAIQALAPELILGTQMERHIAKRLGIPCAVISAPVHVQDFPARYSPQMGFEGANVIFDTWIHPLTMGLEEHLLTMFREDFEFHDEAGPSHHGGKAVPASAPRAEATADEGSTPEEAVPPVAAEATSGEIVWLSDAEKELKKIPFFVRGKARRNTEKFAAEKGLTRISIETLYEAKAHYAR", "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": "MAPSLWKGLVGIGLFALAHAAFSAAQHYFPSSGIKWKRKCEFLQSSSFQDKIFRSMYYVYDRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGIVHIAGEFKDMDATSELKNKTFDTLRNHPSFYVYNHRGRVLFRPSDTTNSSNQDALSSNTSLKLRKLESLRR", "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 similarity). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. May be involved in Mg(2+) transport (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane magnesium transporter (TC 1.A.67) family."}
{"protein": "MAKVLINGYGSIGKRVADAVSMQKDMEVIGVTKTRPNFEADMAVQKGYDLYSAVEGRESLFEEKGIDIQGNIFDIIEEADIVVDCAPGGIGKDNIENIYKKYNKKAIVQGGEKAPFVEDSFNSLWSYDRCYGKNIIRAVSCNTTGLCRTLYAINSTTDILKARVVLIRRGADPNDAKRGPINAIVPNPPTVPSHHGPDVGTVIPEFKDKIITSAIIVPTTLMHMHSLMVETTGTTKDDVIDAIEKTPRIFTVSAENGLDSTATIIEYARDIGRPRYDLWEIPVWEESVNVVDNEIFLMQAVHQESDVIPENIDCIRSMLKMEEDNIKSIEMTNKAMGILK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MATRIRLKRLGMKKAPFYRVVVADSRSPRDGRFIEEIGYYNPTKEPAILQIDEEKAIKWLSSGAQPSDTVKALLNKAGILDKMAEKKAQA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MALLHKEKLIECIDNELQNSGTLLLLTKNIVVSEISYNGNDYKYFTFNENHDLIGQENLKGATSNNIAKMVYNWIAKNPQTNKVWVGEPRIRIYFKNNLYHTNNNHVCIKDFYKVSISVSPNIFNDRSIWCTKCTSFYPFSSILSPNLFQ", "text": "FUNCTION: May participate in a redox cascade for the formation of disulfide bonds in viral proteins. SIMILARITY: Belongs to the asfivirus A151R family."}
{"protein": "METLELQGAKLRYHQVGQGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELAEPLPDSASNPDSDYRVKRDAQDIAELAKSLSDEPVYILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDSTYWKDKNDDIVHQILTEGLEKGMKTFGETLNIAPIDAKMMSQPADTEEGRIEQYKRTMFWSKFEIRQYTHSDITLDDFTKYSDKITLLNGTDSRGSFPQDVNFYINKETGIPIVDIPGGHLGYIQKPEGFADVLLNMWG", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily."}
{"protein": "GSVLNCGETCLLGTCYTTGCTCNKYRVCTKD", "text": "FUNCTION: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. Has no hemolytic activity. SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
{"protein": "MAVSSKHIPAPDLHRVRRALLSVSDKTGLIDFAKALHANGVEILSTGGTAKSIAAAGIPVKDVSEITGFPEIMDGRVKTLHPAVHGGLLAVRNDPEHVAAMEEHGIGGIDLAVINLYPFEEVRFKGGDYDTTVENIDIGGPAMIRASAKNHAYVATVVDPADYADVVAELEKHSGSLPLAFRKKLAAKAFSRTAAYDAAISNWFAEAIDEETPTYRAAAGKLHSVMRYGENPHQTAGFYLTGEKRPGVATATQLQGKQLSYNNINDTDAAFELVAEFDPARTAAVAIIKHANPCGVAEASTIKEAYLKALACDPVSAFGGIVALNRTLDEEAAEEIVKTFTEVIIAPDATEGAQAIVAAKKNLRLLVTGGLPDPRAKGIAAKTVAGGLLVQSRDNGVVDDLDLKVVTKRAPTEAELNDLKFAFRVGKHVKSNAIVYVKDGATVGIGAGQMSRVDSARIAARKAEDAAEAAGLAAPLTKGCVVASDAFFPFADGLLSAVEAGATAVIQPGGSMRDDEVIAAADEHGIAMVMTGMRHFRH", "text": "SIMILARITY: Belongs to the PurH family."}
{"protein": "MESFPVINMEKMNGEERAATMGLINDACENWGFFELVNHGIPPELMDTVERVTKAHYKKCMEQRFKELVASKALEGIQAEVTDMDWESTYFLRHLPQSNISEVPDLDEEYRRVMKDFAERLEKLAEYLLDLLCENLGLEKGYLKKAFYGTKGPNFGTKVANYPPCPKADLIKGLRAHTDAGGIILLFQDDKVSGLQLLKDDQWIDVPPMKHSIVINLGDQLEVITNGKYKSVLHRVVAQTDGTRMSIASFYNPGNDAVIYPAPALVEKEVEEKEVYPKFVFDDYMKLYAALKFQAKEPRFEAMKAVEANVNLGPIATV", "text": "SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLKAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGIVHTSYNLTPLSQSLISDKDGSSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRMNGLFNRAMQNVTCTEMKRIVECYNGFQGVKEIIDVGGGLGISLATIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDEYCVKILKNCWRALPKDGKVVVIEQMQPEYPETNLISKNSSSVDMLMMTMLDGGKERTKQQFEDLAKQAGFTVFKIVARAYYCWVIELYK", "text": "FUNCTION: Flavonoid 3-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti- viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti- inflammatory effects (PubMed:22711283). Catalyzes S-adenosylmethionine- dependent regioselective 3-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates (PubMed:22711283). Active with myricetin, quercetin, kaempferol, 4'-methyl kaempferol (kaempferide), 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin), 3'-methyl myricetin (laricitrin) and 3',5'-dimethyl myricetin (syringetin), thus producing 3-methyl myricetin, 3-methyl quercetin, 3-methyl kaempferol, 4',3-methyl kaempferol, 3',3-methyl quercetin, 7,3-dimethyl quercetin, 3',3-dimethyl myricetin and 3',5',3- dimethyl myricetin, respectively (PubMed:22711283). Inactive with flavonol substrates methylated at the 3-hydroxyl position such as 3-O- methyl quercetin (PubMed:22711283). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MSGELNGNDTSAQAAVSAGSVLEGAAFADEGEQHNESMKTLVLGALGVVYGDIGTSPIYAFREALHAAATNGILARSDILGVVSLIFWALTLVVTVKYVLFVLRADNNGEGGILSLMALVRGALKGRPDLILGVGICGAALFFGDAVITPAISVLSAMEGLEIVAPNLTPFVVPAAVVILVTLFSVQKLGTGRVAIVFGPIMALWFVALGASGLWHIFDDPTVMAALNPYYAVRFLTVSPAVAFVTVGAVFLAMTGAEALYADLGHFGRKPIVRAWLWIVFPCLLLNYFGQAAFILSHGEAAALPFFQMIPSFALWPMVLLATAATVIASQAVITGAYSVARQAVQLNILPRLEIQHTSEKLHGQIYIPRVNLLLGLAVVILVLGFEKSSNLAAAYGIAVTGNMLVTTVLLYIAMTRIWNWRVSRALPIILGFLVIDMLFFSANIIKVHEGGWASIGIATVLVLIMWTWVRGTRHLFQKTRKAEVPLDLIVEQMAKRPPTIVPGTAVFLTGDPKSAPTALMHSLKHYKVLHENNVILTVVTASKPWVASADRARVSQYNERFMLVTLTFGYMQQPNIPRALGLCRRLGWKFDIMTTSFFLSRRSLKASVHSGMPLWQDKLFILLARTASDATEYFQIPTGRVVEIGTQVNI", "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": "MKANELREKSAQQLNEQLLGLLRDQFNLRMQKATGQLGQSHLLSQVKRDIARVKTVLNQQAGK", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MSHEKSESCLQEKKHSSSFERFHDGTSLENNLLQNLKLSSQRVLEIAQKKGRSKCPKCNSSRMFYCYTCFVPVESVPSDEIPVVKLPLKIDIIKHPNETDGKSTAVHAKLLAHEDVTVYTYPCVPQYQDQKHEVVLVFPGPDSVSLSDSLLYIRGSGDMQNDSSCEPSLKRPKCSQQYDKSKNEGVEEKKPMHFLKKLIFIDSTWNQTNKIISDERLQGLQQVELMERKTCFWRHQKGTPNTYLSTIEAIYYFMIDYHTIILQKDYKGEYDDLLFFFSFMYRIINDAKKSAGKL", "text": "FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs (acp3U(20)). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TDD superfamily. DTWD1 family."}
{"protein": "MPPKPSAKGAKKAASKAKAARTGDKKRRKRRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNRRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK", "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": "MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF", "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). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (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 Note=Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
{"protein": "MSQEGVELEKSVRRLREKFHGKVSSKKAGALMRKFGSDHTGVGRSIVYGVKQKDGQELSNDLDAQDPPEDMKQDRDIQAVATSLLPLTEANLRMFQRAQDDLIPAVDRQFACSSCDHVWWRRVPQRKEVSRCRKCRKRYEPVPADKMWGLAEFHCPKCRHNFRGWAQMGSPSPCYGCGFPVYPTRILPPRWDRDPDRRSTHTHSCSAADCYNRREPHVPGTSCAHPKSRKQNHLPKVLHPSNPHISSGSTVATCLSQGGLLEDLDNLILEDLKEEEEEEEEVEDEEGGPRE", "text": "FUNCTION: Isoform 4 does not inhibit programmed ribosomal frameshifting (-1PRF). Does not bind to ribosomes. FUNCTION: Inhibits programmed -1 ribosomal frameshifting (-1PRF) of a variety of mRNAs from viruses, such as HIV1, and cellular genes, such as PEG10. Interacts with the -1PRF signal of target mRNA and translating ribosomes and causes premature translation termination at the frameshifting site (PubMed:30682371). Regulates HIV1 GAG-POL expression by inhibiting -1PRF (PubMed:30682371). Exhibits antiviral activity against dengue virus (DENV) and can inhibit the replication of all DENV serotypes. May block the protein translation of DENV RNA via its association with cellular mRNA-binding proteins and viral RNA. Interrupts also Zika virus replication by promoting viral NS3 degradation via a lysosome-dependent pathway (PubMed:32150556). Can also limit the replication of hepatitis C virus (HCV) by restricting formation of viral replication organelle, West Nile virus (WNV), Chikungunya virus (CHIKV), herpes simplex virus type 1 (HHV-1), herpes virus type 8 (HHV-8) and human adenovirus (PubMed:26735137, PubMed:27974568, PubMed:30944177, PubMed:32294532). Binds nucleic acids with a higher affinity for ssRNA and ssDNA than for dsDNA (PubMed:27974568). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, P-body Note=Predominantly found in the cytoplasm (PubMed:26735137). After infection, relocalizes to the DENV replication complex in perinuclear regions (PubMed:27974568). SIMILARITY: Belongs to the SHFL family."}
{"protein": "MIKGETIKNNSVKIVVATGIGAALFVIIGWLINIPTPIPNTSIQLQYAVLALFSALFGPLAGFLIGFIGHALKDSFLYGAPWWTWVLGSGLMGLFLGFGVKRESLTQGIFGNKEIIRFNIVQFLANVVVWGLIAPIGDILVYSEPANKVFTQGVVAGLVNALTIAVAGTLLLKLYAATRTKSGTLDKE", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0397 family."}
{"protein": "MRLLILAVGKLKQGPERELAERYRARFDDLGRKLGFRGLDVHEIAESRAREAPARMAEEAAAIIAQVPDGAVLVTLDERGQSLGSTAFAAQLGRWRDEQVPGTIFVIGGADGLLPELRRKAKLSMSFGGATWPHQMVRVMLLEQIYRAATILAGHPYHRA", "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": "MATRLQYENSCDVGVFLKLTNKYCLVGQCGSKQFLHTVENRLADHIPVVETSIAGTRIVGRLSAGNKNGLLLPNTCTDQELQQIRNSLPDDVVVQRIEEKFSALGNCIATNDYVALVHPDIDRETEEIIADVLGVEVFRQTVSGNVLVGTYCALTNQGALVHPMTSIADQDELSSLLQVPLVAGTVNRGNECVAAGCVVNDWTAIVGADTTATEISVIESIFALQGSKPSNIINNIRNSIVDNV", "text": "FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May also be involved in ribosome biogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Shuttles between cytoplasm and nucleus/nucleolus. SIMILARITY: Belongs to the eIF-6 family."}
{"protein": "MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKQNGLNVFAVPTVLLSNTPHYDTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGYMGTASQIKILAEWLTALRKDHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQYLLPLAQGITPNIFELEILTGKNCRDLDSAIAAAKSLLSDTLKWVVITSASGNEENQEMQVVVVSADSVNVISHSRVKTDLKGTGDLFCAQLISGLLKGKALNDAVHRAGLRVLEVMRYTQQHESDELILPPLAEA", "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": "MVKRSSHRQVVLDEDDEENYNNNLDDEKMEVLLIPQSNSTTFASSDATQMYKKSRISSNSENKKQIPDTKTLLETFQKIKKTLECPICTEALQRPFTTHCGHTYCYECLLNWLKESKSCPTCRQKLYTQPSPAYLVYEIMNVVAASNSGFPLVGINENPAKKQKEVLFDGMFKQEDSHYPRSILVDSEDGVLRCARCQWELENPYHCDHCGFQISDDQDSGREWFWDGENAESDSSLNGDNTRGGNISTNRAFNNMGHAPITAVPQDWLRFDEGEEFVGSDLESDFSGPGEYDVDDGFIDNRATSQLSPVESDDDFVAPVNGSNGNGITALDSTDSEEIDIMNGFDEERDSGGTNMVSRSETCYNDGQRYDELRRELADIQNESLDSLNSSSNNSPSHNNIHSRQHPFSSDEDEGNIVTNGTGLRSSQSSSQNRGFDLEPYSEVFTASYPRRQARRTRTIQLDSDEES", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDSTTNSDSPILDPNPEDVEKLLDESEEESEDQSTERLLPSELFILPLNKRPFFPGMAAPILIESGPYYEVLKVLAKSSQKYIGLVLTKKENADILKVSFNQLHKTGVAARILRIMPIEGGSAQVLLSIEERIRIIEPIKDKYLKARVSYHADNKELTEELKAYSISIVSVIKDLLKLNPLFKEELQIFLGHSDFTEPGKLADFSVALTTATREELQEVLETTNMHDRIDKALILLKKELDLSRLQSSINQKIEATITKSQKEFFLKEQLKTIKKELGLEKEDRAIDIEKFSERLRKRHVPDYAMEVIQDEIEKLQTLETSSAEYTVCRNYLDWLTIIPWGIQSKEYHDLKKAEIVLNKDHYGLDEIKQRILELISVGKLSKGLKGSIICLVGPPGVGKTSIGRSIAKVLHRKFFRFSVGGMRDEAEIKGHRRTYIGAMPGKMVQALKQSQAMNPVIMIDEVDKIGASYHGDPASALLEVLDPEQNKDFLDHYLDVRVDLSNVLFILTANVLDTIPDPLLDRMEILRLSGYILEEKLQIAKKYLVPKARKEIGLTASEVNFQPEALKYMINNYAREAGVRTLNGNIKKVLRKVALKIVQNQEKPKSKKITFKISSKNLQTYLGKPIFSSDRFYESTPVGVATGLAWTSLGGATLYIESVQVSSLKTDMHLTGQAGEVMKESSQIAWTYLHSALHRYAPGYTFFPKSQVHIHIPEGATPKDGPSAGITMVTSLLSLLLETPVVNNLGMTGEITLTGRVLGVGGIREKLIAARRSRLNILIFPEDNRRDYEELPAYLKTGLKIHFVSHYDDVLKVAFPKLK", "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": "MNKKLELMYGSLLHDIGKIVYRSNSVDFAKGTHSKIGSQFLNKFKPFQLSGIVDSVSYHHYKELASSSLLDDSVAYITYIADNIASGTDRRASEGDYEGEGNRQRFDKRAPLASIFNVVNSETKGLANYTYSFEKEQVYRYPTDAKKEYTSSQYAALVNKMTDDLSNKLKVGPDSFSSLLQWTESLWSYIPSSTDTNQVMDVSLYDHSKITCAIASCIYDYLTEMNCVNYRKELFSPYEKTKQFYQEDVFLLVSLDMSGIQDFIYNISGSKALKSLRSRSFYLETMLESLVDDLLSDLELSRANLLYTGGGHAYLLLPNTERARDVLASFEGEMKEWFIKIFKTDLSVAIAYKACTGEDLMNSNGTYSDLWQTVSRKLSDKKAHKYSLNEIKLFNSTIHAGTQECKECLRSDIDISEDSLCKICEGIIAISNDLRDYSFFVVSPEGKVPLPRNRYLSVENQDGAERKIKMNKETRIYSKNQPFVGKQLVTNLWMCDYDFSTLNPETKKQGIASYVNREVGIPRLGVLRADIDNLGTTFIKGIPEQYRSISRTATLSRQLSMFFKFELSNILKGARISVIYSGGDDLFLIGAWDDVISKALVLRKAFTRFSAGKLTFSAGIGMYPVKYPISKMASETGVLEDLAKRGEKNQVALWNDSKVFGWSQLEEQILKEKMIPLQEALTNSQEHGKSFLYKMLELLRNEDQINIARLAYLLARSSLSEELTQSIFAWSQNKQQKVELITAIEYLVYQIREAD", "text": "FUNCTION: This subunit is a single-strand-specific deoxyribonuclease (ssDNase) which digests both linear and circular ssDNA; it has both exo- and endonuclease activity. FUNCTION: When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP, producing (mostly) cyclic hexaadenylate (cA6). cA6 synthesis occurs in the Csm effector complex and requires cognate target RNA and ATP; other NTPs are not incorporated. cOAs are second messengers that induce an antiviral state important for defense against invading nucleic acids. 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: ssDNase activity is stimulated in the ternary Csm effector complex; binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases. SIMILARITY: Belongs to the CRISPR-associated Cas10/Csm1 family."}
{"protein": "MDMAMSSRLALCLAVVAACAAGGAVADWSPATATFYGGSDGSGTMGGACGYGNLYDQGYGVDNAALSQALFNDGASCGQCYLIVCDTSRAPQWCKAGTAVTVTATNLCPPNWALPSDGGGWCNPPRPHFDMSQPAWEQIGVYQAGIVPVLYQRVRCWRQGGVRFTVAGLNYFELVLITNVAGSGSVASAWIKGTNTGWIQMSRNWGANWQSLAGLAGQALSFAVTTTGGQYLQFQDVAPAWWQFGQTFSTYQQFDY", "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": "MAAKKVVKQIKLQVEAGKANPAPPVGPALGQAGLNIMEFCKQFNERSKNQMGLKLPVVITVYSDRSFTFVTKSPPAALLVMKALGLQGGSATPHTVKVGTIKRAQLEEIAKTKMEDLNANDMDAAVKIIAGTCRSMGVNVE", "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": "MEEAILVPCVLGLLLLPILAMLMALCVHCHRLPGSYDSTSSDSLYPRGIQFKRPHTVAPWPPAYPPVTSYPPLSQPDLLPIPRSPQPLGGSHRTPSSRRDSDGANSVASYENEGASGIRGAQAGWGVWGPSWTRLTPVSLPPEPACEDADEDEDDYHNPGYLVVLPDSTPATSTAAPSAPALSTPGIRDSAFSMESIDDYVNVPESGESAEASLDGSREYVNVSQELHPGAAKTEPAALSSQEAEEVEEEGAPDYENLQELN", "text": "FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR- mediated signaling, both in mature T-cells and during their development (PubMed:25907557, PubMed:23514740). Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules. SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein Note=Present in lipid rafts."}
{"protein": "MLVGIISLFPEMFKAITEFGVTGRAVKQNLLQVRCWNPRDFTHDKHKTVDDRPYGGGPGMLMMVQPLRDAIQAAKAEVGEGAKVIYLSPQGRKLDQAGVKELAQHQKLILLCGRYEGIDERLIETEVDEEWSVGDYVLTGGELPAMTLIDAVARFIPGVLGKQASADEDSFAEGLLDCPHYTRPEVLDGLAVPPVLMSGNHEEIRKWRLRQSLERTWLRRPELLESLALTDEQRKLLKQIKAEHS", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
{"protein": "MVAEGLCQCYIRRMSTGGPHGAAPDRSCLARDTEGRSPCKNCQGCTQGAADPIPIRILMADSDVEQAPSVSVLPRNKILILAPAGKAYQAEVIRDLFNIEASESDRIVRDVKWSNKYYEVDLDLYIDSYESLQTWGAEFCSDECADLRDVVAGIFLVFEETEDAETFQQLIEDCHFTDERVLVACDLSSAEHPASLERALEVHDVALVRWRERGTNELGEQQGRERVRELLDIHPWSERMLRMHASTAAALAELDPLQADIPLDSVVTRIKQARERYLEITDVHAADEYAARIAHELTEQLLPE", "text": "FUNCTION: Involved in gross chromosomal rearrangements (GCRs) and telomere healing. SIMILARITY: Belongs to the IRC6 family."}
{"protein": "MKVNSTTEIIKSLLECLSKEISNGEDEDTMITDITELFNLSKEFDVRKEISNKHNEFLNILMNYIIKSTTANGDNNEKLFKFNLTSIRFLRNLCANVSENQNIIISNSNFINFIINQLINENNNIKITLNKKNILTSLYQLLINGIVLNDKTQSLLWSNIYPNNLIILIEKYKDNDEFKLLPTNLMLIYNCILNSKDRMKDLVCNKRLVQLIIELIKEDDTFDHEYNTQNFHWIHLISKSLFINDLFIDLYKSLSDNKYSTELVKSTTESTTESTTTESTDSTTDSTTTTTTGKTNKNQVKLLNLLDSIIHDGDKKNIKEYIEKDSIIDLKTCYFMIDELASLYNLDFARKDLKVETQQLTTSLNQSDFDAIFFFIKIFANITSYTEEMLSLSLSIFKPNQIPTKQQEGEEDPVNQILNDPFSKDSAIDPSASKKFDLNTLLRKKGLVAICIGSLHGNYGSDTNKSSSSSSSSSSSTTTDGETVTSKGFNKNIESQDKGFKIELIRILGNLSYKNRGNQDEIRELGGIEIILNHCRFDVNNPYIKEWSVFAIRNLCEDNVENQNLIESLKVKGVANNDELKDLGLEVGVTENGTIKFKNVPKKEKENNQ", "text": "SIMILARITY: Belongs to the ATXN10 family."}
{"protein": "MSTTYIPYRLDGKVALVTGSGRGIGAAIATQLGRLGAKVVVNYANASEAAEKVVSEIKSFGTDAVAFKADVRQVAQTAKLMDDAVAHFGSLDIVCSNSGVVSFGHIGEVTEEEFDRVFSLNTRGQFFVAREAYRHLNNGGRIILMSSNTAKDFSVPKHSLYSGSKGAIDSFVRVFSKDCGDKKITVNAVAPGGTVTDMFHDVSQHYIPGGEKYTAEERQEMAAHASPLTRNGFPVDIARVVGFLASNEAEWVNGKILTVDGGAA", "text": "FUNCTION: Short chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the dimeric xanthones cryptosporioptides (PubMed:30996871). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase dmx- nrPKS (Probable). The atrochrysone carboxyl ACP thioesterase dmxR1 then breaks the thioester bond and releases the atrochrysone carboxylic acid from dmx-nrPKS (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase dmxR15, and oxidized by the anthrone oxygenase dmxR16 to yield emodin (Probable). Emodin is then reduced to emodin hydroquinone by the oxidoreductase dmxR7 (Probable). A-ring reduction by the short chain dehydrogenase dmxR18, dehydration by the scytalone dehydratase-like protein dmxR17 and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:30996871). Baeyer-Villiger oxidation by the Baeyer-Villiger monooxygenase (BVMO) dmxR6 then yields monodictylactone in equilibrium with monodictyphenone (PubMed:30996871). In the case of the cryptosporioptides biosynthesis, monodictylactone is reduced at C- 12 to an alcohol (by the short chain dehydrogenases dmxR12 or dmxR8) and hydroxylated at C-5 by dmxR9, yielding the electron-rich aromatic which could eliminate H(2)O to form the ortho-quinonemethide, followed by tautomerisation to paraquinone and complete the formal reduction to produce the 10-methylgroup (Probable). Conjugate addition of C-4a-OH to the resulting paraquinone by the monooxygenase dmxR10 then gives cyclohexadienone, which is then reduced at C-5 by the short chain dehydrogenase dmxR3 to give the dihydroxanthone (Probable). The 6,7- epoxide in the cryptosporioptides could be introduced by the cytochrome P450 monooxygenase dmxL3 (Probable). The highly reducing PKS dmxL2 manufactures butyrate, which is further carboxylated by dmxL1 to form ethylmalonate (PubMed:30996871). It is not yet clear whether the carboxylation occurs while the butyrate is attached to the ACP of dmxL2, but this unusual fungal metabolite could then be esterified to O-5 by the O-acetyltransferase dmxR13 (PubMed:30996871). Finally, dimerization performed by dmxR5 gives the observed dimers cryptosporioptides A, B and C as the final products of the pathway (PubMed:30996871). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSADQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTTSFDEYWKKDSDAELYHFIGKDIVYFHSLFWPAMLEGSHFRKPTNLFVHGYVTVNGAKMSKSRGTFIKASTWLKHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLAAELADPQLYKTFTDAAAVIGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPTLSERVEAFLNSELNWDAIEQPLLGHKVNTFKALYNRIDMKQVEALVEASKEEVKAAAAPVTGPLADFPIQETITFDDFAKIDLRVALIENAEFVDGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRQTVMVANLAPRKMRFGVSEGMVMAAGPGGKDIFLLSPDDGAKPGQQVK", "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": "MTDILTNMFTIVAELPLGEEEGFAFNGNILETNLINLAAVIGLLFYSGRSFLTNLLRNREDNILKSIRDADERYKEATEKLQQAKNEFEQAKIEADEIRAQSRITAKEIEVSLMGLVSEDTKRLIDMKQATISFEEEKAINEVRRQVIRLALQRALEQSKNRLNHRLQKRVTRLNIGLLGQLVGVND", "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": "MKRRASDRGAGETSARAKALGSGISGNNAKRAGPFILGPRLGNSPVPSIVQCLARKDGTDDFYQLKILTLEERGDQGIESQEERQGKMLLHTEYSLLSLLHTQDGVVHHHGLFQDRTCEIVEDTESSRMVKKMKKRICLVLDCLCAHDFSDKTADLINLQHYVIKEKRLSERETVVIFYDVVRVVEALHQKNIVHRDLKLGNMVLNKRTHRITITNFCLGKHPVSEGDLLKDQRGSPAYISPDVLSGRPYRGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDGRVSENTVCLIRKLLVLDPQQRLAAADVLEALSAIIASWQSLSSLSGPLQVVPDIDDQMSNADSSQEAKVTEECSQYEFENYMRQQLLLAEEKSSIHDARSWVPKRQFGSAPPVRRLGHDAQPMTSLDTAILAQRYLRK", "text": "FUNCTION: May be a negative regulator of NF-kappa-B and p53-mediated gene transcription. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
{"protein": "MALDNPTVLARLQAALPDALLGSSEFRGDLSVHVRPERIVDVARFLRDDPELRYHFLENLCGVDYLGREPRFEVVYHLLSFANRHRICLKVGVSERNPSVPSLTELWPGANYHERETFDMFGIVFTGHPCLDRILMPEDWEGHPLRKDVPLGAEEVAFTFNQDRIYAHKPFAKE", "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 30 kDa subunit family."}
{"protein": "MPSAEVLQETPRVVISVGKKKTAVARAIIKPGIGRVRINGYPLELWPIEMARIKMSEPLILAGELAKKVDIDVNVSGGGYMGQAVAVRIAMARGLVAFFQSQELKELYERYDPYMLKGDPRRTEHKKPGIKHARSKRQKAYR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MADDDPFGTGQMFHLNTALTHSIFNAELYSTDIPLSTADGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGSTGSPGPGYGFPHYGFPAYGGIAFHPGATKSNTGITHGTINTKFKNEPRDCAKSDDREILNPPEKETQGEGPSLFMASTKTEAIAPASTMEDKEEDVGFQDNLFLEKALQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGSISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAALLINHPNGEGLNAIHIAVMSNSLSCLQLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWEKAGEDEGVVPGTTPLDMAANWQVFDILNGKPYEPVFTSDDILPQGDIKQLTEDTRLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELVEALRQMGYTEAIEVIQAAFRTPETTASSPVTTAQAHLLPLSSSSTRQHIDELRDNDSVCDSGVETSFRKLSFSESLTGDGPLLSLNKMPHNYGQDGPIEGKI", "text": "FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain- containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I- kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. FUNCTION: [Nuclear factor NF-kappa-B p50 subunit]: Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65- p50 complex to form a transcription factor. Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. FUNCTION: [Nuclear factor NF-kappa-B p105 subunit]: P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B. Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105. SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p105 subunit]: Cytoplasm. SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p50 subunit]: Nucleus Cytoplasm Note=Association with NFKBIA inhibitor (I-kappa-B), promotes its retention in the cytoplasm in an inactive form. Translocates into the nucleus following NFKBIA degradation."}
{"protein": "MTNEFLHFEKISRQTWQSLHRKTTPPLTEEELESIKSFNDQISLQDVTDIYLPLAHLIQIYKRTKEDLAFSKGIFLQRESKSQPFIIGVSGSVAVGKSTTSRLLQILLSRTFTDATVELVTTDGFLYPNQTLIEQGILNRKGFPESYNMEALLNFLDRIKNGQDVDIPVYSHEVYDIVPEEKQSVKAADFVIVEGINVFQNPQNDRLYITDFFDFSIYVDAGVDDIESWYLDRFLKMLSLAQNDPDSYYYRFTQMPIGEVEAFAHQVWTSINLTNLQNYIEPTRNRAEVILHKSKNHEIDEIYLKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic pantothenate kinase family."}
{"protein": "MSALANHAFAKMNGIGNEIVVVDMRDSTAKVTPDDARAVASAQGGVPYDQLMVLQKPRLDGTEAFISIYNNDGSEAGACGNGMRCVVRRIFEKTGQATATFETAAGLLNAWQGPAPDLYTVDMGVPKFGWQDIPLAEEFRDTRYIELQIGPIDNPILHSPSVVSMGNPHAIFWVDDVNAYDLARFGPLLENHPIFPERANITLAHIVDRDHITIRTWERGAGLTRACGSAACATAVAAARLKRAERNVEITLPGGKLGIEWRERDDHVLMTGTATFEYEGNFDPALFAPAG", "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": "MWIQVRTIDGSKTCTIEDVSRKATIEELRERVWALFDVRPECQRLFYRGKQLENGYTLFDYDVGLNDIIQLLVRPDPDHLPGTSTQIEAKPCSNSPPKVKKAPRVGPSNQPSTSARARLIDPGFGIYKVNELVDARDVGLGAWFEAHIHSVTRASDGQSRGKTPLKNGSSCKRTNGNIKHKSKENTNKLDSVPSTSNSDCVAADEDVIYHIQYDEYPESGTLEMNVKDLRPRARTILKWNELNVGDVVMVNYNVESPGQRGFWFDAEITTLKTISRTKKELRVKIFLGGSEGTLNDCKIISVDEIFKIERPGAHPLSFADGKFLRRNDPECDLCGGDPEKKCHSCSCRVCGGKHEPNMQLLCDECNVAYHIYCLNPPLDKVPEEEYWYCPSCKTDSSEVVKAGERLKMSKKKAKMPSASTESRRDWGRGMACVGRTRECTIVPSNHYGPIPGIPVGSTWRFRVQVSEAGVHRPHVGGIHGRSNDGAYSLVLAGGFADEVDRGDEFTYTGSGGKNLAGNKRIGAPSADQTLTNMNRALALNCDAPLDDKIGAESRNWRAGKPVRVIRSFKGRKISKYAPEEGNRYDGIYKVVKYWPEISSSHGFLVWRYLLRRDDVEPAPWTSEGIERSRRLCLRLQYPAGYPSDKEGKKPKGQSKKQPSGTTKRPISDDDCPSASKVYKASDSAEAIEAFQLTPQQQHLIREDCQNQKLWDEVLSHLVEGPNFLKKLEQSFMCVCCQELVYQPVTTECFHNVCKDCLQRSFKAQVFSCPACRHDLGQNYIMIPNEILQTLLDLFFPGYSKGR", "text": "FUNCTION: E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:29506131, PubMed:27743347, PubMed:23404503). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:27129234, PubMed:24813944). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Ubiquitinates also PCNP leading to its degradation by the proteasome (PubMed:14741369, PubMed:12176013). Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteasomal degradation (PubMed:29923055). Promotes also DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation (PubMed:30335751). Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (PubMed:33848395). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Enriched at genomic loci that are enriched for 5-hydroxymethylcytosine (5hmC)."}
{"protein": "MRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLRDGEREGWGEISPLPGFSQETWEEAQTALLTWVNDWLQGSEGLPEMPSVAFGASCALAELTGVLPEAADYRAAPLCTGDPDDLVLRLADMPGEKIAKVKVGLYEAVRDGMVVNVLLEAIPDLHLRLDANRAWTPLKAQQFAKYVNPDYRARIAFLEEPCKTRDDSRAFARETGIAIAWDESLREADFTFEAEEGVRAVVIKPTLTGSLDKVREQVAAAHALGLTAVISSSIESSLGLTQLARIAAWLTPGTLPGLDTLHLMQAQQIRPWPGSALPCLKREELERLL", "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": "MNIILLDKIANLGGLGDQVTVKSGYARNFLFPQGKAVPATKDNVEKFEARRAELEAKIAEQLAAANARAEKVAELAEVTIAAPAGDEGKLFGSVGTRDIADAITAAGVEVQKAEVKLPTGTLRETGEYDIDLQLHSDVITSIKVIIIAEA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MKSSVPSLLFVSLVMSLNSYTQQVLYCPPDPAPENITEFVCNSPSLHEFPTGFPVRTKIISVEFTQVSSLGVEALQGLPNLQELHLSNNRLKTLPSGLFRNLPELHTLDLSTNLLEDLPPEIFTSTTSLTLLSISENRLAKLRLSWFETLKELRILSLDNNQLKEVPISCFDKLEKLTFLDLSSNHLHRLSPDMFSGLDNLERLSLENNPIRCIAPKSFHGRPKLSIISLKNCSLTNIITGVFQPLNHXVLLDLSDNELTMLDPPVAIPSANLSLDLTGNPWACNCRMDNLLTWVKEHKIDLYSKQEIVCAFPKSFKGEEATSLHRSQICPC", "text": "FUNCTION: Inhibits the enzymatic activity of the basic phospholipase A2 (PLA2). SUBCELLULAR LOCATION: Secreted Note=Secreted in plasma. SIMILARITY: Belongs to the beta-type phospholipase A2 inhibitor family."}
{"protein": "MTTLFISDLHLDPSRPEITDLFLRFLREQAPGADALYILGDLFEAWIGDDTPSPAADAVADALKVLSDSGVPVYFIRGNRDFLLGEDYARRAGLRILPDPCMIDLYGRPVLLQHGDLLCTDDIPYQQFRAQTRDPAFQAQFLSQPLAARIAFAQKAREASQARQSEMKQGDRAQFETVTDVAPSEVDATFARHGVDTMIHGHTHRPAIHSLQAGGRACTRIVLGDWYEQGSVLRVDAGGWSLDTLARE", "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": "GLCPDKYKRYSLQHSFCLPTCVSCAFYSKDVRYWLKNYILYQHNNLRNVVASGRSYGVDHVPRICLTVVTRIGCGYLFRKYTNVICNYGPRGNVEGEEIYKGGDICSACPANTCCGDGCKYHGLCKFGEPNLPEIFYCGFNGESDCR", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRANGPDGAIGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRVVKEEEARGLAEKYGIPYFETSAANGTNVSLAIETLLDLIMKRMERCVDKSWIPEGVVRSNGHTSADPLNEEKEKGSCGC", "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 homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion. Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. SUBCELLULAR LOCATION: Membrane; Lipid- anchor Melanosome Late endosome Lysosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes to endosomal exocytic vesicles. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MSRVCELTNRKKSFGNKVSHSNRKTKRTFLLNLHKVTLTSDILNKKFRFRVATRTLRTIDYKGDLDAFLLNTRTIKLSEKAQKIKRRLKKVLVKQEVELAVSDA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MKISAAVLTVVLMAASLCAPASASPNGSDTIPCCFAYLSAVLPRAHVKEYFYTSSKCSNFAVVFVTRRNRQVCANPKKKWVQEYINYLELK", "text": "FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. May also be an agonist of the G protein-coupled receptor GPR75. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MKLLAATVLLLTICSLEGALVRRQAKEPCVESPVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLNYFLEL", "text": "FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein A2 family."}
{"protein": "MRSSKYLLSTLKETPSDAEIVSHQLMLRAGMIRKVAAGLYTWTPTGLRVLRKVENVVREEMEAINALEILMPMVQPADLWQESGRWDDYGPELLRIKDRNQRDFLLGPTHEEIISQLVRKEVSSYKQLPLTLFQIQTKFRDEIRPRFGVMRAREFLMKDAYSFHLTDESLQKTYDDMYKAYCRIFERLGLDYRPVIADTGSIGGSHSHEFHVLASSGEDAIAFSDSSDYAANVEMAEALAPAGERPAPNQKVEKHEVQGDELAAVLQPLSVESQQATKSFIVKAADDIDSEYVQLVLRADHELNTVKAEKLAQVAAPLEILTETEKATGVEAPYIGVVNAKLPLLVDSSAAHLADFACGANENGQWLTGVNWKRDTGDFSVVDIRNVVAGDPSPCGQGKVKIARGIEVGHIFQLGKKYSDAMKVGVLSESGKHETLTMGCYGIGVSRIVAAAIEQNNDERGICWPEALAPFQVVIVPMNMHKSARVQEAAEKLYTDLKAQGIDVLFDDRKERPGVMFTDMELIGIPHQVVVGERNLDENQVEYQSRKGGEKQKINLDDCISFIQQQL", "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": "MTAFFKKPKRYMPLRQREPKIDAPQGLMTKCPSCKYMHYTKQLNENHKVCDCGYHFPLHAQERIDMLVDEGSFERFAGPSVKANPLDFPDYEEKLTKDRKRTGIEEAVVCGKATIDGLPLVVCVMDARFRMGSMGAYVGEAIASAVRTATSLGLPVVLFTASGGARMQEGMVSLMQMANTSIALKEHDEAGLLYIAYLTHPTTGGVSASFAMLGDLNVAEPGALIGFAGRRIIEQTIREKLPENFQTAEFLLESGQLDAVIHREQMRSFLKKMIELHDGGVRHV", "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": "MAAETASGSNRSISNSPLIENSDSNQILVPEKKSWKNFFSYLGPGFLVSIAYIDPGNFETDLQSGAQYKYELLWIILVASCAALVIQSLAANLGVVTGKHLAEHCRAEYSKVPNFMLWVVAEIAVVACDIPEVIGTAFALNMLFNIPVWIGVLLTGLSTLILLALQQYGIRKLEFLIAFLVFTIALCFFVELHYSKPDPKEVLYGLFVPQLKGNGATGLAISLLGAMVMPHNLFLHSALVLSRKIPRSVTGIKEACRYYLIESGLALMVAFLINVSVISVSGAVCNASDLSPEDRASCQDLDLNKASFLLRNVVGKWSSKLFAIALLASGQSSTITGTYAGQYVMQGFLDLRLEPWLRNFLTRCLAIIPSLIVALIGGSAGAGKLIIIASMILSFELPFALVPLLKFTSSKTKMGSHANSLVISSVTWIIGGLIMGINIYYLVSSFIKLLLHSHMNLVAIVFLGVLGFSGIATYLAAISYLVLRKNRESSSTHFLDFSNSQTEETLPREDIANMQLPNRVAVIGDLN", "text": "FUNCTION: Probable intracellular cadmium (Cd) transporter that participates in the distribution or availability of Cd within the cell. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family."}
{"protein": "MRANSPTQGISLKMHQARPLFLVTVALQLIGLGYSYQSEGDGAREVSNILSPVIPGTTLDRTLSNSSRKNDIPEGARLWDSLPDSSTLGESAVPVSRCCHNGGTCVLGSFCVCPAYFTGRYCEHDQRRRDCGALGHGAWTLHSCRLCRCIFSALYCLPHQTFSHCDLKSFLSSGARGSRECSIPSLLLLVLCLLLQGVAGKG", "text": "FUNCTION: Nodal coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted. SIMILARITY: Belongs to the EGF-CFC (Cripto-1/FRL1/Cryptic) family."}
{"protein": "MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRRSSSGFRVDGFEKRAAASESNNYMNHVAKQQSEEAFPQEQQKAPPVVGGFNSNVGSKVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNKPNDWTVPKGCFMANVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFTIHYVSNAQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTKIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFLSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPVFKEFVKRWKSYLKGSRAKHN", "text": "FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the D-glucuronyl C5-epimerase family."}
{"protein": "MGMSKSLSCFGYPLSIFFIVVNEFCERFSYYGMRALLILYFRNFIGWDDNLSTVIYHTFVALCYLTPILGALIADAWLGKFKTIVWLSIVYTIGQAVTSLSSVNELTDNNHDGTPDSLPVHVAVCMIGLLLIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTIITPMVRVQQCGIHVKQACYPLAFGIPAILMAVSLIVFIIGSGMYKKFKPQGNILSKVVKCICFAIKNRFRHRSKQFPKRAHWLDWAKEKYDERLIAQIKMVTRVLFLYIPLPMFWALFDQQGSRWTLQATTMSGRIGILEIQPDQMQTVNTILIIILVPIMDAVVYPLIAKCGLNFTSLKKMTIGMFLASMAFVAAAILQVEIDKTLPVFPKANEVQIKVLNVGSENMIISLPGQTVTLNQMSQTNEFMTFNEDTLTSINITSGSQVTMITPSLEAGQRHTLLVWAPNNYRVVNDGLTQKSDKGENGIRFVNTYSQPINVTMSGKVYEHIASYNASEYQFFTSGVKGFTVSSAGISEQCRRDFESPYLEFGSAYTYLITSQATGCPQVTEFEDIPPNTMNMAWQIPQYFLITSGEVVFSITGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQINKQWAEYILFAALLLVVCVIFAIMARFYTYVNPAEIEAQFEEDEKKKNPEKNDLYPSLAPVSQTQM", "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:8139693, PubMed:9051570, PubMed:12082113). Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (PubMed:8139693). Mediates transepithelial transport of muramyl and N-formylated bacterial dipeptides contributing to recognition of pathogenic bacteria by the mucosal immune system. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
{"protein": "MAPNIRKSHPLLKTINNSLIDLPTPPNISTWWNFGSLLGICLMAQIITGLLLATHYTADSTLAFTSVSHTCRNVQYGWLIRNLHANGASMFFICIYLHIGRGLYYGSYLYKETWNTGVLLLLALMATAFVGYVLPWGQMSFWGATVITNLFSAVPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFIIAALTLVHLAFLHESGSNNPLGIPSSCDKIPFHPYYTMKDILGLMFMLTPLMTLALFSPNMLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILLLMPFLHKSKQRTMTFRPLSQILFWMLIANLLILTWIGSQPVEDPFIIIGQLASITYFTLILVLLPMASTLENKLLKY", "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": "MPDLSHEASAKYWFEYLDPMIYRVITFMESVENWTLDGNPELEEAMKQLGQELDDIEKIDLGLLAEEDKFIRIVGNIKSGRGLRLLQAIDTVHPGSASRVLIHAEETSLSSSDPAGFFLKRNIVFERLRLLSRVFCQYRLKLVLRALEGDE", "text": "FUNCTION: Component of the Dot/Icm type IVB secretion system (T4BSS), which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:15661013, PubMed:18069892, PubMed:17040490, PubMed:22694730, PubMed:32513920). Part of a subcomplex which recruits effector proteins and delivers them to the core transmembrane subcomplex (PubMed:23028312, PubMed:32513920). The IcmS/IcmW protein complex plays an important role in protein translocation by interacting with multiple Dot/Icm effector proteins to facilitate their translocation into host cells (PubMed:15661013, PubMed:18069892). Interaction promotes conformational changes in the effector protein, which may facilitate display of a C-terminal translocation signal (PubMed:18069892). May maintain the substrates in a translocation competent form (PubMed:23028312). Required for intracellular growth in host cells, replicative phagosome formation and phagosome trafficking (PubMed:10361301, PubMed:11115108). SUBCELLULAR LOCATION: Cytoplasm Note=Associates with the inner membrane at the poles in a DotL/DotM/DotN-dependent manner."}
{"protein": "MVASIRSGVLTLLHTACGAGILAMPYAFKPFGLIPGVIMIVLCGACAMQSLFIQARVAKYVPQGRASFSALTRLINPNLGIVFDLAIAIKCFGVGVSYMIVVGDLMPQIMSVWTRNAWLLNRNVQISLIMLFFVAPLSFLKKLNSLRYASMVAISSVAYLCVLVLLHYVAPSDEILRLKGRISYLLPPQSHDLNVLNTLPIFVFAYTCHHNMFSIINEQRSSRFEHVMKIPLIAISLALILYIAIGCAGYLTFGDNIIGNIIMLYPQAVSSTIGRIAIVLLVMLAFPLQCHPARASIHQILQHFAEENVSISATSADEPTVATESSPLIRDSSLDLNEVIEEESIYQPKETPLRGKSFIVITCSILVASYLVAISVSSLARVLAIVGATGSTSISFILPGLFGYKLIGTEHKTAVPLTTKIFKYTGLLLFIWGLIIMITCLTAALKLN", "text": "FUNCTION: Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting aspartate and glutamate. Requires ATP for function. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "MREETVSWKYFKRDVVPFTAMIAIECTTVGSSILYKAATLRGFSFYVFVFYAYVGATLVLLLLSLIFGRSRSLPTAKSSLFFKIFLLALLGLTSRVAGCKGIEYSSPTLSSAISNLTPAFTFILAIFFRMEQVMLRSSATQAKIIGTIVSISGALVIVLYKGPKLLVAASFTSFESSWIIGGLLLGLQFLLLSVWFILQTHIMEIYPEEIAVVFCYNLCATLISGTVCLLVEKDLNSWQLKPGFSLASVIYSGLFDTSLGSVIHTWGLHVKGPVYISLFKPLSIAIAVAMAAIFLGDTLHLGSVIGSVILSFGFYTVIWGKAREDSTKTVSDSEQSLLLPSHDREED", "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": "MARQTDVRPIVRLRSTAGTGYTYVTRKNRRNDPDRLVLRKYDPIARRHVEFREAR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MKKILLACSSGMSTSLLVTKMKEYAQSIGEEAEIWAVGQDKAKEDMRKADAVLIGPQMSFLKSELQKEADQYNIQVEVIDMMAYGMADGKKAYEQALSLMVNQ", "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": "MQVKETVTDGLKREFQVTLAVSDIGSQVDARLDELKDKVRLNGFRPGKVPLSHLKRTYGRSVTAEVLEKLIRETNDNIFTERGFRLATEPKITMPTEAKEVEDVLAGNADLNYTVAVEVVPEIQLVDFKTISVEKPVVEVGDSDVDDAIKRIVEANRGYDDKGEGATAASGDRVTVSFKGSIDGTPFDGGSAEGIPVVIGSGTFIPGFEDQLIGIAVGETRTIKATFPTNYATAELAGKAAEFETTATLVEAPKDTPADDEFAKTLGLESLDKLKEAARGRLAAEYAGVSRQRVKRALLDRLDEAHQFEAPATLVEQEFEALWRSIVGEMTSTGSTFESENTTEDAAKEEYRKIADRRVRLGLVLSEIGEKNKIQVTDDEVSRAVMERARQMPGREKEVWEFYRKTPEAVAQLRAPIFEDKVVDFILELATVTEKPVSKEELYKDDDADKSAA", "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": "MAKDPVRVLVTGAAGQIGYALVPMIARGVMLGADQPVILHMLDIPPAAEALNGVKMELVDAAFPLLKGVVATTDAVEACTGVNVAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEKHAAPNCKVLVVANPANTNALILKEYAPSIPEKNISCLTRLDHNRALGQISERLNVQVSDVKNVIIWGNHSSSQYPDVNHATVATPAGEKPVRELVADDAWLNGEFISTVQQRGAAIIKARKLSSALSAASSACDHIRDWVLGTPEGTWVSMGVYSDGSYNVPAGLIYSFPVACKNGEWSIVQGLPIDEFSRKKLDATAEELSEEKALAYSCLT", "text": "FUNCTION: Catalyzes the reduction of the carbonyl group of oxalacetic acid. No activity with pulegone. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MSLDQYLPIFLFILVGIGVGVAPQVLGYILGPNLPDSAKNSPYECGFEAFGDARMKFDVRYYLVAILFILFDLEIAFLFPWAVALKDIGALGFWSVMVFLTILVVGFIYEWKKGALDWE", "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": "MGQKVHPHGLRVGVIKDWDAKWYANSQNFADNLIEDDKIRKFVKKRSYSAGIAKIEIERTAKRVKINIHTGKPGMIIGKGGKGIEELKSEILKMIKEKNVIINIVEVKRPETDAQLMAENVAQQLEKRISFRRAMKQTIQRAMRSGAKGVKTACSGRLGGAEIARTEQYHEGTIPLQTLRADIDYGFAEADTTYGKIGVKVWLYKGEVLPTKKVRTEEISQ", "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": "MKRLHYAWIIVSVTFLILLAVQGVRLSFGAFVEPWERQFSIDRSTISLISTVSFIVYGISQPVIGRLVDKWGARAVLAWSALLTGVSIFLTYLVTSPWQLFLLYGLGVSLGVGGASNVAASVLVVNWFSKKRGLAFGIMEAGFGAGQMLLVPGSLMLIHWFSWKLTVVVLGLLLIVIVFPAALLMLRNNPSEKNTEPIGGLAASEKETAPKTTALSVAGMFRMRQFWFLIFPFLICGFTTVGLMDTHLIPFSHDHGFSTTVTSAAVSLLAGFNIAGILLSGIVADRWSSRKILCILYAVRALSIVILIYSHEPYLLLAFAILFGLVDFATVAPTQMLATQYFQNYSIGLMIGWLSLAHQIGSALGAYVPGVIYTVTGEYTLAFYLSIGMLVLASVMNVMLREPAAVTRDSAAVVDK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MSSSIPPRLYDMSPTESKKQEDVSETELVYPVELADATIQPSKSDDDLFDSNDFSKTYLAKSRILSNAMNEIGFGRYQWYLFFVAGFGWMSDNIWPVCTSLILMRLDEVDGPHPPAEGRAPYLTLSQNLGLLVGAMVWSLSADTIGRRWAFNLTFLFTGVFAVIAGASPNFASICVFDALWSFGVGGNLPVDSAIFLEALPSSHQWLLTVMSFWWAIGQVIANLVSWGLISNFSCPDDESVCHRADNKGWRYFLFTMGGMTLLMFAARFLVSVYESPKFYLAKGDDYKAVETIHKIARINGKTCTLTVEELYAIDRQEQEESDLDDSKSSDAKSVTQGTTNLIVEKLRKYNFEHIRQCFGSRKLAISSILVILSWAVIGLAFPLYNAFLPYYLETRGNANEPLSVAKTYRNSLIVSAIGVPGSLIAGVLVEFRIGRKGTLCLSLILTGVFLFASTTAKTSNAYLGWNCTFSFFSDIMYGVLYAYTPEVFPSKVRGTAVGLAASANRILGIFSPVIAMRANLTTSAPIFVSGALFIFAGILVVFFPYEPRGKSSF", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MKGTISHRESFLTHIRQQLGKDSSSSASIQRPAWKHQVQWETNGLLSKEELVEQLKMQCQRIHTRVVETTPEEAPSALRSLMTEYGEGSVMTSGDHRFEQYGFYPMFDSLQHEGFAVTSWNAEASREENIRLAEQAAYSVVFSDYTLAESGTIVLSSHQGQGRALHFLPMMYIVCIEKSTVVPRMIQAVSTLNRLVEEGEQAKGAIHFISGPSNSADIEMNLVVGVHGPVRAVYLLIDDE", "text": "FUNCTION: Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. SIMILARITY: Belongs to the LutC/YkgG family."}
{"protein": "MEGGGGGADGQAQPVAQAPPAMQPMQQLSRYESQKRRDWNTFLQYLKNHRPPLTLARCSGAHVIEFLKYLDQFGKTKVHASGCAYYGQPSPPAPCPCPLRQAWGSLDALIGRLRAAYEESGHAPESNPFAARAVRIYLREVRDAQAKARGIPYEKKKRKRTQQQQPPPPPPPPPQHQPGAAAGEASSSSSAAAAAVAAEGSGSSAAAAAATSQTGGGGGGSTTTTTASAAAPTTATRV", "text": "FUNCTION: Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the plant homeotic and developmental regulators ALOG protein family."}
{"protein": "MKSFPVAFLVLLIFILSVHRGVTTRGSDVAKFCCFQYSHKILPWKWIQSYKFTRSSCSQQAVIFTTKKGHKVCAQPKEKWVQRYIALLREQQQS", "text": "FUNCTION: Chemoattractant for eosinophils and basophils. Acts as a ligand for C-C chemokine receptor CCR3 which triggers Ca(2+) mobilization in eosinophils. Also acts as a ligand for CX3C chemokine receptor CX3CR1, inducing cell chemotaxis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVTLQPLRRYPLDAAILFSDILTIPDAMGLGLYFEAGEGPRFTAPVTCKADVDKLPIPDPEDELGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYADPQALHLLLDKLAKSVTLYLNAQIKAGAQSVMIFDTWGGVLTGRDYQQFSLYYMHKIVDGLLRENDGRRVPVTLFTKGGGQWLEAMAETGCDALGLDWTTDIADARRRVGHKVALQGNMDPSMLYAPPARIEDEVATILAGFGQGEGHVFNLGHGIHQDVPPEHAGAFVEAVHRLSAQYHN", "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": "MKVNDRVTVKTDGGPRREGVVLEVEEFSEGVMYLVSLADYPAGVWFFNEVDSQDGTFVGPLSQ", "text": "SIMILARITY: Belongs to the DsrB family."}
{"protein": "MIQQESRLKVADNSGAREILVIKILGGSRVKTANIGDIIVATVKQATPGGVVKKGDVVKAVVVRTKYGTHRPDGSYIKFDENAAVIIGEDKSPKGTRIFGPVARELRDGNFMKIVSLAPEVL", "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": "MLELDLQLASDGQHPDEAQLRRWCELALRQRTADSELTIRLVDEEEGRELNRTWRHKDYATNVLSFPAEIPDGILDIPLLGDLVICVPVLEREAAEQGKTLEAHWAHLVIHGCLHLLGYDHIEEDEALEMEELERQLLAELGHPDPYAGDE", "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": "MTQVIIDGDACPVTNSIIELTKGTGIFVTVVRSFSHFSTVIQPEHVNIIYVDDGPDAVDYRIVKLVHSDDLVVTQDYGLASLLLNKAKIVMHHKGFIYNQENINTLLEQRHASAQFRKSGGRTKGPAAFTEEDVSKFESIFSNLIHKYFLETED", "text": "SIMILARITY: Belongs to the UPF0178 family."}
{"protein": "MKEHHIPKNSIITVAGTVGVGKSTLTKTLAKRLGFKTSLEEVDHNPYLEKFYHDFERWSFHLQIYFLAERFKEQKTIFEAGGGFVQDRSIYEDTGIFAKMHADKGTMSKVDYKTYTSLFEAMVMTPYFPHPDVLIYLEGDLENILNRIEQRGREMELQTSRSYWEEMHTRYENWISGFNACPVLKLRIEDYDLLNDENSIENIVDQIASVIHDNQKK", "text": "FUNCTION: Plays an essential role in generating the deoxyribonucleotide precursors dATP and dCTP for DNA metabolism. The phosphate acceptor specificity is strict toward deoxyadenosine (dAdo) and deoxycytidine (dCyd). The specificity toward the sugar moiety of the nucleoside is less strict. Both 2-deoxyribose, ribose, and arabinose nucleosides are phosphorylated, although the 2-deoxyribonucleosides are preferred. The phosphate donor specificity is dependent on the deoxyribonucleoside substrate, but GTP is efficient with both deoxycytidine and deoxyadenosine. Only nucleoside triphosphates can act as phosphate donors. SIMILARITY: Belongs to the DCK/DGK family."}
{"protein": "MLSASDLRKGLKLDIEGSPYIIIDFDFSKPGKGQALYRCKMRNMITGNQLVKTYRSSDKFEKASLEERKMQFLYSQGEEYHFMDNENYDQLFITKDMLGDNIYFLQDNMDVDVLFFDEKPIDITLPIFVNLEVTRADPWVKGDTSGTDTKPITVETGYQLQVPPFVEQGDKIQIDTRTGQYVTRVKQ", "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": "MFVYGSIINPCPTEHVMSVLAISITTVALAEIGDKTQLLSLLLASRYRKPIPIIAAIFLATLANHALAAWLGVVVADYLSPDILKWVLVVSFLTMAGWILIPDKLDGEESISTRGPFVASFIAFFMAEIGDKTQIATSILGAQYADALSWVIVGTTLGMLLANVPVVLIGKLSADKMPLGLIRKVTAGLFLLMALATAFF", "text": "FUNCTION: Involved in manganese homeostasis. May function as a manganese exporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDT1 family."}
{"protein": "MASRESGGSRAAALLLVLGVERALALPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPGPNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCPENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS", "text": "FUNCTION: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity). In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containg-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol (PubMed:29745899). 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": "MPAAAVQEAVGVCSYGMQLSWDINDPQMPQELALFDQFREWPDGYVRFIYSSDEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCTQACTLPDGSRLQLRPAICDKARLKQQKKACPNCHSALELIPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEARRSAIKRQMASFYQPQKKRIRESEAEENQDSSGHFSNIPPLENPEDFDIVTETSFPIPGQPCPSFPKSDVYKATCDLATFQGDKMPPFQKYSSPRIYLPRPPCSYELANPGYTNSSPYPTLYKDSTSIPNDTDWVHLNTLQCNVNSYSSYERSFDFTNKQHGWKPALGKPSLVERTNHGQFQAMATRPYYNPELPCRYLTTPPPGAPALQTVITTTTKVSYQAYQPPAMKYSDSVREVKSLSSCNYAPEDTGMSVYPEPWGPPVTVTRAASPSGPPPMKIAGDCRAIRPTVAIPHEPVSSRTDEAETWDVCLSGLGSAVSYSDRVGPFFTYNNEDF", "text": "FUNCTION: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MQFQLFSFVLIILNCVDYSHCQANRWRRSKRASYGTNPICKGCLSCSKDNGCLRCQPKLFFYLRREGMRQYGECLQSCPPGYYGVRGPDMNRCSRCRIENCDSCFSRDFCIKCKSGFYSHKGQCFEECPEGFAPLDDTMVCVDGCEVGPWSEWGTCSRNNRTCGFKWGLETRTRQIVKKPAKDTIPCPTIAESRRCKMAMRHCPGGTRTTKKKDKKNKKKKKKLLERAQEQHSVVLATDRSSQ", "text": "FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for lgr4-6 receptors. Upon binding to lgr4-6 (lgr4, lgr5 or lgr6), lgr4-6 associate with phosphorylated lrp6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Acts both in the canonical. Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway (By similarity). Activates neural markers and promotes muscle formation. Overexpression blocks activin, nodal and BMP4 signaling, suggesting that it may negatively regulate the TGF-beta pathway (By similarity). During embryonic development, plays a crucial role in limb specification, amplifying the Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3, hence governing the number of limbs an embryo should form (PubMed:29769720). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the R-spondin family."}
{"protein": "MATKSTSKPLLLSFLMMSYLISTFHVITVAEGRTLQFTKMATDHSGAGNLMDCWNAGLELKSCTDEIVKFFLSQTGTSEPPVKGGIDKDCCGAIGLVVKDCWSVMFTSLGLTTMEGNNLREYCEFQAEKSELSPSPAPETLALSPVEITYPGLDY", "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": "MAKVNFDYSIAKQFFSKEELSYMKGAAEAAKQILLEKTGAGNDFLGWIDLPVDYDKEEFERIITSAKKIQSDSEVLLVIGIGGSYLGARAAIEFLRHSFYNSVSKEVRKTPEIYYVGNNISSTYLSHLIEVIGDRDFSVNIISKSGTTTEPAIAFRIFKKLLIQKYGKVEAAKRIYATTDKSKGALKNLATEEGYESFVVPDDVGGRFSVLTAVGLLPIAVSGADIKQLMDGAASMRERCLNNKFEENDSLLYASIRNILLRKGKNIEILANYEPALHYVGEWWKQLYGESEGKDKKGIFPASVDLTTDLHSMGQFIQDGQRTMFETVINLEKSTCEVILEEEDVDLDGLNYLAGKSVDFINKSAMKGTLLAHTDGDVPNLIVNIAEQSEFCLGELFYFFEFACGVSGYILGVNPFDQPGVESYKKNMFALLGKPGFEELSKKLQERLQ", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MSHEYDTVAPPNAKRMKTDNQLEDKKILYVVLEGCSLETAKVGGEYAILSSDKHANFLRKQKKDPADYRPDILHQCLLNLLDSPLNRAGKLRVFFRTSKNVLVDVSPQCRIPRTFDRFCGLMVQLLHKLSIRAAETTQKLMSVVKNPVSNHLPVGSRKMLMSFNVPELTMANKLVAPETDEPLVLIIGGIARGKIVVDYNDSETKISNYPLSAALTCAKVTSGLEEIWGII", "text": "FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)- methyltransferase that methylates a pseudouridine in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3- carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre- ribosomes. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family."}
{"protein": "MTTAHILGFPRIGAQRELKFALERYWRDGASADAERALVDTGRALRAEHWRIERDAGLDCVTVGDFAWYDHVLTTLAHVGGLPRRFGFDARALTLADYFAAARGNAAQPAMEMTKWFDTNYHYLVPEYSPATTFGPGVEWLFDEVREARALGYRAKAALVGPLTLLWLGKARDGLVERLALLPRLVPAYRALLARLREAGVDWVQIDEPIFSLDLPDAWRDAARPTYEALAPGAPKLLVATYFDDASEHAALLKALPVAGLHVDLVRADAQLDAFVADYPADKVLSCGIVDGRNVWRNDLDRSLARLAPVRDALGERLWVATSCSLLHVPVDLAHEPRLDEELKTWLAFAAQKTREVAALRDALVKGRAAVAAEFDDAAVVAAARRTSARIHNPLVKRRVAALTDADARRASAYSVRAAAQRARFGLPLLPTTTIGSFPQTPEIRRARAAFKQGVLDHLGYLEAMREQVRIAIDKQLAYGLDVLVHGEAERNDMVEYFGELLWGFAITSNGWVQSYGSRCVKPPLVYGDVYLPEPMTVGWASYAQSLSAKPVKGMLTGPVTMLQWSFVRDDQPRATTALQIALALRQETLDLEKAGIGMIQIDEPALREGLPLKARERAAYLDWAVRAFGIAASGVADDTQIHTHMCYSEFGDILPSIAALDADVISIETTRSNMELLDAFETFDYPNEIGPGVYDIHSPRVPDADEIERLILLALERIPAQRLWVNPDCGLKTREWRQVDAALAAMVDAAKRVRQKVEEAAPA", "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": "FTIFLGVALLQGVLTLSPIPVPEEEWAEFSRMLRDPSYRLPTTTRPRHYAVTLTPYFDVVPAGVSGLTTFSFDGEVTIYISPTQANVNEIVLHCNDLTIQSLRVTYVSGNSEVDITATGQTFTCEMPYSFLRIRTSTPLVMNQEYIIRSTFRGNLQTNMRGFYRSWYVDRTGKRWMATTQFQPGHARQAFPCYDEPGFKATFDITMNREADFSPTISNMPIRATTTLTNGRISETFFTTPLTSTYLLAFIVSHYQVISNNNNAARPFRIYARNNVGSQGDWSLEMGEKLLLAMENYTAIPYYTMAQNLDMKQAAIPDFSAGAMENWGLLTYREALILYDPLNSNHHYRQRVANIVSHEIAHMWFGNLVTCAWWDNLWLNEGFARFSQYYLTATVDPELGYEIRFIPEQLQVAMFSDSVDSAHALTDTSVNDPVAVSAHFSTITYARGAAILRMTQHLLSYDTFVKGLRQYLRARQFDVAEPYHLFSALDAAAAEDNALAAYRGITIDAYFRTWSEKAGHPLLSVTVDHESGRMTLVQARWERNTGVSRFPGLWHIPITWTRAGAPDFENLKPSQVMTGQSLVIDRGTRGQEWVIFNKQVSGFYRVNYDNTTWGLITRALRSANRTVIHELSRSQIVDDVFQLARSGVMSYQRALNILSYLRFEDAYAPWLSAISGFNWVIRRFAHDAANLQTLQNQIIGLSEAVVARLGFTEVSGGTYMTDLQRLHVMQFLCNVGHQQCIDAGRQNFLNWRNGSFIPANMRPWVYCTGLRYGSAEDFNYFWNRYIVEDLSNEKVVMLEAAGCTRDQASLEKFLNAIVSGNDDVRPQDHSSALSSAITSNDVNTMRAFDWLTKNVDQITRTLGSITSPLNTITSRLLTEAQMTQVQTWLDANRNTIGAAYNTGVNGIATSRANLQWSANRMSEFLRFFETGFVDDVPSEATTVAPPAETTVTPSTFPPTVAPATTPAPGSGNIAALSVVSLLVTLAINMVA", "text": "FUNCTION: Binds to the B.thuringiensis toxin, CryIA(C). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "MAEQPAGQAGTTDNRDARGDREGRRRDSGRGSRERDGEKSNYLERVVAINRVSKVVKGGRRFSFTALVIVGDGNGMVGVGYGKAKEVPAAIAKGVEEARKSFFRVPLIGGTITHPVQGEAAAGVVLLRPASPGTGVIAGGAARAVLECAGVHDILAKSLGSDNAINVVHATVAALKLLQRPEEVAARRGLPIEDVAPAGMLKARRKSEALAASVLPDRTI", "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": "MLRFKELYQQKIIENLQKKFSYKNKHEIPQIKKIVINMGVGEATADSKVINNAVNDLTLISGQKPVVTLARKSIATFKLRENMKIGCKVTLRKDRMYDFLERLVIVALPRVKEFRGFSYKSFDGKGNFTFGLKEQIVFPEINYDKIDTIRGMDITIVTSAKTDQESKFLLSGFNLPFYN", "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": "MAFNFNWSPLMADASFYTRAQDLLTAALNKSPKPPIIVDDIIVTELNLGSIPPELEILEIGDLAEDRFRGIFKMSYSGDAFLTLKTRVQANPLNTYLLTRPSFASPLPLAAATPLTIPLQITLSDFKLSGFVILVFSKQKGITVVFRNDPLESLKVSSTFDSIPFVRDFLQREIEAQLRILFMDELPAIIHRLSLRLWVPEYRAGEEDQDQNTNTAGEGPGQDPLASPPQDPVDALGNALNESEIASLSLDSSVETHSLFSQKNLLRLAALTDSQRTLSLFTPSIQEVVYRAWTSPSDQGDISGGVTSPLSPALSRTQSQVGGMSSFQDNASTISSYSRTSTSTHTFSTYGLNLGAGRHSKAHARKRKKRVVDLRRPKQPESETASVTDESSFTETTSAPSVRSAPLPRVNEQPDDPVTPPLSPDSDFHLPPIPERHRFSISRPALRRDIATEMLRETGESSSEPARRHAEVDDIDATPRTIIRHEPSRYEGEKQEAGPSRQLPSTILPFTEEKSTPGPVDQALVERIAGEIARRMREDKLMGTNSCAFWNRPGHEESPPPAYGQ", "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": "TITEETTGFFALGSGPARALSRVEDLFKELNYADQGPNTALVIEGDKAPPAAVIENIAKHCGINPKGLSILYATTWSLAGTVQIAARVLEVAMHKAHALHFALENIIDGTATTPIAPPFPDFVKAMGRTNDAIIYGGRAHLFVKGTDAEAKRLAEGLPSSTCASFGKPFAEIFADVNG", "text": "FUNCTION: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl- H(4)MPT. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MCH family."}
{"protein": "MVEEVVRRLDIPDGVDVQISGRSVRVKGPKGELSRELWYPDIEIKREDSKILIRSVARKKQHLAMVGTIAAHIKNMIRGVTDGFEYRMRVVYSHFPIQVKVADGKVAISNFLGERKPRFATIVGDVNVEVGKDEILIRGMDKEAVGQTMANIEQATRVRGFDVRIFQDGIYLVEKR", "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": "MTVVPRKGAVGIGTLIVFIAMVLVAAVAAAVLINTSGYLQQKASGTGRETTQEVASGIKVDRVVGYAPDITGDITRLAVYISPNAGSSGIDLNKVRVILSNGQKEVSLKYNYVYNATSSTQTYVALPQGNIFNDIVLGVNGTSENAASTQVNFNWSLLTGSTFGLIVLQDADGSVKASTPTLNQGDLVIIAIDVDAALGGIPPRTSITGEVIPEQGAPGVIEFTTPSTYTAHVMELQ", "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": "MDAPKEIFLKNYTKPDYYFETVDLSFSLGEEKTIVSSKIKVSPRVKGSSAALVLDGHDLKLLSVKVEGKLLKEGDYQLDSRHLTLPSLPAEESFVLEIDTEIYPHKNTSLEGLYKSSGNFCTQCEAEGFRKITFYQDRPDIMAKYTCRVEGDKTLYPVLLSNGNLISQGDIEGGRHYALWEDPFKKPCYLFALVAGQLVSRDDTFTTRSGRQVSLKIWTPAEDLPKTAHAMYSLKAAMKWDEDVFGLEYDLDLFNIVAVPDFNMGAMENKSLNIFNSKLVLASPETATDADYAAILGVIGHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDMGSRTVKRIADVSKLRIYQFPQDAGPMAHPVRPHSYIKMDNFYTVTVYEKGAEVVRMYKTLLGTQGFRKGIDLYFERHDEQAVTCEDFFAAMRDANNADFANFLQWYSQAGTPVVKVVSSYNADARTFSLKFSQEIPPTPGQPTKEPTFIPVVVGLLDSSGKDITLSSVHHDGTVQTISGSSTILRVTKKEEEFVFSDIPERPVPSLFRGFSAPVRVETDLSNDDLFFLLAHDSDEFNRWEAGQVLARKLMLNLVSDFQQNKPLALNPKFVQGLGSVLSDSSLDKEFIAKAITLPGEGEIMDMMAVADPDAVHAVRKFVRKQLASELKEELLKIVENNRSTEAYVFDHSNMARRALKNTALAYLASLEDPAYMELALNEYKMATNLTDQFAALAALSQNPGKTRDDILADFYNKWQDDYLVVNKWFLLQSTSDIPGNVENVKKLLDHPAFDLRNPNKVYSLIGGFCGSPVNFHAKDGSGYKFLGDIVVQLDKLNPQVASRMVSAFSRWKRYDETRQGLAKAQLEMIMSANGLSENVFEIASKSLAA", "text": "FUNCTION: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. Plays an essential role during prophase I of meiosis. Required for correct meiotic reconbination in both male and female gametophytes. SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "MKKLFGLLGHPVGHSLSPLMHNQMFQLLDFDGYYHAFDVEPSQLEKAVEGARALQMQGFNVTIPHKVTIMDYLDMVDEEAQEIGAVNTVVMKDGQLFGSNTDGQGYLESLMDVVTTPFPTQDVLIIGAGGAARAIGTVLKREKVRSITIANRTLAKAEEFSGVLESSETSCSALSLKEAEQQLERFSVIINTTSVGMSPRVDDMPLSLERLSRETVVSDLIYNPLETKFLREAKQKGAKTVDGLGMFVNQGALAFELWTGLRPDREKMRRCVLEQLGG", "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": "MTLYSKKDIVQQARNLAKMISETEEVDFFKRAEAQINENDKVSTIVNQIKALQKQAVNLKHYEKHEALKQVEAKIDALQEELEEIPVIQEFRDSQMEVNDLLQLVAHTISNQVTNEIITSTGGDLLKGETGSKVKHSNNSCSL", "text": "FUNCTION: May work together with YlbF to regulate community development."}
{"protein": "MMDESADIKPVPTSEDVAAPSGTEPVAPAPKKKRARTSTKAIMAAIEQRLGHTFADISLLTTAFTHVSALKSSRGRCDSYQRLEFLGDHVLGLVVSDMLYRAFPKADEGELSKRLADLVRKETCIDVAKSLDLQEGVKLGAVGAGAGARLRRSVLGDICEAVIGAVYLDGGYAAAAAFVERNWLERMRKPVRPLRDPKTVLQEWAQGKGLPTPVYREVERTGPHHDPRFRVAVELPGLESSEGIGGSKRAAEKAAASAMIVREGVK", "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": "MPLFGAHMSAAGGVSNAIRDIVEIGGEVLQLFTANQRQWTPKAPSAADVEAFRRRRAAFGGPVFSHASYLINIANGDGAASAKAVEALVREFERCTALGVDAVVLHPGAHLGAGRGAGILRAARNIDEVFDRCGGQTPALLLENTAGQGTCLGGGLNDLAEIIDASRHASQLGVCLDTAHAFGAGYALHTDEGYRRCMEDIEYGPGLAAVRLFHVNDSLVPCGSRKDRHTHIGEGQLGEAAFVRLLNDPVFAMHPMVLETPKEDGHAADRRNLATLRRLAGR", "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": "MIQGIGVDIVDIARMQQRIDAASGFRELVFSPAEITYCESKANKYESYAARFAAKEAFLKAVGIGIDFSIDLNQIEITNNKAGKPYFVYTKQVEALLLTHIGFVPDAQVSLSHSREQAIAFVLFNKN", "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": "MAKITELDHHLNQEKEALDKVVSNLNELCEHNQKLQGFIEIQKEVKELKKEHIKSLSWFKKLINTVSNIKYVFVKSEEQLAKDAIEQNNKLLKRIDNTILSVADKSGPLKQELQKELRKNFENLAKKDLSKDQRERLSNLLNNEYAANPQKFAQLPMSKPLHFPNAEELENQHNDLKVIQQNVLNLLTENSNIEELKKIQKQVAEIREEVPFTKLEKLNNFWQKIKNIFVNNSEQVLAKNKENNTKTIINIEEKLHKANNKFFELVSNKKQDIENIISNLPDSKRLEAIKEKLQKHINVKDTNNIAEQASAAQLQSAETKPTAVVLPNNAIPTTPPVTEEKTFTPPPAPPPPMPTDNIPTPLPVSKAEATEHKNVETAASNVPPPPPPPMPTGNVPPPPPVGDNTVTSTPQKAKETNQPRPAVDTTNLMKQIQGGFNLKKIEYGEDGKPIPKNKEDTKETSDPIIAALNKIRSAKVSSDSERSNSDSGTDSGWASDVSTRSKKVLTRRERNAKQSQQR", "text": "FUNCTION: Recruits and activates the Arp2/3 complex, which in turn leads to actin polymerization, promoting Rickettsia motility during infection. SUBCELLULAR LOCATION: Cell surface."}
{"protein": "MGRKKLEIKRIENKSSRQVTFSKRRNGLIEKARQLSVLCDASVALLVVSASGKLYSFSSGDNLVKILDRYGKQHADDLKALDHQSKALNYGSHYELLELVDSKLVGSNVKNVSIDALVQLEEHLETALSVTRAKKTELMLKLVENLKEKEKMLKEENQVLASQMENNHHVGAEAEMEMSPAGQISDNLPVTLPLLN", "text": "FUNCTION: Putative transcription factor that seems to play a central role in the regulation of flowering time in the late-flowering phenotype by interacting with 'FRIGIDA', the autonomous and the vernalization flowering pathways. Inhibits flowering by repressing 'SUPPRESSOR OF OVEREXPRESSION OF CONSTANS 1'. At elevated temperatures (e.g. 29 degrees Celsius), maintained at high levels in a JMJ30/JMJ32- dependent manner to prevent extreme precocious flowering (PubMed:25267112). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MIPLVALLVLLTLQASPGDIVSVNVTDTATLTVGDSCMYFVDNLQPSINATPGEYEVKIGINCTPGLKEVYADGSVLAQIDVNETTIDYQAYAASLEKENLALQKEVESLKEKLKISQEQIETLKSQLEDLQNKAKMLGIQNELQKQQIEELQKKLERAKTELQKKKSDLDELEEKIRELNRQSSIYRLATFFMVSLFVGSFVALVFVARKE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: To A.fulgidus AF_0540."}
{"protein": "MNPARCRILAVGKVRRGWIQDGIDLYLKRLPGLTISELRDSNPDKEADAIRAALRPDETLIALMEQGDTLASVPFAQRLEQFGNQRLAFVIGGADGLTAELKAQAQWRLSLSPMTFPHELARLMLVEQLFRAQAIVQGSPYHRA", "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": "MASKSWLNFLTFLCGSAIGFLLCSQLFSILLGEKVDTQPNVLHNDPHARHSDDNGQNHLEGQMNFNADSSQHKDENTDIAENLYQKVRILCWVMTGPQNLEKKAKHVKATWAQRCNKVLFMSSEENKDFPAVGLKTKEGRDQLYWKTIKAFQYVHEHYLEDADWFLKADDDTYVILDNLRWLLSKYDPEEPIYFGRRFKPYVKQGYMSGGAGYVLSKEALKRFVDAFKTDKCTHSSSIEDLALGRCMEIMNVEAGDSRDTIGKETFHPFVPEHHLIKGYLPRTFWYWNYNYYPPVEGPGCCSDLAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPTLPERILKEISQANKNEDTKVKLGNP", "text": "FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T subfamily."}
{"protein": "MTNPRETIPPGNSGEETIEEAFDWLDRTVEAINREAVNHLPRELIFQVWQRSWRYWHDEQGMSRSYTKYRYLCLMQKAVFMHFKKGCTCRGEGHGPGGWRSGPPPPPPPGLV", "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": "MQNAKLMLTCLAFAGLAALAGCSFPGVYKIDIQQGNVVTQDMIDQLRPGMTRRQVRFIMGNPLIVDTFHANRWDYLYSIQPGGGRRQQERVSLFFNDSDQLAGLNGDFMPGVSRDEAILGKEGSTTVTQPADQQKPEAQKEEPPKPGSTLEQLQREVDEAQPVPVPTPEPLDPSPQ", "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 (By similarity). May have a structural role in maintaining the cell envelope integrity. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the BamE family."}
{"protein": "MAAKIGEIVQVHNDNPVKRVPIARPSFGREGKQIKLLSNHFTVKLSGIDAVFYQYSVSIKSEDDKVIDGKGIGRKVMDKVLQTYSSELAGKEFAYDGEKCLFTVGPLPQNNFEFTVILEETSSRAAGGSLGHGSPNQGDKKRSKCTHLAKKIVVGISYAAKIPLKSVALALQGSESDHAQDALRVLDIVLRQQQAKRGCLLVRQSFFSDDFRNLVDLTGGVSGCRGLHSSFRTTIGGLSLNMDVSTTMIVTPGPVFDFLLTNQNVRDIRDIDWPRAKKMLKNLRVKAIHNNMEFKIIGLSDEPCSRQTFPMKVRNGSSEGETVEITVQEYFKSKQVDLTMPYLPCLDVGKPKRPNYVPIELCHMVSLQRYTKALSSQQRATLVEKSRQKPQERMRVVTDAVKNNRYDDDPILSSCGIKIEKQLTRVDGRVLSAPTLVVGNSEDCIPNRGRWNYNNKRLFEPVKIERWAIVNFSARCDMSRISRDLINCGRTKGIIIERPFTLVDEDSQSRRCTPVVRVESMFEKVKANLPGPPEFLLCVLPERKNCDLYGPWKKKNLHEMGIITQCIVPSVKMNDQYYTNVLLKINAKLGGMNSKLSLEHRHMIPIVNQTPTLILGMDVSHGSPGRADVPSIAAVVGSRCWPLISRYRASVRTQSPKVEMIDSLFKPLDDGKDDGIIRELLLDFYKTSQQRKPKQIIIFRDGVSESQFSQVLNVELNQIIKAYQYMDQGPIPKFTVIIAQKNHHTKLFQENTPDNVPPGTVVDSGIVHPRQYDFYMYAHAGPIGTSRPTHYHVLLDEIGFLPDDVQKLVLSLSYVYQRSTTAISVVAPICYAHLAAAQMGQFMKFEEFAETSSGSGGVPSSSGAVVPELPRLHADVCSSMFFC", "text": "FUNCTION: Probably involved in the RNA silencing pathway. May bind to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them (By similarity). SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
{"protein": "MSIDWNWGIFLQQAPFGNTTYLGWIWSGFQVTIALSICAWIIAFLVGSFFGILRTVPNRFLSGLGTLYVELFRNVPLIVQFFTWYLVIPELLPEKIGMWFKAELDPNIQFFLSSMLCLGLFTAARVCEQVRAAIQSLPRGQKNAALAMGLTLPQAYRYVLLPNAYRVIVPPMTSEMMNLVKNSAIASTIGLVDMAAQAGKLLDYSAHAWESFTAITLAYVLINAFIMLVMTLVERKVRLPGNMGGK", "text": "FUNCTION: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane. FUNCTION: (Microbial infection) Probably transports the toxic C- terminal region of CdiA from P.luminescens strain TTO1 across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins. FUNCTION: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for 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 binding-protein-dependent transport system permease family. HisMQ subfamily."}
{"protein": "MSKYSDAKELAGLTLGKKTDYANQYDPSLLQPVPRSLNRDDLQLGDELPFMGHDIWTLYELSWLNNKGLPQVAVGEVYIPATSANLIESKSFKLYLNSYNQTRFDSWEEVRQRLITDLSHCAGEAVEVAVNSVTHYTQQPIVTMEGECIDEQDIDISSYDFDDRLLEGAAGEEWVTETLHSHLLKSNCLITNQPDWGSVEIRYQGHKIDREKLLRYLVSFREHNEFHEQCVERIFTDLMKYCQPESLTVFARYTRRGGLDINPYRSTEQAKPDHNHRMARQ", "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": "MIKLGSHVSFKSPNYLYDSIKESIKNGANCAMIFLGAPQNTKRVDFEKYQYEKYLKDFSNLIKPEDIVVHAPYIINPASLEKADFAISFLSSEIKRMDKAKFKYLVLHPGFYGKNNVKDSLDQLARSIQKIFEITKDSNVEIMLETMSGKGSEVGKSYEEILYVIDKVKSPRLGACLDTCHVWDAGYNINDYQVFKDELIKTGILKHIKVIHLNDSKNELGSHKDRHANIDKGLIGLKNLKRIVHDPIFENIPIILETPWTEKGPIYDQEIAMLLEK", "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": "MAIERKFVNDGFVKASMDEYFAEQLNRAGYGGMELNRTPMGTQIVIYSEKPGMVIGKAGKVIRKLTRDVAARYNLENPQIDAQEVKKPELNAQMMASRLAASIERGWYFRKAGHNTLRAVMNAGALGCEVVISGKLTGARSRVEKFVDGYIKHSGNPVDEVVDEGFAVAIKKLGTLGCKVRIIQPGVVLPDSYTTTEPSEPVTEPVEKPAEKPAAKPAEKPVEAPKKESAAKPKTPAVAPEKPVETAEVAEPEEAEEEPQAEVAEDLEEAEVIQVEGSEELRRQVNGVWQHKHEGYDYWHPMARVHKEAKE", "text": "FUNCTION: Binds the lower part of the 30S subunit head. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MKQYLDLMKHILAEGVDKSDRTGTGTRSVFGYQMRFDLSKGFPLVSTKKCHMRSIIHELLWFLKGETNVAYLRENKVSIWDEWADDNGDLGPVYGAQWRSWPTQSGDAIDQISQVIAQIKSQPDSRRLIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLTMMVAQQCDLALGDFVWTGGDTHLYSNHMEQTALQLSREPMPLPTMTILRKPESIFDYQFDDFELTNYAPHPHIKAPVAV", "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": "MTGQGQPAAGSAAWSTVFRHVRYENLVAGVSGGVLSNLALHPLDLVKIRFAVSDGLEVRPKYKGILHCLTTIWKVEGLRGLYQGVTPNVWGAGLSWGLYFFFYNAIKSYKTEGRAEQLEPLEYLVSAAEAGAMTLCITNPLWVTKTRLMLQYGGVVNPSQRQYKGMFDALVKIYKYEGVRGLYKGFVPGLFGTSHGALQFMAYELLKLEYNKHINRLPEAQLSTPEYISVAALSKIFAVAATYPYQVVRARLQDQHVSYGGVMDVIVKTWRKEGIGGFYKGIAPNLIRVTPACCITFVVYENVSHFLCGLREKKVS", "text": "FUNCTION: Transports folate across the inner membranes of mitochondria (PubMed:15140890, PubMed:17279620, PubMed:21768094). Can also transport FAD across the mitochondrial inner membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MTFELRAAFSPCGDQPEAIAKLTQGVRNRTPSQVLLGTTGSGKTFTIANVVANVNRPTLVLAHNKTLAAQLYQEFKEFFPNNAVEYFISYYDYYQPEAYIARNDTYIEKSLLINSEIDKLRLSATRSILERRDTLIVSSVSCIYGIGSPENYTSMALELTVGTEYPRALLASQLVKMHYQASSVPQRSTFRERGSVIDIFPAYESELAIRLEFFNDTLTSIDYSDPLTMMPKESVTSVILYPGSHYVTPEAVREQAIRSIREELEERLAFFQDRPIEQDRLFHRTTHDIEMIKETGFCKGIENYSRHFTNTPPGAPPTCLLDYFPEDFLLVIDESHQTLPQIRAMYRGDFSRKQSLVEYGFRLPSAYDNRPLTYEEARKYFHNVIYVSATPGETELNESQGHIVEQILRPTGIPDPIPEIRPATGQVDDLLEEIRKRLSKSQEKILVISITKKLAEDIAAFLSELDIAAAYLHSGIETAERTRILSDLRLGNIDVLIGVNLLREGLDLPEVSLVAILDADKEGFLRSTSSLIQFCGRAARNVDGKVIFYADHKTLSIEQTLKETERRRHIQLEYNKANNITPKPIIKAIFANPIPQGGKKAVQDTPQKPLSTQELEKLIKKYENLMLQAANAFRFDEAAQYRDKMKAAKEQLLYLS", "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": "MMDSSEHDYYEYFDEFRGILLYKQFIKYWDNVEAFQARPDDLVIAAYPKSGTTWISEVVCMIYAEGDVKKCRQDAIFNRVPFLECRNDKMMNGVKQLEEMNSPRIIKTHLPPRLLPASFWEKRCKMICICRNAKDVAVSYYYFFLMVANHPDPGSFPEFVEKFMQGQVPYGSWYDHVKSWWEKSTDPRILFIFYEDMKEDIRKEVLKLIHFLGRKPSEELVDKIIKHTSFQEMKNNPSTNYTMLPEEIMNQKVSPFMRKGISGDWKNHFTVALNESFDKHYQQQMKGSTLQLRTEI", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone (PubMed:1406700, PubMed:7980593). Is a key enzyme in estrogen homeostasis, the sulfation of estrogens leads to their inactivation. Also sulfates dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesteroland xenobiotic compounds like ethinylestradiol, equalenin, diethyl stilbesterol and 1-naphthol at significantly lower efficiency. Does not sulfonate cortisol, testosterone and dopamine (By similarity). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4- EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MELFGTDGVRGKAGKLLSAQLSMRLAMAAGIYFRKNSRTNKIVVGKDTRRSGYMIENALVSGLTAVGYNVIQVGPMPTPAIAFLTEDLRCDAGIMISASHNPYYDNGIKFFNHQGDKLQPEDEKAIEAIFFDEQTIEENQKTDQDIGSSKRIDDVIGRYIVHLKNSFPKDLTLNGLRVVIDTANGAAYKVAPTVFSELGAEVFVINDEPNGFNINEKCGAMYPGELAKKVREYRADIGFALDGDADRLVVVDEKGKIVPGDLVIGALATYLKQEGMLQADAIVATVMSNKALEDYLATLGIELVRSNVGDKYVLDEMKKRGINFGGESSGHIIFGDYSKTGDGIVTALQITAYMLRSQKGASEILYPFSLYPSKMENVTVKEKKPLETIEEFPELQKRIEKSGIRSLIRYSGTENKLRILLEGKDQKKLEKLMEELIQFFKERLS", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MPGLFAAKKLKSKRQKFKWKDTHYKRRSLRLDVKADPLEGAPQARGIVIEKVGIEAKQPNSAIRKCVRVQLIKNGKQITAFAPGDGAIGFIDEHDEVVVEGIGGPSGRSMGDIPGVRWKVTKVNNVSLQEMVKGKIEKPVR", "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": "MLVFYAILFVTVFSNTVMGATIDKPIPKPIFREAIEEMEVNKRAKNPYCKEEKCPVGKHCPKKPIVCRIGPCCV", "text": "FUNCTION: Inhibits voltage-gated potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-07 family."}
{"protein": "MERKVLALQARKKRTKAKKDKAQRKPETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKENPPNKMTQEKLEESSTIGQDQTLMERDTEGGAAEINCNGVVEVINYTQNSNNETLRHKEDLHNANDCDVQNLNQESSFLSSQNGDSSTSQETDSCTPITSEVSDTMVCQSSSTVDQSFSEQHISQLQESIRVEIPCEDEQEQEHNGPLDNKGKSTAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWLNS", "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. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Can induce splicing of exon 10 in MAPT/TAU. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus matrix Microsome Nucleus speckle Chromosome Note=Shuttles between the nucleus and the cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus. KAT5/TIP60 inhibits its nuclear translocation. Preferentially localizes to the promoter of gene coding regions. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family."}
{"protein": "MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIEANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDTKEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPALREALTKQVDAPRERSLLQTHILWNESHRCMETTPSLACANKCVFCWWHHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPLFKDFWQQFLDSLKALAVKQQRTVYRLMLVKAWNVDELQAYAQLVSLGNPDFIEVKGVTYCRESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAHRKFKIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGANERSFDPKDTRHQRKNKSKAISGC", "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": "MKTTLIVVGRTVEQHYITAINDYIERTKHFISFDMEVIPELKNTKSLTPEQQKEKEGELIAKALQPGDVVVLLDEHGKEMRSVEFARWMEKKLVNVNKRLVFIIGGPYGFSQKVYDAAHEKISMSKMTFSHQMIRLIFVEQIYRAMTILNGGPYHHE", "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": "ATDYEDEEFPGAVPPSVGAR", "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": "MLIKNNDLIFSSVDKIKYSARRGMLELDIILAPYLNNCYMHEDLANKKLFVEFLTSEDSDMFDWLFKGVTPPQRYQQLIDKIIKEKKKFNQTKLK", "text": "FUNCTION: An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins. Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH and other flavinylated proteins as well. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SdhE FAD assembly factor family."}
{"protein": "MKLTNYTDYSLRVLIFLAAERPGELSNIKQIAETYSISKNHLMKVIYRLGQLGYVETIRGRGGGIRLGMDPEDINIGEVVRKTEDDFNIVECFDANKNLCVISPVCGLKHVLNEALLAYLAVLDKYTLRDLVKNKEDIMKLLKMKE", "text": "FUNCTION: Nitric oxide-responsive transcriptional regulator. It represses the expression of flavohemoprotein hmp and the nitrite reductase nasD. Probably plays a role in the up-regulation of the resDE regulon in the presence of nitric oxide."}
{"protein": "MALWGGRFTQAADKRFKDFNDSLRFDYRLAEQDIQGSIGWSKALVKVNVLTIEEQHQLEQALNELLVEVRSNPQAILQDDAEDIHSWVESKLIDKVGNLGKKLHTGRSRNDQVAVDIKLWCKQRVVELQESVRNLQRHLVQTAENTQQAVMPGYTHLQRAQPITFAHWCMAYVEMFDRDYSRLTDAYNRMNTCPLGSGALAGTAYAVDRDSLAHDLGFAFATRNSLDSVSDRDHIVELLSIASLSMAHLSRFAEDMIIFNSGEANFVELSDRVTSGSSLMPQKKNPDACELIRGKTGRVIGSLTSMLITLKGLPLAYNKDMQEDKEGIFDALDTWQNCVDMATFVLDELKVNVERTREAALKGYSNATELADYLVSKGVPFRDSHHIVGETVVYAIEKGKGLEDLTIPEFRQFSEVVGDDVYEILSLQSCLDKRCAKGGVSPLRVAEAIAEAKTRFA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MEAQKLSAQEIIQFIGNAEKKTGVKVTLSGMPSFKSAGFLAENGRPNFKALANKGIQVLGDFHTHYSLKIIIGDWQAVRPLLEGLTENKDYTIEFEGRNSAVPLLDTRAINARIEPGAIIRDQVTIGDNAVIMMGAIINIGAEIGEGTMIDMGAVLGGRATVGKNSHIGAGAVLAGVIEPASAEPVRVGDNVLVGANAVVIEGVQVGSGSVVAAGAIVTQDVPENVVVAGVPARIIKEIDEKTAQKTALEDALRNL", "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": "MKSGFVSIIGRPSTGKSTLLNSICEHQISIISSIPQTTRNKIKGIFTDKRGQIIFIDTPGFHLSKKQFNIALMHNVHSAIKETELILYVIDIQDKPGIEENEILTIISKSKINFLVVINKIDIQKTKEREIMIFLEEKGIKKDNIIKISAEQKINIEEIKDKIYENLQEGPLYYPEEYYTDQEMNLRTSEIIRGVTIKKLKEELPYSLYIEIEILEDRKNKLFIKANIIVAVESQKGIIVGKGGKGIKTIGEEARKIISEIFEKKCDLFLQVKLRKNWNKNPKLIKNLIN", "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": "MKFRPLHDRILVKRVEEETKTKGGIIIPDTAKEKPIEGKVMAVGNGRLGEDGKLIPLEVKKGDRVLFGKYGGTEVKMDGQEYLIMREDDILGILE", "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": "MTDRLHIVGGGMAGSEAAWQAAQQGIDVVIHEMRPTVGTFAHQTGNLAEMVCSNSFRSDDDEQNAVGLLHWEMRAAGGLIMSAADAHRLPAGGALAVDRDPFAETVTARLHAHPRVSVTAEEVTELPRDGHWIFATGPLTSPALGAAIQAETGAEALAFFDAIAPIVYADTIDMSRAWMQSRYDKGETEEERTAYLNCPMDRDQYEAFIDALLAADKTEFHEGETATYFDGCLPIEVMAERGRETLRHGPMKPVGLTNPHQPDVKAYAVVQLRRDNALGTLYNIVGFQTKMKYGAQTAVFKTIPGLENASFARLGGIHRNTFLNSPTLLDAQMRMKSRPNIRFAGQITGVEGYVESAAMGLLAGRLAAAEIQGRALPEVPQDSAMGALIHHITGGAEAKTFQPMNVNFGLFRPVDGLKGGRRGRKDRYKAYTDRAKEAWTSWLAEAENG", "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": "MLGLKGCLTILIGYVIAVCALFSSRGRNPSLTDWEKLKDQKISNIDNFGLTGQHLLAFFQENLPFLSFSEEKYRHKHVSLYYDVFKEYILRRASSKKCLPVDSAIAKLNKDVNPMPVHSHNDYWRKLPLFEGLAYGASSTEADVWNIDEKILAVGHNEAYLDPVELTLDKLYTGPLLEILDEVNCQDSDSDRKNGVFFNSPETSLFFYIDFKSDDNELTYKLLMEQYFKSLIDSGYLTYYDMKKDEIIWRPVTVILTGNYPTSLDILDNGNDNGYFESSQRFAFLDAPLLSLEPKYSKLSVAATVSFSQLMKHCGSDHWKVSLRGRMDSNEISCAKSIIDGAHALKLKTRIWGAPTWPANLVETISRQIIHDLGSDLLNLDNLFMASSLI", "text": "SIMILARITY: Belongs to the AIM6 family."}
{"protein": "MSASEAQVIARALFDSLTGTALQALRAAASVNGELTPERVLAALPEDAPREIRNLVMALGREGNLDRLPAVVTAFEQMTRRGGARPLTGEVISAVELNPQQRERITAQLTARYGPDLELRFSVDESLIGGLIIRIGDQVLDTSLRTRMAAIQRNMMTS", "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": "MPIQVLPPQLANQIAAGEVVERPASVVKELVENSLDAGATRVDIDIERGGAKLIRIRDNGCGIKKEELALALARHATSKIASLDDLEAIISLGFRGEALASISSVSRLTLTSRTAEQAEAWQAYAEGRDMDVTVKPAAHPVGTTLEVLDLFYNTPARRKFMRTEKTEFNHIDEIIRRIALARFDVTLNLSHNGKLVRQYRAVAKDGQKERRLGAICGTPFLEQALAIEWQHGDLTLRGWVADPNHTTTALTEIQYCYVNGRMMRDRLINHAIRQACEDKLGADQQPAFVLYLEIDPHQVDVNVHPAKHEVRFHQSRLVHDFIYQGVLSVLQQQTETTLPLEDIAPAPRHVPENRIAAGRNHFAVPAEPTAAREPATPRYSGGASGGNGGRQSAGGWPHAQPGYQKQQGEVYRTLLQTPATSPAPEPVAPALDGHSQSFGRVLTIVGGDCALLEHAGTIQLLSLPVAERWLRQAQLTPGQSPVCAQPLLIPLRLKVSADEKVALQKAQSLLGELGIEFQSDAQHVTIRAVPLPLRQQNLQILIPELIGYLAQQTTFATVNIAQWIARNVQSEHPQWSMAQAISLLADVERLCPQLVKAPPGGLLQPVDLHSAMNALKHE", "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": "MLALGKLLELTLAGREPAEKTQLTVEGVRMRWMGEGALEVRPPEARDNGTDLLLSAGIHGNETAPIELLDELIRSIARGDLKPRARILFLFGNPDAMRRGARFVEQDVNRLFNGRHLQSGGAEALRACELERLAASFFSLPERYRLHYDLHTAIRGSTIEQFALYPWKEGRQHSRLELARLRAAGMSAVLLQNKPSIVFSAYTYDQLGAEAFTLELGKARPFGQNQQVNLGPLRVCLEQLIEGTEPERDDDLEGLQLFSVAREVIKRTDAFTFNLADDVENFSPLEKGYVLAEDAGGSRWVVEEEGARIIFPNPRVKNGLRAGILIVPTDADSLG", "text": "FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate. SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily."}
{"protein": "MSHIPANLRYTDSHEWVLDNGDGTVTIGITDHAQEALGDVVFVELPETGRELDAGEEFGVIESVKAASDLYLPLSGEIIAVNESLEDAPETVNDNPYEDGWIIKLKLAEPEALESLLDATAYDALVSAEED", "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": "MRHEELLTKTFQGPAVVCGTPTSHVYMFKNGSGDSGDSSEEESHRVVLRPRGKERHKSGVHQPPQAGAGDVVLLQRELAQEDSLNKLALQYGCKVADIKKVNNFIREQDLYALKSVKIPVRNHGILMETHKELKPLLSPSSETTVTVELPEADRAGAGTGAQAGQLMGFFKGIDQDIERAVQSEIFLHESYCMDTSHQPLLPAPPKTPMDGADCGIQWWNAVFIMLLIGIVLPVFYLVYFKIQASGETPNSLNTTVIPNGSMAMGTVPGQAPRLAVAVPAVTSADSQFSQTTQAGS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MGYYKKYKEEYYTWKKTYYKKYYDNDKKHYDCDKYYDHDKKHYDYDKKYDDHDKKYYDDHDYHYEKKYYDDDDHYYDFVESYKKHH", "text": "SIMILARITY: To B.subtilis spore coat protein C."}
{"protein": "MSKSKEAAASSIILKYLNDQNRPYSTQDVFSNLQRDHGLGKTAVVKTMELLAQKGKIKEKVYGKQKIYFADQEQFPSVSDSELKDLDAQVTELSSKLQSSQQSCRQLESELKDLTSSLTTEEMLKEVSCLKEECDRHEHKLTNIKSATNHVTPAEKEKVYGERKHFCKEWKKRKRMATDIFDAILEGYPKSKKQFFEEVGVETDEDCNVTVPDV", "text": "FUNCTION: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing of homologous chromosomes during meiosis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HOP2 family."}
{"protein": "MKKRFERIFLIVMDSVGIGEAPDAKEFGDEGANTLGSIAEAFNGLHVPELEKLGLGKIAPLKGVKNVPTPLASYGIMQEASLGKDTMTGHWEIMGLHITKPFQVFPDGFPTELLEQLKSETGRGIIGNKVASGTEILDELGEEHVKTGDLIVYTSADSVLQIAAHEEVVPLEELYDICEKARKLTLAPEYMVGRVIARPFVGEPGKWKRTANRHDYALKPFGRTVMNTLEDAGLASIALGKISDIYDGEGVTKAVRTTSNEDGMDKLAEQINTSFEGLCFLNLVDFDALYGHRRDVIGYGEAIMAFDQRLGEILPQLGDEDLLIVTADHGNDPTHTGTDHTREYVPLLVYNKGIKPVNLGKRRTFADIGATVADNFQVERPSNGTSFLTELKPE", "text": "FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of pentose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphopentomutase family."}
{"protein": "AAPGSSPHQVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALHGPPHWGLEYQAPYSSPPGPPCCSGSGGSSPGCSRDCNEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRAYWKPSSSWDYITVDNNLTTNQAVQVCKDNKWCNPLAIQFTNAGRQVTSWITGHYWGLRLYVSGQDPGLTFGIRLKYQNLGPRVPIGPNPVLADQLSFPLPNPLPKPAKSPPVSNSTPTMISPSPTPTQPPPAGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPTNCSVASQHKLTLSEVTGRGLCIGTVPKTHQALCNTTLKTNKGSYYLVAPAGTTWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKR", "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). 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."}
{"protein": "MAQRTWLGDILRPLNSEYGKVAPGWGTTGLMGVFMLLFFVFLLIILQIYNSSLLLEGFKVDWRSLGQ", "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": "MTDKTSLSYKDAGVDIDAGNALVDRIKGVVKKTRRPEVMGGLGGFGALCALPQKYREPVLVSGTDGVGTKLRLAMDLKRHDAIGIDLVAMCVNDLVVQGAEPLFFLDYYATGKLDVDTAASVINGIAEGCLQSGCALVGGETAEMPGMYHGEDYDVAGFCVGVVEKSEIIDGSRVAEGDVLIALGSSGPHSNGYSLVRKIIDVSGCDPQTTLLEGKPLADHLLEPTRIYVKSVLELIENIDVHAIAHLTGGGFWENIPRVLPENTQAVINESSWQWPAIFTWLQTAGNVSRHEMYRTFNCGVGMVIALSAPEADKALALLNEKGENAWKIGIIKASDSEQRVVIE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
{"protein": "MTDLQSIAPRDKAEILAQALPYIRKFHGKTIVIKYGGNAMTDPALQADFAEDVVLLKLVGMNPVVVHGGGPQIETALKRLGKQGHFIQGMRVTDAETMEVVEWVLAGEVQQDIVGLINQAGGKAVGLTGRDGGLIRARKLKMVDKDDPSKEHDIGQVGDIVSIDPSVVKALQDDAFIPVISPLGFGEENESYNINADVVASKLATVLKAEKLMMLTNIPGVLNKSGALIPELTAREIDELVVDGTISGGMLPKIAGAIDAAKSGVNAVHIVDGRVPHAMLLEILTEQAYGTMIRSH", "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": "MATLCTSAINMNPNLTNSLSNSINLSSTPTNLSSLRSTFTNSCSLGLNVAVKSVQISRNKPNVVCMSWDGPLSSVKLILQGRNLEVSDNVRSHVEDKVGKSVAKHSHLVREVDVRLSARGGDLSKGPKLRRCEVTLFTKRHGVIRAEEDAESLYSSIDLVSSIIQRKLRKIKDKVSDHGRHMKGFNRSKVRDPEPVRITREEVLEEVESAPAPVSVEDDDFIEEVVRTKYFDMPPLTITEAVEQLENVDHDFYAFRNEETGDINILYKRKEGGYGLIIPKDGKTEKLESLPVQTDKQPSFAE", "text": "FUNCTION: Ribosome-binding factor involved in light- and temperature- dependent control of protein synthesis. Interacts with 16S sRNA nucleotides at the A-site and P-site, where it protects the decoding center and inhibits translation by preventing tRNA binding. Stabilizes 70S ribosomes against dissociation. May be recycled by the combined action of ribosome-recycling factor (RRF) and EF-G. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family. Long plastid HPF subfamily."}
{"protein": "MLYFESLKDKFALNEKQLNKFVFYYEFLKQENQKMNLTSIISLSDVCYKHFYDSLILKEIFNFNTVTNLCDVDSGAGFPSFPLKILFPHLKIVIIESSLKKINFLKQLSSHLELDNICFFHQRVEQYDIAKNGSYDCVVARALARLELILKWCVPLVKKKGYFIAMKGKNFQQELEASKKIIKQIRVKLVSAKTLELPMQLGTRTNLLFQNE", "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": "MKIAIIGAMEEEVTILRDKIEEREETVIANCEFSTGRLNGADVILLKSGIGKVNAAMSTAILLERFRPDYVINTGSAGGFLSTLNVGDVVISNEVVHHDVDVTAFGYEYGQVPGMPARYKADETLVKIAEQNAKQIKDIQVVTGLIATGDSFMNDPARVEFVRSKFPELCAAEMEAAAIAQVCTQFAVPFVIIRALSDIAGKESNVSFEQFLDTAAKHSADLVLSIVSSLQK", "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": "MSLSVAEKSYLYDSLASTPSIRPDGRLPHQFRPIEIFTDFLPSSNGSSRIIASDGSECIVSIKSKVVDHHVENELLQVDVDIAGQRDDALVVETITSLLNKVLKSGSGVDSSKLQLTKKYSFKIFVDVLVISSHSHPVSLISFAIYSALNSTYLPKLISAFDDLEVEELPTFHDYDMVKLDINPPLVFILAVVGNNMLLDPAANESEVANNGLIISWSNGKITSPIRSVALNDSNVKSFKPHLLKQGLAMVEKYAPDVVRSLENL", "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 cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. 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. RRP42 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the RNase PH family."}
{"protein": "MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKTQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGLREMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC", "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": "MSKNSVIIVAAGKGKRMNSSISKQFLQIKNKPILYYTLSKFSTHESIDEIVLVTLEDKIEVCGDIIDKYNINKVSKIVPGGKERQDSVYNGLKAVSKDCEVVLIHDAARPFVTSDIIENGIRYTNQYGAAACGVIPKDTIKIKNEKGFAIDTPNREDLFIVQTPQCFNYNIILSCHEKLKKHNKKVTDDTMVLENYGKSVYLYEGSYSNIKITTPEDLILGEQILEKLT", "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": "MQQLIDNLKKRGILDNSSAGLESLTVPVSAYLGFDPTAPSLHIGHWIGICFLRRLAAYGITPVALVGGATGMIGDPSGKSVERSLLDQAQVLDNSKKIAAALASYLPGIRIVNNADWLGSLSMVDFLRDVGKHFRLGSMLAKDVVKQRVYSEEGISYTEFSYLLLQSYDFAHLFKEHNVVLQCGGSDQWGNITSGIDYIRRRGLGQAYGLTYPLLTDSKGKKIGKTESGTIWLDPALTPPYELFQYFLRLPDQEISKVMRTLTLLDNEEIFALDERLTSDPQAVKKYIAEVIVKDVHGSEGLAQAQAATESFFASKGKSITEAELVALVESGVGVKVARTDLIGKRWLDIVVELGFCSSRGQARRLIQQRGLYINQEPLADEQSILDGTQLCFDRYVLLSQGKRKKQVIDLN", "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": "MAVKTYKPTSPGRRFVTVSSFEEITKTEPEKSLIVPLKKHAGRNNQGRLTVRHRGGGHKRMYRIIDFKRNKDGIPAKVVAIEYDPNRTARIALLAYADGEKRYIIAPHGLKVGDVLMSGPDADIKVGNALPLANIPVGTLVHNIELYPGKGGQLVRAAGTAAQLLGKEGRYAILRLPSGEMRKVLLECRATIGQVGNLEHENITIGKAGRARWLGIRPTVRGVVMNPVDHPHGGGEGRSPIGRHPVTPWGKPTLGVKTRKKNKASSKLIIKRRK", "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": "MASDHQTQAGKPQSLNPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKIILYENPNFTGKKMEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSN", "text": "FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SIMILARITY: Belongs to the beta/gamma-crystallin family."}
{"protein": "MNFQELILTLDNFWARQNCIIQQPYDVEKGAGTMNPATFLRALGPEPWRVAYVEPSRRPTDGRYGENPNRLQHYYQYQVILKPSPDDVLEVYLDSLKAIGIDPDEHDIRFVEDNWESPTLGAWGLGWEVWLDGMEVTQFTYFQQCGGIDCRPVSAEITYGLERLAMFIQGVDNVFDITWVDGITYGDVHHRGEVEHSHYNFELADTEMLFKLFDMYEREALRVVEKGFVLPAYDYVLKCSHTFNLLDARGAISVTERTGFIGRVRNLARTCAQAYIEQRQAMGYPLLKRKED", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWATAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA", "text": "FUNCTION: AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis (PubMed:11882383, PubMed:21620960, PubMed:21432781, PubMed:26095253, PubMed:26107252, PubMed:32350463). This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported (PubMed:11882383, PubMed:21620960, PubMed:21432781). AKT is responsible of the regulation of glucose uptake by mediating insulin- induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (PubMed:9415393). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (PubMed:11579209). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (PubMed:11994271). AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity (PubMed:22057101). Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (PubMed:22057101). AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating the TORC1 signaling pathway, and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Also regulates the TORC1 signaling pathway by catalyzing phosphorylation of CASTOR1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF- kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1 (By similarity). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (By similarity). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (PubMed:10454575). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (By similarity). The Rho GTPase- activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (PubMed:19778506). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I) (PubMed:11282895, PubMed:18288188). AKT mediates the antiapoptotic effects of IGF-I (PubMed:11282895). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (By similarity). May be involved in the regulation of the placental development (PubMed:12783884). Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro- apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility. Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation. Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation (By similarity). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (By similarity). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (PubMed:32228865). Acts as a negative regulator of the cGAS-STING pathway by mediating phosphorylation of CGAS during mitosis, leading to its inhibition (PubMed:26440888). Acts as an inhibitor of tRNA methylation by mediating phosphorylation of the N-terminus of METTL1, thereby inhibiting METTL1 methyltransferase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1) (By similarity). Nuclear translocation is enhanced by interaction with TCL1A. Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily."}
{"protein": "MQRVSFEVKDTEAEKSSSEILSGSLPSTYRNPAMENVGNAVDDGSSVKNNPKLDMQKQNGLVKWFKKCLTMVSGESKAPRLDRSKSTAGQALKGLKIISKTDGNAAWTVVEKRYLKITANTDGLLLRSKFGECIGMNSKEFALELFDALARKSHLKGDVITETELKKFWEQINDKSFDSRLITFFDLMDKDSDGRLTEDEVREIIKLSSSANHLSCIQNKADEYAAMIMEELDPDHMGYIMMESLKKLLLQAETKSVSTDINSEERKELSDMLTESLKPTRDPNHLRRWYCQLRFFVLDSWQRVWVIALWLTIMAILFAYKYIQYKNRAVYEVLGPCVCLAKGAAETLKLNMALILLPVCRNTITWLRNKTRLGVFVPFDDNLNFHKVIAVGIAIGVAIHSVSHLACDFPLLIAATPAEYMPLGKFFGEEQPKRYLHFVKSTEGITGLVMVFLMVIAFTLAMPWFRRGKLEKKLPGPLKKLASFNAFWYTHHLFVIVYILLVLHGYYIYLNKEWYKKTTWMYLAVPVALYAYERLIRAFRSSIRTVKVLKMAAYPGKVLTLQMSKPTNFKYMSGQYMFVNCPAVSPFEWHPFSITSTPQDDYLSVHIKALGDWTEAIQGVFSEVSKPPPVGDMLNGANSPRFPKIMIDGPYGAPAQDYKKYEVVLLIGLGIGATPMISIIKDIINNTETKEQLSQMEKGSPQEQQGNKETFKTRRAYFYWVTKEQGTFDWFKNIMNEIAERDKSKVIELHNHCTSVYEEGDVRSALIRMLQSLNYAKNGLDIVAGTRVMSHFARPNWKNVYKQIAMDHPGANVGVFYCGAPVLTKELRQLALEFTHKTSTRFSFHKENF", "text": "FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family."}
{"protein": "MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMTRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPTLRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKSHIL", "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": "MAATSLVLTCASPLFSSPRVISATKKLTTELSISTAKFRRRCSGNNDEVLLEGMPPEYYDDEWQARQREKTKELRRMQREEEEEEERKIEEYREIGTRLKEFPEQDLRKARKLVSSFIRAAEEVEERIEEAAEKGELDELVLMIIWNRLDLARRDDEKDAIRSLDLLYRRVETEILKRQASPAMKLLNDLLNMHDGFEDDAWLKDCRKRMAETFPREDPFSILMPPGFDIDMHQGQLRPPIETETDNTLLRVDFVREVDALLQEVRIEEDATTGSKGEGLDPEAIALKFKQQEKQRTIRQIEAILDLALNLKW", "text": "FUNCTION: Required for the differentiation of chloroplast from proplastids or etioplasts, probably by modulating some chloroplast- encoded genes expression and mRNA maturation. Involved in leaf-cells differentiation. SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chromoplast Plastid, etioplast Plastid, amyloplast Note=Present in thin tubular projections emanating from plastids and often connecting organelles each other."}
{"protein": "MDNVLARPADICCLKGSFHSGDATGSTIQIDGIDTYVAKPHPDKSNGNVLLFFPDAFGLHINSFLMMDAFAECGYLTLGVDYFLGDPVTKHSLTPLSDPNFDFESWKNKHLKASEDAAARWVKAVKAQYGSSEDVRFACVGYCWGARFVCQQLSADAPIFFSVPSTDKLFEPEQRSRTIEILTENNKQFNMQVFANVGHGFASRARLTDPYEKWAKEATFKSFVDWFDFWMEKK", "text": "FUNCTION: Dienlactone hydrolase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2- AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N- malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N- malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases and other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable). SIMILARITY: Belongs to the dienelactone hydrolase family."}
{"protein": "MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGSTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "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": "MKKEKPLILLSNDDGVEAKGLNELIRGLRGMGEIIVMAPDGPRSGASGAITSEHPVKYYKVREEEDLTVYKCTGTPVDCVKLALHTVVPRRPDVVIGGINHGDNSSVNVHYSGTMGVVIEGCLKGISSIGYSLCNHFADADFSSSLPYIRRITEQVLEHGLPLGICLNVNFPDTASLKGVRICRQTNGAWINEWKRSLHPRGGEYFWLTGEFDNYEPEAEDSDHWALGHGYVAVTPTQIDVTAYGMMNELKNWNLEV", "text": "FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family."}
{"protein": "MVLHVYNTLTKSKEEFIPLEPGKVKFYVCGVTVYDLSHIGHARSAIVFDVIYRYLRFLGFEVTYVRNFTDVDDKIIRRANDAGTDCRSIAQRYIAAFYEDMDALGVLRPDLEPLATENVPGMIEIIRVLMDKGIAYQAGADVFFEIEKFPGYGKLSGRQIEDMLAGARVEVDARKRNPLDFVLWKGSKPGEPSWDSPWGPGRPGWHIECSAMGSRFLGKTFDIHGGGKDLIFPHHENEIAQSEAAFGMPFVRYWLHNGFVNINNEKMSKSLGNFLTIRDVLQKVHPETVRFFVLSKHYRSPVDFSDETIGEAEKGLERLYGTLGAVKERAAAGVEEAFQEKALRGQDPELFDQIAALSGAFREAMDNDFNTAQALGNLFSLQRHLQRFLDKFGRKQLKGPASALARAGADAIRDHALVLGLLTREPEAFQAEQRSLKIKSTGLTEAEVERCIELRRQARQDKNFAEADRLREEIEKKGIQLEDSPAGTRWRVG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MKQPSALSALVEALRALPGVGPKSAQRMAYHLMQHDREGAEKLGRSLLFATEHLQHCEKCNTFTEAQICEVCSDTERDPTLLCVVETPADQIMLEQTMTWRGLYFVLMGRLSPLDGIGPKEIHFDRLVKRATDGVVKEVVLATNFTNEGEATAHYLGQTLKSRGLSVTRLARGVPVGGELEYVDAGTIARAMLDRRSI", "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": "MRSDGRKEDQLRPVSIQRDFLEYPEGSCLISFGKTKVICTASVIENVPNWLKGKGQGWITAEYSMLPRATQQRTIRESVQGRIGGRTHEIQRMIGRAMRTAVELTKIGERTIWVDCDVIQADGGTRTAAITGAFVAVADAIIKLHKEGIIEETPIKDFVAAVSVGIVNDRILLDLNFEEDSAAQVDMNVVGTGSGRLSEVHTMGEEYSFTKDELIKMLDLAQKGINELIELQKKLYVIQDGKWERSELKEVSSTT", "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": "MPFDSTNADLSVIPVKTPAELKRFIALPARLNAKDPNWITPLFMERTDALTPKTNPFFDHAEVQLFLATRGGRDVGRISAQIDQLTPQPTEGRLDGHFGMIAAEDDPAVFNVLFRAAEDWLRARGRTHAVGPFNLSINEEVGLLVWGFDTPPMVLMGHDPVYAGPRVEEQGYAKAQDLFAYKADETGDIPEIAQRRVKRGLPSGVVLRQLDMSRYDQEVQTLTEILNDAWSDNWGFTPTTEAETRQLAKSLKQVIDQRLVWFSEIDGEAAGVVVFLPNVNEAIADLKGKLLPFGWAKLLWRLKVKGVKSARIPLMGVKKKFQTSQRGRMLPFWMMKASRDMAMSLGYNRYEISWVLEANKAMTHIAENVGGTHYKTYRVYEKAL", "text": "FUNCTION: Involved in de novo bacterial ceramide synthesis (PubMed:33063925, PubMed:34969973). Catalyzes the condensation of 3- oxosphinganine with an acyl-CoA to generate oxidized ceramides (PubMed:34969973). Can use acyl-CoA substrates ranging from C8 to C24, with highest in vitro activity with C14 and very little activity with acyl-CoA thioesters of 18 carbons or longer (PubMed:34969973). May have a preference for monounsaturated acyl-CoA substrates, as it has a threefold greater preference for C16:1-CoA over C16:0-CoA as a substrate in vitro (PubMed:34969973). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGFIYARKLLLCMAVSIYAIGSTTTTETTTSSSSTSGSGQSTSSGTTNSSSSPTTSPPTTSSSPPTSTHTSSPSTANAQKHAGHHRGRAGGRRGSPQGGSHTTPHPDRLTPSPDDTYDDDTNHPNGRNNSIEIVPQLPPDRPIIELGVATLRKNFMEASCTVETNSDLAIFWKIGKPSVDAFNRGTTHTRLMRNGVPVYALVSTLRVPWLNVIPLTKITCAACPTNLVAGDGVDLNSCTTKSTTIPCPGQQRTHIFFSAKGDRAVCITSELVSQPTITWSVGSDRLRNDGFSQTWYGIQPGVCGILRSEVRIHRTTWRFGSTSKDYLCEVSASDSKTSDYKVLPNAHSTSNFALVAATTLTVTILCLLCCLYCMLTRPRASVY", "text": "FUNCTION: The glycoprotein gp2 from the avirulent strain Kentucky A (KyA) is probably non functional since this strain harbors an in-frame deletion of 1,242 nucleotides in gene 71. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein."}
{"protein": "MHELSIAQSLLALIEDEMAKHGKEKLITVKVRHGRLSSVVPEALSMAFEVMTADSRLAGAALVMEETPVLLRCRDCSREFTPDPPTAAFAPCPGCGQELGHTVVSGRELYIEYLELE", "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": "MSDTMQLDSIWHNGKQYRKGYTTGSCATAAAKVAALMVLRQQVIDHVSIVTPSGVTLRLNVEQPLIEGQQATAAIRKDGGDDVDATHGMLIFARVTLCDHGEIHLRGGEGVGTVTRKGVGLPVGSSAINRTPRQTIEAAVREAIGPLRGAEVEIFAPEGEERAKKTYNGRLGILGGISIIGTTGIVTPMSEESWKRSLAIELEMKRSAGAEKVILVPGNHGERFVREQLGLDGQLVVTMSNFVGYMLQEAVRLGFRHIMLVGHPGKLVKVAAGIFHTHSHIADGRMETLIAYLALMGASQELLLEVSHCDTTEAAMELIAEHGLQAVYDRIAERICERMSEMLRFAVNPPRCDAIMFSFDNQILGTSRPLNDILEAMR", "text": "FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. SIMILARITY: Belongs to the CbiD family."}
{"protein": "MDVTRLLLATLLVFLCFFTANSHLPPEEKLRDDRSLRSNSSVNLLDFPSVSIVALNKKSKQIGRKEAEKKRSSKKEASMKKVARPRTPLSAPCVATRNSCKPPAPACCDPCASCQCRFFRSACSCRVLSLNC", "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": "MSKIAKTAIISPKAEINKGVEIGEFCVIGDGVKLDEGVKLHNNVTLQGHTFIGKNTEIFPFAVLGTQPQDLKYKGEYSELIVGEDNLIREFCMINPGTEGGIKKTLIGDKNLLMAYVHVAHDCVIGSHCILANGVTLAGHIEIGDYVNIGGLTAIHQFVRIAKGCMIAGKSALGKDVPPYCTVEGNRAFIRGLNRHRMRQLLESKDIDFIYALYKRLFRPIPSLRESAKLELEEHANNPFVKEICSFILASSRGVAYKSSEYSSEEKQEE", "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": "MARSPRIRIKDNDKAEYARLVKNTKAKIARTKKKYGVDLTAEIDIPDLDSFETRAQFNKWKEQASSFTNRANMRYQFEKNAYGVVASKAKIAEIERNTKEVQRLVDEKIKAMKDKEYYAGGKPQGTIEQRIAMTSPAHVTGINRPHDFDFSKVRSYSRLRTLEESMEMRTDPQYYEKKMIQLQLNFIKSVEGSFNSFDAADELIEELKKIPPDDFYELFLRISEISFEEFDSEGNTVENVEGNVYKILSYLEQYRRGDFDLSLKGF", "text": "FUNCTION: Acts as a primer for DNA elongation during viral genomic replication (PubMed:6813861). Acts as the small terminase protein during packaging (PubMed:18674782). Recruits the phage DNA polymerase to the bacterial nucleoid (PubMed:20823229). 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) (PubMed:6813861). 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 (PubMed:22210885, PubMed:25081208). 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 (PubMed:19011105). FUNCTION: Hydrolyzes host peptidoglycans during virus entry. SUBCELLULAR LOCATION: Virion Host nucleus Note=Associates with the host bacterial nucleoid through its N-terminal region. SIMILARITY: Belongs to the phi29likevirus DNA terminal protein family."}
{"protein": "MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGKTGRASDQRDLTEHKPSVSNHTQDHSNDPPNKMNEVTYSTLNFEAQQPTQPTSASPSLTATEIIYSEVKKQ", "text": "FUNCTION: [Isoform 8]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Promotes populations of T cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (By similarity). FUNCTION: [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils (PubMed:18424730, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR- mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Also inhibits T cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T cell through its interaction with HAVCR2 (PubMed:25363763). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome. Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by down-regulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (By similarity). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia. Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1- MAPK1/ERK2 pathway (By similarity). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (By similarity). Inhibits cell migration and cell scattering through interaction with FLNA; interfers with the interaction of FLNA with RALA (PubMed:16291724). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (By similarity). SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 4]: Secreted. SUBCELLULAR LOCATION: Cell projection, microvillus membrane; Single-pass type I membrane protein Apical cell membrane; Single-pass type I membrane protein Note=Localized to the apical glycocalyx surface (PubMed:10436421). Colocalizes with CEACAM20 at the apical brush border of intestinal cells. SUBCELLULAR LOCATION: [Isoform 8]: Cell membrane; Single-pass type I membrane protein Cytoplasmic vesicle, secretory vesicle membrane Lateral cell membrane Apical cell membrane Basal cell membrane Cell junction Cell junction, adherens junction Note=Predominantly localized to the lateral cell membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions (By similarity). Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (PubMed:14522961). SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein Lateral cell membrane Apical cell membrane Basal cell membrane Cell junction Cell junction, adherens junction Note=Canalicular domain of hepatocyte plasma membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions. Found as dimer in the solution. Predominantly localized to the lateral cell membranes. SUBCELLULAR LOCATION: [Isoform 3]: Secreted. SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family."}
{"protein": "MSGTVVAVPPRVARALDLLNFSLADVRDGLGPYLSIYLLLIHDWDQASIGFVMAVGGIAAIVAQTPIGALVDRTTAKRALVVAGAVLVTAAAVAMPLFAGLYSISVLQAVTGIASSVFAPALAAITLGAVGPQFFARRIGRNEAFNHAGNASAAGATGALAYFFGPVVVFWVLAGMALISVLATLRIPPDAVDHDLARGMDHAPGEPHPQPSRFTVLAHNRELVIFGAAVVAFHFANAAMLPLVGELLALHNRDEGTALMSSCIVAAQVVMVPVAYVVGTRADAWGRKPIFLVGFAVLTARGFLYTLSDNSYWLVGVQLLDGIGAGIFGALFPLVVQDVTHGTGHFNISLGAVTTATGIGAALSNLVAGWIVVVAGYDAAFMSLGALAGAGFLLYLVAMPETVDSDVRVRSRPTLGGK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MSYYFKNLKPGYESDEELEDDEILKTLSKRYADEDESASDDELSSLSFDALRRAERQLEEESRKEKAGSQNESKPALKNAKRSKEKELELADSFKAKSYTEESFGENSDSSSENEGLFEEEEVVRGNKNSKADHGKNRKKSHAPSEQSSKKKVSRIRKIPGLETPKSMNENLYQDIRFDKSLGKAEDYESIRKRYQFLDEYRQKEISELSRLLSDRKFVNKISERERDEMQEKLTSMRSKLQTLKNRDLDRKILKDYETEINKGNKTKYHLKESEKRKVIQKYKFDHMKAKQREKVMDRKRKKRLGKEFKQFSFHNR", "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": "MRVTNRSLKGREGEIAVTAETLDDLWHLKYIIEKGDMVFALTRRKADSASDKLRPEKVEKVKVRLGIRVEELEFHKFANRLRIHGPIEHGMDTGSYHTLNVEIGTNISIIKEHWKNDQLQRIQDAEEAGKRPKVVIVAVEEGDADIGFVRHYGIEVYSHIRQSSGKRETGLRNEFFREIVEQLRHAVPEDASIVIAGPGFTKEDFLKYFNETESEMASKALTEDTSMIGMSGFQEVLRRGAVDRIMQESRIARESSLMEDLIREISMDGKAAYGFADVKNALGYGAVETLLIADETLREGREKGEDIDKLLMEVEQAQGKVVVFSTAFEPGEKLHKLGGIAALLRFKVTG", "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": "MRTTFMAKATDVERKWLLIDAEGKTLGRLSSEVASLLRGKHKPTFTPHVDCGDHVILINVEKIVLTGNKLDKKVYYRHSGHPGGLKQTVARDLLANKPERMLELAIKGMLPKGSLGRQMFNKLHVYAGDTHKQEAQQPEVYELRG", "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": "MTIILKPGSVPLETLEKIYREGLPVRIDPAFHAGIEKAAARIAEIAAGDAPVYGINTGFGKLASIRIAAGDVATLQRNLILSHCCGVGEPLSENIVRLIMALKLVSLGRGASGVRLEVITLIEAMLEKGVIPMIPEKGSVGASGDLAPLAHMTAAMIGEGEAFYRGERLSGAKALGKAGLKPVVLAAKEGLALINGTQTSTALALAGLFRAHRAARTALITGALSTDAAMGSDAPFHEEIHQLRGHKGQIDAGRALRTLLEGSAIRRSHLEGDQRVQDPYCIRCQPQVDGACLDILRQAARTLEIEANAVTDNPLVLSDGRAVSGGNFHAEPVAFAADQIALAVCEIGAISQRRIALLVDPSLSFGLPAFLARKPGLNSGLMIAEVTSAALMSENKQMAHPASVDSTPTSANQEDHVSMACHGARRLLQMTANLNAIIGIEALTGALGVELRKPLTTSAELAKVIAALRAKVATLEEDRYMADDLKAAAELVADGTLSGVISAGILPDLEA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAL/histidase family."}
{"protein": "MSDSSSSSTSAFVSSLVFNFAIFCAFIGLFLCLRPREKHVYQPRCIIDTQPKEEKPEPSPSSPFGLFAYVVKRSETYLIQYAGVDGYFFIRYLFTFGALCILGCLVLFPILLPVNATNGVGEKGFDILSFSNVKNHNRFYAHVFLSWLFFGFTIFIIYRELRYYVIFRHAMQSSGLYNNLPSSSTMLLTELPNSVLNDEETLHELFPNASEFTCVRDLKKLEKKVKKRSDLGNKYESTLNSLINKSVKKHNKLVKKHKPLPSTLDYTAYVKKRPTHRLKFLIGKKVDTIDYCRDTIAELDEVVDKLQTSLEERKKVGSVFIRFRSQTDLQTAYQAFLYSKKFRKYRFGRALVGIAPEDIVWSNLDLSMYTRRGKKTISNTILTLMIIFWAFPVAVVGCISNVNYLIEKVHFLKFIDHMPPKLLGIITGILPSVALSILMSLVPPFIKFLGKFGGALTVQEIENYCQNWYYAFQVVQVFLVTTMTSAATSAVVQVIKEPASSMTLLASNLPKASNFYISYFLLQGLSIPGGALLQIVTLLLSKVLGRIFDNTPRKKWNRWNQLSAPSWGTVYPVYSLLVTIMICYSIIAPIIIGFAAVAFVLIYFAYSYNLIYVLGHNADAKGRNYPRALFQVFVGLYLAEVCLIGLFVLAKNWGATVLEAVFLGFTVACHLYFKYKFLPLMDAVPISAIESVSERPEIKYPMDLGTSEMKNVGRAYPEILEKLSSSSGSDEFLETSSRTSENTKEKIDKDDEGFAITNISSVHKMPSFVLSYFSDLAASNRILTGFDRVLQLLPSFYDIPVRVRNVQYVSPALKATPPSVWIPKDPLGLSTYAIEDARGKVDIFDDNTTFNEKGNLQYTGPPPDYDEAIRS", "text": "FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family."}
{"protein": "MMSAPKITFIGAGSTIFVKNILGDVFHREALKTAHIALMDIDPTRLEESHIVVRKLMDSAGASGKITCHTQQKEALEDADFVVVAFQIGGYEPCTVTDFEVCKRHGLEQTIADTLGPGGIMRALRTIPHLWQICEDMTEVCPDATMLNYVNPMAMNTWAMYARYPHIKQVGLCHSVQGTAEELARDLNIDPATLRYRCAGINHMAFYLELERKTADGSYVNLYPELLAAYEAGQAPKPNIHGNTRCQNIVRYEMFKKLGYFVTESSEHFAEYTPWFIKPGREDLIERYKVPLDEYPKRCVEQLANWHKELEEYKKASRIDIKPSREYASTIMNAIWTGEPSVIYGNVRNDGLIDNLPQGCCVEVACLVDANGIQPTKVGTLPSHLAALMQTNINVQTLLTEAILTENRDRVYHAAMMDPHTAAVLGIDEIYALVDDLIAAHGDWLPGWLHR", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 4 family."}
{"protein": "MARTQVPDPATSAPAERALWLRDELERANYAYYVLDQPDLPDAEYDRLFKELQQIESEHPDLITPDSPTQRVGGEVASGFRPVVHDMPMLSLNNGFSDEDIAAFDKRVSDTLHHTPVDYACELKFDGLAISLRYVDGQFTQAATRGDGATGEDVTENVRTIRSIPLKLKGKRVPKLVDVRGEVLMFRRDFDKLNQRQRDAGQREFANPRNAAAGSLRQLDPKMTAQRPLSFFAYGIGVLDGIEMPGTHSELLDWYHEMGLPVNSERAVVQGAEGVLGFFHKVGEKRDKLPYDIDGVVYKVNRRDEQDALGFVSRAPRFALAHKFPAQEALTKLIAIDVQVGRTGAITPVARLEPVFVGGATVTNATLHNEDEVRRKDIRIGDTVIVRRAGDVIPEVVGALLERRPPDAREFVMPTQCPVCGSAIERLPDEAIARCSGGLFCPAQRKQALWHFAQRRALDIDGLGEKIIDQLVELNLVRTPADLFNLGFATLAELDRFAEKSAQNLIDSLEKAKHTTLARFIYALGIRHVGESTAKDLARHFGSLDPIMSATVEELLEVNDVGPIVAEAIHQFFAEEHNRTVIEQLRAPGKVTWAEGPPAPKAPQGVLAGKTVVLTGTLPNMGRDEAKELLEAAGAKVAGSVSKKTDYVVAGAEAGSKLAKAEELGIPVLDEDGMRKLLEGQTT", "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": "MDSLRDVKPIKLIFSIFCLVIILSACNSTAELPRFVQPPEPDGSLSFLVVGDWGRRGSYNQSQVALQMGKIGKDLNIDFLISTGDNFYDDGIISPYDSQFQDSFTNIYTATSLQKPWYNVLGNHDYRGNVYAQLSPILRDLDCRWICLRSYVVNAEIVDIFFVDTTPFVDRYFDEPKDHVYDWRGVLPRNKYLNSLLTDVDVALQESMAKWKIVVGHHTIKSAGHHGNTIELEKQLLPILEANEVDLYINGHDHCLEHISSINSGIQFMTSGGGSKAWKGDVNDWNPQEMRFYYDGQGFMSVYTSEAELRVVFYDGLGHVLHRWSTLKNGVYSDI", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family."}
{"protein": "MAEALPPRSPPDDVDIDPDFGPQSRPRSCTWPLQRLDSQGSPGKPNSGAGEAADTSSMIPEEEDDDYEGAASTATVLGTAGDKGTLVLLSGGESGQLAVLASPVGGVETLQVSLGGEGAGGAVSGAGGQQQQRKCSSRRNAWGNMSYADLITRAIESTQDKRLTLSQIYDWMVRSVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFIRVQNEGSGKSSWWMINPEGGKGGKAPRRRAVSMDNSNKYTKSRGRAAKKKASLQASSDATDDSPSQLSKWPGSPTSRSSDKLDTWTDFRSRTNSNASTISGRLSPIPATTELDDVQDDDSPLSPMLYNSPGSLSPSISKPCTVEMPRITDMAETMNLNDGLPENLMDDLLDDISLTSSQQSSPGVLMQRSSSFTYGTKGSGIGSPSNNFNNTGSFNFPLTSLRQSPMQTIQENKQATFSSMNHYSNQSLQDLLNTDTLSHSDVLMTQSDPLMSQASTAVTAQNSRRNIILRNDPMMSFAAQPNQGGNLVNQNSLHQQQSLNSFQGGSRALSNNLSNTGLNDSSILESTKHQQQSSVSHSMQTISDTLSGSLYSSGVTLPTLGHEKFPTDLDLDIFNGSLECDMETIIRNDLMDADGLDFNFDTLISAQNVSLSVGSFTGAKQTSSQSWVPG", "text": "FUNCTION: Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy. Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (By similarity). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of sox9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Retention in the cytoplasm contributes to its inactivation (By similarity). Translocates to the nucleus upon oxidative stress and in the absence of survival factors (By similarity)."}
{"protein": "MAGSLSEIKAKIISTEKTSKITSAMRMVSSAKLVKSEQAARDFQIYASKIRQITTDLLKSDLTTGSDNPMLVSRPVKKTGYIVITSDKGLVGGYNSKILKSIMDMIQEYHAAGDYEIISIGSIGSDFFKARGMNVAFELRGLADQPSFDQVGRIISQSVGMFVNEIFDELYVCYNHHVNSLTSQVRVQRMLPISDLVAEEAAEEGVTGFELEPNRHVILEQLLPQFTESLIYGAIIDAKTAEHAAGMTAMQTATDNAKHVINDLTIQYNRARQAAITQEITEIVAGANALE", "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": "MSVLQEIIDGVREDLEPRRRDLPEARLAELVAAAPAPRDAHAALHGGRTDPAGIRVISEVKRASPSKGALAEIPEPATLARAYERGGASAVSVLTEARRFGGSLADLDAVRAAVDLPVLRKDFTVTEYQIHEARAHGADLVLLIVAALDDAELAGFLQLTESLGMHALVEAHTPEEIERGVAAGARILGVNVRNLKTLDVDPARYAALADGLPEDVVRVAESGVESEAQIKAYAAAGADVVLVGEALVRHGAPEEALRAFRAASLTVR", "text": "SIMILARITY: Belongs to the TrpC family."}
{"protein": "MSDENKSTPIVKASDITDKLKEDILTISKDALDKYQLERDIAGTVKKQLDVKYGNTWHVIVGKNFGSYVTHEKGHFVYFYIGPLAFLVFKTA", "text": "FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 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 changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex where it may contribute to the stable association of the Nup82 subcomplex with the NPC (PubMed:17546040, PubMed:23223634, PubMed:25646085). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus, nuclear pore complex. SIMILARITY: Belongs to the dynein light chain family."}
{"protein": "MRVVLLGPPGAGKGTQAVLLSEKLGVPHISTGDLFRANISQQTPLGREAQKYMDAGDLVPSDVTNRMVEARVNEPDAANGFVLDGYPRTVDQADALEKILGDMNSKLDAVLCFVVPEDTVVERMLARGRNDDTEDVIRNRMRVYREETEPLLDHYDGLVVTVDGVGEVDEVNERALRALGR", "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": "MAETNSPRYSRILLKLSGEALSGNKDMGIDAQVLDQMSLSIAHLVGLGVQVGIVVGGGNLYRGSQLQKDGLVGRVTGDQMGMLATVMNGLAMRDALVRRNIKTRLMSALSIGTVVEPYSSRDAIRYLSQGEVCVFVAGTGNPFFTTDTAACLRGIEIEANLILKATKVDGVYNKDPSKYDDAVKYDNLTFDQVLDEKLGVMDLTAICLCRDHNVPLQVFDMNKPGALLSVIMGEKEGTHVTK", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MNAKKQSRIRRARRARAKMKELGVSRLCVNRTPRHIYAQVISAEGDRVVASASTLDKDLRSGSTGNRDAASAVGKLIAERAKAAGVSTVAFDRSGFKYHGRVKALADAAREGGLEF", "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": "MYQLLSVASVPLLASLVHGYADPGACSGVCTTHDPGLIRRESDGTYFLFSTGNKISYVSASSIEGPWTSVGSMLPDGSSIDLDGNDDLWAPDVSYVDGLYYVYYAVSTFGSQDSAIGLATSETMEYGSWTDHGSTGIASSSAKIYNAIDPNLIYADGTYYINFGSFWDDIYQVPMKSTPTAAASSSYNLAYDPSGTHAEEGSYMFQYGDYYYLFYSAGICCGYDTSMPASGEEYHIKVCRSTSPTGDFVDSDGTACTDGGGTMVLESHGEVYGPGGQGVYDDPNLGPVLYYHYMNTTIGYADSDAQFGWNTIDFSSGWPVV", "text": "FUNCTION: Its preferred substrate is linear 1,5-alpha-L-arabinan. The enzyme activity is progressively reduced as 1,5-alpha-chains become shorter or more highly substituted. SIMILARITY: Belongs to the glycosyl hydrolase 43 family."}
{"protein": "MALLPSLLTALVVYELWPCGALGCDLPQNHILVSRKNFVLLGQMSRISSAICLKDRKDFRFPQDMADGRQFPEAQAASVLHEMLQQIFSLFHTERSSAAWNTTLLDELCTGLLRQLEDLDTCLEQEMGEEESALGTVRPTLAVKRYFRGIHLYLKEKKYSDCAWEIVRMEIMRSFSSSANLQGRLRMKDGDLGSP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha/beta interferon family."}
{"protein": "MFEINPVKNRIQDLTERSDVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKERSSLEAIVDTLDQMSQGLEDVAGLLELAVEAEDEETFNEAVAELDGLEEKLAQLEFRRMFSGEYDSADCYLDIQAGSGGTEAQDWASMLMRMYLRWAEARGFKTEIIEESEGEVAGIKSVTIKIIGDYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIEINPADLRIDVYRASGAGGQHVNRTESAVRITHIPTGLVTQCQNDRSQHKNKDQAMKQMKAKLYELEMQKKNAEKQAMEDNKSDIGWGSQIRSYVLDDSRIKDLRTGVETRNTQAVLDGSLDQFIEASLKAGL", "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": "MTSVLDVTNRDRLIESESLAARTLQERLRLVEEVLVDVLAAESGQELVDLLRRLGALSSPEGHVLHAPEGELLKVIESLELNEAIRAARAFNLYFQIINIVEQHYEQQYNRERAAQEGLRRRSVMSEPISGVSGEGFPLPHTAANATDVRSGPSERLEHSLYEAIPATQQYGSFAWLFPRLQMLNVPPRHIQKLLDQLDIKLVFTAHPTEIVRQTIRDKQRRVARLLEQLDVLEGASPHLTDWNAQTLRAQLMEEIRLWWRTDELHQFKPEVLDEVEYTLHYFKEVIFAVIPKLYRRLEQSLHETFPALQPPRHRFCRFGSWVGGDRDGNPYVKPEVTWQTACYQRNLVLEEYIKSVERLINLLSLSLHWCDVLPDLLDSLEQDQRQLPSIYEQYAVRYRQEPYRLKLAYVLKRLQNTRDRNRALQTYCIRRNEAEELNNGQFYRHGEEFLAELLLIQRNLKETGLACRELDDLICQVEVFGFNLAALDIRQESTCHAEALNEITAYLGILPCPYTELSEAERTRWLLSELSTRRPLIPGELPFSDRTNEIIETFRMVRQLQQEFGTDLCNTYIISMSHEVSDLLEVLLFAKEAGLFDPATGASTLQAIPLFETVEDLKHAPAVLTQLFSLPFCRSYLGSNSTPFLQEVMLGYSDSNKDSGFLSSNWEIYKAQQQLQKIAESFGFQLRIFHGRGGSVGRGGGPAYAAILAQPAQTIKGRIKITEQGEVLASKYSLPELALFNLETVATAVIQASLLRSSIDEIEPWHEIMEELATRSRQCYRHLIYEQPEFIEFFNEVTPIQEISQLQISSRPTRRGGKKTLESLRAIPWVFSWTQTRFLLPAWYGVGTALKEFLEEKPAEHLSLLRYFYYKWPFFRMVISKVEMTLAKVDLEIARYYVQELSQPQNREAFCRLYDQIAQEYRLTTELVLTITGHERLLDGDPALQRSVQLRNRTIVPLGFLQVSLLKRLRQHNSQTTSGAILRSRYGRGELLRGALLTINGIAAGMRNTG", "text": "FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SIMILARITY: Belongs to the PEPCase type 1 family."}
{"protein": "MTPTSHVTLVSSDGKSFEVPRERAMLSPTLAKMLDSSFAEAKEAKVTLPTIESSMLAKVVEYLEYLEEYKHKDDGEDIPQFEVPPEISLELLLAADYLQI", "text": "FUNCTION: As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; plays a role in global genomic repair. Prevents degradation of interacting proteins by the proteasome. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SKP1 family."}
{"protein": "MSQPPIGGAAPATAAASPAAAATEARLHPEGSSRKQQRAQSPARPRDSSLRQTIAATRSPVGAGTKLNSVRQQQLQQQQQQGNKTGSRTGPPASIRGGGGGAEKATPLAPKGAAPGAVQPVAGAEAAPAATLAALGGRRPGPPEEPPRELESVPSKLGEPPPLGEGGGGGGEGGGAGGGSGEREGGAPQPPPPRGWRGKGVRAQQRGGSGGEGASPSPSSSSAGKTPGTGSRNSGSGVAGGGSGGGGSYWKEGCLQSELIQFHLKKERAAAAAAAAQMHAKNGGGSSSRSSPVSGPPAVCETLAVASASPMAAAAEGPQQSAEGSASGGGMQAAAPPSSQPHPQQLQEQEEMQEEMEKLREENETLKNEIDELRTEMDEMRDTFFEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKELSLKRRGSKDLPKSEKKAQQTPTEEDNEDLKCQLQFVKEEAALMRKKMAKIDKEKDRFEHELQKYRSFYGDLDSPLPKGEAGGPPSTREAELKLRLRLVEEEANILGRKIVELEVENRGLKAELDDLRGDDFNGSANPLMREQSESLSELRQHLQLVEDETELLRRNVADLEEQNKRITAELNKYKYKSGGHDSARHHDNAKTEALQEELKAARLQINELSGKVMQLQYENRVLMSNMQRYDLASHLGIRGSPRDSDAESDAGKKESDDDSRPPHRKREGPIGGESDSEEVRNIRCLTPTRSFYPAPGPWPKSFSDRQQMKDIRSEAERLGKTIDRLIADTSTIITEARIYVANGDLFGLMDEEDDGSRIREHELLYRINAQMKAFRKELQTFIDRLEVPKSADDRGAEEPISVSQMFQPIILLILILVLFSSLSYTTIFKLVFLFTLFFVL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SOGA family."}
{"protein": "MMSHQQVQMDLILMQGIWHSVLNMQNQSILLQLGSSSSMPQRPRLLSRVSQRGRQILNLESGRWRLSIIIFLETGTIQLTATILPSTDCQDI", "text": "FUNCTION: Inhibits host transcriptional machinery, by producing modifications to the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Inhibits phosphorylation at serine 2 in the heptapeptide repeat (YSPTSPS) of the CTD of RNA polymerase II, suggesting that the elongation step of transcription and/or 3'-end processing is prevented. Inhibition of host transcription machinery leads to shut off of host cell protein synthesis and inhibition of the host innate immune response. NSs also seems to be involved in the nuclear relocalization of host PABP1 (By similarity). SIMILARITY: Belongs to the orthobunyavirus NS-S protein family."}
{"protein": "MEEFQRYLELDRSQQHYFLYPLIFQEYIYALAHNHGLTRSILLENSGYDNKSSLLIVKRLITRLYQQNHLIVSANDSNQNQFFGCNKNLYYQMISEGFAVILEIPFSIQLMSSLERKGIVKSHNLRSIHSIFPFLEDPFSHLNSALDILIPYPVHLEILVQTLRYRVKDVSSLHLLRLFLYEDPNSNNLITPKKAGSSFSKTNQRFFFFLYNSHVCEYESIFVFLRNQSSHLRSTSFGDLLERIYFYGKIEYLVEVLAKAFQANLWLFKDPFMHYVRYQGKSILASKGTSFLMNKWKYYFVNFWQCYFYLWSKPGRVYINQLSNHSLDLLGYLSSVRLNPSMVRSQMLEKAFIIDNAMKKFDAIVPIIPLIGSLAKAKFCNVLGHPISKAFWTDLSDSDIIDRFGRICRSLSHYHSGSSQKKSLYRIKYILRLSCARTLARKHKSTVRAFLKRLGSELLQEFFTSEEQILSLTFPRVSYTSRRLYRRRIWYLDIICINDFANHE", "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": "MAKRDYYEILGVQKGADDKEIKRAYKRLAMKYHPDRTKGDKESEEKFKEINEAYEVLADKEKRAMYDQYGHAAFEQGGGAGGFGGFSGADFGDIFGDMFGDIFGGGRSRQRVVRGEDLRYDIEISLEEAVKSCKKDIQINTLVHCGTCHGSGAEAGSKIESCPTCHGAGRVRRQQSFFVTEQTCPHCHGTGKKIEKPCHTCHGEGRVHKTQNLTVTIPMGVDTGNQLRLAGKGAAGENGAPAGDLYVVIHVKKHHIFERDGNNLYCEVPISFTMAALGGEVEIPTLDGRLKVKIPAETQTGKLLRLRGKGITSRGYAGDLICEIVIETPIKLNEEQKELLRKLEESLEGKTLQRPKSSGFLDGVKKFFDNLGK", "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": "MLTKKQLDLLEFIHKRVQRDGVPPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPETLGGAARGGFTPRVIEGDKPDAPLPAGAQAVSSADAVALPLVGRIAAGLPIEAINQNSASVAVPGQMLSGKGDHYALEVKGDSMIDAGINDGDVVVIRETSVADNGDIVVALIEDHEATLKRYMRKGSSIALEAANPAYETRVFTEDKVKVQGKLVGLIRTY", "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": "MKRQNQSCVVEFILLGFSNFPELQVQLFGVFLVIYVVTLMGNAIITVIISLNQSLHVPMYLFLLNLSVVEVSFSAVITPEMLVVLSTEKTMISFVGCFAQMYFILLFGGTECFLLGAMAYDRFAAICHPLNYPVIMNRGVFMKLVIFSWISGIMVATVQTTWVFSFPFCGPNEINHLFCETPPVLELVCADTFLFEIYAFTGTILIVMVPFLLILLSYIRVLFAILKMPSTTGRQKAFSTCASHLTSVTLFYGTANMTYLQPKSGYSPETKKLISLAYTLLTPLLNPLIYSLRNSEMKRTLIKLWRRKVILHTF", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MQVLPACQSSALKTLCPSPEAFRKLGWLPTSDEVYNEFIDDLTGRTCNEKYSSQVTLLKPIQDFKTFIENDPIVYQEFISMFEGIEQSPTNYHELCNMFNDIFRKAPLYGDLGPPVYMIMARIMNTQAGFSAFTKESLNFHFKKLFDTWGLFLSSKNSRNVLVADQFDDKHYGWFSERAKTAMMINYPGRTFEKVFICDEHVPYHGFTSYDDFFNRRFRDKDTDRPVVGGVTDTTLIGAACESLSYNVSHNVQSLDTLVIKGEAYSLKHLLHNDPFTPQFEHGSIIQGFLNVTAYHRWHSPVNGTIVKIVNVPGTYFAQAPYTIGSPIPDNDRDPPPYLKSLVYFSNIAARQIMFIEADNKDIGLIFLVFIGMTEISTCEATVCEGQHVNRGDDLGMFHFGGSSFALGLRKDSKAKILEKFAKPGTVIRINELVASVRK", "text": "FUNCTION: L-tryptophan decarboxylase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine- derived natural product (PubMed:28763571, PubMed:30283667). The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD. PsiD does not decarboxylate phenylalanine, tyrosine, or 5-hydroxy- L -tryptophan (5-HTP) (PubMed:30283667). 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well. The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O- phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin. The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin. 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 (By similarity). SIMILARITY: Belongs to the phosphatidylserine decarboxylase family."}
{"protein": "MFKEFKTFIMRGNVLDMAVGIIIGAAFGKIVTSFVTDVLTPVLSLGMGKVDFSNLFFVLNGDSYPTLDAAKAAGVATLNYGTFLNVVLDFVIVAFSIFLIIKAANKLKRAEEPAPVTTKECPECCSSIPMKARKCAHCGSAVAS", "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": "MGGEEESDKPKVSPSPLPFRRWKGSWPTAERGRQRRSRGFRAPSRRPSQPRRSDDGGTDVAAPSRRPLPVRRGAGQAARGRAAQSREPREAGATPWMQSPRFSPPPPRAEPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGISFPLGGPAVAGASLYGASSPFQRAGLPVAPVGLYTAHVGYSMYHLT", "text": "FUNCTION: Probable morphogenetic role. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Msh homeobox family."}
{"protein": "MKPQKSLRARAMDILSRQELSRIGLKRKLAPHAESEEELENVLNEFAERNWQSDLRYAEAYIRSKSRKHGSLRLKQALAQQGIDEETSRNLLPDRSSEKLAAIAVLRKKFKHPAADLKEKQKQARFLAYRGFDADTVQTALKHAWDDGWEEDC", "text": "FUNCTION: Modulates RecA activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecX family."}
{"protein": "MNWEIVIGLETHTQLSTDSKIFSGSSTRFGAAPNTQANAVDLALPGSLPVMNRGAAERAILFGLAVGGKVAPRSVFARKNYFYPDLPKGYQISQYELPVVEGGTLSFFVGEEEKTVNLTRAHLEEDAGKSLHDEFSLASGAPASGIDLNRAGTPLLEIVTEPEMRSAAEAVAYARALHSLVVWLGICDGNMQEGSFRCDANVSVRPVGQKEFGTRTEIKNVNSFRFLERAILFEARRQIELIEDGGTVVQETRLYDADRDETRSMRSKEDAHDYRYFPDPDLPPLVIGQDWVDAVRAGMPELPAAQRARFEADYGLPAYDAAQLTVSRAMADYFEAVARALPAGQAKLAANWIMGEVAATLNREEKDIDAAPVSAAALAALINRIIDGTISNKIARDVFAAMWAGENGGDADAIIAARGLKQISDSGAIGAMIDEVLAANPAIVEEYRAGKQKAFNSLVGQIMKAAKGKANPQQVNELLKEKLG", "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": "MSNTLKKDETFKGLDLNKNQKEEKPAKLPALSKRADVIKVSDFNFFYKGKKQALFNINMEIKENSITTFIGPSGCGKSTLLRSINRMNDLISGSSVEGSIEVFNEEIYKQGTDVSKLRTEVGMVFQKANPFPLSIYENVVYGPKTQGVKSKKILDQICEDSLRKAALWEEVKDKLETPALGLSGGQQQRLCIARAIAMHPKILLMDEPTSALDPIATLKVEELVLELKKEYTIVMVTHSLQQATRISDMTAYFLKGELIEYNTTKKIFINPKDSRTEDYISGRYGD", "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": "MSAISPFVAIRRDLHQIPELGFQEFKTQQYLLRYIQSLPQERLQVRTWKTGIFVKVNGTSPRKTIGYRADMDGLPIREETGLPYRSKHEGRMHACGHDVHMSIALGVLTHFAHHPLKDDLLFVFQPAEEGPGGAKPMLESDIMREWKPDIIVALHIAPEYPVGTIATKEGLLFANTSELFIDLKGKGGHAAFPHLANDMVVAACALVTQLQSIVARNVDPLDSAVITIGKIAGGTVQNVIAEHARLEGTIRTLSTAAMQKVKRRIEAIVHGIEVAYECEASIDYGAMYHEVYNDPDLTAEFMKFAKAHGGVNVIRCKEAMTGEDFGYMLADIPGFMFWLGVASPYGLHHAKLAPNEEAIDRAIAFLIDYFSWKGNAE", "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": "MSMKYLMLLFAAMIIRSFADSGNAIETTLPEITNATTDIPAIRLCGPEGDGYCLHGDCIHARDIDGMYCRCSHGYTGIRCQHVVLVDYQRSEKPNTTTSYIPSPGIVLVLVGIIMCCLLSVYRFTRRTKLPIQDMVVP", "text": "FUNCTION: Stimulates cellular proliferation (hyperplasia)and mobility around infected cells to promote rapid and efficient spread of infection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the orthopoxvirus OPG019 family."}
{"protein": "MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAVGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGVGVGVGGSGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEHSHSSPGGGGRYSDTPSHPCLCSGTQRSAISSVSTGLHSLAAFRGLMKRRSSV", "text": "FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family."}
{"protein": "MNIHEYQAKEILHKFNVPVPKGFVAMSAEEAETKINQLKSDVLVVKAQIHAGGRGKAGGVKLAKSAEEAQQFVKGMLGITLVTHQTGPNGQQVRRVYIEEGSSIKKEYYLSIVIDPKLSRPAFIFSSEGGMDIEEVAKNFPTKIVKLDIDYAADFASFDSRKLSNIFNLSPEQIEKITNVAKNIYDTFIATDANQIEINPLVETNSGDFIALDAKISFDDNALYRHPEIVELRDYDEEVKEEIEASKHGLSYIKMDGNIGCMVNGAGLAMATMDIIKYYGAEPANFLDVGGGASKETVTEAFKIILSDSNVKGILVNIFGGIMRCDIIASGIVEAAKGMSIKVPLVVRLSGTNFEKGKRILEESGLNIIAADELDEAAQKIVKEVE", "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": "MNRIKKGDTVVVISGKNKNKSGVVIQVNPKEQTALVEGVNKIKRHQKKDQTHEQSGIIEKEAPIRLCKLALVDPKGKDKGKATKVKYLLKDNKKVRVARKSGSELDVNKK", "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": "MSELPAFWLRRPPDWRAHALRPLAALYGGVMRLRRYGYRKGWIRRGRLPVPVVVVGNIFVGGTGKTPLVAWIADTLAAMGRRPGIVSRGYGGRSREWPRRVAADSDPAEVGDEPLLLARGTGCPVAVGPDRVAAAQLLLAAGCDVVVSDDGLQHYRLPRALELVVCDGHRGLGNGLCLPAGPLREPADRLADVDMVISNGRAPALTPWWFELVPGPLRPLAADAAPEGGPEPGTTVHAVAGIGHPARFFATLEGLGYRVIPHPFPDHHPYRAGELRFGDDRPVIMTEKDAVKCAGLAPARSWFLPVEARPEPATRERLEASLARLHSLTNR", "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": "MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNLGGLLHFPLVKTLEQLTNLPSIAINDAQAAAWAEYQALEGDITDMVFITVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADARTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCVVVGGSVGLAEGYLALVEMYLAQEPAAFHVDLLAAHYRHDAGLLGAALLAQGEKL", "text": "FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily."}
{"protein": "MLTVIPIPAFQDNYIWLLRQDASDKVVIVDPGDAQPVIEYLEREGLSLAAILVTHHHHDHTGGIDALVKRYSPRVIGPDNSAIPAIDEVVGDEDECRVQGRRFEVFAVPGHTLDHIAFYAPGTPGLLFCGDTLFSGGCGRLFEGTAEQMHRSLARLAALPDDTLVFAGHEYTLANLRFAQAAEPDNPARDAHLGECERARQLERPTLPSTIGRERQINPFLRIDQPGLLNALAEQGSVDDDSAAFATLRGWKDRF", "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": "MATVLRIDSSALSNGSHSKALADFFQTQWLEKHPTDSFQTLDLSQTPPPHLSEATIGAMFTPTEERSKEQTQQLALSTDYIEQLKKADVILISTPMYNFGIPSTLKAYLDHSLRVGETFVYTDKGPKGLLEGKKAIVVAASGGDYTQSPLDAMNFVTPYLKTALGFIGIEDVTLVEAPGMAGDEASINKSIKQAKQTLQNCL", "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": "MLKKDKSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMLRTEVRSEESNSHLGHVFNDGPKESGGLRYCINSAAIQFIPYEKLEELGYGDLISHFDK", "text": "SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family."}
{"protein": "MPLRLDIKRKLAQRSERVKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFIARKQWIVAGADDMFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWMCTQIFEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPITLTGSEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMIKIGREVPVASMDSSGKIIWSKHNEIQTVNIKTIGADNEIADGERLPLAVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWSVDGEYAVRESTSRIKIYSKNFQERKSIRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIRRIDVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNSSSRLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSVARFLESQGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLLLYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWKKDLQKVNPKAAESLADPDEYPNLFEDWQIALNVEANVAPKRGIYPPAEEYIIHAERPNETLVEAFKSMHIHLEEVLPDENGDDTHEAIEENGVEESQEDAVEVDVEADGSTDGAVLVNGNDTEEQWGTNNEESSA", "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 WD repeat COPB2 family."}
{"protein": "MNTVRVTFLLVFVLAVSLGQADKDENRMEMQEKTEQGKSYLDFAENLLLQKLEELEAKLLEEDSEESRNSRQKRCIGEGVPCDENDPRCCFGLVCLKPTLHGIWYKSYYCYKK", "text": "FUNCTION: Weakly inhibits Kv1.2/KCNA2, Kv1.3/KCNA3, Kv2.1/KCNB1 voltage-gated potassium channels, and Nav1.5/SCN5A voltage-gated sodium channels (PubMed:29483648). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 01 (HNTX-16) subfamily."}
{"protein": "MKLQLVAVGTRMPAWVTTGFEEYQRRFPRDMAFELIEIPAGKRGKNADIARILQKEGEQMLAAIPKGNHIVSLDLPGKNWTTPELATQLNRWQLDGRDVSLLIGGPEGLAPACKQAANQSWCLSALTLPHPLVRVLVAESLYRAWSINNNHPYHRE", "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": "MFGSKIFSRLFFKRTYATYKRFDNTTSSSSFTTSYAHLLTNRKTLYIGGGLLGFYVYNLHDAPYTHRSRFIWVPYWLETKIGDYSYRQIYQQFQSQILPHSNPLYNRVSTIMNKLLDVALNDNINDDLNARFLNHLKSLKWEINIIQNDSLPPNAFILPNGKIFIFSSIMPICKNEDGLATVLSHELSHQLAQHSSEQLSKQPIYMVLSTILYTITGVSWFNDLLINGVLTMSASREMESEADHIGCELLARACFNPQESINFWHRMSQAEKKAAGIVSQEGGYLNTWEFFSTHPATSRRIADIQKWMPQLLQIRESSGCYEYGRFYNFNKSYFSH", "text": "FUNCTION: Protease that is part of the quality control system in the inner membrane of mitochondria (By similarity). Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane protein (By similarity). Required for TOR signaling (PubMed:27325672). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase M48 family."}
{"protein": "MFEIHPVKKVSVVIPVYNEQESLPELIRRTTKACESLGKEYEILLIDDGSSDNSAHMLVEASQAENSHIVSILLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSWFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIVDAMLHCHERSTFIPILANIFARRAIEIPVHHAEREFGESKYSFMRLINLMYDLVTCLTTTPLRMLSLLGSIIAIGGFSIAVLLVILRLTFGPQWAAEGVFMLFAVLFTFIGAQFIGMGLLGEYIGRIYTDVRARPRYFVQQVIRPSSKENE", "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": "MLTSGLLLVAAVAFLSVLVLMSVWKQRKLSGKLPPGPTPLPFIGNFLQLNTEQMYNSLMKISQRYGPVFTIYLGPRRIVVLCGQEAVKEALVDQAEEFSGRGEQATFDWLFKGYGVVFSSGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDSFRKTNGAFIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSMGQLYEMFSSVMKHLPGPQQQAFKELQGLEDFITKKVEHNQRTLDPNSPRDFIDSFLIRMLEEKKNPNTEFYMKNLVLTTLNLFFAGTETVSTTLRYGFLLLMKHPDIEAKVHEEIDRVIGRNRQPKYEDRMKMPYTEAVIHEIQRFADMIPMGLARRVTKDTKFRDFLLPKGTEVFPMLGSVLKDPKFFSNPKDFNPKHFLDDKGQFKKNDAFVPFSIGKRYCFGEGLARMELFLFLTNIMQNFHFKSTQAPQDIDVSPRLVGFATIPPTYTMSFLSR", "text": "FUNCTION: Exhibits a high coumarin 7-hydroxylase activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MTSRRTRLRLIERLRKNGIQNEAVLEAMTEIPRHIFVDEALAHRAYEDTALPIGHSQTISQPYIVARMTELLCSGWKPKRVLEVGAGSGYQTAILARLSTQVYTVERIAPLLEKAKLRFKALKLNNVSAKLSDGRWGWPEQGPFDAIMVTAAPEQTPSELLEQLADGGRLVIPVGSGSEQMLKVYKRQGAEIEESSLEQVRFVPLLGGVVR", "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": "MTTSADQTDVLVIGSGPGGAGVTLKLVQAGYKVTCLEQGPWVTPPEHPHYHREWEIEKQRGWAYDPNVRGLPEDYPVTGFTTPYLMNNVGGSTMHYAGHWPRYKPVDFRKGTEHGLEGTIDWPISYEELAPYYDENDAIYGISGMVGDPSYPDRTGVDRDPPVKPGKLGRNFAQALGDLGWHWWPSDNAIITRPREGREADIAAGNELSGSPTGSLSTPTHTHWPTAIALGADLRTHARVEQIHTKNGKATGATYIDTRTGARHEINAKIVVVSASGIGTPRLLLMSAQKGHPDGLANSNGLVGKYLMHHILRVLASVVRTSRMEGYKGAFGAPLYSHEFYHTDTNRGFVNGFGMQVARSFGAAYTAMGSHTGYVAPWGKSHRKFFNEHFGNHLMVFMFGEDLPVETNCVTLDPDAKDSSGLPAARVNWEPHENDIALANYGIDRIFEAARALGAVETNDTGVLNPPPGWHLMGTCRMGNNPEDSVTNKWHQTWDVPNLFVVDGSSLTTGGAVNPTSTIGALAVRAGDYISRRFSDIVDQRTTPSNEDAPAI", "text": "FUNCTION: Involved in the degradation of methyl tert-butyl ether (MTBE). Catalyzes the conversion of 2-methyl 1,2-propanediol (2-M1,2- PD) to hydroxyisobutyraldehyde. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MNYFELFSLLPSYDVDTALLADRYRELQRAVHPDKFANASEQDKRLSVQRTAQINDAFQTLKNPIQRAEHLLALKGLELSHESTTLKDTQFLMQQMDWRESLEEIKHSDDPDSEIAELYDSFEQYAKHITAELKLLLVSELEADHLQAADQIRKLKFMAKLQDELTRVEDALLD", "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": "MPWWLISLTFIYRLFLCATIRTVEAPDEWWQSTEVAYNMVFGKGHLPWEWRYGLRSVLFPAVVALPFYLLKLLGRDTTWAVWFAPRVLQALVLTLIDVSVFCMGATLDELLAKRELELAEETRQSKTKGFSYFCEVSVSRSRRGICNSISYTALLLSLSNWYMAYCGVRLYGNVIEALLVLLTLQQRRYVPFLLLTGLASAIRVTSAVVLSPLVFRHLANATREHGFIRGLFRIVLTGLIVLVAVLGGVMVLDYCFYGRWVLTPLAFFRFNVLHNLSRFFGEHPWYFYVGPVLVGIVGPHVLFTIAAPLVLWRDTASRAVSRPVLGMLGIGAWTLGFYSLIDHKEMRFVFVVIPLSLITAAFVLVRWSRTSAVVVKMNRLFVLFNIVMIYLMGYVYRRGPLDVMAEVRDGPRINRLDVIATCYTVPGYSYMHKKVNHLGFVDCSIDLDEKTGLPKVTEDIMFRRYPKEYVLWRYDGKHSFNMSDLEESRKASELQSVVMPKSAPHPDAMVMTRAVAKEIEEPFLKRHGYRLYRTFLHSPLTLAPYEDIYIQMWVKVTK", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2- GlcN-acyl-PI during GPI precursor assembly. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB subfamily."}
{"protein": "MLNFGASLQQASEGKMELISEKPREGMHPWDKAEQSDFEAVEALMSMSCDWKSHFKKYLENRPVTPVSDTSEDDSLLPGTPDLQTVPAFCLTPPYSPSDFEPSQGSNLTASAPSTGHFKSFSDAAKPPGATPFKEEEKNPLAAPPLPKAQATSVIRHTADAQLCNHQSCPVKAASILNYQDNSFRRRTHGNVEATRKNIPCAAVSPNRSKPEPSTVSDGDEKAGAALYDFAVPSSETVICRSQPAPSSPVQKSVLVSSPTVSTGGVPPLPVICQMVPLPANNSLVSTVVPSTPPSQPPAVCSPVLFMGTQVPEGTVVFVVPQPVVQSPRPPVVSPSGTRLSPIAPAPGFSPSAARVTPQIDSSRVRSHICSHPGCGKTYFKSSHLKAHVRTHTGEKPFSCSWKGCERRFARSDELSRHRRTHTGEKKFACPMCDRRFMRSDHLTKHARRHLSAKKLPNWQMEVSKLNDIALPPTPASAQ", "text": "FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. May play a role in the cell cycle regulation (By similarity). Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
{"protein": "MQFVSTRPQPQQLGIQGLGLDSGSWSWAQALPPEEVCHQEPALRGEMAEGMPPMQAQEWDMDARRPMPFQFPPFPDRAPVFPDRMMREPQLPTAEISLWTVVAAIQAVERKVDAQASQLLNLEGRTGTAEKKLADCEKTAVEFGNHMESKWAVLGTLLQEYGLLQRRLENLENLLRNRNFWVLRLPPGSKGEAPKVPVTFVDIAVYFSEDEWKNLDEWQKELYNNLVKENYKTLMSLDAEGSVPKPDAPVQAEPREEPCVWEQRHPEEREIPMDPEAGAEPLVPAQDASSQVKREDTLCVRGQRGLEERAIPTESITDSPISAQDLLSRIKQEEHQCVWDQQDLADRDIPTDPNSESLISAHDILSWIKQEEQPYPWGPRDSMDGELGLDSGPSDSLLMVKNPPPAPPQPQPQPQPPQPQLQSQPQPQSLPPIAVAENPGGPPSRGLLDDGFQVLPGERGSGEAPPGGDRSTGGGGGDGGGGGGGAEAGTGAGGGCGSCCPGGLRRSLLLHGARSKPYSCPECGKSFGVRKSLIIHHRSHTKERPYECAECEKSFNCHSGLIRHQMTHRGERPYKCSECEKTYSRKEHLQNHQRLHTGERPFQCALCGKSFIRKQNLLKHQRIHTGERPYTCGECGKSFRYKESLKDHLRVHSGGPGPGAPRQLPPPPERD", "text": "FUNCTION: Binds to the U5 repressive element (U5RE) of the human T cell leukemia virus type I long terminal repeat. It recognizes the 5'- TCCACCCC-3' sequence as a core motif and exerts a strong repressive effect on HTLV-I LTR-mediated expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MSNHDQLHRYLFANHAVRGELVSVNETYQQVLANHDYPPAVQKLLGEMLVATSLLTATLKFDGDITVQLQGGDGPLTLAVINGNNRQEMRGVARVKGEISDDSTLQEMVGNGYLVITITPAQGERYQGVVALEGETIAACLENYFMQSEQLPTRLFIRTGHVADKAAAGGMLLQVLPAQERNEDEFDHLAQLTATIKAEELFTLPANEVLYRLYHQEEVTLYEPQNVSFRCTCSRQRCADALVTLADDDVTEMLEQDGNIDMHCEYCGNHYLFDAVDIATLKNGNSASSEQIH", "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": "MNICVNSLYRLSTPQFHSLYSEEVSDETLALLIGEVENGNQNCIDLLCNLALRNDNLGHKVEKLLFDLFSGKRSGSPDIDKKINQACLVLHQIANNDITKNNTEWKKLHAPSRLLYMAGSATTDLSKKIEIAHKIMGDQFAQTDQEQVGVENLWCGARMLSSDELAAATQGLAQESPLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHNEVFLVNTGDHWLLCLFYKLAEKIKCLIFNTYYDLNENTKQEIIEAAKIAGISENEDIDFIETNLQNNVPNGCGLFCYHTIQLLSNAGQNDPATTLREFAENFLTLSVEEQTLFNTQTRRQIYEYSLQ", "text": "FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease targets the host cell ubiquitin pathway by acting as a deubiquitinase in infected host cells (By similarity). SUBCELLULAR LOCATION: Secreted Host cytoplasm Note=Secreted via type III secretion system 2 (SPI-2 TTSS), and delivered into the host cytoplasm. In phagocytic cells localizes to the Salmonella-containing vacuole (SCV). In epithelial cells localizes to the Salmonella-containing vacuole (SCV) and to the Salmonella-induced filaments (Sifs), which are tubular membrane extensions from the SCV that are formed at late stages of infection (By similarity). SIMILARITY: Belongs to the peptidase C79 family."}
{"protein": "MTIGYIIGSATINEATAILEQKIRAGYYVILEYDGDKILGLITNVYTGSPLLDDNLNDVKFVQRIKQLEANKIPFFIKARIKLLCKLDGKFTQPDLPPVAGTPVRLASDEELSTVFSAGDVRIGKLIGSNVEVKIRLNPLSRHLAILAATGSGKSNTVAILSQRLVEIGGSILIFDYHGEYYDSTLPNLNIIEPKLNPLYLSVNEFATLLEIRENANIQYRIIRRTFNQLKEEINNEIKEGKTSLAELNSNFFERLKVKIEEEGRNEKRKESKDEVLNKVEDFAERYSDIIDITFGDVINKIKLGKINVVNLSSLDEDAIDAIVAHYLRRILTSRKENKIKKDSGLKFPILTVVEEAHVLLSKDTNTLTKKWAGRIAREGRKFGVGLIIVSQRPKGLDENILSQMTNKIILKIVEPSDKKYVLETSDNLSEDLADGLSSLDTGEAIIIGNVVKLPTIIKIDKFEGKLSGSDPNLTEEWKRAKEEEIVHSDVSDWG", "text": "FUNCTION: Involved in DNA double-strand break (DSB) repair (PubMed:14990749). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (PubMed:14990749). Loads on either a 3' or a 5' DNA tail for subsequent DNA unwinding (PubMed:14990749). SIMILARITY: Belongs to the HerA family."}
{"protein": "MKFVDEAVIRVEAGDGGSGCVSFRREKYIPDGGPDGGDGGDGGSVYLEADENFNTLIEYRFERFHMAERGENGRGRDCTGHSGKDLILKVPVGTRAIDHDTEEVLGDLTTHGQKLLVAKGGFHGLGNTRFKSSTNRAPRQKTLGTPGEVRSLKLELLLLADVGLLGMPNAGKSTFIRAVSRATPKVADYPFTTLVPNLGVVNPRPGQSYVIADIPGLIEGAAEGAGLGIRFLKHLERCRILLHIIDIEPIDGTDPVDSARAIVGELEKYSPKLASKPRWLVFNKADLLLEDELKEKAERVVKELGWEGEVYTISAYGRDGTKELAAKLWDFIQSLPPEDKDANPEDEVEFKWDNYHQANIDAINEDYDDDFDDDFDDDDYDVEVIYQR", "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": "MGDKKDDKDSPKKNKGKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQEILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNRAVFKGGQDNIPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQLSIHETEDPNDNRYLLVMKGAPERILDRCSTILLQGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDLKDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLISMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQRKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY", "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: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily."}
{"protein": "MVRPNAPDRFNEEKATYVVRGDGEGGDKPDLDRGAEVIRSVVRKLPARPGVYRMLDARGDVLYVGKARALRNRVTSYTQVARLPQRLQRMVAQTRAMEIVTTTSEAEALLLEAQLIKRYRPPYNVLLRDDKSFPFILLRTDHDFPRVQKHRGARRAKGRYYGPFASAGSVARTLNALQKTFLLRSCTDSFFANRSRPCLLYQIRRCSAPCVDRISKEDYAGLVSDAQDFLEGRSTAVQKRLGEAMTRAADAMDFEQAAVLRDRLKALTFIQGSQSVHADGLGDADVFALAAKGGQLCIAGFFIRGGQNWGHRSFFPAHVAGVPETEVMASFLMQFYEGVPPPKLILVDREPDESALLAEALGETAGRKVEISVPQRGNRKRLLDQAVRNAGEELDRRLAESSSQAKLGRELADLFDLENPPQRIEIYDNSHIQGTSALGAMVVAGPEGWMKGAYRKFNIKRAETQPGDDFAMMREVFQRRFARAIEEDPERTKGEWPDLVLIDGGKGQVSAVAAVFSELGIDDLPFVGVAKGPDRNAGRETFYLPDGREFTLPTNNAVLFYIQRLRDEAHRFAIGAHRAKRAKAMGSSPLDEVPGIGPARKKALLMHFGTTRAIKGASLEDLQKAPGVSAAVAQAVYDFYNPGG", "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": "MATDPIHQFQISKLIPIEIGGLDFSFTNSSLFMVATVAAAGAFLYLTTSSRGLVPSRMQSVSEMSYEFVASMLRDAAGSHGMRFFPFVFSLFMFVLVANLLGLFPYFFTVTSHIVVTFALALLVIGTVLVYGFWKHGFGFLKLFVPEGVPGVLLPLVVLIEVISFLSRPISLSVRLFANMLAGHITLKVFAGFVTSLGALGVAGAAGAVLPLAMTVALTGLELLVAFLQAYVFAVLTCMYLNDALHPGH", "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": "MSKTTIIERIWPAKEIIEDLSELRKQSPLTHVITNIVVTNWTANVLLAIGSSPAMVIAKEEAGEFAKIASGLLINIGTVTSNDAITMKIAAEAAHQAKIPWVLDPVAVGALGFRTELAKELLNFKPTVIRGNASEILALAGTDGGGKGVDSTALSSDALPLAQMLAEKTGAVIAISGEIDYVTNGKETISISGGDPIMTKVTGVGCSLGGVIASFLGVQKDPLRATASASAVFAIAGTRSAKISKGSGSFAVNFLDQLNLLSTEK", "text": "FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ). SIMILARITY: Belongs to the Thz kinase family."}
{"protein": "MTAQLIDGNALSRQLRTEVAQRAALLRARGITPGLAVVLVGDNPASQVYVRNKVKACEDNGLHSVLERYPAEMSEADLLARVEALNNDPAIHGILVQLPLPAHIDAQKVIEAISPAKDVDGFHVGSAGALMVGQPGFWPCTPYGCMKMLESIGYDLRGKHAVVIGRSNIVGKPMALMLLQKNATVTICHSATADLKAMTLQADVIVAAVGKRNVLRADMVKPGAVVIDVGMNRNEEGKLCGDVDFDGVKEVAGYITPVPGGVGPMTITMLLVNTLEAAERG", "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": "MPEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK", "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": "MFHQIWAALLYLYGILLNSIYQCPEHSQLTTGGVDGKEFPEPHLGQWYFIAGAAPTKEELATFDPVDNIVFNMAAGSVPMQLQLRATIRTKNGLCVPRKWIYRLSEGNTDLRTEGRPDMKTKLFSSTCPGGIMLKETGQGYQRFLLYNRSPHPPEKCVEEFQSLTSCLDFKAFLLTPRNQEACELSSN", "text": "FUNCTION: Probably involved in lipid transport. Can bind sphingosine-1- phosphate, myristic acid, palmitic acid and stearic acid, retinol, all- trans-retinoic acid and 9-cis-retinoic acid (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. Highly divergent."}
{"protein": "MNLVMLILALWAPVAGSMPELSLTLFDEPPPLVETEPLPPLPDVSEYRVEYSEARCVLRSGGRLEALWTLRGNLSVPTPTPRVYYQTLEGYADRVPTPVEDISESLVAKRYWLRDYRVPQRTKLVLFYFSPCHQCQTYYVECEPRCLVPWVPLWSSLEDIERLLFEDRRLMAYYALTIKSAQYTLMMVAVIQVFWGLYVKGWLHRHFPWMFSDQW", "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": "MHYKKAFLASLLSSIALTAYAPPEPWATLTPSSKMDGGTTEYRTSFGLAVIPFTVTESKVKRNVISQINDGQVQVTTQKLPHPVSQIGDGQIQVTTQKVPPVVSHIVSQIGDGQLQITTAKNVVTKSTIAVPSKTATATATSTATAVSQIHDGQVQVTISSASSSSVLSKSKLEPTKKPNNENVIKVQACKSSGTLAITLQGGVLIDSNGRIGSIVANRQFQFDGPPPQAGAIYAGGWSITKHGTLAIGDNDVFYQCLSGTFYNLYDQSIGGQCNPVHLQTVGLVDC", "text": "FUNCTION: Component of the outer cell wall layer. May be involved in meiosis and sporulation (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Note=Covalently attached to the cell wall. SIMILARITY: Belongs to the PIR protein family."}
{"protein": "MLKEWAIKQGILLKVAETIKSWIFFSQCNKKDDLLHKLDIGFRLDSLHTILQQEVLLQEDVELIELLDPSILSAGQSQQQENGHLPTLCSLATPNIWDLSMLFAFISLLVMLPTWWIVSSWLVWGVILFVYLVIRALRLWRTAKLQVTLKKYSVHLEDMATNSRAFTNLVRKALRLIQETEVISRGFTLVSAACPFNKAGQHPSQHLIGLRKAVYRTLRANFQAARLATLYMLKNYPLNSESDNVTNYICVVPFKELGLGLSEEQISEEEAHNFTDGFSLPALKVLFQLWVAQSSEFFRRLALLLSTTNSPPGPLLTPALLPHRILSDVTQGLPHAHSACLEELKRSYEFYRYFETQHQSVPQCLSKTQQKSRELNNVHTAVRSLQLHLKALLNEVIILEDELEKLVCTKETQELVSEAYPILEQKLKLIQPHVQASNNCWEEAISQVDKLLRRNTDKKGKPEIACENPHCTVVPLKQPTLHIADKDPIPEEQELEAYVDDIDIDSDFRKDDFYYLSQEDKERQKLEHEESKRVLQELKSVLGFKASEAERQKWKQLLFSDHAVLKSLSPVDPVEPISNSEPSMNSDMGKVSKNDTEEESSKSTTTDNEISRTEYLCENSLEGKNKDNSSNEVFRQGAEERMCYQCESEDEPQADGSGLTTAPPTPRDSLQPSIKQRLARLQLSPDFTFTAGLAAEVAARSLSFTTMQEQTFGDEEEEQIIEENKNKIEEK", "text": "FUNCTION: Plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life. Required for morphogenesis of the preimplantation embryo, and for the implantation process. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, stereocilium membrane Cell junction, adherens junction Nucleus Cytoplasmic vesicle, secretory vesicle, acrosome. SIMILARITY: Belongs to the vezatin family."}
{"protein": "MRFFRKTSLYLSLFLYFFLYESSMAANTIRRGESLRDGINHKPLVSPQKTFELGFFSPGSSTHRFLGIWYGNIEDKAVVWVANRATPISDQSGVLMISNDGNLVLLDGKNITVWSSNIESSTTNNNNRVVSIHDTGNFVLSETDTDRPIWESFNHPTDTFLPQMRVRVNPQTGDNHAFVSWRSETDPSPGNYSLGVDPSGAPEIVLWEGNKTRKWRSGQWNSAIFTGIPNMSLLTNYLYGFKLSSPPDETGSVYFTYVPSDPSVLLRFKVLYNGTEEELRWNETLKKWTKFQSEPDSECDQYNRCGKFGICDMKGSNGICSCIHGYEQVSVGNWSRGCRRRTPLKCERNISVGEDEFLTLKSVKLPDFEIPEHNLVDPEDCRERCLRNCSCNAYSLVGGIGCMIWNQDLVDLQQFEAGGSSLHIRLADSEVGENRKTKIAVIVAVLVGVILIGIFALLLWRFKRKKDVSGAYCGKNTDTSVVVADLTKSKETTSAFSGSVDIMIEGKAVNTSELPVFSLNAIAIATNDFCKENELGRGGFGPVYKGVLEDGREIAVKRLSGKSGQGVDEFKNEIILIAKLQHRNLVRLLGCCFEGEEKMLVYEYMPNKSLDFFLFDETKQALIDWKLRFSIIEGIARGLLYLHRDSRLRIIHRDLKVSNVLLDAEMNPKISDFGMARIFGGNQNEANTVRVVGTYGYMSPEYAMEGLFSVKSDVYSFGVLLLEIVSGKRNTSLRSSEHGSLIGYAWYLYTHGRSEELVDPKIRVTCSKREALRCIHVAMLCVQDSAAERPNMASVLLMLESDTATLAAPRQPTFTSTRRNSIDVNFALDSSQQYIVSSNEITSTVVLGR", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MGIDINHKHDRVARRTAPKSENPYLRLLSKLYAFLARRTGEKFNAIVLKRLRMSRRNRQPLSLAKLARAVQKAGNENKTVVTLSTVTDDARLYTVPKISVAALHVTEGARARILAAGGEIITLDQLALKSPKGENTVFLQGPRSAREAEKHFGPAPGVPHSHTKPYVRSKGRKFERARGRRASRAYKN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family."}
{"protein": "MATKLFPKFSQGLAQDPTTRRIWFGLAVAHDFESHDGMTEENLYQKIFASHFGQLAIIFLWTSGNLFHVAWQGNFEQWVTDPVHVRPIAHAIWDPHFGTSAVEAFTRGGASGPVNIATSGVYQWWYTIGMRTNQDLFTGSVFLALVSAVFLFAGWLHLQPNFQPSLSWFKDAESRLNHHLSGLFGVSSLAWTGHLVHVAIPESRGRHVGWDNFLSVLPHPQGLAPFWSGNWAAYAQNPDTASHAFGTSEGSGQAILTFLGGFHPQTQSLWLSDMAHHHLAIAVIFIVAGHMYRTNFGIGHRLQAILDAHVPPSGNLGAGHKGLFDTVNNSLHFQLGLALASVGTITSMIAQHIYSLPPYAYLAIDFTTQAALYTHHQYIAGFIMCGAFAHGAIFFIRDYDPEANKGNVLARILDHKEAIISHLSWVTLFLGFHTLGLYVHNDVMQAFGTPEKQILIEPVFAQWIQAAQGKTVYGFDLLLSSSTSVASTAGQSVWLPGWLDAINNNQNTLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAYDAFYLAVFWMLNTIGWVTFYFHWKHLALWQGNVAQFDESSTYLMGWLRDYLWLNSSQLINGYNPFGMNSLSVWAFCFLFGHLIYATGFMFLISWRGYWQELIETLVWAHEKTPLANIVYWKDKPVALSIVQARLVGLVHFSVGYIFTYAAFLIASTSGRFG", "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": "MPELPEVETVRRGLQPAMEGATIVRAETRRKDLRFPFQTDFVARLEGQAVTGLGRRAKYLLADLASGDVLLMHLGMSGSFRVIDAAGVTVPGDFHRPRGEDRVHDHVRFTMSSRAEIVFNDPRRFGYMKIVARSALGDEPLLKGLGPEPLGNEFDAAVLAHGCRNRKTSLKAALLDQRVVAGLGNIYVCEALFRARLSPRRLAATLAMKTGAPSERAERLVGAIRDVLNQAIEAGGSSLRDHRQTTGELGYFQHSFQVYDREGDKCRTPACKGAVKRFTQNGRSTFWCPVCQT", "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": "MDNPGPSLRGAFGILGALERDRLTHLKHKLGSLCSGSQESKLLHAMVLLALGQDTEARVSLESLKMNTVAQLVAHQWADMETTEGPEEPPDLSWTVARLYHLLAEENLCPASTRDMAYQVALRDFASQGDHQLGQLQNEAWDRCSSDIKGDPSGFQPLHSHQGSLQPPSASPAVTRSQPRPIDTPDWSWGHTLHSTNSTASLASHLEISQSPTLAFLSSHHGTHGPSKLCNTPLDTQEPQLVPEGCQEPEEISWPPSVETSVSLGLPHEISVPEVSPEEASPILPDALAAPDTSVHCPIECTELSTNSRSPLTSTTESVGKQWPITSQRSPQVPVGDDSLQNTTSSSPPAQPPSLQASPKLPPSPLSSASSPSSYPAPPTSTSPVLDHSETSDQKFYNFVVIHARADEQVALRIREKLETLGVPDGATFCEEFQVPGRGELHCLQDAIDHSGFTILLLTASFDCSLSLHQINHALMNSLTQSGRQDCVIPLLPLECSQAQLSPDTTRLLHSIVWLDEHSPIFARKVANTFKTQKLQAQRVRWKKAQEARTLKEQSIQLEAERQNVAAISAAYTAYVHSYRAWQAEMNKLGVAFGKNLSLGTPTPSWPGCPQPIPSHPQGGTPVFPYSPQPPSFPQPPCFPQPPSFPQPPSFPLPPVSSPQSQSFPSASSPAPQTPGPQPLIIHHAQMVQLGVNNHMWGHTGAQSSDDKTECSENPCMGPLTDQGEPLLETPE", "text": "FUNCTION: Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF- kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis (PubMed:12855817, PubMed:16002681, PubMed:21703541). Ligand binding to these receptors results in TRIF recruitment through its TIR domain (PubMed:12855817, PubMed:16002681, PubMed:21703541). Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively (PubMed:12855817, PubMed:16002681, PubMed:21703541). Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens (By similarity). 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 (PubMed:21703541). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasmic vesicle, autophagosome Mitochondrion Note=Colocalizes with UBQLN1 in the autophagosome. Colocalizes in the cytosol with DDX1, DDX21 and DHX36 (PubMed:21703541). Colocalizes in the mitochondria with DDX1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-helicase- TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (PubMed:21703541)."}
{"protein": "MEQTKYRMELVLLLGLISMLSFIPASIAAEEGQEHDNLTTYIVHVKKLEIEGPLQSTEELHTWHHSFLPETSNKDRMVFSYRNVASGFAVRLTPEEANALQEKEEVMSIRPERTLSLHTTHTPSFLGLRQGQGLWNDSNLGKGVIIGVIDTGIYPFHLSFNDEGMPPPPAKWKGHCEFTGGSVCNNKLIGARNLVKSAIQEPPYEDFFHGTHTAAEAAGRFVEGASVFGNARGTAAGMAPDAHLAIYKVCSSKVKDECPESAILAAMDIAIEDGVDVLSLSLGLGSLPFFEDPIAIGAFAATQKGIFVSCSAANSGPHYSSLSNEAPWILTVGASTIDRKISASAKLGNGAEYEGETLFQPKDFSSQLLPLVYAAAEKNNSSALCAPGSLRNINVKGKVVVCDLGGGIPFIAKGQEVLDAGGSAMILANIENFGFTTLANAHVLPAVHVSYAASLAIKAYINSTYTPTATVLFQGTIIGDSLAPSVAAFSSRGPSQQSPGILKPDIIGPGVNILAAWAVSVDNKIPAFDIISGTSMSCPHLSGIAALLKSAHPDWSPAAIKSAIMTTANTLNLRGLPILDQRLQPADIFATGAGHVNPVRANDPGLVYDIQPEDYVPYLCGLGYSDREVTIIVQRSVRCFNVKSIAQAELNYPSFSILLGSDSQFYTRTLTNVGPANSTYTVKIDVPLAMGISVSPSQITFTQVNQKVAYFVDFIPQIKENRGNHTFAQGAITWVSDKHVVRTPISVIFK", "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": "MKNIYNTYDVINKSGINFGTSGARGLVTDFTPEVCARFTISFLTVMQQRFSFTTVALAIDNRPSSYAMAQACAAALQEKGIKTVYYGVIPTPALAHQSISDKVPAIMVTGSHIPFDRNGLKFYRPDGEITKDDENAIIHVDASFMQPKLEQLTISTIAARNYILRYTSLFPMPFLKNKRIGIYEHSSAGRDLYKTLFKMLGATVVSLARSDEFVPIDTEAVSEDDRNKAITWAKKYQLDAIFSTDGDGDRPLIADEYGNWLRGDILGLLCSLELAADAVAIPVSCNSTISSGNFFKHVERTKIGSPYVIAAFAKLSANYNCIAGFEANGGFLLGSDVYINQRLLKALPTRDALLPAIMLLFGSKDKSISELVKKLPARYTYSNRLQDISVKTSMSLINLGLTDQEDFLQYIGFNKHHILHSDVTDGFRITIDNNNIIHLRPSGNAPELRCYAEADSQEDACNIVETVLSNIKSKLGRA", "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 group C2 O antigen. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MSLFPSLPLLLLCVVATSYSETVNCEDSQKICPAVIACNSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDCDSSLAASERKALQTEMAHIKKWLTFSLGRQVGNKFFLTNGEMMTFDKVKALCAKFQASVATPSNAAENRAIQNLIKEEAFLGITDENTEGQFVDLIGNRLTYTNWNNGEPNNADSDEDCVLLLKNGKWNDVPCSSSHLALCEFPI", "text": "FUNCTION: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKKRFPTLLATLIWTALYSQHTLADLAEQCMLGVPTYDQPLVTGDPNQLPVRINADKTEANYPDNALFTGNVIVQQGNSTLTANQVELTQVQKPGEAIPVRTVTATGDVNYDDPQIKLKGPKGWSNLNTKDTDMDKGKYQMVGRQGRGDADLMKLRGQNRYTILENGTFTSCLPGDNSWSVVGSEVIHDREEQVAEIWNARFKIGKVPVFYSPYMQLPVGDKRRSGFLIPNAKYTSNNGLEFMLPYYWNIAPNFDATITPHYMERRGLQWQNEFRYLLAPGSGTMALDWLPSDRLYHGTDGTEKDPTRWLYYWGHSGVMDKVWRFNVNYTRVSDPDYFTDLTSQYGSTTDGYATQIFSVGYADQNWDATLASKQFQVFTTGGNNNAYRAQPQLDMNYYKNDIGPFDLHIYGQAAKFTSVNPENPEAERFHIEPSINLPLANGWGSLNTEAKLLATHYQQDIPNGFASNYKNQNGQDATVPNLKDSVNRVIPQFKVDGKVVFDRPMDWSEGFTQTLEPRVQYLYVPYRNQDDIYIYDTTLMQSDYSGLFRDRTYSGLDRIASANQVSTGLTSRIYDDELVERFNVSVGQIYYFSRSRTGNSETIDNSDDTGSLVWAGDTFWRINDQLGLKGGAQYDTRLGSLTLGNAVMEYRKDAERMIQLNYRYASPEYIQAAVPNVKSPGYQQGISQIGTTASWPIADRWALVGAYYYDTKANQPASQLVGVQYNTCCWAINLGYERKITGWNNQNETSKYDNKVSFNIELRGLSSDHSLGTAQMLGSGILPYQSAF", "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": "MRRKSGCSAGLDDRSAYEEVVLDSMLYSARLKETVARGNSAVVVAMARLIAGVFETGGKLLICGNGGSAADAQHLATEFTIRYRSSVHRPALPAIALTTDSSALTAGANDLGYDEVFRRLVEAYGRPGDLLLGLSTSGNSRSVVHALDYARKHGMRTLALLGGDGGALKGLADLSVVVPHNGSADRVQECHITLGHVIIDLVERMMGYGTECNNQQNEQGYADQTD", "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": "MSPQTETKAKVGFKAGVKDYKLTYYTPDYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYEIEPVPGEDNQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPYAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMLKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDYIKKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNAIIREACKWSPELAAACEVWKEIKFEFPAMDTL", "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 (Probable). Binds to abscisic acid (ABA); only half of the possible binding sites are occupied in the crystal and there are indications this is a low affinity site (PubMed:26197050). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MINEIKKETEDKMKKTVEALRKEYQHIRAGRANPALLEKVTVEYYGAPTPVNQLANISAPEARLLVIQPWDKSVLPALEKAILKSDLGLTPTSDGAVIRLVIPQLTQERRSELVKTVKKRAEEHRVILRNLRRDANEDVKDLQKEHIISEDEGKRAQEEIQKLTDKYIREVDQVAERKEAEIMEV", "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": "MVTLKMAIIFLMEQIRTPFSLIWTIMSPTVLFFFLHFNEIELHYGDTAWLGKQISWFVGYISFSVVLFNYCLYLVGRRESGFIATFVHNMDGRLLFIRSQLIASLIMSILYVFFFILVVLTGFQASPDYQIVMIILKSIYINAFMMVSLTFMASFRVTFQTASTIYSVLITVCMVSGIVSLKYNEGIVYWINQVNPIAIYSTILQSDQELSLMTIFFYSIMLIISIISALTFKTEPVWSSQ", "text": "FUNCTION: Together with two further proteins McbF and McbG this protein causes immunity to the peptide antibiotic microcin B17 (MccB17), which inhibits DNA replication in enterobacteriaceae. Immunity is determined by two different mechanisms. McbE is involved in the production of extracellular MccB17 and, in a complex with McbF it also serves as 'pump' for the export of active MccB17 from the cytoplasm to the periplasmic space. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MMDDSFKNYWMNKLKYFSLFILLFAIYWFPDVILGYPEIYLKSLVGYDRQATATWIFLGNMAISLFLGILICYKLGYYKNTLSIFKIKNILFLLFTTIVLFIIYFFTFTYYNSHFITPGIAKEQAAYSRQIVFPFVQFISFAICAPIFEEAAFRTTIYRFFKNDKIAFIVSSISFAWMHTGANPILIVYLPMSVVLTLIYHRRRVLGESILVHCLMNALLPTIIVFLQTITGLYYL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0177 family."}
{"protein": "MRTGVIAKKMGMTRLFQDDGRHVPVTVLSLEGCQVVSVRDKERDGYVAVQLGAGTAKAKNVAKPQRGAYGKAEVEPKAKLVEFRVADDATLDVGAELSADHFVAGQMVDIQGVTQGKGFAGAMKRWGFGGMRATHGVSISHRAHGSTGNRQDPGRVFKNKKMAGHMGARNRTQQNLEIVRTDAERGLLFVKGSVPGSKGGWLLVRDAVKLPRHPEAPYPASIKSAANTNTAPADAPVETPAEEAVVDTAATDGAQES", "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": "MEARRLAILCSHLNPPGPNPTRDPTLRVSDCSSGSSGDGKVESSTLQNDCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFNLLVNNGAAAGQVIFHTHIHIIPRKERDCLWASESLRRHSLKLDKEASQLVSCVRRHLCSLPEEQLVQPS", "text": "FUNCTION: Possesses adenylylsulfatase activity in vitro. SUBCELLULAR LOCATION: Peroxisome."}
{"protein": "MAKGGNKKATAAARAAANRLLADNRLARHQYEILDTLETGIELVGTEVKSIRAGQANLRDGFCLIRKGELQLHNVHISPHSHAGSYFNHDPLRTRKLLAHRREIDKLRGQLDRKGLTLIPLNLHLKGSWIKLTIGLGKGRKLHDKRQEEKRKQADREVKSALARY", "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": "MIDDNGYRLNVGIVLCNTYGQVLWAKRYKQCSWQFPQGGINIGETPEQAMYRELFEEIGLNYCDVRILSITRCWFCYKLPTQLVRWRIKPLCLGQKQKWFLLKLLSKDTKINMKTSKVCTFDTWQWVSLWYPIRQVVFFKRHVYRKVMKEFVKLIISR", "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": "MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKSPCT", "text": "FUNCTION: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore Note=Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I- anaphase I (MI-AI) transition. SIMILARITY: Belongs to the WD repeat BUB3 family."}
{"protein": "MNDKVFTKAIKKQFEFDEEVAAVFDDMLQRSVPFYKESQKISEFFAQKALQNGGIAYDLGCSTATLLINISRKLQNKATLIGLDNSEAMLQRARKKCEAFKADIELENADILEYDYREANLFISNYTLQFVRPLIREELVKKIASSLKKDGLFIFSEKVISHHSKLHKDLIECYYDFKKEQGYSEYEIVQKREALENVLIPYSEEENIKMAKNCGFSHCEVVFRWANFATFIAIK", "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": "MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDSKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDECALKEYGVMRVRNVRESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIVDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLVDQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQRSFR", "text": "FUNCTION: Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus (By similarity). Positively regulates MAPK signal transduction pathway (By similarity). Dephosphorylates GAB1, ARHGAP35 and EGFR (By similarity). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity (By similarity). Dephosphorylates CDC73 (By similarity). Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification (By similarity). Dephosphorylates tyrosine-phosphorylated NEDD9/CAS-L (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class 2 subfamily."}
{"protein": "MAVSGSHRPLTGPQAESWTAEYLTARGLRLIERNYRCRLGEIDLVMAEGATLVFVEVRYRSGKRYGGALASVDRHKCRRLLATAQHYMVEHRVTGAVRLDVVAVSPGAAGPQAEWIRNAIEAQ", "text": "SIMILARITY: Belongs to the UPF0102 family."}
{"protein": "MSSNTRVALVTGANKGIGFAIVRDLCRQFAGDVVLTARDVARGQAAVKQLQAEGLSPRFHQLDIIDLQSIRALCDFLRKEYGGLDVLVNNAAIAFQLDNPTPFHIQAELTMKTNFMGTRNVCTELLPLIKPQGRVVNVSSTEGVRALNECSPELQQKFKSETITEEELVGLMNKFVEDTKNGVHRKEGWSDSTYGVTKIGVSVLSRIYARKLREQRAGDKILLNACCPGWVRTDMGGPKAPKSPEVGAETPVYLALLPSDAEGPHGQFVTDKKVVEWGVPPESYPWVNA", "text": "FUNCTION: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2- alpha (PubMed:1377683, PubMed:1597188). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH- dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MLVNPATKYRPAATVDIPDRTWPGRTITRAPRWMSTDLRDGNQALIEPMNPARKLRLFEQLVKIGLKEIEVAFPAASQTDFDFVRMLIEERRIPDDVTIVVLTQSREDLIRRTVESVRGAARATVHLYNPIAPAWRRIVFNASRDEIKAVAVSGTRLIKALTDAMPETAWTYEYSPETFSLAELDFSLEVSDAVSAAWQAGPGRPMILNLPTTVECSTPNVFADQIEWMHRRLARRAHIVLSVHPHNDRGTAVAAAELALMAGADRVEGCLFGNGERTGNVDLVTLALNLYTQGVAPELDFSDIDAVRQCVEHCNQLPVHPRHPYVGDLVFTAFSGSHQDAIRKGFAQQQPDAIWEVPYLPIDPADLGRSYDAVIRVNSQSGKGGMAYLLEQVHGLYLPRRLQIEFSRAVQAMTDDTGLEASADDLYGLFRREYLARETPLRYVSHQLASDATGATAITVQMERDGQPCTVRGTGNGPIDAFIDALDLPVRVMDYHEHAMTAGADARAACYVEVRVGDSPTGFGAGIDASLVTASLRAVVSGVNRHLQAGFGARAQATQTASASAATEA", "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": "MTQLAIGKPTPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDAPLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNDRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGLGGTLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALMENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR", "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": "MGANQFDVVVVGSGAAGLYACLCLPGHYRVALVTKAELKTGASDWAQGGIAAAIAPTDSPQSHYEDTLAAGAGLCDGEAVDFLVNHAPQAIAELVQFGVSFDRHGQHLALTLEAAHSQPRVLHAADTTGRAIVSTLMGQVQARPNVEIFSQAIALSLNIEPTTGHCRGIQVFVNQTIETFHSRAVLLATGGGGQVFAQTTNPKVSTGDGIALAWRSGAQVRDLEFFQFHPTALTKPGVPHFLISEAVRGEGAHLLDRQGKRFAFDYHPRGELAPRDVVSRAIFQHLANTEKDPTQATVFLDLSPIEPERIQRRFPNIIRRCLHWGVDIFREPIPVAPAAHYWMGGITTDINCQTTIPGLYALGETASTGVHGANRLASNSLLECIVFASQLRNLSLPPLASSDSNVNQSIKEIRLDTTNDLALLNHWRSELPRLMWQTAGICRQAETLQMAIAKLEQWQEQWQQLSSSKLLAHLPEDQKISLSGPGLNEFMQLWAETHNLLDIAQLILTSALFREESRGGHYRLDCPDTKREWQSHTVIEGTRVFLQPSQSQD", "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": "MEGIDLGNAFAQSLSGLGVPADVARALWLPLPMIVILLTVTVGVIAAVWGERKWSGMMQQRMGPTIIGLGGSIQGAADGVKLLVKEDIIPVKADPWLFTLGPAIVIIPVFFSYLVIPFGQGLVLSDITIGIFFIIAVASISPIGALMAGYASNNKYALLGGLRAAAQSISYEIPLALSVLAIVMMSSSLSTVDIVEQQETLGLFSFFSWNIWRQPIGFVIFLISALAETERAPFDLPEAESELVAGHHTEYTGMKFALFYLSEYANLILASLIASVLFLGGWSFIVPLEPLAALFGIEASNPIFQVVNALVGISVTILKATFFVFLAILARWTLPRVRIDQLLDLGWKFLLPVSLFNLLLTAALVLLSNTLKTTLPLYLPLIIFVGLVFVAMSLQKRPAAKPTAARA", "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: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MLITNPALLGILASLAPLALGAPNQSTQARSRKCVIPSSYTSSQGTADDSPAVAGAFAQCAENSVIIFQEGVDYNIFHPIKATNLSNVEIRVLGNLHLPQDITAVQNIVKSGQNTWFTFQGPRVDWTGADDINNGWINSYGQAWWDANPANSSSFPNRPHLMSYKTSQASIKNFRSRKPIAWNVKLHGDDITVTHAIVDAKSTGGFPFNTDGFDVEGTNISITDSVMYNGDDAIAVNTPSHNIVFARNTIGYQSHGMSIGSLGKDPTDFANITNLRFEDVTVIDALYAARFKSWSGGKGLVKNVVWKNIRVFNVTFPIFVTQSYSDQSASRSGTIDPSSSVMMEDFTWSNFSGSINTYHPGDGSCVTNPCWYNAGLPNLKHTEAIVLECNTESSCKNFRTEGIRLYPQSKDSPSVICMKATAELNPKLGFECKNGTFVPQ", "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": "MAKEIFRRDKPHLNIGTIGHVDHGKTTLTASITKVLAKKGLAVAKEFSSIDNAPEEKERGITINTSHVEYQTEIRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPNLVVFMNKVDQVDDKEILELVEIEIRELLSKYEYDGENIPIIQGSALGALNGEKKWEKQIETLMKTVDNYIKEPIRNIDKPFLMPIEDVFTITGRGTVATGRIETGTINTGDSIDIIGMGIDKLNSIVTGVEMFRKILDKGQAGDNVGLLLRGIEKKDIRRGMVISKPGYITPHKKFNAQIYILKKEEGGRHTPFHNKYKPQFYLRTTDVTGTIYLLNNLEMVMPGDNISVEVELLQPVAISEGLRFAIREGGRTVGAGQVIKIIE", "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": "MEKLWGGRFQGKSEAWIDDFGASISFDQKMAKEDLTGSLAHVAMLGKCGIISDAEAAEITAGLKIMQEKLALGELEFSTANEDIHLNIETLLYTEIGPIAGKLHTARSRNDQVATDMHLYLKQAVADIIHSLKHLREVLVQKAGFHVETIMPGYTHLQHAQPISFAHHLLAYFGMFTRDLERLEESVKRIDISPLGSAALAGTTFPIDRAYSAELLGFSAIYENSLDGVSDRDFIIEFLSNSSILMMHLSRFCEELILWTSHEFQFVELTDAFSTGSSIMPQKKNPDMAELIRGKTGRVYGNLFGMLTVLKGLPLAYNKDLQEDKEGMFDTVETVQTSLDIFAGMIETMKVNEEIMEESTQKDFSNATELADYLAKKGVPFREAHEIVGKLVLECTQNGIYLQDVPFSRYQEINPLIEKDIYDVLSSKTAVQKRNSYGGTGFDQIKVALANAKKSL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MMDINEIREYLPHRYPFLLVDRVVDLDVEGQRIRAYKNVSINEPFFNGHFPQHPIMPGVLIIEAMAQAAGILGFKMLDVKPADGTIYYFVGSDKMRFRQPVIPGDQLILEARFLSAKRSIWKFECQALVDDKQVCSGEIICAERKL", "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": "MSEIASRVKAIIVDKLGVEESEVTTEASFTNDLGADSLDTVELIMEFEKEFGISIPDDQAEKIGTVGDAVSYIEANAK", "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": "MNKLSNAFSVLAFADEDAPMASSSSTGKQEESVNGSLEDGDYKQPLVWIDLEMTGLNVEVDRILEIACIITNGDLTQSVEGPDLVVRQTKDCLDKMDDWCQTHHGASGLTKKVLLSAITEREAEQKVIEFVKKHVGSGNPLLAGNSVYVDFLFLKKYMPELAALFPHILVDVSSVKALCARWFPIERRKAPAKKNNHRAMDDIRESIKELKYYKKTIFKARR", "text": "FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SIMILARITY: Belongs to the oligoribonuclease family."}
{"protein": "MSKETKLQVEAIKNGTVIDHIPAKVGIKVLKLFDMHNSAQRVTIGLNLPSSALGSKDLLKIENVFISEAQANKLALYAPHATVNQIENYEVVKKLALQLPERINNVFACPNSNCISHNEPVESSFKLSEKNNDIRLKCKYCEKVFARDVVTEIEA", "text": "FUNCTION: Involved in allosteric regulation of aspartate carbamoyltransferase. SIMILARITY: Belongs to the PyrI family."}
{"protein": "MFQFCLLILLLAPGRFFSALGKPQETLTVENREGSDSKAIPTCREASFCAFLQKNPIDSNLDVLPTCTCTGGTTCSHSWDPNDGKSITEGNKQFKFCSNVPDTIKHECSAEEKALTGIFEEDKVTKKHLAYYGFLHCICPEHSDYPENSYDGTETVEGDKKITTEYYHCERLKTCKSDDTCHALAIGETKKIYYKDCNCPEGQTCPFELKSAYKTEYKETTDKFTTYSMRCQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-11 family."}
{"protein": "MVEPREQFFQDLLSAVDQQMDTVKNDIKDIMKEKTSFMVSFENFIERYDTMEKNIQDLQNKYEEMAANLMTVMTDTKIQLGAIIAQLEILMINGTPLPAKKTTIKEAMPLPSSNTNNDQTSPPASGKTSETPKKNPTNAMFFTRSEWASSKTFREKFLTPEIQAILDEQFANKTGIERLHAEGLYMWRTQFSDEQKKMVKEMMKK", "text": "FUNCTION: Induces host endoplasmic reticulum stress and consequently activates autophagy and NF-kappa-B signaling pathway. In turn, may induce autophagy-mediated STING1 degradation and innate immune evasion. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus K205R family."}
{"protein": "MVGVQICQGMTSEILFFSLQPQFSNMMNKNSRLHIDSNIRNTFFTEIGIGVSANSLLLLFNIFKFIHGQRSRLTDLPIGLLSLINLLMLLIMACIATDIFISCRRWDDIICKSLLYLYRTFRGLSLSTTCLLSVLQAIILSPRSSCLAKYKHKPPHHIFCAMLFLSVLYMFISSHLLLSIIATPNLTTNDFIHVSQSCSILPMSYLMQSMFSTLLAIRNVFLISLIVLSTWYMVALLCRHRKQTRHLQDTSLSRKASPEQRATRSILMLRSLFVLMSIFDSIVSCSRTMYLNDPTSYSIQLLVVHIYATVSPFVFMITEKHIVNYLKSMYVRVLNV", "text": "FUNCTION: Putative pheromone receptor implicated in the regulation of social as well as reproductive behavior. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRTPLVMGNWKLNGTKESVSALIKGIEAAADAAKNVEVAVCPPTIFIEQVANLVANNSIELGAQDVSTNISGAFTGETSPVMVKEFGAKYSLVGHSERRQYHNETDAVVAAKFVAIQANGLVPVLCIGETLEERETDKTFNVVETQLKAVIDVSGIDALENAVIAYEPVWAIGTGKVASSEQAQDVHAHIRTWLAEQSKVVAAKVQILYGGSVKASSAKELFAQPDIDGGLVGGAALLVEEFVGIIEGAK", "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": "MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPISQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNGQLEEFLANIGTSVQNVRREMDGDVETMQQTIEDLEVASDPLYLPDPDPTKFPINRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPGGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSGGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELSKQKQIEKDLEEQSRLIAASSRPNQAGSEGQLVLSSSQSEESDLGEEGKKRESEA", "text": "FUNCTION: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism (By similarity) (PubMed:25328665, PubMed:25568335, PubMed:27219021). Regulates signaling pathway leading to cell proliferation through interaction with RAB5A and subunits of the NuRD/MeCP1 complex (By similarity). Functions as a positive regulator of innate immune response via activation of AKT1 signaling pathway by forming a complex with APPL1 and PIK3R1 (PubMed:25328665). Inhibits Fc-gamma receptor-mediated phagocytosis through PI3K/Akt signaling in macrophages (PubMed:25568335). Regulates TLR4 signaling in activated macrophages (PubMed:27219021). Involved in trafficking of the TGFBR1 from the endosomes to the nucleus via microtubules in a TRAF6- dependent manner. Plays a role in cell metabolism by regulating adiponecting and insulin signaling pathways (By similarity). Required for fibroblast migration through HGF cell signaling (PubMed:26445298). Positive regulator of beta-catenin/TCF-dependent transcription through direct interaction with RUVBL2/reptin resulting in the relief of RUVBL2-mediated repression of beta-catenin/TCF target genes by modulating the interactions within the beta-catenin-reptin-HDAC complex (By similarity). SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein Nucleus Cytoplasm Endosome Cell projection, ruffle Cytoplasmic vesicle, phagosome Note=Early endosomal membrane- bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF."}
{"protein": "MLRGQRLGQLGWHRPAAGLGSLMTSLMLACASAASCREVCCPVGPSGLRCTRAGSLDTLRGLRGAGNLTELYVENQQHLQRLEFEDLQGLGELRSLTIVKSGLRFVAPDAFRFTPRLSHLNLSSNALESLSWKTVQGLSLQDLTLSGNPLHCSCALFWLQRWEQEGLCGVHTQTLHDSGPGDQFLPLGHNTSCGVPTVKIQMPNDSVEVGDDVFLQCQVEGLALQQADWILTELEGAATVKKFGDLPSLGLILVNVTSDLNKKNVTCWAENDVGRAEVSVQVSVSFPASVHLGLAVEQHHWCIPFSVDGQPAPSLRWLFNGSVLNETSFIFTQFLESALTNETMRHGCLRLNQPTHVNNGNYTLLAANPYGQAAASVMAAFMDNPFEFNPEDPIPVSFSPVDGNSTSRDPVEKKDETPFGVSVAVGLAVSAALFLSALLLVLNKCGQRSKFGINRPAVLAPEDGLAMSLHFMTLGGSSLSPTEGKGSGLQGHIMENPQYFSDTCVHHIKRQDIILKWELGEGAFGKVFLAECYNLLNDQDKMLVAVKALKEASENARQDFQREAELLTMLQHQHIVRFFGVCTEGGPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFSTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERPRACPPDVYAIMRGCWQREPQQRLSMKDVHARLQALAQAPPSYLDVLG", "text": "FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Early endosome membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Recycling endosome membrane; Single-pass type I membrane protein Note=Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport. Localized at cell membrane and early endosomes before nerve growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with RAPGEF2 at late endosomes. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily."}
{"protein": "MCTPDENDYKTSTDPDTSANTNHTLEKKKRKKRKNTNVACVNCSRLHVSCEAKRPCLRCISKGLTATCVDAPRKKSKYLAGIPNRELPMSIQPDLPPRKIMIPIYNNSSNSSLNVNNMGEQQKFTSPQHIVHKAKFLSNAADSEYSILSNIIYQDTLSNKIPIDILYSNTNSTSNSTIGNSSNNSPTGTNTSPEETEMEKIRQLYSEQRANMPPHPYPSSNQNVYSILLGPNSAKIVASQVNLFANHFPLVPVDSADNSLNFKRLLPRDPSEKSSQINWDSSINQYYLNSETVTFPELAIPLKRRKNHLVSVSLESCSPDAANIKSNVGWEHSLRYSTPMEIYTSINAPFSHTPGFHHLLVYLKHRFNQQDLVKMCRSIAEFRPIFIACSVTLTEEDMIFMEQCYQRTLLEYVKFIAQIGTPTCIWRRNGQISYVNEEFEILCGWTREELLNKMTFIVEIMDDESVRDYFKTLSKVAYRDFRGSEKMKVCRLLSPIKGKIIHCCCMWTLKRDVSGLPLMILGNFMPILN", "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": "MNKISKVVVVFIALLTFLALMMQSQEVKTPGLLIQFENETSEAEVKAILENYDIPVNYTIDYNSNIGRGMYYIEVDEDKIYELRKDENWTSVVEIKKGNYNIIMLSEEFVPDENVLAMLEKNNLQLKKAVVCYIQFGDGSAPWVVGENCILERDAIRIKNELETNEKVLIVGLDDIVG", "text": "SIMILARITY: Belongs to the UPF0228 family."}
{"protein": "MDFLKPFCQYKVLKSVVVGASNQSSVVSRFFGPKITKLIYSTKVSNRDQFLDSLPRGYLDGLASGDFSKIDLLVEQLDFTSAGRLTASLSLLVLVVEEWSARSCVSFDILTELLLVPAWRKIIATAWKGRAPPSADV", "text": "SIMILARITY: Belongs to the adenoviridae E1B 19 kDa protein family."}
{"protein": "MSFIPHKLEQIKKMLDTIGASSVDQLFDEIPRHLRADTLKIKDGINEIQLANLMRKRANKNHHNINYIGAGAYSHHIPAAIWDIVARGEFYTAYTPYQAEASQGGLQVIYEFQTMMAGLTGMDASNASMYDGATALAESVLMAIRSNKKAKSQKVLIAEALHPTYLRVLETITKHQGIEFDIVNLDSKNGKTDVTKLEDFANTNYAAVVIQSPNFLGQLADVDGITNWAHKHGALVVAVTNPMSLAILKSPAEWGDNGADIVCGEGQPMGVPLASGGPYFGFMTCKMAHVRQMPGRIVGRTVDLDGNEGFCLTLQAREQHIRRAKATSNICTNQGLMVTAATIYMSLLGAEGLERVASISHENTQTLATELAKINGVSIRFNSAFFNEVVIDLPVNAETFVTEMEKEAIDAGYFLGEYHSDLANSIMVCATEIHTSEDIKEYIEATKKVLARIGG", "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": "MTDITQKMNELSVQDGGSGAGNSPGAGNGPSGGNGSRRSQYVPPHLRNRNTSSGSGFGGNGGGRGRGSFGGSNYNNAGNRDNTIFGGSGRSRDRGFGGRGGFRSNQSRPGVGRWVDGKHEPSARNERIELELFGTAEDTSFQSSGINFDNYDDIPVEASGDGVPDPITSFTAPPLDELLVENITMSRFTKPTPVQKYSVPIVAGGRDLMACAQTGSGKTGGFLFPVLSESYINGPAPIAESTGAFSSHKVHPTILVMAPTRELVSQIYDEAKKFAYRSWVKPAVVYGGADIGQQIRNLDKGCDLLVATPGRLKDLLERGRVSLANIKYLVLDEADRMLDMGFEPQIRHIVQECDMPDVQDRQTLMFSATFPTDIQMLARDFLKDYIFLSVGRVGSTSENITQKILYVEDEEKKSVLLDLLSAGDAGLTIIFTETKRMADNLADFLYDQGFPATAIHGDRSQYEREKALAAFKSGAAPILVATAVAARGLDIPNVAHVINYDLPSDIDDYVHRIGRTGRAGNVGIATAFFNRNNKNVVKGLIDLLSEANQEVPDFLAKIGRESAFGGKTGGMRGGRGGSRGPVRDFRRGASGGSSGGWGNSSGSAGGWGAAPSGGNSYNSGYSSRSNSYNSSYGSSGYGNPTSTNSWW", "text": "FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1 subfamily."}
{"protein": "MVVTKLATQRPKLPSVGRLGLVDPPAGERLAQLGWDRHEDQAHVDLLWSLSRAPDADAALRALIRLSENPDTGWDELNAALLRERSLRGRLFSVLGSSLALGDHLVAHPQSWKLLRGKVTLPSHDQLQRSFVECVEESEGMPGSLVHRLRTQYRDYVLMLAALDLAATVEDEPVLPFTVVAARLADAADAALAAALRVAEASVCGEHPPPRLAVIAMGKCGARELNYVSDVDVIFVAERSDPRNARVASEMMRVASAAFFEVDAALRPEGRNGELVRTLESHIAYYQRWAKTWEFQALLKARPVVGDAELGERYLTALMPMVWRACEREDFVVEVQAMRRRVEQLVPADVRGRELKLGSGGLRDVEFAVQLLQLVHARSDESLRVASTVDALAALGEGGYIGREDAANMTASYEFLRLLEHRLQLQRLKRTHLLPDPEDEEAVRWLARAAHIRPDGRNDAAGVLREELKKQNVRVSKLHTKLFYQPLLESIGPTGLEIAHGMTLEAAGRRLAALGYEGPQTALKHMSALVNQSGRRGRVQSVLLPRLLDWMSYAPDPDGGLLAYRRLSEALATESWYLATLRDKPAVAKRLMHVLGTSAYVPDLLMRAPRVIQQYEDGPAGPKLLETEPAAVARALIASASRYPDPERAIAGARTLRRRELARIGSADLLGLLEVTEVCRALTSVWVAVLQAALDVMIRASLPDDDRAPAAIAVIGMGRLGGAELGYGSDADVMFVCEPATGVDDARAVKWSTSIAERVRALLGTPSVDPPLELDANLRPEGRNGPLVRTLGSYAAYYEQWAQPWEIQALLRAHAVAGDAELGQRFLRMVDKTRYPPDGVSADSVREIRRIKARIESERLPRGADPNTHTKLGRGGLADIEWTVQLLQLQHAHQVPALHNTSTLQSLDVIAAADLVPAADVELLRQAWLTATRARNALVLVRGKPTDQLPGPGRQLNAVAVAAGWRNDDGGEFLDNYLRVTRRAKAVVRKVFGS", "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": "MKPAILITITSTVVLGTMIVLFSSHWFMIWVGFEMNMLAIIPILMKKYNPRAMEASTKYFLTQATASMLLMLSIIINLLCSGHWTVSTIPNPVASTMITIALTMKLGLSPFHFWVPEVTQGISLSSGMILLTWQKIAPLSILYQISPSVNSNLLLMMAITSMLVGGWGGLNQTQLRKILAYSSITHMGWMAAIMVYNPTLAILNLTIYIMMTLGTFMLFMHSSSTTTLSLSYTWNKFPLMAPLILMLMLSLGGLPPLSGFIPKWMIIQELTKNDMIIMPTLMAITALLNLYFYTRLTYTTALTMFPATNNMKMKWQFETTKKTTLLAPLIVTSTMLLPLTPMLAALD", "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": "MLDGLKMEENFQSAIDTSASFSSLLGRAVSPKSVCEGCQRVILDRFLLRLNDSFWHEQCVQCASCKEPLETTCFYRDKKLYCKYDYEKLFAVKCGGCFEAIAPNEFVMRAQKSVYHLSCFCCCVCERQLQKGDEFVLKEGQLLCKGDYEKERELLSLVSPAASDSGKSDDEESLCKSAHGAGKGTAEEGKDHKRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRQQQQQQDQQNTQRLSSAQTNGGGSAGMEGIMNPYTALPTPQQLLAIEQSVYSSDPFRQGLTPPQMPGDHMHPYGAEPLFHDLDSDDTSLSNLGDCFLATSEAGPLQSRVGNPIDHLYSMQNSYFTS", "text": "FUNCTION: Acts as a transcriptional activator by binding to an A/T-rich sequence, the FLAT element, in the insulin gene promoter. Required for development of the roof plate and, in turn, for specification of dorsal cell fates in the CNS and developing vertebrae (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGFMGEITRALISVSDKRGVVEFARRLQDFGVEILSTGGTAKALMADGVAVQEVGDYTGFPELLEGRLKTLHPKIHGGLLAKRDDSSHTRQMAEYGIPAIDLLCVNLYPFAETIASADCTLEEAMENIDIGGPTMLRAAAKNWEGVTVLVDPDDYAAVLQEMEQSYGGVGASTRFRLATKVFAHTARYDGAIANYLSSLGPDGNRTTFPQTLSLQFKKAQDLRYGENPHQAAAFYRDGSGGGLADAHQLQGKELSYNNIGDGDAAVALVMEFAEPACCVVKHGNPCGVAVGPDLLGAYQRAWAGDPISAFGGIVACNRPLDAQTAELISDQFIEMVLAPAILPDARPILAKRKNLRVLAFDDGRAWRRTGWDYKRVRGGLLVQNFDQAMEAETDWKVVSERAPTVQEARDLAFVWRVGKYVRSNAIVYGREGQTVGIGAGQMSRVDAARCGVAKALELGFDLHGAALASDAFFPFRDGIDAAAAAGVKAIIQPGGSIRDEEVIASANEHGIAMVFTGVRHFRHG", "text": "SIMILARITY: Belongs to the PurH family."}
{"protein": "MSGPVTEAARAKINLTLRVLGKRADGYHELQSLVVFAQSGDRLTAREADELRLDVAGRFAAALQGEPDNLVLRAARMLREETGIKSGAHLTLEKNLPVASGIGGGSADAAAALRALTALWGVAPGDEVLSRIAAALGADVLVCLHSRTAMMWGKGEKIMPLADLPRFWLVLANAGIALSTAAVFRELAAAPLAAAPSDPAPVPPGTLDDLAAWLAAEGNDLEPPALTLAPEIGETISALALTAGCLLARMSGSGATCFGLYAAEEEAREAALVLQAAHPGWWLEVSAAGG", "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": "MRHQRRIPQLSLPADQRKALLRGLTTQLIREGRVTTTKARAKALRNETERMITLAKDGSLASRRRAIGYVYDKQLVHALFEKAQERYGDREGGYTRIVRTTPRRGDNSEMAIVELV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MMKALVIEDIKVITTAPEGINLVAVKVTTNDPSIYGVGCATFTQRYEVVVTAIDKYLKPFLIGKDPQRIEDIWRTASVSSYWRNGPVLNNALSGIDMALWDIKGKLANMPLYQLFGGKVRDAVPAYIHADAQSVSDAVELVQTRVDQGWKQIRVQIGGYGGNNQAMHLPKDNTPGVYYDPDVYMKTMIEGFEKLREKFGDSIKLCHDVHERLSPSEAVKFANQLEKFDLLFLEDALPPEQVQWFEHLRSHTNIPLAMGELFNNPHEWTGLIQNRTIDYLRLHLSQVGGITPTRKIISLADAYGVRTAWHGPGDMTGIGHAVNTHLSITSTNFGIQEWSCSIKENTYKVFPGTPVAKDGYIYLNDQPGIGVDIDEEAAAAFPTHDRMADWTLCRLPDGSAGRP", "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": "MVEDKSQVKVKFFTREQDESLHVLDAPLFAPVSLKRYGLSEIINHLLGLAEPVPFDFLIDGQLLRCSLQDYLTRKGLSSEAVLNVEYTRAVLPPSYLKSFSNEDWVSALDVGAERIVSGSYDGVVRTWNLSGKIEKQYSGHTGAVRAVKFISSTRLVSGGNDRTLRLWKTKNDDVKHVDELEGTEEAHTLAILEGHQAPVVSVDVQGDRILSASYDNSIGFWSTNHKDMTAVDPMDSLGDKASSAAKKRRKLTMKDGSVRRRAPLSLLESHKAPVEQVIFASNDSTVAYSVSQDHTIKTWDLVTSRCVDTKSTSYSLLSMVELPKLRLLACGSSARHITLHDPRADSSAKITQQQLLGHKNFVVALDTCPENEYMLCSASHDGTVKVWDIRSSSSIYTITREDQSVEKGINDKVFAVKWAKGVGIISGGQDKKIQFNKGDNIFKN", "text": "FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family."}
{"protein": "MRHRKSGRQLNRNASHRKAMFKNMANSLFLYKTIRTTLPKAKELRRVVEPLITKAKIDSVANRRNAFSKLRDSAIVAKLFTELAPFYKDRPGGYIRILKAGFRTGDKAAMAIVQLIDLETMTDTTAGTTTS", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MINTWPSPAKINLFLYVTGIRSDGYHYIQSLFQFLNYGDTLTIIPNTKGTIELFTESNSLVNIKNSIITAAELLKEKALHSLGKKTSHFGAKIFLNKKIPIGSGLGGGSSNAATTLVVLNNLWKTKFTLQELAELSLKIGSDIPAFIMGKTTIVEGIGEILYPIHRKEKWYLIVYPNISISTKNIFSIYSIKKNTIKKPIDFLLRSRFHNDFENVIKKKFKKIKQLISMLSLYAPSRITGTGSCIFAEFNDKKSAQKIHSLLPHNVQGTIVKSVNVSPLHHAFYKKNINLFN", "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": "MSTSVFNRRWATLLLESLTRHGVRHVCIAPGSRSTPLTLSAADNHALICHTHFDERGLGHLALGLAKASREPVAIIVTSGTAAANLYPAIIEAGLTGERLVVLTADRPPELIDCGANQAIRQHALYASHPTLALDLPRPTPDIPASWLVSSVDSAMARLAHGALHINCPFAEPLYGADDGTAYQDWLIALGDWWSSREPWLREMRQSALAEQPDWPQWRQKRGVVLVGRVSPEQGARLAAWANELGWPLIGDVLSQSGQPLPCADIWLAHPDAADRLRQAEIVLQFGGSLTGKRLLQWQEQCQPQEFWLIDDLPGRLDPAHHRGRRLVADVGEWLSAHPAHKQAPWADMLVDIADKTQRQIDTHLASRFGEAQLAQRIPALLPPDGQLFVGNSLVVRLIDALAQLPQGYPVYGNRGASGIDGLISTLAGVQRATAKPMLGIVGDLSALYDLNALALLRQAPAPLVLIVVNNNGGQIFSLLPTPVAQRETFYCMPQNVEFGHAAAMFGLNYVRADNWEQLANTVTDCWAQGGVTLLEVVVEPKDGAATLNELVAQVATWAH", "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": "MRYTNVSILLGMLVIFVSPMVFADDLTPIPEGKPQVVQWFNTHVGPLAQRKGLDPALVAAEAAPRIINVNPKGGEFKTLTDAIKSVPAGNTKRVIIKMAHGEYREKVTIDRNKPFITLMGQPNAMPVITYDGTAAKYGTVDSASLIILSDYFMAVNIVVKNTAPAPDGKTKGAQALSMRISGNFAAFYNCKFYGFQDTICDDTGNHFFKDCYVEGTFDFIFGSGTSMYLGTQLHVVGDGIRVIAAHAGKSAEEKSGYSFVHCKVTGTGGGIYLGRAWMSHPKVVYAYTEMTSVVNPTGWQENKTPAHDKTVFYGEYKCSGPGSHKAKRVPFTQDIDDKEANCFLSLGYIQGSKWLLPPPAL", "text": "FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the pectinesterase family."}
{"protein": "MLDKLITELDKGLRTLCAPAHSGRAHPDQDIAEADLSAAEKKHALGLMRVNHCGEVCAQALYQGQALTARDASAREALRQAAQEEVEHLAWTERRIRELGGRPSLLNPLWYTGSLALGVAAGVLGDKWNLGFLQETERQVGAHLDSHLSALPPDDARSRAIVRQMRDDELQHAEMAHELGAAELPAPVKAAMKLSAKVMTGSSYRV", "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": "MLGKLRDLMGLTPETDIYDEEYPQGTARTLTTEPGVEPLPASPPTPTHDFDTRPSPSVATGSVPTGSTASNVIGMPNAGRWWGAVAEVLVMQPRSFSEMPEVIKALKERKSVVLNLTLMEPEQAQRSVDFVAGATFTIDGHQERIGESIFLFTPSCVQVSTQVGGVRPSATPTPTPPSAWGMDAQQHHSA", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to the division site, in a FtsZ-dependent manner. SIMILARITY: Belongs to the SepF family."}
{"protein": "MTTQLEQAWELAKQRFAAVGIDVEEALRQLDRLPVSMHCWQGDDVSGFENPEGSLTGGIQATGNYPGKARNGSELRADLEQAMRLIPGPKRLNLHAIYLESDTPVARDQIKPEHFKNWVEWAKANQLGLDFNPSCFSHPLSADGFTLSHADDSIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWIPDGMKDITVDRLAPRQRLLAALDEVISEKLDPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYVPQLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAELRKLEAAGDYSARLALLEEQKSLPWQAVWEMYCQRHDTPAGSEWLESVRAYEKEILSQRG", "text": "FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose isomerase family."}
{"protein": "MAQKRGTRLGCNDCNEINYITRKNAKKNPEKLSLNKYCSRCRGTTVHKEVKRK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MATELSLSVQYGVADARLPRWRLRRWVQYALAGAAGDGHAGLAGAELGLRLVGLAEGRRLNREFRGRDYATNVLTFEYGTGPDGVARGDIVVCVPVLAREAREQRKTLLDHAAHLTVHGTLHALGYDHIKAGEARRMEALETVVLARMGIADPYLAA", "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": "MTESVLDYMTRLGRAAREASRVLARASTAQKNRALQAAAAALDAARDELVRANELDLAGGRANGLDAAMLDRLALTPKVIDGMIEGLRQVATLPDPIGAIRDMRYMPSGIQVGKMRVPLGVVGIIYESRPNVTIDAASLCLKSGNATILRGGSEAIHSNQAIARCIQLGLAEAGLPAAAVQVVDTTDRAAVGALISMPDYVDVIVPRGGKGLIERISRDARVPVIKHLDGICHVYVDLAADVDKAIRIADNAKTQRFAPCNTMETLLVHQGIAEQVLPPLAAIYRDKGVELRGCPRTRALLGNEVLAASEEDWSTEYNAPILSIRMLDSLDEAIEHINRYGSQHTDAIVTENFTDARRFLTEVDSASVMINASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSEKYVVFGDGHVRT", "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": "MGQKTHPIGFRLGAIRGWDSNWYSETNFQDKLVEDEELRRYLHTRLKRAGLSRAVIERTPERVILTLHTSRPGVVIGRGGSEVEKLKGELETLTGKDIQINISEIKRPELDATLVAKNIVQQLEGRISFRRAMKQAMQAAMRMGAEGVRIRAAGRLGGAEMGRTEEYMEGRVPLHTIRADIDFAQETALTIYGTIGVKVWIHRGEILGKPDLSPNVQAQQRKMKESPQQRRQRRGG", "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": "MADDDVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAIIRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRDPEALFQPAFLGMESAGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEISSLAPPTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "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": "MEEFKRNLELDRSQQHDFIYPLIFQEYIYALAHDRGLNRSIFLENTGYENKSSLLIVKRLITHLITQMYQQNHFLFSGNDSNQNKFLGYNTNLYSQMIFGGFAVVVEIPFYLRLLSFLEAKERVKSHNLRSIHSIFPFLEDKFSHLVYVLDILISHPIHLEIVIQTLRYWVKDASSLHLLRFFLHEYPIWNSLITPKKSSFSFSIRNQRFFLFLYNFHVCEYESIFVFLRNQSSHLRSISSETFLERISFYRKIELEVFTKDFKAIIWVFKEPFLHYVRYRGKAILASKGTSLLMNKWKYYLVNFWQCYFYMWSQPRRIHINQLSNHSLDFLGYLSTVRLKPLMVRSQMIENSFIIGNASKKFDTLMPITPMIGSLSKAKFCNVLGHPMSKPVWAALSDSDIIERFGRIYRNLSHYYSGSLKKMSLYRIKYILRLSCARTLARKHKSTVRAFLKRLGVGLLEEFFTEEEQVFYLTFAKASSNSGELYRRRVWYLDIICINDLANYE", "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": "APIQAPEISKCVVPPADLPPGAVVDNCCPPVASNIVDYKLPAVTTMKVRPAAHTMDKDAIAKFAKAVELMKALPADDPRNFYQQALVHCAYCNGGYDQVNFPDQEIQVHNSWLFFPFHRWYLYFYERILGKLIGDPSFGLPFWNWDNPGGMVLPDFLNDSTSSLYDSNRNQSHLPPVVVDLGYNGADTDVTDQQRITDNLALMYKQMVTNAGTAELFLGKAYRAGDAPSPGAGSIETSPHIPIHRWVGDPRNTNNEDMGNFYSAGRDIAFYCHHSNVDRMWTIWQQLAGKPRKRDYTDSDWLNATFLFYDENGQAVKVRIGDSLDNQKMGYKYAKTPLPWLDSKPVPTKKKGGYASKSKAPFVASVFPVTLDKVVQVKVARPKKSRSAEEKEAEEEILLIVGIEVEIDKYAKFDVYLNDSDDPSGGKDKAEYAGSFAHLPHKHKGMKKIRTTLSLGLNEPLEDLGAEDDDTILVTLAPKVGGGVVSVDNVKVVYGS", "text": "FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o- diquinones. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the tyrosinase family."}
{"protein": "MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPVFGANSNNPDWDFNPIKDHWPAANQVGVGAFGPGFTPPHGGVLGWSPQAQGMLTPVSTIPPPASANRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQALQDPRVRGLYFPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLPVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSRSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLILGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSSFIPLLPIFFCLWVYI", "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": "MSGHPGLTTHVLDTARGKPAAGVRVQLCRVTGDTRTPVTEAVTNSDGRTDAPLIERGSLKQGTYELTFHVADYFKGFVAAADPPFLDVVTLRFTVGDTSGHYHVPLVMTPWSYSTYRGS", "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": "MDFLTLMENKLDEGRMITFEEAVELAKGKIEDEKLFLLADKLCKKNMGRRVDLCSIINAKSGGCSENCKFCAQSGHYDTGVKIYPLLDVDDVLKAAKENEKEGVHRFSLVTSGKSVSDEEFEKILGIYSVLRKETNLKLCASLGSLSYERAVRLKEAGVSMYHHNIETCREYYPKICDTHTYDDRINTVKNAAKAGLEICCGGIIGMGESMEQRIKMAFEIRELGVKSVPINVLNPIKGTPFENVRSLSPDEILRTIALFRLIMPYAHIRYAGGRMCLGEHQSKGFKAGVSAMLVGNYLTTVGNKISDDLEMIQRMGLEI", "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": "MIFMVIKKIFGENFNFNKNIDIKKIFKLDKNVKKDREENESYLDALKEIYEEIKNLEIYEKMTIGMAEIIIGYDNVEKTKKYIVIEPILTKEEIKLFLKLRKVVQALLDVPVEEIDKEKLEDYLKEKIKEIFDDLKLTLDDVTRHKLIYFLIKYLIGYGKIDALMKDENLEDISCTGVGKPVYVFHRKYEHLKTNIKFETDEELDSFCISLAQRCGKSLTLANPIVDGSLPDGSRLNVTLGRDISDMVQHLQ", "text": "SIMILARITY: Belongs to the GSP E family."}
{"protein": "MDPKKIARINELAKKKKTVGLTGPEKVEQAKLREEYIEGYRRSVRHHIEGIKIVDEDGNDVTPEKLRQVQREKGLHGRSLDDPES", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0291 family."}
{"protein": "MNWFTKLLPKISTAKKKGVPEGVWHKCPSCTAVLYRVELERNLEVCPKCYYHIRLDPRKRLAQFLDEGEQEELAEDILPVDRLKFRDSKKYKDRLSAAQKATEEKEALVVYKGNIYGNPIVAAAFNFFFVGGSMGAAVGERFAAGVEAAISERLPFVCFSTSGGARMQEGLFSLFQMAKTSAVLARLAEYKLPYISVLTDPTMGGVSASLAMLGDVIIAEPNALIGFSGPRVIEQTIRQTLPEGFQRSEFLLEHGAIDMVVDRRELKSTIASLITKLTHQPPPDLPVEESV", "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": "MAKVCYFTGRKTVSANNRSHAMNKTKRVAKPNLQKVTVLIDGKPKKVWASARALKSGKVERV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MSKIIRSSDESRGALENGVNSLADAVKVTIGPKGRNVVLEKKFGAPDIVNDGVTIARDIELENPFENLGAKLIEQVASKTKDKAGDGTTTATVLAQVMVHEGLKNTAAGASPIEIRRGMEKAVSHIVDKLQQQSKKISGDKVLQVATVSSGGDEEIGAMVAEAMDKVSVDGVITVEESKSLNTELEITEGMAFDRGYSSPYFVTDAERQICEFENPLLLITDRKISSIADLVPVLETVQKSSSPLVILAEEVDGEALATLVVNKNRGVLQVASVRAPSFGERRKAALADIAVLTKGTLISEDKAMTLDKVSLADLGKARKITITKESTTIVANDDTKKEVASRVASIKRELDQTDSDYDKEKLNERIAKLAGGVAVIKVGAPTETELKNRKLRIEDALNATRAAVEEGIVAGGGSTLIKLGEELDSLSKSLDGDQATGVDIIKKALSAPAKQIALNAGENGDVVVSEIQRLGKGFNAATGQYEDLISAGIIDAVKVIRLALQDAVSIASLLITTEVIIADKPEPPSPAGGEGGGDPMGGMGGMGGMGGMGMPGMGGMGMPGMM", "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": "MLDQISLEIPKGTIYGLVGHSGAGKSTLLRTINGLEGFDEGELWVDGVDLQSLQGDALRVFRKNIGMIFQHFSLMARQNVFENVALPLRCWKYPEAEIQKRVFNLLSLVGLESKSDSYPSALSGGQKQRVAIARALTLEPQILLSDEATSALDPSMTQSILDLLQTINQELGVTVVLVTHEMEVVKKLCHHAAFLEGGKLLRSGNIEELFLQPDPKMRHFLGESEVLPKEGVNIRLYFPKEVAQNPIITQMARQLSLDFSIVWGKLERFGEDVLGSLVINIPEARQEEAERFLESSGVRWEVL", "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": "MPITANTLYRDSFNFLRNQLAAILLLALLTAFITVMLNQAFIPDTEQLSILSSTESDFASSGNLSITELVAQLTPEQQIILLKVSAAATFSALVGNVLLVGGMLTLISMVSQGRRVSALQAIGISVPILPRLLLLMFIGTLLIQLGITLFIVPGIIIAVALSLSPIIVSTEKMGVFAAMKTSVKLAFANVRLIIPAMMLWIAAKLILLYLVNHLTALPTPIASVVLSALSNLVSALLLVYLFRLYMLLRPTDITV", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0259 family."}
{"protein": "MSRPRLLPEPVGLKFVTQETPPDWDAEFGFSGPLELEIGSGAGGHALEYCRRHPEVRFVAFEWRKKYARDTQDRADKAGLRNLRVIESDARFIVPRIFAPDSLAAIHLQFPDPWWKRSHAKRAVIQPAFAELLYGKLAPGGLFDMRTDVQDRGVTMLAILESVGFKNPLGSGVFHPYDPEEVPSTRERRYLASGEPVYRARLLKPA", "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": "MSQALRIVFAGTPEFAAEHLKALLDTPHRIVAVYTQPDRPAGRGQKLMPSAVKSLALEHGLPVMQPQSLRNAEAQAELAALRADLMVVVAYGLILPQAVLDIPRLGCINSHASLLPRWRGAAPIQRAVEAGDAESGVTVMQMEAGLDTGPMLLKVSTPISAADTGGSLHDRLAALGPKAVVEAIAGLAAGTLHGEDQDDALATYAHKLNKDEARLDWSRPAVELERQVRAFTPWPVCHTSLADAPLKVLGASLGQGSGAPGTILEASRDGLLVACGEGALRLTRLQVPGGKPLAFADLYNSRREQFATGQVLGQ", "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": "MHDDIKLVSGEEIVKPTGEVHVVYFSSISNNTHRFIQKLSVKNSRIPYELEEEINVDSDYVLITPTYSGGGEFTSGAVPKQVIKFLNKENNRNYCRGVIASGNTNFGNTFAMAGPILSKKLNVPLLYQFELLGTQNDVEKINEILKEFWGK", "text": "FUNCTION: Probably involved in ribonucleotide reductase function. SIMILARITY: Belongs to the NrdI family."}
{"protein": "MTDKTSNQMWGGRFAAGPDAIMEAINASIGFDKRLAAQDIAGSRAHAAMLAATGVITDSDAEAIREGLLTVLSEIEAGEFTFSTALEDIHMNVEARLKEIIGEPAGRLHTARSRNDQVATDFKLWVRDQFDAAEAGLLALLRALLGQAEAGADWVMPGFTHLQTAQPVTWGHHMMAYVEMFGRDLSRVRDARARMNESPLGSAALAGTSFPIDRHMTAAALGFDRPTANSLDAVSDRDFALEFLSVASICAMHLSRFAEELVIWSSAQFRFVTLSDRFSTGSSIMPQKKNPDAAELIRAKVGRIFGANTALMMVMKGLPLAYSKDMQEDKEQVFDAADNWMLALAAMEGMVRDMTANRDSLAAAAGSGFSTATDLADWLVRVLGLPFRDAHHVTGALVALAESKGCDLPDLSLDEMQSAHAAITEDVYGVLGVENSVNSRQSYGGTAPAQVRAQVARWKEMLA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MTFVIADRYELGASIGSGGMSEVFAATDLLIGREVAVKMLRTDLAKDVNFRERFRREAQNAGKLSHPSIVAVFDTGEVDRDGISVPYIVMERVHGRDLRDIVREDGPYSPSQAATIMIPVCHALQSSHEAGIIHRDVKPANIMINNTGGVKVMDFGIARALDDSTSAMTQTAAVIGTAQYLSPEQARGKPADARSDVYAAGCVLYELVTGRPPFEGESPFAVAYQHVQEEPTPPSEYISDLSPTAALNVDAVVLTAMAKHPADRYQTAAEMAADLELLSRNAVSRAARAHVEKPDEPETVVVPQRLSTPPPPPTPAMPAATVAAPAAAPTAVGSRPAAARQPKRGSRALTVLAIVLTLGVIGVGGAFTYDFLSNSSSASTQQIPNIVGLPENEAVLELERLGFTVVLTTEPSPDVAEGLVIRTSPNVGSEIREGATVTLTISSGREVVTIPDVTGLTLAEATREIEGAGLVLDQSIREENSDDYPAGTVIQQNPRAGGETSVGASITLTVSTGPSLVRVPVITGMQWSQAESNITSLGLVPDIYYVDSLLPEGQVISASGQGTELPRGSTVTVEISNGMLIEAPDLARLDVDNALKALRDAGWTAPDTSLIEGAPIPTGALVDQGRIGFQDPSPGQPLRKDAVVNIRLYRFDLTALVPEP", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MLLASAVVVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQVDSRLAPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSAPGKGVVWEWENDNGSWTPYDMEVGITIQYAYEKQHPWIDLTSIGFSYIIDFSTMGQINRQTQRQRRVRRRLDLIYPMVTGTMPKTQSWPVSPGPATSSPAPPCSCPQCVLVMSVKAAVVHGGTGPPAVRKNMALSGVGKLPQPPGPGAKPLDTTGTIRGPGKTAPSQVIRRQVSNAPAGATVGSPASPQGSNRKTGRVALATLNRSNLQRLAIAQSRVLIASGVPTVPVKNLNGSSPVNPALAGITGILMSAAGLPVCLTRPPKLVLHPPPVSKSEIKSIPGVSNTSRKTTKKQAKKGKTPEEVLKKYLQKVRHPPEEDCTICMERLTAPSGYKGPQPTVKPDLVGKLSRCGHIYHIYCLVAMYNNGNKDGSLQCPTCKTIYGVKTGTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFSARGFPRHCYLPDSEKGRKVLKLLLVAWDRRLIFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQGISEDSTSHEKD", "text": "FUNCTION: Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 requires interaction with NLRP4 (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Deltex family."}
{"protein": "MRLTDIEIEQCLDNGTIIIDPRPGIEAISGVSVDVRLGSQFRVFKDHTAPYIDLSGPSAEMQIALDRIMSDKIEIADDQAFFLHPGELALAVTYESVTLPADIVGWLDGRSSLARLGLMVHVTAHRIDPGWQGKIVLEFFNSGKLPLALRPGMTIGALNFERLSSAVARPYNTRKSSKYKDQQEAVASRISQDK", "text": "FUNCTION: Catalyzes the deamination of dCTP to dUTP. SIMILARITY: Belongs to the dCTP deaminase family."}
{"protein": "MTRLTDLGVTDLRDGIAKGDFSAKEVAESFLTATNEAEKLNAFITLTPDHALKQAEKADKDRASGQLKPLSGVPLGIKDLFCTNGYRTTAASKIIDNFVPPYESTITEKLFSAGAGMVGKLNLDQFAMGSSNETSAFGNVISPWRQKGDDTALTPGGSSGGSAAAVAAKLVPAATGTDTGGSIRQPASFTGITGLKPTYGRCSRYGVIAFASSLDQAGPMAHSVKDCAALLEVMAGFDPKDSTSVDVMVPNWEKLLSSDIRGKKIGIPKEYRVDGMAPEIESLWQRGIDMMKDAGAEIIDVSLPHTQHALAAYYIIAPAEASSNLARYDGVRYGERKTPEGGNLADMYAATRAAGFGDEVKRRIMIGTYVLSAGFYDAYYIKAQKIRALIARDFEAAFDKCDILLTPATPTAAFALGQKQEDPIAMYLNDVFTVPASLAGLPAMTVPVGLNEQGLPLGLQLIGKPLDEQSVLNAGLALEERAGFTSQPKKWW", "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": "MGPTSLLSFFFTFLTLFHGFTAQQWPNECQLDQLNALEPSQIIKSEGGRIEVWDHHAPQLRCSGFAFERFVIEPQGLYLPTFLNAGKLTFVVHGHALMGKVTPGCAETFNDSPVFGQGQGQEQGQGQGQGQGQGFRDMHQKVEHLRSGDTIATPPGVAQWFYNNGNEPLILVAAADIANNLNQLDRNLRPFLLAGNNPQGQQWLQGRQQQKQNNIFNGFAPQILAQAFKISVETAQKLQNQQVNRGNIVKVQGQFGVIRPPLRQGQGGQQPQEEGNGLEETLCTMRCTENLDDPSSADVYKPSLGYISTLNSYNLPILRFLRLSALRGSIHNNAMVLPQWNVNANAALYVTKGKAHIQNVNDNGQRVFDQEISKGQLLVVPQGFAVVKRATSQQFQWIEFKSNDNAQINTLAGRTSVMRGLPLEVISNGYQISPQEARSVKFSTLETTLTQSSGPMGYGMPRVEA", "text": "FUNCTION: This is a seed storage protein. SUBCELLULAR LOCATION: Rough endoplasmic reticulum. SIMILARITY: Belongs to the 11S seed storage protein (globulins) family."}
{"protein": "MKIILASKSPRRIELLKLLKIDFEVIPSNIDENISEKDPKLLAEKLSYLKAMSIKKDGVVLAADTVVTLDKEIFGKPRDYKDAFRMLKSLSGKWHTVITGVTIKFKDEVITFSEKTNVKFKNLSKELIEFYINTAKPFDKAGGYGIQELGSVLVEKIEGDYFNVVGLPISKVWDILWDRGMIDASKGEINK", "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": "MRVSALLLVTLRDDPAEAEIPSHKLLLRGGYIRRVASGIYAYLPLMWRVLRKVSAIVRQEMDAAGALETLLPQLQPAELWQRSGRWSGYTAGEGIMFHLQDRQDRELGLGPTHEEVITALAADLLRSYRQLPVNLYQIQTKFRDEIRPRFGLMRGREFIMKDAYSFHASAEDLGRGYAAMDQAYRRIFSRCGLQVVAVQADSGAIGGSASQEFMVTAEAGEDLILSSADGSYAANQERAESLPAEPVPLQSATAAELDTPGQTSIDALVEAQGWHASQLVKVILLVARFEQGRQQPLLVSLRGDQQLNEVTLANWLNQQHGQAWGALLGIEPLEAKHLAAEKVPAFGYLGPDLSDAVLQGSKKLESSFLRLADPTALDLPLFICGANRFNAHRLAANWSEPGMASPQRVELRAALPGDRCCHDPSQQLQARRGIEVGHIFQLGLKYSEALGATFANEQGQDAPLWMGCYGIGVSRLAQAAVEQHHDSAGMVWPVPIAPFEVVIVIASSKEAQQVELAEDLYGQLQQAGVDVLLDDRNERAGVKFKDAELIGIPWRLVVGRGAVNGQVELVERCSGEKQEGPHQDLMAQLLQTLDQQRQGL", "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": "EFTISFSSPVISTGQHIDVGDEDYHDGDDDVDYTDDVDDVDDSHGSPSQLLQGGYQRNQHYGGGNYQSGYYRPNKQHGNGYGGQYPKKYGSGHKY", "text": "SIMILARITY: Belongs to the immunogenic miracidial antigen family."}
{"protein": "MKPFNELVQHFSDAQGRAALLGMLRGIEREALRIDESGYLALDGHPLELGSALTHSRITTDYSEALLEFITPVNHQVESLLQGLTETHAYSVRHLHGQRLWPVSMPCYVKDEANIPIARYGTSNTGKMKTLYRKGLTYRYGALMQIISGVHFNFSVSQELWQSLYELSDKSLSFDDFISESYFGLIRNYRRLVWVLPYLFGASPALCNSFIKGQKTDLRFEKSGRGTLYLPYATSLRMSDLGYTNKEQADLNISYNSLPEYLAGIRAAIKMPSANFANIGVKVDGEYRQLNANVLQIENEFYSPIRAKRVTKSGEKPSEALARAGVEYIEVRALDVNPFSPIGIEASQVRFLDLFLLYCLLTPSPKSDAAEEARLSANLKSVVLEGRKPGLELHTATGTLSLQTWLLELFDNLSSLAVLLDGETNAYQAALAHWRDAVVDPQKTLSGQVLQQLVTKGQDHGQWVMSLAQQYHQYFIDYPLSSEAASDYDAEAQSSLAKQVELEAAQSAVSLDDYLTDYFGAPA", "text": "SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily."}
{"protein": "METISNPQELQNLCLMLRAEGKKIGLVPTMGYFHEGHLSLMDAARKQCDVLIVSLFVNPTQFGENEDLDAYPHNLERDSELAEKRGVDILFTPIRDDMYFEDHSTWVEVPDLATNLCGKSRPIHFRGVATVVTKLFMTAQPHVAVFGQKDWQQLAIIKRMVRDLNIPVDVQGHEIVREESGLALSSRNVYLTEDEKSVAPNIQKGLQKMRDWVTAGESDAAKLKSDLVEFYAETIPTGRVDYIEIVHPENINILKNVGDSALCAVAIQLGNARLIDNLLIKV", "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": "MPDSTIPLLCVLGLLALSSACYIQNCPRGGKRSFPDLKRPCMSCGPGNRGLCFGPSICCGEGMGCYMGSPEAASCVEENYLTSPCEVGGRVCGSEEGHCAAPGVCCDAESCLLDSDCLDDSKRQPPSEQYSSLMEGLAGDLLQWMLHATRRERPQ", "text": "FUNCTION: Vasotocin is probably an antidiuretic hormone. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vasopressin/oxytocin family."}
{"protein": "MSQLCPCGSAVEYSLCCQRYLSGNQLAPDPVQLMRSRYSAFVMKDADYLIKTWHSSCGVAQLRDDIIAGFAHTEWLGLTVFDHALTTDGKTGYVSFVARYSERGRAGAIIERSRFIKENGQWYYIDGTRPQFGRNDPCPCGSGKKFKKCCGQ", "text": "SIMILARITY: Belongs to the UPF0225 family."}
{"protein": "MANVMKAPKRQLTYVTDLNKCIGCQTCTVACKKLWTTGPGQDFMYWRNVETTPGLGYPRNWQTKGGGYKNGELQKGKIPPMIDYGIPFEFDYAGRLFEGKKERVRPSPTPRSAPNWDEDQGAGEYPNNSFFYLPRMCNHCTKPACLEACPNEAIYKREQDGIVVIHQDKCKGAQACVQSCPYAKPYFNPVANKANKCIGCFPRIEQGVAPGCVAQCVGRAMHVGFIDDTNSSVHKLIRLYKVALPLHPEFGTEPNVFYVPPVLGPRMELPNGELSTDPKIPLAQLEGLFGKQVRDVLAILQTEREKKMKGLASDLMDVLIGRRSADMMISPLT", "text": "FUNCTION: Component of the perchlorate reductase that catalyzes the reduction of perchlorate to chlorite and allows anaerobic growth on perchlorate as the sole electron acceptor. The beta subunit may be responsible for electron transfer to the catalytic alpha subunit PcrA (Probable). SUBCELLULAR LOCATION: Periplasm Note=Probably translocated together with PcrA, which possesses a Tat- type signal."}
{"protein": "MEGSGGGAGERAPLLGARRAAAAAAAAGAFAGRRAACGAVLLTELLERAAFYGITSNLVLFLNGAPFCWEGAQASEALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPATRAALCGSARLLNCTAPGPDAAARCCSPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFVTGYAIPTVCVGLAFVVFLCGQSVFITKPPDGSAFTDMFKILTYSCCSQKRSGERQSNGEGIGVFQQSSKQSLFDSCKMSHGGPFTEEKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLRIPEISNITTTPHTLPAAWLTMFDAVLILLLIPLKDKLVDPILRRHGLLPSSLKRIAVGMFFVMCSAFAAGILESKRLNLVKEKTINQTIGNVVYHAADLSLWWQVPQYLLIGISEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGVGSFVGSGLLALVSIKAIGWMSSHTDFGNINGCYLNYYFFLLAAIQGATLLLFLIISVKYDHHRDHQRSRANGVPTSRRA", "text": "FUNCTION: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response (PubMed:16289537, PubMed:25238095, PubMed:29224352). Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (PubMed:29224352, PubMed:31073693). Transporter activity is pH-dependent and maximized in the acidic lysosomal environment (By similarity). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand (PubMed:25238095, PubMed:29224352). Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs) (PubMed:25238095). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (PubMed:32433612). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation (By similarity). Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
{"protein": "MARLSRERYAQLYGPTTGDRIRLADTDLLVEITEDRCGGPGLAGDEAVFGGGKVLRESMGQGRVTRAEGAPDTVITGAVIIDYWGIIKADIGIRDGRIVAIGKAGNPNIMSGIHPDLVVGPSTEIIGGNGRIVTAGAIDCHVHLICPQVIAEALGSGITTIIGGGTGPAEGSKSTTVTPGGWHLARMLEALDSWPVNIALLGKGNTVNPDALWEQLRGGASGFKLHEDWGSSPAAIDACLTVADAAGVQVALHSDTLNEMGFVEDTLAAIAGRSIHTYHTEGAGGGHAPDIITVAAHPNVLPSSTNPTRPHTVNTLDEHLDMLMVCHHLNPRIPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRVGEVVMRTWQTAHVMKQRRGALEGDPSGRYSADNNRARRYVAKYTICPAVAHGLDHEVGSVEVGKLADLVLWEPAFFGVRPHAVVKGGAIAWAAMGDANASIPTPQPVLPRPMFGASPAVAAATSVHFVAAQSIEAGLADQIAVDRRLVPVADVRAVGKADMPLNDAQPRIEVDPDTFTVRIDGEVWEQQPATELPMAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "MSIKRSAVHTLALLAAAIFGVVLLLGAIHKDIGFMQMAAVLAVLAIGLFLLTLATAFTTKERLFMAVIYILIACTFLNNAFFAIHLGFFSLFLYRLLLIAAGCLHIFGMVRNRTHIERWHGLQVKGILLFFAFWFIYGLVSLLWAKSVTVGLKYLALLAMGIFFIYLIVMYVQKMERLMIVYAIWLVMTVFLMIIGFYNHITHHHLASSTLYSGPEYKQHYPTSVFFNQNDFATFLSISFFFYITMMKNIKNGYIKAIGLVLSLCALYLIFATGSRASLLGIFAGIAVYIFIVLPPVLKRMAIWLSAAGIALFAVLFASKIYSKFWELFLAPQTLHSFHDRLPSNVARANLLKNAWHFFLDSYGFGVGAGNVSYYLEHYAVYDTDNVAEVHNWLVEILANFGLFIMLGYLSVYAYLIWVLYKFYERKLENQSKLITEGLITAMVSFLVSSISPSSVSNLFFHWVFMALVIAAVNVLRRSRQMPEPMYR", "text": "FUNCTION: Might be involved in the polymerization of teichuronic acid repeating units after their translocation to the outer surface of the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MLKPLGDRVVVQLKEEKEQTVGGFVLAGASQEKTKKAQVVAVGEGVRTLTGELVASSLVQGDTILIENHVGTPVKDDGKDCLIIREADVLAVVND", "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": "MKSTVEQAMLFEEKSIFENQAIEQGYSQVAGVDEAGRGPLAGPVVAGACILPRGKVFLGIDDSKKLTPKQRRYLYELLLEDPEVDCGVGVISVERIDEINILEATKEAMVQAIASLRSTPDFLLVDGLFLPHKIPSLKIIKGDARSVSIAAASIIAKEYRDELMRKLHVEYPEYGFDKHKGYGTAAHLQALKHFGPCVYHRKSFSPVKESIQEGVCQ", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MFKTNVEQNNVPVFGSFESGQDLPEKRMNKESVDPRIAYQLVKDQLIDEGSARQNLATFCQTYMEPEAEQIMAETMEKNAIDKSEYPQTAKLESSCVNMLADLWNVDESEHYMGTSTVGSSEACMLGGMAMKFRWRSAALKNGLDIHAKKPSLVISSGYQVCWEKFCVYWDIELREVPMSEEHLSINTDIIMDYVDEYTIGIVGILGITYTGKFDDIMTLNDLVEDYNNTHDNEVVIHVDGASGAMFTPFVEPGLEWDFRLPNVVSINTSGHKYGLVYPGVGWILWRDKEYLPEELVFDVSYLGGHMPTMAINFSRSASQIIGQYYNFLRFGYEGYRQIHMRTRDGALQLSQAVAETGLFEIYNDGANLPIVCYKLKDDANVAWTLYDLADRLQMKGWQVPAYPLPKEMGNTIIQRYVCRGDLGQNMVTAFKNDLSESIEELNNAHILYHDVNTSKTHGFTH", "text": "FUNCTION: Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance in gastric fluid. SIMILARITY: Belongs to the group II decarboxylase family."}
{"protein": "MARITPLDRYRNVGIMAHIDAGKTTTTERILLYTGRTHKIGEVHDGGATMDWMEQEQKRGITITSAATTCFWKGMDKQFEDHRINIIDTPGHVDFTIEVERSLKVLDGACAVFCAVGGVEPQSETVWRQANKYNVPRIGFVNKMDRAGADFLRICEQIKTRLGGNPVPMQIAIGAEENFEGVIDLISMRAIFWNEADQGATYETRDIPAELQELAEKKREFMIESAAEANDELMEKYLEEGELSHDEIKEGIRSQTIKSEIIPMFCGSAFKNKGVQVVLDAMIMYMPSPLDVDAIAGILNDKDEAVASRNVGDDEPFAALAFKIATDPFVGNLTFFRVYSGVLKAGDFVYNSSQGKKERIGRMVQMHANEREEIKEVRAGDIAAAIGLKDVTTGDTLCDLKQKIVLEKMEFPEPVIALAVEPKTKEDQEKMGIALGKLAAEDPSFRVSTDEESGQTIIAGMGELHLDIIVDRMVREFDVECNVGAPQVSYREAITTMVEHQYKFAKQSGGRGQYGHVYLRIEPQEPGAGYEFVDEIKGGVIPKEYVPAVNKGIQEQIKNGVLAGFPIVDIKVTVYDGSYHDVDSNEIAFKIAASKCLSEGVRMANPQLLEPMMAVEVSTPENYMGDVIGDINRRRGIVSAMEDTPTGKQIKAEVPLIEMFGYANDLRSMTQGRASYSMEFKKYTAAPKNVADEVIEKLNK", "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": "IIFSMWLLFSFSESTEYIAGDSESSWKVNFPSREALIDWATRHQFTYSDTVVNEDEDHDCNTKIHSKLGDMVVTKRPLVLPPLITLPLSPSPAPAPNTSGAAAGCGFMAFLEVSVAMLMFLIWL", "text": "FUNCTION: Involved in the infection process during the plant-rhizobium interaction."}
{"protein": "MDFYSNLDSRSLDSETPTLFEIISAQELEKLLTPSIRYILVHYTQRYPRYLLKVANHFDELNLAIRGFIEFRQLSHWNSTFIDKFYGLKKVRNHQTISTERLQSQVPTLLEQRRRLSKTQIAVSLFEIVGVPYLRDKLDHLYDKLYPKLMMNNLDPKESLKTFVQYYFLKLYPILLSVLTTIQVLLQVLYLSGTFKSPSIIMWLFKMKYARLNSYDYTLDEQRVNKFLNKTSPGKLGTGNNRIRPITLTESLYLLYSDLTRPLKKGLLITGGTLFPASIFLLKFLEWWNSSDFATKMNKPRNPFSDSELPPPINLSKDLLADRKIKKLLKKSQSNDGTCPLCHKQITNPAVIETGYVFCYTCIFKHLTSSELDEETGGRCPITGRRLLGCRINKTTGEWTVDGIRRLMM", "text": "FUNCTION: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 and/or PEX20 receptors from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 recycling (PubMed:23344950). 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 and/or PEX20 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 and/or PEX20 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (By similarity). When PEX5 or PEX20 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5 and/or PEX20, leading to its subsequent degradation (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the pex2/pex10/pex12 family."}
{"protein": "MTNIRKSHPLIKIINESFIDLPAPSNISAWWNFGSLLGVCLILQILTGLFLAMHYTSDTATAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHIGRGMYYGSYTFSETWNIGILLLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAAVHLLFLHETGSNNPSGLTSNSDKIPFHPYYTIKDILGLLLLIMALMLLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVVALVLSILILAVMPLLHTSKQRSMMFRPLSQCLFWLLVADLLTLTWIGGQPVEHPFITIGQLASILYFFTILVLMPISSMIENRFLKW", "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": "MMKFAFKIAYFGDNFHGSQFQPDQRTVEGEVINALRRLGVENPRLRSAGRTDAGVHAYGQVISFYSEDKIFPRMLNAELPEDITAWAWAKVSEDFDPRRAKSRVYTYVMYGSDYDISAMRKAVKELIGVHDFSNFTKKFGEGESCVREIISADIRADREFIIFEIEGNAFTWNMVRCIVTAIMEIGKQHRSIEWFRDLLNPEKHKERVEPAPPYGLILKDVKYDDVEFEIDDYAFKTLQSRIEDRIIYHGTIFKLFSLFRQSGIS", "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": "MHPHLDVNNQKQCADLIRALEECHKSFGKFFGECNTIKYELKACLTKDRNDKARLNRENARMRKKVIEENRKKEEIEERILTDRILQQERKKSHANEGAGDNNN", "text": "FUNCTION: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Note=Imported into the mitochondria via the mitochondrial mia40-erv1 machinery. SIMILARITY: Belongs to the CMC family."}
{"protein": "MNLQEMNARKEKIRNFSIIAHIDHGKSTLADRILEQTETVSKREMQAQLLDSMDLERERGITIKLNAIELNYKAKDGETYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPEMVRQEIEDVIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPQGEVDAPLKALIFDSVYDAYRGVILQIRVIDGSVKVGDRIQLMSNGKEFDVTEVGIFTPKAVSRDFLMAGDVGYVAAAIKTVADTRVGDTVTLASNPATEALEGYKEMNPMVFAGIYPIESNKFNDLREALEKLQLNDASLRFEPETSQALGFGFRCGFLGLLHMDVIQERLEREFGIDLIMTAPSVVYHINTTDGETLEVANPSEFPDPTRIENIEEPFVKAQIMVPNDFVGPVMELAQRKRGIFLTMDYLDANRVNIIYHIPLSEIVFDFFDKLKSSTKGYASFDYEISDYRPSNLVKMDILLNAEKVDALSFIVHKDFAFERGKVIVEKLKKLIPRQQFEVPIQATIGNKIVARSDIKALRKNVLAKCYGGDISRKRKLLEKQKAGKKRMKAIGSVEVPQEAFLSVLSMDEE", "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": "MSDMRLIVAGAGGRMGRTLIHALHEADGAALVGALEAPGSELLGQDSGLLAGLGPNGIPVSADLWSLSKDADGIIDFTVPAATIANVAIAAERGIVHVIGTTGLSASDNAVIKSVTSRAIVVQSGNMSLGVNLLAALVKQVAKSLDEDFDIEILEMHHRAKIDAPSGTAYLLGQAAADGRGVPLEEKSVRSRDGFTGARGRGDIGFATLRGGTVTGEHSVIFAGPYERIELTHRAEDRMIFARGAVKAACWARGRKPGLYSMADVLGLGSQS", "text": "FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapB family."}
{"protein": "MSGALNMTLDEIVKRGKTARSGGRGISRGRGRGRGGGGRGAGPARRGPLAVNARPSSFTINKPVRRVRSLPWQSGLFEDGLRAAGASGVEVGTRLHVTNLDQGVTNEDIRELFSEIGEVERYAIHYDKNGRPSGTAEVVYPRRSDAFQALKKYNNVLLDGRPMRLEILGGNNSSEAPLSGRVNVNVTGLNGRLKRTVVIQQGGGGRGRVRGGRGGRGPAPTVSRRLPIHNQQGGGMRGGRGGFRARGRGNGGRGRGGGRGNGKKPVEKSAADLDKDLESYHADAMNTS", "text": "FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA (PubMed:11432957). Plays a role in disease resistance. Mediates multiple defense responses triggered by NEP1, including stomatal closure, hypersensitive cell death (HCD) and defense-related gene expression (PubMed:24723400). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the ALYREF family."}
{"protein": "MPSLEVKLRKAVLAATDGKLRSDNWQYIIGVCDLVKEDPEDASQIVMEMIEKRLGQNDANVMLRSLALVVALAENCGSRLKQQVSSKHFTGILAQLLESGDVHMTVKKEIAKVVKQLSDSFKSDPSLKTMGDLNTRIRRKWPGLLEEPEKPSKQKVSHQEATDEDQELQRALKMSLEEFEKSKQQSNGSAVQSNSLQDHNQGQQQPQQQTTSGIRRVRALYDLNANEQDELSFRKGDVIVVLEQVYRDWWRGSLHGKIGIFPLNYVTPITEPSPVESQREQQIEEGVLSQAQNVQVLSAKMQMASGKGLSELNQDPEFNDLYSTVTPIRPHVTKLIGKYAKEKDDVIALRQVLLNAESTYNELLDRAAKSYSIPNTQAPPYAPAVTSQPGYVSNNTYQTTNGQYTQHNITPQQQYQVPSQNYQSQPPSMQSNHYIGYQHPGINDQPPPNY", "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": "MRTTNYLLSTQKEAPSDAVIVSHQLMLRAGMIRKLASGLYTWLPTGLRVLRKVETIVREEMERAGGVEVLMPIVQPADLWLETGRWDQYGGELLRIKDRHTRDFVLGPTHEEVITELVRKEVNSYKQLPLNLFQIQTKFRDETRPRFGVMRAREFTMKDAYSFHMDQACLEKTYQKMFDAYCRIFDRLGLEYRPVIADTGSIGGSASHEFHVLAQSGEDAIVFSTESDYAANIEKAEALAPSTVLAAPTAEMGLLDTPNAKTIAELVSKHGIAIEKTVKTLFVKASDQIETELIALIIRGDHELNEIKAENLASVAAPLEFASESEIRALVNAGPGSLGPVSLPVPFIVDRSVAVMSDFSAGANIDNKHYCNINWGRDVELAQVEDLRNVVEGDPSPCGSGTLSMARGIEVGHIFQLGDTYTKAMNAGVLNQQGKNQILTMGCYGIGISRIVAAAIEQNNDKNGIIWNNTLAPFSVVIVPMNMHKSHRVAELAEKYYAELQAAGIEVLFDDRKERPGIMFADAELMGIPHTLVIGDRSLDNGVIEYKDRLSGVKQEVAIDEVINFIKAQLA", "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": "MSITGQPHVYKKDTIIRLKPLSLNSNNRSYVFSSSKGNIQNIINHLNNLNKIVGRSLLGIWKINSYFGLSKDPSESKSKNPSVFNTAKTIFKSGGVDYSSQPKEIKSLLEAQNTRIKSLEKAIQSLDEKIEPEPLTKEEVKELKESINSIKEGLKNIIG", "text": "FUNCTION: This protein is involved in virus transmission. SIMILARITY: Belongs to the caulimoviridae ORF II family."}
{"protein": "MFGLSVNHAYAGPGIFINDGTDDGCIWTFDKEDYSPIGDYFGNTAPADKDSAGRNSPASVKYHIPSIQQLGGAATLKCLSKDRDTQTDRVLFYGNSKEQGSISLTLGGELFVNNGNLGLGGGTDTKAMRIGSMATLTGPSGLRSLAIGAGEIATVASGDDAIAIGTAAQAAHVGSIALGLQSTTELPSLVKDVTINGIKLSAFAGSNPASVLSIGNDTLKRSITNVGAGRVSKDSTDAVNGRQLFAVSEQAASGWSLTVNGMDKSRVGPGDTVDLSNSDGNLVLSKKGKDVTFNLASDLKVTSLVAGNTFLDTNGLVITGGPSMTVSGIDAGQLKISHVADGAVTVTSTDAVNGSQLHRVAHTIAEHLGGDAHVNADGSVIGPQYTVQKKRYKTIYDAFGGVDENLANINDILHDIESGGGIKYFHANSIGADSRALGTNSIAVGSDSVASGEGSISVGNGAQASAHGSVALGENAAAPDANSVALGAGSKTSEVVATKGTTINGQYYDFAGDAPSGTVSVGDKGAERTITNVAAGRISVESTDAVNGSQLNAVNQAIENLAAGVTENDKFSVKYDRHSDGTKKNSMTLQGWDSATPVVLANVADGVHKNDAVNVSQLKAGLSTTLGEAKAYTDQTALQTLDQANAYTDKKFGKLNEDIVATRIEARQAAAIGLAAASLRYDDRPGKISAAIGGGFWRGEGAVALGLGHTSEDQRMRSNLSAATSGGNWGMGAGFSYTFN", "text": "FUNCTION: Binds to hyaluronic acid and epithelial cells, and is required for full virulence in the mouse model. 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:23319562). SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family."}
{"protein": "MDLGKVITAMVTPIHPEKDKVCKKRIHHLVNHLIENGSDGLVIAGTTGESPTLSHDEKIKLFRQVIETNDGRAKLIAGTGSNNTAETIAFTKEVAELGGIDAVLIVAPYYNKPNQDGLYAHFAAVAEASDLPVVIYNIPGRSVVNIEPETIIRLAALPNIVGVKESSGNLDNISKIIAETSDDFQVYSGDDSLTLPILAVGGNGVISVASHVVGNEMQEMIQAFERGEVQKAAQIHRELLPLMNGLFSVPNPAPTKYLLNQQGISVGPVRLPLVDLNAEQGTKLQAILEGLSK", "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": "MTRPLSYFHLHLISDATGETLLAAGRAAAAQYANARAIEHIYPLIRTEKQLRKVLEGIDAEPGIVLYTIVDQKLAAIIDDSCAEMGVPSVSVLEPVLNTFQSYLGAPAHRRASAQHVLNADYFRRIDALNFTMEHDDGQLPYDIEEADVILVGISRTSKTPTSIYLANRGIKATNVPIVLGIPLPEVLFTAKRPLIVGLVATAERISQIRQNRPLGNVPSLDTGLYTDRVSISEELAYARNICNRNGWPIIDVSRRSIEETAAAILALLRAHNEKG", "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": "MGDLWLFLLLPLSAFHGVKGCLECDPKFIEDVGSLLGNLIPSEVPGRTQLLERQIKEMIHLSFKVSHSDKRLRVLAVQQVVKLRTWLKNEFYKLGNETWKGVFIYQGKLLDVCQNLESKLKELLKNFSEIACSEDCIVVEGPILDCWTCLRMTNRCFKGEYCGDEDPRKAENREIALFLILLATAVILGSAVLLFHFCIFHRRKMKAIRRSLKEYVEKKLEELMGKIDEKEEKDFRLRK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the Izumo family."}
{"protein": "MTNLAQKLRYGTQQSHTLAENTAYMKCFLKGIVEREPFRQLLANLYYLYSALEAALRQHRDNEIISAIYFPELNRTDKLAEDLTYYYGPNWQQIIQPTPCAKIYVDRLKTIAASEPELLIAHCYTRYLGDLSGGQSLKNIIRSALQLPEGEGTAMYEFDSLPTPGDRRQFKEIYRDVLNSLPLDEATINRIVEEANYAFSLNREVMHDLEDLIKAAIGEHTFDLLTRQDRPGSTEARSTAGHPITLMVGE", "text": "FUNCTION: Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae. SIMILARITY: Belongs to the heme oxygenase family."}
{"protein": "MKRPDYRTLQALDAVIRERGFERAAQKLCITQSAVSQRIKQLENLFGQPLLVRTIPPRPTEQGQKLLALLHQVELLEEEWLGNETNSDIPLLLSLAVNADSLATWLLPALQSVLVDSPIRLNLQVEDETRTQERLRRGEVVGAVSIQSQPLPSCLVDKLGALDYLFVASPTFAARYFPNGVTRSALLRAPAVAFDHLDDMHQAFLQQNFDLSPGSVPCHIVNSSEAFVQLARQGTTCCMIPHLQIERELANNELVDLTPGLFQRRMLYWHRFAPESRMMRKVTDALLSHGHQVLRQS", "text": "FUNCTION: Controls the transcription of genes involved in arginine and lysine metabolism. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MSDEREVAEAATGEDASSPPPKTEAASDPQHPAASEGAAAAAASPPLLRCLVLTGFGGYDKVKLQSRPAAPPAPGPGQLTLRLRACGLNFADLMARQGLYDRLPPLPVTPGMEGAGVVIAVGEGVSDRKAGDRVMVLNRSGMWQEEVTVPSVQTFLIPEAMTFEEAAALLVNYITAYMVLFDFGNLQPGHSVLVHMAAGGVGMAAVQLCRTVENVTVFGTASASKHEALKENGVTHPIDYHTTDYVDEIKKISPKGVDIVMDPLGGSDTAKGYNLLKPMGKVVTYGMANLLTGPKRNLMALARTWWNQFSVTALQLLQANRAVCGFHLGYLDGEVELVSGVVARLLALYNQGHIKPHIDSVWPFEKVADAMKQMQEKKNVGKVLLVPGPEKEN", "text": "FUNCTION: Possesses ATPase activity (By similarity). Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2). SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein. Note=The majority is localized in the cytoplasm and a small amount is associated with mitochondria. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MSEQKLAVNEYLKTDSDYLRGTIQQGLNTAVTGAFSEGDQQLIKFHGFYQQDDRDLRNERKEQKLEPLYSFMLRARVAGGVCSPEQWLAVDKIASNLTSANSIRLTTRQTFQYHGIPKRNLKTIIQDLDREALDSIAACGDVNRNVMCNPNPVESKLHQQAYAYAKQLSDNMLPHTKAYAEIWLDNEKLVTTEGEEVEPVYGQTYLPRKFKMAVAVPPDNDVDVYTNDLGFIAVAEGDELVGFNMVAGGGMGSTHGEVSTFPRLADDFGYIKAEDSLKFAEAVMTIQRDWGNRENRKLSRLKYTIVKHGFETFKAEIEARTGIKFEPRRDVVIGDRGDRYGWKQGVDDNWHLTLFIEGGRVKDLPGQPLQTGLREIAKIHRGDFRMTSNQNMIIAGVASADKEQIEGLARQYGLLGKLITETRGHSIACVALPTCALAMAEAERYFPDFLTKVEALQQKHGFLDQGIVIRMTGCPNGCARPFAAEIGLVGKAPGRYNLYLGASFEGTRLNKLYRENIQEAEILDQLDTLFAQYASQRQAGETFGNYTVRSGVVAAVNDAAKDFHG", "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": "VRDAYIAKPENCVYHCAGNEGCNKLCTDNGAESGYCQWGGRYGNACWCIKLPDDVPIRVPGKCH", "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 mammals. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MPRISTSLIRKASRIRPGLHLLLPECRTLEQAKLEYKWLTEELPPDKSIRWACLQRYKHVPLQYILRSQPFGALDIVCKPGVLIPRWETEEWVMAIIRALNNSMLSRHTIPLHICDTFTGTGCIALALSHGIANCTFTAIDVSTRAIKLVKENMLKNKVSGGKLVQHNILSSKASDEYPSHIDILTGNPPYIRKRDFNRDVKTSVKLFEPRLALVGELECYINLVNYWLPKTDSFFYEIGDVEQFNYVERRIKEDSYLSRIWSIGLKYDSNGKARVVYGFKATPKGRILHQIFASFGTIRHLATALSGHKANCN", "text": "FUNCTION: Methylates MRF1 on 'Gln-287' using S-adenosyl L-methionine as methyl donor. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the protein N5-glutamine methyltransferase family."}
{"protein": "MSSTATQPRYSLNRKVAVMGYPHVGKSSIVQRFTQNMFPDRYETTIEDQHTKHHTAFHRDFNLRVTDTAGQQEYTVFPRSCSLDVAGFLLVYAIDDRKSFDICSSIYEKIISVYGDPSIPIIIVGNKCDLGTQRVVQQEEGKELAKQCEAKFVEITARETNRVNEVFELLLREIEISRGNLRGPPQQQTKEQTSSDPNDPKNCVIS", "text": "FUNCTION: Binds GTP and exhibits intrinsic GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rheb family."}
{"protein": "MTLVYEGKAKRVYSTDEDHVFRIEYKDEVTAGNGAKKDNMAGKGRLNNLITSYFFERLARQGLESHFIKKLSDTEQLVKAVTIIPLEVVVRNYAAGSIVKRLGFDKGVQFKSPLVEFYYKEDALNDPIITDDHVKLLGIADDDDIAELKRQALIINDMLVKMMDEMNLQLIDFKIEFGKDQDGNILLADEISPDTCRIWDKDTKENFDKDVYREDTGSLIDTYTQFYNKLEAL", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MNIQALLSEKVSQAMIAAGAPADCEPQVRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLSGIASKVEIAGPGFINIFLEPAFLAEQVQQALTSDRLGVSQPTRQTIVVDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHHVIRANHVGDWGTQFGMLIAWLEKQQQENAGDMALADLEGFYRDAKKHYDEDEAFAERARNYVVKLQSGDTYFREMWRKLVDITMTQNQITYDRLNVTLTRDDVMGESLYNPMLPGIVADLKAKGLAVESEGATVVFLDEFKNKEGDPMGVIIQKKDGGYLYTTTDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWTIVRKAGYVPDSVPLEHHMFGMMLGKDGKPFKTRTGGTVKLADLLDEALERARRLVAEKNPDMPADELEKLANAVGIGAVKYADLSKNRTTDYIFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKADIDEQALASAPVIISEDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDVAGLFSGFYEHCPILSAENDAVRNSRLKLAQLTAKTLKLGLDTLGIETVERM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MSTQEEMEERLLREGSDAEGQSNNRESIYLRTKVWSEVNKMWRIALPSSLFRMTSFGSIIVAQAFIGHSSELGLAAYALLQSTFIRFLYGLMGGMSSATETLCGQAYGAEQYHTMGIYLQRSWIVDMAVTTLFLPFIVLAGPILRLLGQNVEITKTVDEIYPWMIPYVYSLIFTMTIQMYLQAQMRNAIVGVLSTLSLALDLVVTWWCVSVMGMGIGGALLGLNVGSWAMVLAEFVYIFGGWCPFTWTGFSIAAFVDLIPMLKLSISSGFMICLEYWYMSILVLMAGYTKDAKIAISAFSICQYIYTWELNICLGFLGAACVRVANELGKGDAHAVRFSIKVILTISTLMGVIFSALCLAFCGRISYLFSNSDEVSDAVNDLSVILAVSILLNSIQPILSGVAVGAGMQSIVAVVNLASYYAIGIPLGLILTYVFHLGVKGLWSGMLAGIAIQTIILCYIIYKTDWELEVKRTCERMKVWSLKPSNEESNPIIREESRSK", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MIFNVLTIFPQMFPGPLGVSNLGSALKKGLWTLNVFDIRAFANNKHNTVDDTPYGGGPGMLLRADVLGRCIDEVLSLHPNTKLMFTSPRGVSFTQDIARQTMNFDNITLLCGRFEGIDERVVDFYKLQEVSIGDYVLSGGELAAMVIIDTCVRMVPGVIGNAESLKQESMEGSLEYPQYTRPASWKGMEVPEVLLTGNHGEIEKWRRNASLSITAARRPDLLKDRYGENDVE", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
{"protein": "MAAGGGGGGVSRAALARPPIHRGTSAPGGAIAAAGGDGDGDEASRLLGRAQPREAPYLIPRPDGDLAVPDDLQYATLDLTGDPVAVGAGSYGSVLVYGSVAVKTLRAGFGHEAVMTLLAAEEARSAGVRGVVRLMGLSAPLRQLMFPAYEMDMDAYRRSLTARPGHVVHALGRVFTELGRALVFLNGRGLSHLDVKGGNIFVRTCGNMVVTAVIGDFSLMALNSRSALADPRFRLARRKALKITSLARSPPTGVLLGHARDRPTRVLMDFINGRPPPPGPLPYEVGLAIDLCALGHVLLDVALGLRPQRGQALTREYAVEVLARRCVLFAALLPPGSGPSAEALAGDILEEELAAGFREGVASSRPGNQPPRTVAPLLELVARFCGEDGGARFAELAA", "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 factors UL34 and UL31, by phosphorylating the US3 kinase, 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 ICP22 (By similarity). SUBCELLULAR LOCATION: Virion tegument Host nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MTMYVKSNTTGKDMLSLLEWNKEELIDIIKLAVAMKTNPAHYSHILSGKILGMIFDKPSTRTRVSFEAGILQLGGQAIVMSSKELQIGRGEPIKDTAHVMSEYIDAIMIRTFSHEKVEELAYHAEIPIINGLTDLHHPCQALADLMTIYEWKDQLEGVKLAYIGDGNNVCHSLLLAGAMVGLDIRLAMPKGYEVDETILATAENLAKESGAKIFVTEDPKHAVTDADFIYTDVWTSMGQEEENAKRLADFGEKYQVNAELASIAKPDYHFLHCLPAHREEEVTAEIIDGNHSVIYQQAGNRLHAQKALLAAILEAK", "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": "MAHKKGGGSTKNGRDSNPKYLGVKAAGGSTVAAGTIILRQRGTVIKPGVNAGIGRDHTIFALVDGIVSFRNGRNNKKQVSVEPCC", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MAALRALRCLRGVGAPVLRPGSGIRLPSQPSRGARQWQPDIEWAEQFSGAVMYPSKETAHWKPPPWNDVDILKEKAVTNMTLNFGPQHPAAHGVLRLVLELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSIAVEKLLNIQPPPRAQWIRVLFGEITRILNHIMAVTTHALDIGAMTPFFWMFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLLDDIYEFSKNFSLRIDEVEEMLTNNRIWRNRTVDIGVVTAEDALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPIGSRGDCYDRYLCRVEEMRQSLRIIEQCLNKMPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEIDR", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:26437605, PubMed:29887397, PubMed:31297047). Essential for the catalytic activity and assembly of complex I (PubMed:26437605, PubMed:29887397, PubMed:31297047). Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174). Plays an important role in carotid body sensing of hypoxia (PubMed:26437605, PubMed:29887397). Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation (PubMed:31297047). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 49 kDa subunit family."}
{"protein": "MNSPQPPDTTAAGSVHTAPTYTLRQLVMYFLRLGTLGFGGPVALAGYMHRDLVEAKQWITDADYKEGLALAQLAPGPLAAQLAIYLGYVHYRIVGATLVGVAFVLPSFLMVLALGWAYVRFGGLTWMQSVFYGVGAAVIGIIAISAYKLTKKSVGNDKLLWFIYLVLVAVTVITESEVAWLFLAAGVLVWFWRAPPKWLRQGKMNAFAATPLPAASGMMSTLDWPLLSQIGVFFAKAGAFVFGSGLAIVPFLYGGVVTEYHWLNDKQFVDAVAVAMITPGPVVITVGFIGYLVAGLPGACVAAAATFLPCYLFTVLPAPYFKKYGKLPAILAFVDGVTAAAIGAITGAVIVLAKRSIVDIPTALLALVTVALLLKFKKLSEPMIVAGAALIGLVAYPLLHH", "text": "FUNCTION: This protein reduces chromate accumulation and is essential for chromate resistance. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family."}
{"protein": "MHERYVPADVEAAAQGDWRAADAYKTREDSQKPKFYCVSMLPYPSGKLHMGHVRNYTINDVMYRYLRMNGYNTLMPMGWDAFGMPAENAAMANGVPPAKWTYDNIDYMKGQMQSMGLAIDWSREIATCKPDYYKWNQWLFLKMLEKGIAYKKTGTVNWDPVDQTVLANEQVIDGRGWRSGALVEKREIPMYYLRITQYADELLNDLDGLGWPERVKIMQQNWIGKSFGVNFGFPYELDGEKALLRVFTTRADTIMGVTFCAVAAEHPLATRLAQGKPELQAFIDECKRGGVAEADVATMEKKGVATGFSVSHPLTGEPVEVWIGNYVLMSYGEGAVMGVPGHDERDFAFAKKYGLPIKQVIASEGQTYSLDAWQEWYGDKETAVCVNSGKYDGLRYADAVDAVAADLKAGGYGDKQVTWRLRDWGVSRQRYWGTPIPIIHCPSCGDVPVPEQDLPVVLPEDLVPDGSGNPLAKSEAFLNCSCPKCGAAAKRETDTMDTFVDSSWYFSRYTAPDADTMVDARTDYWMPMDQYIGGIEHAILHLLYSRFWTKVMRDLGLVKFGEPAKNLLTQGMVLNETFYREDASGKKTWYNPADVTVTHDDKGRPVGATLNTDGQPVVLGGIEKMSKSKNNGVDPQVLIDQYGADTARLFTMFAAPPEQQLEWSGAGVEGASRFLRRVWSFGATNREALAARAGFDAAALGDADKALRREIYSVLKQADFDYQRLQYNTVVSAAMKMLNAIDGAKGATPAVLRETYGVLLRVLYPVVPHVTFELWKALGYADEFGPLLDAPWPKVDEAALEQAEIELVLQVNGKVRGALKVAKGASRDAIEAAAVADEAFAKFSDGKPAKKIVVVPGRLVNIVV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MAAPEDVAALQAEITRREEELASLKRRLAAALTAEPEPERPLRVPPPPLAPRAALSRDEILRYSRQLLLPELGVRGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDHDVVETSNLARQVLHGEAQAGESKARSAAAALRRLNSAVECVAYPRALAEDWALDLVRGYDVVADCCDNVPTRYLVNDACVLAGRPLVSASALRFEGQMTVYHHDGGPCYRCVFPRPPPPETVTNCADGGVLGAVPGVLGCAQALEVLKIAAGLGSSYSGSMLLFDGLGGHFRRIRLRRRRPDCVVCGQQPTVTRLQDYEAFCGSSATDKCRALKLLCPEERISVTDYKRLLDSGAPHVLLDVRPQVEVDICRLPHSLHIPLSQLERRDADSLKLLGAALRKGKQESQEGVALPVYVICKLGNDSQKAVKVLQSLTAVPELDSLTVQDIVGGLMAWAAKIDGTFPQY", "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": "MVRVGLQISATLENIDKLETSHPDYPFFVKLTCSNCGEQSDKWHDITESERVQQDTRNTAGFNFFMKCKMCSRENSIDIVEKSNVPYTADDSGKLKTIVIFDCRGLEPVDFSPRSGWKVFSSENGQSFEDVDLSEDDWVEYDQKNNNSVGVYEFVSKFIKLKK", "text": "SIMILARITY: Belongs to the UPF0587 family."}
{"protein": "MANPIVGRVWKFGDDINTDAIIPGKYLRTRDMQIFGTHAMEGIDPEFTKKAKPGDIIVAGTNFGCGSSREQAPLALKHSGIACIVAKSFARIFFRNAINIGLPLMEADVECQEGDEIKVDLFKGEVLVPEKGIFKGNKLPDFLLDILNDGGLVAHRKKVKGEHK", "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 LeuD family. LeuD type 2 subfamily."}
{"protein": "MTETAFLKLFVAIVITFILVLPEFFKTPKERTLELSCLEVCFLPNSTYPLSSFNFSSVAFLQPAEETQTIMGILPNHSSFQSFAEICQGITSGLPMCSLCLVCESKGDVDFTSQEQTSKGLVMRGSKEVKASDFYSPCEYFNVTVALLADPVKEDTTCTPEGHPGEAIALDEDPVREKSLNHTCRFMKNTDNCTHIFLHLEMDVKSVTCSMKITWYVLVLFVFMLGIIFIIYKILEEHRRVWRRQSHNYKSSSVLFRGHDSGKLSTLNVRVIPGYPWTIWTRDFDE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MHYPEPITKLMDSFMKLPGIGPKSAARLAFYVLDMKEDDVLDFAKALVDAKRNLSFCSVCGHITDKDPCYICSDTSRDRSVICVVQESKDVIAMEKMRDFHGLYHVLHGTISPMDGIGPEDINIPDLLKRLQDDTIEEVILATNPNVEGEATAMYISRLLRPSGIKVTRIAHGLPVGGDLEYADEVTLSKAMEGRREV", "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": "MVIGSGVFLTRTCYLRLQPPSLVLRRRFCAATTACSVPLNGNKKKKSEKEKVIVISGPTGAGKSRLAMELAKRLNGEIISADSVQVYKGLDVGSAKPSDSDRKVVPHHLIDILHPSQDYSVGQFYDDGRQATKDILNRGRVPIVTGGTGLYLRWFMYGKPDVPKPSPEVIAEAHDMLVGFQTEYNWDAAVELVVNAGDPKASSLPRNDWYRLRRSLEILKSTGSPPSSFRIPYDSFRVNLVAPDADDFLEDGSSADISIQNIETDLDYDFLCFFLSSPRVALYRSIDFRCEDMLSGPNGVLSEARWLLDLGLLPNSNPATRAIGYRQAMEYLLQCRRYEGESSPREFYAFLNKFQTASRNFAKRQMTWFRCEPMYHWLNASKPLDSILQCIYDAYESEAEMVEIPESLRMSKDVRDSREASELKGYRSKNRHFVRREDCSSVLEWIRSEGCKSEASCVESAIA", "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). Involved in the cis-type cytokinin biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IPP transferase family."}
{"protein": "MQFPVDTHSHTVASTHAYSTIHDYLAVAKEKGIRLFATTDHGPAMKDAPHFWHFVNLRVLPRIWNGVGILRGIEANIMNEKGEIDYFGEYLSELDLVQAGFHEPVFAPADRLTHTRAMIATMESGLVDIITHPGNPAYPIDVEAVVGAAKACNVALEINNSSFTASRKGSEENCLAIARMATKLDAQLVMGSDAHVAFDLGGFDRSLAIVDAADYPRQRLLNESPMALLHFLQQRGHQHLDELIRYFRPVL", "text": "SIMILARITY: Belongs to the PHP family."}
{"protein": "MLSRKGIIPEEYVLTRLAEDPAKPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTVKVPTPLCTARQLDEDHSLLEALTLASARGPLRKRSVPMAKAKPKFSISPDSLS", "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. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ11 subfamily."}
{"protein": "MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGGGPGQARPLGPPGTSLLGRGARRSGEGWCPGAFESGARAARPPSRVEPRLATAASREGAGLPRAEVAAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR", "text": "FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine- rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre- mRNA in endothelial cells. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus speckle. Note=Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm Cytoplasmic vesicle, secretory vesicle, acrosome. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily."}
{"protein": "MLDLARLDQLQNASVLVIGDVMLDRYFIGDTNRISPEAPVPVVRVAHTEDRAGGAANVARNIAHLDGQAAILGIIGNDTDGRLLKDLLIKEKVHSELLELDDARTISKTRIISRHQQMVRLDMEDTFPVAQAESVKQRYAELIEQYNTVIISDYAKGTLACVGDLIQAARKAGKQVLVDPKSKDFSLYRGATVITPNLSEFKAAGGDASSDDAMLSSARAMLTDAGIDTMLLTRSEQGMSLITPTEHHHFPAEVLEVSDVTGAGDTVIATLGTLLSAGFDLKDAAWLSNLAAGIVVAKLGAATVSPEELAARASHQWSAKTSGYHPSVEQSLLHIDYARQQGERIVFTNGCFDILHAGHVRYLAQARALGDRLVVGLNSDASVRRLKGEERPVNSLEDRMEVLSALACVDWVIPFGDNTVENDTPEQLIKRVNPQVLAKGGDYSIDTIVGADFVQENGGEVAILPTVEGRSTTGLIKKVRG", "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": "MSRQVSLDRLRNIGIMAHIDAGKTTTTERILFYTGRTHKLGETHEGAATMDFMVQEQERGITIQSAATTCSWKDHRINIIDTPGHVDFTVEVERSLRVLDGAVAVFCAKGGVEPQSETVWRQADKYGVPRLAYVNKMDTIGADFFRVIRMMEERLGARPVPIQIPIGAEDTFRGVVDLVRNVAIMYYDDLGKDIREEPIPEDMRELVEQYRTRMIEAATEADDALMEKYLMGEELTVEEIKRGLRKLTVECKINPVCCGSSYKNKGVQPLLDAIVDYLPSPLDIPPVQGTDPETGEPAERKADDNEPFSALAFKVVSDPYVGKLCFFRVYSGQLKSGSYVLNATKGKRERIGRLVRMHANHREEVEVVETGDIAAAVGLKDTGTGDTLCTDAAPVILESMEFPEPVIQLAVEPKTKADQDKLSTALLKLAEEDPTFRMFTDPETGQTIIAGMGELHLEIIVDRLQREFKVGVNVGKPQVSYRETVRGRVENVEGRFVRQSGGRGQYGHVVINLEPAEPGSGFIFENKIVGGVIPKEFIGPVEQGIKEALQNGVLAGYPMIDVKVELVFGSYHEVDSSEAAFKIAGSMALKAAAQKAQPVLLEPYMRVEVTVPEEYMGDVIGDLNARRGRIEGMEARGNAQVIRAQVPLAEMFGYATDLRSRTQGRGVYSMQFDHYEEVPPNVAKPIIEKAQGKA", "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": "MAVTKARTFRELMNAPEILVVPSAYDALSAKVIQQAGFPAVHMTGSGTSASMLGLPDLGFTSVSEQAINLKNIVLTVDVPVIMDADAGYGNAMSVWRATREFERVGIVGYHLEDQVNPKRCGHLEGKRLISTEEMTGKIEAAVEAREDEDFTIIARTDARESFGLDEAIRRSREYVAAGADCIFLEAMLDVEEMKRVRDEIDAPLLANMVEGGKTPWLTTKELESIGYNLAIYPLSGWMAAASVLRKLFTELREAGTTQKFWDDMGLKMSFAELFEVFEYSKISELEARFVRDQD", "text": "FUNCTION: Catalyzes the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos (BA). Catalyzes the rearrangement of the carboxyphosphono group of CPEP to form the C-P bond of phosphinopyruvate. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily."}
{"protein": "MPKLTYKSVSEISGPLLFVENVPNAAYNEMVDIELDNGETRQGQVLDTRKGLAIVQIFGATTGIGTEGTRVKFRGETARLPISEDMLGRVFNGIGEPIDGGPEILAKERMEITSNAINPYSREEPSEFIETGISAIDGMNTLVRGQKLPIFSGSGLPHNQLAAQIARQAKVLDSSENFAVVFGAMGITSEEANYFTNQFRETGALSRSVMFLNLSSDPSMERIILPRIALTTAEYLAFQKEMHILVILTDMTNYCEALREISSAREEVPGRRGYPGYMYTDLSTIYERAGKLKGNNGSITQIPILTMPGDDITHPVPDLTGYITEGQVVVSRDLNRKGIYPGIDVLLSLSRLMNQGIGKGHTREDHRGLADQLYSAYASGKDLRSLTAIVGEEALSQNDRKYLRFADTFEERYLKQDFFEDRSIEDTLNLGWELLADLPESDMKRVKPDHIKKYGKWKKE", "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": "MSILTTTALASILDWLAANAPKAELASDSRRIAQGDVFVAYPGDEADGRSYIANAIERGAQAVIYEAAGCTWDAEWDVAHLAIDDLKEHAGEIAAAYYAHPDRSMFTVAITGTNGKTSCAQWLGSALSRLGQPTAVIGTLGVGIFTNGGHGSFDVTGYTTPDAVLLQRSLVNVSNLGATALAIEASSIGLHQGRLSGMHFDMALFTNFTRDHLDYHGDMAAYEEAKAMLFDWPGLQHAVINLDDAMGVRLVQRLQSRQADVGITGYTLSDKKIDGIAVLRATDIRSNQSGTVFQLESSAGNTQVKTQLVGQFNVSNVLGIIGILLAKGIALQDAVNAVEALTAVPGRMQQLGGGEAPLVVIDYAHTPDALEKTLATLRSVANDRGGELWCVFGCGGDRDPGKRPQMGKVSMAADHIVVTTDNPRNEEPANIIGDIVAGITAPKNAPQIIEDRASAILWAGRHAARQDVILLAGKGHEAYQEVKGRKLPFLDADHAALALSTRVMQGAS", "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": "MQTTTITMGDVQYPYRLGTGCVDGIVTRLGELEASHYLVLCDATVAELYGHDLAARLRRSAGPASVLTHPAGEEHKGLGTLDTLADAALHAGVDRRGVVVALGGGVTGNIAGLLAALLFRGIRLVHVPTTVVAMLDSVLSLKQAVNAQVGKNLVGTFYPPVEVLADTAMLGTLPVREIRSGLCEVVKNALAIRPSMIDFLAAELRPDGRYADDVLRWMIDESVAAKAQVTEHDKYERREGLVLEYGHTVGHALEHASHGAVSHGAGVGVGMVAAAEVARRLGHVDADLVELHRELVGKVGVATTLPADVPTEEITYRLGFDNKRGYQPLPADHYAMVLLADVGQPLYQDGLPLTPAPRALVDEVVRELADAPSRIGASVGSAGGAS", "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": "MSGHDSKYFSTTKKGEIPELKEELNSQYKDKRKDAVKKVIAAMTVGKDVSSLFTDVVNCMQTENLELKKLVYLYLINYAKSQPDLAILAVNTFVKDSQDPNPLIRALAVRTMGCIRVDKITEYLCDPLQKCLKDDDPYVRKTAAICVAKLFDINAELVEDRGFLEALKDLISDNNPMVVANAVAALAEIQENSTSPIFEINSTILTKLLTALNECTEWGQVFILDALSRYKASDPREAENIVERVTPRLQHANCAVVLSAVKMILQQMELITSTDVIRNLCKKMAPPLVTLLSAEPEIQYVALRNINLIVQKRPTILAHEIKVFFCKYNDPIYVKMEKLEIMIKLASDRNIDQVLLEFKEYATEVDVDFVRKAVRAIGRCAIKLERAAERCISVLLELIKIKVNYVVQEAIIVIKDIFRRYPNTYESIIATLCESLDTLDEPEAKASMIWIIGEYAERIDNADELLESFLENFPEEPAQVQLQLLTATVKLFLKKPTEGPQQMIQVVLNNATVETDNPDLRDRAYIYWRLLSTDPEAAKDVVLAEKPVITDDSNQLDPSLLDELLANISTLSSVYHKPPEAFVTRLKTTVQKTEDEDYVEGSETGYPEASGNPVDGAASPSATTGYVTKLAAAPAPVPDLLGDLMGSDNAAIVPVDEPTTPSGRPLPVVLPASKGQGLQISAQLTRQDGQVFYSMLLENNSQSLLDGFMIQFNKNSFGLAAVGSLQVPPLQPGASARTMMPMVLSQNMSTGSTSSVLQVAVKNNQQPVWYFEDKIVLNALFSEDGRMERGTFLETWKSLPDSNEVQKEFPGITITSVESTLDLLAASNMFFIAKRKNGNQDVLYLSAKVPRGIPFLIELTAIVGQPGLKCAVKTPTPEIAPLFFEAVEILFKA", "text": "FUNCTION: Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity). SUBCELLULAR LOCATION: Golgi apparatus Golgi apparatus, trans-Golgi network Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=Associated with the trans-Golgi network. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). SIMILARITY: Belongs to the adaptor complexes large subunit family."}
{"protein": "MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS", "text": "FUNCTION: Probably involved in copper and silver 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": "MELTTRTLPARKHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGLEVNAMLSGPMGGDQQVGALISEGKIDVLIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNVATADFIIQSPHFNDPVDILIPDYQRYLAERLK", "text": "FUNCTION: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. SIMILARITY: Belongs to the methylglyoxal synthase family."}
{"protein": "MAFSFQLQQVFPFPVKFCSQPKSIKLQIFPNLTKRLPIHPLASAQNNATSNIDHNYIAMDESSINEEEVPLPTELSRELMPKHIAVIMDGNRRWAKRRGLPVALGYAAGIRVLRNFVKLSYNWGISALTLFAFSSENWFRPKAEVDLLMGLFDKVLKDELENLARTGIRLSIIGDASQLPKSLQDLIDKAVMATKANSRLHILVAINYSGQYDVVQACQTIAQRVKDGNIEPEDINSLLVEQELQTKCTEFPSPDLLIRTSGELRLSNFLLWQLAYTELFFSHSQWPDFGEAEFLEALCSFQQRQRRYGGQSS", "text": "FUNCTION: Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the UPP synthase family."}
{"protein": "MSPMDLQESAAALVRQLGERVEDRRGFGFMSPAIYDTAWVSMISKTIDDQKTWLFAECFQYILSHQLEDGGWAMYASEIDAILNTSASLLSLKRHLSNPYQITSITQEDLSARINRAQNALQKLLNEWNVDSTLHVGFEILVPALLRYLEDEGIAFAFSGRERLLEIEKQKLSKFKAQYLYLPIKVTALHSLEAFIGAIEFDKVSHHKVSGAFMASPSSTAAYMMHATQWDDECEDYLRHVIAHASGKGSGGVPSAFPSTIFESVWPLSTLLKVGYDLNSAPFIEKIRSYLHDAYIAEKGILGFTPFVGADADDTATTILVLNLLNQPVSVDAMLKEFEEEHHFKTYSQERNPSFSANCNVLLALLYSQEPSLYSAQIEKAIRFLYKQFTDSEMDVRDKWNLSPYYSWMLMTQAITRLTTLQKTSKLSTLRDDSISKGLISLLFRIASTVVKDQKPGGSWGTRASKEETAYAVLILTYAFYLDEVTESLRHDIKIAIENGCSFLSERTMQSDSEWLWVEKVTYKSEVLSEAYILAALKRAADLPDENAEAAPVINGISTNGFEHTDRINGKLKVNGTNGTNGSHETNGINGTHEIEQINGVNGTNGHSDVPHDTNGWVEEPTAINETNGHYVNGTNHETPLTNGISNGDSVSVHTDHSDSYYQRSDWTADEEQILLGPFDYLESLPGKNMRSQLIQSFNTWLKVPTESLDVIIKVISMLHTASLLIDDIQDQSILRRGQPVAHSIFGTAQAMNSGNYVYFLALREVQKLQNPKAISIYVDSLIDLHRGQGMELFWRDSLMCPTEEQYLDMVANKTGGLFCLAIQLMQAEATIQVDFIPLVRLLGIIFQICDDYLNLKSTAYTDNKGLCEDLTEGKFSFPIIHSIRSNPGNRQLINILKQKPREDDIKRYALSYMESTNSFEYTRGVVRKLKTEAIDTIQGLEKHGLEENIGIRKILARMSLEL", "text": "FUNCTION: Bifunctional terpene synthase that possesses both prenyltransferase and type II terpene cyclase activity, converting isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into geranylgeranyl diphosphate (GGPP) and further converting GGPP into copalyl diphosphate, respectively. 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": "MKRGKLIVFSGPSGVGKHTILSKIINRKDLNLAYSISMTTRKKREGEVNGVDYYFVNDEEFKKAILNNELIEWAEFVGNKYGTPRTIVEKLRDEGKNVILEIEVVGALKVLDLYKNDDLISIFLLPPSIDELKKRLLKRNTETLETIKKRIQKATHEITIKDYYQYNIINDNPDHAANQLAEIILNEIKQS", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family."}
{"protein": "MELVLVGKFLYNGRIIDGSIGVKDGKITKFSLRELKGDNKIKVEKGKIILPGLIDVHVHLRDFNETHKETIETGTKAAVHGGITTVFDMPNTKPPVMDEKTLKMREFLFKKKSYADYALGFLLAGNEPVKADFYKIFMGASTGGIYSKNFEEDYAKALDITSVHAEDYELISKYPERPPIVEISAIKKALNAARKVKKPLHICHVSTREGLKEILEANIPWVSFEVTPHHLFLTRKDYEKSKLLKVYPPLRDESDRRYLWEKLDNVPIIASDHAPHTLEDKERGAAGLPGLETEVALLLDAVNRGMLELWDVVEKMSLNPARIFRIKNKGWGEGKDADFAIVDMKKEWTIKAEEFYTKAGWTPYEGWKVRGKVIMTILRGEIVMEDDEVIGKPRGERIVKEGDD", "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": "MLLVLIDVDGFMGQLYNENGTQTILIPREVVIFYWEKNTASKILQLFFHGGIDPIFEKINQRSFSFQSRHIHHFTLDESPLPNSIALPTDTLQAFKAGKKMIFQHLVKITKDHEQILLLHKGGPEGEWVRSFNIPNATVQNLNDLCCPSVEKLVLKKRDYISSSIGCPKHIQGSNHCPVFECHVLFKWIQENTSIVQGVLKRPSLPYEEAVLFIEHRINMVDNHPFKKDSVKQNQKKKNWIATQFVQHGIYVDNGILSKIYNKYSLF", "text": "FUNCTION: Plays a role in the inhibition of host RNA Pol-III-RIGI- mediated innate antiviral response. Mechanistically, interacts with host E3 ubiquitin ligase RNF135, disrupting RNF135-RIGI interaction and impairing RNF135-mediated 'Lys-63'-polyubiquitination and activation of RIGI. SIMILARITY: Belongs to the asfivirus I267L family."}
{"protein": "MIKVRLQKDNDLMDILNIMAPGTPLRDGLENILRAKTGGLIVIGDSEEILDIVDGGFTIDAEYSPSYVYELAKMDGAIILSGDVKRIIRANAQLMPDPSVPTFETGTRHRTADRIAKQTGNIVIAISQRRNIITIYRNNIKYVLRDSSVILGKANQALQTLEKYVSVLDKVINNLNVLEFRDLVTLFDVMTAIQRTEMVMRIVWEMERYICELGNEARLISMQLNELVRYVEEDEILLIRDYCETYMDYTEVYDEIQSMSSEELINLDQISKILGYTGVPLVDTFISPRGYRMLHRIPRIPSNVIENVVKNFKELKAVMEASYEQLDKVEGIGEARAKAIKNGLRRLKEQANIDKNIVTR", "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": "MALSFSKYHGLGNDFILVDNRQSTEPCLTPDQAQQLCDRHFGIGADGVIFALPGQGGTDYTMRIFNSDGSEPEMCGNGIRCLAKFLADLEGVEEKTYRIHTLAGVITPQLLADGQVKVDMGEPQLLAELIPTTLAPAGEKVVDLPLAVAGQTWAVTCVSMGNPHCLTFVDDVDSLNLTEIGPLFEHHPQFSQRTNTEFIQVLGSDRLKMRVWERGAGITLACGTGACATVVAAVLTGRGDRRCTVELPGGNLEIEWSAQDNRLYMTGPAQRVFSGQAEI", "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": "MPELPEVETSRRGIEPHLVGNILHYAIVRNSKLRWPVSEKIKTLLDEPILSVKRRAKYLLIELNQGWIIVHLGMSGSVRILPEEQPEEKHDHIDLVFRDGKVLRYTDPRRFGAWLWCEDLATSSVLAHLGPEPLSAQFNAQYLYQQSKNKKIAIKPWLMDNKLVVGVGNIYANEALFSSGIMPDRKASSLTEQECDVLVNAIKTVLTRSIEQGGTTLKDFLQSDGKPGYFAQELFVYGRKDKACLICGHTIESIKQGQRSTFFCRHCQHGEITD", "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": "SFREQCVPGREITYECLNACAEYAVRQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha- amylase inhibitor) family."}
{"protein": "MAASISGYTFSSLCFHSANSCSDHEGFLLGEVRQEETFSISDSQISNTELLQVIEIHRHEPCTNLFSFYDYAGTVNEESLDRILKDRRKNVIGWYRFRRNTQQQMSYREQILHKQLTRLLGAPDLVFLLITFISTANTSTHALEYVLFRPNRRYNQRVSLTIPNLGTTSQQEYKVSSVPNTSQNYAKVIKEHGINFFDKDGVMKDIRLIYQVYNALQEKVQAVSEEVEKSERVVESCQAEVDKLRTQICRRKAEKEREENLRHSLQLQTEDTTDCVMTLSSTDFIAAASRPQDLHPPAYTEENADAKDGVDSPPDMPRPQAVGSSCQLLIEIKDGEPSACKTSASEETETEESQSDYKKSRHLSESPDSDMADDQPCQLSTQPDGDLAQQ", "text": "FUNCTION: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys- 63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K- fibers. SIMILARITY: Belongs to the FAM175 family. Abro1 subfamily."}
{"protein": "MSDKKIKGLEWQEKPLSDNERLKTDSNFLRGTILDDLKDGLTGGFKGDNFQLIRFHGMYEQDDRDIRAERLEEKLEPLKFMLLRCRLPGGIIKPYQWIEIDKFAREHTRYQSIRLTNRQTFQYHGVPKGKLQPMHRLLHSIGLDSIATAADMNRNVLCTSNPIESELHQQAYEFAKKISEHLLPRSRGYLDVWVDGKKVESSDDLLKIEDEPILGKTYLPRKFKTAVAIPPLNDVDVYANDLNFIAIQDENGQLCGFNVLVGGGLSFEHGNTKTYPNVAYSLGFVPLEHTLAAAEGVVKTQRDFGNRSDRKNARVRYTVQNMTLDGFRAEVERCMNIKFEPTRPYEFTERGDRIGWVKGIDNNWHLTLFIESGRITDKPEKPLMTGVLELAKVHKGDFRITANQNLIVANVAEQDKAQIEAIARQYGLIQEISKLRENAMSCVSLPTCPLAMAEAERVLPDFISELDKVLSKHNVADESIITRITGCPNGCRRAMLAEIGLVGKAIGRYNLHIGGDRAGLRIPRLYKENITLQEIVNEIDQLVARWATERQTNEAFGDFVIRSNIIAPVVNAHIDFWDATKIIPTTII", "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": "MPALPILALALAPLLVNGQLSGSVGPLTSAHSKAATKTCNVLDYGAVADNSTDIGSALSEAWDACSDGGLIYIPPGDYAMDTWVSLSGGKATAIILDGTIYRTGTDGGNMILVENSSDFELYSNSSSGAVQGFGYVYHREGDLDGPRILRLQDVSNFAVHDIILVDAPAFHFVMDDCSDGEVYNMAIRGGNSGGLDGIDVWGSNIWVHDVEVTNKDECVTVKSPANNILVESIYCNWSGGCAMGSLGADTDITDILYRNVYTWSSNQMYMIKSNGGSGTVNNTVLENFIGHGNAYSLDVDSYWSSMTAVDGDGVQLSNITFKNWKGTEADGAERGPIKVVCSDTAPCTDITIEDFAMWTESGDEQTYTCESAYGDGFCLEDSDSTTSYTTTQTVTTAPSGYSATTMAADLTTDFGTTASIPIPTIPTSFYPGLTAISPLASAATTA", "text": "FUNCTION: Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)- alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
{"protein": "MRDALGREVRSVRISVTMRCNMACVYCHREGERPGRSELSAAEWGRLLRACAEIGVRKVKITGGEPLLRRDLIEIIENAEGFEEVSLVTNGVLLADYAGDLAEAGLDRVNVSLDTVDRKLYRKLTRSRFSPDDVIRGIEAAVSEGLTPVKVNVVLTSETVKTLPTLVEELADLEGLKLQLIEPMGSIPGFRPAHAEDGLRALGEYEPELERVRTFHSREVYRLNNGMAVEVVKPMDGVMCEACTRIRLTHDGKYKGCLMAPPKPLPRDDFGELVRTLKEYVRTRDDTFEVHQGTSVMGRMRGDVSGR", "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": "MRHYELVLLVHPDQSDQVVGMVERYIKLVQDNNGTIHRLEDWGRRQLAYPINKIHKAHYVLFNIETDGETLAELEELFRYNDAIIRSLVMRRDDAVTEESQLAKNADEKRARKATTRRPDRDDSDDNDHSED", "text": "FUNCTION: Binds together with bS18 to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family."}
{"protein": "MKLSFDLKKKNGNARRGQLTFERGTVQTPAFMPVGTYGTVKGMTPEEVKGTGAEILLGNTFHLWLRPGQEVMKMHGDLHDFMNWHGPILTDSGGFQVFSLGKMRKITEKGVHFRSPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHNEAKKSMEMSLRWAQRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSIKGLTEIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAKHKTDTTPLDPHCDCYTCQHYSKSYLHHLERCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFDEFVTEFYERRGREVPPLAKEQ", "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": "MINYFELSLKNLGVSFTSESIDKLKFYIKRVLLFGSRFNLVSKNDLRFDAVLLHALDSVVGFPIIKDNNPHQVLDVGSGAGFPGIILAIFDNSRKYVLLERSNKKVTFLRMMSLELGLDNVKVLERDVADEKDKYEFITIRAFRDIREYASILRLILKNGGLIMAYKGRFDKIKFEISHIESLFSKIEIKESAISDAKERNFLLLYK", "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": "MEKMVMKMLVIFVFGMNHWTCTGFPVYDYDPASLKEALSASVAKVNSQSLSPYLFRAFRSSIKRVNALDEDSLTMDLEFRIQETTCRRESEADPATCDFQRGYHVPVAVCRSTVRMSAERVQDVWVRCHWSSSSGSSSSEEMFFGDILGSSTSRNSHLLGLTPDRSRGEPLYERSREMRRNFPLGNRRYSNPWPRARVNPGFE", "text": "FUNCTION: Could coordinate an aspect of bone turnover. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SPP2 family."}
{"protein": "MSLLCHNKGCGQHFDPQTNLPDSCCHHPGVPVFHDALKGWSCCRKRTVDFSEFLNIKGCTVGPHCAEKLPEAPQPEGPATSSSLLEQKPPNTIPKSAETLRRERPKSDLPPKLLPLNISQALEMALEQKELDQEPGAGLDSSLIQTGASCQNPGCDAVYQGSESDATPCTYHPGAPRFHEGMKSWSCCGIQTLDFGVFLAQPGCRVGRHDWGKKLLASCRHDWHQTDSLVVVTVYGQIPLPAFNWVEASQTELHIHIVFDGNRVFQAQVKLWGVVNVEQSSVSLMPSRVEISLVKADPGFWAQLEHPDALAEKSKSGVGLEMDEEESEDSDDDLSWTEEEEEAMGE", "text": "FUNCTION: May play a role during maturation and/or organization of muscles cells."}
{"protein": "MNNTTSDINDQRYEPREVEAYWQKEWANDDLYRTNTEVNKENTFYALSMFPYPSGSLHMGHVRNYVITDVLARYKRMKGLNVLHPMGWDSFGLPAENAAIERETSPSTWTDKNISQMKDQLDRLGLSIDWSKEVTTCKEDYYKWTQYIFNQLHKNNLAYQKKATVNWDPIDQTVLANEQVDAEGKSWRSGAKVEKKELNQWFLRITSFAEDLNKDLVTLNDWPDRVRVMQKNWIGKSIGAEITFDIKNSDQKITAFTTRIDTVYGVSYLVLASNHPLIDQLISSNDIDKLNDFRQTQEKLSDLERNSDTRQKLGMYLGVDAINPANNKEIPIWIGDYVIMEYGTGAVMGVPAHDSRDYQFAKSYDLPIQYVIKPNIGEDESYLNAEFVDKGVMINSDKFNGIESDIAKTKILEFGSNSNWAKPKITYKLRDWLISRQRYWGCPIPIINCKKCGQVRVPDDDLPVVLPIDIKLTGKGKSPLTTKTEWINTCCPKCGTDAKRETDTMDTFMCSSWYFLRYINPDNCEKPFLKSEIDKWLPVKQYVGGIEHAILHLLYSRFLTKALKRCGLINIDEPFKKLLTQGMVQAVTFKNPNTNKYFSKDQIKDIDNPKDPLTGENIEIIYEKMSKSKYNGVDPSVVIDKYGADTARMFILFKAPPEKDLEWDDSDVEGQYRFIQRLWKFVINTFKLTNNNSRSNIEKEKSKDEEALRLINIAIKEITDDLDNLQFNTAISELMKVVNGLSLIVNYCSNETLNKVISILVKITSPFSPHIAEELWKTIGNTQSIHLQSWPEFDAGAIEQDTFKLMIQINGKVRGSINASKNLSKENLEDLAIKTEAAIKWMDGKEPKRIIVVPNKLVNIVI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGVWRFKENVEDGRASIYQSVVTNTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVLSVRKCPDFSSSGQWKVVTQSNGKEQNAVFDAVMVCSGHHILPHIPLKSFPGIERFKGQYFHSRQYKHPDGFEGKRILVIGMGNSGSDIAVELSKNAAQVFISTRHGTWVMSRISEDGYPWDAVFHTRFRSMLRNVLPRTAVKWMIEQQMNRWFNHENYGLEPQNKYIMKEPVLNDDVPSRLLCGAIKVKSTVKELTETSAIFEDGTVEENIDVIIFATGYSFSFPFLEDSLVKVENNMVSLYKYIFPAHLDKSTLACIGLIQPLGSIFPTAELQARWVTRVFKGLCSLPSERTMMMDIIKRNEKRIDLFGESQSQTLQTNYVDYLDELALEIGAKPDFCSLLFKDPKLAVRLYFGPCNSYQYRLVGPGQWEGARNAILTQKQRILKPLKTRALKDSSNFSVSFLLKILGLLAVVVAFFCQLQWS", "text": "FUNCTION: Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FMO family."}
{"protein": "MAKHIVELTDALSNKIAAGEVVERPASVVKELVENAIDAGSTVIDILVEEAGLNKITIIDNGSGIEEEDVATAFLRHATSKIKNEADLFRVHTLGFRGEALPSIASVSHLEMETSTGEAKGTTISLEGGKIIEQKSGHARKGTQIEVSQLFFNTPARLKYLKSLPTELGNITDILNRLALAHPDISFRFSHNGKPLLQTNGNGDLRQVIAAIYGVSIAKKSVPVKAESLDFKISGYAVLPEVNRSNRNYISTIINGRFIKNFALVKAIQEGYHTLLPIGRFPIIVLQIEMDPIIVDVNVHPAKLEVRLSKEKELGQLISQMIKETFHKLQLIPDGEISKKQKEDQKSEQIQISFEEKKPVKETPTLFSKPTIPEYVPSDEDAPREDDFILETMPSYEPESQAEQEEHTKERIPKMYPIGQMHATYIFAQNENGLYIIDQHAAQERIKYEFYREKIGEVSRELQELLVPIVLEFPADEYVRLEEQKAKLEEVGVFLENFGQNSFIIRAHPTWFPKDQEEEMLREIIDEALSAPSISIHKLREDTAIMMSCKKSIKANHYLTTQDMEALLDTLREASDPFTCPHGRPVIIQYSTYELEKMFKRVM", "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": "MTKTRILNPTRFPSPKPLRGCGDANFMEQLLLHCATAIDSNDAALTHQILWVLNNIAPPDGDSTQRLTSAFLRALLSRAVSKTPTLSSTISFLPQADELHRFSVVELAAFVDLTPWHRFGFIAANAAILTAVEGYSTVHIVDLSLTHCMQIPTLIDAMASRLNKPPPLLKLTVVSSSDHFPPFINISYEELGSKLVNFATTRNITMEFTIVPSTYSDGFSSLLQQLRIYPSSFNEALVVNCHMMLRYIPEEPLTSSSSSLRTVFLKQLRSLNPRIVTLIEEDVDLTSENLVNRLKSAFNYFWIPFDTTDTFMSEQRRWYEAEISWKIENVVAKEGAERVERTETKRRWIERMREAEFGGVRVKEDAVADVKAMLEEHAVGWGMKKEDDDESLVLTWKGHSVVFATVWVPI", "text": "FUNCTION: Probable transcription factor involved in plant development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MNNSKIISKVLLSLSLFTVGASAFVIQDELMQKNHAKAEVSAEEIKKHEEKWNKYYGVNAFNLPKELFSKVDEKDRQKYPYNTIGNVFVKGQTSATGVLIGKNTVLTNRHIAKFANGDPSKVSFRPSINTDDNGNTETPYGEYEVKEILQEPFGAGVDLALIRLKPDQNGVSLGDKISPAKIGTSNDLKDGDKLELIGYPFDHKVNQMHRSEIELTTLSRGLRYYGFTVPGNSGSGIFNSNGELVGIHSSKVSHLDREHQINYGVGIGNYVKRIINEKNE", "text": "FUNCTION: Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS). SIMILARITY: Belongs to the peptidase S1B family."}
{"protein": "MGKVIGIDLGTTNSAMAVYEGNEAKIIANKEGKNTTPSIVAFTDKGEILVGESAKRQAVTNPEKTIYSIKRIMGLMFNEDKAKEAEKRLPYKIVDRNGACAIEISGKVYTPQEISAKILMKLKEDAESYLGESVTEAVITVPAYFNDSQRKATKEAGTIAGLNVLRIINEPTSAALAYGLDKKESEKIMVYDLGGGTFDVTVLETGDNVVEVLATGGDAFLGGDDFDNRVIDFLSAEFKSETGIEIKNDVMALQRLKEAAENAKKELSSAMETEINLPFITADATGPKHLVKKLTRAKFESLTEDLMEETISKIESVIKDAGLTKNEISEVVMVGGSTRIPKVQERVKAFINKDLNKSVNPDEVVAVGASIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMTKVIDRGTTIPAKKSQVFSTAEDNQPAVSIMVLQGERELARDNKSLGKFDLQGIAPAPRGVPQIEVTFDIDANGILTVSAQDKNTGKSQEIKISGSSGLSDSEIEKMVKDAELHKEEDARKKEVIEARNHADSLAHQTQKSLDEHKTNLNENDANEIQNAINALKDCIKNDNATKAELEDKTKLLAQAAQKLGEAMANKNNAEQPKKKDDDVIDAEVE", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MNNSINHKFHHISRAEYQELLAVSRGDAVADYIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHIESSMMTPVTFETATLPRGLTTVICDPHEIVNVMGEAGFAWFARCAEQARQNQYLQVSSCVPALEGCDVNGASFTLEQMLAWRDHPQVTGLAEMMDYPGVISGQNALLDKLDAFRHLTLDGHCPGLGGKELNAYITAGIENCHESYQLEEGRRKLQLGMSLMIREGSAARNLNALAPLINEFNSPQCMLCTDDRNPWEIAHEGHIDALIRRLIEQHNVPLHVAYRVASWSTARHFGLNHLGLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDAQTLQAEESARLAQSAPPYGNTIARQPVSASDFALQFTPGKRYRVIDVIHNELITHSHSSVYSENGFDRDDVSFIAVLERYGQRLAPACGLLGGFGLNEGALAATVSHDSHNIVVIGRSAEEMALAVNQVIQDGGGLCVVRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAARECGPLPDEPFIQMAFLSLPVIPALKLTSQGLFDGEKFAFTTLEVTE", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family."}
{"protein": "MRDKIRLNSSAGTGHFYTTDKNKKTMPEKFEIKKFDPVVRKHVMYKEGKIK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MDPAPSLGCSLKDVKWSPVAMPLDLLVSTYRLPQIARLDSGECVEGLRENDFLLIHSCRQWTTITAHSLEEGHYVIGPKIEIPVHYAGQFKLLEQDRDIKEPVQYFNSVEEVAKAFPERVYVMEEITFNVKVASGECNEDTEVYNITLCTGDELTLMGQAEILYAKTFKEKSRLNTIFKKIGKLNSISKLGKGKMPCLICMNHRTNESISLPFQCKGRFSTRSPLELQMQEGEHTIRNIVEKTRLPVNVTVPSPPPRNPYDLHFIREGHRYKFVNIQTKTVVVCCVLRNNKILPMHFPLHLTVPKFSLPEHQVKGDMWPETLVHHWLGICQEQFDIDEYSRAVRDVKTDWNEDCKSPKKGRCSGHNHLPNSLSYARDELTQSFHRLSVCVYGNNLHGNSEVNLHGCRDLGGEWAPFPHDILPYQDSGDSGSDYLFPEANEESAGIPGKTEVPYEELWLEEGKPSRQPLTRSLSEKSRCDTLRGSTRSTCAPSSPPTPATLGATIKSSEIALPPPPVPPKSEAVREECRLLNAPPVPPRSAKPLSTSPSIPPRTVKPVRPQTRSPSPTLSYYSSGLHNIITQSDTSPPNSAPVSCYPCTRVKSDSVDPKSPFGSPSAEALSSRLSWPNHYSGASENQTRSDFLLDPSRSYSYPRQKTPGTPKRTCPAPFDFEGCELLGSPPSTTSAEFSSSGVPSCPKSASYCLENSEDNSFAAGMTKQSVSCPALPPRAPKPVEQKATPETSPLPLKIDGAEEDPTAGSLDLSEDQYFVRKGMQDIFSVSYPFSSPLHLQLAPRSCGDGSPWQPPADLSGLSIEEVSKSLRFIGLSEDVIAFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKILQFINGWRPKI", "text": "FUNCTION: Acts as an adapter protein that plays a role in intracellular signaling cascades triggered either by the cell surface activated epidermal growth factor receptor and/or cytoplasmic protein tyrosine kinases. Promotes activation of the MAPK/ERK signaling pathway. Plays a role in the regulation of cell proliferation (By similarity). SIMILARITY: Belongs to the GAREM family."}
{"protein": "MSKPILSTASVLAFERKLDPSDALMSAGAWAQRDASQEWPAVTVREKSVRGTISNRLKTKDRDPAKLDASIQSPNLQTVDVANLPSDADTLKVRFTLRVLGGAGTPSACNDAAYRDKLLQTVATYVNDQGFAELARRYAHNLANARFLWRNRVGAEAVEVRINHIRQGEVARAWRFDALAIGLRDFKADAELDALAELIASGLSGSGHVLLEVVAFARIGDGQEVFPSQELILDKGDKKGQKSKTLYSVRDAAAIHSQKIGNALRTIDTWYPDEDGLGPIAVEPYGSVTSQGKAYRQPKQKLDFYTLLDNWVLRDEAPAVEQQHYVIANLIRGGVFGEAEEK", "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 and Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). Involved in crRNA production or stability. The Csy ribonucleoprotein complex binds target ssDNA with high affinity but target dsDNA with much lower affinity. SIMILARITY: Belongs to the CRISPR-associated Csy3 family."}
{"protein": "MFISEIQLKNYRNYEKLELSFEDKVNVIIGENAQGKTNLMEAIYVLAMAKSHRTSNDRELIRWDEDFGQIKGKLQKRNSSLSLELNISKKGKKAKLNQLEQQKLSQYIGVMNVVMFAPEDLNLVKGSPQVRRRFLDMELGQIAPVYLYELSQYQKVLTQRNHLLKKMQGNSKNEETMLDVFTLQLIEHGTKILRKRFEFLHLLQEWAAPIHRGISRGLEELEIVYKPSVDVSESMDLSKIKEVYYESFQSVKQREIFRGTTLIGPHRDDLQFFVNSKNVQVFGSQGQQRTTALSLKLAEIELIYSEVKEYPILLLDDVLSELDDYRQSHLLNTIQGKVQTFVTTTSVDGIEHETLKEAKTIHVTNGTVDCEIDRA", "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": "MQLDDDLEFAKKIFNPNRAFAKQARIKNMCEYKDLVHEANEDYEHFWGELAKQKLTWFKPFDKVLNSDNAPFFKWFENGKINVSYNCIDRHLKDKKNKVAIIFEGEMGDYNVITYRKLHSEVNKTANLLKNEFNVKKGDRVIIYMPMIVESVYMMLACARIGAIHSIVFAGFSPEALRDRINDAQAKLVITADGTFRKGKPYMLKPALDKALENNACPSVEKALIVIRNAKEIDYVRGRDFVYNEMVNYQSDKCEPEMMDSEDPLFLLYTSGSTGKPKGVQHSNAGYLLWAQMTMEWVFDIRDNDNFWCTADIGWITGHTYVVYGPLACGATTLILEGTMSYPDYGRWWRMIEEYRVDKFYTSPTAIRMLHAKGENEPLKYNLESLKVLGTVGEPINPTAWKWFYEKIGNSKCSIVDTWWQTETGGHIISPLPGATPIRASCATLPLPGIHAEVLNEDGTKTKPGEQGFLCITKPWPSMVRNIWGDEKRYIDSYFSQIKLNGEYVYLSGDGAIVDENGYITIIGRTDDIVNVSGHRIGTAEVESAISKHEMVVECAVVGIPDTIKGEGLFAFVVLCDGAKCNLGESLELLKEMNHILSVEIGKIAKLDNVMYVPGLPKTRSGKIMRRLLKSIAKKEPITQDLSTLEDVNVVKEIMSIVQMEE", "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": "MSNDEKQLTKEEMKAIKLQAKEEAKMNDLLKERRQKLSDAQERGKDPFDVYKVERTHTSKQIVDNYDELEDKIVTVAGRLMSKRVHGKAGFSDIYDRYGKIQLYLKIDDVGEEKLKEFKTFDIGDFVVITGKVFKTKTGEITLHVTKLELIAKSLKPLPEKFHGLKDPDLKYRQRYVDLIINQDVRETFMKRTAIIKAVREFLDNKDYLEVETPVLSTIASGASARPFSTHHNALDLDMHLRIATELYLKRLIVGGFEKVYEIGKDFRNEGIDVRHNPEFTMIELYEAYADYNDMMEITENMVAYACQKVNGTTKITYEGTEIDLTPPWRRVTMVDIVKEHSGIDFSTVKTDEEAREIAKEKKLELKKELKDCTKGDILNALFEEYGEKKLIQPTFVCDYPVEISPLTKKKRGNPEYTERFEGFIYGREICNAYSELNDPIVQKDRFMQQLKERELGDDEAYQMDDDFINALEIGMPPTGGMGMGMDRLVMFLTDSPSIRDVILFPTMKPTPNRD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MAVAVVTSRRMINIGNSIRRCFILNHRFFSTELTPTTITPINQDHLLRVCTILYQQQNSPDSRLVSKLSSTKFQLTHEFFLQVCNNFPLSWRPVHRFFLYSQTHHPDFTHTSTTSNKMLAIIGNSRNMDLFWELAQEIGKRGLVNDKTFRIVLKTLASARELKKCVNYFHLMNGFGYLYNVETMNRGVETLCKEKLVEEAKFVFIKLKEFIKPDEITYRTMIQGFCDVGDLIEAAKLWNLMMDEGFDVDIEAGKKIMETLLKKNQFDEASKVFYVMVSKRGGDLDGGFYRVMIDWLCKNGRIDMARKVFDEMRERGVYVDNLTWASLIYGLLVKRRVVEAYGLVEGVENPDISIYHGLIKGLVKIKRASEATEVFRKMIQRGCEPIMHTYLMLLQGHLGRRGRKGPDPLVNFDTIFVGGMIKAGKRLETTKYIERTLKRGLEVPRFDYSKFLHYYSNEEGVVMFEEMAKKLREVSLFDLADIFQRYGEKMTTRERRRDRDQLLKT", "text": "SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MNLVAVGVNHTTADVELRERLAFSTQQAEVALASLREMPGVREAALLSTCNRTELYCLTDDVTPNFAQWLASSRNLSVERLSTVLYQHTGEQALEHMMRVAGGLDSLVLGEPQILGQMREAYARAHEAGLLNGELSRLFQEVFSVAKRIRTETGIGANPVSVAYAAVSFARHIFADLKKSRALLIGAGEMIELVARHLSEQQVQEITIANRTQERASELAAAVGGRGISLEELPVALERADILISCTAAPLPIMGKGMVERALKKRRHRPMFMVDIAVPRDIEPEVGELGDVYLYTVDHLQEAIQENVRSRQQAAQEASELIRDAIVRHRRQRREQDAVKVLRDYREQRKAMAESELEKALQQLRNGGDAEQVLRRFQHSLVNKWLHSPSVTLRKMAADGRAEALLLARELLLDDDQS", "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": "MAAQRHIDINSTQVWAKLHQHQRATRHMHMRELFELDPQRFQRFSLELDGLLLDYSKNRVTERTLELLFDLARKADLRGWMDRMRSGERINVSENRSVLHTALRLPAGARLDLEGHNVAADVHQVLARLKDFSEQVREGRWLGFAGQPIRDVVNLGIGGSDLGPLVAADALAAYAHPDLKVHFVSNVDGQHLARTLERLNPATTLFIVASKSFTTPETLLNAQAARAWFLQAAGEAQIAKHFVAVSTNEPAVRAFGIDPQHMFGFWDWVGGRYSVWSAIGLPVMLSIGYDNFRAFLDGGHAMDRHFFESPFDANMPVLLALIGIWYNTFYRAHTHAIMPYDHGLRRLPAHIQQLDMESNGKRVGRLGEALDFDTGPVIWGEEGANSQHAFFQLLHQGTRLVPCDFILPLNSHYPLGNQHDVLVANCLAQTEALMRGKNEAEVMRELSHLSGEQLDMLLPQKLFPGNQPSNTLALDRVTPYSMGMLMALYEHKVFVQGVIWGINSFDQWGVEYGKQLARRILPELSGDTGALGHDSSTNGLIRHYRERHGK", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MTDKTFADRIDALEMRLTYQEETIETLNQAVTAQWKQIDALTRQVAELGERMREAEANRPGPTNEPPPHY", "text": "SIMILARITY: Belongs to the SlyX family."}
{"protein": "MALQIYNTLTRRKEPFVPLEAGTVKMYVCGVTVYDYCHLGHGRTYVVWDTVRRYLISRGYAVTYVQNFTDVDDKILRRAQQEGTTMEAVAEKYIAAYFEDMDRLNVLRADSYPRATQTMPEIGALIDRLTSIGYAYPAAGDVYYSVRRFAEYGKLSGKRLAELEAGASERLQDEELARKKDPFDFALWKGAKPGEPAWDSPWGAGRPGWHIECSAMVRKSLGETIDIHAGGEDLQFPHHENEIAQSEAVTGKPLARYWMHNAFLNVVNSSGAEEKMSKSLGNFKTLRDLFEVFPPMALRLFLLKTSYRNPIAFSAEAFKGSEQNWRELEEVLQLAGWIAGQGRPATDDIESEPWVRRFNEAMDDDFNTAAALAEVIALGKQLAGRYHAAIHGTPLADPARFAREWRTFALLCDILGLKAAEPEARQSALPEAEIEAQIALRRQAREERNWAEADRIRKQLLDQGIVLIDHKEKPTTWRHADP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MAAESDVLHFQFEQQGDVVLQKMNLLRQQNLFCDVSIYINDTEFQGHKVILAACSTFMRDQFLLTQSKHVRITILQSAEVGRKLLLSCYTGALEVKRKELLKYLTAASYLQMVHIVEKCTEALSKYLEIDLSMKNNNQHTDLCQSSDPDVKNEDENSDKDCEIIEISEDSPVNIDFHVKEEESNALQSTVESLTSERKEMKSPELSTVDIGFKDNEICILHVESISTAGVENGQFSQPCTSSKASMYFSETQHSLINSTVESRVAEVPGNQDQGLFCENTEGSYGTVSEIQNLEEGYSLRHQCPRCPRGFLHVENYLRHLKMHKLFLCLQCGKTFTQKKNLNRHIRGHMGIRPFQCTVCLKTFTAKSTLQDHLNIHSGDRPYKCHCCDMDFKHKSALKKHLTSVHGRSSGEKLSRPDLKRQSLL", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAGHTQQPSGRGNPRPAPSPSPVPGTVPGASERVALKKEIGLLSACTIIIGNIIGSGIFISPKGVLEHSGSVGLALFVWVLGGGVTALGSLCYAELGVAIPKSGGDYAYVTEIFGGLAGFLLLWSAVLIMYPTSLAVISMTFSNYVLQPVFPNCIPPTTASRVLSMACLMLLTWVNSSSVRWATRIQDMFTGGKLLALSLIIGVGLLQIFQGHFEELRPSNAFAFWMTPSVGHLALAFLQGSFAFSGWNFLNYVTEEMVDARKNLPRAIFISIPLVTFVYTFTNIAYFTAMSPQELLSSNAVAVTFGEKLLGYFSWVMPVSVALSTFGGINGYLFTYSRLCFSGAREGHLPSLLAMIHVRHCTPIPALLVCCGATAVIMLVGDTYTLINYVSFINYLCYGVTILGLLLLRWRRPALHRPIKVNLLIPVAYLVFWAFLLVFSFISEPMVCGVGVIIILTGVPIFFLGVFWRSKPKCVHRLTESMTHWGQELCFVVYPQDAPEEEENGPCPPSLLPATDKPSKPQ", "text": "FUNCTION: Associates with SLC3A2/4F2hc to form a functional heterodimeric complex that translocates small neutral L- and D-amino acids across the plasma membrane. Preferentially mediates exchange transport, but can also operate via facilitated diffusion (By similarity) (PubMed:10863037). Acts as a major transporter for glycine, L- and D-serine in the central nervous system. At the spinal cord and brainstem regulates glycine metabolism and glycinergic inhibitory neurotransmission by providing for glycine de novo synthesis from L- serine and glycine recycling from astrocytes to glycinergic motor neurons (By similarity). At Schaffer collateral-CA1 synapses mediates D-serine and glycine release that modulates post-synaptic activation of NMDA receptors and excitatory glutamatergic transmission (By similarity). May regulate D-serine release from mesenchymal progenitors located in developing subcutaneous adipose tissue, favoring white adipocyte over thermogenic beige adipocyte lineage commitment (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Colocalizes with OLIG2 in astrocytic processes. Localizes to the plasma membrane in mature adipocytes and to intracellular structures in preadipocytes. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
{"protein": "MASKLFLAAALLQGALSSPLAVEERQACAAQWGQCGGQDYTGPTCCQSGSTCVVSNQWYSQCLPGSSNPTTTSRTSTSSSSSTSRTSSSTSRPPSSVPTTPTSVPPTITTTPTTTPTGGSGPGTTASFTGNPFAGVNLFPNKFYSSEVHTLAIPSLTGSLVAKASAVAQVPSFQWLDIAAKVETLMPGALADVRAANAAGGNYAAQLVVYDLPDRDCAAAASNGEFSIADGGVVKYKAYIDAIRKQLLAYSDVRTILVIEPDSLANMVTNMGVPKCAGAKDAYLECTIYAVKQLNLPHVAMYLDGGHAGWLGWPANLQPAADLFGKLYADAGKPSQLRGMATNVANYNAWDLTTAPSYTTPNPNFDEKKYISAFAPLLAAKGWSAHFIIDQGRSGKQPTGQKEWGHWCNQQGVGFGRRPSANTGSELADAFVWIKPGGECDGVSDPTAPRFDHFCGTDYGAMSDAPQAGQWFQKYFEMLLTNANPPL", "text": "FUNCTION: Exoglucanase that plays an important function in biomass degradation by catalyzing the hydrolysis of the non-reducing end beta- 1,4-glucosidic linkages in cellulose and cellotetraose to release cellobiose. Shows higher hydrolytic activities on phosphoric acid- swollen cellulose (PSC), beta-glucan, and cellooligosaccharide derivatives than on cellulose, of which the best substrates were cellooligosaccharides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family."}
{"protein": "MGLKAKHKENLCSDSQRSKRLYVWIALAIVLSDFTSIFSHWIWGLLILILRTLMDLPTFVMNV", "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": "MDAKVYVGGLPSDATSQELEEIFDRFGRIRKVWVARRPPGFAFVEYDDVRDAEDAVRALDGSRICGVRARVELSTGQRRGGGGRGGGFGGRGGGGRDRSPYRGDRGRSRSRSRDRGRDRSRDRSRDRSRDRSRDRSRERSRERERTRSRSRSPQERDRSHSKSRSRSRSRSRSRSASPH", "text": "FUNCTION: Plays a functionally redundant role in shifting germ cell sexual differentiation in hermaprodites. Required for the development of somatic gonad structures and for progression from larval stage to adulthood. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
{"protein": "MEGVFNNKKFILVFVFMLGLCIGITTVHGQGTRVGFYSRTCPRAESIVRSTVRSHVNSDPTLAAKILRMHFHDCFVQGCDGSILISGPATEKTAFANLGLRGYEIIDDAKTQLEAACPGVVSCADILALAARDSVVLSGGLSWQVPTGRRDGRVSQASDVSNLPAPSDSVDVQKQKFAAKGLNTQDLVTLVGGHTIGTSECQFFSNRLFNFNGTAAADPAIDPSFVSNLQALCPQNTGAANRVALDTGSQFKFDTSYFSNLRNRRGVLQSDQALWNDPSTKSFVQRYLGLRGFLGLTFNVEFGKSMVKMSNIGVKTGTDGEIRKICSAFN", "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": "MASVKLASLMVLFATLGMFLTKNVGAASCNGVCSPFEMPPCGSSACRCIPVGLVVGYCRHPSGVFLRTNDEHPNLCESDADCRKKGSGNFCGHYPNPDIEYGWCFASKSEAEDFFSKITQKDLLKSVSTA", "text": "FUNCTION: PA1b binds to basic 7S globulin (BG) and stimulates its phosphorylation activity. Involved in the signal transduction system to regulate the growth and differentiation as a hormone peptide. Toxic to various insects through binding to a high affinity binding site in the insect gut (By similarity)."}
{"protein": "MTALTGRPVVYCGVCSLPPEYCEYGGTVKKCQQWLEKNQPTMYSRIWSPEVLEAEMASLSVEAQERAMKDAKKKAAKAEAAEQKQADKRANSVVTIKRIERNKRKYVTSVSGLEAFGLELKKVAKDFGKKFATGSSVTKVPSGGEEIVVQGDVSGEIEEFILEKYKEVPEDNIELVEDKKKKKGEGN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DENR family."}
{"protein": "MSENGLKEQITGKVEKTKGQVKEGIGEVTEDRKLKNEGKWDKTKGTIKEKVGKVKQKISDGLDNKE", "text": "SIMILARITY: Belongs to the UPF0337 (CsbD) family."}
{"protein": "MSFSLFRKAPKFWERRGPTSLLLWPLSWLYGLILRARKLIHDLGIVRTKPTPVPIIIVGNIRVGGTGKTPIVIALAKRLSQLGWKPGIISRGYGSSSQTAPLLVRSDSSPSLVGDEPVLIAKRTDNQFPIWVYPKRQQSIQALLKHSPEVDVIISDDGLQHRGLTRWPAREGGRDIEFVVRDSRGEGNRFLLPAGPLREPATRDRDATLFTGNPSFNEKKTGILDEYFLGRRAFSLGTYLGRPYQLIDHANTQSLEQIAEQFLPKSMTAIAGLGNPQRFFDDLAKQGVTCKQIPLPDHAQYTPEFFAKVKAQCLLITEKDAVKCAEISDERIWVVPMSLHLPENFVEWLQSILQRPDPHRYTL", "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": "MTCCGCSGGCGSSCGGCGSSCGGCGSGCGGCGSNCGGCGSSCCKPVCCCKPVCCCVPVCSCSSCGGCGSSCGGCGSCGSSCGGCGSSCCKPVCCCVPVCSCSSCGGCKPCCCQSSCCKPCCSSGCGSSCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCSSGCGSSCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCSSGCGSSCCQDSC", "text": "FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated protein (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 5 family."}
{"protein": "MRLFVGLGNPGAKYARNRHNIGFMAVDEIARRHGFSPWRRRFQGETSEGALGTERVILLKPTTYMNDSGRSVQEAAGFFKIAPGDVTVFHDELELPPGKVRVKVGGGIAGHNGLRSISAHIGNDYRRVRLGIGHPGVKELVHGHVLSDFAKADNDWVATLCDAVAEHAALIAKGTDATFANRVHLAMQAKGFLTKDDNGKE", "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": "MTAFKSDFLNILQERGFIHQCSDFEGLDALAAKGEATAYVGYDCTARSLHIGNYLTMMMLHWLQQSGNKPITLMGGGTTMVGDPSGKDETRAMRTVAEIEANKESIRGVFAKVLRYGDGKSDAVMLDNAEWLTKLNWIEMLRDVGRHFSVNRMLTMDSVRLRLEREQEMSFIEFNYMVCQAYDFVELAKRTGCKLQMGGSDQWGNIIMGVDLGRRMGTHQLFALTTPLLTTASGAKMGKTAQGAVWLNADQFSPYDFWQYWRNTEDADVGKFLKLFTTLPMSEIGKLEALGGSEINEAKKVLATEATALLHGRDAANEAAETARRTFEEGALAESLPTVEIPRGELDAGFGVLNAFVKAGLVASNGEARRQIKGGGLRVNDEPVTDDKMALSAAHLTPEGVIKLSFGKKKHILIKPA", "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": "MVFVKMTDVYLMIVMLMGLGFSIELSNGHKFYVGGRDGWVLTPSEDYSHWSHRNRFQVNDTLYFKYVKGKDSVLEVSEKEYNTCNTTHPLTSLSDGDSLFLLSRSDPFFFVSGNSGSCLKGQKLAVTVMSTGHHSHTPRHPSPSPSPSASPVRKALLSPAPIPVHKALSSPAPTPGVDPSHSEVLAPAPGPAAAVRNLAGSVAPGVISLGLVLVIMISSMV", "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": "MNIILMGPPGAGKGTQAELLKARFPIPHISTGDIFRDAVNQGSELGQEAQKYMSSGQLVPDEITTAIVKERITQADCDSGFLLDGFPRTTDQAQALDQSLAELGKKVDLAINIDVPTQLLIERLSGRISCRECKRVYNLNFNPPREQGKCDSCGGELVQRNDDRGETVVKRLEVYNQQTRPLLQYYEAQGVLFNIEGSRGSGQVFADIQEKLESL", "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": "MIDLPFLLAEEIEGGLFDFNGTLPLMALQFLTLMVLLNTIFYKPVTKVLDERDEYIRTTLTTASSMLVKADELAAKYEEDLSEARRNAQLKIASSQKEAQNIVSEDIKKAQLNAEKLIAEASKQLNVQKEEALKTLENQVDTLSDQIKVKLLSSQS", "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": "MTQGKRKHPCDLKNPSKRAPPATCNKPNGAILCGDFCLHEGYNIGKCVMRRTGKACICSQCEGW", "text": "SIMILARITY: Belongs to the DEFL family."}
{"protein": "MTEQIKKTFLKAKEENKNVLVTFVTCGFPNVDETIKIMQGLQNGGAGIIELGIPFSDAVADGPTICKGNEIALKNNITLEKVFETVKLARDAGVTIPIILMGYYNPIFSYGDAKTIQKAKEVGANGFIIVDLPPEEAVGFREECKKQGVSFVPLVAPSTTDRRMELLASVADSFIYVVSRMGSTGSSATGVINTALPQLCQRVRKFAGDTPLAVGFGVNTSEHFHQVGSVSDGVVVGSKIIDLILKAEPGTAATVVEEYCKYLTKEDPSAPVPKQFQSGGSVATAPPAAVVEPINEMYLPQKYGMFGGMYVPEALTQCLVELESVFYKALHDEKFWEEFRSYYEYMGRPSALDYAKRLTEYCGGAHIWLKREDLNHGGSHKINNCIGQILLAKRLGKNRIIAETGAGQHGVATAICAAKFGMKCTIYMGAEDCRRQALNVFRIRLLGAEVVPVTSGTQTLRDAVNEALKAWVEQIDTTHYLIGSAIGPHPFPTIVKTFQSVIGEETKAQMQEKRKKLPDAVVACVGGGSNSIGMFSPFKADKSVMMLGCEAGGDGVDTPKHSATLTMGKVGVFHGVRTYVLQREDGQIQDTHSISAGLDYPGVGPELSELKYTNRAEFIAVTDAQCLEGFRALCHLEGIIPALESSHAVYGGMELAKKLPKDKDIVITISGRGDKDVQSVAEQLPILGPKIGWDLRF", "text": "SIMILARITY: In the N-terminal section; belongs to the TrpA family. SIMILARITY: In the C-terminal section; belongs to the TrpB family."}
{"protein": "MVCLFENLMNMIKYSIYILPLIILIVLSISIKKDVQRVHIIIQSLKLTLIVIMIVIGIEESIYVKLNGHLIKTELIKLFEYLLLGVSYMIIKMFEEGVTEGKKTKITDEGLILIYSSIIGMLISMEAHNLITLFLSLEISSICFYILALNKNSRKGIEGGLKYYIIGGIATTILLLGIVSIYKSTGSLMYTDLLVIVMENTDDYRIQMGIALIVLGLILKLGIAPFHGWLIDVYEGAGMLMTFYLTITQKLVTLMVLINLYQNLIIYTNAIMFTNGLIILILVTLVVGTIGSLRQQKLIRFIAYSAIVNSALLILMLAGSMSEELMVNSVYYLINYIIGLTVLMSLIMGFLRLNDRGTIEDIYQLKNMWVINMFGAIVYILVLMYLAGLPPMTNFISKILILLPYMVLGRVYLTMLAFFLSVGVMIYYMNLVKIIIIDKVQTHEQGVAELEITSKPTKGGRRIVLGVMWLIFSQLYLDEILNVIKVIVALI", "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": "MANLQERKSFSKPRISIQASGGTPEAKGIEKRKLSQKRRTLPLQLSLGGHLSPWPTYTSGQTVLHNRKPCSDDSRNRANSCQQQSMSISKPKYLEQLENYLRKELLLLDLSTDSAQELRLQPYREIFEFFIEDFKTYKPLLSSIKNAYEVMLAHQKERIRSLEPLKAKIVTMNEDCSERVLAMRAEERYEISVLKKEKMNLLKLIDKKNEEKISLQSEVAKLRRSLAEEYLRYLTERDARKILIGDLNELRYQQEDMSLAQTPGVWGEDPVKLTLALKMTRQDLTRTQMELNTMKANSGDVVPRRDLEMQEKTNMELQEQLESLKADYEEVQKEHELLLQLHMSTLKERDQFYNELQEIQRTSTPRPDWTKCESIIAGGPERWLVLAEGKNSDQLVDVLLEEIGMGLLREKDFFPGLGFGDAIPPFLRFDGPVKNKKPSKKEVVNLLKDAWKERIAEEQKEPFPDFFFNFLERRFGVNDAMAWAYTIFENIKLFRSSEIMNQFYAVLMGKNLESVYINQKKTLSHLLKELLSVDTQNEGSITMEQFSTILKTTFPLKKEEQIQELMEAVGWGPDSSNTDMLNYRSLFNEDEEGQSEPFVQRLWEQYESDKEAYLEELKQELDLDPLEDVTLLKMRGTLMNIDPTMDKQTLSAYLSQAYQIPAIDVPLEDEEKQGIISIKVETALDRLRMADTKRVGPREPDPAS", "text": "FUNCTION: Possible role in spermatogenesis. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region."}
{"protein": "MNTFGRELRITTFGESHGRAIGVVIDGVPAGLPLTEEDIRKELDRRMFCHIHWLNPRCEPEEFEILSGVKDGHTQGTPIAIVIWNKKAISSYYDELWMKPRPGHADLAYYLKYGKFYDHRGGGRASGRTTAAIVAAGAVAKKLLALVGAEVAGHIVELGGVEVKRPYTFEDVKKSWEKPLPVVDDDALAAMLEVLRKNAAEGDSVGGGVEIWAVGVPQGLGEPHFGKIRADLAHAAFSVPAVVALDWGAGRQLAKMRGSEANDPIVVKGGKPGLETNKIGGVLGGITIGEPLYFRVWLKPTPSVRKPQRTVDLAKMEPATLQFKGRYDVSVVPKALVALEAMTAITLADHLLRAGVIRRDRPLKDPVV", "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": "MDKVTSEEFLITLLLSYFRIVSFLFTFPFYGSFLIPNTIRLYLAFALSFAVLSFINITPVKVNTFVEFLVYALNELLFGFSAGLILRLLFDALIIAGELIALHTGLGFLQMFIPGMTQMSLFSGFFTLYGTLIFLSLGGGEFIILGLAESFKRLPVGSFNIFYLNPEVFLNFFYESFRLGVKIAMPLILTALILNLVLAVVNRFIPQMNVFMVGLPLQVSIGLIILLLSLPLITITMSNHFQDFFKVFEYFIQSFKSP", "text": "FUNCTION: Role in flagellar biosynthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Bacterial flagellum basal body. SIMILARITY: Belongs to the FliR/MopE/SpaR family."}
{"protein": "MAVSRATLFDKVWDLHTVGTLASGQTQLFIGLHLIHEVTSPQAFAMLRERGLGVLYAERTVATVDHIVPTQSQQRPFADTLAEQMIRALEDNCAEFGIRFYNIGSGSQGIVHVIAPEQGFTQPGMTIACGDSHTATHGAFGAIAFGIGTSQVRDVLATQTLALDKLKVRRIEMNGSLHPGVFAKDVILHIIRKLGVKAGVGYAYEFAGTTFEAMNMEERMTVCNMAIEGGARCGYINPDAVTYAYLKGRDFAPQGADWERAVAWWENLRSDPDAQYDDTIHFDAAEIAPTVTWGITPGQGIAVDEIVPRPEELPGEDRPLAEEAYRYMDLAPGVPIVGTKVDVCFIGSCTNGRLSDLREAANLARGRHVAPGVKAFVVPGSERVKRQAEAEGLHEVFLEAGFEWREPGCSMCLAMNPDRLEGRQLSASSSNRNFKGRQGSASGRTLLMSPAMVVAAAVSGAVADVRALLEPTP", "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": "MAVISVKPRRREKILQEVKNSSVYQTVFDSGTTQMQIPKYENKPFKPPRRVGSNKYTQLKPTATAVTTAPISKAKVTVNLKRSISAGPTLNLAKKPNNLSSNENTRYFTIMYRKPTTKKHKTWSGDGYATLKASSDKLCFYNEAGKFLGSSMLPSDSDSLFETLFKAGSNEVQLDYELKENAEIRSAKEALSQNMGNPSPPTTSTTETVPSTKNDGGKYQMPLSQLFSLNTVKRFKSVTKQTNEHMTTVPKTSQNSKAKKYYPVFDVNKIDNPIVMNKNAAAEVDVIVDPLLGKFLRPHQREGVKFMYDCLMGLARPTIENPDIDCTTKSLVLENDSDISGCLLADDMGLGKTLMSITLIWTLIRQTPFASKVSCSQSGIPLTGLCKKILVVCPVTLIGNWKREFGKWLNLSRIGVLTLSSRNSPDMDKMAVRNFLKVQRTYQVLIIGYEKLLSVSEELEKNKHLIDMLVCDEGHRLKNGASKILNTLKSLDIRRKLLLTGTPIQNDLNEFFTIIDFINPGILGSFASFKRRFIIPITRARDTANRYNEELLEKGEERSKEMIEITKRFILRRTNAILEKYLPPKTDIILFCKPYSQQILAFKDILQGARLDFGQLTFSSSLGLITLLKKVCNSPGLVGSDPYYKSHIKDTQSQDSYSRSLNSGKLKVLMTLLEGIRKGTKEKVVVVSNYTQTLDIIENLMNMAGMSHCRLDGSIPAKQRDSIVTSFNRNPAIFGFLLSAKSGGVGLNLVGASRLILFDNDWNPSVDLQAMSRIHRDGQKKPCFIYRLVTTGCIDEKILQRQLMKNSLSQKFLGDSEMRNKESSNDDLFNKEDLKDLFSVHTDTKSNTHDLICSCDGLGEEIEYPETNQQQNTVELRKRSTTTWTSALDLQKKMNEAATNDDAKKSQYIRQCLVHYKHIDPARQDELFDEVITDSFTELKDSITFAFVKPGEICLREQ", "text": "FUNCTION: Involved in the recombinational repair of double-strand breaks (DSB) in DNA during mitosis and meiosis. Has DNA dependent ATPase activity. Promotes D-loop (displacement loop) formation with RAD51 recombinase. Modifies the topology of double-stranded DNA during the D-loop reaction to facilitate the invasion of the homologous duplex molecule by the initiating single-stranded DNA substrate. Required for adaptation from G2/M checkpoint arrest induced by a double strand break, by participating in monitoring the extent of single-stranded DNA produced by resection of DNA ends. This role is distinct from its roles in recombination. Promotes colocalization of RAD51 and DMC1 during meiotic recombination. Involved in crossover interference. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNF2/RAD54 helicase family."}
{"protein": "MVGGERFNIPVPQSRNITKNHQQLKNRQKNKDQNSQMKKTYMKKERGHGCNSLSGAWQAMQKAGKNNVHFPCNQNWSPNLSNRNLFFSPQTNQNYAGAKFSEPPSPSVLPKPPSHWVPVSFKPSDKEIMTFQLKTLLKVQA", "text": "FUNCTION: Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Also acts as a nuclear receptor coactivator (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, P-body. SIMILARITY: Belongs to the PNRC family. PNRC2 subfamily."}
{"protein": "MVEVTIWLAFFAGVVSFLSPCVFPLVPVYLAQLTGTQISGNEITADRKLILMRSLGFILGFTSIFIFLGASSTFIGQLFWGNRQLFEQIGGIIITVFGLQMMGVISIRMLLSEKRLQAKPRQSASFANSVLIGFLFATGWTPCIGLVLGAILVLAGDANTMWSGMSMLFVYSMGLAIPFFLVALLWSRSLHKVRKLNKWLPTIQKGSGVVMVALGVLLFTGQFSTIAAYLARINPFGI", "text": "FUNCTION: Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbD family."}
{"protein": "MTPTIITDVKAFAIKPDRHNLVVVKVETNKGVSGLGCATFQFRPLAVKTVVDEYLRPLLLGRDANQIEDLWQVMNVNSYWRNGPITNNAISGVDMALWDIKGQLADMPLYQLLGGKARTAIPAYTHAVADNLEDLYQEIDRFLAEGYRYIRCQLGFYGGNPSQLQTPDQPIAGSYFDQTDYMDTTLKMFAAIQERYGNQFQMLHDVHERLHPNQAIQFAKAAEPFNLFFLEDILPPDQNKWLQQLRSQSATPIATGELFNNPMEWQELVKNQQIDFMRAHVSQIGGITPALKLAHFCDAMGIRIAWHTPSDISPVGLAVNNHLNIHLHNAAIQETIAIPANTQSVFGGSPQPENGYFYPIEKSGIGITFDEAAAAEFPVVYRPHEWTQSRTPDGTLITP", "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": "MADDATRKAVSEIPLLKTNSGPRDKELWVQRLREEYLAPIKYVENNKAADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDIPVTYPTTAPEVAIPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLISKGLITHREQQGS", "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": "MLHCITTIFLSISRMTMEDGPIAESYFTAYADVCFREFGNHVKFWTTINEANVFTIGGYNDGTSPPGRCSNCSSGNSSTETYIVGHNLLLAHASVSRLYQQKYKDKQGGSVGFSLYAFEFIPQTSSSKDDEIAIQRAKDFFYGWILGPLTFGDYPDEMKRAVGSRLPIFSKEESEQVKGSSDFIGIMHYFPALVENIKLKPSLSRNTDFYSDMGVSLTYLGNFSGFGYDVFPWAMESVLEYIKQTYGNPPVYILENGTPMKPDLELQQKDTRRIEYLQAYIGAVLKAVRNGSDTRGYFV", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MVTRKKPVKRNAEAAEIQVEQEEDASQPKVAKELMVVAQEVKIIRALACNDVVERNRQIRILRKWFKARAGSSFPFNEDDFMRIWKGLYYTMWMSDKPLVQEELAEKLAQMVDSFGGNTACSLAYFSAFMRTMCQEYFGIDQWRMDKFLMLTRRMVRYLLRFLKQNNWNADLIAAFNSSMQLSVMSEQPKSRGMTMHYLDVFFEELAKAANGEITAAQVNMFLRPFVTYIATQRDAKLVAQCRTRVLYHLMYQSDLGRQYSEKYNAWKQMGFPTASIDDIEKLDSGFDEEDDEVNAEEEQPRATSLDPRAGNVDVHMPELPLNADCVLDELQTQLRTNDFNSKRRKGLRKLIQIFETYQRGEFPLGVRTMPKVEGQTLSEMVEQKVAALDKMEDEVFATGRKLKKLNKSKRKRLLQSINFEEVDEHNYDEVISKALPPELQKKVNYNAKVRSSINNAWVVEEVKEAEPKSKKAKKEEPPQQNKDDQTKVKKKSQLKPKNDQSKPKIEDQPTLKAEKEEPAKRKKLDHSKTKEEQSKPKTDEQPKPTPKVEGQSKAKPTPKTKAAGVDDDAPTNGWDAPLEDGEQDIFVPSRKLQVKQANSKLPQSTPKQPARAEFATPQTGSGKHVRIVTKSNCIYPKSDYYRQLKLSPQVPYDANRLPGKSALKPHWIPGPIHPSYKAKRLFNDTL", "text": "FUNCTION: May be involved in the generation of 28S rRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRP1 family."}
{"protein": "MGAAASIQTTVNTLSERISSKLEQEANASAQTKCDIEIGNFYIRQNHGCNLTVKNMCSADADAQLDAVLSAATETYSGLTPEQKAYVPAMFTAALNIQTSVNTVVRDFENYVKQTCNSSAVVDNKLKIQNVIIDECYGAPGSPTNLEFINTGSSKGNCAIKALMQLTTKATTQIAPKQVAGTGVQFYMIVIGVIILAALFMYYAKRMLFTSTNDKIKLILANKENVHWTTYMDTFFRTSPMVIATTDMQN", "text": "FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Note=Localizes to the membrane surrounding the core of mature virus particles (MV). SIMILARITY: Belongs to the orthopoxvirus OPG095 family."}
{"protein": "MEWKIDKDCVDYQMSLMFMQERVKQVINGSGDELVWMLQYEALYTGGTSADPQDLLNSDLFPVFNVGRGGKYTYHGPGQRVIYPILNLRSRNICDLHKYIYLLEEVVIVTLDNFGINGCRKEGHIGVWVGTGCQPPKKIAAIGVRVSKWVSYHGIAVNLYPDLSHYDAIIPCGIKNFGVTSAKEMGIEIRSFNAFDRYFKKSFVKIFGE", "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": "MSNTGLPKPWIVKISRSRNRPYFFNTETHESLWEPPAATDMAALKKFIANELQESVTPTEASNSPKIRASHLLVKHRESRRPSSWKEEHITRSKEEARKLAEHYEQLLKSGSVSMHDLAMKESDCSSARRGGELGEFGRDEMQKPFEDAAFALKPGEISGVVETSSGFHIIQRHA", "text": "FUNCTION: Has a role in the G1/S stage transition of mitosis where it is involved in the dephosphorylation of cdc25 and wee1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGLSISKLFQSLFGKREMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYRNISFTVWDVGGQDKIRPLWRHYFQNTQGIIFVVDSNDRERISEAHEELQRMLNEDELRDALLLVFANKQDLPNAMNAAEITDKLGLHSLRHRQWYIQATCATSGDGLYEGLEWLSTNLKNQ", "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": "MSHDADDKTYPYRKDDAELRRRLTPLQYEVTQHAATERAFTGEYTDKEDDGIYKCVVCDTPLFESGAKFHSGCGWPSYFKPLNGEVIDEKIDYSHGMVRVEVRCNHCGAHLGHVFEDGPRDKTGLRYCINSAALNFESRPEND", "text": "SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family."}
{"protein": "MKKNSFISVISDEKKEENKGSVEFQVFCFTNKIRRLTLHLELHKKDYSSQRGLRKTLGKRQRLLAYLLKINGVRYKELISKLNIRELKTR", "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 uS15 family."}
{"protein": "MDPTSKSGLNQVSDVVFVIEGTANLGPYFESLRNNYILPTIEYFNGGPPAETDFGGDYGGTQYGLVVFNTVDCAPESYVQCHAPTSSAFEFVSWIDSIQFMGGGAESCSLIAEGLSVALQLFDDFKKMREQIGQTHKVCVLLCNSPPYLLPAVESVSYTGCTADSLVQIIRDRGIHFSVIAPRKLPALRSLFERASSVAGLPESSHPDYSQDPFHMVLVRGIALPVAPGGGSVPVSLKPVLPPQSLPVNQNPLVPVASTAPQMNTFQNVSLHAAHDAAQKALEEAANQQQKNRFGQISTPPFSQSPVLPPGGKPSLSTVTTVSPPVLTQQQVPPQQPQQQTQVPQPGLPAVNQQPPQASQQQPNNQQTPPPTQPGMAAVPAPPPGAQQGVANKVVAWSGVLEWQEKPKASSMDSNTKLTRSLPCQVQVSQGENLNTDQWPQKLIMQLIPQQLLTTLGPLFRNSRMVQFLFTNKDMESLKGLFRIMTSGFAGCVHFPHSAPCEVRVLMLLYSSRKRIFMGLIPNDQSGFVNGIRQVITNHKQVQQQRSMQPGQVQPNQNFLNRPPGPIPVTHGNVPQQLRAAATGNQQAPVTGAPPNQVQGQAQAPGGGMLRLQNPGANPQLRSLLLSQQPQGGMQGMQGMHPIQQMVHAAPGGGAQMQPQWRQPHQGPLMVPTGPRGPVTQNPGMPSVSSVMEDEILMDLI", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 25 family."}
{"protein": "MRILGLDLGKKTIGVAVSDPLGFTAQGITTIRRANKEKDMEELRKICDEYKVETIVIGLPKNMNGTIGPSGEIAMEMGKLVEEALNIKVEFWDERLTTVAAHKAMLEADLSRSKRKKIVDKVASTYILQGYLDRISK", "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": "MKPSGLTFAFLVVFMMAIMYNSVQVTADADADAEAEALANALAEAGILDWGKKVMDWIKDKMGK", "text": "FUNCTION: Antimicrobial peptide with activities against E.coli (MIC=1.3 uM), S.aureus (MIC=3.1 uM), and S.cerevisiae (MIC=50 uM). Also shows histamine-releasing activity (32.9% at 10 uM). Does not show hemolytic activity, even at 50 uM. It is a short peptide for which no alpha- helical region has been predicted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily."}
{"protein": "MCCAVSEQRLTCADQMMPFGKISQQLCGVKKLPWSCDSRYFWGWLNAVFNKVDYDRIRDVGPDRAASEWLLRCGAMVRYHGQERWQKDYNHLPTGPLDKYKIQAIDATDSCIMSIGFDHMEGLEHVEKIRLCKCHYIEDDCLLRLSQLENLQKTILEMEIISCGNITDKGIIALRHLRNLKYLLLSDLPGVREKENLVQAFKTALPSLELKLQLK", "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": "MKLAGLKSIENAHEDSVWAATWVPATEDRPALLLTGSLDETVKLWRPDELDLVRTNTGHSLGVAALAAHPSGIIAASSSIDSFVRVFDVDTNATIAVLEAPPSEVWGMQFEPKGTILAVAGGSSASVKLWDTASWRLISTLSIPRPDAPKPSDKTSSKKFVLSVAWSPNGKRLACGSMDGTICVFDVDRSKLLHQLEGHNMPVRSLVFSPVDPRVLFSGSDDGHVNMHDAEGKTLLGSMSGHTSWVLSVDASPDGGAIATGSSDRTVRLWDLKMRAAIQTMSNHNDQVWSVAFRPPGGTGVRAGRLASVSDDKSVSLYDYS", "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:12750345, PubMed:18725930). Required for histone H3 trimethylation on 'Lys-4' (H3K4me3) and histone dimethylation on 'Lys- 36' (H3K36me2) at the FLC locus. Prevents trimethylation on 'Lys-27' (H3K27me3) at the same locus (PubMed:18725930). Not required for meiotic recombination or progression (PubMed:16716192). Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C) (PubMed:22511887). Required for proper progression of cell differentiation process (PubMed:23134555). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MMEELHSLDPRRQELLEARFTGVGVAKAPLNSESSNQSLCSLGSLSDKELEQTPEKKQNDQRNRKRKADPYETSQGKNTPRGHKISDYFEFACGSGPGTSPGRSVPPVARSSPQHSLSNPLPLPSQQCSPPSTAPVNPEHSCASFKHISVQHRCTQSDLTMDKISALENSKSSDLEKKEGRIDDLLRVNCDLRRQMDEQKKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINTQREEIERQRKMLAKRKPPAMGQTPPANNEQKQRKNKTNGAENEALTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMTEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSIPANAAVASTSGSSNNSLSN", "text": "FUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Cytoplasm, perinuclear region Cytoplasm, cytoskeleton Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle (By similarity). Present in the perinuclear region at S phase and in the nucleus at late G2 (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MARSPRIRIKDNDKAEYARLVKNTKAKIARTKKKYGVDLSAEINIPDLESFETRAQFNKWKEQASSFTNRANMRYQFEKNAYGVVASKAKIAEIERNTKEVQRLVDEKINAMKDKEYYAGGKPQGTIEQRIAMTSPAHVTGINRPRDFDFSKVRTYSRLRTLEESMEMRTDPQYYEKKMIQLQLNFIKSVEGSFNSFDAADELIEELKKIPPDDFYELFLRISEISFEEFDSEGNTVENVEGNVYKILSYLEQYRRGDFDLSLKGF", "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": "MAKKSMIAKAARKPKFKVRAYTRCQICGRPHSVYRDFGICRVCLRKMGNEGLIPGLKKASW", "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": "MLDRFLPEFDRALRAVAGITRASRPNPADAIVAPTDDGAKLSDTERRHAAGLMRVNHVGEVCAQALYQGQALFARDPAIRAQLDEAAREEEDHLAWCAQRLQELHDRPSLLNPLWYAGAFAIGALAGRLGDKISLGFVAETERQVEHHLDGHLDRLPEHDARSRAIVAQMRDDEVRHGDNARAAGGIDLPEPVRQAMRLASRIMTTAAYRI", "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": "MTLTALLALLLSYLIGAIPAAAWLARARGVDIRKVGSGNSGATNVLRSLGKGPALLVASFDILKGVLAVLLARALGLSAEWAALCGVLAVIGHNFSPFLAFRGGKGVATSFGVIAILDPVLGLTTFVLAIACMWLTRFVSAGSIMGAFIAGALVLVLPRPTWDRAAVLFLAALLVWQHRENIRKLQAGTERRLGEKVS", "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": "MNLRLCVQALLLLWLSLTAVCGGSLMPLPDGNGLEDGNVRHLVQPRGSRNGPGPWQGGRRKFRRQRPRLSHKGPMPF", "text": "FUNCTION: (Microbial infection) Endogenous ligand for the apelin receptor (APLNR), an alternative coreceptor with CD4 for HIV-1 infection (PubMed:11090199). Inhibits HIV-1 entry in cells coexpressing CD4 and APLNR (PubMed:11090199). Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives (PubMed:11090199). FUNCTION: Endogenous ligand for the apelin receptor (APLNR) (PubMed:10525157). Drives internalization of the apelin receptor (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates (By similarity). Plays a role in early coronary blood vessels formation (By similarity). Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Note=Abundantly secreted in the colostrum. Lower level in milk. Decreases rapidly within several days after parturition in milk, but is still detectable even in commercial milk. SIMILARITY: Belongs to the apelin family."}
{"protein": "MANRNDSRNNRRNKDDIEDQLVAVNRITKVVKGGRRMRFAALVVVGDKKGRVGFGTGKAQEVPEAIRKAVEDGKKKMINVPKVGTTIPHEVIGHYGSGNILLKPAEAGSGVAAGGAVRIVMDMAGISDVTSKSLGSNTPINVVRATIDGLKKLRTSEEVSKLRQPERA", "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": "MAASDAHNNNKKRSNRRRKKRRTEDFSSSSESSSSSSSESDHEDLDEPEKEISKQDINIDDIDIESDNENSALTNDKGNKLIPQNLSITEKQQLSTVPFTTTSISNITNDNQIKNTPNINEISKNLDQKKTQLNNEFLKIMTTEFGDDLDELRKKPDFTEKSLVILAKTLQSGVNMFDIDVLNGLIQESGNTSNQ", "text": "FUNCTION: Required for efficient biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RSA3 family."}
{"protein": "MLSLESEVLTRHLPLFANKSILLFGDVRDRFADQIKANAKSVAVFSSYFDYARQYADVSFGLYCEIKAELAVFYWTKNKQECQYQLLQWLSQVDVGQEMLIIGENRAGVRSVEKLLEPYGNIAKIDSARRCGLYHFELQSVPDFDGKKFWKSYRLQDLNIFALPAVFSSAELDDGTQLLLSTFNKADRLKGKVLDLGCGAGVIGASLKQQFEKIKLTMSDIHAMALESSRRTLAENALDGTVVASDVFSNIEERFDLIVSNPPFHDGIDTAYRAVEDLIAQAKQRLNRGGELRIVANAFLPYPDLLDKAFGSHQVIAKSNKFKVYSAKA", "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": "MANALASATCERCKGGFAPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVSCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSETLGRK", "text": "FUNCTION: Adapter protein in a cytoplasmic complex linking beta- integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation. SUBCELLULAR LOCATION: Cell junction, focal adhesion Cell membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MPLPDFHVSEPFTLGIELEMQVVNPPGYDLSQDSSMLIDAVKNKITAGEVKHDITESMLELATDVCRDINQAAGQFSAMQKVVLQAVTDHHLEICGGGTHPFQKWQRQEVCDNERYQRTLENFGYLIQQATVFGQHVHVGCASGDDAIYLLHGLSRFVPHFIALSAASPYMQGTDTRFASSRPNIFSAFPDNGPMPWVSNWQQFEALFRCLSYTTMIDSIKDLHWDIRPSPHFGTVEVRVMDTPLTLSHAVNMAGLIQATAHWLLTERPFKHQEKDYLLYKFNRFQACRYGLEGVITDPHTGDRRPLTEDTLRLLEKIAPSAHKIGASSAIEALHRQVVSGLNEAQLMRDFVADGGSLIGLVKKHCEIWAGD", "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": "MSFVEICLVLATIGLLLFKWSTGTFKAFEGRNLYFEKPYPFLGNMAASALQKASFQKQISEFYNRTRHHKLVGLFNLRTPMIQINDPQLIKKICVKDFDHFPNHQTLNIPNERLVNDMLNVMRDQHWRNMRSVLTPVFTSAKMRNMFTLMNESFAQCLEHLKSSQPIAAGENAFELDMKVLCNKLSNDVIATTAFGLKVNSFDDPENEFHTIGKTLAFSRGLPFLKFMMCLLAPKVFNFFKLTIFDSTNVEYFVRLVVDAMQYREKHNITRPDMIQLLMEAKKESKDNWTDDEIVAQCFIFFFAAFENNSNLICTTAYELLRNLDIQERLYEEVKETQEALKGAPLTYDAAQEMTYMDMVISESLRKWTLSAAADRLCAKDYTLTDDEGTKLFEFKAGDNINIPICGLHWDERFFPQPQRFDPERFSERRKKDLIPYTYLPFGVGPRSCIGNRYAVMQAKGMLYNLMLNYKIEASPRTTRDMWESARGFNIIPTTGFWMQLVSRK", "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": "MADDKGTDPKEGCSEWFIDNEADCSDLENDLEQLFDESPKSNISNLLNDEEDVEQGNSRDLLRQQEFEESAEQVQKLKRKYFSPKAVQQLSPRLQSMSISPRQKSKRRLFEEDSGLELSGLEQSLTNEIEDTPAELEVPAATPAEQGGQGEGNLHYKELMRCNNSRAKLLSKVKEYFGVGFYELARQYKSDKTCCKDWVIAAYGVREELVESAKQLLLNHCSYVWININGIMTLYLLCFNHAKSRETVGRLLMSILDVQLLQLICEPPKLRSVVSALYWYKGSMDSSVYAHGAYPDWIVNQTMISHQAAADAMQFDLSEMIQWAYDSDLTDEADIAYLYAKMANSDSNARAWLAHNNQARYLRECAQMVRHYRRGEMRDMSMSEWIHHRIQQVEGEGHWSEIVKFIRFQEINFIIFLDAFKQFIHGKPKKSCLLIHGPPDCGKSMFAMSLLKVLKGKVISFVNAKSQFWLSPLSECKIGLLDDATDPCWQYIDTYLRNGLDGNVVSVDCKHKTPMQIRFPPLLITSNYNIKANDKYKFLYSRIAIFEFKHKFPFKEDGTPVFQLTDQSWKSFFERLWTQLELSDPEDEADNGGTQRSFQCTTRDVNGHL", "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": "MAGGPGPGDPAVPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSGQRTASVLWPWINRNARVADLVRILTHLQLLRARDIITAWHPPAPLLPPSTTSLTPSSISAPSEAAVPGHRKLPSLASTFLSPAFPGSQTHSDPELCPGPSPAAHQPPLPSPAPSSTKPSPESPMSLLPGAPSSSFCWPLHEICQGTHDFSEELKIGEGGFGCVYRAVMRNTVYAVKRLKEEADLEWTTVKQSFQTEVQQLSRFRHPNIVDFAGYCAQSGFYCLVYGFLPNGSLEDRLHVQTQAWPPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDVKSSNVLLDERLMPKLGDFGLARLSRFTGANPGQSSSVARTRTVRGTLAYLPEEYVKTGRLAVDTDTFSFGVVLLETLAGQRAVRMHGAQPKYLKDLVEEEAEEAGVTLKGTQTAVQGGPAADTWAALVAAQIYKKHLDPRPGPCPPQLGLALGQLACCCLHRRAKRRPPMTQVYQTLEELQVVVAGPCLELEAASRSPPSPQENSYVSTSGSALSRASPWQPLAAPLGAQAQATDWPQKGANQPVESDESVSDLSAALHSWHLSPSCPAGPGAPSWVPAPFGQAACTQGGAARESSCGSGPGLQPTAVEGPLLGSSMSSRPPQIVINPARRKMLQKLALYEDGVLDSLQLLSSSSLPDSGQDLQDRQGPEERDEFRS", "text": "FUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Lipid droplet Note=Translocates to the nucleus when sumoylated. RSAD2/viperin recruits it to the lipid droplet (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily."}
{"protein": "MGKINAENTSKHVTFSKNAFIPVCNWCRNVCGYCTFRNENFKLLKMDEMKEILTKADTFGCREALFTFGENVDENEKVKEELKKMGYSGILEYLYEISAWCLENTNLIPHTNCGILSYDELKYLREVNASMGLMLENSSARLCGTIAHEKSPGKDPKLRIEMIENAGKLKIPFTTGILIGIGETFEERVNSIFEIKRIHEKYGHIQEVIVQNFRSKPQIPMENYKEPSPVEMFKMIILSKLILEDISIQVPPNLNRETGQLFLMAGIDDWGGVSPLTKDFVNPEAPWPDIEELNIFSKELGFTLKERLPVYEKYITEEWVDKKILEKIKK", "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": "MEVKAIHRGARISAQKTRLVADQIRGLPIERALNILAFSPKKAAGIVKKVVESAIANAEHNEGADIDELKVKSIFVDKATSLKRFTARAKGRGNRIEKQTCHITVTLGN", "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": "MATATTKAKATERIKMRIRKGDTVQVIAGKDKGKTGAVLRTLPNENRVVVEGVNMRTRHEKPTQEGETGRIVTEEASLHASNVMLYSTDKKVASRVEIVVEKDGTKKRRLKKTGEVLD", "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": "MRRALFIAGQTYLWLNLTHLLLIFSWSSTMAFSQSRRLLTPTVPCPTLLGIDFLILVLRHFDEIFI", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MPRLRVYELAKKLNMSTKDLLQELEELGLNVKNHMSYIDEETVGLLLEIFEEEEETAAKAKAAKPKKEKEELEEIFQEVVLKPEDLQLNTLAVKIGVPLNRIIQDMFVKGIVLKPTQQIDEKTAKDIAKIYGYRAKFYQPEEEISELETIENELERLEKYFETLYETHKDELSIRPPVVTVMGHVDHGKTTLLDKIRRTRVAEKEVGGITQSIGAYQVVHKGKKITFIDTPGHELFTEMRAKGAQATDIVVLVVAADDGVMPQTIEAYNHAKVANVPVIVAINKIDKPNANIEATKRQLVDKLNIIPEDWGGDTITVPISARTGHGIDELLEMILLVAELREIKCYPKGPARCVIIESKLDRSLGPVANVIVKDGELRVGDYLVAGPTYCKVRILIDDKGKSIKIAEPSQPVMIVGFEEVPDIRYSIYAVESLESARTVTQQLKERLERDKMAKRRVRLEELLKMMEESEKKELNLVLKADTFGSLSAVQNAIASLKSEEIKINIVHSGVGTVNNSDVMLASASNGIIVGFRVKVDAQARKTAENEGIQIKTYEIIYDLLDNMKLALEGMLKPETVEELVGRGEIRKIFDIKKVGKIAGVQLLEGHVSKDCIVKVYRNGTFLFSDQIDSLKHYKEDVDKVSAPQECGLKLKSNEDLRENDELEFYEQHQVQKKL", "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": "MFEARLVQGSILKKVLEALKDLITEACWDVSSSGISLQSMDSSHVSLVQLTLRSDGFDSYRCDRNLAMGVNLSSMSKILKCAGNEDIITLRAEDNADALALVFETLNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSQIGDAVMISCAKDGVKFSASGELGTGNIKLSQTSNVDKEDEAVTIEMNEPVQLIFALNYLNFFTKATPLSKTVTLSMSADIPLVVEYKIADMGHVKYYLAPKIDEESS", "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": "MTRIDPKAVVDPSAELDEGVTVGPFTVIGPDVQVGAGTRVGPHVVINGPTRLGRNNRIHPFASIGDDPQDKKYAGEPTRLEIGDDNVIREYVTLNRGTPEAGGLTRLGDRNWIMAYSHVAHDCRLGNDITFANSASLAGHVDVEDHAILGGFALVHQFCRIGAYAFCGFGSVINRDVLPFTTVSGHMAQPHGINVVGLRRHGMGPERIRELKRAYRLIFKSGKRLDDALEELRLLGKENPDLEHLAAFIAASNRGILR", "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": "MVSSMKVEWYLDFVDLNYEPGRDELIVEYYFEPNGVSPEEAAGRIASESSIGTWTTLWKLPEMAKRSMAKVFYLEKHGEGYIAKIAYPLTLFEEGSLVQLFSAIAGNVFGMKALKNLRLLDFHPPYEYLRHFKGPQFGVKGIREFMGIKDRPLTATVPKPKMGWSVEEYAEIAYELWSGGIDLLKDDENFTSFPFNRFEERVKKLYRVRDRVEAETGETKEYLINITGPVNVMEKRAELVANEGGQYVMIDIVVAGWSALQYMREVTEDLGLAIHAHRAMHAAFTRNPKHGITMFALAKAARMIGVDQIHTGTAVGKMAGDYEEIKKINDFLLSKWEHIRPVFPVASGGLHPGLMPELIRLFGKDLVIQAGGGVMGHPDGPRAGAKALRDAIDAAIEGLDLEEKAKSSPELKKALDKWGYLKPK", "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": "MNYYSTSIAKLIEELSKLPGIGPKTAQRLAFFIINMPLEEVKSLSQAIIDAKEKIKYCRICYNITDTEVCNICSDKERDHSLICVVSHPMDVVAMEKIREYKGVYHVLHGVISPIEGVGPEDIKIKELLDRVKNGNVKEVILATNPDIEGEATAMYIAKLLKPLGIKVTRIAHGVPVGGDLEYTDVVTLSRALEGRREL", "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": "MFKKLFGQMQRIGKALMLPVAILPAAGLLLAIGTAFQGEALQHYLPFIKNDIVQQIANMLTGAGGIIFDNLPIIFALGVAIGLAGGDGVAAIAAFVGFIILNKTMGAFLHVTPDKLSDPTNGYANVLGIPTLQTGVFGGIIIGALAAWCYNKFYNITLPSYLGFFAGKRFVPIMMATTSFILAFPMAIIWPTIQNGLNAFSEGLLDSNTGLAVFLFGFIKRLLIPFGLHHIFHAPFWFEFGSWKNAAGEIIRGDQRIFIEQIREGAHLTSGKFMQGEFPVMMFGLPAAALAIYQTAKPENKKVVAGLMISAALTSFLTGITEPLEFSFLFVAPFLFVIHAVLDGLSFLTLYLLNVHLGYTFSGGFIDYVLLGILPNKTAWWLVIPVGIIYAVIYYFVFRFLIVKFNYKTPGREDKKSSVTTTSASQLPFDVLKAMGGKENIKHLDACITRLRVEVNEKSKVDVAGLKSLGASGVLEVGNNMQAIFGPKSDQIKHDMAKIISGEITKPSETTIDEEVSDDPVHVEDIVETEIYAPGHGEIIPLSEVPDKVFSEKMMGDGIGFVPDSGEIVAPFDGTVKTIFPTKHAIGLESDSGVEVLIHIGIDTVKLNGEGFESLVNTDEPVTQGQPLMKIDLEYLKEHAPSIITPVIITNQEDKTLTIEDVKQVDPGKAIMTIK", "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": "MPGRSSTNSGSTRYISFSGVESALSSLKTFQSCISSGMDTVSSVALDLVETQTEVSSEYSMDKAMVEFAKMDRELNHYVKAVQSTINHVKEERPEKVPDLKLLVEKKFLALQDKNSDADFKENEKFVQFKQQLRELKKQYGIHADRENDGIEGMDEDMIVTQSQTNFICPITQLEMKKPVKNKMCGHTYEEEAIVRMIESKHKRKKKACCPKIGCSHTDMRMSDLIPDEALRRAIESHNKKKKRHSE", "text": "FUNCTION: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere Nucleus, PML body Note=Localizes to PML nuclear bodies in ALT cell lines. SIMILARITY: Belongs to the NSE2 family."}
{"protein": "MSVIIDIHAREILDSRGNPTVEVDVTLEDGTMGRAAVPSGASTGAYEAVEKRDGDKARYKGKGVLAAVEAVNGEIADTLVGFDATEQVAIDQTMCELDGTDNKGRLGANAILGVSLATAKAAADFTAQPLYRYVGGTMAHVLPVPMMNIINGGEHADNPIDIQEFMIMPVSATSIAEAVRMGSEVFHTLKSELSAAGLSTGIGDEGGFAPNLSSTRDALDFVLKSIEKAGYAPGDDMVLALDCAATEYYRDGKYELSGEGKSLTSDENVAYLAALVANYPIFSIEDGMGEDDWDGWIALTEALGDKVQLVGDDLFVTNPARLKDGIDRKAANSLLVKVNQIGTLTETLAAVNMATRAGFTSVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEQLEETANFAGRSILRG", "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": "MATDISESSGADCKGDTKNSAKLDADYPLRVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPNEFAKLTVENSPKQETGITEGQGPVGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIDLKEAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK", "text": "FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). SIMILARITY: Belongs to the DENR family."}
{"protein": "MHRSVPEQVSAELPATLEQFQITLGADVEDRVEECVREAARCLYRGAIVQCGALGELLIDYSWEKLNARNWREVGREWRAVYSYGCLFRAVGLCSVTGSIEEALQVCDIGLLMGAEIMDNLLGRIISVLQRIAPSREETKLEAERGVREPGLESSKLHSPGEHSNKKSFASVTGRKRIREGPEADFDPKGCSISEKVPCLLVPVLDSETAIPKLHCPSLEHFRDHYLVPQKPVVLEGVIDHWPCLKKWSVEYIQRVAGCRTVPVELGSRYTDAEWSQRLMTVNEFITKYILDKQNGIGYLAQHQLFEQIPELKEDICIPDYCCLGEASEDEITINAWFGPAGTVSPLHQDPQQNFLAQIVGRKYIRVYSVAETEKLYPFDSSILHNTSQVDVESPDQNKFPRFSQASYQECILSPGQVLFIPVKWWHYIRALDLSFSVSFWWS", "text": "FUNCTION: Histone demethylase required for G2/M phase cell cycle progression (By similarity). Specifically demethylates dimethylated 'Lys-36' (H3K36me2) of histone H3, an epigenetic repressive mark, thereby acting as a transcription activator (By similarity). May play a role in the regulation of the circadian clock (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRYLTAGESHGPGLTTIIEGLPAGMPLLAEDVNKELKRRQGGHGRGARMRIEKDQVQITAGIRHGKTLGAPVAMFVENKDWKHWETVMSIEPVPEKNEKSRRVSRPRPGHADLVGGMKYGHNDMRNVLERSSARETTVRVAAGAVAKKLLHELGIEVAGHVLEIGGTRANLTRDYAVSEIQETSEASPVRCLDGVAAEEMMQKIDDAKKNGDTIGGIVEVVVGGVPAGLGSYVQWDKKLDAKIARAIVSINAFKGAEFGVGFEAARKPGSEVMDEILWSKEDGYTRRTNNLGGFEGGMTNGMPIVVRGVMKPIPTLYKPLQSVDIDSKETFNASVERSDSCAVPAASVVAEAVVAWEVAVAVLEKFDGDRFDTLKKHVEEHRNLTKEF", "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": "MRMIGFWQRALCVLMLTLPVLASAQTAPVTVFAAASLKESMDEAATAYEKATGTPVRVSYAASSALARQIEQGAPADVFFSADLEWMDYLQQHGLVLPAQRHNLLGNTLVLVAPASSKLRVDPRAPGAIAKALGENGRLAVGQTASVPAGKYAAAALRKLGQWDSVSNRLAESESVRAALMLVSRGEAPLGIVYGSDARADAKVRVVATFPDDSHDAIVYPVAALKNSNNPATAAFVSWLGSKPAKAIFARRGFSLKD", "text": "FUNCTION: Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (Probable). Binds molybdate and tungstate with high affinity in vitro (PubMed:16879982). SIMILARITY: Belongs to the bacterial solute-binding protein ModA family."}
{"protein": "MVDDSTRKTLSNIPLLQIRAGPREKDIWVQRLKEEYQALIKYVENNKQSGSDWFRLESNKEGTKWFGKCWYMHNLLKYEFDVEFDIPVTYPTTAPEIALPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGIAHAMALGLAPWLAVEIPDLIEKGVITYKDNC", "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": "MFSAVKPLSKYLQFKSIRIYDSVFTIHSRCTVVILLTCSLLLSARQYFGDPIQCISEEKNIEYIQSYCWTMGTYILKLDDFGDQEQALVSPNQEVSYNSAFFSSATTNAPQSSSRVRTRPHFRSSLRRIGEYNEAYARSLSIAEGVGPEIRGQTERQYLRYYQWVIILLLFQSFVFYFPSCLWKVWEGRRLKQLCSEVGDALLSEETYNTRLRMLVKYFTTDYEDMHFCYMAKYVFCEVLNFLISVVNIIVLEVFLNGFWSKYLRALATIPFYDWDRWNRVSSSVFPKIAKCEVLKFGGSGTANVMDNLCILPLNILNEKIFVFLWAWFLLMALMSGLNLLCRLAMICSRYLREQMIRSQLRFMTKRHVKRALRDLTIGDWFLMMKVSVNVNPMLFRDLMQELCELRTSASGSTLESPV", "text": "FUNCTION: Structural component of the gap junctions. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, gap junction. SIMILARITY: Belongs to the pannexin family."}
{"protein": "MSLGEINENVKLAREYALLGNYSSAVVCYQGVLEQIKKYLYSVRDSSLQQKWQQVWQEINEETKQVREIMTTLESFQMESTPSKPSSFAQDNDIMPVHVEHRSSPCVVRKSSVPYKDSKGHGNRLSVGPRGQARPSPRVANGDKGKPQKSKEKKENPSKPKEDKNKAEAVETEVKRFDRGGEDKDLIDALERDIISQNPNVTWDDIADLEEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECRTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGRVDLLKINLKELDLANDVNMDKIAEQMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLPKDEMHMPTTMEDFETALKKVSKSVSAADLEKYEKWIAEFGSC", "text": "FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with katnb1. SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily."}
{"protein": "MDLKHSRSVKLNDGNLMPVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPFLEEY", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of substrates including aromatic and aliphatic aldehydes, quinones, ketones, dicarbonyl compounds and 17-ketosteroids (PubMed:17574202). Catalyzes the NADP(+)-dependent oxidation of aromatic, alicyclic and aliphatic alcohols, and 17beta-hydroxysteroids (PubMed:17574202). To a lesser extent, can also catalyze the reduction of some aldoses and ketoses and the oxidation of some sugar alcohols (PubMed:17574202). In the stomach, lung and colon tissues, mediates the reduction of farnesal and geranylgeranial into farnesol and geranylgeraniol respectively (PubMed:21187079). By reducing 4-hydroxy-2-nonenal (HNE), produced during lipid peroxidation, into 1,4-dihydro-2-nonene (DHN), protects vascular endothelial cells from damage elicited by oxidized lipoproteins (PubMed:21187080). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MKFSESWLREWVNPAVSREALSHQITMAGLEVDGVDAVAAEFNGVVIGEVVECGLHPDADKLRVTKVSVGSSELIDIVCGAPNCRQGLKVAVAMVGAVLPGDFKIKKAKLRGMPSEGMLCSYSELGIDIDSDGIIELPLDAPLGTDLREYLKLDDAVIEVDLTANRADCLGMVGLAREVGVLNRQAVTEPQWQAVTPTTDAKVTINVKESAACPRYLGRVVKNVNVKAATPLWMQEKLRRSGIRSIDPIVDITNFVLVEFGQPMHAFDLAKLTGDIQVRLGNGEEKITLLDGSEVTIPSDTLVIADDARPLALAGVFGGEYSGVSDTTQDILLECAFFAPLAIMGKSRRLGLHTDSSHRFERGVDPEMQHKVIDRATRLVLDICGGEAGPVVEAKSDADLPKPAQILLRRSKLDKILGHYVPDSDVVEILERLGFSVVKGEGCWQVITATYRFDMAIEEDLIEEVARIYGYNNIPNVAPIASLRMSDHKETDLSLKRVRSLLVARGFQEAVTYSFVDPKLQNLVHPGEQAMVLPNPISSEMSAMRLSMFTGLLTAVGYNQSRQQGRVRLFETGLRFVPDINAESGVRQQAMLGCVITGPQNDEHWAMESKTVDFFDLKGDLEAIIGLTVSASEFSFRVATHSALHPGQCAEILRNDRVIGHIGAIHPSLEKPFGLNGKTIVFELELDALLHTSLPLAQAVSKFPANRRDIAVVVDESVSAGDVMKLIRKVGENQLVGINLFDVYLGKGVEPGKKSLAIALTLQDTTRTLEEKEIAETVESVVSALKTEFNASLRD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily."}
{"protein": "MTTAAPTPSLFGQCLAEFLGTALLIFFGTGCVAALKVAGASFGLWEISIIWGVGVSMAIYLSAGVSGAHLNPAVSIALWLFAGFEGRKLPFYITAQVAGAFCAAALVYTLYSSLFIEFEQAQNIVRGSQDSLALASVFSTYPHPALSVGQAFLVEVVITAILMAVIMALTDDGNGLPRGPLAPLLIGLLIAVIGSAMGPLTGFAMNPARDFGPKLMTYLAGWGPIAFTGGREIPYFLVPIFAPILGACLGAGGYRVLIARHLPSAAAPAEAEPEKVRAS", "text": "FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MEEIVEMSLLLDFYGSLLTEKQNKIMDLYYNNDYSLKEISELTNTSRQAVHDIVKRCHKALIQYEEKLHMMERFINLENSKEKLLNMLNKVTKENIKEIDHIKKYIIDNI", "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": "MVRRAPGASLALLLWVTAVSGSPAGPGAATARRQDEAFSTARCTSRCLSLQITRISAFFKHFQNNGSLAWCQNHKQCSKCLEPCKESWDLKKNHCQSFCEPLFPKKNYECLTSCEFLKYILSVKQGDCPAPEKASGFAAACVESCEADSECSGVKKCCSNGCGHTCQVPKNLYKGVPLKPRKELKFIELQSGDLEVKWSSKFNISIEPVIYVVQRRWNQGIHPSEDDATNWQTVAQTTDERVQLSDIRASRWYQFRVAAVNVHGTRGFTAPSKHFRSSKDPSAPPAPSNIRIANISANNDGTVNVMITWDLPEEPDIPVHHYKVFWSWTYSKYVIPAKKKRRKITDGPQNYVVLEGLQPNSNYNVELQAVTRWGQIRLKSAKVSLHFSTAQDNRNNNEQTSAGKPPKGLVDPYPTFQRRKPTRFLKIGTPFYQDNQLQVKVYWKKTDINMNQFQVHSLLESCVHNDTKGLEKVTELTYENYMILKDLSFSCKYKVTVLPAKSKSRFKAESIFFVTPSCSAFKEKTHKHINCAAEEVPVLPKVLAKPENLSASFIVQEGNITGHFSWKISKAVLHQPMTGFQVTWAEVTTESRQNSLPNSIISQSQILPADHYVLTVPNLRPSMLYRLEVQVLTTGGEGPATIKLFRTPDLPPFLPHRPHLKQHHPHHYKPPPEKY", "text": "FUNCTION: May be an adhesion-like molecule with anti-protease activity. SUBCELLULAR LOCATION: Cell surface."}
{"protein": "MYNYLDFEKPVADLDVQILELKKIAQEKGSLDMSDEIARLEMRSQTALRDLYKKLSPWQKTQVARHPDRPHFMDYSAQLLRDVTPLAGDRKFAEDEAIQAGFARFKGEAIAYIGQEKGHDTQTRLRYNFGSARPEGYRKAVRIMELADRFGLPLLTFVDTAGAYPGVSAEERGQAEAIAQSTAATLRLRVPVVSVIIGEGGSGGAIAIAAANKVYMLEHSIYSVISPEGAASILWRDPARAKDAATNMQITAQDLYRLKIIDGIIPEPLGGAHRQKEAAIEAAGDGIAAALKSMIGKDGETIKQERWDKYLQIGRSLA", "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": "MATASGASDLSGSGAPPPGVGAQAAAAAEEEEREVVRVRVKKCESFLPPEFRSFAVDPQITSLDVLQHILIRAFDLSGKKNFGISYLGRDRLGQEVYLSLLSDWDLSTAFATASKPYLQLRVDIRPSEDSPLLEDWDIISPKDVIGSDVLLAEKRSSLTTAALPFTQSILTQVGRTLSKVQQVLSWSYGEDVKPFKPPLSDAEFHTYLNHEGQLSRPEELRLRIYHGGVEPSLRKVVWRYLLNVYPDGLTGRERMDYMKRKSREYEQLKSEWAQRANPEDLEFIRSTVLKDVLRTDRAHPYYAGPEDGPHLRALHDLLTTYAVTHPQVSYCQGMSDLASPILAVMDHEGHAFVCFCGIMKRLAANFHPDGRAMATKFAHLKLLLRHADPDFYQYLQEAGADDLFFCYRWLLLELKREFAFDDALRMLEVTWSSLPPDPPEHEVELVGPPSQVADAGFGGHRGWPVRQRHMLRPAGGGGSTFEDAVDHLATASQGPGGGGRLLRQASLDGLQQLRDNMGSRRDPLVQLPHPAALISSKSLSEPLLNSPDPLLSSFSHPDSPSSSSPPSTQEASPTGDMAVGSPLMQEVGSPKDPGKSLPPVPPMGLPPPQEFGRGNPFMLFLCLAILLEHRDHIMRNGLDYNELAMHFDRLVRKHHLGRVLRRARALFADYLQSEVWDSEEGAEATAAS", "text": "FUNCTION: Acts as a GTPase-activating protein specific for RAB33B. Involved in the regulation of autophagosome maturation, the process in which autophagosomes fuse with endosomes and lysosomes. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, autophagosome Note=It is dispersed in the cytoplasm under nutrient-rich conditions. Localizes at autophagosomes under cell starving conditions."}
{"protein": "MDVKIFDNDTEAGKYAFDLIKQGMDNGAKVLGLATGSTPVTMYKAMVNSDVDFSNMTSINLDEYVGLAPDNDQSYRYFMQSNLFDKKPFKETFVPNGLAKGPEEETTRYNKVIADHPINIQVLGIGRNGHIGFNEPGSPFDAETRKVPLTQSTIDANARFFASEDDVPRYAYSMGIGSILKSKKILLLAFGENKADAVKKMIEGPVTNDVPASALQKHSDVVVILDKAAASKLSKK", "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": "MESEQLFHRGYYRNSYNSITSASSDEELLDGAGVIMDFQTSEDDNLLDGDTAVGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDCGPLESSSLCDYRNDMNASKIVDDIPDRPAGVGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYFHHDWFIFKEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAADVMRPRRNDPPLAVLTQDNMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESARKKQEGIVGSSRVCFAQHTPSLPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQTANQDPASIMFN", "text": "FUNCTION: Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons (By similarity). The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity). SUBCELLULAR LOCATION: Early endosome membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 3/CLCN3 subfamily."}
{"protein": "MSSDSSQVKLRFFTREQDESLHVQDAPMYAPISLKRYGLSEVVNHLLGFEKPVPFDFLIDGELLRISLQEYLTKHGLSSETFLNVEYTRAVLPPSFLSSFSNEDWVSSLDVGDNNKIISGSYDGVVRTWNLSGKIEKQYSGHSAPIRAVKYISNTRMVSGGNDRTLRLWKTKNEDLKQPVVDEDDEDIEDGKTLAILEGHKAPVVSIDVSDNSRILSGSYDNTIGFWSTIYKEMTVVDPMEELKNNDSKMSTAAKKRRKLTLKDGTIRRRAPLALLESHTGPVEQVSFDFKDNTVGYSISQDHTIKTWDLVTSRCIDTKTTSYSLLSLAQLPTLNLLACGSSARHITLHDPRIGSTSKITQQQLVGHKNFVVSLDTCPENEYMLCSGSHDGTVKVWDVRANSPMYTITREEQSVEKGVNDKVFAVNWSKNVGIISAGQDKKIQINKGDNIFKS", "text": "FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family."}
{"protein": "MNRLKEKYLNEVVPALMSKFNYKSIMQVPKIEKIVINMGVGDAVQNPKALDSAVEELTLIAGQRPVVTRAKKSIAGFRLRQGMPIGAKVTLRGERMYEFLDKLISVSLPRVRDFRGVSKKSFDGRGNYTLGIKEQLIFPEIDYDKVNKVRGMDIVIVTTANTDEEARELLALLGMPFQK", "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": "MAIILGVDPGSRITGYGVIQCQGRQQIYLGSGCIRTSADDLPQRLQQIYAGLCEIITQYKPDEFAIERVFMAKNADSALKLGQARGAAIVAATCAGLPVAEYSATQIKSAVVGTGRAQKTQVQHMIKQLLKLPASPQADAADALGVAICHFHTYQSLIAMGGKASSRTYGRYK", "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": "MAVQKVKLFTEAPFTLSLGGTLQDIEIAYQTYGELNKEKTNAILICHALTGDAEPYFADHSQRGWWQTFMGEGLALDTSQYFFICSNVLGGCKGTTGPSSINPKTNKPYGSQFPNIIVQDIVALQRALLTHLNIPRLHAVIGGSFGGMQATQWAIDYPDDVSNVINLCSSLLFGAEAIGFNHVMRQAVINDPNFNGGDYYDSQPPEKGLAIARMLGMLTYRTDLQLTKAFGRATKAETEFWGDYFQVESYLSYQGKKFLARFDANSYLHLLRALDLYDPGFQYESLSAALARIKARYTLVAVENDQLFKLTELQKSKKLLEESGVDLVYYQFSSDYGHDAFLVDYAFFEKKIRLALANQD", "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": "MDILKEEFEIIKQRIKDKPEGSYVAYLTTADKKTPINKICEKVGEEATETILAAKDQDKQELIYESADLIFHILVLLANNGIEYEELMEEFERRRK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MNQLDGIKQFTTVVADSGDIESIRHYQPQDATTNPSLLLKAAGLEQYGHLIEDAIAWGKKHGGTQEQQVAAASDKLAVNFGAEILKSIPGRVSTEVDARLSFDKEKSIEKARHLVDLYQQQDVDKSRILIKLAATWEGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVYLISPFVGRIYDWYQARSPLEPYVVEEDPGVKSVRNIYDYFKQHRYETIVMGASFRRTEQILALTGCDRLTISPNLLKELKEKEEPVIRKLVPSSQMFHRPTPMTEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL", "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": "MMADEEEEAKHVLQKLQGLVDRLYCFRDSYFETHSVEDAGRKQQDVQEEMEKTLQQMEEVLGSAQVEAQALMLKGKALNVTPDYSPEAEVLLSKAVKLEPELVEAWNQLGEVYWKKGDVASAHTCFSGALTHCKNKVSLQNLSMVLRQLQTDSGDEHSRHVMDSVRQAKLAVQMDVLDGRSWYILGNAYLSLYFNTGQNPKISQQALSAYAQAEKVDRKASSNPDLHLNRATLHKYEESYGEALEGFSQAAALDPVWPEPQQREQQLLEFLSRLTSLLESKGKTKPKKLQSMLGSLRPAHLGPCGDGRYQSASGQKMTLELKPLSTLQPGVNSGTVVLGKVVFSLTTEEKVPFTFGLVDSDGPCYAVMVYNVVQSWGVLIGDSVAIPEPNLRHHQIRHKGKDYSFSSVRVETPLLLVVNGKPQNSSSQASATVASRPQCE", "text": "FUNCTION: Cofactor involved in the regulation of various cellular mechanisms such as actin regulation, autophagy, chromatin regulation and DNA repair (PubMed:11511361, PubMed:15448695, PubMed:18451878, PubMed:30420355). In physiological conditions, interacts with cofactor JMY in the cytoplasm which prevents JMY's actin nucleation activity and ability to activate the Arp2/3 complex (PubMed:30420355). Acts as a negative regulator of nutrient stress-induced autophagy by inhibiting JMY's interaction with MAP1LC3B, thereby preventing autophagosome formation (PubMed:30420355). Involves in tubulin autoregulation by promoting its degradation in response to excess soluble tubulin (By similarity). To do so, associates with the active ribosome near the ribosome exit tunnel and with nascent tubulin polypeptides early during their translation, triggering tubulin mRNA-targeted degradation (By similarity). Following DNA damage, phosphorylated by DNA damage responsive protein kinases ATM and CHEK2, leading to its nuclear accumulation and stability (PubMed:15448695, PubMed:18833288). Nuclear TTC5/STRAP promotes the assembly of a stress-responsive p53/TP53 coactivator complex, which includes the coactivators JMY and p300, thereby increasing p53/TP53-dependent transcription and apoptosis (PubMed:11511361). Also recruits arginine methyltransferase PRMT5 to p53/TP53 when DNA is damaged, allowing PRMT5 to methylate p53/TP53 (PubMed:19011621). In DNA stress conditions, also prevents p53/TP53 degradation by E3 ubiquitin ligase MDM2 (PubMed:11511361). Upon heat- shock stress, forms a chromatin-associated complex with heat-shock factor 1 HSF1 and p300/EP300 to stimulate heat-shock-responsive transcription, thereby increasing cell survival (PubMed:18451878). Mitochondrial TTC5/STRAP interacts with ATP synthase subunit beta ATP5F1B which decreased ATP synthase activity and lowers mitochondrial ATP production, thereby regulating cellular respiration and mitochondrial-dependent apoptosis (PubMed:25168243). Mitochondrial TTC5/STRAP also regulates p53/TP53-mediated apoptosis (PubMed:25168243). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasmic vesicle Mitochondrion matrix Note=Phosphorylation at Ser-203 results in nuclear localization, while unphosphorylated protein localizes to the cytoplasm (PubMed:15448695). Nuclear localization may be necessary for DNA damage-dependent stabilization of the protein (PubMed:15448695, PubMed:18833288)."}
{"protein": "ALTYRGVDWSSVVVEERAGVSYKNTNGNAQPLENILAANGVNTVRQRVWVNPADGNYNLDYNIAIAKRAKAAGLGVYIDFHYSDTWADPAHQTMPAGWPSDIDNLSWKLYNYTLDAANKLQNAGIQPTIVSIGNEIRAGLLWPTGRTENWANIARLLHSAAWGIKDSSLSPKPKIMIHLDNGWDWGTQNWWYTNVLKQGTLELSDFDMMGVSFYPFYSSSATLSALKSSLDNMAKTWNKEIAVVETNWPISCPNPRYSFPSDVKNIPFSPEGQTTFITNVANIVSSVSRGVGLFYWEPAWIHNANLGSSCADNTMFSQSGQALSSLSVFQRI", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 53 family."}
{"protein": "MVTLAELLVLLAALLATVSGYFVSIDAHAEECFFERVTSGTKMGLIFEVAEGGFLDIDVEITGPDNKGIYKGDRESSGKYTFAAHMDGTYKFCFSNRMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVRRVV", "text": "FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. 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. In COPII vesicle- mediated anterograde transport involved in the transport of GPI- anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I membrane protein Cytoplasmic vesicle, COPI-coated vesicle 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 Endoplasmic reticulum membrane; Single-pass type I membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein Note=Cycles between compartments of the early secretatory pathway. SIMILARITY: Belongs to the EMP24/GP25L family."}
{"protein": "MAKHQHKKRFGQNFLNNDRIIQQIVAAIAPKPDQHLVEIGPGEAALTGPLLDIVKKLDIIEIDNDLIGPLTKRFSHNPAFHLHHTDALLFDYSQLLEAETETPSLRIVGNLPYNISSPLLFHLLKYARYIQDMHFMLQKEVVERITAQPGVKAYGRLSVMIQYTCETEYLLTVGPENFTPPPKVDSAIVRLRPFEKRPFQAIDDKDFAKLVKQAFSQKRKTLRNNLKGFLNDEQIEACGLDPSVRAEKVPVEAFVLLSNLYHKDKA", "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": "MMIQSHPLLAAPLAVGDTIGFFSSSAPATVTAKNRFFRGVEFLQRKGFKLVSGKLTGKTDFYRSGTIKERAQEFNELVYNPDITCIMSTIGGDNSNSLLPFLDYDAIIANPKIIIGYSDTTALLAGIYAKTGLITFYGPALIPSFGEHPPLVDITYESFIKILTRKQSGIYTYTLPEKWSDESINWNENKILRPKKLYKNNCAFYGSGKVEGRVIGGNLNTLTGIWGSEWMPEILNGDILFIEDSRKSIATIERLFSMLKLNRVFDKVSAIILGKHELFDCAGSKRRPYEVLTEVLDGKQIPVLDGFDCSHTHPMLTLPLGVKLAIDFDNKNISITEQYLSTEK", "text": "FUNCTION: Involved in specific self-immunity to microcin C7. SIMILARITY: Belongs to the peptidase S66 family."}
{"protein": "MRKIKFFDTTLRDGEQSAGVNLNLQEKLEIARQLERLQVDIIEAGFPASSKGDFEAVKQIAETVRTCSVTGLSRSVRSDIDAAWEALKGGAEPRLHLFIATSPIHMVHKLRMTPEQVIEAAVEAVKYAKRFFPIVQWSAEDACRSELPFLAKIVTEVIKAGASVINIPDTVGYITPKEYGEIFLYLRNNVPNIENISLSAHCHDDLGMAVINSLSAIEHGATQVECTINGIGERAGNAALEEIAVALHIRKDYYQVETRLNLQEIKRTSNLVSKLTGMVVPPNKAVVGKNAFAHESGIHQDGVLKEKTTYEIISPELVGVSSNSMVLGKHSGRHALRNRVEELGYTLSEEEINQLFVRFKELADKKKDVTDDDLIALIFEEKFDHFKDFYQLSSIQVQYGTNQIPTAVVVLKDGKGNTIQEAATGAGSVEALYNTLERCFQTAVTLLDYRIESVGGGRDALAQVFVKVRVNDVETSGRGTAQDVLEASAKAYINAMNRMFMIEAMRAENEKVTTP", "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": "MTTTTTNVTDLYPTRGATEVATPRQDPVVWGSPDAPGPVSAGDLQALDRDGFLAIDQLITPDEVGEYQRELERLTTDPAIRADERSIVEPQSKEIRSVFEVHKISEVFAKLVRDERVVGRARQILGSDVYVHQSRINVKPGFGASGFYWHSDFETWHAEDGLPNMRTISVSIALTENYDTNGGLMIMPGSHKTFLGCAGATPKDNYKKSLQMQDAGTPSDEGLTKMASEYGIKLFTGKAGSATWFDCNCMHGSGDNITPFPRSNVFIVFNSVENTAVEPFAAPIRRPEFIGARDFTPVK", "text": "FUNCTION: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2- oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine. SIMILARITY: Belongs to the PhyH family. EctD subfamily."}
{"protein": "MSTEVRLTQYSHGAGCGCKISPKVLETILHSEQEKFLDPHLLVGNETRDDAAVYDIGNGTGIISTTDFFMPIVDDPFDFGRIAATNAISDIYAMGGKPIMAIAILGWPIDKLAPEIARKVIEGGRAACKEAGIVLAGGHSIDAPEPIFGLAVTGIVNIDRVKQNSAAKVGSQLFLTKPLGIGVLTTAEKKGLLLPEHQGIAIETMCRLNKLGMDFAEVAGITAMTDVTGFGLLGHLSEICAGSGVQATLHFAKVPKLPEVESYIAKGCVPGGTGRNFDSYGHLIGEMTELQRKLLCDPQTSGGLLLAVLPEAMDEVKAIARCHGIELTAIGELSEQQSGRVLIEVNE", "text": "FUNCTION: Synthesizes selenophosphate from selenide and ATP. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily."}
{"protein": "MEKSKRLFMKSKRSFRRRLPPIQSGDRIDYKNMGLISRFISEQGKILSRRVNRLTLKQQRLITIAIKQARILSSLPFLNNEKQFEKSESTARTTTLRKKKYRN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
{"protein": "MLEKEFFTEYGEASQYQIQEVVGKGSYGVVASAECPHTGGKVAIKKMTNVFEHVSDAIRILREIKLLRLLRHPDIVEIKHIMLPPCRKEFKDIYVVFELMESDLHHVLKVNDDLTPQHHQFFLYQLLRGLKFMHSAHVFHRDLKPKNILANADCKIKICDLGLARVSFTDSPSAVFWTDYVATRWYRAPELCGSFYSNYTPAIDMWSVGCIFAEMLTGKPLFPGKNVVHQLELVTDLLGTPSPITLSRIRNEKARKYLGNMRRKDPVPFTHKFPNIDPVALKLLQRLIAFDPKDRPSAEEALADPYFQGLANVDYEPSRQPISKLEFEFERRKLTRDDVRELMYREILEYHPQMLQEYLQGEENINSHFLYPSGVDQFKQEFARLEEHNDDEEEHNSPPHQRKYTSLPRERVCSSEDEGSDSVHAQSSSASVVFTPPQTPNTATGLSSQKASQVDKAATPVKRSACLMRSDSICASRCVGVSSAVS", "text": "SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
{"protein": "MTHIVTDTPLWKKLSDHHWEVVGTHLRELFDTDPDRGVDLIVTAADLYIDYSKHRVTRETMGLLVDLARAAGVERHREAMFTGAHINTSEDRAVLHTALRANPERELIVDGQDVVGDVHTVLRRMGEFTDRVRSGAWRGATGERIRTVVNIGIGGSDLGPAMAYRALRHYVDGPEVRFVSNIDPADLLSNLTDLDPRTTLFVVVSKTFSTLETMTNASAARRWITEALGEHAVPRHFVAVSTDEERVTAFGITARNIFGFWEWVGGRYSVGSAAGLSVMIAIGRERFTEFLGGMRAIDEHFRTTPLESNAPVILGMLGVWYSSFFGADARAVLPYAHDLARFPAYLQQLTMESNGKSVRTDGTPVGTFTGEIFWGEPGTNGQHAFHQLLHQGTHLIPVDFLGFAEPIEDLPTLDGIGSVHDVLTANLFAQSKVLAFGKNADEVAADGTPSALVPHKVMSGNRPSTTILGAKLTPSTLGQLIALYEHQVFVQGIVWGIDSFDQWGVELGKTSALELGPALWDLDGAAYVGDSSTTGLIRTYRLARGERRCLP", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MFHKHSVEIDWGGRPLKLETGKIARQADGAVVATYGETVVLATVVAAKTPREGVDFLPLTVDYIEKTYAAGRIPGGYFKREGRPTEKETLVSRLIDRPIRPLFVDGWRNETQVIVTVLSHDMENDPDILALVATSAALTLSGAPFKGPIGAARVGFINDEYVLNPVLDEMIETQLDLVVAGTADAVLMVESEAKELNEDIMLGAVMFGHRHFQPVVQAIIELAEKAAKEPRDVKVIDESVLEKEILGLIEQDLRAAYAIPVKQDRYAAVGKAKDKVMAHYFPEGQEPQYDKLRIAGVFKELEAKIVRWNILDTGKRIDGRDSTTVRQIIAEVGVLPRAHGSALFTRGETQALVVTTLGTGEDEQYIDSLSGTYKEQFLLHYNFPPFSVGETGRMGGTKRREIGHGKLAWRALHPVLPPHHEFPYTLRVVSEITESNGSSSMASVCGASLALMDAGVPLKRPTAGIAMGLILEGERFAVLSDILGDEDHLGDMDFKVAGTDHGITSLQMDIKIAGITEEIMKVALGQAKEGRIHILGEMSKALTNARAELGEYAPRIETFKIPTDKIREVIGTGGKVIREIVEKTGAKVNIDDDGTVKVASSDGESIKAAIKWIKSIASDPELNAIYDGTVVKVMEFGAFVNFFGAKDGLVHISQLAAGRVQKTSDVVKEGDKVKVKLLGFDDRGKTRLSMKVVDQETGEDLEAKQKAEAEKAKAEGAPAAE", "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": "MFSMSRKQHASMYGPTTGDRLRLADTGLFAEIEEDLTIAGEEAVFGGGKVVRVGMGQNGHRTREEDPDIPDTVITNVIVLDWSGIYKADIGIRDGIITGIGHAGNPDTMDGGTIPIGVSTDIIAGEGKVLTAGGIDTHIHFISPEQIEAALVSGITTMIGGGTGPSESTKATTITPGPWHIHQMLRSLDGFPMNIGLLGKGHATASAPLIDQIRAGAIGLKVHEDWGATPATIDLSLSVADEFDIQVAVHTDTLNEAGFVESTREAIGGRVIHTFHTEGAGGGHAPDIIALAGEPNVLPASTNPTLPYTVNTVEEHLDMLMVCHHLNPDVPEDVAFADSRIRTETIAAEDVLHDMGIFSITSSDSQAMGRVGEVIIRTWQVADSMKRQRGPLEGDTADSDNNRIKRYVAKYTINPALAQGISHVVGSVETGKFADLVLWEPKFFGVKPFMILKGGQVVNSIMGDAGASIPTPQPELYRPMFGSYGSATSSNSITFLPRVAIAAGIPEQLGLNRRIEECHGIRTLTKQSLKLNGETPSIHVDPETYEVRIDGALITCEPAEKLPLAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "MALDVLTVAPLYQGPDINKIRLIAQTTKKSTIPPKALTPARSKLTTIETKRIMSVLDETIHKVELVSLLSHAASESKTSEGMLGPDIAKAVREHEDLCQALLDRVSYLQEEERKLQEAEDFEDEAWFRERLFAMDLQKSQLPPLMQEIKESTKNVVRLLLSNPQAASLLQAQTLGRSKEAQCFIDSLVELRGFLFEKLLTSPMEARDKIQFIQDITRRNRRHQEIIDTLENELAACVRNRNAEVEKENFVIQELKNHLHQVLRFSENSLLRTKQEAEKQQKADFRASQARVATVQQEILVLQSQFYNLVMENRDTEQALRKKKYKVETEIENWIQKYDSEMSEKQDEYEELDIIHKEEQLQLEELKKRHDVLVEEFSQIQAEREILTKKRLEDEQEMVRMVRAATLIQALWKGYLVRSMLKSKKKKRGKGKGEKKGKGKGKGKK", "text": "FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the DRC10 family."}
{"protein": "MKKFVTSIPNLLLTFTLCFVLSSCSSTGVKMSESSPWETIQFEDQSNALDIDFIDNNHGFLVGSNRLIMESNDGGKSWEKRSLDIAAEENFRLLDIDFKGSEGWLIGQPSLVMHTIDEGKNWTRLSLGKLPGQPFLVSTVDDGVAELATTSAAIYTTSNSGETWEAKVSDPSEQGGIRDLRRTSNGDYVSVSSLGNFFSTLESGSDTWIAHQRASSKRVQGIGFNPDGNLWMLSRGAEIRFNDDSNDLESWTKPIVPILNGYNYLDMGWDPEGNIWAGGGNGTLIVSKDDGKTWDSDPVASNLPTNFIKIQFLEKDELDAKKGFILGERGYILRWNG", "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 membrane; Lipid-anchor; Lumenal side Note=Associated with a PSII precusor complex on the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the Ycf48 family."}
{"protein": "MLFIFLTIAALGLSFWAQFKVKSNFEKYSKVEASSGRTGAETARRILDINGLYDVPVEPVRGTLTDHYDPTRRVVRLSEPVYYGRSISAISVASHEVGHALQHQESYGALVLRHKIFPVVNFASGVAPLLFLGGMLLGSLNLIGLGIILFSAAVFFQLITLPVEFNASSRAKQIIVSEGFIRNNEENGVNKVLSAAALTYVAAALVSLFELLRFVMIFLNGRDEN", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MEASTSLLVLVLAAAAFAAGTVTEAAGDGCSAGCDLALASFYVTPNQNVTNMADLFGIGAANYRSLAPYNPNIPNLDFINVGGRVNVYFTCGCRSLPGSPGATYLAGAFPFQMSRGQIYTSVAANYNNLTTAEWLQATNSYPANNIPDTAVINATVNCSCGDASISPDYGLFLTYPLRAEDTLASVAATYGLSSQLDVVRRYNPGMESATGSGIVYIPVKDPNGSYLPLKSPGKGASAGAIAGGVVAGVVVLAAIFLYIIFYRRRKAKQATLLQSSEDSTQLGTISMDKVTPSTIVGPSPVAGITVDKSVEFSYEELSNATQGFSIGNKIGQGGFGAVYYAELRGEKAAIKKMDMQATHEFLAELKVLTHVHHLNLVRLIGYCIESSLFLVYEFIENGNLSQHLRGMGYEPLSWAARIQIALDSARGLEYIHEHTVPVYIHRDIKSANILIDKNYRAKVADFGLTKLTEVGGTSMPTGTRVVGTFGYMPPEYARYGDVSPKVDVYAFGVVLYELISAKEAIVRSTESSSDSKGLVYLFEEALNSPDPKEGLRTLIDPKLGEDYPIDSILKLTQLAKVCTQEDPKLRPSMRSVVVALMTLSSTSEFWDMNNLYENQGLVNLMSGR", "text": "FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses. Involved in the resistance to pathogenic fungi, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP) (PubMed:21070404, PubMed:22891159, PubMed:24964058). Involved in the detection of microbial peptidoglycans (PGNs) and mediates PGN response (PubMed:24964058). Plays dual roles in PGN and chitin signaling during innate immunity. Acts as an adapter for LYP4 and LYP6 and mediates signal transduction from the extracellular to intracellular spaces. Participates in the activation of defense genes during response to PGN and chitin (PubMed:25335639). Phosphorylates the downstream partner RLCK185 in response to chitin elicitation (PubMed:23498959). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MLTEDPVSEICEAKAVDELAEQEKNYYCQRCLNHGELKPRKGHKPDCRYLKCPCRECTMVEQRRQLNNLLSKKKIHCTPATQTRDGKRVRDPHCARCSAHGVLVPLRGHKRTMCQFVTCECTLCTLVEHRRNLMAAQIKLRRSQQKSRDGKEPKRNSRRKSKDMDMEMMVVTATDGQKIIGTSASPSPSSTTDTMSPSLSMSPPCSPSPLLAQYTLTLAAPIPIYPPIPMNQQLISLQQQQFLMSIIQNMAPSIGQQAPLLPGISAGSVSSAAILNEFWSMYLKNYGLQA", "text": "FUNCTION: Transcription factor which binds the DNA motif 5'- [CGA][TCA][TA]ACAATGT[AT][TGA]C-3', probably as a monomer (PubMed:9490411). Acts partially redundantly with the transcription factor dmd-3 to coordinate tail tip cell fusion and retraction and thereby regulate male tail tip morphogenesis (PubMed:18550714, PubMed:21408209). Promotes male-specific development of two tissues, the peripheral nervous system and the intestine (PubMed:9490411). In the peripheral nervous system, directs differentiation of sensory ray neuroblasts into peripheral sense organs (PubMed:9490411). In the intestine, causes repression of vitellogenin gene transcription (PubMed:9490411). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKAVIFVVDGLGDRPDKNGNTPLKEAKTPVMDRMAKEGICGLMNSVDIGVRPGSDTAHLALLGYDPYTTYTGRGPFEACGVGVTVKPGDIAFRCNFSSVDENFIVTDRRAGRIENTSELEKELDGLKIDDVEIIFKESGGYRAALVLRGPGLSDKITDADPKKEGKKVKEIHPLDDSKEAKKTAEIVNKLLKIAYEKLDKHPVNEERRKQNLPVANMIVPRGVGQVPEIMQFTEKTGLKGACIAGTGLIKGIAKMVGLDVIDVEGCDGTPDSDFMAKACAIVETLENYDFILVNVKGADEAGHDGNYELKKQVIEKVDEMLDYITKNISKDEVYFVLSGDHSTPIEEMDHSADPLPVVLWGKSVRVDDVEKFDEFSTYKGGLNWIKGVHIMPILLDLMGLAKKYGA", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily."}
{"protein": "MKTLYSPRRFYPVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGIGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHSLLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVLKALYFGGVYDTWAPGGGDVRKISNLTLSPSIIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICIFGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVFGFTACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLSTSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDLEPVLFMTPLN", "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": "MALSVETESHIYRALRTASGAAAHLVALGFTIFVAVLARPGSSLFSWHPVLMSLAFSFLMTEALLMFSPESSLLRSLSRKVRARCHWVLQLLALLCALLGLGLVILHKEQLGKAHLATRHGQAGLLAVLWAGLQCSGGVGLLYPKLLPRWPLAKLKLYHATSGLVGYLLGSTSLLLGMCSLWFTANVTGGAWYLAVLCPILTSLVIMNQVSNAYLYRKRIQP", "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": "MQTRLWVTGYRSFELGAFNDKDPKIEVIKRALKENLIDQLENNGLEWIITGGQMGTEQWTCETAIGLKKDFPQLKIALMLPFSNFAANWNQEHQVKLTDLRTRVDFSEALSKESYKSPIQLRNFQAFMLKHTDGALMVYDPDNPGKAEFEYKAIQAYQLEHPDYSLKTIDFDMLTDISNEIEEEKRPW", "text": "SIMILARITY: Belongs to the UPF0398 family."}
{"protein": "MSEYSLFTSESVSEGHPDKIADQISDAVLDAIIAQDKYARVACETLVKTGVAIIAGEVTTSAWVDLEELVRKVIIDIGYNSSDVGFDGATCAVMNIIGKQSVDIAQGVDRSKPEDQGAGDQGLMFGYASNETDVLMPAPICFSHRLVERQAEARKSGLLPWLRPDAKSQVTCRYENGRVVGIDAVVLSTQHNPEVSQKDLQEAVMELIVKHTLPAELLHKGTQYHINPTGNFIIGGPVGDCGLTGRKIIVDSYGGMARHGGGAFSGKDPSKVDRSAAYAGRYVAKNIVAAGLAERCEIQVSYAIGVAQPTSISINTFGTGKVSDDKIVQLVRECFDLRPYAITKMLDLLHPMYQETAAYGHFGRTPQQKTVGDDTFTTFTWERTDRAQALRDAAGL", "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": "MYGIEYTTVLTFLISFILLNYILKSLTRMMDFVIYRFLFVIVVLSPLLKAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSIYFREYTDIVSFSVDPQLYCDYNVVLMKYDAALQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDTATFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDVLDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVNQIIQLMSKRSRSLNSAAFYYRV", "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": "MACCGGGRGEGAAATESEAYLEGEAVREARELVAELCRHFYGQGWVTGTGGSITVKANDPALPLADQLIVMSPSGVQKERMVAEDMYVLSADGKVLSSPVSKPWPNKPPKCTDCAPLFMKAYLMRGAGAVIHSHGMETCIATMLDPGAKEFRMTHMEMIKGIKGHGYRDELVVPIIENTPYEYELTDSLAEAIAAYPKATAVLVRNHGIYVWGDSWINAKTQAECYHYLFDAAIKLYQLGIDWTTPEHGPINSAKRPRSVLSSSIPNGCPDSKSSKHCVVLDIEGTTTPISFVTDVMFPYARDNVRKHLTSTYSSDETKEDIKLLRIQVEEDLKNGIVGSVPIPPDDADKEEVINALVANVESMIKADRKITSLKQLQGHIWRTGFESKELQGVVFDDVPEALKHWHASGMKVYIYSSGSREAQRLLFGNTAYGDLRQYLCGFFDTTTGNKRETRSYFEISQSLGVDSPAQILFITDVFQEAVAAKSAGFEVIISIRPGNAPLPENHGFRTIKSFSEI", "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": "MFRITDFTYEGKTVFLRADLNSPVEKGRITSDARFRAVLPTIQHLLDNGAKLVIATHQSRPYKGDYITTEEHAQILSRLLGQEVEYVEDIFGKYARERISSLKPGEAIILENLRFSAEEVFNRSIEECEKTFFVRKLAPLIDYVVNDAFATAHRSQPSLVGFARLKPMIMGKLMETEVDALSKAYESEERPRVYVLGGAKVDDSLRVAENVLRKGKADLILTGGLVGQIFTLAKGFDLGDANIEFLHRKGLLELVDWAEKILDEFYPYVRTPVDFAIDYKGERLEVDLLGGEKRLFDQYPILDIGSRTVEKYREILIGAKIIVANGPMGVFEREEFAVGTVGVFRAIGESPAFSVVGGGHSIASIYRYNITGISHISTGGGAMLSFFAGEELPVLKALKISYERFKDRVKE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MTASKRVAKELDDLSKELPPYLRHLSSDDANVLVWHMLLLPDQLPYRLKAFGLRIDFPREYPLKPPTLRFTTKIYHPNISEDGLVCLPLISTENWKPYTKAYQVLEALNILVSRPNLEEPVRLELADLLTQDPEMFRKKAEEFTLQYGVDRPS", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MKSSYGSSSNDLHAFVNEIKGEIQLSNINLDPYSFVSPSAYDTAWLSMIEEDINVDDNELKPMFQGCLDWIMCNQNAREGFWMNSTSYTTVADGRDEDGEKDMCILTSTLACVVALQKWNIGCFHLHKGTRYIERNTEMIIGKYINEEGSYPRWFAIKFTGILELAQKLGLHFVFSSRCIEMIKGMFYQRQEIIQREKLVHDCNYKPLLAYLEVLPSKLYVTNQEDIIVKSLDSMDGSLFQSPSATASAFMLTRNTKCLAYLQNLVQKCPNGVPQKYPLNEDLIKLSMVNLIESTGLGEFFGIEIEHVLEQVYSRYEEKDFERMPMSYLADQLHKDSLAFRMLRMHGRDVSPRSFCWFLNDQETRNHLERNIDSFLLVILSVYRATDLMFPGEHDLQEAREYTRNLLEKRRSIKEKMIMHELSTPWIARLKHLDHRMWIEDKNSNVLSMEKASFLRLHSSYSDKLTHLAARNFEFQQAKYCRELEELTMWVKKWGLSDIGFGREKTTYCYFATVTSLPYEYAIKFGKLAAKTAILITIADDFFDEKGSFNDLEGLTKAVLRWEGEELKSYGNIIFRALDDIVRETANTCRTHHKTDIIVHLRNIWGETFESWLREAEWSKKGHTSSMDEYIRNGMISIAAHTIALSISCLMEPCFPHNKLKPGNYDSITTLLMIIPRLLNDLQSYQKEQEQGKMNSVLLHMKNHPGLEIEDSIAHIEKIIDSKRKEFLEHVLVDGLSDLPKPCKEIHMSCCKVFEMFFNKKNRYDSNTEMLHDIKKALYDPINVYELSEMEPMPLMAHGDEYMILPLLLNSLPNILEFKRKDGYGAMKTSMCFGRSYRVNKRVMASQLDDQHKPLKIVASQRKPVPMMQSIFAPCFY", "text": "FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (PubMed:21334702). Involved in diterpene (C20) biosynthesis (PubMed:18398052, PubMed:18842097). Catalyzes the conversion of geranylgeranyl diphosphate to (E,E)-geranyllinalool, the precursor of the insect-induced volatile C16-homoterpene TMTT (PubMed:18398052, PubMed:18842097). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family. Tpsf subfamily."}
{"protein": "MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDPVSALLIDIDFFKKINDTFGHDIGDEVLREFALRLASNVRAIDLPCRYGGEEFVVIMPDTALADALRIAERIRMHVSGSPFTVAHGREMLNVTISIGVSATAGEGDTPEALLKRADEGVYQAKASGRNAVVGKAA", "text": "FUNCTION: Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition. FUNCTION: Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition. FUNCTION: Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger. FUNCTION: Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger. SUBCELLULAR LOCATION: Cytoplasm Note=Phosphorylated PleD localizes to the differentiating pole. SUBCELLULAR LOCATION: Cytoplasm. Note=Phosphorylated PleD localizes to the differentiating pole."}
{"protein": "MGLSDGEWQLVLKVWGKVEGDLPGHGQEVLIRLFKTHPETLEKFDKFKGLKTEDEMKASADLKKHGGTVLTALGNILKKKGQHEAELKPLAQSHATKHKISIKFLEYISEAIIHVLQSKHSADFGADAQAAMGKALELFRNDMAAKYKEFGFQG", "text": "FUNCTION: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. SIMILARITY: Belongs to the globin family."}
{"protein": "MGNKTHPTGFRLGVTEDWRSMWYADSSNFGKYLNTDLEVREFIRERLKNASVSRIQIERPAKNALVTIHTARPGIVIGKKGEDIDRLRGEVAARMGVPVHINIEEIRKPEADSKLVAESIAGQLERRVMFRRALKRAVGNAQRVGAQGIKVQVSGRLNGSEIARTEWYREGRVPLHTLRADIDYGFAEAKTTYGVIGVKVWIFKGEIIDTENEGAPAERVKRAAAAQG", "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": "MMPVAGLLLCVTAVLCTSALGAGPRLDNGKLYRYSYSTEVGLNRPTGSPGGNVGFRISSDVDINLAWRNPEIQDEQLLQVKISNIQVESAGKHSRKNNIFHGSSAESILGKVRLEALQRPFLVLWKMGKIRSLYAQKAEPATVKNLKRGVASMLMMQLKSGKMSEADASGKCLVEYKVNKHQVIRTKHLETCKSQETGFTTHSPVLGISGKCAAETVITLENGIIKSADAKETHVLSINARHKAATKVLSRQSLTLKAIEAGPAEVAGKDVAGVVKALDDKFLSVGVIVEKTKPKCKGCPNLMETWKAVRSQLEPNSLSKAEAPRSFLTLVHSLRKSSKSEILTVLQNCSKTALPQLVDAVTSAQTPSSLSAILEFLDFSKKDGLILQERFLYACGFASHPTESMLQSLLEVSQGKIGSTEIKESVVIIMGALLRKLCLKGACDLPAVLKVKELLLAGPDSTQEESEVQMYLLALKNALLPEGIPVLAKYAESEVGAYSTIAITALQRYDPALITAEVKKALNRIYHQNQRIYEKNVRAAAADVIMSSNPSYMEVKNLLLSIGHLPHEMNKYMLSKIQDVLRFQMPAYKLVRQVMKDMISHNYDRFSKTGSSSAYSGFMAETVDVTCTYNLDILYSGSGVLRRSNMNIYGQSNNALLHGLQVTIEAQGLESLIAATPDEGEEELESFAGMSALLFDVQLRPVTFFKGYSDLMSKMFSMSGDPINVVKGLILLTDHSQVIPLQSGLRASAEFQAGLSIDISGGMEFSLWYRESKTSVNNRGALVIIGNMTVDTDFVSAGVEVGFETEATLDFITTVQFSEYPFLVCMQMDKTTFPFRETVSKQEKLPTGQMFSRKRSRDQVVPGSEFPLHQENSNMCKKVFEPAW", "text": "FUNCTION: Catalyzes the transport of triglyceride between phospholipid surfaces (PubMed:17924655). Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:22581286, PubMed:17924655). Required for yolk lipid utilization and absorption of dietary lipids in larvae (PubMed:17176039). SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum."}
{"protein": "MSFKDLRSFISHLEECGELKRVSYPVDPYLEMTEIADRVLRAGGPALLFEQPKGHSMPVLANLFGTPKRVAMALGKEDPLALRDVGELLAFLKEPEPPRGFKDAIAKIPMFKQALNMPPKTVSRAPCQEVVMTGDDVDLTKLPIQHCWPGDVAPLVTWGLTITKGPRQKRQNLGIYRQQLLGKNKLIMRWLSHRGGALDFRDFQEKHPGENYPVVVALGSDPVTILGAVTPVPDSMSEYAFAGLLRGERTEVVKALSCDLEVPATSEIILEGYIAPGEMAEEGPYGDHTGYYNETDSFPVFTVTHISHRKDAIYHSTYTGRPPDEPAMLGVALNEVFVPILRKQYPEIVDFYLPPEGCSYRMAVISIRKQYPGHAKRVMMGAWSFLRQFMYTKFIVVVDEDVNCRDWQDVIWAITTRMDPTRDTVMIDNTPIDYLDFASPVAGLGSKMGLDATNKWEGETNREWGTPIVMDEAVKRRVDDIWDELGIEQSPTL", "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": "MALKALLGLSQAQLETWAKDQGLPPFRGRQLHDWLYAKGARHWHDITVLPAALRQQEPLPLGRSNELERHLAQDGTLKLLLATDDGLSLETVGIPTRDRLTVCVSSQVGCPMACRFCATGKEGLQRSLEPHEIVDQVLTVREVMQRRPSHVVFMGMGEPLLNSDHVLTAIDCLSRDLGMAMRQITVSTVGVPNTLPRLAELALERLGRAQFTLAVSLHAPDQALREELIPTARAYPYEQLLEDCRHYVAISGRRVSFEYILLGNLNDSPRQAQALAEQVRGFQSHVNLIPYNPIAEEEFQRPEPARVDAFAAALKQRGVAVSVRASRGLDQNAACGQLRRQRQGGR", "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": "MDLKQYVSEVQDWPKPGVSFKDITTIMDNGEAYGYATDKIVEYAKDRDVDIVVGPEARGFIIGCPVAYSMGIGFAPVRKEGKLPREVIRYEYDLEYGTNVLTMHKDAIKPGQRVLITDDLLATGGTIEAAIKLVEKLGGIVVGIAFIIELKYLNGIEKIKDYDVMSLISYDE", "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": "MNAMKRGLCCVLLLCGAVFALPSQEIHARVRRGARSYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVRSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGLAYRGTHSLTESGASCLLWNSMILIGKVYTAQNPNAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFARHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVADNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGEKDVPGVYTKVTNYLDWIHDNMRP", "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": "MRASMFLALAGLVLLFVVCYASESEEKEFPRELLFKFFAVDDFKGEERACKGVFDACTPGKNECCPNRVCSDKHKWCKWKL", "text": "FUNCTION: Lethal toxin with multiple biological activities. Inhibits voltage-gated TTX-sensitive sodium channels in DRG neurons (IC(50)=55 nM) and also shows activity when directly tested on Nav1.7/SCN9A (IC(50)=25.1-630 nM) (PubMed:17451655, PubMed:21731778, PubMed:31234412). Inhibits N-type calcium channels (Cav2.2/CACNA1B (IC(50)=100 nM)) (PubMed:11024489, PubMed:17451655). Also blocks neuromuscular transmission (PubMed:8212049, PubMed:9028007, PubMed:10736477). In vivo, intrathecal injected toxin shows analgesic activity in the rat formalin-induced pain model, without induction of motor dysfunction in rats. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 23 (HwTx-I) subfamily."}
{"protein": "MVHQLKLLKDDFFASDQQAVAVADCYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQGAIPGFSVSAGQPHWRLGSMGMAQARQIIGQLEHESSQHVPFANEMAELLFGQLVMLLNRHRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD", "text": "FUNCTION: Activates expression of the rhaSR operon in response to L- rhamnose. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MARFQEFYKEKVVPGLIEKFGYKSVMEVPRITKITLNMGLGEAVADKKIIENAVGDLTKIAGQKPVVTKARKAIAGFKIRQGYPIGAMVTLRGRAMYEFLDRFVTVALPRVRDFRGVSGRAFDGRGNYNIGVKEQIIFPEIDYDKIDALRGLNISIMTTAKTDDEAKALLASFKFPFRN", "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": "MPIRNIAVGSHQEVYHPGALKAALAEFISTLIFVFAGQGSGMAFSKLTGGGATTPAGLIAAAVAHAFALFVAVSVGANISGGHVNPAVTFGAFVGGNITLFRGLLYWIAQLLGSTVACFLLRFSTGGLATGTFGLTGVSVWEALVLEIVMTFGLVYTVYATAVDPKKGSLGTIAPIAIGFIVGANILVGGAFDGASMNPAVSFGPALVSWSWESQWVYWVGPLIGGGLAGVIYEVLFISHTHEQLPTTDY", "text": "FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. May be involved in transport from the vacuolar compartment to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC 1.A.8.10) subfamily."}
{"protein": "MAAELTSTKLNAENHLLLDQPLLRLPHELARRNLKSFQRIVEREKEYVLPALKEAAKASMSGNQTPEQTLATLDVMISRMQGLKRKMENLQQEEKKIHHQSRKRIQHLNQLYQIPSLTDVKYDQWSRVRLDRLVIDHMLRSGYSESAQRLARAKNIEELVDLNVFVQCQRIAESLRNGETKDALQWCNENKAALKKSQYNLEFELRLQQYIEMIRTRDRAKFVDAMVHARRYLAPYDETQSAEIRRAAGLLAFPPNTRAEPYKSMYASERWVYLSELFIRTHHELLSLPSRPLMHIALSAGLSALKTPACHSAYTSSSSNSHSTATSVCPICSTELNELARNLPYANHTKSSVENDPVVLPNGRVYGLHRLLDMSKKLSSLEAGKVRDPTTGEIFNESELKKVYIM", "text": "FUNCTION: Involved in the proteasome-dependent degradation of fructose- 1,6-bisphosphatase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the FYV10 family."}
{"protein": "MHCPFCSENDTKVIDSRLVADGHQVRRRRQCLACNERFTTFETAELLMPKVIKSNGNREPFNEDKMVGGIQRALEKRPVSADAIELAISMIKSKLRATGEREVPSKMIGNLVMEQLKDLDKVAYIRFASVYRSFEDIREFGEEIARLED", "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": "MAQSVTGIQIGGMSFPPSVKPPGSGNTFFLGGAGVRGMEIQGNFVKFTAIGVYLEDKAVPALAVKWKGKTAEELTESVEFFREIVTGPFEKFTQVTMILPLTGQQYSEKVSENCVAIWKKFGIYTDAEAKAIEKFIEVFKDQTFPPGASILFTQSPDGSLTIGFSKDGCIPEVGNAVIENKLLSESVLESIIGKPGVSPEARKSVATRLSELLKESDHCVAGNGKVDECTKEAEVKA", "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": "MSKITEQIEEIIQPVLDDLNFELVEIEFTKEGKDHFLRISIDKEGGVDLNDCTLASEKISEVMNEEDPIEQMYYLDVASPGAERPIKTDKALHDAVEQPVFVSLYAPIDGSKEWLGVLQSVTDDHIVIKAQVKEKKKEVEIPRNKIAKARHAVLI", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MGTPLRRSRRLEGLNPLSLENLPDPEVSRAKRALVDFKSNPEETRELESPRVPPLDLVSPQPQPETSPESPCPKQDAGFGSPQRQPEPHPGSLQLHQDLGLDSPAGQTESNPESPQREQSSKLSPTQDSEVAHAKEEVIPRSPEPCPGQQAPGPEPSQPAQELAFQAPSSPERQLEPSKLPPAGESVTGSLDLKKRVIASPQAPASKKLKEELPVIPKGKPKSGRVWKDRSKKRFSQMVQDKPLRTSWQRKMKERQERKLAKDFARHLEEEKQRRRQEKKERRAENLRRRLENERKAEIVQVIRNPAKLKKAKKKQLRSIQKRDTLALLQKQPPQRPVAKV", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLIAQRPTLSEEVVSENRSRFIIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFTTVPGVKEDVTEIILNIKNLSVSSEHDEPVVAYLRKQGPGVVTAADIAPPAGVEFHNPDLHIATLNSKGKFELELTIERGRGYVSAAQNKSGDSEIGRIPVDSIYSPVLKVTFRVEATRVEQRTDFDKLIVDVETKQAIAPRDAVASAGTTLVELFGLARELNTAAEGIEIGPSPTDAALAADMALPIEDLDLTVRSYNCLKREGIHTVGELVARSEADLMDIRNFGAKSIDEVKAKLVELGLSLKDSPPGFDLAARAAAIEEDDAAFSDDEL", "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": "MEDLDALLSDLETTTSHMSRLGAPKERPPETLTPPPPYGHQPQTGSGESSGTTGDKDHLYSTVCKPRSPKPVAPVAPPFSSSSGVLGNGLCELDRLLQELNATQFNITDEIMSQFPSSKMAEGEEKEDQSEDKSSPTVPPSPFPAPSKPSATSATQELDRLMASLSDFRVQNHLPASGPPQPPAASPTREGCPSPPGQTSKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFLCSGCSTTLGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGEEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECLAPFSGGSFFEHEGRPLCENHFHAQRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERASKPYCQPCFLKLFG", "text": "FUNCTION: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton, colocalizes with stress fibers. SIMILARITY: Belongs to the paxillin family."}
{"protein": "MSTPNCKITTQRLVVNDMKPLSIETEIISLTKEIITHTFIYLINHECIVRKLNEQQATFTFLVNYEMKLLHKVGSTKYNRYTEYNSKYGTFPMPIFINHAGFLECIGIKPTRNTPVIYKYDLNP", "text": "FUNCTION: Plays a major role in antagonizing the type I IFN-mediated antiviral response. Acts cooperatively with NS1 to repress activation and nuclear translocation of host IFN-regulatory factor IRF3. Interacts with the host cytoplasmic sensor of viral nucleic acids RIGI and prevents the interaction with its downstream partner MAVS. Together with NS2, participates in the proteasomal degradation of host STAT2, IRF3, IRF7, TBK1 and RIGI through a NS-degradasome involving CUL2 and Elongin-C. The degradasome requires an intact mitochondrial MAVS. Induces host SOCS1 expression. Induces activation of NF-kappa-B. Suppresses premature apoptosis by an NF-kappa-B-dependent, interferon- independent mechanism promoting continued viral replication. SUBCELLULAR LOCATION: Host mitochondrion Note=Most NS2 resides in the mitochondria as a heteromer with NS1. SIMILARITY: Belongs to the pneumovirus non-structural protein 2 family."}
{"protein": "MAWQGKLTDRTASIFQGKQMSLKLINIPRVKLSAAAFTKAFCHHKLIEVNATSVDSELLAPDIIHALQSSAWIQKNLQCLVLDSVSIPPNSGLVALSHFTGLHTLSVANVSFCNEDLVSVSQLPNLGSLDISNTLVTNISALLSCKNRLRSLTMHYLKCLAMNSPQVLAVIRQLKCLLHLDISDHQQLRSDLAFYLLQQKDILPNLTSLDISGGTDVTDQAVESFLQHRPAMRFVGLLYTDAGYSDFFTAKQGLKVAGGANMSQISEALSRYRNRSCFVKEALFRLFTETLSLRAVLPVMLKLVAIGMRNHPLDLPVQFTASACALNLTRQELARGMPVRLLAEITDLLFKATKNFPYYQQLQKNCLLSLTSSRILMDVPFDRFDAAKLALRWVCRRESPKLRTMAVSITSILALKLSPEEMGQLQEELIMAIKELLTIIRQKLAENLDDVTFLFTLKALWNLTDECPLACKYFMENEGLATVIRVLETFSISVIQSKVLGLLNNVAEVRELSSKLVTEDVIERIISLLHSSNLEVSFLAAGVLAHLTCDRQHWLSRDLQRTDLLRYLHLAIQNWPSSRCDMSVLVTYRSFKAFSPLLVNFSQPEVQRWALWAIHHVCSKNPRPKDV", "text": "FUNCTION: Probably acts as target recruitment subunit in an E3 ubiquitin ligase complex ZYGA-CUL2-elongin BC. SIMILARITY: Belongs to the zyg-11 family."}
{"protein": "MNTMTLTPGQLSLSQLYDVWRHPVQLRLDASAIDGINASVACVNDIVAEGRTAYGINTGFGLLAQTRIADEDLQNLQRSLVLSHAAGVGDPLDDAMVRLIMVLKINSLARGFSGIRLSVIEALIALVNAGVYPLIPAKGSVGASGDLAPLAHLSLTLLGEGKARWQGEWLPAQAALKKAGLEPVALAAKEGLALLNGTQASTAFALRGLFEAQELFASAVVCGALTTEAVLGSCRPFDARIHAARGQQGQIDVARLFRHLLTDTSAIAESHHHCHKVQDPYSLRCQPQVMGACLTQLRQTKEVLLAEANAVSDNPLVFAEAGEVISGGNFHAEPVAMAADNLALAIAEIGALSERRITLMMDKHMSQLPPFLVKNGGVNSGFMIAQVTAAALASENKALAHPHSVDSLPTSANQEDHVSMAPAAGRRLWEMAANTRGVIAVEWLAACQGIDLREGLTSSPLLEQARQTLRERVAHYTQDRFFAPDIECATTLLAQGALQRLVPDFM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAL/histidase family."}
{"protein": "MPQLQGLNHLLFSVSDLEKSFCFYRDVLHAKPLVRGRKLAYFDLNGYWLALNEEPDIPRNEIAHSYTHMAFTITEESFDEWYAHLEKHGVTILHGRDRSERDKRSIYFIDPDGHKFELHTGTLQDRLAYYRDEKHHMTFFE", "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": "MATNFSDIVKQGYVKMKSRKLGIYRRCWLVFRKSSSKGPQRLEKYPDEKSVCLRGCPKVTEISNVKCVTRLPKETKRQAVAIIFTDDSARTFTCDSELEAEEWYKTLSVECLGSRLNDISLGEPDLLAPGVQCEQTDRFNVFLLPCPNLDVYGECKLQITHENIYLWDIHNPRVKLVSWPLCSLRRYGRDAARFTFEAGRMCDAGEGLYTFQTQEGEQIYQRVHSATLAIAEQHKRVLLEMEKNVRLLNKGTEHYSYPCTPTTMLPRSAYWHHITGSQNIAEASSYAAQGPEQQVASQFLWAWSDTGRICASTVLLASLAVGVLSRGDIWLTPQVKIWF", "text": "FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK4 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway (By similarity). Putative link with downstream effectors of RET in neuronal differentiation. May be involved in the regulation of the immune response induced by T-cells (By similarity). SIMILARITY: Belongs to the DOK family. Type B subfamily."}
{"protein": "MLKSKIHRATITDACIDYEGSITIDKNLMQAANLLPYEQVHVVNVNNGTRLETYVIEGSAGSGQICLNGAAARMGMKGDKIIILGYSLITEEDTLIHQPNLVYVDALNRITKVKNGVANQGLEV", "text": "FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family."}
{"protein": "MEAILDKIFVEEAVSELHTLQDMIRWTVSRFNAANLFYGQGTDNAWDEAVQLILPTLYLPIDVPPHVLSSRLTSSERLRVVERVIKRINDRTPVAYLTNKAWFCGLEFFVDSRVLVPRSPIGELIQNRFEPWLTEEPTRIMDLCTGSGCIAIACANAFPEAEVDAIDISVDALNVAEQNIQDHGLEQQVFPIRSDLFRDLPQEQYDLIVTNPPYVDQEDMDSLPSEFRHEPELGLAAGSDGLKLARRILANAPLYLKENGILVCEVGNSMVHMMEQYPHIPFTWLEFENGGHGVFLLTREQLIDCAADFALYKD", "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": "MRNDLVLEDTTLRDGEQTPGVAFSKETKTAILNALIEAGVTSIEIGIPAMGGEELDFIKSVVDRQDEARLVVWHRGVREDVERSLDLGFTSVHVGLPTSAGHLKASVRKDRTWLLATARDMVKMAKDRGAFVSISAEDIARTEISFLQEYAGVVAEAGADRLRLSDTVGLLGPEAYGERVAAVLSAADIDVQCHAHNDFGLATANTLAGLKAGARYFHVTVNAIGERAGMADLAQVVVALKKLYDRDLGIDLTKLKKVSRLVAEAAGHQVLPWQPITGDNVFAHESGIHANGMFRDTSSFEPFPPEHVGGERRYVLGKHSGRALVAWALEQEGITPREELLPHCLEEVRALSIRIGGAVSHEQLVEIYNKAAA", "text": "FUNCTION: Involved in the biosynthesis of the phosphonic acid antibiotic FR900098, a potential anti-malarial drug, which acts as a potent inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation between acetyl-CoA and phosphonopyruvate to yield (R)-2-(phosphonomethyl)malate. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family."}
{"protein": "MSRVAKAPVAIPAGVEVKLNGQEITVKGAKGELSRVINNAVVIAQEENKLTFGPREGVANAWAQAGTARALVNNMVVGVTEGFTRKLILKGVGYRAAIKGNAVGLTLGFSHPVEHELPAGIKAECPSQTEIVLTGCDKQLIGQVAADIRAYRAPEPYKGKGIRYADENVRSKEAKKK", "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": "MNPQELKSILSAGLLSFPVTDFNAQGDFNRAGYIKRLEWLAPYGASALFAAGGTGEFFSLAASEYSEIIKTAVDTCASSVPILAGVGGSTRQAIEYAQEAERLGAKGLLLLPHYLTEASQDGVAAHVEAVCKSVNIGVVVYNRNVCRLTAPLLERLAERCPNLIGYKDGLGDIELMVSIRRRLGDRFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFIPKTAMDFYHAIAREDHATVGKIIDDFFLPYLDIRNRKAGYAVSIVKAGAKIAGYDAGPVRAPLTDLTGEEYEMLAALIDKQGAQ", "text": "SIMILARITY: Belongs to the DapA family."}
{"protein": "MEAKTLGIATPRKPVLSVSARKLKDNAADWHNLILKWDSLSDKGFTTASSIANLKVSLLSKEKVELESSSPASMEEEEKTNLDYDKGLEALCEELQAILDGLTKIQMKMEKLSSTTKGICELENYHYREESSRPPLFHTWPTAFFYEVSRRLSEAYKKELLLKHTIGAELAHTADRNLSLTYLSMWLHQPYIESNSKLQLESMLLETGHRAL", "text": "FUNCTION: Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling in response to DNA damage. Also 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. Promotes maturation of pre-60S ribosome together with AFG2A, AFG2B and AIRIM. SUBCELLULAR LOCATION: Nucleus Note=Binds to nuclear under G1 conditions, and dissociates from chromatin with the start of DNA replication. SIMILARITY: Belongs to the CINP family."}
{"protein": "VEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE", "text": "FUNCTION: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. SUBCELLULAR LOCATION: Cytoplasm, myofibril Cytoplasm, myofibril, sarcomere Note=Thick filaments of the myofibrils."}
{"protein": "MKYDTSELCDIYQEDVNVVEPLFSNFGGRASFGGQIITVKCFEDNGLLYDLLEQNGRGRVLVVDGGGSVRRALVDAELTRLAVQNEWEGLVIYGAVRQVDDLEELDIGIQAMAAIPVGAAGEGIGESDVRVNFGGVTFFSGDHLYADNTGIILSEDPLDIE", "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": "MTESKRILADVLLRPVITEKATALMEQRKYVFEVMPTATKPLIRAAVEEMFGVRVTAVNTLKLPRKQRRVGRSVGYRSRPKRAIVTLAEGDSITLFPDT", "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": "MAKLAVIRIRGRVNVKRPVRDTLAMLRLHRVNHCVIVDDTPSYLGMLQKAKDYITWGEINAETLAKLIRKRGKLIGNKPVTDEYVKEKLGMTIEEFAQKVINGEMSLKDLPNLKPVFRLHPPRGGFKGSKKRSFQEGGALGYRGEKINELIERML", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MKTFSAKPAEVKRDWYLVDASGKTLGRLASEVARRLRGKHKPEYTPHVDTGDYIVIINADKVRVSGKKAQDKMYYHHTGYIGHMKSMNFNQLMERAPERAIEFAVKGMLPKNPLGRAMFKKLKVYAGTEHKHTAQQPQALEL", "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": "ATYYKVKLLTPEGEKEFECPDDVYILDNAEEIGIDLPYSCRAGSCSSCAGKVVSGKVDNSDNSFLNDDNMDAGYVLTCHAYANSDVVIETHKEEEV", "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": "MEVTLSQGEYRLLKLMAERGFREGTLEEASKILGVDKSSLASLSNLLAEKGVVEVEERVEEHYVLTERGRDALERGLPEEKLVLFLAGRGGEASVEEVRRALGEEAGIALGQAARKGLVVIAGGVVRLAVDQAEALKTITPLKKLLENVASGSKPTVGDELLREALSRGLIRREARRSIVLRLKVNPAEALARARVEAAVLTRDMLKSGEWRRLRFKPYNVKAEPPRVLPARRHFLAEFIERLRDILRELGFREVRGPLVELELFNFDVLFQAQDHPAREIHDSLWIKSPRRGDLSGYSDLVERVASVHERGWKYRWSPEVASRYILRSQTTAVSARILATRPNPPARFFTVGKVFRSDAVGPTRLPEFHQLDGIEGDEGYTFRDLLGRLDEIASMLGLKLKFKPAYFPFTEPSVEGYVKLPNGRWLELFGAGMFRPEVLEAVGVDYPVGAWGFGIERLAMAFYGVSDIRKLYTRNVDEVREMRVRWL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily."}
{"protein": "MDIYGLIGNPVEHSLSPPMHEAAYDARGIDARYVTFEPTKDTLETAINGANALDIAGINVTIPFKQDVLNHIIPDDIAREVGAVNTIKFHDGETPRGYNTDVAGVKRAFQHHNISIDGYDAVVVGAGGAGRAAAFALADAGAHVHIANRTVERAETIATDIGGQATAGGLDTRDEISDADILLNATSVGMDPDSNQTPVPQSYLHDGLVVLDAVYTPIETRLLREATAAGATTIDGAWMLLYQGVVAFEIWTEQDAPIQQMNAALRAELEDA", "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": "MEIIIISLCLATILAFLLLKPLLNRTVAKDNLPPSPWRVPVIGNLHQLSLHPHRSLRSLSHRYGPLMLLHFGRVPILVVSSSDVAHDLMKTHDLKVANRPRLKVIETILNGGREVVFSPYGDYWRQIKTVCVVHLLNKKMVQSFAKVREEERSVMMEKVEKASSDSSPLNLSKLLITLTSDVASRVSFGKKHSNEASMSDFKNQVRKITELVGGFPVSEYIPCLAWIDQIRGLYNRAEEVSKIFGDLMDKVVQEHLDATNKPTKDFVDILLSFERQSKDGIEVRRSDIKFIILDIFLGGTTTTNSLLEWTMTELIRHPECMKKLQDEIRGDATNLTIYRSHEEVEDMKYLKAVIKEGLRLHPPFPLLVLRLLTQDVKLKGYDIAAGTQVITNAWAIQRDIVTWGIDAEEFRPERHLDSPLDFRGTNFEYIPFGSGRRICPGIGFAMALVEVTLANLVNRFNWRMDARLSGDEYDLAEATGIDVCRKFPLIVFPSNA", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MATGSTELLIGWCIFGVLLLAILAFCWVYVRKYQSHQESEVISTITAISSLAIALITSALLPVDIFLVSFMKNHNGTFKDWAENNDTRIQIENTVLIGYYTLYSIILFCVFLWIPFVYFYYEEKDDTDGSHCSQIGSALKYTSGFVLVCSCLLLIGAFAPLDIPSKANATELDKIKLLFQNLGSSNGLAALSFSISSLTLIGMLAAITYTAYGMSALPLNLIKGKRNAHYERLENSEDIEEVEQQVENIKSKCKDGRPLSSKDRQALYKLQEKLRTLKRKDRHLEHHENNCWTKCCLVMRPFKIVWGILFILVALLFIVSLFLSNLDKALHSAGINTGFIIFGTNLTNPLNILLPVLQTVFPLDYIFITTITMYFIFTSMAGIRNMGIWFFWIRLYKIRRRRTRPQALLFLCMILLLIVLHTSYMIYSLAPQYVMYGSQKYLWENNSTQETAIGNSSALVLKDCDASAPEDQCTVTRTYLFLHKFWFFSSIYYFGNWAFIVVFVIGLIVSCCKGKKSVIEGEVEDDDSDLSDDEDHP", "text": "FUNCTION: Lysosomal membrane chaperone required to export cobalamin (vitamin B12) from the lysosome to the cytosol, allowing its conversion to cofactors. Targets ABCD4 transporter from the endoplasmic reticulum to the lysosome. Then forms a complex with lysosomal ABCD4 and cytoplasmic MMACHC to transport cobalamin across the lysosomal membrane (By similarity). May play a role in mediating and regulating the internalization of the insulin receptor (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane Lysosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily."}
{"protein": "MKRIAILTSGGDAPGMNAATRAVVRKAIYEGLEVYGINYGFLGLVNGDIRKLELGSVGDLLHRGGTFLYSARYPEFATEEGQLKGIEQLKKHQIDGLVVIGGDGSYHGAEALTKRGFPTIGIPGTIDNDISGTDFTIGFDTALNTVLDALDKIRDTATSHERTFIIEVMGRDAGDIALWSGLAGGAEAIIVPEESFNMDDVVDRLNKGRERGKKHSIIVVAEGVMSGNEFAKQLAEYGDYHARVTVLGHVQRGGSPTAFDRVLASRLGARSVELLLENRGGLAVGIRENRIVENNIGEILKEKHTLDQKLFDLASILSI", "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": "MKKVLRNVQMLNEQGELQTVNIAMADGKITAIGQEVTVVNAEVIEGNGLIVAPGFVDVHTHLREPGFEHKETIATGSASAAKGGFTTICAMPNTKPVPDSVENMQLINGLIKESAVIRVLPYGSLTKDISGEVRTNVEELKAYGAVAFSDDGVGIQLASTMYEQMKDAAKHDMVVVAHCEDNSLIYDGVMHEGKRNKELDLPGIPSICESVQIARDVLLAEAAGARYHVCHVSTKESVRAVRDAKAAGIRVTAEVCPHHLLLEEMDIPSDDANWKMNPPLRGADDKDSLHAALLDGTIDCIATDHAPHTVEEKCCGMVGAPFGIVGFETAFPLLYTQFVETGKWTLKQLIDWMSVKAAEIFDLPYGTLAVGASADMILIDIQKEQTIDAEGFVSKGRNTPFNGWVAKGWPVLTIFEGNIVYQEAE", "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": "MKKSALEKLLSLIENLTNQEFKQATNSLISFIYKLNRNEVIELVRSIGILPEAIKPSSTQEKLFSKAGDIVLAKAFQLLNLNSKPLEQRGNAGDVIALSKEFNYGLVADAKSFRLSRTAKNQKDFKVKALSEWREDKDYAVLTAPFFQYPTTKSQIFKQSLDENVLLFSWEHLAILLQLDLEETNIFSFEQLWNFPKKQSKKTSVSDAENNFMRDFNKYFMDLFKIDKDTLNQLLQKEINFIEERSLIEKEYWKKQINIIKNFTREEAIEALLKDINMSSKIETIDSFIKGIKSNDRLYL", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-AAGCTT-3' and cleaves after A-1."}
{"protein": "MFGLTTLAANKLPLGNMLFIIISFLVLMVILKKVAYGPLTKVLDERAEKISTDIDGAESARQEAENLAAQRQSELADTRQQATKVVADAKASAQKQSDALVAVAAERANTINQQAQTDAEKLKEDAIANAKNDVAALSVAIASKLMQKELSLNDQQALIDAYISDLETK", "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": "MRADTNNYRELFLRDVPMLDTRAPTEFSKGAFPGAVNLPLMDDAERQQVGLCYKQRGQDAAIALGHQLVSGPIKARRVAAWADFARAHPDGYLYCFRGGLRSQISQAWLKNEAGIEYPRVIGGYKAMRGFLLQTIDDAVAQCGFVVLGGMTGTGKTDLLRQLDNSLDLEHHAHHRGSSFGKHAVGQPTQIDFDNRLAIDILKKRAAGHDRFVLEDESQAIGACSLPFELYRGMQEYPVVWLEDTTENRVNRILRDYVIDLCAEFVDVHGPEQGFDRFAERLRQSLDNISRRLGGERHRQLAGVMDAALAEQQRSGRVDAHRAWIAALLAQYYDPMYAYQRQRKSQRIVFAGDHQSVLQYLRDPPAVGRALKGFP", "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": "MARTKQTARKSTGGKAPRKQLASKAARKAAPSTGGVKKPHRYKPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKSDLRFQSSAIGALQESVEAYLVSLFEDTNLCAIHAKRVTIQSKDIQLARRLRGERS", "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": "MATFSQKPAEVEKKWILIDAEGLVVGRLASIIAMRLRGKHKATFTPHVDDGDNVIVINADKIVLTGKKYEDKVYYWHTGYAGGIKERTARQIIEGRFPERVVEKAVERMVPRGPLGRRQMKNLRVYAGSNHPHEAQQPVVLDVAKLNKKNVRSA", "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": "MARVTVEDAVKQIGNRFDMILVAARRARQIAVQGKDPMVEEQNDKPTVIALREIEKGLVNAGTLDADERQSVREREAAEIAAVAAIAEGRSL", "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": "MFPKSLAVSRKNSNLTKGVSGLRRLCSSSSTITGSPCPPRYDVAVIADLIEKQHWSKLGVHVTDINPNELFRQLISSELDPDLCLRYYSWLVKNSDISVSLELTFKLLHSLANAKRYSKIRSFLDGFVRNGSDHQVHSIFHAISMCDNVCVNSIIADMLVLAYANNSRFELGFEAFKRSGYYGYKLSALSCKPLMIALLKENRSADVEYVYKEMIRRKIQPNVFTFNVVINALCKTGKMNKARDVMEDMKVYGCSPNVVSYNTLIDGYCKLGGNGKMYKADAVLKEMVENDVSPNLTTFNILIDGFWKDDNLPGSMKVFKEMLDQDVKPNVISYNSLINGLCNGGKISEAISMRDKMVSAGVQPNLITYNALINGFCKNDMLKEALDMFGSVKGQGAVPTTRMYNMLIDAYCKLGKIDDGFALKEEMEREGIVPDVGTYNCLIAGLCRNGNIEAAKKLFDQLTSKGLPDLVTFHILMEGYCRKGESRKAAMLLKEMSKMGLKPRHLTYNIVMKGYCKEGNLKAATNMRTQMEKERRLRMNVASYNVLLQGYSQKGKLEDANMLLNEMLEKGLVPNRITYEIVKEEMVDQGFVPDIEGHLFNVSTKS", "text": "SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MPVSDFQVVLGLEVHAQLLTRSKIFCACPTEFGGAPNTHVCPVCLGLPGALPALNAAVVEMAIRTGLALGCEIQRRSVFARKNYFYPDLPKGYQISQYELPICSGGGVDIAVGGEARRIRLTRIHMEEDAGKNVHDVTAAGSGVDLNRAGVPLLEIVSEPDLRSIDEAIAYLKSLRAILMALGVNDGNLQEGSFRCDANVSVMPRGATRLGTRCELKNMNSFRFLRQAIDYEVRRQVELIESGGKVDQETRLFDPDRGETRSMRSKEEAHDYRYFPEPDLPPVLVDEALVERIRRELPELPRARSARYQRDLGLSAQDAELLVSDKGIGDFFDATLAAYGASPDAAKRIANLLNGDVARLANELSLEPAAWRIAPAQLAAILRLQDAQTIGGPGAKQVVEEVFRSGAEPAEVVREKGLAQVSDEGALEAAVDRVLAASAGEVERYRGGNKKLLGFFVGQVMKETRGKGNPAVVNALLKRKLGG", "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": "MAEEKSTLGKIFTDWQVLIVLVLVILSVLSIYAIPPALDKGISGNLQLGLDLVGGSWIQLSFKSEVIGYESDMSQSDFITQLSEKLDADVIPVTSSSVEIREYYTKEELESVLAGMGAKLVTYEQGISKETADTVKGILEDKVNTLGTKDVQINTLTGANDVTKYVRVELAGTDINTAQEIVSSQGKFEIRIVTSGNETERVLSGDAVTSVSTPSQRNNYWGVGFTLSAEGAEALRDACIQYGAVTDPDSHNLVMLLDGEQVYSAPLSSDLAAKLSKGPVNDLSASTGYGEEGYNDAEVLEIHLRAGALPVDVEIAGSSSVTAERGEFIQIVCIAAAILGLLAVAFMVYYRYREPSIVVPMILVNLSEIIILLGIARYIQQLDLASIAGLIAVIGTGIDQLVVITDEVLHEGRVPSPSLYLKRFKRALGIITVSASTTIFAMLPLALMDLSTLKGFAIITILGVLIGVIFTRPAYGKIIMAILSKKPAK", "text": "FUNCTION: Involved in protein export. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily."}
{"protein": "MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKEVSIDMPEGRIHEVLDPEYQLKKSRRKKHKKKSPCTEDVGEPSKNREKKATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRNNEILPQEQNHQKTGQSLRNTEGELDLPADAIVIHLPRSIANWGRDTPDKVNQPWHNADRLLTSQDLVNTGQLCRQEGRRRSKKGKNKNKQGQKLLLVR", "text": "FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. SUBCELLULAR LOCATION: Nucleus Endoplasmic reticulum. SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily."}
{"protein": "MSTRRIFGLETEYGITCAAPPGQQGLSADEVARYLFRKVVAWGRSSNVFLRNGSRLYLDVGSHPEYATAECDDIRQLITYDRGGERILEGLVADAQQRLELEGVPGTIHLFKNNTDSAGNSYGCHENYLVRRQGDFTRLADILVPFLITRQVLTGAGKILTTPAGATFCLSQRADHIWESVSSATTRSRPIINTRDEPHADAELYRRLHVIVGDSSMAEPTAMLKVGATDMVLRMIEAGVPMRDMALENPMRAIREISHDMTGKAPITLASGRTVTAVDLQQEYLVKVRDFVESTGEVSDTDRKVFDLWERGLLALQSGDLTSVERELDWVIKHRLVRRYQEKHSLELSDPRIARLDLAYHDISRTEGLYNLLAARGLVERVTSDVEVLESTAVPPQTTRARLRGEFVRRAQEAKRDYTVDWVHLKLNDQAQRTVLCKDPFQSVDERVDRLIESM", "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": "MARKQVSRKRRVKKNIENGVAHIRSTFNNTIVTITDEFGNALSWSSAGALGFRGSRKSTPFAAQMASETASKAAMEHGLKTVEVTVKGPGQGREAAIRALQSAGLEITAIKDVTPVPHNGCRPPKRRRV", "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": "MITLKEALKYSKEELENLKKELNEKAKKEKKIGAYIEQFLDKDLSVSGEGVPVAIKDNISVKGWELTSASKILQGYIAPYDASVIVNLKANGFSPFGRCNMDEFAMGSSTASSYYGKTLNPLNFERVPGGSSGGSAAAVAGGLALASLGSDTGGSVRQPAAFCGCVGFKPSYGRVSRYGLASYSSSLDQIGVLTQNVEDAAILYDAIAGYDKMDSTSANIEFIKTAPNLNANKKLKIAVIENYVNDADSEVKNALLKTIDMLKANGHEIVYKNLLDSKFDIAAYYIIATAEASTNLSRYDGVRYGKRSENIQNLKEMYVNTRSEGFGEEVKRRILLGTFVLSSGYYDAYYIKAQKARAFIKAKYEEILQDCDLIFMPVTPTTAFKFDTQKSPIQTYLEDVYTISVNLAGLGGISVPVAKDKEGLNISAQLICKAYDEQTLLDGALSLEQMIKN", "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": "MKHFFRLPTAFRPISRVSLRYSSTDTAQPKISKLKISFNKISESNSEKKDNLGSIDTRNCLSTQQDDKLSSTEPSKASLPPSLQYVRDLMDLYKDHVVLTQMGSFYELYFEQAIRYAPELNISLTNRAYSHGKVPFAGFPVHQLSRHLKMLVNNCGYSVTIAEQFKKKDVADNEANKFYRRVTRIVTPGTFIDEAFENLRENTYLLNIEFPENCMSQVADTSLKVGICWCDVSTGEIFVQQVYLRDLVSAITRIQPKEILLDERLLEFHIESGTWYPELVELKKFFIKYQKMPSQHRTIESFYGLFNLGGKEATERQLKIQFQTFTQKELAALRNTLIYVSNHLPDFSINFQIPQRQLATAIMQIDSRTSTALELHSTVRDNNKKGSLLSSIRRTVTPSGTRLLSQWLSGPSLDLKEIKKRQKIVAFFKDNRDITETLRTMLKKVNDLSRILQKFSFGRGEALELIQMARSLEVSREIRKYLLNNTSLMKATLKSQITQLTESLNFEKNLIDDILKFLNEEELAKSQDAKQNADVTRMLDIDVKDKKESNKDEIFELRDFIVNPSFNTKLRKLHDTYQGVWQKKTEYNALLKGFFVGDLGAKTFTLKERQNGEYALHVTGTASSLKKIDELISKSTEYHGSCFHILQKSSQTRWLSHKIWTDLGHELELLNLKIRNEEANIIDLFKRKFIDRSNEVRQVATTLGYLDTLSSFAVLANERNLVCPKVDESNKLEVVNGRHLMVEEGLSARSLETFTANNCELAKDNLWVITGPNMGGKSTFLRQNAIIVILAQIGCFVPCSKARVGIVDKLFSRVGSADDLYNEMSTFMVEMIETSFILQGATERSLAILDEIGRGTSGKEGISIAYATLKYLLENNQCRTLFATHFGQELKQIIDNKCSKGMSEKVKFYQSGITDLGGNNFCYNHKLKPGICTKSDAIRVAELAGFPMEALKEAREILG", "text": "FUNCTION: Important for mitochondrial DNA (mtDNA) stability and repair. Recognizes and binds to base-base and small insertion-deletion mismatches in mtDNA. ATP binding and hydrolysis is crucial for function. Binding to a mismatched base pair attenuates ATP hydrolysis. Also involved in proper sorting of mtDNA during mtDNA transmission. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the DNA mismatch repair MutS family."}
{"protein": "MSDHLSIALKRLDPDLPVPQRAHPGDAGVDLCSTSDVTIEPGHRTLVGTGIAIALPVGTVGLIHPRSGLAAKSGLSIVNAPGTVDAGYRGELKVCLINLDPATAIDIRRGDRIAQLVVQRVELPVFEEVESLDDTTRGTGGYGSSGGHAILDTDAPGAVVGEGV", "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": "MLSEDEAKDLLSFLTLEMRADVKGQATGYILGLTGNRDGCRYLQSKPDFLKALVTLTSDPSIAIVKDCFHALINLSADETLHQPLVKETEILSKLIPKLQDPEFVFSDRICTILSNLSRHEQTCRDVFKALQELNVGLDRLVEIFCTEGFNKKASLHYLAPLLSNLTQLPEARHFILDKDRCVIQRLLPFTQYEESITRRGGVVGTLRNCCFDYVHHEWLLSDAVDILPFLLLPLAGPEELSEEENEGLPVDLQYLPEDKRREEDPDIRKMLLETLMLLTATKVGRQILKSKNVYPIMREFHKWEKDPHVISACEKLVQALIGDEPEVGMENLMEVEIPKDVEEKLQELDAKEQEQMEKDKQELEKSQNESPEGLER", "text": "SIMILARITY: Belongs to the HGH1 family."}
{"protein": "MLYSLFKKYLFRLDAEEVHEKVCKILKILSRSPFFCNLIHAQFGYTNPKLENEILGLHFPNPLGLAAGFDKNASMIRALTAFGFGYLEAGTLTNTAQSGNEKPRLFRHIEEESLQNAMGFNNYGAVLGVRAFERFAPYKTPIGINLGKNKHIEQDNALEDYKAVLIKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVSELFCMAKEMTKKPLFLKIAPDLEIDAMLEITNSAIEAGANGIIATNTTIDKSLVFAPKETGGLSGKCLTQKSREIFKELAKAFFNKTILVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGPNLCQNILKDLVKLLQKDGFLSVKEVIGADLR", "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": "MAKNYYDITLALSGICQSARLVQQLAHQGHCDADALHVSLNSVIDMNPSSTLGVFGGSEANLRLGLETLLGVLNASSRQGLNAELTRYTLSLMVLERKLSSAKGALNTLGDRINGLQRQLDHFDLQSDTLMSAMAGIYVDVISPLGPRIQVTGSPAVLQSPQVQAKVRASLLAGIRAAVLWHQVGGGRLQLMFSRHRLTTQAKQILAYLTPEL", "text": "SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the HflD family."}
{"protein": "MDKVCAVFGGSRGIGRAVARLMAQRGYRLAIVARNLEGARAAAGDLGGDHLALSCDVAKEHDVQNTFEEIEKNLGRVNFLVNAAGINRDNLLVRTNTEDMLSQLHTNLLGSMLTCRAALKTMIKQQRGSIVNVGSVVGLKGNSGQSVYSASKGGLVGFSRALAKEVAKKKIRVNVVAPGFIHTDMTKDLNEELLKKNIPLGRFGDALDVAQAAVFLLESPYVTGHVLVVDGGLQLTM", "text": "FUNCTION: Component of the heterotetramer complex KAR (3-ketoacyl-[acyl carrier protein] reductase or 3-ketoacyl-[ACP] reductase) that forms part of the mitochondrial fatty acid synthase (mtFAS). Beta-subunit of the KAR heterotetramer complex, responsible for the 3-ketoacyl-ACP reductase activity of the mtFAS, reduces 3-oxoacyl-[ACP] to (3R)- hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length preference, thereby participating in mitochondrial fatty acid biosynthesis. The homotetramer has NADPH-dependent quinone reductase activity (in vitro), hence could play a role in protection against cytotoxicity of exogenous quinones. As a heterotetramer, it can also reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o- quinones and p-quinones (in vitro). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MGGSDSDSRSRSRNREENKSRSLSSSSARRPSPNHEKKHEHSSEKKKMKRRRSSSSSSSSSSPSPSREKKAKKKKKRREAKKLKREKKKEKKEKKRQKKLALKAERAAALTASVPAPVPEEKPQTYLKTWQSEETKEHGPAMTDEQKAKLSTRRPLTKEEYEARQSVIRRVLDPETGRTRLIRGDGEILEEIVSKERHKDINKQSTRGDGDAFQKRLGISR", "text": "FUNCTION: May be involved in modulating alternative pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus speckle. SIMILARITY: Belongs to the ARL6IP4 family."}
{"protein": "MTRPIVADISAAALRHNVAVVREHAPRARIMAAVKANAYGHGVTLCAPVLAEAGVDAFAVASLEEAEALHALGLERPICLLGGPFDADEVSVAAERAYLLVIHEQRQLQWLETRAADAALRLFIKVDTGMHRLGFAPERLPALFAALQRHPRWEVLGLMSHLARSDTPDDPFNRQQAGVFADAIAHVGHVTAGQHSLANSGGVLALPFTHQYWVRPGLMLYGLSPFAGRRGSEIGLQPVLSWRSAVVAIRELGPGDWLGYGAAWQAPARCRVGVVAAGYGDGYPRHLGCGAPVTVAGQTTRTLARVSMDMLFVDLTAVEADIGAPVVLMGAGGPPLESLAAELGTISYEMSCRMQMRVPRRLVS", "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": "MATFSYFQNYPHSLLDPLLFPTPHSSINLTSFIDQNHLYPLPNISTVEDISFLEYNVDKTENSGSEKLANTTKTATTGSSSCDQLSHGPSAITNTGKTRGRKARNSNNSKEGVEGRKSKKQKRGSKEEPPTDYIHVRARRGQATDSHSLAERVRREKISERMRTLQNLVPGCDKVTGKALMLDEIINYVQTLQTQVEFLSMKLTSISPVVYDFGSDLDGLILQSEMGSPEVGTSFTNAMPTTTPIFPSLLDNSVVPTHAQVQEEGEERENFVDRSGFNNNNFCSFP", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAPPQGKPENVLRLADELIALDQHSSALQSLHETIVLKRSRNAQGFSLEPIMMRFIELCVHLRKGKIAKEGLYTYKNAVQNTSVTAIENVVKHFIELANKRVQEAQEKADKISVEYVDDLEATETPESIMMSLVSGDLSKSRTDRALVTPWLKFLWDAYRTVLDILRNNARLEVMYQLIANSAFQFCLKYQRKTEFRRLCELLRSHLGNASKFSNAPHSINLNDAETMQRHLDMRFSQLNVAVELELWQEAFRSIEDIHSLLTFSKRAPAAVMLGNYYRKLIKIFLVCDNYLLHAAAWNRYFTFTNVQKPATANFVILSALSIPIIDANKLSGPSIEAEDAKSKNARLALLLNLSKTPTRETLIKDAISRGVLSFCDQAIRDLYQILEVEFHPLSICKKLQPIIKRLAESNDTAQYIRPLQQVILTRLFQQLSQVYDSISLKYVMDLATFEEPYDFNPGQIEKFIMNGNKKGAFSIRLNHIENSISFSSDLFSNPIKSSDSVSLQSTPSELITSQLTRIAKSLSSVLMRFDTDFCLLRKQQAEAAYERAQAGVEQERKAVIAQRSLLELRRGQADTLATQREAELAAQRALKQKQESEAESLRVQEEINKRNAERIRREKEAIRINEAKKLAEELKAKGGLEVNAEDLEHLDADKLRAMQIEQVEKQNKSMNERLRVIGKRIDHLERAYRREAIPLWEEDAKQQAEHDREIFYEREKQRKEVQERKHEQAIKDKKAFAQFASYIHAYKQNIDDERDKAYQEAYAKAKNVIDAERERQRKEIFEQKLAEAIREAEEEAARAAEEEANRELHEQEEAQKRAIEERTRAAREAKEREQREMAEKLERQRRIQQERDEEISRKLAEKAAARRANIGASSPSPGAWRRGGASAGGVSRDSPRYSRGGYSRGSVPPRETLAPSKGAYVPPSRRNQQQQ", "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": "MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNGKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITENNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA", "text": "FUNCTION: Promotes bacterial attachment to multiple substrates, such as fibronectin (Fn), fibrinogen (Fg), elastin peptides and tropoelastin. This confers to S.aureus the ability to invade endothelial cells. Promotes adherence to and aggregation of activated platelets (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor Note=Anchored to the cell wall by sortase A (By similarity)."}
{"protein": "MGLLSKKLLVASMVAAVLAVAAVELCSAIPMEDKDLESEEALWDLYERWQSAHRVRRHHAEKHRRFGTFKSNAHFIHSHNKRGDHPYRLHLNRFGDMDQAEFRATFVGDLRRDTPAKPPSVPGFMYAALNVSDLPPSVDWRQKGAVTGVKDQGKCGSCWAFSTVVSVEGINAIRTGSLVSLSEQELIDCDTADNDGCQGGLMDNAFEYIKNNGGLITEAAYPYRAARGTCNVARAAQNSPVVVHIDGHQDVPANSEEDLARAVANQPVSVAVEASGKAFMFYSEGVFTGDCGTELDHGVAVVGYGVAEDGKAYWTVKNSWGPSWGEQGYIRVEKDSGASGGLCGIAMEASYPVKTYNKPMPRRALGAWESQ", "text": "SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MNRSVHPMKVIYPGTFDPVTNGHLNLIERTHEMFDEVVIGVAASPSKNTMFTLEERVALMEEVVAHLPGVTVKGFSGLLVDFARQEQAKVLIRGLRTTVDFEYEFGLTNMYRKLLPGIESVFLTPEEEFAFLSSTIVREVAIHGGSIEQFVPAAVANAIEKKVNERQ", "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": "MPYIVDVYAREVLDSRGNPTVEVEVYTETGAFGRALVPSGASTGEYEAVELRDGDKDRYLGKGVLTAVNNVNEIISPELLGFDVTEQNAIDQLLIELDGTENKGKLGANAILGVSMACARAAADFLQIPLYQYLGGFNSKTLPVPMMNIVNGGEHADNNVDIQEFMIMPVGAPNFREALRMGAQIFHSLKSVLSAKGMNTAVGDEGGFAPNLGSNEEALQTIVEAIEKAGFKPGEEVKLAMDAASSEFYNKEDGKYHLSGEGVVKTSAEMVDWYEEMVSKYPIISIEDGLDENDWEGHKLLTERLGKKVQLVGDDLFVTNTKKLAEGIKNGVGNSILIKVNQIGTLTETFDAIEMAKRAGYTAVISHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDQLAETAQYHGINSFYNLNK", "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": "MFQSCLPGALRSWSRGVFSTSTRPRLVLGIETSCDETGAAVLDETGRILGESLHSQKETHLKTGGIIPLVAQRLHRENISRVVQEALNRSAIEPSELTAVATTVKPGLALSLGIGLDYSLKFVRQHQKPFIPIHHMEAHALTVRMLHPLDFPFLVLLVSGGHSLLALAKGIDEFLLLGQTLDEAAGDTLDKIARRLSLRNHPECGTLSGGQAIERLAKEGDRLAFHFISPMGQNYDCNFSFAGLRTQITGAINKKEKEEGVEAGQFLSCVKDIAAASQHTVASHLAKRTHRAILFCKSKGLLPEQNPTLIVSGGVASNEYIRQILKIITDATGLHLLCPPSKFCTDNGVMIAWNGIERLKQGKGILSYSEEVSYEPKAPLGLDITSEVKEAAIKVPKLKLRTNS", "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": "MGNTAIAKKGSEVESVKEFLAKAKEDFLRKWENPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIRVSITEKCGKEFCEF", "text": "FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux (PubMed:9368018). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA (By similarity). FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA. FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, and differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Membrane; Lipid-anchor Nucleus Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily."}
{"protein": "MSHLPLHHPAAVVTLRPLRPRAAVATRLRRHRLAGGPTRRLRRRPAVTRRRRPDRRFVRCRPSPTRRGLPGCWRHSSTGPHT", "text": "SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSQRPLDVLNEALNSPVIVRLKGGREFRGELQGYDMHMNLVLDNAEELKENEASRKLGTIIVRGDTVVYVSP", "text": "SIMILARITY: Belongs to the snRNP Sm proteins family."}
{"protein": "MAPKKDAKKPEPPKKAEPAPAPAPAPEPPKADAVDLSGVKLDFTQDQMEDYREAFLLFDRVGDSKVAYNQIADIMRALGQNPTNKEVTKILGNPTADDMVNKRVDFEGFLPMLQVVINNPNKATYDDYVEGLRVFDKEGNGTVMGAELRIVLSTLGEKMSEAEIDALMQGQEDENGCVNYEAFVKHIMSV", "text": "FUNCTION: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function."}
{"protein": "MTLVDKFVTHVISESSFEEMDRIYLTNRVLSRVGEGVLEVETNLDKLIDLKDQLVEETVRLETIEDSQTAREILGTELMDLVTPCPSQVNRDFWEAYAYSPEQAIEDFYQLSQKNDYIKLKAIAKNIAYRVPSDYGELEITINLSKPEKDPKEIAVAKLVQASNYPQCQLCLENEGYHGRVNHPARSNHRIIRFEMVGQEWGFQYSPYAYFNEHCIFLDGQHRPMAISRQSFERLLAIVEQFPGYFAGSNADLPIVGGSILTHDHYQGGRHVFPMELAPLQKTFRFAGFEQVKAGIIKWPMSVLRLTSDSKEDLINLADKIFQEWRQYSDSSVQILAETDGTPHHTITPIARKRDGQFELDLVLRDNQTSAEHPDGIYHPHKDVQHIKKENIGLIEVMGLAILPPRLKEEVEQVASYLVGEAVTVADYHQEWADQLKSQHPDLTDKEKALAIVKDSVGAIFVRVLEDAGVYKQTEQGQTAFMRFVEQVGILLD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 2 family."}
{"protein": "MLFQLNIVFKELKNPDFFFFFFFFSLPLSSFKLNLSSSSSFKLWLIVFLLDFGEIMFPAPPLPIANFSGALLPLSLFLGFLDVDLIAAKALPLEVTTNRLSSFALIVSSSSILPPRISSSSFPPLLATFFLLKKMFPAPPLPTTIGALLFGDEVVACKD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MIPVLLVTICLAVFPFQGSSIILESGNINDYEIVYPKKVAVLPTGAMNSAHPCYDPVTCQPKEKEDCESGPCCDNCKFLKEGTICKMARGDNMHDYCNGKTCDCPRNPYKGEHDPMEWPAPAKGSVLM", "text": "FUNCTION: The disintegrin ocellatusin-10c1 is a 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-2b/beta-3 (ITGA2B/ITGB3) is low, and there is no inhibition on alpha-1/beta-1 (ITGA1/ITGB1), alpha-2/beta-1 (ITGA2/ITGB1) and alpha-6/beta-1 (ITGA6/ITGB1) (By similarity). FUNCTION: The short monomeric disintegrin ocellatusin inhibits ADP- induced platelet aggregation (IC(50)=168 nM). Inhibits alpha-5/beta-1 (ITGA5/ITGB1) integrin and induces the expression of a ligand-induced binding site epitope on beta-1 integrin subunit. Has a direct chemotactic stimulus on human neutrophils in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the disintegrin family. Short disintegrin subfamily."}
{"protein": "MDMQSRIRQLFQASIDTKQQAMDVLAPHIEQASQVMVNALLNEGKMLSCGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPANVTARIQEVHLLAIHCLCDLIDSQLFGSEE", "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": "MMMNKSKTDWAKDTPCKNITIYGYCKYENDGCIFNHGKPLSTSSNTGGAAAGSAEDSAASGGVTVGNTGKSTFNAKTATSFTPSVAIPDFNNIPSFTPERIVSSPAGDGATAFTPSFNPYGSDSFNPSANVSGPGSAVFAAASGNAGASATAAPRSQSVHVGTGGYLPLAGTAFPTVYPPSHSILQYHLYAPDPPPHLQVPLKANERTPETLFIPNNLREHLLKRNLSALQVFPSDGNLPDIVGDYFGLVPLEFHNRQTGKGRYLGHQNSLYKVFSNFDGKVYIIRRIHDVKTTDVGQISLPFRKWQKVSCPNVVKVKDAFTTLAFGDSSLCVVHDYYPQSNSLYETHVANYTVVPVTQKYLWSYLVQLSNALNEVHRHGLSMNNISLDKVIVTGDPGRIKVGDSAVHDILAFDEGRDIAKEQQADYSAVGALLMDLAQRMLGTRDQPLDSMDIDPLFKRVLAYLLSDEKKTIAEFTALFSHKMLDIISSSQTYSEYIEQHLSRELENGRLFRLMCKLNFIFGRMESSMDIHWSEAGDKFPIILFYDYVFHQVDENGKSVMDLTHVLRCLNKLDTGVSEKIILVTPDEMNCIIISYKELKDSIDSTFRSMTQ", "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": "MNINPFANVSLQDYLEIVQIVDSTFPIGSFNHSFGMENYLREDTVTDDKGYEEWQEAYLASQFKYGEGLVIKLVYDAMATDNLEQVWHYDKVLTVSTQARETRQGTKMIAKQMLRLIQRLHAIPVLDDYQSKIRKGEVFGNPAIVFALYVFNKGLGCSEAIALYGYSVISTMVQNAVRAIPLGQFAGQEIVLRSFSQLEKMTQEIQELDASYLGANTPGLELAQMKHETQVFRLFMS", "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": "MSMQSHHVHLVSDATGETVSNVVRACLAQFEDVRVVQHRWWLLRSPSQVGRVIEGIQRDPGTVVFTVVDPEIRRALEEACRLINIPCVALLDPVMDALALVLETKGNQQPGRQYTLDEGYFSRIEAMHFALALDDGQSLDRLKQAEVVVVGVSRTSKTPTCMFLANKGIRAANVPLVPGIDPPAELMDLAGPLVVGLTRDPKSLSDMRRSRLRLMREDGDSPYAEEDSVAREVREARRLYARMGWTVIDVTRKSIEEVAATIMQKLGTAPWGEGL", "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": "KRGFLDVVKHIGKAALGAVTHLINQGEQ", "text": "FUNCTION: Has antimicrobial activity against Gram-negative bacterium E.coli (MIC=13.32 uM), aginst Gram-positive bacterium S.aureus (MIC=13.32 uM) and against fungus C.albicans (MIC=13.32 uM). At higher concentrations also has a bactericidal and fungicidal effect. Has hemagglutinating activity against horse erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Cruzioseptin subfamily."}
{"protein": "MADIKSRHFPRSANKRGAARLAAVQALYQMDIVGSGVMETAAEYEAYRLGKDIDGDQYLDADFQWFLAIITGVVQDQKQLDPLLHQQLSAEWSLSRLDSILRAILRAALWELINRKDVPVAVVVNEYVDIAKAFFEGDEPKLVNAVLDSMAKKIRL", "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": "MGAYKYMQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGATYGKPVHHGVNQIKFARSLQSVAEERAGRHCGGLRVLSSYWVGEDSTYKFFEVVLVDTFHKAIRRNPDTQWITKAVHKHREMRGLTSAGKKSRGLGKGHKFHLTIGGSRRAAWKRRNTLQLHRYR", "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": "MTLSAYLALALILFCIGLYGALTKRNTVIVLICIELMLNAVNINFVAFAKYGAHPGVHGHVFALFAIAIAAAEAAVGLAALIAFYRNRKTVQVDEANSLKH", "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": "MSDRIDRDVINALIAGHFADPFSVLGMHQTTAGLEVRALLPDATEVWVIEPKTGRKVGKLECIDSRGFFSGVLPRRKNFFRYQLAVVWHGQQNLIDDPYRFGPLIQEMDAWLLSEGTHLRPYETLGAHADTMDGVTGTRFSVWAPNAQRVSVVGQFNYWDGRRHPMRLRKESGIWELFIPGAQHGQLYKFEMIDAHGKLRIKADPYAFEAQMRPETASLICGLPEKVVQTEERKQANRFDAPVSIYEVHLGSWRRHTDNNFWLSYRELADQLIPYVKWMGFTHLELLPVNEHPFDGSWGYQPTGLYAPTRRFGTRDDFRYFINAAHQAGLNVILDWVPGHFPSDDFGLADFDGTKLYEHSDPREGYHQDWNTLIYNYGRREVSNYLVGNALYWIERFGIDALRVDAVASMIYRDYSRKEGEWIPNEFGGRENLEAIEFLRNTNRILGEQVSGAVSMAEESTDFAGVSRPQDMGGLGFWYKWNLGWMHDTLDYMKLDPVHRQYHHDKLTFGMLYNYTENFVLPLSHDEVVHGKKSILDRMPGDAWQKFANLRAYYGWMWAFPGKKLLFMGNEFAQGREWNHDASLDWHLLEGGDNWHHGVQRLVRDLNHTYRHHKALHELDFDAYGFEWLVVDDNERSVLIFVRRDKVGNEIIVASNFTPVPRHDYRFGINQPGKWREIVNTDSMHYHGSNTGNGGVVHSDEIASHGRQHSLSLTLPPLATIWLVREGE", "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": "MKESRNLENFVEKKLYECKKKYVDIPKDEGQRYGGKHYEALTSKIFEILRKENPELDIIIAEFSLEGSVGMLKIAKPNEFDLVFKLKFPYYKSIAVTRDPKIPGNVLLDMTRVLELLKDDPREDFQRIRELIQGRLVDAQNFFVVDRLRSWLQSLFSQALNRISYRVELVAGVVSHLKYRTCGPAHTIYVYGDYEYSVDYVPAICLAAEQNVLPTKQLECFKRANTSYWEAIPKPLKPLTETSMISFRSSFYAVEKILLQDVHENCRNAIRFMKKFRDVKTNLGNCKSYYIKTLFLWKIIQEPESYWLNPLSFILADMFDDLAENLRRGVITFFWDPELNMIDALTRDQVWEMYLCVQRIPRDLRGAEISRNKWSFFVLREFSHKKERNVNLKCSSRRKRNVIKGLKTTSICKLRNARTNGTWTAGLWTRPGHAYRGPSETVSTWDTVKDAAWSEGIVE", "text": "FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP from ATP and GTP and plays a key role in antiviral innate immunity (PubMed:34261128). Directly binds some unknown nucleic acid, activating the nucleotidyltransferase activity, leading to synthesis of both 3',2'-cGAMP and 2',3'-cGAMP second messengers (PubMed:34261128). 3',2'-cGAMP and 2',3'-cGAMP bind to and activate Sting, thereby triggering the antiviral immune response via activation of the NF- kappa-B transcription factor Rel (Relish) (PubMed:34261128). SIMILARITY: Belongs to the mab-21 family."}
{"protein": "MADGTHSTHRNPSTAQLIELALSRGEGELTANGALVAKTGERTGRSPNDRFIVKEPGSEADIDWGTVNKPFEQTVFTALWNRVESYLGDKELFVSDLEVGADPEHYQPVRVTTETAWHQLFARNLFIVPEQFNAADKPIWQIMNAPGFECIPERDGTHSDATVIINFAERKVLLAGLKYAGEMKKSMFSVQNFLLPAKGVLPMHCSANVGIKGDTTLFFGLSGTGKTTLSADPKRFLIGDDEHGWAPGGVFNIEGGCYAKCIDLSQKNEPVIWNAIRFGTVLENVTMDENRVPDYTDSTLTENSRAAYPLEHIELRKEENLGAEPHAVVFLTCDVSGVLPPVSILTKEQAAYHFLSGYTAKVGSTEMGSSSAIQSTFSTCFGAPFFPRPAGVYAELLMKRIESFGSQVYLVNTGWTGGPHGIGKRFDIPTTRAIVDAIVNDDLKGVETEHLAKLNLNVPLAIPGVETKLLNPVNTWEDKAKYAEYAQQLAESFTENFAKYQVPDSIKNAGPNA", "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": "MEKRTTYCGNVSAEFIEKEVVLKGWVQKRRDLGGVIFIDLRDREGIVQVVFNPEKSKEAWEIADKCRSEYVIEVKGQVVYRDKEAINPKMKTGEFEVMATDITILNTAKTTPFTIEDDNNVNDELRMKYRYLDLRRPSMTNNIKLRHQVTKTIRHYLDNHDFLDIETPYLGKSTPEGARDYLVPSRVHAGHFYALPQSPQLFKQLLMGAGFDRYYQIVRCFRDEDLRGDRQPEFTQIDIETTFLTPEEIQTYTENMLAEVMKETKGIEISVPFPRMSYDEAMARYGSDKPDTRFAMELIDVAEVVKDVDFKVFQAALENGGHVKALNAKGAADKYSRKDMDNLGKYVSQFGAKGLAWLKVEEDGLKGPIAKFLTEVSDELIAATNAEVGDILMFGADKPEIVAAALGAVRTRLGKELGLIDESKFNFLWIVDWPLFEYDEEAGRYVSAHHPFTQPKAEDVDRLATDPASVYAEAYDVVLNGYELGGGSLRIHTRELQEKMFETLGFTKEEAQDQFGFLLDALDYGFPPHGGIALGLDRLAMLLAGEENIREVIAFPKNGKAIDPMNNAPSLVSPLQLFELNIDVTAIDE", "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": "MHAPQPITAATGEAGEDRALRYLQARGLAVVSRNYRCKGGEIDLVMRDAAGALVFVEVRARVARSTQRFGGAAASVTPAKQRRLIAAAEDFLARQVEDVPACRFDVIAIDGARIEWMRDAFGVDA", "text": "SIMILARITY: Belongs to the UPF0102 family."}
{"protein": "VHLTADEKTAVTTLWGKVNVEEVGGEALGRLLVVYPWTQRFFESFGDLSSADAIMGNPKVKAHGKKVLNSFSEGLKNLDNLKGTFAKLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
{"protein": "MLVIPAIDLYRKKVVRMVKGKKENTIFYEKDPIELVEKLVEEGFSLIHVVDLSRAIEESDENLPVLEKLSSYADHIQIGGGIRILEYAKKLLGMGFRRQIVSSKVLEDPSFLKKLKEIGVNPVFSLDTREGKVAFKGWLDEKDIDPVFLVNRLKEFGLEEIVHTEIEKDGTLKEHDFSLTERIALETGVKVIAAGGISSERSLEEALEVHRRTNGLLKGVIVGRAFLEGTLTVEVMKRYACQENNSVS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MLHVNFTEEESLNTQALIVFIDDKLKLDSELINLDQQHHGLISKTIANKLQFTGKYGQIKIIPSVVKSGEVKYLVLAGLGSEEKLTEVKIEELGGKILQNVTNAKIATIGLKIKNRISNFTSSHVASLIASGALLASYRFDKYRTTLKEADKFVVESFEISTDNNAEATKLFEVKKLIAEGVFFTRDISNEPSNIKTPQIYAERIADILEELNVDVSILGEREMKNLGMGALLGVGQGSQNESKLVVMEYQGTNKDAPYIALVGKGVIFDTGGISLKPSNNMHLMRYDMCGSAAVVGTMIAVASQELPVNIVGVVGLVENMPSGNAQRPGDVVTTMSGQTAEVLNTDAEGRLVLADAVWYAQEKFKPKCVIDVATLTGAIVVSLGPTYAGCFSNNDELADKLIKAGEEVNEKLWRMPLHEDYDAMINSDIADMANIGNVPGAAGSSTAAHFIKRFIQEGVEWAHLDIAGVANSNKPSSLGPKGAVGYGVRLLEKFIKENYEQ", "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": "MANEDCPKAADSPFSSDKHAQLILAQINKMRNGQHFCDVQLQVGQESFKAHRLVLAASSPYFAALFTGGMKESSKDVVPILGIEAGIFQILLDFIYTGIVNIGVNNVQELIIAADMLQLTEVVHLCCEFLKGQIDPLNCIGIFQFSEQIACHDLLEFSENYIHVHFLEVHSGEEFLALTKDQLIKILRSEELSIEDEYQVFLAAMQWILKDLGKRRKHVVEVLDPIRFPLLPPQRLLKYIEGVSDFNLRVALQTLLKEYCEVCKSPKENKFCSFLQTSKVRPRKKARKYLYAVGGYTRLQGGRWSDSRALSCVERFDTFSQYWTTVSSLHQARSGLGVTVLGGMVYAIGGEKDSMIFDCTECYDPVTKQWTTVASMNHPRCGLGVCVCYGAIYALGGWVGAEIGNTIERFDPDENKWEVVGNMAVSRYYFGCCEMQGLIYVIGGISNEGIELRSFEVYDPLSKRWSPLPPMGTRRAYLGVAALNDCIYSVGGWNETQDALHTVEKYSFEEEKWVEVASMKVPRAGMCVVAVNGLLYVSGGRSSSHDFLAPGTLDSVEVYNPHSDTWTEIGNMITSRCEGGVAVL", "text": "FUNCTION: May play a role in organizing the actin cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton."}
{"protein": "MSDQQLDQHELQQEENKLIAQRKEKLAAVREARAIAFPNDFRRDAYFADLQKQYADKTKEELEAAAIPVKVAGRIMLNRGSFIVLQDSSERLQVYVNRKTLPEETLAEIKTWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRYVDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQAVLGSTDVPYGDKVFHFGEPFVRLSVYDSILKYNPQITPADLNDVEKARAIARKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSVTDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFPHMRPQA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MRYKITVEYNGSNFSGWQKQQHSANSIQEKIENAIFNFSGEKVTLYCGGRTDAGVHALGQVAHFDMEKEFELYRIRNAINYHLKSIPIVVLNAEVVDDAFHARFSAKKRYYEYRIVNRYAPAALETGYVWQVFSPLDVNIMREAAKHLLGKHDLSSFRSKDCQAANPIRTIDDIDIIQNGNHIHIKISAISFLHNQVRIIVGTLVEFGKNRTNPQEMLNILNQCKRSAAGVTAPPFGLYLVKIDY", "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": "MPTINQLVRKPRKTPARINRVPALNKNPLKRGICSKVYTTTPKKPNSALRKVARVRLSGGAEVIAYIPGEGHNLQEHSVVCIRGGRVKDLPGVRYHIVRGVFDTEGVKGRKKGRSKYGAKKS", "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": "MTLKVAINGFGRIGRSVLRALYESGKHHHINVVAVNELAEPEAMAHLLQYDSSHGRFFKPVSHDQEHLFIAHENGERDDIRILHQSDITLLPWHDLDVDIVLDCTGVYGSREDGLAHIKAGAKKVLFSHPAANDIDNTIIYGVNHKTLTSEHRIVSNGSCTTNCIVPVIKIIDDAFGIESGTITTIHSAMNDQQVIDGYHSDLRRTRAASQSIIPVDTKLHLGIGRIFPKFVDKFEAISVRVPTINVTAMDLSVTVKTNVKVNDVNQALSEVSRCTLEGIVDYTEAPLVSIDFNHDPHSAIVDGTQTRVSNKHLIKLLVWCDNEWGFANRMLDTALAMHASDAAQHSNKELRSKIAIKNS", "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": "MSKAREIRTKIASIKNTQKITRAMELVAASKMRKAQDRMAMSRPYASKIRKVISHVAASHAEYPHPYLQQRENIKRVGYIIVTTDRGLCGGLNVNLFRTAIADMKKWQADNIGMDLCVIGRKGEAFFRRYGGNVLAVADHLGDAPEVQDIIGIVKVMLDQYDKQQIDAIYIATNEFVNTMVQKPLVRQLLPLKTDEEEVEGGYWDYIYEPDESKDLLEMLLVRYIESQVYQAVIENIACEQSARMVAMKNATENAGQLIDELRLIYNKARQAGITREIAEIVAGAAAVE", "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": "MADGRPAALDDFCRRFDISFFDLHLTCIFCSHTVDLQDLASFYLKKLSLVFRGGCYYACCSECLRLSARFEQENYFQCSIKAVNLEEVAQRKIKEICIRCICCLRLLDIVEKLDLLYSDQACYLIRGLWRGYCRNCIRKQ", "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": "MPVIKVRENESFDVALRRFKRSCEKAGILAEVRSREFYEKPTTIRKRENATRAKRHAKRVARENARNTRLY", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family. SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
{"protein": "MALRAQFENSNEIGVFSNLTNSYALVALGGSENFYSVFEAELGDVVPVVHTTIGGTRIIGRLTCGNRKGLLVPSSTTDNELQHLRNSLPDPVKIQRVDERLSALGNIVACNDYVALVHPDIERETEEIIADVLDVEVFRQTVAGNVLTGSYCALSNQGALVHPRTSIQEQDELSSLLQVPLVAGTINRGSDVIGAGLVVNDWCAFAGLDTTATELAVCESIFKLQDAQPSAIISNRDTLVESYT", "text": "FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Shuttles between cytoplasm and nucleus/nucleolus. SIMILARITY: Belongs to the eIF-6 family."}
{"protein": "MNIPADLLYTKDHEWIKVLDDGTTALVGITDFAQSELGDIVFVETKPVGTELSEHDVFGTVEAVKTVADLFAPVDGVIVEVNEALDAAEVVNSSPYEDGWMVKVSLKDASQFDALMSAAEYSEMVGE", "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": "MAAFGGPAKPLLSLNPQEDAKFKKEVAQVRRRATKQQEKQKPTPGVIYVGHLPPTLYETQIRAYFSQFGTVTRFRLSRSKKTGNSKGYGFVEFESEDVAKIAAETMNNYLFGERLLKCHFIPPEKVHEELFREWHMPFKRPSYPAVKRYNQNRSLVQKLRMEERFKKKEKLLRKRLAKKGIDYNFPSLVKVLHKNEENASNTGPQNSRKHQALRKKKKAASVTPETPEKAVDSQGPTPVCTPAFLEKRKSEVAKMNDDDKDNEIVFKQPVSGVKEETQETQSPASSKKKRRRKHNQ", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome Note=Localizes to mitotic chromosomes in conjunction with MKI67."}
{"protein": "MSEDRQSRSGDGNKILYCSFCGKSQREVRKLIAGPSVFICDECVELCNDIIREELEEKSQSARSSLPKPKEILEVLDQYVIGQQRAKRTLAVAVYNHYKRIESRHKNDDIELAKSNILLVGPTGSGKTLLAETLARLLNVPFTIADATTLTEAGYVGEDVENIIQKLLHKCDYDVEKAQHGIVYIDEIDKISRKSENPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTKNILFICGGAFAGLDKVIQQRCNEVGGIGFGVKVKSSESKRDVGKVLAGVEPEDLIKFGLIPEFVGRLPVVATLDELDESALVKILTEPKNAITKQFKKLFEMENVELEFRQDALSAVARKALKRKTGARGLRTIVELVLLDTMYELPSQEGISKVVVDESVIENKSEPYLIYQTMPAKVASGE", "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": "MKVLFFTIALSLFSILHADDVAFSAFTPSEGTYYVQVIAVDKEFPEEEIPRDMSPLTIMYLDDGKMEARFTMKKDDNCEEINIMLEKTADPRKITMNRRLRYTCAAVRTSKQKHWILVCPREFQGETIRMAKLVGPNTDKNPKALEDFYRFIYRERFDKRRIITPKQTEACAPEHA", "text": "FUNCTION: Probably serves a role in the transport of a small ligand released during the hydrolysis of milk fat. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MIITIDGPSGTGKSTIAKALAKDLNFNYCNTGAMYRTLAYTYLCEPWKHLAIQELIDNPPFSFSFVSGQPLEAFLEGNLLSVELGTPEVANMASKLSQLPEVRFFMQQLQRKYAELGNCVFEGRDMGSKVFPDADVKIFLTASAEVRALRRLKDLPHNSLSKEAVYAQLIKRDETDSQRSLDPLVIPEGAVVLDSSDLTISQVLEKISALISPKLP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily."}
{"protein": "MSTHDPISDLITRIRNAQMRSKSKVTTPGSKMRASVLEVLKSEGYIRGYATMEHPSGRSEIEIELKYFDGEPVIREIERVSKPGRRVYTSVKNLPRVNNGLGISVLSTPKGIMADHSARDANVGGEVLFTVF", "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": "MARKVEKENGSGPIKSNHDLVRGVWQLFRLHTIEGLSTASIGWLALFFYATQQQLAFDLVRNAFIGIFATYQMTHCVFCLWNDICDRDFDGKVARTRDRPLPSGMVTLTEAMWVFVLGVFASMGVTYWLLGADVTLTMVPIWVLSFIYPLCKRIIWAPQVVLGLTMALCVLPPWVAVRKNSGSAGLLPASLFGAIFCWLVYLDLIYASQDRPDDQKAGVKSLAIFLGDYLKAGLTVLGVLQVVCFVLAASEASAGFLLWVFGIAVWSASVPWSIMSLDTRDRKSGGRIFLVNAILGIYMAAVSGLNVSLAMW", "text": "FUNCTION: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids (PubMed:29797385). The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids (PubMed:29797385). The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (PubMed:29797385). The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA (PubMed:29797385). The terpene cyclase/mutase atnI 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 (PubMed:29797385). The cytochrome P450 monooxygenase atnM is responsible for hydroxylating both C1' and C10' (Probable). The next steps may involve ketoreduction and acetyl transfer by the ketoreductase atnB and the acetyltransferase atnC, and lead to the production of arthripenoid B, the final biosynthetic product of the atn cluster (PubMed:29797385). The hydroquinone moiety in arthripenoid B is prone to undergo spontaneous oxidation to afford a benzoquinone compound, a key intermediate for generating structure diversity (Probable). For instance, addition of a cysteine followed by ring contraction gives arthripenoid A, tautomerization gives the main product arthripenoid C, addition of a molecular of water or amine affords arthripenoid D or E, respectively, and loss of one water forms arthripenoid F (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
{"protein": "MAAVAAPMASKPRGSKAESFVDNKRREDIRFANINSARAVSDAVRTSLGPKGMDKMISTANGEVIITNDGATILNKMEVLQPAAKMLVELSKSQDSAAGDGTTTVVVIAGALLKECQSLLTNGIHPTVISDSLHKACGKAIDILTAMAVPVELTDRDSLVKSASTSLNSKVVSQYSTLLAPLAVDAVLSVIDPEKPEIVDLRDIKIVKKLGGTVDDTHTVKGLVFDKKVSRAAGGPTRVENAKIAVIQFQISPPKTDIEQSIVVSDYTQMDRILKEERNYILGMIKKIKATGCNVLLIQKSILRDAVTDLSLHYLAKAKIMVIKDVERDEIEFVTKTLNCLPIANIEHFRAEKLGHADLVEEASLGDGKILKITGIKDMGRTTSVLVRGSNQLVLDEAERSLHDALCVVRCLVSKRFLIAGGGAPEIELSRQLGAWAKVLHGMEGYCVKSFAEALEVIPYTLAENAGLNPIAIVTELRNKHAQGEINAGINVRKGQITNILEENVVQPLLVSTSAITLATECVRMILKIDDIVTVR", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MSWFESLVLGLVQGLTEFLPVSSSAHLRLTAAFSGWHDPGAAFTAITQIGTEAAVLIYFRKDIGRIIAAWTRSLTDKSMRHDPDARMGWLVIVGSIPIGVLGLTLKDQIEGPFRDLRITATMLIVVGVIIGIADRMAARDEKGGRHRAPQQRKELENLGVRDGLIYGLCQAAALIPGVSRSGATISGGLFMGYRREAAARYSFLLAIPAVLASGVFELKDAMESDHVSWGPTLFATVIAFATGYVVIAWFMKFISTKSFMPFVWYRIALGIVIIVLVSVGVLSPHAAESGG", "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": "MLDVPVLLAAVSPDSPCGDDLEYDAAFLELERIAQGQPERQMGDAVLPAEPPEWPRVRALASELFGRSKDLRVANLLLQSNVALDGLDGLADGLLLVRELLGQYWDGVYPLLDADDDNDPTFRINALTGLVAEPLLQLVWAIPLVRSRAFGPVNLRAALNAAGLQRFASETLSPEQIAGAFADADADALAATRRALDGAQEHALAIESGVAERVGSAQGLDLGPLRQLLRQALQVFDLYGPQGAGESLAPGAEAVADEQVGAAPVAAVAAPAPRASGEIANREDVLRQLDRLLEYYVRHEPSSPVPVLLKRAKTLVTADFAEIVRNLIPDGISQFETLRGPESE", "text": "FUNCTION: Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. Forms a dodecameric ring-shaped structure located at one end of the T6SS sheath. May properly attach the pre- assembled sheath onto the baseplate and/or stabilize the sheaths tubular structure."}
{"protein": "MKESPLITLVKRHSETHFANIKYGYYVLIISLVYLIGLALLRAFGRRTPSRSSSAFKNKIIYRLYDIDPAIHLGILFFAVLIPFYYHYSLTTQSTVYLKRLGRLSYALIPLNLFLTLRPNWFLRKNCTYTDFIPFHKWFSRIITVIGLLHGIFFIIKWAIDDNVSLKQKLILKTFNFAGFIISILVLFLLICSIGPMRRYNYRLFYIVHNLVNVAFILLTPIHSRPGVKFPFLLLNCTLLFIHIINRIVFAKSLMILNKNANYSKTNLVHVRLPRAILPDYFEPGSHIRISPYRRINPLYWLLPSHPYTIASLAEDNSIDLIIKETSTAEPGSQIESLRSNPKSFHLDQEKTYTLINSYPPSVPEECYSQGTNIAIICGGSGISFALPLFRHFFNKENVKYLKMIWLIKDYSEYELVLDYLKTNGLTFEKKLSNNKRISVFISGEYTAETRLDEITTNIDDENSEYEMGSFNNEDEDLSISNFNSENADSNDNTPETSHSPTKENGSMIEVKSKHSFTLSNELKSFNNESAQVNQNETWLFSCGPPSLLQLSKKYCNDERINFVCETYGL", "text": "FUNCTION: Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14 subfamily."}
{"protein": "DSPGGASDAQKTFDVNSLMPVKYEEIRDPHLKELSLSFDPLSGHYDDDGVSAKRLMKELNEHRLLQQSHWFSLFNPRTREEDLMLYNVDEHSGNWDTFAGNAAFFRVHVNEGFFVYASYSVVIHSKLTQHVVLPPLYEVTPHLFTNSEVIQKAYAAKMTQTPTKIFAHFTGSKSNPEQRVAYFGEDIGMNTHHVTWHLEFPFWWDDAHYDHHIERKGESCSSWVHHQLTVRFDAERLSNYLDPVRELHWDDVIHEGFAPHTSYKYGGYFPDRPDNVNFEDVDGVARVRDMLLFEERIQDAIAHGYLRYNGSTINIRDNHGIDVLGDVFESSMYSPRQDYYGALHNQAHRVLGSQADPHGKFALPPGVLEHFETATRDPAFFRLHKYMDNIFRKHKDSLTPYTKNELKFEGVNIDSIYEKGNLETYFESFMYTGVNIMLLTNDVDDVDIATYITDLAHKELSFQEDVTNEGDIGVLETVRIFAWPHIDDDHVEFSFNEGRWDVIEMDKFWVMLEHGHHSIDRSSFDSTVTIPDRPSFHDIEDRTSEAIPHGKELHIEEFESVTGLPNRFLIPKGLVKGKDMDVMVAVTSGEGLAAVEGLHRSANFAHHGCPEVRYPDKRPHGYPLYRPVDDERIITGVTNFKHIQVKVFHH", "text": "FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily. SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily."}
{"protein": "MSRYRGPRFKKIRRLGALPGLTNKRPRAGSDLRNQSRSGKKSQYRIRLEEKQKLRFHYGLTERQLLKYVRIAGKAKGSTGQVLLQLLEMRLDNILFRLGMAPTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDTIAARDEQKSRALIQNSLDSSPPEELPNHLTLQPFQYKGLVNQIIDSKWVGLKINELLVVEYYSRQT", "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": "MKALWALLLVPLLTGCLAEGELEVTDQLPGQSDQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLRKMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQALSDRIRGRLEEVGNQARDRLEEVREQMEEVRSKMEEQTQQIRLQAEIFQARIKGWFEPLVEDMQRQWANLMEKIQASVATNSIASTTVPLENQ", "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": "MQEPREQTLSQVNNPDASDEKPETSSLASNLSMSEEIMTCTDYIPRSSNDYTSQMYSAKPYAHILSVPVSETTYPGQTQYQTLQQSQPYAVYPQATQTYGLPPFASSTNASLIPTSSAIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDAETTTLAATTYQTEKPSAMVPAPATQRLPSDSSASPPLSQTTPNKDADDQARKNMTVKNRGKRKADASSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCANVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL", "text": "FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr- 142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (By similarity). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. The phosphatase activity has been shown in vitro. Coactivates SIX1. Seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity. May be involved in development of the eye. May play a role in mediating the induction and differentiation of cranial placodes. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family."}
{"protein": "MPEIDMKPRSRDVTDGIEATSSRGMLRAVGMGDEDWEKPQIGVASSWNEVTPCNLSLDRLAQGAKEGVHAGGGYPLQFGTISVSDGIAMGHEGMHFSLVSREVIADSVETVMMAERLDGSVLLAGCDKSLPGMLMAAARLDLSSVFLYAGSIAPGWVKLSDGTEKEVTIIDAFEAVGACKAGTMSQEDLTRIEKAICPGEGACGGMYTANTMASVAEALGMSLPGSAAPPSADRRRDYFAHRSGEAVVNLIAKGITARDIMTKEAFENAISVVMAFGGSTNAVLHLLAIAREAEVDLQLSDFNRIADRVPHLGDLKPFGRFVMNDVDRVGGVPVVMKALLDAGLLHGDVMTVTGRTMRENLEAMDLADLDGTVIRKMDDPIHATGGISVLHGSLAPEGAVVKTAGFDLDVFEGPARVFERERAAMDALTEGRISKGDVIVIRYEGPKGGPGMREMLAITGAIKGAGLGKDVLLLTDGRFSGGTTGLCIGHMAPEAVDAGPVAFVRDGDRIRVDIAARTLDLLVDEAELAARREGWAPLPPRYTRGVLAKYAKLVHSAAEGAITG", "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": "MTIMRKSHPLMKIVNHAFIDLPTPPNISGWWNFGSLLGLCLILQIFTGLFLAMHYTSDTLTAFSSVTHICRDVNYGWLIRYLHANGASLFFMCLYIHIGRGIYYGSYLYMETWNIGILLLFLTMATAFMGYVLPWGQMSFWGATVITNLLSAMPYIGQDLVEWIWGGFSVDKATLTRFFALHFIMPFIITALVMVHLLFLHETGSNNPLGLPSDCGKVPFHPYYTTKDFMGVILLLTLFMTLVLFFPDKLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVMALAFSILVLTLLPYLHTSKQRSLSFRPLSQTLFWMLISDVIALTWIGGQPVESPYIVIGQVASVLYFSIILIFMPIAGLIENKMLKL", "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": "MNNDRRFGLKRHITLPGELALDGGSLLTGIEIAYETYGHLNADASNAILICHPLTADQFAASDHPITGKPGWWSRMIGKGKPIDPERYCIICSNVLGSCLGSTGPSSFTPGTETPYAMNFPVITIRDMVRAQAKLLDYLGIRQLKAVIGGSMGGMQALEWASTYPDRVKSVVIIASTARHSAQNIAFHEVGRQAIMADPKWRQGNYYEEKDPPVAGLAVARMAAHITYLSESGLTARFGRRLQSRQEKSFGFDADFQIESYLRHQGIRFVERFDANSYLYITRATDYFDLAEEHGGKLANAFRGTKSRFCVISFDSDWLYPTSESRVIVHALNAAGAAVSFMELSNPNGHDSFLLDAPDLHRTVHGFLEGDRA", "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": "MTMTDPIADMLTRVRNANMVRHEKLELPASNIKKEIAEILKSEGFIKNVEYVEDDKQGVLRLFLKYGQNDERVITGLKRISKPGLRVYAKASEMPKVLNGLGIALVSTSEGVITDKEARKRNVGGEIIAYVW", "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": "MATRTQARGAVVELLYAFESGNEEIKKIASSMLEEKKIKNNQLAFALSLFNGVLEKINEIDALIEPHLKDWDFKRLGSMEKAILRLGAYEIGFTPTQNPIIINECIELGKLYAEPNTPKFLNAILDSLSKKLTQKPLN", "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": "MKHFLTYLSTAPVLAAIWMTITAGILIEFNRFYPDLLFHPL", "text": "FUNCTION: May help in the organization of the PsaE and PsaF subunits. 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": "MAKADLDKDPFDVASMFDDVGKNYDLTNTVLSFGQDRVWRKRTRQRLDLKPGEKVLDLAAGTAVSTVELAKSGAFCVACDFSQGMLAAGKDRDVSKVVGDGMQLPFADNSFDAVTISYGLRNIHDFRAGLKEMARVTKPGGRLTVAEFSTPVIPVFGTVYKEYLMRLLPQAARAVSSNPEAYIYLADSIRAWPSQAELAREINQNGWSDCGWQNLTFGIVALHSAIKPEN", "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": "MTIAIGRAPAERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLLLNEGIRAWMAPQDQPHENFVFPEEVLPRGNAL", "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": "MTQMNFTDKIKVAIIANGKYQSKRLTAKLFAILRNDDRFYLTKKNPDIVITIGGDGMLLSAFHMYEKCLDHVRFVGIHTGHLGFYTDYRDFEVDKLLENLHSDKGEKASYPILKVTATLADGRQLTSRALNEATIRRIEKTMVADVVINKVHFERFRGDGISVSTPTGSTAYNKSLGGAVLHPTIEALQLTEISSLNNRVFRTLGSSIIVPKKDKIEIVPKRLGSYVLSIDNKTYTHRNVAKIEYEIDRKKISFVSTPSHTSFWERVKDAFIGDFDS", "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": "MIIVLSPAKSLDYETPAHVESYTKPAFVDDASELIDGLRKLSPQDIATLMDISDPLARLNFQRYADWSPTFTPANAKQAVLAFNGDVYEGFDAKSLSSTDLDYAQQHVRVLSGLYGLLRPLDLLQPYRLEMGTRFANARGKDLYAFWGDRITRALNEQLETRSGAARVLVNCASTEYFKSVKPKLLAAPVITPVFEDWKGGRYKIISFHAKRARGLMARFVVENRITDPNALKEFATEGYAFDAAASNDSTYVYRRRVGE", "text": "SIMILARITY: Belongs to the UPF0246 family."}
{"protein": "MQKNAAHTYAISSLLVLSLTGCAWIPSTPLVQGATSAQPVPGPTPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTNFGFDTVPRYLQGVFGNARADVEASGGNTFNGKGGANASNTFSGTLTVTVDQVLVNGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNTVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM", "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": "MAYRKRGVKREDLPQQNERLQEKEIENNTDVTMENKDKNKNKNNNRKQQLSDKVLSQKEEIITDVQDDIKIADEVKKSSKEESKQLLEILKTKEDHQKEVQYEILQKTIPTFEPKESILKKLEDIRPEQAKKQMKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQILIEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGVIRRFIADMRQQVQADRNIVNYPSILHPIDHAFNEYFLNHQLVEPLNNEIIFNYIPERIRNDVNYILNMDMNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKEKELVSTEAQIQKMSQDLQLEALTIQSETQFLAGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVIPNDMFLRESLVACELAIINTIVYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFINNNRFRQVVIDGVLNQTLNDNIRNGQVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLSYNYETLMACITMNMQHVQTLTTEKLQLTSVTSLCMLIGNTTVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKSIVEDFLKRLQIFDVPRVPDDQMYRLRDRLRLLPVERRRLDIFNLILMNMEQIERASDKIAQGVIIAYRDMQLERDEMYGFVNIARNLDGYQQINLEELMRTGDYGQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWIPTSTTKVYKQVPQPFDFRASMHMLTSNLTFTVYSDLLSFVSADTVEPINAIAFDNMRIMNEL", "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": "MSTGQTIYHSLLKLPLSVMVKSTPIPSNPIEDLNIDIERPIIYALPFRSHVDLLTLQKSAKELGLPDPLSPIEIDGVSYPRYVFTSIGPKMFDTDDDLPQESLDLFKIVLKHHADNPDADFQLIPTSILWGRRPGKEGTSRPHLMPLNGPQKFVTLIKAGRDSTVRISPVVSLRYMADNHGADDAIAHKLARVAKIHFSRQKLAASGPNLPNRQALFNRLLKSQAIEKVILEEARIRNVDVEKVRKEAMGIMEEIATNFSYSLIKNGNRILKWLWNRLYQGLNINNAATVRKLAQEGHEIVYVPCHRSHMDYLLLSYVLYHEGLVPPHIAAGINLNFFPAGPIFRRGGAFFIRRSFKGNRLYSTIFREYLAELFAKGYSVEYFSEGGRSRTGRLLQAKTGMLAMTVQAMLRGLNRPVTLVPVYIGYEHVMEVTTYAKELQGKRKEKENAGQVLRTLRKLRNFGQGYVNFGEPISLNHYLNEHAPNWSESINPIEPQKPEWMSPVVNGIANKMMTHINDAVAANALTLCATALLAARQRALSKEDLTEQLDCYLQLLRNIPYSNTATVPTQDAEALLEHAIALDKFVIEKDTLGEIISLDRNQSILMTYYRNNIIHLFALPSLIAKLVVQYRSISIDNVQAQIQQIYPFLKAELFLHYDESELNDVVSQHIDELVRQKLIERENDVLQLNATNILKVHLLAHTISETLQRYAIALTHLQASPKLGKNDLEEQSQIMAQRLSRLHGINAPEFFDKGVFGILFNTLKAEGYLNSDGVAVISKVEPFSRDMSRLLNPEIKLTIQAVMTKED", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family."}
{"protein": "MEAERGPERRPAERSSPGQTPEEGAQALAEFAALHGPALRASGVPERYWGRLLHKLEHEVFDAGEVFGIMQVEEVEEEEDEAAREVRKQQPNPGNELCYKVIVTRESGLQAAHPNSIFLIDHAWTCRVEHARQQLQQVPGLLHRMANLMGIEFHGELPSTEAVALVLEEMWKFNQTYQLAHGTAEEKMPVWYIMDEFGSRIQHADVPSFATAPFFYMPQQVAYTLLWPLRDLDTGEEVTRDFAYGETDPLIRKCMLLPWAPTDMLDLSSCTPEPPAEHYQAILEENKEKLPLDINPVVHPHGHIFKVYTDVQQVASSLTHPRFTLTQSEADADILFNFSHFKDYRKLSQERPGVLLNQFPCENLLTVKDCLASIARRAGGPEGPPWLPRTFNLRTELPQFVSYFQQRERWGEDNHWICKPWNLARSLDTHVTKSLHSIIRHRESTPKVVSKYIESPVLFLREDVGKVKFDIRYIVLLRSVRPLRLFVYDVFWLRFSNRAFALNDLDDYEKHFTVMNYDPDVVLKQVHCEEFIPEFEKQYPEFPWTDVQAEIFRAFTELFQVACAKPPPLGLCDYPSSRAMYAVDLMLKWDNGPDGRRVMQPQILEVNFNPDCERACRYHPTFFNDVFSTLFLDQPGGCHVTCLV", "text": "FUNCTION: Negatively regulates post-translational modifications of tubulin, including detyrosination of the C-terminus and polyglutamylation of glutamate residues (PubMed:20162578, PubMed:23251473). Also, indirectly promotes histone H4 trimethylation at 'Lys-20' (H4K20me3) (PubMed:23251473). Probably by controlling tubulin and/or histone H4 post-translational modifications, plays a role in mitosis and in maintaining chromosome number stability (PubMed:20162578, PubMed:23251473). During RNA virus-mediated infection, acts as a negative regulator of the RIG-I pathway by preventing MAVS binding to TBK1 and IKBKE (PubMed:28011935). SUBCELLULAR LOCATION: Cytoplasm Midbody Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Nucleus Note=Predominantly localizes in the cytoplasm (PubMed:28011935). Partially colocalizes with vimentin in prostate cancer cells (PubMed:20162578). SIMILARITY: Belongs to the tubulin--tyrosine ligase family."}
{"protein": "MLSKLLTKVIGSRNDRTLRRMRKIVDEINKLEPQFDSLQDEDLKAKTVEFRERLDQGESLDLLLPEAFATVREASKRVFGMRHFDVQLLGGMVLNNCQIAEMRTGEGKTLTATLPAYLNALTGKGVHIVTVNDYLAARDAETNRALFEFLGMTVGINVPNMPPQAKKEAYSADVLYGTNNEFGFDYLRDNMAFRPEDRVQRERFFAVVDEVDSILIDEARTPLIISGPAEDSSDLYTRINLLIPQLVKQDQEDSEDFRGDGHYTVDEKSKQTHLTENGQEFVEELLTQQGMMAEDDTLYSPSNISLLHHITAALRAHVLFERDVDYIVKDDEVIIVDEHTGRTMPGRRWSEGLHQAVEAKEGVKIQNENQTLASITFQNYFRLYSKLSGMTGTADTEAFEFQSIYGLETVVMPTNKPMVRDDMGDLVYMTEAEKFAAICEDIKERFAKGQPVLVGTVSIEKSELLSNALKKEGIKHEVLNAKFHEKEAYIIANAGQSGAVTIATNMAGRGTDIVLGGSWQEEISNLQDPTDAQIAQIKVDWKVRHETVLAAGGLHITGTERHESRRIDNQLRGRSGRQGDAGSSRFYLSMEDGLMRIFASDRVSNMMKKLGMEEGEAIEHPWVTKAIENAQRKVEGRNFDIRKQLLEFDDVANDQRQVVYELRDELMNADDISGMITQNRDDVILAVVDTYIPQQSLEEMWDIKGLEERLKADFDLELPIQEWLDTEEKLYEEALRERIVAKAIEVYQQKEEVVGAEVLRNFEKTVMLQNLDTLWKEHLAAMDHLRQGIHLRGYAQKNPKQEYKRESFELFEEMLDSLKSDVVSILSKVRVQQQEEVDRMEEERRQQAEELARRQQYQHQNAASQIADESDAGQPAESGTFEREARKVGRNEPCPCGSGKKYKQCHGKIN", "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": "MELLKLNSSVQGPGPGSGSSLCHPGVSLLNSSSAGNLSCEPPRIRGTGTRELELAIRITLYAVIFLMSIGGNMLIIVVLGLSRRLRTVTNAFLLSLAVSDLLLAVACMPFTLLPNLMGTFIFGTVICKAVSYLMGVSVSVSTLNLVAIALERYSAICRPLQARVWQTRSHAARVILATWLLSGLLMVPYPVYTVVQPVGPRVLQCMHRWPSARVRQTWSVLLLMLLFFIPGVVMAVAYGLISRELYLGLRFDGDNDSDTQSRVRNQGGLPGGTAPGPVHQNGGCRHVTVAGEDNDGCYVQLPRSRLEMTTLTTPTPGPGLASANQAKLLAKKRVVRMLLVIVLLFFLCWLPIYSANTWCAFDGPGAHRALSGAPISFIHLLSYASACVNPLVYCFMHRRFRQACLDTCARCCPRPPRARPRPLPDEDPPTPSIASLSRLSYTTISTLGPG", "text": "FUNCTION: Receptor for gastrin and cholecystokinin. The CCK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. 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": "MTLRTTNQRRQLARQQPPLLPEDATTIAHCLDALWIKHGLSRHTLNSYRRDLEGLARWNNGRAGPLATLTPPALLDYLTWRTQQHYSPLSNARLRSVLRTFFSYAVECGWRNDNPSTLLAHPVLPHPLPKALTESQIEALLAAPSIETPEGLRNRAMLELMYAAGLRVSELVTLPVAMLNQRQGVLRITGKGGKERLVPLGEESQHWLQRYLEQARPSLAADKPIPADSDGDVPLFINTNLKRLSRQQFWRWIKHYAALVGIAPNKVSPHVLRHSFATHLLNHGADLRALQMLLGHRSISTTQIYTLIARQHLQQLHAQHHPRG", "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": "MSIHGILGEQTTDYPTEYSPETLYPIARSMGREVIGWQDDKLEVGFDWWQAFELSWLNEQGISQVAIARFGIPASSPFIVESKSLKLYLNSINFTEFGSLETVQTLIAKDLSKCVQAEVNVELFDLEDEHSGLLIAQPDGICIDDALADSTEKVALTLHPDASLLERNTSDAKISEGKTFSFYSNLLRSNCPVTNQPDWGTLAVSITSNKPVNNANMLRYILSFRQHNGFHEQCVEQIFADLSQYYEPSELMVRAWYTRRGGIDINPCRVSDIALLPVPSRLIRQ", "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": "MTFDFDVITLFPEMFNAVTRYGVTGRANENAIYRLYTWNPREFTEDNYRRVDDRPYGGGPGMVMLAEPLEKAITAARERQRACGIGSTKVVYLSPQGRPLNQNVVMELSELSALVLLAGRYEGVDERLIERQVDYEISIGDYVVSGGELASMVLMDCVVRQLPGVLGDPESANQDSFTAGLLDFPHYTRPEVYRGSVVPEVLLSGNHARIERWRLQQSLGRTWLRRPDLLALKMEKGLTAEERKLLEEFQHAYEAN", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
{"protein": "MQYGNLTTVLLLRNTLLSLNSSSICHVHWLQVIVALLVLIVCIFLYWRTPTGINAPFAGYRSPWEPPLLVQMRYVFNAASMIREGYAKWKDSLFQISRYDGDILIVPPRYLDDLHNKSQEELSAIYGLIRNFGGSYSGITLLGENDVGIRALQTKITPNLAKLCDDIRDEFQYCLDTDFPACRDWTSVSVHPLFLKAVERITHRIFVGLPLCRNPQWVQATSKHAHYATMIQIAMRSVPKFIQPLLNFCLPWPWKNAACVREAKNALILEMQRRRNLEKVNSFDYIKSNDLLQAVMEMSSPSHEDSQLDVVAQIMLTMNTIAGHSTAASGAHALFDMVSHSKYIELLREEALQVFRHVELRVTKQALGDLRKLDSFLRESQRHNPLSLLGFFRVVLDPAGITLQDGTHVPYNTLLCVAPHAISNDPDVIEDPTSFNGLRYYEQRCRDASQEKKHQYATTDKSHLHFGYGTWACPGRFLASDMLKVILTMLLLQYDIRSPERAKRPVAGHFHEFPLFNINTPLLMKRRNDSLVL", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene clusters 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, PubMed:22750140). 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; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLRGSIVALITPMNEYGHVCETSLEKLINYHINNGTKAIVSVGTTGESSTLSQEEHINVVMLTLEITNKRLPIIAGTGANATSEAILLTKKFENTGISACLTVTPYYNRPTQKGLYQHFKAISENTKIPQILYNVPIRTGCDLIPETIIKLSKFKNIIGIKEATGDLSRVQKIKNSVHKNFFIISGDDTTFLDFIQLGGHGVISVTANIAAKIMSNICHLALNKNFKLARFMNNKLIPLHQGLFHEPNPIPIKWLAKKIGLIASDTLRLPMTPVSNKTRLILEKALYFSKITAK", "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": "MAPNLRKSHPLLKMINNSLIDLPTPSNISAWWNFGSLLGICLTTQILTGLLLAAHYTADTTLAFSSVAHTCRNVQHGWLIRNLHANGASFFFICIYMHVGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTIVEWAWGGFSVDNPTLTRFFTLHFLLPFMIMGLTLIHLTFLHESGSNNPLGIVSNCDKIPFHPYFSLKDILGFMLMFLPLMTLALFSPNLLGDPENFAPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASMLVLFLAPLLHKSKQRTMTFRPLSQLLFWTLTANLLILTWVGSQPVEHPFMIIGQLASLTYFTILLILFPLTGALENKMLNY", "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": "MASSIPNAPSAFNSQSYVGLRAPLRTFNFSSPQAAKIPRSQRLFVVRASDSEFEAAVVAGKVPPAPPVRPRPAAPVGTPVVPSLPLHRRPRRNRKSPALRSAFQETSISPANFVYPLFIHEGEEDTPIGAMPGCYRLGWRHGLVEEVAKARDVGVNSVVLFPKIPDALKSPTGDEAYNENGLVPRTIRLLKDKYPDLVIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCKQAVAQAQAGADVVSPSDMMDGRVGALRAALDAEGFQHVSIMSYTAKYASSFYGPFREALDSNPRFGDKKTYQMNPANYREALTEMREDESEGADILLVKPGLPYLDIIRLLRDNSPLPIAAYQVSGEYAMIKAAGALKMIDEEKVMMESLMCLRRAGADIILTYSALQAARCLCGEKR", "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). FUNCTION: Is committed to plant tetrapyrrole synthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ALAD family."}
{"protein": "MSSSDCPSPLPTAPKLQVDSVTFPPSVISPASSNTLFLGGAGVRGLEIQGKFVIFTVIGVYLDPVSVPSLSVKWEGKTTEELTESVPFFREIVIGAFEKFIKVTMKLPLTGQQYSEKVTENCVAIWKSLGIYTDSEAKAVERFLEVFKDETFPPGASILFALSPEGSLTVAFSKDDSIPETGKAVIENKLLAEAVLESIIGKNRVSPGARLRVAERLAQLMKENKVEEDATKTDQEEANDLSLAKEN", "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": "MPKRTGDILMSSPLSKFRRKLNFDSPYTSRAAAPTVQGIKRRSWTYRPMYRKPRMYRMYRSPDVPFGCEGPCKVQSYEQRDDVKHTGVVRCVSDVTRGSGITHRVGKRFCIKSIYILGKIWMDENIKKQNHTNQVMFFLVRDRRPYGTSPMDFGQVFNMFDNEPSTATVKNDLRDRYQVMRKFHATVVGGPSGMKEQCLLKRFFKVNTHVVYNHQEQAKYENHTENALLLYMACTHASNPVYATLKIRIYFYDAVTN", "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": "MGFRTLDDVDVTGKRVLVRVDFNVPMSQGKVCDETRLKRHKETLLELQKRGAKLILLSHCGRPKGQGEPEFSLRPVVRVLEKIINQPVAFAPDCVGVAAQTAIEALQNGGLLLLENVRFHPGEEKNDCSFAEALAHNGDLYVNDAFSVSHRAHASVEGITHLLPSYAGRSLQCELQALEKGLDNPKRPVVALVGGAKVSSKLFVLNHLVEKVDYLVIGGGMANSFLAAQGVHIGKSLCEHALMQTIKKVIEKAQEYQCTLLLPVDAVVGFRFEKGAPHRLYDIGDIPDDGMILDIGTRSIAHINEVIDKAATLVWNGPLGVFEMSPFDQGTIAVARHAAECSLTGKCVSIAGGGDTVFALNHAGVANDFTYLSTAGGAFLEWMEGKVLPGIFALRQA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MSRTAFFISDGTGITAETLGRSLLAQFEGVDLTLVVKPYIDTLEKAHDLAAIIAQTADRDGERPIVIDTIVDQSIRDIIAAAPGFKVDIFSTFLAPLEEELATHSTYTVGRTHAIGRDDVYMHRIDAVHFALDNDDGARTHQYDQADVILVGVSRCGKTPTSLYLALQFGIRAANYPLTEDDLDEDGVLNMPKALAPYRHKLFALTIDPRRLAAIRSERRPNSRYCSMDQCMQELQQAEALFRRYHIPYIDTTRFSIEEISTRMIAETHLTRRFSPR", "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": "NKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPNFTFEDPKFEAVEKPQS", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes (By similarity). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family."}
{"protein": "MLKVEERYTNAVPELQKFFNYGNIMQVPKLVKVVINTGVGEAVSNSKAMETAEADIVAIAGQHPVVTRAKRSVANFKLRAGMPIGLKVTLRGQRMYDFLNKLFFITLPRVRDFQGVPNTAFDERGNYTLGFKDHSVFPEIDFNKIEKPRGLEICIVTTANTPEEGKKLLELLGMPFSKD", "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": "METMDTSVDLPGRWIDIEKIIKRTGPFASPSFEPDTKASPNIMNGLQNDFKVLVIGAGGLGCEILKNLALSGFRNIDVIDMDTIDISNLNRQFLFRRKDVGKSKAEVAAAFINSRITGCNVTPHKCRIQDKDEDYYRQFKIVIAGLDSIEARRWINGLLVNLVVVNDSGDIEPDTIIPLVDGGTEGFKGQARVILPKISSCFECSLDAFPPQVSYAICTIANTPRVPEHCIQWALLFGLQDATLEKPFDPKQFDNDNPDHMNWLFECAKKRAEKFNINGVTYKLTQGVAKNIIPAIASTNAIIAAACCNEVFKFCTDSSGYLNNYMMYNGLNGVYTFTFEYEIKEGCAVCGTNLVTFEIDKSNTLSTFLEKITTDSRFQFKKPSLRSNGRNLYMQGLLHQSTVPNLEKTLSELNVQEDDEITITDPALPGNLAVRMRIKYTS", "text": "FUNCTION: Regulatory subunit of the dimeric uba3-nae1 E1 enzyme. E1 activates nedd8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a nedd8-uba3 thioester and free AMP. E1 finally transfers nedd8 to the catalytic cysteine of ube2m (By similarity). SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3 subfamily."}
{"protein": "MKNLLSMEALTVHEIEHLLGQAAQFKRGKKATFTEQAFAVNMFFEPSTRTHTSFEVAEKKLGVEVVSFDAASSSMTKGETLYDTLLTMQAVGVNVAVIRHSEENYYEGLENLDIAIVNGGDGCGEHPSQSLLDLFTIKEQFGTFQGLKVAIAGDIRHSRVANSNMKVLKRLGAELFFSGPREWFDESCLAYGTYLPVDEMVEKVDVMMLLRVQHERHSGTEAFTKESYHEKFGLTIERAAKLKADAIIMHPSPVNRDVEIADSLVESEKSRIVTQMTNGVFIRMAILEAILKEQEMRAKLCTY", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
{"protein": "MKPVIALVGRPNVGKSTLFNRLTRSRDALVADLPGLTRDRHYGEGRVGERPYLVVDTGGFEPVAKDGILHQMARQTRQAVEEADVVVFIVDGRNGLAPQDKSIADYLRKTGRPIFLVVNKAEGMKYTAVATDFYELGLGDPRAISAAHGDGVTDMINEALEVAYAGQPEEADDDDPSRGIKIAIVGRPNVGKSTLVNALIGEDRVIAFDMPGTTRDSIYVDFERNGKKYTLIDTAGLRRRGKVFEAIEKFSVVKTLQSISDANVVILLLDAQQDISDQDAHIAGFVVEQGRALVIGVNKWDGLDDHARDRAKADLTRKLKFLDFAKSHYISAAKKTGIGALMRSVDDAYAAAMAKLPTPKLTRALIEAVEFQQPRRRGPVRPKLRYAHQGGQNPPLIVIHGNALDAVTDTYKRYLENRFRETFSLTGTPLRIEFRSSNNPYADKG", "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": "MAPKKKKKVTGLIKLQIQAGQANPAPPVGPALGAHGVNIMEFCKAYNAATENQRGNVVPVEITVYEDRSFDFKLKTPPAAKLLLKAAGLQKGSGVPHTQKVGKVSMAQVREIAETKKEDLNARDIDAAAKIIAGTARSMGITVEG", "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": "MEPIQKMDSLNNKEGQPDKKRKKHESEKEGENEVLEIDVTKPVPPSKKLMRKLRKAGKIDKDGNWTPEALEEAKKKEEKRLKRLDAKYGRKEEGESQEESKRSPWGIWVGNLSFHTTKEILTDFFVRETSEMIKEVSEENIKPITTEQITRIHMPMSKEKRFQNKGFAYVDFATEDALKLALQCSEKALNGRNILIKSNTDFSGRPSKPANTLSKTASIQSSKKEPSSILFVGNLDFETTDADLKEHFGQVGQIRRVRLMTFEDTGKCKGFGFVDFPDIDTCMKAMELGHNSWRLEYGEDRSKRMRNKSPMARSGRFNDAESLGQEDKPNFKRARKIDPRSVRPGAALAKAQRSSAAIVEPAGQKIKFD", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAVAAAAAATAMSAAGGGGASAARSISRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESLEPDPGTPGSARTETLYYTDDTAMTRALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFKKLLNPKCRDVYEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGVSSSEHFLEQLLGHMEELEGDAQSVLDAKELGMEERPYSSRLKKVGELLDQDVVSREEVVSELGNGIAAFESVPTAIYCFLRCMEPHPEIPSTFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPESWQQSCEGFEETDVLAQSLHRVFQESS", "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 (By similarity). 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 (By similarity). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP- ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). 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 (PubMed:24191052, PubMed:30830864). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). 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 (By similarity). 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": "MNIDDDLQALTKQEATLTFSHFDHNTAWELGSALRSAAERARLSIAIEIQLAGQTLFYYAMPGTTPDIADWVRRKRNVVNHFHKSSYAIGLRLQQRQSTLEERYGLSVRDYSAHGGAFPINLAGLGCIGTISISGSPQLEDHNLLVSTLAHFLGLSLPAVH", "text": "SIMILARITY: Belongs to the UPF0303 family."}
{"protein": "MTLRVAINGFGRIGRNVVRALYESGRRAEISVVAINELADAAGMAHLLKYDTSHGRFAWDVRQEGEQLWIGNDVIRLLHERDINALPWKALDVDVVLDCTGVYGSRADGIAHLEAGARKVLFSHPGGNDLDATVVYGVNEEELRAEHRIVSNASCTTNCIIPIIKLMDDAFGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTRLAAGITRIFPKFHDRFEAIAVRVPTINVTAIDLSVTVQKPVKAYEVNLLLQKAAQGAFHGIVDYTELPLVSTDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFANRMLDTTLAMAAIGFR", "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": "MDFHSVLKMAAAKPGSDGIAKRYSLAVGPPKKDPKVKGVDSAAVQAFLRKKDEESRRKETVEKRKKEDLLAKRKELKHDRKARAMASRTKDNFKGYNGIPIEEKPRKRKRSGTEEDQNDNMAAEGEEYMTEEELYEYSQSESEQEEEEELPPQKVPKPAPGKKPPTPALNFNDLLRLAERKQYEPVEVVRPVKKEERLRTAEELKELEFLERKAQKADRKDPKRNEQLVKVSKGSGDKYSSLKGTHSGNSKSSSTEQNGTIRKSSSDTGSRTEKSGSVFHTKESKKPSSAKDLGGKGSRPNVTGDGKDRHSSSQPSAASNSAFGRPSGSARPSGSSGPGRPLGGSGSSSGKSTGGSASGSARSVGGSGSGSGKPMGGSGSGKPIGGLHSSHGSGKPTGGTGSGSGKPTGASGSGSGKPTGSSGSAKSVRESGSGSRSVRESGSGSRSVRESGSGSGSARSVRESGSGSGSARSVRESGSGSGSARSVRESGSAKQAGGPGSGRALGSGSSFARPSSNSSPAPGKPAAGSGSARPSSSGTPRSSSMGHSTSNSSRQPSSSGAVRPSSGPPTGATPKGPSPRPGAGPTSVRPNSTSVPGSARSSLGSGPGRPVAASATGQLAPAKPKCTVVAETISSKNFVPKSINGHMNGIRTAAPPGHRPAMRPPGPPLPPITSSYKRRIDDDDDYDSEMDDFIDDGGECQDEISKHIREIFGYDRTKYRDESDYALRYMESTFREQQKEEARSLRLGIQEDLEELQREEEELKRKAKQLKAAKKMSR", "text": "FUNCTION: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription. Binds DNA and histones and promotes nucleosome assembly (in vitro). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (By similarity). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the SPT2 family."}
{"protein": "MATSARRAYGFGRADEATHPDSIRATLAEFLSTFVFVFAGEGSILALDKLYWDTAAHTGTNTPGGLVLVALAHALALFAAVSAAINVSGGHVNPAVTFAALIGGRISVIRAIYYWVAQLIGAILACLLLRLATNGLRPVGFHVASGVSELHGLLMEIILTFALVYVVYSTAIDPKRGSIGIIAPLAIGLIVGANILVGGPFDGASMNPARAFGPALVGWRWSNHWIYWVGPFIGGALAALIYEYMIIPSVNEPPHHSTHQPLAPEDY", "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": "MARINYSINGDPETTSKAMGSELHISPKKSREVCCKIKGMKASEARKFLEDVIAMKQAVPFKKHHDGSGHRKGPMAAGKYPISASKEILKVLKNAESNAEYKGLEPANMYIIHAAIQRGRVIHGFMPRARGRATPKDTETVNIEMILSEVR", "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": "MHLRLLKLHPNAIIPKYQHEGDSGVDLHAIEPVAIAPHKTALIKTGLAAEIPIGTELQIRPRSGLALKQSVTVLNSPGTIDANYRGEIGVILINHSDTVFEVKAGMRIAQMVMVPVMHLDITVVDKVSDTSRGTGGFGSTGT", "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": "MRKAERVRKTNETDIELAFTIDGGGQADIKTDVPFMTHMLDLFTKHGQFDLSINAKGDVDIDDHHTTEDIGICLGQALLEALGDKKGIKRYGSAFVPMDEALAQVVIDLSNRPHLEMRADFPAAKVGTFDTELVHEFLWKLALEARMNLHVIVHYGTNTHHMIEAVFKALGRALDEATTIDPRVKGIPSTKGML", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MAQEQTRRGGGGDDDEFTSSTSVGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ", "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": "MALILERLYLLSSPRNAIIRNTRSEAGRELIFSFGLPSLSLPSCIASQYGKRRRLYFTTQLHVNSFLHWTCDANDAVNITLVQPDEQKLKTVSSFHPQFTYPIFGDDERIFGYKGLIIRLRFAAHDLRPQLHISYDEKFKPVEDIAAVDIPKTLKPWIPEDAFVTLPDYEKAVLEDKAAKDFKPPGKLVHCYVSRNRNFEIWAGSLADPEVRRLLDRAQIFVSLFIEAGTPLATDDPEWTLQRWTVYFVYEIVKPPTPTASKYSIVGYATTYRWWHYRRDRTQVPVVKNDPFPSGPEIHPSQLPSRLRIAQFLILPPHQNSGHGRHLYTAIHSACVQDPSVVELTVEDPNEAFDVLRDSADYHILRPEFIKHEVNINPDPYEAHSRNQRPRRVPTAALIPVKLLHDIRTSYKIDSTQFAHILEMFLLSQIPLKNRHAGGANMSRLLIKKHRAEDPNERRYYWWRMLTKQRLYKRSKDILIQLDLDERIQKLEETVSNVEEGYEVLLKEFSEREEKLKARGVVESPAATVSDDASAGPSGTSRDQRVKRKFTVEDDEDKVEEEDTAKRTKV", "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": "MIVIPAIDLKEGRCVRLEQGLMEKDTVYNDNPGAQARSWQEQGGELLHIVDLDGAFAGVPRNRDAIRAIAEAVSIPTELGGGIRDLPTIEAYLELGIDRVILGTVAKENPELVREACRLFPGRIVVGIDARDGLVAVRGWADVTEKLATELAKEMEGFGVEAIIYTDIARDGMMGGPNLEATRALAESISVPVIASGGVSCLEDIARLMTIEDSGVTGVITGKALYTGSLDLREAVALTKGKA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MIQNSRPSLLQPQDVGDTVETLMLHPVIKAFLCGSISGTCSTLLFQPLDLLKTRLQTLQPSDHGSRRVGMLAVLLKVVRTESLLGLWKGMSPSIVRCVPGVGIYFGTLYSLKQYFLRGHPPTALESVMLGVGSRSVAGVCMSPITVIKTRYESGKYGYESIYAALRSIYHSEGHRGLFSGLTATLLRDAPFSGIYLMFYNQTKNIVPHDQVDATLIPITNFSCGIFAGILASLVTQPADVIKTHMQLYPLKFQWIGQAVTLIFKDYGLRGFFQGGIPRALRRTLMAAMAWTVYEEMMAKMGLKS", "text": "FUNCTION: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis. FUNCTION: Plays a role as pro-apoptotic protein that induces caspase- dependent apoptosis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily."}
{"protein": "MKGIIYPRKSSADAYVYLSPGVREHLFSLLVKYTSSQRDSPAGSSTKVAPDTPQTNFIVEIQWVCHKILLEMEEQFGSLGGLVADINICLIWTLFRNYKHKHRMNNSDTGKSCAEYAQSVVKHLTERMVYCTDKFFINSACSGVTVPQNLALVIASISQVCRNKCQGAWRRMGNGRRTLIDLGLQLVNTYNLLNACGAIDDKCKAFIKLTFPYLNLETVYSPVHAASTGLHQKMAISLYKGQEKRKVPNATIYSNLVTQEKFALPEILLGEITDEGLLANKGPDLEKLLSEPQTILKLVTKLSPVSQFQVFMARWGDKLPSHLKDVCVSDSSQLPQQYENFKVVWPQHQTWPNDETSALPIASASLLSLQAENLPTSVQNSVAQETTGLPPQVPAGEMPPRGNCPVEDHGLLNSDAPDDLSGKGDYDLFTSDDLLPMSSGNVAIPVCEDPLAPPCKKQRMEPPDPLSTPGDNQWGDGAASAWIQSYMENEDAYLELILQGLYHLDEPPKLEDSIQVQDVSNSTNDPLEGPSRSQASCFEDTENIANPLDLFV", "text": "FUNCTION: Transcription activation. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae TAF50 family."}
{"protein": "MEAKKLWGGRFEASLEEWVEEFGASIRFDQKLAKYDIQGSLAHVKMLGQTRIISQAEAQVIQAGLEELLEEYEAGKLVFDIRNEDIHMNIESLLTEKIGSVAGKLHTARSRNDQVATDMHLYLKDTLFQVVDKLTNLRQILVDLAQEHVETIMPGYTHLQHAQPISFAQHLLAYYNMFSRDSERFAFNMQHTNVSPLGAAALAGTTFPIDRQMTSDLMGFAKPYSNSLDAVSDRDFILEFLSNASILMMHMSRLCEEIINWCSYEYQFVTLSDTFSTGSSIMPQKKNPDMAELIRGKTGRVYGNLVGLLTVMKSLPLTYNKDLQEDKEGMFDTAETVLISIDILAGMLKTMTVHKERMAQSTEKDFSNATELADYLASKGLPFRQAHEIVGKLVLECSKAGHYLQDVSFETYQAISPLIQADIYDALSSKVAVSRRNSLGGTGFESIADQLKSAKEEIQNAKSL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MQKKYFGTDGIRGKVGNSLINAEFMLKLGWAVGRVLANSHSATVLIGKDTRISGYMIESALQAGLSAAGVNIKLTGPMPTPAIAYLTNSVRADAGIVISASHNHYPDNGVKFFNKDGFKLSDELELAIEKQIDKPMKTVVADRLGKAARMNEAHGRYIEFCKSTFPSNLTLKGLKIVVDCANGAAYAVAPSIFHELGAEVVAIADDPDGFNINQTCGATDTAHLQEMVVKHNADVGIAFDGDGDRLIMVDHHGLRVDGDELLCIMAIDRFYLKENAPLGVVGTIMSNLGLEQTLKRHHIAFERSPVGDRYVLDLMQQKGWFLGGESSGHIVDLGFTTTGDGVITALQILRIMQQAEKPLADLKKVMVKNPQVLINVPIKGILDIAQNPNIKKAITEAEKQLNGAGRILLRPSGTEPVIRVMVEGSDEGIVRQTAEMLAAAVQQSTL", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MLLPIVVLVGLPGAGKSTIGRRLARALNTELVDSDELIERATGKACGAVFSELGEPAFRELEAIHVAEALKSSGVVSLGGGSVLTESTRELLKGQDVVWIDVPVEEGIRRTANERSRPVLQAADPAEHYRNLVKVRTPLYEEVATYRLRTNNRSPQQVVAAVLHHLEID", "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": "MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGTDALVLALDVRIDEQGNKQVAVSGWQENSGVSLEQLVETYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAIACWQNV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MSKRDYYEVLGVARGASDEELKKAYRRCAMKYHPDRNPGDAAAEATFKECKEAYEVLSDGNKRRAYDAHGHAAFEHGMGGGGGGPGGPDMGDIFGDIFGNIFGGGAAGPRAARRGADVGYVLELDLEEAVAGIERRIEIPTLIECEPCHGSGSEDGKVEVCATCHGRGQVRIQRGIFAMQQSCPHCDGRGTLIQNPCKTCHGAGRVEEDKVLSIKVPAGVDTGDRIRLAGEGEAGPAGTPPGDLYVEVRVREHAIFQRDGDDLHCEVPIRISQAALGDTVRVATLGGEAEIRIPAETQTGKLFRLRGKGVRSVRSRSEGDLYCRVVVETPVNLTADQRELLKQFEATFTGEDARKHSPKSATFIDGVKGFWDRMTS", "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": "MGLLTFRDVAIEFSLEEWQCLDTAQRNLYKNVILENYRNLVFLGIAVSKQDLITCLEQEKEPLTVKRHEMVNEPPVMCSHFAQEFWPEQNIKDSFEKVTLRRYEKCGNDNFQLKGCKSVDECKLHKGGYNGLNQCLPTMQSKMFQCDKYVKVFNKFSHSDRHKIKHMENKPFKCKECGRSFCMLSHLTRHERNYTKVNFCKCEECEKAVNQSSKLTKHKRIYTCEKLYKCQECDRTFNQFSNLTEYKKDYAREKPYKCEECGKAFNQSSHLTTHKIIHTGEKPYKCEECGKAFNQFSNLTTHKKIHTGEQPYICEECGKAFTQSSTLTTHKRIHTGEKPYKCEECGKAFNRSSKLTEHKNIHTGEQPYKCEECGKAFNRSSNLTEHRKIHTEEKPYKCKECGKAFKHSSALTTHKRIHTGEKPYKCEECGKAFNRSSKLTEHKKLHTGKKPYKCEECGKAFIQSSKLTEHKKIHSGEIPYKCEECGKAFKHSSSLTTHKRIHTGEKPYKCEECGKAFSRSSKLTEHKIIHTGEKPYKCERCDKAFNQSANLTKHKKIHTGEKLQNWNV", "text": "FUNCTION: May be involved in transcriptional regulation. May play a role during osteoclast differentiation by modulating TRAF6 signaling activity. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MEFAHLTVLSLFCLAFVGITATSSGEDYWQSIWPNTPLPKTFSDLLIPSGKTNSLPIKSEELKQYSTLFFEHDLHPGKNFILGNTNSVGSIIRPFTKSRQGVTDSIWLANKEKQSLEDFCYSPTAIAEHKHCVSSLKSMIDQVISHFGSTKIKAISSNFAPYQDQYVVEDVKKVGDNAVMCHRLNFEKVVFNCHQVRDTTAYVVSLVASDGTKTKALTVCHHDTRGMNPELLYEALEVTPGTVPVCHFIGNKAAAWVPNHTADNLCVM", "text": "SUBCELLULAR LOCATION: Secreted Note=Translocated in vitro across the endoplasmic reticulum membrane with concomitant removal of its signal peptide."}
{"protein": "MNKDYDVIVVGAGHAGVEAALASARLGNKTALITLYLDTISMMSCNPSIGGPGKSNLVTEIDVLGGEMGRHIDEFNLQLKDLNTSKGPAARITRGQADKYKYRRKMREKLEKTENISLIQDCVEEILVEDIKDTQNSNYIKKITGIKTRLGIIYNAKVIVLATGTFLKGKIVIGDVSYSAGRQGETSAEKLSDSLRELGIKIERYQTATPPRLDKKTIDFSQLEELKGEEHPRYFSLFTKKEKNNTVPTWLTYTSDKTIEVIKEMMKFSPIVSGMVNTHGPRHCPSIDRKVLNFPDKEKHQIFLEMESENSDEIYVNGLTTAMPAFVQEKILKTIKGLENAKIMRYGYAVEYDYAPASQLYPSLENKKISGLFFAGQINGTSGYEEAAAQGFIAGVNAAKKIKGEKPVIIDRSEAYIGVLIDDLIHKKTPEPYRVLPSRAEYRLTLRYDNAFMRLFDKIKEVGIVDKDKIEFLEKSINDVYMEINNLKNISVSMNEANKFLESLDIEERFVKGVKASEILKIKDVSYDNLKVFLNLNDYEDFVKNQIETMIKYEIFIERENKQIEKFKKLEHMYIPENINYDEIKGISNIARAGLDEVRPLSIGEATRISGVTSNDITLIIAYMNIKL", "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": "MVVIGEHRHTQVTVDLQAIKTNISNEMAQKDELTELWAVVKANGYGHGIIQVAQAAKEAGATGFCVAILDEALALRAAGFAEPILVLGITEPEYAPLVAEKDISLAVGTQDWLTTAAAILAANQVTTPLHVHLALDTGMGRIGFQTPEELATAVTTLRQPQSPFDFEGIFTHFATADQADDTYFTHQLNNWKHLIAVVDELPRYVHVSNSATSLWHQACNGNMVRFGVALYGLNPSGRELSAPYPLQPALSLTARLTFVKRLARGKSVSYGATYTAAQDEWIGTVPIGYADGYERRLQGFHVLVDGEFCEIVGRVCMDQLMVRLPHEVPVGAKVTLVGTDGARTISLQDIADYCGTIHYEIACGLAPRVPRVYID", "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": "MFGTFLQNQSVRLNMVCAPWLLAVVVVCVCNPGVEGQCWDSSHCKDLPSEDKILECIHLFRSGLQDESPEPRSAAQQSTEESLSLGILLAALTSGERALDADPEPHSDKRHSYSMEHFRWGKPIGHKRRPIKVYASSLEGGDSSEGTFPLQARRQLSSWEDEMVGALGNQGAKAQTKVVPRTLTVTGLQDKKDGSYRMGHFRWGSPTAIKRYGGFMKPYTQQSHKPLITLLKHVTLKNEQ", "text": "FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol. FUNCTION: Melanocyte-stimulating hormone beta: Increases the pigmentation of skin by increasing melanin production in melanocytes. FUNCTION: Beta-endorphin: Endogenous orexigenic opiate. FUNCTION: [Met-enkephalin]: Endogenous opiate. FUNCTION: Melanocyte-stimulating hormone alpha: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. 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": "MKKTFYHYMMKHRAALFKNEISDLAEAMYDDLSFPKQSEDYDVISSYLELSGMLESMSIFDDAWDLYIQER", "text": "SIMILARITY: Belongs to the UPF0346 family."}
{"protein": "MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEKGDMGDKGQKGSVGRHGKIGPIGSKGEKGDSGDIGPPGPNGEPGLPCECSQLRKAIGEMDNQVSQLTSELKFIKNAVAGVRETESKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCEFDKENM", "text": "FUNCTION: Lectin that plays a role in innate immunity, apoptosis and embryogenesis (PubMed:23954398, PubMed:25912189, PubMed:21258343). 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 (PubMed:25912189). Primarily recognizes the terminal disaccharide of the glycan (PubMed:25912189). Also recognizes a subset of fucosylated glycans and lipopolysaccharides (PubMed:17179669, PubMed:25912189). 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 (PubMed:20956340, PubMed:25912189). 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 (Probable). 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 (PubMed:21258343, PubMed:28301481). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the COLEC10/COLEC11 family."}
{"protein": "MKINGNEIRPGNVIEHQGSLWVAVKCNAVKPGKGGAFNQVELKNVIDGTKLNERFRAAETVEKVRLEQKDFTFLYQQGEALVFMDTESYEQLELQRDFVGDRAAFLQDGMTVTVELHEEKPLGISLPDQVTVTIAEADPAIKGQTVTSSYKPAILENGIRILVPPFVQAGERIIVDTNELTYIRRVSEKG", "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": "MAPHSSSADAGPPVWHGTTILTVRKGGKVVIGGDGQVSIGQTVIKANAKKVRKLGKGDVIGGFAGATADAFTLFERLEAKLEQYPGQLTRAAVELAKDWRTDRYLRRLEAMMIVADKDVSLVLTGTGDVLEPEAGVMAIGSGGNYALAAARALIDTDQDAETIVRKSLGIAADICVYTNGNLTLETLTA", "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": "MTTEDPDSNHLSSETGIKLALDPNLITLALSSNPNSSLHSPTSDEPVPESAGKADTSIRLEGDELENKTKKDNDKNLKFLKNKDSLVSNPHEIYGSMPLEQLIPIILRQRGPGFKFVDLNEKELQNEIKQLGSDSSDGHNSEKKDTDGADENVQIGEDFMEVDYEDKDNPVDSRNETDHKTNENGETDDNIETVMTQEQFVKRRRDMLEHINLAMNESSLALEFVSLLLSSVKESTGMSSMSPFLRKVVKPSSLNSDKIPYVAPTKKEYIELDILNKGWKLQSLNESKDLLRASFNKLSSILQNEHDYWNKIMQSISNKDVIFKIRDRTSGQKLLAIKYGYEDSGSTYKHDRGIANIRNNIESQNLDLIPHSSSVFKGTDFVHSVKKFLRVRIFTKIESEDDYILSGESVMDRDSESEEAETKDIRKQIQLLKKIIFEKELMYQIKKECALLISYGVSIENENKVIIELPNEKFEIELLSLDDDSIVNHEQDLPKINDKRANLMLVMLRLLLVVIFKKTLRSRISSPHGLINLNVDDDILIIRPILGKVRFANYKLLLKKIIKDYVLDIVPGSSITETEVEREQPQENKNIDDENITKLNKEIRAFDKLLNIPRRELKINLPLTEHKSPNLSLMLESPNYCNALIHIKFSAGTEANAVSFDTTFSDFKEVEDFLHFIVAEYIQQKKV", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 17 family."}
{"protein": "MTIAVYPASFDPITNGHLDVAARASRLFDELVLAVAHRPYKKLLFTTEQRIAMIRESVAHLPNVRVDAFSSLVVEYALEIGATVLVRGLRAATDFEHEFQMAHINHHLAPTLDTVCLMADQRFTLLSSSAVREIAAYGGDVSSFVPAHIALALKQAYQTHEESRA", "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": "MIIFTDVISGDELLSDAYDVKLVDDVVYEADCAMVNVNNGDVDIGANPSAEEGGEDLEDGTETVNNVVYSFRLQQTSFDKKSFMTYMKGYMKRVKAHLAEKNPEAIEAFENGAKTYFKKVVSSFGDWDFYTGESMDPDGMVVLLNYREDGTTPYVAIWKHGVSEDKI", "text": "FUNCTION: Involved in protein synthesis. Involved in microtubule stabilization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TCTP family."}
{"protein": "MVPPVQVSPLIKLGRYSALFLGMAYGAKRYNYLKPRAEEERRLAAEEKKKRDEQKRIERELAEAQEDTILK", "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": "MSLEQRSLHCKPEEALEAQQEALGLVCVQAATSSSSPLVLGTLEEVPTAGSTDPPQSPQGASAFPTTINFTRQRQPSEGSSSREEEGPSTSCILESLFRAVITKKVADLVGFLLLKYRAREPVTKAEMLESVIKNYKHCFPEIFGKASESLQLVFGIDVKEADPTGHSYVLVTCLGLSYDGLLGDNQIMPKTGFLIIVLVMIAMEGGHAPEEEIWEELSVMEVYDGREHSAYGEPRKLLTQDLVQEKYLEYRQVPDSDPARYEFLWGPRALAETSYVKVLEYVIKVSARVRFFFPSLREAALREEEEGV", "text": "FUNCTION: May be involved in transcriptional regulation through interaction with SNW1 and recruiting histone deactelyase HDAC1. May inhibit notch intracellular domain (NICD) transactivation. May play a role in embryonal development and tumor transformation or aspects of tumor progression. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
{"protein": "MVILSNVSLFSCCNISQKPSLFSPSSRSSHCPIRCSQSQEGKEVVTSPLRSVVWSLGEEVSKRSLFALVSASLFFVDPALAFKGGGPYGQGVTRGQDLSGKDFSGQTLIRQDFKTSILRQANFKGAKLLGASFFDADLTGADLSEADLRGADFSLANVTKVNLTNANLEGATVTGNTSFKGSNITGADFTDVPLRDDQRVYLCKVADGVNATTGNATRDTLLCN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen."}
{"protein": "MKPLTPRQQQVFDLIKSKIEDCGMPPTRAEIARELGFRSANAAEEHLKALARKEAIEIIPGASRGIRILLEDAANEEQGLPLIGQVAAGEPILAQEHVEMHYQVDPGMFKPQADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSTVLLHAENEEFSPIHVDLESQHLSIEGLAVGIIRNTDWM", "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": "MRKILFFGLLSICFLFVFFFYKQKENKIIYNKIVEKFEDNVVIDETYTHLFKDSNLKELVFIKSRLIIPELEHKKMMKATGYRADAYRALSTVYKFDFKVHDNKILGFKSVIFEGFEDAKVSKHENNLPSEKWQQLKDFNIGDPNINEKFFHLEFPFVVKNTLCVTISKGFFKKIKKLKRLKIMLISNEDREYKIDIENFLPKYNL", "text": "FUNCTION: Virulence-associated protein essential for survival of the bacterium within the tick host and therefore within the natural life cycle of the spirochete. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the BptA family."}
{"protein": "MRFKGLDLNLLVALDRLMTERKLTAAARAINLSQPAMSAAISRWRDYFRDDLFIIQRRELNPTPAAEPLAPVVREALLHIQLSVIAWDPINPAEFDRRFRIILSDFMALVFFEKIIVRLAREAPGVSFKLLPLDDDPEELLRRGDVDFLILPDLFMSGAHRKARLFEERLVCVGCSTNEQLQGKLFLEQYMSMGHVAAKFGRGLKPSVEQWLLLQQGLKRRIELVVPGFNLIPPLLSGTNRIATIPLRLVKHYEQTIPLRIIEHPLPLLSFTEAVQWPALHNSDPGNIWMREIMIQEASRHWNPRPKVVRLKRPRSFHSRSS", "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": "MSIKILSESEIKQVANSYQAPAVLFANPKNLYQRRAKRLRDLAQNHPLSDYLLFAADIVESQLSTLEKNPLPPQQLEQLNAIEPLNAKTFKRDSIWREYLTEILDEIKPKANEQIAATIEFLEKASSAELEEMANKLLAQEFNLVSSDKAVFIWAALSLYWLQAAQQIPHNSQVENAENLHHCPVCGSLPVASIVQIGTSQGLRYLHCNLCESEWNLVRAQCTNCNSHDKLEMWSLNEELALVRAETCGSCESYLKMMFQEKDPYVEPVADDLASIFLDIEMEEKGFARSGLNPFIFPAEDA", "text": "FUNCTION: Necessary for formate dehydrogenase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FdhE family."}
{"protein": "MKFTGKVWKFGDNIDTDAIIPARYLNTFDPQALAAHCMEDADPDFPKKVSAGDIIVAGENFGCGSSREHAPIAIKAAGVSCVIAKSFARIFYRNAFNMGLPIFESAELFDRVDEGQTITVDGDSGVILLEGAQTPLSIQPIPPFMQELIADGGLMKHLARKNRG", "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": "MSLENFGNFLTLDEKHSFIKKYFKEFYTKDFKLFASKDKHYRTRAELSFYHENDTLFYAMFDPKSKKKYIIEYLDFADEKICAFMPRLLEYLRQDNKLKEKLFGVEFLTTKQELSITLLYHKNIEDIKSNLENLSNILHINLIARSKGKKLIFKTENLRQTLNIQDRKIFYEFNNDCFIQPNTAINEKMITWVCEILNTQKRMDLLELYCGYGNFTLALAPFFFKILATEISKSNINFALKNCELNNTTNIHFARLSSEELSLAIKKEREFFRLKDIRLDDFNFSHVLVDPPRAGLDKSVIDLIKKYGNIIYISCNPMTLKENLKELSLTHRVEEFALFDQFVNTPHLECGVFLSKV", "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": "MDVSGQETDWRSAAFRQKLVSQIEDAMRKAGVAHSKSSKDMESHVFLKAKTRDEYLSLVARLIIHFRDIHNKKSQASVSDPMNALQSLTGGPTPGAAGIGMPPRGPGQSLGGMGGLGAMGQPLPLSGQPPPGTSGMAPHGMAVVSTATPQTQLQLQQVALQQQQQQQQQQQFQQQQAALQQQQQQQQQQQQQQQFQAQQNAMQQQFQAVVQQQQLQQQQQQQHLIKLHHQSQQQQIQQQQLQRMAQLQLQQQQQQQQQQALQAQPPMQQPSMQQPQPPPSQALPQQLSQLHHPQHHQPPPQAQQSPIAQNQPPQIPPQSQSQPLVSQAQALPGPMLYAAQQQLKFVRAPMVVQQPQVQPQVQQVQPQVQPQAAVQAAQSAQMVAPGVQMIAEALAQGGMHVRARFPPTSTMSAGPSSSISLGGQPTTQVSQSSLTMLSSPSPGQQVQTPQSMPPPPQPSPQPGSQPNSNVSSGPAPSPSSFLPSPSPQPSQSPVTARTPQNFSVPSPGPLNTPVNPSSVMSPAGSSQAEEQQYLDKLKQLSKYIEPLRRMINKIDKNEDRKKDLSKMKSLLDILTDPSKRCPLKTLQKCEIALEKLKNDMAVPTPPPPPVLPTKQQDLCQPLLDAVLANIRSPVFNHSLYRTFVPAMMAIHGPPIVSPVVCSRKRRFEEDERQSIPNVLQGEVARLDPKFLVNLDPSHCSNNGTVHLICKLDDKDLPSVPPLELSVPADYPAQSPMWIDRQWQYDANPFLQSVHRCMTSRLLQLPDKHSVTALLNTWAQSIHQACLSAA", "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 cholesterol- dependent gene regulation. Positively regulates the Nodal signaling pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 15 family."}
{"protein": "MSRSETLFANAQKHIPGGVNSPVRAFKSVGGTPLFFKHAEGAYVTDEDDKRYVDYVGSWGPMILGHSHPDVLDAVRNQLQHGLSYGAPTAMETEMADLVCSLVPSLEMVRMVSSGTEATMSAIRLARGFTGRDSIIKFEGCYHGHSDSLLVKAGSGALTQGVPSSAGVPAAFAKHTLTLPFNDIDAVEKMLAEVGQDVACIIVEPVAGNMNCVPPAPGFLEGLRSLCDKHGVVLIFDEVMTGFRVALGGAQAYYGVTPDLTTFGKIIGGGMPVGCFGGKRLIMERIAPLGPVYQAGTLSGNPLAMAAGLTTLRLISRPGFHAELTDYTTRLLDGLQQRADAAGIPFVTTQAGGMFGLYFSGADDIVTFEDVMASDAALFGRFFHLMLEGGVYLAPSAFEAGFTSIAHGEAELKLTLDAAERAFAKLK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
{"protein": "MSTAASPAPAAPIRVAAGTTAGAAVRDAGLPGRGAPDAIVVVREADGRLRDLSWTPDADVEVVPVPADSEDGRSVIRHSAAHVLAQAVQDLFPEAKLGIGPPITDGFYYDFDVPRAFTPEDLEALEKKMRKIVKDGQLFERRVYESEEEARRELANEPYKLELVDDKSGDPEVMEVGGDELTAYDNLNPRTRERVWGDLCRGPHIPTTKYIPAFKLTRSSAAYWRGDQTNASLQRIYGTAWESQEALDRHLELIEEAQRRDHRKLGVELDLFSFPDELGSGLPVFHPKGGIVRKELEDYSRAKHLQAGYEFVNTPHITKEQLYVTSGHLEWYADGMFPAMHIDAEYDADGAVRKPGQNYYLKPMNCPMHHLIYRSRGRSYRELPLRLFEFGSVYRYEKSGVVHGLTRVRGMTQDDAHIYATREQMRDELTSLLQFVLDLLSDYGLDEYYLELSTKDPDKYVGSDEIWDEATETLREVAEASGLDLVPDPGGAAFYGPKISVQVKDALGRNWQMSTIQLDFNMPERFELEYTAADGSRQRPVLIHRALFGSIERFFGVLTEHYAGAFPAWLAPVQVVGIPVADAHIPYLEDVAAQLRSRGVRVEIDGSDDRMAKKIVNHTNQRVPFMLLAGDKDVAAGAVSFRFGDRTQINGVPRDEAVEAIVGWIVERRNTAPTADLVKAGAGT", "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": "MTREDLPDSTPEESKLPMEFQSPLLEKRRRPVVHPSAPAPLPKDYAFTFFDPNDPACQEILLDPQTSVPELFAIIRQWVPQVQHKIDIIGSEILKRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLTNQLLLLGADITLRSRWTNMNALHYAAYFDVPELLRTLLKASKPKVLNSTCSDFNHGTAMHIAASNLCLGAVKCLLEHGANPSARNSKSQVPADVVPDPMDMGLDKADSAMIAKELKQLLLDAVPLTCNLPKITLPNYDNIPGNLMLASLGLKLGDRILLDAEKAGTLRFCGTTEFASGQWVGVELDEPDGKNDGSVGGIRYFICPPKQGIFAPVSKISKAPDQPPSSVTSTPRTPRVDFSRVTGKGRKEKKATHKKSLSVGSLDREGLKIEIGDQVLVAGQKQGIVRFYGKTDFAPGYWFGIELEKPTGKHDGSVFGVRYFTCSAKNGVFAPPSRVQRMGGPKDPQTDNNDMKKVHQVTMTQPKRNFTKVRTPKEIASENSMSRILFCCWFPWLLRAEMKS", "text": "FUNCTION: Functions as a cytoplasmic linker protein. Involved in TGN- endosome dynamics (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack. Note=Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae."}
{"protein": "MTLQLNTIALLLVILLILGVLSNNSAITISAAVLLIMQQTFLSSHIPLLEKYGVKIGIIILTIGVLSPLVSGKIQLPDLSGFLSWKMALSIAVGVLVAWLAGKGVPLMGEQPILVTGLLIGTIIGVAFLGGIPVGPLIAAGILALLLGKI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0756 family."}
{"protein": "MKIGVFDSGVGGFSVLKSLLKARLFDEIIYYGDSARVPYGTKDPTTIKQFGLEALDFFKPHEIELLIVACNTASALALEEMQKYSKIPIVGVIEPSILAIKRQVEDKNAPILVLGTKATIQSNAYDNALKQQGYLNISHLATSLFVPLIEESILEGELLETCMHYYFTPLEILPEVIILGCTHFPLIAQKIEGYFMGHFALPTPPLLIHSGDAIVEYLQQKYALKNNACTFPKVEFHASGDVIWLERQAKEWLKL", "text": "FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family."}
{"protein": "MRIDQSIINEIKDKTDILDLVSEYVKLEKRGRNYIGLCPFHDEKTPSFTVSEDKQICHCFGCKKGGNVFQFTQEIKDISFVEAVKELGDRVNVAVDIEATQFNSNIQIASDDLQMIEMHELIQEFYYYALTKTVEGEQALTYLQERGFTDALIKERGIGFAPDSSHFCHDFLQKRGYDIELAYEAGLLSRNEENFSYYDRFRNRIMFPLKNAQGRIVGYSGRTYTGQEPKYLNSPETPIFQKRKLLYNLDKARKSIRKLDEIVLLEGFMDVIKSDTAGLKNVVATMGTQLSDEHITFIRKLTLNITLMFDGDFAGSEATLKTGQHLLQQGLNVFVIQLPSGMDPDEYIGKYGNDAFTAFVKNDKKSFAHYKVSILKDEIAHNDLSYERYLKELSHDISLMKSSILQQKALNDVAPFFNVSPEQLANEIQFNQAPANYYPDDEYGGYDEYGGYIEPEPIGMAQFDNLSRQEKAERAFLKHLMRDKDTFLNYYESVDKDNFTNQHFKYVFEVLHDFYAENDQYNISDAVQYVNSNELRETLISLEQYNLNDEPYENEIDDYVNVINEKGQETIESLNHKLREATRIGDVELQKYYLQQIVAKNKERM", "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": "MEFEVKKTFGKARLGVMKLHHGAVETPVFMPVGTNASVKLLTPRDLEEAGAEIILSNTFHLMLKPGVEIIKLHRGLHNFMGWKRPILTDSGGFQVFSLPKIRIDDEGVVFRSPIDGSKVFLNPEISMEVQIALGSDICMVFDHCPVPDADYEEVKEATERTYRWALRSKKAFKTENQALFGIVQGGIYPDLRRESALQLTSIGFDGYAIGGLSIGEERSLTLEMTEVTVEFLPEDKPRYFMGGGSPELILELVDRGVDMFDSVFPTRIARHGTALTWNGKLNLKASYNKRSLEPVDERCGCYTCKNFTRSYIHHLFDRGEVLGQILLTIHNINFMISLMKEVRRSIESGTFKELKSKVVEVYSSGGVNV", "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": "MPYRKYREKKYETKYREAFKVFQEKIGITFTDEKLLIQAFTHSSYVNEHRKKPHEDNERLEFLGDAVLELTVSQYLFQKYPTMSEGELTKLRAAIVCEPSLVRFANELSFGSLVLLGKGEEMTGGRERPALLADVFEAFIGALYLDQGLETVWGFLKEIVYPKINEGAFSHVMDYKSQLQELIQRDGSGNIEYQILQEKGPAHNREFVSRVTLNNVALGLGSGKSKKEAEQQAAAEALKKLKEQL", "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": "MQKATYYDNTAAALFGGYSSYPGSNGFGYDGPPQPPFQAATHLEGDYQRSACSLQSLGNAAPHAKSKELNGSCMRPGLAPEPLPAPPGSPPPSAAPTSTTSNSNNGGGPSKSGPPKCGAGSNSTLTKQIFPWMKESRQTSKLKNSSPGTAEGCGGGGGGGGGGGGGGGGSSGGGGGGGGGGDKSPPGSAASKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLSERQIKIWFQNRRMKYKKDQKAKGLASSSGGPSPAGSPPQPMQSTAGFMNALHSMTPSYDSPSPPAFGKGHQNAYALPSNYQPPLKGCGAPQKYPPTPASEYEPHVLQANGGAYGTPTMQGSPVYVGGGGYADPLPPPAGPSLYGLNHLSHHPSGNLDYNGAAPMGPNQHHGPCDPHPTYTDLSSHHAPPQGRIQEAPKLTHL", "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": "MNNNLQGDAIAAAIDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKPYIDDTMLTDAQRETIFSRWPGPVTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVDEVRAQFGAAFPVVPGETGGRLNPSEIRDALTGELFRQG", "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": "MRVSQSLIPFAIIALVLSFVNAYDPSPLQDFCVAIDDLKGVFVNGRFCKDPERVDAKDFFFSGLNVPGNTNNQVGSNVTTVNVDQIPGLNTMGISLVRIDYAPHGQNPPHTHPRGSEILVLVEGTLYVGFVSSNQDNNRLFAKVLHPGDVFVFPIGMIHFQLNIGKIPAIAFAGLSSQNAGVITIANTVFGSNPPIYPELLARAFQLDANVVKELQAKFGSI", "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": "MMQRDRWFRCRLSSYQTHRLPPPSEDSVPIATMERTPGLLECEHLNMHYVSEVRSIPSCAPFVVLQEWPMWWDMILSKWEKHVCKIYMRVCVCCATINVDFNQIVRGFERWTIHCHCIKPGSLQCKAGGVVLANWFKMMIYGSLYNLRFPWYREIVNCGMPKEVLFMGSVFVRGRHFIYIRLLYDGHAAIVLERMSFGWSFFSYGIMNNMVVLGCTYCKNLDELSVRCCARRTRRLLAKAVKVLGSFTVRSLMRSLVEPRRQGLLRGLMERYCPFTLADYNRGENPWRA", "text": "SIMILARITY: Belongs to the adenoviridae E4 30 to 34 kDa protein family."}
{"protein": "MSTAVTILTDTWTRREKRFDGHAKILAIGTAIPANWVDQTTYPDFYFRITNSEHLLEYKEKFRRICNKSKIRKRHLVITEELLKKNPNLCTYNDASLNTRQDILVSEVPKLGKEAAMKAIKEWGRPISEITHLVFCTSSGVDMPGADFQLAKLLGLSSSVNRLMMYQQGCNAGAVMLRLAKDLAENNKGGRVLVVCSEVMLSVFRGPSLQQEDNLLAQCLFGDGSAAVIVGTEPRPGLETPLFELVSAAQTTIPDTDSYLKLQLREMGLTFHCSKAVPSLITQNIEDCLVKAFEPFGISDWNSIFWILHPGGNAILDGVEEKLGLEPEKLRASRDVLSQYGNLTSACVLFKP", "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": "MYEYIKGEYMGINKDYIIIENNGIGYKIFTSGATMSSMPCCGEKIKIYIEQIVREDFIGLYGFESLEELDMFKLLLSINGVGAKAALSLLSISRLNNLKYAIITGDEKHLCRGTGIGKKIAGRIILELKDKLKSDELLNCIDEFDDVTQDNSLALSEALSALISLGYTEKEAEKVLKDVDKSESVENIIKSALVKLMG", "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": "MNPTAIFDYLQGLQTRIVEAIELVDGKRFLHDSWQRAEGGGGTSCMLEEGNVFERAGIGFSHVIGNKLPPSASVAHPEAAGRSWQAMGVSLVFHPRNPYVPTVHMNVRFFVAEKPGEEPIWWFGGGMDLTPYYGFEEDAVHFHRTCRDAVAPFGEQYYPRFKKECDDYFYLKHRKEARGIGGIFFDDFNELGFEQSFAFQRSVGDAFINAYLPIVQRRKDIPYSERERDFQAYRRGRYVEFNLIYDRGTIFGLQSNGRTESILLSMPPIVKWRYDWKPEAGSPEARLYSDFITGRDWLTEHK", "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": "MRGAGRQMGRDSRSRSRSVGRRGRKQRSRSRGRSRSRSRSRSRSRSRSRSRSRSHGRSSRRRREHERRRERKRRSRGRRSDSEGEQRQKSRRRSQSLRPPRWHSQNQSSCSDSGEERAQGSWARKGHRRSWSPGSSASSLDSPRRSRSPGTATLALSQQQSLQERLRLREERKQQEELLKAFETPEEKRARRLAKKEAKERKKREKMGWGEEYMGYTNTDNPFGDNNLLGTFIWNKALEKKGISHLEEKELKERNKRIQEDNRLELQKVKQLRLEREREKAMREQELELLQREKEAEHFKTWEEQEDSFHLRQAKLRSKIRIRDGRAKPIDLLAKYISAEDDDLAVEMHEPYTFLNGLTVADMEDLLEDIQVYMELEQGKNVDFWRDMTTITEDEIAKLRKLEASGKGPGERREGVNASVSSDVQSVFKGKTYNQLQVIFQGIEGKIRAGGPNLDMGYWESLLQQLRAHMARARLRERHQDVLRQKLFKLKQEQGVESEPLFPILKSEPSAAHSPEPEERPPSPGTSVDPVEPVEPEEATAPGEAEGEAEGEAVLMEEDLIQQSLADYDAGRYSPRLLTAHELPLDAHVLEPHEDLQRLQLSRQQLQATGDASESAEDIFFRRAREGMGQDEAQFSVEMPLGGRAYLWADKYRPRKPRFFNRVHTGFEWNKYNQTHYDFDNPPPKIVQGYKFNIFYPDLIRKRATPEYFLEACADNRDFAILRFHAGPPYEDIAFKIVSREWEYSHRHGFRCQFANGIFQLWFHFKRYRYRR", "text": "FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Required for the splicing of CDCA5/Sororin, a regulator of sister chromatid cohesion (By similarity). Involved in the regulation of innate immune response (By similarity). Acts as negative regulator of Toll-like receptor, interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling pathways (By similarity). Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with NFKBIL1 in the nucleus (By similarity). SIMILARITY: Belongs to the CACTIN family."}
{"protein": "MSLFDLKLKDVHTKLHEKEISVSDLVDEAYKRIEQVDGQVEAFLALNEEKARAYAKELDAALDRSEARGLLFGIPIGVKDNIVTKNLRTTCSSRILGNFDPIYDATVVHKLREAQAVTIGKLNMDEFAMGSSTENSAFQKTKNPWNLEYVPGGSSGGSAAAVAAGEVPFTLGSDTGGSIRQPAAYCGVVGLKPTYGRVSRYGLVAFASSLDQIGPITRNVEDNAYLLQAISGHDPMDSTSANLDVPDYLSALTGDIKGLKIAVPKEYLGEGVKEEVKQSVLDALKVLEGLGATWEEVSLPHSKYALATYYLLASSEASANLARFDGVRYGFRSDNADNLLDMYKQTRAEGFGDEVKRRIMLGTFALSSGYYDAYYKKAQQVRTLIKQDFEKVFEQYDVIIGPTTPTPAFKIGEKTDDPLTMYANDILTIPVNLAGVPAISVPCGFDNGLPLGLQIIGKHFDEGSVYRVAHAFEQATDYHTKRPTL", "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": "MSEFKRLMRLKLKMKQKRPEFKRQDSHRFQRIGTMWRRPTGHHSGQRIQVTYRLSPVKIGFRGPALVRGLHPSGLEDIIVNNVKQLAALNPKTQGARIASAVGTRKRIEIVKKANELGIRVFNVSKQKQGEFLSL", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family."}
{"protein": "MRLSELTHPNQLHGLSIAELEDVARQIRERHLEVVSTSGGHLGPGLGVVELTLALYQTLDLDHDRVVWDVGHQAYPHKLITGRYGDFNTLRQQGGVAGYLKRCESSFDHFGAGHASTSISAALGMAVARERRGESFKCVAVIGDGALTGGIALEAINHAGHMPNTPFLVVLNDNDMSISPPVGALSTHLNRMRHSAPVQFISDSVEERVKSLPFMGGELPAELDLLKGSMRRLSVPKVGAVFEELGFTYMGPIDGHDIERMVRTFETAHKVGGPVLVHVVTTKGKGYPYAEADQVGYHAQSAFDLITGKALPSKGKKPPSYSKVFGETLIKLCQQDSTVVGITAAMATGTGLDLLQKAVPEQYIDVGIAEQHAVTLAAGMACEGLKPVLAIYSTFLQRAFDQLIHDVGIQNLPVTFVMDRAGIVGADGPTHQGQYDISYFRAIPNFTVMAPKDEAELQRMLVTCLQHQGPAALRIPRGSGEGVPLLDEGWEPLAIGRGEVLCEGDDLLIVAYGVMVPAAMITAQLLQEAGVKATVINARFLRPLDQALIHPLARRIGRVVTMEEGALAGGFGAAVVESLSDQDVLVPTFRIGIPDQLVDHASPQQSREALGLTPTQMSERIQEHFCLNSQPSLVGQEAPQALST", "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": "MADITRLKGELRTEFGKGASRRLRRDFRVPAVVYGNDLDPMHVHVDILEFQAILRNEGVNAVLELEIEGQDHLVMIKAVDQNVLTLDVDHADLLNVKRGEKVEVDVPVIFTGQAAPGALVTQEADVITILADVLNIPEEITVDVEGKEIGDQVLAGDLQMPGNASLVSEEDTLIINVVEPEEEELPETDEEGEGAEGEAAEAAEGESAEGESEE", "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": "MKGIVLAGGAGTRLHPITRGVSKQLLPVYDKPMIYYPISVLMLAGIQDILIISTPEDLPSFKRLLGDGSQFGIRLQYAKQPSPDGLAQAFIIGEEFIAGERCALVLGDNIYFGQSFGKQLREVASRNDGATVFGYQVVDAERFGVIEFDENFNALSIEEKPQKPKSDWAVTGLYFYDKDVVEMAKEIKPSERGELEITTLNEMYLAKGKLRVELLGRGFAWLDTGTHDSLIDASLFIHTIEKRQGFKVACLEEIAYQNQWLSREKLNELAEALNKTYYGQYLLKLAKES", "text": "FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family."}
{"protein": "MSRFWSPFVKDLVPYVPGEQPKLARLVKLNTNENPYGPSPKALEAMRGELNDNLRLYPDPNGDRLKQAVAEYYGVTTGQVFVGNGSDEVLAHIFHGLFQHGGPLLFPDISYSFYPVYCGLYGIPFEPVALDEQFQIRVEDYQKPNAGIIFPNPNAPTGCLLPLQAIEQLLQANRDSVVVVDEAYIDFGGQTAISLVDRYDNLLVTQTLSKSRSLAGLRVGLAVGHPDLIEALERIKNSFNSYPLDRMAIVGAAAAFEDQAYFEATCRKVIDSREALVEQLTAKGFEVLPSAANFIFARHPQEDAAQLAARLREQGVIVRHFKQQRIAQFLRITIGTPEMNQALIDALS", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
{"protein": "MGQAAAITMPIDPRNLNTLWSSVLAESFVRLGLQTVVICPGSRSAPLAIAFAEHPEIDAIPILDERSAGFFALGRAKASHRPVALICSSGTAGANFYPAVIEAKESGVPLLVITADRPPELRQCHAGQAIDQLRLFGSYALWEAELALPVLDLGLLRYLRQTAQQAWQQALRGGPVHLNQPLREPLAPIADPATQTWLAQQWPGENFFAELLTAVPTPQIQQPLPPLPSQGLITVGPIAPEDPAAFVQAIAQLSAHLGWPVLSDAVTPLRQFADHCPRLISSYDLILRQPHWRASLQPEAVLQIGELPTSKELRLWLTEQTCPRWIVSPRPENFDPLHGSSHHLPVTVEAIAIPATIAPASDYSRQWQQAETAVQAAIAQHLAQVPDLTEPGIARLLSQHLPAQTPIFVANSTPIRDLEWFWLANDQRRSLYCSRGANGIDGTLSTAIGIAHQNRPSVLITGDLSLLHDSNGFLQRSQLQGHLTVVLIDNSGGGIFELLPIRDCGPSFEPFVATPQTVDFAALCQAYGVDYQAIATEAELIKAIQTLPTSGIRVLHLFTDRRQNAAWRRALFAELAAIPSQS", "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": "MTDKLATLQSALEKALGNRIQSLTEAVGEITLVVKAADYLETMRTLRDDATLKFEQLIDLCGVDYSAYGDGAWNGPRFAAVSHLLSVTHNWRVRVRVFAPDDDLPVVASVVDVWNAADWFEREAFDLYGLVFEGHPDLRRILTDYGFIGHPFRKDFPVSGYVEMRYDPVQRRVIYQPVTIEPREITPRVIREDQYGGLKH", "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": "MNLSLCIASPLLTKSSRPTALSAIHTASTSHGGQTNPTNLIIDTTKERIQKLFKNVEISVSSYDTAWVAMVPSPNSPKSPCFPECLNWLINNQLNDGSWGLVNHTHNHNHPLLKDSLSSTLACIVALKRWNVGEDQINKGLSFIESNLASATDKSQPSPIGFDIIFPGLLEYAKNLDINLLSKQTDFSLMLHKRELEQKRCHSNEIDGYLAYISEGLGNLYDWNMVKKYQMKNGSVFNSPSATAAAFINHQNPGCLNYLNSLLDKFGNAVPTVYPLDLYIRLSMVDTIERLGISHHFRVEIKNVLDETYRCWVERDEQIFMDVVTCALAFRLLRIHGYKVSPDQLAEITNELAFKDEYAALETYHASQILYQEDLSSGKQILKSADFLKGILSTDSNRLSKLIHKEVENALKFPINTGLERINTRRNIQLYNVDNTRILKTTYHSSNISNTYYLRLAVEDFYTCQSIYREELKGLERWVVQNKLDQLKFARQKTAYCYFSVAATLSSPELSDARISWAKNGILTTVVDDFFDIGGTIDELTNLIQCVEKWNVDVDKDCCSEHVRILFLALKDAICWIGDEAFKWQARDVTSHVIQTWLELMNSMLREAIWTRDAYVPTLNEYMENAYVSFALGPIVKPAIYFVGPKLSEEIVESSEYHNLFKLMSTQGRLLNDIHSFKREFKEGKLNAVALHLSNGESGKVEEEVVEEMMMMIKNKRKELMKLIFEENGSIVPRACKDAFWNMCHVLNFFYANDDGFTGNTILDTVKDIIYNPLVLVNENEEQR", "text": "FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones (PubMed:10504563). Catalyzes the conversion of ent- copalyl diphosphate (ent-CPP) to ent-kaurene (PubMed:10504563). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MSELNMTPREIVAYLDEYIIGQKEAKKSIAIAFRNRYRRLQLEKSLQEEITPKNILMIGSTGVGKTEIARRIAKIMKLPFVKVEASKYTEVGFVGRDVESMVRDLVNNSVLLVENEHKEKLKDKIEEAVIEKIAKKLLPPLPNGVSEEKKQEYANSLLKMQQRIVQGELDSREIEIEVRKKSIEIDSNVPPEILRVQENVIKFFHKEQDKVKKTLSVKEAKEALKAEISDTLLDGEAIKMEGLKRAESSGVIFIDEIDKIAVSSKEGGRQDPSKEGVQRDLLPIVEGSVVNTKYGPIKTEHILFIAAGAFHLSKPSDLIPELQGRFPLRVELESLTEEIMYMILTQTKTSIIKQYQALLKVEGVGIAFEDNAIKELAKLSYNANQKSEDIGARRLHTTIEKVLEDISFEAENYSGQNVTITKELVQSKLEDLVADENLVKYIL", "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": "MPNILSLTCICFNSVLCPTSFFFAKLPEAYAIFNPIVDVMPVIPVLFFLLAFVWQAAVSFR", "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": "MAFRPLHDRILVRRVESEEKTKGGIIIPDTAKEKPQEGEVLAVGPGARGEQGQIQPLDVKVGDRILFGKWSGTEIKIDGEDLLIMKESDVMGIIEARAAEKIAA", "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": "MQYLTQEQAIKLDEELMGKYKYSLVQLMEIAGLAVAQVVTKEYPIEKGNKRVLILCGPGNNGGDGLVCGRYLSLFGYEVTVFYPKQSKNEHLQLLIKQLEIQDIPVVTELSSFEYDAIVDAVFGFSFKGPVRGIFKDIFSHINSLKVPIISVDIPSGWDVEQGYLQDGIQRCDVLISLSAPKLGVKNFKGIHYLGGRFIPLELKDKLHLILPYKENELIVKIN", "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": "MATVNQLVRKPRVRKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKNAKA", "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": "MKLLIAGGGTGGHLFPGIAVAEEFLARDKQNEVLFVGTWKGIEARVLPKTGYRLECITAAGIRGKGSLARAKGLAKFLYGYAQSRKILKEFRPDLVLGVGGYASAPTLMAARGMQIPRFIHEQNAIPGFTNRMLAKVADKIFISLEESRTYFPEDKTLLTGNPLRRQILEQVALAESRERGDDAFHLLVFGGSAGAHRINLTMGEALPSLKEAKGRLRITHQTGENDLEDVTAAYEEQGFTADVVAFIDSMADAYRWADLIVCRAGATTLAEVTACGKPCIFIPYPHAVDDHQRRNAESLLKRGAGFVIIEQELSGEVLAQAIRDLMDDPARLKAVGEAAQELARLDAAQAIVDEMVASTRKEE", "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": "MASPFSGALQLTDLDDFIGPSQECIKPVKVEKRAGSGVAKIRIEDDGSYFQINQDGGTRRLEKAKVSLNDCLACSGCITSAETVLITQQSHEELKKVLDANKMVAPSQQRLVVVSVSPQSRASLAARFQLNPTDTARKLTSFFKKIGVHFVFDTAFSRHFSLLESQREFVRRFRGQADCKQALPLLASACPGWICYAEKTHGSFILPHISTARSPQQVMGSLVKDFFAQQQHLTPDKIYHVTVMPCYDKKLEASRPDFFNQEHQTRDVDCVLTTGEVFRLLEEEGVSLPDLEPAPLDSLCSGASAEEPTSHRGGGSGGYLEHVFRHAARELFGIHVAEVTYKPLRNKDFQEVTLEKEGQVLLHLAMAYGFRNIQNLVQRLKRGRCPYHYVEVMACPSGCLNGGGQLQAPDRPSRELLQHVERLYGMVRAEAPEDAPGVQELYTHWLQGTDSECAGRLLHTQYHAVEKASTGLGIRW", "text": "FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect (By similarity). SIMILARITY: Belongs to the NARF family."}
{"protein": "MFLPQEFIRRKRDGQPLDRDGMAAFVRGVTDGSVTEGQVAAFAMAVYFNDLSTDERVALTLAQRDSGDVLDWRALGLGGPVIDKHSTGGVGDVVSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLSAIPGYDVMPDTDAFRRTVREVGVAIIGQTARLAPADKRIYAIRDVTATVESVAMITASILSKKLAAGLDGLVMDVKVGSGAFMPTAEKSAELARSIVDVGNGAGMKTTAILTDMNQSLAPCAGNALEVACAIDYLTGKSRPARLHDVTMALSAELLVTGGLARDAAHAREKLQQALDSGAAAERFARMVVALGGPADLLDAPARHLARAAVIVPVPAPASGVVQRVDCRALGLAVVALGGGRTRAEDAIDVSVGLSALAEIGQRIESGEPLGFVHARDEAAAAHAADAIRRGYVLGDTGEAPPTLYRQIG", "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": "MNFFCKEKRQAYVELMRINKPIGTLLLLWPTLWALWIAAQGFPDLGVLIVFSAGVFLMRSAGCVINDFADRNIDGFVERTKHRPLPSGRATSTEAIILFFILAIVSFLLVLTQNSLTIQLSFAGLLLAFAYPFMKRFTQLPQLVLGLAFSWSIPMAFAAQANALPAVVWIIFAVNIIWTIAYDTLYAMVDREDDLKIGVKSTAILFASNDKIIIALLQLTSLILLSLLGWLEDLNWIYFIALLVVGGLFLRQQLQIKNREKTACFKAFLDNNYVGFVIFAGLFLGYL", "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": "MQIELEKILNQNREKIAFGNLPTYIPELTRANKDALGIYISQLDGSEFKAGDYDYKFTIQSISKVITLIMALEDWGAEYIFECVGKEPTGDAFNSMMKLEIVRPSKPFNPMINAGAIAVTSKIKGKSPEERIQRIMDFFKLVTGNPDLKVNESIYMSEKSTGDRNRAMAYFMKDVGVITGDVEENLDLYFKQCSIEVTCKDIARIGLFLSSDGVLLETGKQIINPKHSKIAKALMTTCGMYNASGEFAINVGIPAKSGVGGGIMAVVPGKMGIGVIGPSLDEKGNSIAGVGVLEQLSKMLELSIF", "text": "SIMILARITY: Belongs to the glutaminase family."}
{"protein": "MTDVVPDSNAPAYSVSELAFALKRTLETSYAFVRLRGELSKVTHHGNGHVYLTIKDDKSAIDGVVWKGNVRGLGIRPEHGLEVIVTGKITTYPAGSRYQIVIETMEAAGVGALLAQLERLKAKLNAEGLFAPDRKRPLPSMPAVVGVITSPTGAVIRDILHRIRDRWPCQVLVWPCVVQGDAAAGQVSAAIRGFNALTPGGPVPRPDILIVARGGGSVEDLWAFNDEGLARTVAEGTIPLISAVGHETDTTLIDFVSDRRAPTPTAAAEMATPVLAELRALVSDYDRRLNNCGGRAVEERRTRLTSAARGLPRPADLLALAQQRLDLAVRGLPRLDDLTAPAERRFKEAAARLDTALQRNTDIHARDLLKVTARLSPDTLHRQRADAGRRVGDLGRRLDLAARRVPERVAQHARLPALQDRLNAVARRRLERETDRLAGLEKLRQSLNPTRPLELGFALVHKADGGIARSASELASGERVRLQFRQGDRDAVIDGESSGVLPPSAAPAPTRPTPRPKPASSSDQGSLF", "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": "MIYQGESIRVDFIEPGFAELQFDAKGSVNKFDQATLEEFSEALTKLQNTDDLRGVIVTSSKSTFIVGADITEFLTLFSDQEKTRSWVAKASRVFDQLEDLPVPTVGAVTGFALGGGCEALLACDYRVADTTATIGLPEVKLGLIPGFGGTMRLPRVIGPDNALEWITTGKNNKALDALKVGAVDAVVEPENLTKAALNLAKAAAAGQQDWKAKRQPKLEPLKANDTELMMTLVTAKGMIAAKAGKHYPAPHKALEAIENGAREHREGALTAENNAFFDLTQTEACQAQVGIFLADQAVKGKSKKYAKAATKEIKTAGVLGAGIMGGGIAYQSALKGVPAVMKDIKQDALDLGMKEAGKILKKGVERGKVNNEKMIKILSSITPTLLNDAVKDVDIVVEAVVENPKVKGSVLAEIEGVIGDDAILTSNTSTISITELAKNLKRPEKFCGMHFFNPVHKMPLVEIIRGEKTSDDTVNAVVAYALKLGKTPIVVNDCPGFLVNRVLFPYLAGFAGMVDEGVDFVGIDKVMEKQFGWPMGPAYLSDVVGIDTADHCTVVMEAGFPTRMKRDESSAIAKLAAAERYGQKNGKGFYVYGTDKKGKPTKEADPATYELLGCEQGKKLDADEVIARCMIPMVNEVVRCLEEDIVGSAAEADMALLYGLGFPPFRGGPFRYLETLGMDNFIQLADKYAHLGEIYQVTDGMREMAKAGKSYFDTTSAK", "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": "MAATPVRTRFAPSPTGYLHIGGARTALFSWAYARRHGGRFILRIEDTDVARSTPEAVQAILDGMKWLGLEHDEGPFYQMQRMDRYKEVIQQMLAAGTAYYCYTSKEELDALRAEQEAKKEKPRYDGRWRPAPGKTLPTPPAGVQPVVRFCNPTTGVVAWDDLVKGRIEISNTELDDFIIARADGTPTYNFCVVVDDWDMGITQVIRGDDHVNNTPRQINVLQALGASVPQYAHLSMILGDDGTKLSKRHGAVSVMQYDDEGYLPEAVINYLARLGWSHGDDEIFSREQFVEWFDLDHITPSAAQFNTEKLNWLNAHYIKQADNAYLAAEVANRLARRGVDPEAGPALEQVVALYKDRSANLNELADAAELFCVDVHAAPEVIAQHLTDTARAALASLRARFEAVAWDKAALNQAIKDTMAEHGLKMPQVAIPLRVALLGVPQTPSIDAVVEVLGRERVLARLARHLG", "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": "MAHKKAGGSSRNGRDSDGRRLGVKRFGGQDVIPGNIIVRQRGTKWHPGTNVGMGKDHTLFALVEGKVTFQTKANDRTYVSVLPLAAEAAE", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MPREDAHFIYGYPKKGHGHSYTTAEEAAGIGILTVILGVLLLIGCWYCRRRNGYRALMDKSLHVGTQCALTRRCPQEGFDHRDSKVSLQEKNCEPVVPNAPPAYEKLSAEQSPPPYSP", "text": "FUNCTION: Involved in melanosome biogenesis by ensuring the stability of GPR143. Plays a vital role in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is critical to the formation of stage II melanosomes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein. Golgi apparatus. Golgi apparatus, trans-Golgi network membrane. Melanosome. Note=Also found in small vesicles and tubules dispersed over the entire cytoplasm. A small fraction of the protein is inserted into the membrane in an inverted orientation. Inversion of membrane topology results in the relocalization of the protein from a predominant Golgi/post-Golgi area to the endoplasmic reticulum. Melanoma cells expressing the protein with an inverted membrane topology are more effectively recognized by specific cytolytic T-lymphocytes than those expressing the protein in its native membrane orientation."}
{"protein": "MTKETETTCSFCGKSQDEVGKLIAGVDGYICGECIDLCHDLLHDEETREQQSAEEAVETEEKLPTPHEIRAHLDDYVIGQDYAKKVLAVAVYNHYKRLRSNHGIADVELGKSNILLIGPTGSGKTLLAETMARMLNVPFAMADATTLTEAGYVGEDVENVIQKLLQNCDYDTEKAQRGIIYIDEIDKITRKSENPSITRDVSGEGVQQALLKLIEGTVASIPPQGGRKHPQQEMLRVDTSKILFICGGAFAGLDRVVQKRIHKGSGIGFDAEVKGKEDEVSLTDLLKQIETEDLIKYGLIPEFIGRLPVVAPLSELDEKALVQILTEPKNALTKQYQALFGLENVELEFTPEALNAMAKKALERKTGARGLRSIVEGALLDTMYDLPSLEGLVKVVVDEAVINEHSAPKLEY", "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": "MSQIDKASRRQKIKDRSRKQVHGNEKKPRLCVYRSLSQIYAQLIDDDNGKTIMSVSSMSKENRALEGTKCDVCRIVGLQLGEKAKAQGITKVIFDRNGFRYHGRVKALADGAREAGLVF", "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": "MQSYDIAQFIDHTALTAEKTEQDILDLCNEAIEHNFFSVCINSGYIPLARQKLQNTNVKICTVVGFPLGANLSTVKAFEAKEAIKAGATEIDMVINIGWIKSNQWESVKADIQAVLAACEGALLKVILETCLLTKEEIITACKICRELGVGFVKTSTGFNKGGATVENIALMRQVVGENIGVKASGGVRDTKTAIEMIKNGATRIGSSSGIAIINGLTDNNAIY", "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": "MLDVHKDIKKIFHEEQVLAEAAARYGFSKDQVRFLADAENYVYECMKDNQPYILKITHTIRRSSDYMMGEMEWLRHLAIGGISVAKPLPSLNGKDVEAVPDGNGGSFLLRVYEKAPGQKVDESDWNETLFYELGRYTGSMHSLTKSYKLSNPAFKRQEWDEEEQLKLRKYVPEDQIKVFQQADSLMNELRRLPKSQDNYGLVHADLHHGNFNWDHGKITAFDFDDIGYNWFVNDISILLYNVLWYPVVPYDDKAAFTEEFMTHFMKGYWEENELDPAWLMIIPDFLRLRHMLIYGLLHQMFDLNTIGEEEKEMLAGFRRDIENGTPITAFDFSALV", "text": "FUNCTION: Phosphorylates the antibiotic amicoumacin A (Ami), leading to its inactivation. Mediates natural B.subtilis resistance to the drug. SIMILARITY: Belongs to the pseudomonas-type ThrB family."}
{"protein": "MSQSLLDRFGTPLERVHLAIDRLRQGRGVLLVDDENRENEGDLIFPAETITPAQMAMMIRECSGIVCLCLTEDKLKQLELPQMVSDNTSANQTAFTLSIEARQGVTTGVSAADRVTTIRTAVADDCRPDDLARPGHVFPLRARPGGVLTRRGHTEGTVDLMRMAGYKPAGVLCELTNEDGTMARLPEIITFAERHYLSVVSIEDLALALESHMEKSA", "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": "MLEKGTQSLVNRTIKLRVLGGLTKKLAAPQNESLPELKPQLDVYQKFLENLRAFPTKNKSVPNSPIRYSYYKIANKESEAVNRNLLELFASKKYLPFLASEIPKLPPPYVAAAAPMNPKISVTQLLTDSWCELRSYYDSYACSRAAPSAAMVSGTEQHKSLEDRTHKPEINVTKEIQKNFTPIMMDQLKNFERTLNLISRFIDLLTIGKAREFAVTAIINKETKELIDVNNLQKLAFVHQKSPCYNDQFILASGYLDYLRSESYVNGLEKEKWIQNNYSLNTLLETSIKGPLTVIDVKTRGKPIVTKSKGVLIGHRYQIGLYRKFLGLMSGENVSGINSPISVDQINETAYTLLVTDSVQRGYDVDEPVDPVVGLVMLANNPWIITMLEQICVNDLLGNSLYDTFHAQQSTDYSWDLSQVNPKDFYQVLEPSLLQRTEQLFTKWKRPLSLRSITALISKFYPLISKKLSQNTKIMYYTDGECFHTSNYLYNPKAINTFMEDKVKFLIGQRPPRPIEKSEIPQKCGFCRFQSICEYSNLYNPVT", "text": "FUNCTION: Single strand DNA specific 5'exonuclease involved in mitochondrial DNA replication and recombination. Releases dinucleotides as main products of catalysis. Has the capacity to slide across 5'double-stranded DNA or 5'RNA sequences and resumes cutting two nucleotides downstream of the double-stranded-to-single-stranded junction or RNA-to-DNA junction, respectively (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the EXO5 family."}
{"protein": "MMAAGTALGLALWLLLPPVGVGGAGPPPIQDGEFTFLLPAGRKQCFYQSAPANASLETEYQVIGGAGLDVDFSLESPQGVLLVSESRKADGVHTVEPTEAGDYKLCFDNSFSTISEKLVFFELIFDSLQDEEEVEGWAEAVEPEEILEVKMEDIKESIETMRIRLERSIQVLTLLRAFEARDRNLQEGNLERVNFWSAVNVAVLLLVAVLQVCTLKRFFQDKRPVPM", "text": "FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side. Plays a positive role in IL-33-mediated IL-8 and IL-6 production by interacting with interleukin-33 receptor IL1RL1. Plays also a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMP24/GP25L family."}
{"protein": "MAFKIASSPHVTRNLHTSTVMQRVILCLLPGLVVQCAFFGWGTLVQVLLAILVALSCEAAVMKLRNRNIKASLSDNSAMLTAILIGVAIPPLAPWWMIVMGTAFAIVIVKHLYGGLGHNLFNPAMAAYVLLLVSFPVQMTTWIAPSTVALHSPSLVESLQLIFNVGAHVNMEQFRLGIDGMTMATPLDTLKTDLSMGLTTTESLTKAIFDGSTGVGWFWVNLAYLAGGLVLLKLKAIRWHISTGVLLGLFVASSIGFLLSPDTQASPLMHLFSGATMLAAFFIATDPVTAATSPRGRIIFGALIGVLVYIIRTKGGYPDAFAFAVLLANLCAPFIDYYVRPRTYGHSTS", "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": "MDKTQSRLRRARQTRIKIAELQVARLAVHRTNTHIYAQVFSPCGTKVLASASTLEAEVRAELADKSGKGGNVNAATLIGKRIAEKAKAAGIESVAFDRSGFRYHGRVKALAEAAREAGLKF", "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": "MPRYTVHVRGEWLAVPCQDGKLSVGWLGREAVRRYMKNKPDNGGFTSVDEVRFLVRRCKGLGLLDNEDLLEVALEDNEFVEVVIEGDVMSPDFIPSQPEGVFLYSKYREPEKYIALDGDSLSTEDLVNLGKGHYKIKLTSIAEKKVQQSREVIDSIIKERTVVYGITTGFGKFARTVIPANKLQELQVNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLETLKQVIEVFNASCLSYVPEKGTVGASGDLAPLSHLALGLIGEGKMWSPKSGWADAKYVLEAHGLKPIVLKPKEGLALINGTQMITSLGCEAVERASAIARQADIVAALTLEVLKGTTKAFDTDIHAVRPHRGQIEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKDIITTELNSATDNPMVFASRGETISGGNFHGEYPAKALDYLAIGVHELAAISERRIERLCNPSLSELPAFLVAEGGLNSGFMIAHCTAAALVSESKALCHPSSVDSLSTSAATEDHVSMGGWAARKALRVIEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDIEAAHRLLLDQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLESLRKNSATIPESDDL", "text": "SIMILARITY: Belongs to the PAL/histidase family."}
{"protein": "MGKAKVPASKRAPSSPVAKPGPVKTLTRKKNKKKKRFWKSKAREVSKKPASGPGAVVRPPKAPEDFSQNWKALQEWLLKQKSQAPEKPLVISQMGSKKKPKIIQQNKKETSPQVKGEEMPAGKDQEASRGSVPSGSKMDRRAPVPRTKASGTEHNKKGTKERTNGDIVPERGDIEHKKRKAKEAAPAPPTEEDIWFDDVDPADIEAAIGPEAAKIARKQLGQSEGSVSLSLVKEQAFGGLTRALALDCEMVGVGPKGEESMAARVSIVNQYGKCVYDKYVKPTEPVTDYRTAVSGIRPENLKQGEELEVVQKEVAEMLKGRILVGHALHNDLKVLFLDHPKKKIRDTQKYKPFKSQVKSGRPSLRLLSEKILGLQVQQAEHCSIQDAQAAMRLYVMVKKEWESMARDRRPLLTAPDHCSDDA", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the REXO4 family."}
{"protein": "MAASMRALLKVRDGFVAGVRCNSQYNKTRGNLKLNGDSRVICQGFTGKQGTFHSQQALEYGTKLVGGISPKKGGTQHLGLPVFASVAEAKKATDPHATVIYVPPPGAAAAIIEALEAEIPLIVCITEGVPQHDMVKVKHALISQSKSRLVGPNCPGIIAPEQCKIGIMPGHIHKRGKIGVVSRSGTLTYEAVHQTTEVGLGQTLCVGIGGDPFNGTDFIDCLEVFLKDPETKGIILIGEIGGVAEEKAADYLTEYNSGIKAKPVVSFIAGVSAPPGRRMGHAGAIISGGKGGANDKIAALEKAGVIVTRSPAKMGHELFKEMKRLELV", "text": "FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
{"protein": "MIDDAAPPYVGRFAPSPSGPLHFGSLVAAVGSFLDARAHHGQWRLRIEDVDTPRTVPGAAQDILATLERFGFEWDGKPVWQSARLDAYRDAFERLRAAGQVFPCACTRREMADSALARDGSRLYPGTCRNGLPPGRSAHAWRVRAHGRIAFADRIQGPQEEDLATEVGDYVVLRGDGQFAYQLAVVVDDAAAGVTDIVRGADLLGSTGRQIHLQHLLGYPTPAYAHLPVVVNTAGEKLSKQTLAAPVAALPPARALFAALTFLGQNPPPALGRASLRETWKWAVTHWSLVDVPRQLQAEAPGAFSARARENPSSL", "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": "MSFHKEDGVNSLCQKALHIVTELCFAGQVEWEKCSGIFPRDRGSQGGSSTDISVSLLAVVVSFCGLALLVVSLFVFWKLCWPCWKSKPVTSNITTLPQSISSAPTEVFETEEKKEIKENEKPAVKAIEPAIKISHTSPDIPAEVQTALKEHLIKHARVQRQITEPTSSTRHSSFRRHLPRQMQVSSVDFSMGTEPVLQRGETTTSIGRIKPELYKQKSVDSEGNQNEDVKICGKLNFTLQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKMYLLPDRKKKFQTRVHRKTLNPLFDETFQFPVAYDQLSNRKLHFSVYDFDRFSRHDMIGEVILDNLFEVSDLSREATVWKDIHCATTESIDLGEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLSIAVMDYDRVGHNEVIGVCRTGLDAEGLGRDHWNEMLAYHRKPITHWHPLLELPGRATSFDSQGSCPSPKPPSTP", "text": "FUNCTION: Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb. Exocytosis of IGF1 is required for sensory perception of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis (By similarity). 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. Does not colocalize with synaptic vesicles or with the Golgi apparatus. SIMILARITY: Belongs to the synaptotagmin family."}
{"protein": "EAEEAARLQAEAEEAARQQAEAEEAARLQAEAEEAARLQAEAEEAARLQAEAE", "text": "SUBCELLULAR LOCATION: Membrane."}
{"protein": "MTNLIKNVKDAFNSVLSYAPTHIVQAPGRVNLIGEHTDYNDGFVLPCAINYQTVVAAAKRDDNIVRVVSVDYGNETDEFDITQEITFQENKMWSNYIRGVVKCLIDRGYEFKGADISVSGNVPQGAGLSSSAALEVVIGQTFKELYNLNISQAEIALNGQQAENEFVGCNCGIMDQMISAEGNENHAMLLDCRSLETTAVSMPEDMSVVIINSNKKRGLVDSEYNTRREQCEEAARIFGVKALRDVTIEEFNAKAHELDEMVAKRARHVITENDRTEEAAKVLASGDMKRMAVLMAESHASMRDDFEITVSEVDTLVDIVKNVIGAEGGVRMTGGGFGGCIVALVPPMLVDEVKAAVEELYEAKTGLKESIYVCQATNGAGLVL", "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": "MKSSQRRIKRHAMRDMSISTLLLSVVLLPSVVSANDHVYFNPPSPGSPFLGPQIPLTGPPSLTNEHEFTLRHIYERGTNDQPDLHRRLDIKPHTRLWAVSDDGLEKELVTFDTPLVASSSPLTIQRLADRRPSVIEGYLTAARYNGEAVALSSSDWVMDTLAGPDVTKKETVLTFAKMTANDYIEEPGTEDWNYIHGRFNYSSSFGWQSDGLRGHIYADTKNNTIVISLKGTSPALFDGAGTTTNDKINDNLFFSCCCGQGGSYLWRQVCDCQQSAFTANLTCIAEAMNDENKYYRAAIDLYTNVTDMYPDANVWMTGHSLGGAMSSLLGLTFGLPVVTFEAVPEALPAARLGLPSPPGHDPRLPQTRKYTGTYHFGHTADPVYMGTCNGVGSICTWGGYAMESACHTGQMCVYDTVEDKGWRVALSTHRIKAVISDVLEVYDNVPPCAAEEECYDCELWKFFRSNGSETTTTSRTSTTTTPTTTRTLTCETPGWWGCLDESTTTTATTATSTTTTTSTCKTPGWFGCKDSTTTVDATAAPTVTTTIATPTTFPISSTTCKDPGWFGCRDPSSTTASVTAPPFSTSTSSDHVRADHSIGDGAAHPLTRMYLERLRQVEFAWGSDIEHYEI", "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": "MTTFSVPIDNGDSMKIAEEESQRTLYPYVTGTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMWDDGNSLGPKEIHNYLTRVMYNRRNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVKLLEKCMRVLLYRDRSAINKLQIAKITEEGVTVSQPYSLKTYWEFSSFHNPTAGAAGSW", "text": "FUNCTION: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPHPRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMAAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHVTQSSRKLIRADSVSELPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRDLCSLLPPTESKPLATKEKATRPSQGHQP", "text": "FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family."}
{"protein": "MKLCVVIVLLMLAMPFNGGEASRFFNQHARSQRSGMKTRGIWCDPPCPKGETCRGGECSDEFNSDVGR", "text": "FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MAGNTIGQLFQVTTFGESHGIALGCIVDGVPPGLSLSEADIQPDLDRRKPGTSRYTTPRREDDEVQILSGVFEGKTTGTSIGMIIKNADQRSQDYGDIKDRFRPGHADFTYQQKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLREHFGVEVRGFLAQIGDVAIAPQVIEQIDWQQVNSNPFFCPDPSAVEKFDELIRQLKKEGDSIGAKLTVVAENVPVGLGEPVFDRLDADLAHALMGINAVKAVEIGDGFAVVNQRGSAHRDEMTPEGFLSNHAGGILGGISSGQPIVATIALKPTSSITIPGRSVNLANEPVEVITKGRHDPCVGIRAVPIAEAMVAIVLLDHLLRHKAQNR", "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": "MATKSKYQDKQIEALLNDLIVTLEKHKAPVDLSLMALGNMITNILVTNVQSPQQREVLAEAFSSALKNSLKSAK", "text": "SIMILARITY: Belongs to the UPF0352 family."}
{"protein": "IDESQTSLDTGVQRFTSSKIASSVQCFEDTKARIVKLIHKPELSVSTYDTAWVAMVPSPNSSNEPCFPDCLAWLLENQCCDGSWACPHHHPFLKKDVLSSTLACILALKKWGVGEEQINKGARFIEVNFASATEKSQISPTGFDIIFPAMLDYARDLFLDLRLEPTTFDNLIFRRDLELKRCYESHREAYLAYIAEGMGKLQDWESVMKYQRKNGSLFNSPSTTAAAFIALPNSGCLSYLHSALKKFGNAVPAAYPLDVYSRLRTVDNLESLGISRYFQKEIQQVLDETYRWWLQGSEEIFLDASTCALAFRTLRMNGYNVTSDAITKLLPDSFCGNMKDIGTTLELYRASEFILYPDEKDLEQQNLRLKDILEQELSSGFIHSEVNRALNYPFYAIMDRVAKRRNIEHYNFDNTRILKTSYCSPNFANKDFLFLSVEDFNNCQAMHREELKGKMRWVTENRLDELKFARSKSAYCYFSAAATFFAPDLSDARMSWAKNGVLTTVVDDFFDVGGSEEELKQLIRLVEIWDLDAITECSSQNVQIIFSSLKRTISEIGDKGFKLQGRSVTNHIIEIWLDLLYSMMKEAEWARDNHAPPMDDYISNAYVSFALGPIVLPCLYLVGPKLSEEMVRHSECHTLFRLMSTCGRLLNDIQTCERELKDGKLNAIPLYMINSGGETSKEAATQEMKSLIDRQRQELLRLVLTREGSLLPKPCKELFWHMSTVLHLFYCKDDGFTSQDLIKVVNEVIHEPVVLN", "text": "FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase that produces ent-kaurene from ent-copalyl diphosphate (ent-CPP) (PubMed:24990389). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Single-pass membrane protein. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MESKMILKDGCQELGFHIDDNQVQQLLTYKDILLEWNEKMNLTAITEEEEVMVKHFLDSLSCIQSQYLKEEGTMIDVGTGAGFPGIPLKVYFPKLKLTLLDSLNKRVEFLKEVSQELGLEDVNFVHGRAEECGQEETHREQYDYAVARAVASLNVLVEYCLPFVKVGGYFICQKGPQLKEEIQNSQNAITVLGGKVVEQKEITLPFSDITHSLLVIEKIKQTPTKYPRKPGTPSKKPIK", "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": "MSNVHLISHPLVQHKLTLMRRKNASTSTFRTLLAELSNLMAYEVTRDMPLQDIEVETPLETTTGKIIDGKKLVLVSILRAGNGFLDGFLNVVPGARVGHIGLYRDPETLSPVEYYFKMPQEMQERDIVIVDPMLATGNSAIAAVDRLKQLKPRSIKFVCLLTCPEGVAALQKAHPDVDIYTAAIDRQLNEHGYILPGLGDAGDRIFGTK", "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": "MKFPEFKDYYQQLISTSSISSTDSSWDEGNAEVINKLAQWCEDLGCEVEIEEIEKGKLNLLAKLGSGEGGLLLAGHTDTVPYDEGRWNYEPHALTEANDRFYGLGTADMKGFFAFILEAIKNINWKDQSKPLYILATCDEETTMLGARHFASNTKIQPDYCIIGEPTSLKPIRGHKGHVANAIRVTGKSGHSSDPAHGVNALEIMNEIMFALMTLKNKLVKEYHNPGFSIPYPTLNLGHIHGGDSPNRICGCCELHYDVRPLPGISLDGLDNMLRDALKEIEAKWPGRIDITPLHEPIPGYECSADSPIVTSTADICGQDVETVNYCTEAPFLQDLCPTLVLGPGSIEQAHQPDEYLAFSFIDPTISILSKLMYKHCF", "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": "MKIIFLVLMMILSEVYSDRDGYPVHDGTNCKYSCDIREKWEYCTPLCKRRNAKTGYCYAFACWCIGLPDEVKVYGDDGIFCKSG", "text": "FUNCTION: Toxin with unknown target. In vivo, induces severe neurotoxic events in mice such as excitability and convulsions, leading to the death of the animals within a few minutes after injection (PubMed:22819772). Exerts very strong cytotoxic effect on a mouse brain tumor cell line (BC3H1) (IC(50)=5 mg/ml). It exerts its effects by inducing a stronger necrosis than apoptosis in BC3H1 cells (PubMed:24055552). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MAAAAAADEAATRDVQRLLVQFQDEGGQLLGSPFDVPVDITPDKLQLVCNALLAQEDPLPLAFYVHDAEIVSSLGRTLESQAVETEKVLDIIYQPQAIFRVRAVTRCTSSLEGHSEAVISVAFSPTGKYLASGSGDTTVRFWDLSTETPHFTCQGHRHWVLSISWSPDGKKLASGCKNGQILLWDPSTGKQVGRALTGHSKWITALSWEPLHANPECRYVASSSKDGSVRVWDTTAGRCERTLTGHAQSVTCLRWGGDGLLYSASQDRTIKVWRAHDGVLCRTLQGHGHWVNTMALSTDYALRTGAFEPAEASVNAQDLRGSLQELKERALSRYNLVRGQGPERLVSGSDDFTLFLWSPAEDKKPLARMTGHQALINQVVFSPDSRVIASASFDKSIKLWDGRTGKYLASLRGHVAAVYQIAWSADSRLLVSGSSDSTLKVWDVKAQKLSTDLPGHADEVYAVDWSPDGQRVASGGKDKCLRIWRR", "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": "MPTTTEFDTIAAISTPPGEGGISIIRISGDQTFNVVTQIFKGKDLSRVQSHTINYGHIVDPDTHQEVDEVMATVMRAPKTYTREDVVEINCHGGLVATNEILQLILSHGARMAEPGEFTKRAFLNGRLDLSQAEAVMDLIRAKTDKSMKVALNQLDGDLSKLIRHLRQDILDVLAQVEVNIDYPEYDAVETMTTKMLKEKATEVAQSINQLLATAKQGKVLREGLATAIIGRPNVGKSSLLNHLLHEDKAIVTDVAGTTRDVIEEYVNVRGVPLKLVDTAGIRDTEDKVEKIGVERSRKAIGAADLVLLVLDNSQPLTAEDRELLQETDQSKRIVILNKTDLPARLDQAELAQLVDLSDVLSMSVLEQSGVTQLEQRIAKMFFNEGIESSQNNVMVTNARHIGLLNQAKQALQDVQTGLAAGMPVDLVQIDMTRCWEFLGQITGDSYEDELLDQLFSQFCLGK", "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": "MFEGAMPALITPFTKDDRIDREGLRRNIAFVEEGGVSGIVPCGTTGESATLSALEHEEVIDIAVECAKVPVVAGTGSNNTGEALQFTKHAADAGVDGVLLISPYYNKPNPAGLLAHFKKIAEAVDIPMILYNVPSRTGQDMPVDVITKLAKVENIVGIKEASGSVGKVSQILEQTIDDDFVVLSGEDGLTLPIISVGGSGVISVAANIVPDKMSGMVSAALKGDYETARKIHFEIAPLIRALFLETNPIPAKKAAELIGLASGHLRLPLAPMSDANQLKLVTELKKLGVMK", "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": "MALLRDVSLQDPRDRFELLQRVGAGTYGDVYKARDTVTSELAAVKIVKLDPGDDISSLQQEITILRECRHPNVVAYIGSYLRNDRLWICMEFCGGGSLQEIYHATGPLEERQIAYVCREALKGLHHLHSQGKIHRDIKGANLLLTLQGDVKLADFGVSGELTASVAKRRSFIGTPYWMAPEVAAVERKGGYNELCDVWALGITAIELGELQPPLFHLHPMRALMLMSKSSFQPPKLRDKTRWTQNFHHFLKLALTKNPKKRPTAERLLQHPFTTQHLPPALLTQLLDKASDPHLGTLSPEDSELETHDMFPDTIHSRSHHGPAERTPSEIQFHQVKFGAPRRKETDPLNEPWEEEWTLLGKEELSGSLLQSVQEALEERSLTIRPALELQELDSPDDAIGTIKRAPFLGLPHTESTSGDNAQSCSPGTLSAPPAGPGSPALLPTAWATLKQQEDRERSSCHGLPPTPKVHMGACFSKVFNGCPLQIHAAVTWVHPVTRDQFLVVGAEEGIYTLNLHELHEDTMEKLISQRCSWLYCVNNVLLSLSGKSTHIWAHDLPGLFEQRRLQHQAPLSIPTNRITQRIIPRRFALSTKIPDTKGCLQCRVVRNPYTGSTFLLAALPASLLLLQWYEPLQKFLLLKNFSSPLPSPAGMLEPLVLDGKELPQVCVGAEGPEGPGCRVLFHVLPLEAGLTPDILIPPEGIPGSAQQVIQVDRDTVLVSFERCVRIVNLQGEPTAALAPELTFDFTIETVVCLQDSVLAFWSHGMQGRSLDTNEVTQEITDETRIFRVLGAHRDIILESIPTDNPGAHSNLYILTGHQSSY", "text": "FUNCTION: Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:8643544). Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N- terminal kinase (SAP/JNK) signaling pathway and to a lesser extent of the p38 MAPKs signaling pathway (By similarity). Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine- polycytidine (poly(IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin (By similarity). To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2- mediated JNKs activation (By similarity). The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8 (By similarity). Enhances MAP3K1 oligomerization, which may relieve N- terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation (By similarity). Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3 (By similarity). May play a role in the regulation of vesicle targeting or fusion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Basolateral cell membrane; Peripheral membrane protein Golgi apparatus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MQMTFRWYGDSDPVTLEYIRQIPGVTGIVSAIYDIPVGEAWPYEKIVELKEKIENHGLSLSVIESVPVHEDIKLGLPTRDQYIENYKTTIRNLAKAGVKIVCYNFMPVFDWTRSSLDYALEDGSTALIYEEEKVRQMNPLHGELKLPGWDTSYEDGQLKNLFQQYQHMTEEDLWENLSYFIKAVIPAAENEQVKMAIHPDDPPWPIFGLPRIITNKENLERLIHLYDSSFNGLCLCSGSLGVKSTNDIPELIRYFGKKGKVNFVHLRNIKIIGEKSFQESSHRSEDGSLDMYEIVRALRDIDFAGPARPDHGRMIWGETGKPGYGLYDRALGAVYLNGMWETLTKEKKRIALECNK", "text": "FUNCTION: Catalyzes the dehydration of D-mannonate. SIMILARITY: Belongs to the mannonate dehydratase family."}
{"protein": "MIETREEVGSANFVSLERAIEDLRAGKFVIVVDEASREDEGDLIIAGEKITVEKMTFLLQHTTGVVCAALSQERLLSLDLPPMVKDNRCRFKTPFTVSVDAAHGVTTGVSAADRTKVVQLLADPKSKPEDFISPGHFFPLASSPGGVLKRAGHTESTVDLMELAGLQPCGVLAELVNEDYSMMRLPQILEFARKHNIAVIPVTSIIAHRMLSDRLVSKISSARLPTIYGDFTIHVYESLLEGMQHLALVKGNVAGKSNVLVRVHSECVTGDILGSKRCDCGEQLSSAMSYIAEKGTGVLVYLRGQEGRGIGLGHKVRAYALQDNGYDTVDANLAMGFPVDSREYGIGAQILVDLKLTTIKLITHNPQKYFGLQGFGLSITERVPLPVRISEDNEQYLRTKQERMGHWLDLPCCNNRVQ", "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": "MLAAKSIAGPRAFKASAVRAAPKAGRRTVVVMARKNEVSESYAKALVELADEKGKLEAVHADVDAVAGLMKENAKLSALIMNPVVESDKKRAVLAKIAKEAGFQQYTINWLNLLVEKDRLSLVPEICECFEDLYCQMTDTQVATLRSAVKLEQEQQFLIAKKLQELTGSKNIKLKPVIDSSLIAGFVVEYGSSQIDLSVRGQIERVADQLTKEMTAKLS", "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 seems to be part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) into CF(1) or is implicated in proton conduction. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MKVYKDIFTNDEVCSDSYAQEDPFGNPEFREIAFEVKSNKRIKGNDDYGIADNSEDAVEGMGADVEHVIDIVDSFQLTSTSLSKKEYSAYVKNFMQRILKHLEEKKPDRVEIFKTKAQPLIKHILTNFDDFEFYMGESLDMEAGLIYSYYKGEEITPRFVYISDGLFEEKY", "text": "FUNCTION: Involved in calcium binding and microtubule stabilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCTP family."}
{"protein": "MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV", "text": "FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:1330647, PubMed:18703043, PubMed:19057895). 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) (PubMed:28129538). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors (PubMed:28129538). Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways (PubMed:28129538). 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 (PubMed:18703043, PubMed:28129538). Affects neural activity, perception, cognition and mood (PubMed:18297054). 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. FUNCTION: (Microbial infection) Acts as a receptor for human JC polyomavirus/JCPyV. 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": "MSSFETTIGLEVHVELKTKSKAFSLSPVNFGDPANENTNVIDWGYPGVLPSANKGALESGMMAALALNAQITRDVHWDRKNYFYPDNPKSYQVTQQQTPIGHDGYVEIKKEDGTSKRIGIKELHVEEDAGKNSHSGKGYSLVDLNRQGTPLVEIVSQPNISSPDEAYLYLEKLRQLIQFTGISDVKMQEGSMRVDINISVRPIGAEKYGTKVEIKNVNSFQYAKNALAYEEQRQRDELMAGHIIGQETRRFDEPTKSTILMRVKEGADDYRYFPEPDLPVIHVSDEWIKAVKSSLPETADDRIARYINKFALSKKEAAVLTQTLEMANFYDQVVDDGADPKRTANYLIGDVNAYLNETQLDLQDTKLTPGHLSGMIKLIDNGTISTKQAKKVFTAITDGEEPKAYVEKNGLVQLSDPNKLTPIINQILDDNQQSIDDFKGGKDRTIGYLTGQVMKKTHGNANPKIVHEILLAELKKR", "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": "MDPLKICENYLTFRAIIRGSTLSPGFFRRWCFPALADVVGNIVEQEEGRFWQILPENHAFWGLLRRGFTVASFTEIITAAQLENRGRQLAFLAFISFLLRNWPSDSVVPEADRLDLVCAPAWSRMQIWSQTARLINDLQDSVLEEQGSAEEEECEEALLAGDSDDPLFG", "text": "SIMILARITY: Belongs to the adenoviridae E1B 19 kDa protein family."}
{"protein": "MGKLFGTDGIRGFANIYPMTVEVALKTGRAVARFAKEHGGTVVIIGRDTRRSGDMLEAALAAGISSMGINVLEAGVIPTPGVAFLTATVKGAGAGVVISASHNPFHDNGIKVFKSGGLKLTDPEEAKIESYIFDAGPDRADSSICEPKTSDSAIEPGTISTISNASAQYANFLTSCYQRDLDKNTPDQPLKIVVDCSNGASFKVAPMVFPTLGFETQFIFDTPDGKNINHNCGSQHTETLAKRVISTGADLGLAFDGDADRLIAIDEQGVKLTGDKILAICANHAKAQGRLTNNLVITTVMSNIGLSKALERLGIDHIKTGVGDREVLKEMWATGAVMGGEDSGHMIFSEFHSTGDGILSALCLIRVMVDTNKSLSDLATIMTVYPQVLMNVEVDPSRPDFMKIETIAREIKRVEQALNSSGRVLVRYSGTQPLLRVMVEGPDLEATKSHCQSICDAIKQASI", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MQTANEIRRTFLDFFEKNGHTVVNSSPLVPRNDPTLMFTNAGMVQFKNVFTGIEKRDYVRAASSQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKDLAIEHAWNLITKDFGIDKSRLLVTVYHDDDQAADAWKKIAGLPESRIIRIPTSDNFWAMGDTGPCGPCSEIFYDHGEHIFGGPPGSPDQDGDRFIEIWNLVFMQFEQVDKETRIPLPKPSIDTGMGLERLAALLQGKHDNYDVDLLRALIEASAEASNTDPDGPHKVSHRVVADHLRSSSFLIADGVLPSNEGRGYVLRRIMRRAMRHAHLMGCTEPLLHKLVPALTRQMGEAYPELVRANALITETLKLEETRFKVTLDKGLKLLDDEITRIGSGQKLAGEVAFKLYDTYGFPLDLTQDALKAKGIGVDTDGFASAMERQRAEARKAWAGSGDTATETVWFELREKLGASEFLGYDAEQAEGKIVALVENGKVVEAVHPGHQVAVIANQTPFYGESGGQMGDTGVITLGTPGTGGKATIAVTDTQKKLGDLIVHFGTVEGGPVAVGEDAHFAVESTRRDATRGHHSATHLLHAALRDILGDHVTQKGSQVGPDRLRFDFAHTKALSAEETRAVEAEVNRRIRLNAEVATKVMTPDDAIKAGAMALFGEKYGEEVRVVSMGDLSTELCGGTHANRTGDIGGFKIVAESAVASGVRRIEAVTGPAFLAWAQAQEDLLAKAADTLKAAPADLPARIAGLMDDRRKLERELAEVRKQLATGGGQGAATKTVNGITYAGKVLSGVPAKDLKGMADEIKKQIGSGIIALVSDADGKASIVVCVTEDLTSKHSAVDLVRIGSEALGGKGGGGRPDMAQAGGPDASAAQAAVDRIEQALGG", "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": "MASSSVSSLQFLFVTPQTPSSLKPNSTLSFFSLPSSSLNLSLSSSSTGLCSIKPFESSFSTRVALSGFDQLEDDVEVAEQPRFSEDLKLFVGNLPFSVDSAALAGLFERAGNVEMVEVIYDKLTGRSRGFGFVTMSTKEEVEAAEQQFNGYEIDGRAIRVNAGPAPAKRENSSFGGGRGGNSSYGGGRDGNSSFGGARGGRSVDSSNRVYVGNLSWGVDDLALKELFSEQGNVVDAKVVYDRDSGRSRGFGFVTYSSSKEVNDAIDSLNGVDLDGRSIRVSAAEERPRRQF", "text": "FUNCTION: Could be involved in splicing and/or processing of chloroplast RNA's. SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "LKCHNKLVPFLSKTCPEGKNLCYKMTMLKMPKIPIKRGCTDACPKSSLLVKVVCCNKDKCN", "text": "FUNCTION: This protein lyses red blood cells and has cardiotoxic and hypotensive activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IB cytotoxin sub-subfamily."}
{"protein": "MPDYEGNGEDIDNYTGGSSPPPKSRSSHGHGPTPDDYSDSKSQHSSRENEKDRDSSRSREKDRERGRDKDRDRDRDRDRGRDRDRGRDRDKDREREKDRDRHHGDRHRDRSDRREKERTRDRDDDDRHRTRDYDQQREHAKDRESRHRHRSRSRGRSEHRSRSRSRSRSKSKRISGFDMAPPTSAMLPGITAAAGQVPGTNPPIPGMFPNMFPLASGQFGALPVMPIQAMTQQATRHARRVYVGGLPAHANEQSVATFFSHVMSAIGGNTAGPGDAVVNVYINYEKKFAFVEMRSVEEASNAMALDGIIFEGAPCKVRRPSDYNPSLAATLGPSQPNPNLNLAAVGLSPGSAGGLEGPDRIFVGGLPYYFTEAQIRELLESFGPLRGFDLVKDRETGNSKGYAFCVYQDVSVTDIACAALNGIKMGDKTLTVRRANQGTTQPKPEQESVLLHAQQQIALQRLMLQPATLATKVLSLTEVISADELNDDEDYQDILEDMRTECGKFGSLVNVVIPRPSPNGEPTPGVGKVFLEYADVDSSSKARQSLNGRKFGGNQVVAVFYPENKFYEGDYDG", "text": "FUNCTION: Necessary for the splicing of pre-mRNA. Binds to the U -enriched regions of plant introns. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
{"protein": "MAKVLYEKDIQDGVLKNKKIAVIGYGSQGHAHAMNLRDSGYDVVVGLRPGKSQEKAEEDGFNVLSVAEASSQADVVMVLLPDEMQPKVYEESIKDNLEQGNALVFAHGFNIHFTQVVPPANVDVFLVAPKGPGHLVRRTFEEGAGVPALYGVHQDYTGEAKDVALAYSKGIGAARAGVLETSFQEETETDLFGEQAVLCGGVTSLIKAGFETLTDAGYQPEVAYFECLHEMKLIVDLLYEGGLENMRYSISDTAQWGDFVSGQRVVDDQTKERMKSILDDIQTGSFAKGWILENQAGRPQFNAINRRENRHPIETVGRELRELMPFVKQPINAKKKDVNVHVPN", "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": "MADGGSERADGRIVKMEVDYSATVDQRLPECEKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAIVKMCYEAKEWDLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPIKLRLIDTLRMVTEGKIYVEIERARLTKTLATIKEQNGDVKEAASILQELQVETYGSMEKKERVEFILEQMRLCLAVKDYIRTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSYLSICKHYRAIYDTPCIQAESEKWQQALKSVVLYVILAPFDNEQSDLVHRISGDKKLEEIPKYKDLLKLFTTMELMRWSTLVEDYGMELRKGSLESPATDVFGYTEEGEKRWKDLKNRVVEHNIRIMAKYYTRITMKRMAQLLDLSVDESEAFLSNLVVNKTIFAKVDRLAGIINFQRPKDPNNLLNDWSQKLNSLMSLVNKTTHLIAKEEMIHNLQ", "text": "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 p55 family."}
{"protein": "MDIKEIALGQIRDSIATKQKCIDSILEDIIKAGEIVSKILQAGNTIFLCGNGGSSCDASHIAAELVVRYKSGNERKALPALSLSADSAVLTACSNDYGYEEIFSRQIEAFGRKGDLLIGLSTSGNSKNVLLALEKAKTRGVKTISLLGGDGGKMKNLSDLDVIVPSNVTARIQESHILIGHIICSIVEYNLFKME", "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": "MTQAVMLQGTASDVGKSVLAAGLCRIFYQDGLRTAPFKSQNMALNSGITSDGKEMGRAQIFQAEAAGITPDVRMNPVLLKPTSDRQAQVVLMGKVATNMDAVSYHDYKPRLREQILAVYNSLAQEYDVIVLEGAGSPAEINLRDRDIVNMGMAEMAQCPVILVADIDRGGVFAAIYGTLALLHKQERDRVKGVIINKFRGDVALLYSGIEQIESLTGVPVLGVMPWLDVDLEDEDGVALQNDKYRGNAPRDITIAIVQLPHISNFTDFNALAAQPDVRIRYIRRPEALTDADLVILPGSKNTLSDLAWLRESGMADAVLQTHRQGVPVMGICGGYQMLGDTIVDEVESGLGTQPGLGLLNTITRFAQDKITTQVNATMSGELPSWLAAAAGLPVRGYEIHMGETVLQEGCCTAMTLQKNGCSVADGAVTADGLAFGTYLHGLFDSDAFTRAVVNGLRARKGLAPWETTFCYAEHKARQFDLLAEAMRQHIDIDKIYTIMQQHQEPV", "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": "MQLYHHPYSIDSQRVRLALEEKGIDYTSYHVNPITGKHMDPSFFRMNPNAKLPVFRNGSHIILDTIEIIEYLERIAEVSSGIEDATFNREVVEWMRKIREWESKLFTLAHIPDNRRLYVSKFLRMVVIARMAESPDLASAYHRKLREAYDTEDKLKDPGALRRSKDHLLRLLDEVETKLEGTTYLAGNEFSMADVMLIPVLARLSLLDLEEEYISSRKNLAEYWALVRRRPSYKKVIGRYFNGWRKYATLVKTWMFVRVRSLLRKY", "text": "FUNCTION: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the GST superfamily."}
{"protein": "MNSFRFTKMHGLGNSYIYVNQFEEHLPEELLSDLAVKVSSVYTGIGSDGMILICPSDRAPVKMRIFNSDGSEGKNCGNGLRCVAKYAYEHKLVEETSFLIETLSGLVKAQVEVDEGKVVSATVDMGEPRLLKSDMPMRGEQGSETINEKMIFGGREMKGTAVSMGNPHIVFYLDDIEKAPLTTMGPLIEKDERFPEGVNVEFVEVENENELHFRVWERGSGITQACGTGACAAAVSSVLNGYSKRDTDITVHLAGGDLIINWKNDGRVMMTGPAETVCEGEFFIS", "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": "MVFTPEDRLGKQCLLLPLLLLAAWKVGSGQLHYSVPEEAKHGTFVGRIAQDLGLELAELVPRLFRMASKDREDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVDVEVRDINDNPPLFPVEEQRVLIYESRLPDSVFPLEGASDADVGSNSILTYKLSSSEYFGLDVKINSDDNKQIGLLLKKSLDREEAPAHNLFLTATDGGKPELTGTVQLLVTVLDVNDNAPTFEQSEYEVRIFENADNGTTVIRLNASDRDEGANGAISYSFNSLVAAMVIDHFSIDRNTGEIVIRGNLDFEQENLYKILIDATDKGHPPMAGHCTVLVRILDKNDNVPEIALTSLSLPVREDAQFGTVIALISVNDLDSGANGQVNCSLTPHVPFKLVSTFKNYYSLVLDSALDRESVSAYELVVTARDGGSPSLWATASLSVEVADMNDNAPAFAQPEYTVFVKENNPPGCHIFTVSARDADAQENALVSYSLVERRVGERALSSYISVHAESGKVYALQPLDHEELELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLAPRVGGTGGAVSELVPRSLGAGQVVAKVRAVDADSGYNAWLSYELQPPASSARFPFRVGLYTGEISTTRVLDEADSPRHRLLVLVKDHGEPALTATATVLVSLVESGQAPKASSRASVGAAGPEAALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSAPPTEGACTADKPTLVCSSAVGSWSYSQQRRQRVCSGEGPPKMDLMAFSPSLSPCPIMMGKAENQDLNEDHDAKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ", "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: [Isoform 1]: Cell membrane; Single- pass type I membrane protein."}
{"protein": "MIDRKLLLQDFDKVALSLKKRNHAMDDELERLREAIAHYKKQLIELEGLQAFQNKVSKEFGIKMAQKMDTSDLKKELENNKIKLNELSKSVGEAEQEMDLKLSIIPNLVDEKTPLGASEEDNIEIKKILTPRNFTFKPKEHFELAQQNGWIDFESGVKLAKSRFSVIRGFGAKIYRALIHLMLDFNEKNGFEIIYTPALVNEKMLFGTGQLPKFKEDVFKIENENLYLIPTAEVTLTNLYNDTIISVENLPIKMTAHTPCFRSEAGSAGKDTRGMIRQHQFDKVELVAITHPKESDAMQEHMLESASEILKALELPHRFVQLCSGDLGFSASNTIDIEVWLPGQNCYREISSVSNTRDFQARRAKIRFKENQKNQLVHTLNGSSLAVGRTMVALMENHQQADGSIHIPKALEKYL", "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": "MTLPLLGPMTLSGFAHSWFFLFLLVVAGLIAIYVVLQLARQKRMLRFANMELLESVAPQRPSRYRHIPAMLLALSLVLFTVAMAGPTHDVRIPRNRAVVMLVIDVSQSMRATDVEPNRMVAAQEAAKQFADELTPGINLGLIAYAGTATVLVSPTTNREATKAALDKLQFADRTATGEAIFTALQAIATVGAVIGGGDTPPPARIVLFSDGKETMPTNPDNPKGAYTAARTAKDQGVPISTISFGTPYGFVEINDQRQPVPVDDETMKKVAQLSGGNSYNAATLAELNSVYVSLQQQIGYETIRGDASMGWLRLGALVLVAAALAALLINRRLPT", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0353 family."}
{"protein": "MRKRSRKVKNDLVVLESKEKKVGMWGIFALILIVFGFIIAPLLPGIFDNAHSSGLKFGSYKGQPIYYKKDSKFAKYVNYYSNLYSRLQGNAKNINTDYNAWYLAFMKYVEDVAFLDLVKKYNFYISKEMLNKNLLKSPEYLDSSGNFSSKRYNKASDYQKVKIYDDMVENILFSNVKIFLNSNLIFPDSLFDMIKNMSTVERHISYLSLSYQDFSNKEVISYAEKNLNLFKRLSLASIRFKNMNDARTAHDKLLNKTPFEELAKLYSDDIANFKGVVSLDKYYFDLDLNVEKKEDLNSIFSLREGEFSKPIKIKNKNEYQIYKAFSNVHDFDKNSDRDISSVKNYIETYEPSVIEGYLENKLSDFLGDVKFSSLSQVLEKYQLSLKEEIVNLSYNINVYPNTLKELVEFNNSKSFYDIIFGLKENSWSKPFVANKKVYLFFLNSVKKRSNQLKDEIKNEKILDNFNIANSGLITDFLLNKKDFVNNFNESFFALQNFSQN", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MILEGGGVMNLNPGNNLLHQPPAWTDSYSTCNVSSGFFGGQWHEIHPQYWTKYQVWEWLQHLLDTNQLDASCIPFQEFDINGEHLCSMSLQEFTRAAGTAGQLLYSNLQHLKWNGQCSSDLFQSTHNVIVKTEQTEPSIVNTWKDENYLYDTNYGSTVDLLDSKTFCRAQISMTTTSHLPVAESPDMKKEQDPPAKCHTKKHNPRGTHLWEFIRDILLNPDKNPGLIKWEDRSEGVFRFLKSEAVAQLWGKKKNNSSMTYEKLSRAMRYYYKREILERVDGRRLVYKFGKNARGWRENEN", "text": "FUNCTION: Transcriptional activator that may play a role in regulating epithelial cell differentiation and proliferation. May act as a repressor for a specific subset of ETS/AP-1-responsive genes, and as a modulator of the nuclear response to mitogen-activated protein kinase signaling cascades. Binds to DNA sequences containing the consensus nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5 expression through Ets-binding sequences on the TNFRSF10B/DR5 promoter (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
{"protein": "MRDAIPLGRIAGFVVNVHWSVLVILWLFTWSLATMLPGTVGGYPAVVYWLLGAGGAVMLLASLLAHELAHAVVARRAGVSVESVTLWLFGGVTALGGEAKTPKAAFRIAFAGPATSLALSATFGALAITLAGVRTPAIVISVAWWLATVNLLLGLFNLLPGAPLDGGRLVRAYLWRRHGDSVRAGIGAARAGRVVALVLIALGLAEFVAGGLVGGVWLAFIGWFIFAAAREEETRISTQQLFAGVRVADAMTAQPHTAPGWINVEDFIQRYVLGERHSAYPVADRDGSITGLVALRQLRDVAPSRRSTTSVGDIALPLHSVPTARPQEPLTALLERMAPLGPRSRALVTEGSAVVGIVTPSDVARLIDVYRLAQPEPTFTTSPQDADRFSDAG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
{"protein": "MSWLSNTIQKLCRVTLLSAGSNPLPAISATSTTVRQLSHAERRARGPTVRRYGYKDKIFKSGLLPHLDNGQKLPMPVYRPKNPWSEKRALFGQNDYIDILGNDRLHPVRVMYSVPSWLRGVSGNEYQVLLRKRRLLEKSKYPIARPTKWRDMQKRILYLYKFLNRKTKTGYSKQ", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL51 family."}
{"protein": "MIEYVQAGTIQVAKVLYEFVNEELLPNSGLDQDKFWSDFAALIADLTPRNKELLARRDEIQEKLNEWYKEHRGRFDFHEYKAFLTDIGYLEPEVEDFEITTDNVDEEIAVQAGPQLVVPLTNARYALNAANARWGSLYDALYGTDAISEEDGAERGSSYNPVRGAKVIAYGRQFLDEAVPLVEHSHKDAVQYAIVDGKLVVTTEGGATTGLKEPEKLIGFQGEPQNPTAVLLKNNGLHIEIQIDREHPVGKTDKAGIKDIVLEAAVTTIMDGEDSVAAVDAEDKVVVYRNLFGLIKGDLTATFEKNGKRLTRTLNPDREYKTPDGGELVLPGRSLMFVRNVGHLMTNNAILDANGEEVYEGIIDAVVTSLIMKHSLIGNTRYLNSRKGSIYIVKPKMHGSAEVAFANELFDRVEDMLGLERNTIKIGVMDEERRTSLNLKNCIYEVRDRIVFINTGFLDRTGDEIHTSMEAGPMRRKNDMKSSTWLAGYEKSNVAVGLAAGFRGRAQIGKGMWAMPDLMAEMLKQKGAQLKAGANTAWVPSPTAATLHALHYHQVNVAAVQNELANDRNDYRDDILQIPVVDNPQWTADEIQEELDNNCQSILGYVVRWIDQGIGCSKVPDIHNIGLMEDRATLRISSQILANWLHHGICTKEQVLETFKRMAKVVDEQNAGDPNYRPMAPNYDDSVAFQAACDLVFLGYEQPNGYTEPILHRRRQEAKAKFAAVQQ", "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": "MEIIPNLSIETWVLLATSLMLFYIYGTYSHGLFKKLGIPGPKPVPLFGTIFNYGDGMWKFDDDCYKKYGKIWGFYEGPQPFLAIMDPEIIKMVLVKECYSVFTNRRCFGPMGFMKKAITMSEDEEWKRLRTILSPTFTSGKLKEMFPLMRQYGDTLLKNLRREEAKGEPINMKDIFGAYSMDVITGTSFGVNVDSLNNPQDPFVQKAKKILKFQIFDPFLLSVVLFPFLTPIYEMLNFSIFPRQSMNFFKKFVKTMKKNRLDSNQKNRVDFLQLMMNTQNSKGQESQKALSDLEMAAQAIIFIFGGYDATSTSISFIMYELATRPNVQKKLQNEIDRALPNKAPVTYDALMEMEYLDMVVNESLRLYPIATRLDRVSKKDVEINGVFIPKGTVVTIPIYPLHRNPEYWLEPEEFNPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALISMKLAVIGVLQNFNIQPCEKTQIPLKISRQPIFQPEGPIILKLVSRD", "text": "FUNCTION: Catalyzes 16-beta- and 6-alpha-hydroxylations of testosterone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "LAAVDCSEYPKPACTMEHRPLCGSDNQTYDNKCNFCNAVVESNGTLTLSHFGKC", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MLTKYALVAIIVLCCTVLGFTLMVGDSLCELSIRERGMEFKAVLAYESKK", "text": "FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system (By similarity). When overexpressed kills cells within minutes; causes collapse of the transmembrane potential and arrest of respiration (By similarity). Its toxic effect is probably neutralized by an antisense antitoxin Sok RNA (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Hok/Gef family."}
{"protein": "MAFMGRELKWGVAHIYSSLNNTIIHITDLTGAETVSRWSGGMVVKADREKPSPYAAMIAASRAAAEAMDKGITALHIKVRAPGGHGPKTPGPGAQAAIRALARAGFIIGRIEDVTPIPHDTTRRPGGRRGRRV", "text": "FUNCTION: Located on the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "TVKVTVTGAAGQIGYALLFR", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MQYGDKTTFKQSLAIQGRVINALLMREIITRYGRQNIGFFWLFVEPLLMTFFIVMMWKFIRADKFSTLNMIAFVMTGYPMAMMWRNASNRAIGSISANLSLLYHRNVRVLDTIFTRVLLEVAGASIAQILFMAILVMIDWIDAPHDVFYMLIAWFLMAMFAFALGLIICAIAQQFDVFGKIWGTLSFVLLPISGAFFFVHNLPAQAQSIALWFPMIHGTEMFRHGYFGDTVVTYESIGFLVVSDLALLLLGLVMVKNFSKGVEPQ", "text": "FUNCTION: May form an ATP-driven capsule polysaccharide export apparatus, in association with the BexA, BexC and BexD proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-2 integral membrane protein family."}
{"protein": "MPGPSLSLALVLSAMGALLRPGTPREEVFSTSALPREQATGSGALIFQQAWDWPLSSLWLPGSPLDPLCLVTLHGSGNGSRAPLRVVGVLSSYEQAFLEAVRRTHWGLSDLTTFAVCPAGNGQPVLPHLQRLQAWLGEPGGRWLVVLHLEEVTWEPTPLLRFQEPPPGGASPPELALLVVYPGPGLEVTVTGAGLPGTQSLCLTADSDFLALVVDHPEGAWRRPGLALTLRRRGNGALLSTAQLQALLFGADSRCFTRKTPALLLLLPARSSAPMPAHGRLDLVPFPQPRASPEPEEAPPSADPFLETLTRLVRALAGPPARASPPRLALDPGALAGFPQGQVNLSDPAALERLLDGEEPLLLLLPPTAATTGVPATPQGPKSPLWAAGLARRVAAELQAVAAELRALPGLPPAAPPLLARLLALCPGNPDSPGGPLRALLLLKALQGLRAEWRGRERSGSARAQRSAGAAAADGPCALRELSVDLRAERSVLIPETYQANNCQGACGWPQSDRNPRYGNHVVLLLKMQARGATLARPPCCVPTAYTGKLLISLSEERISAHHVPNMVATECGCR", "text": "FUNCTION: Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation and plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles. AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MHFQLEMVTRETVVIRLFGELDHHAVEQIRAKISAAIFQGTVTTIIWNLEGLSFMDSSGVGLVLGRMRELEAVAGRTILLNPSPTMRKVFQFSGLGPWMMDATEEQAIDRVRGIVNG", "text": "FUNCTION: In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition. SIMILARITY: Belongs to the anti-sigma-factor antagonist family."}
{"protein": "MLHVEMLTLVFLVLWMCVFSQDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL", "text": "FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Membrane, caveola; Lipid-anchor, GPI-anchor Note=Compartmentalized in discrete caveolae-like membrane microdomains. SIMILARITY: Belongs to the ephrin family."}
{"protein": "MTMQTMTAASGHDAEAGTPPDGPLLALDGITVTFPGVRALDAVSLSVRAGEVHGLMGENGAGKSTLLKVLSGVNQPQAGTLTLNGTAQRFASTRAALEAGIAIIYQELHLVPELTVAENLMLGQLPSRLGVVDERTLAARALDALERLGEHIDPGIPVKYLSIGQRQMIEIGKALMRHARVIAFDEPTSSLSARETTQLFRIIRALRAEGRAIIYVTHRMEEVYELCDRVTVFRDGRRIDTFDSVADLDRDRLIGCMVGRSIEDVYGYRSRPAGDVLIEAKGLAGPGLAEPVSFTARRGEIVGFFGLVGAGRSELMKLLYGAVRPSAGHVELNGKRVAFGSPRDAVRAGIALCPEDRKQEGIVAIASVADNLNISARRHFSPARVLLDGRRERELAQKYIERLAIKTRDGDTPIGALSGGNQQKVVLARWLAERIDVFLMDEPTRGIDVGARAEIYNLFYELAEAGRTVILVSSDLAEVIGVSDRIVVMKEGRIAGEVAKAHATPDALIKLALPR", "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": "GDGENGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGYFDDDDWDDFDWDDDDWNDNGNGDNGDDDDFWDDWDDDRFDDDRFDDDRFDDDRFDDDRWDDDDNDDWDDDDRWGDDDNDDWDDDDRWGDDDNDDWDDDDRWGDDDNDDWDDDDRWGDDNGNGNGNGNGNGNGDDDDDNGGYAFLRRALARASARARAAASAAGRSRGGSGGSGGSGGSGGSARARARARARAFASARASSGNGVNGGNGKKRSYTSY", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MVKVGVNGFGRIGRLVTRAAFTSGKVEVVAINDPFIDLNYMVYMFQYDSTHGKFKGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNQDKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYEDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDSHSSTFDAGAGIALNDNFVKLISWYDNEFGYSNRVVDLMAYMASKE", "text": "FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a 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 (By similarity). Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1- dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF- induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton Nucleus Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with CHP1 to small punctate structures along the microtubules tracks. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MDKVQSGFLILFLFLMECQLHLCLPYADGLHPTGNITGLPGSKRSQPPRNITKEPKVFFHKTQLPGIQGAASRSTAASPTNPMKFLRNKAIIRHRPALVKVILISSVAFSIALICGMAISYMIYRLAQAEERQQLESLYKNLRIPLLGDEEEGSEDEGESTHLLPENENELEKFIHSVIISKRSKNIKKKLKEEQNSVTENKTKNASHNGKMEDL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MKKDSVIFDLIEKEHQRQLKGIELIASENFVSEQVMQAMGSCMTNKYAEGYPGKRYYGGCEVVDQSEQIAIDRIKQLYGAEWANVQPHSGAQANMAVLLACLEAGDTFMGLNLEHGGHLSHGSLVNSSGILYRPIGYNLSEETGMVDYDHMEKMAIEHKPKLIIGGGSAYSREWDYKRMREIADKVGALLMIDMAHPAGLIAAGLLENPVKYAHIVTSTTHKTLRGPRGGIILMGKDFDNPWGKKTPKGEIKKMSALLDSAVFPGVQGGPLEHVIAAKAVAFGEALDPSFKEYQTQVKKNAAVLAQAFMDKGYKVISGGTDNHSMLIDLRPKFPELTGKVAEKALVAADITVNKNMVPFDSRSAFQTSGFRVGTPAITTRGVKEDKMGYIVELIDRVLSAPEDEAVIASVRTEVNRMMADYPLFAW", "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": "MIDLKYLQNNFNEVSMKLQKKGVDAASLEHLQTLFKTLKEANAKLEAAKAEQNSMSKLFGQYKREGKDITELKAKVDANKEAMVPLQEAAREAEEALYAVALAIPNLPDDSVPEGADEEDNVELIKVLEPRSFDFEPKEHWDLAEKNGWIDFERGVKLAKSRFSVLRGDAARLERALINFFLDTNRERGFEEFCVPFMNNAAMLQGTGQLPKFEDDLFKIEDEDLYLIPTAEVPLTNMYHDEILAEIDLPVLMTGYTPCFRKEAGSAGRDTRGMIRQHQFDKVEMVAIAHPDNSDEVFDMMVQNASDILTALGLPHRVVELCGGDLGFSAAKTIDLEVWLPGQNKYREISSISNTRDFQARRAKIRFKDGKKNRLVHTLNGSALAVGRTLIAIMENYQNEDGTIEIPEVLKKYM", "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": "MRTRAGMSEENPCPRNIFLLCKQYGLELEDLRLLCVYCRRALSDADVLAFAIKELSVVWRKGFPFGACGKCLIAAGKLRQYRHWHYSCYGDTVETETGIPIPQLFMRCYICHKPLSWEEKEALLVGNKRFHNISGRWTGHCMQCGSTCTAPDPASRTLH", "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": "MGKEMKQTAFEKSIDSASQIMLQKAEDEGIETAWDRYEQQLPQCSFGQLGICCRNCNMGPCRIDPFGEGTEKGICGATADIIVARNLLRMIAAGAAAHSDHARDAVLTFKKMSEGKAGSYRIKDEAKLYSLASEYGISAEEKSREEVAVELASALLSEFGKQEGPILCTKRAPESRLKLWSELGIEPRGIDREIVECMHRTHIGVDNDATHILLHGLRTSLSDGWGGSMIATEIQDVLFGTPEPKKSTVNLGVLSHDKVNVIVHGHEPILSEMIVEAAEDPELLELAEEKGATGINVAGICCTGNETLMRHGTPIAGTFLQQELAVITGAVEAMVVDVQCIMPSLGNLTGCYHTKFISTSPKADFPGTARMEFHEEEAYATAKEIVKAAVENFPNRNLKKVSIPEEKQECMVGFSAEAILKALGGSPAPLIEAIAGGAIKGIGAVVGCNNVKIQHNYGHVNLVKELIKNNVLVVTTGCNAIACAEAGLLVPEAAALAGDGLKGVCEALGIPPVLHMGSCVDISRILVLASAVANSLGVDISDLPAAGAAPEWMSEKAVSIGAYVVSSGVFTVLGTIPPVLGSQAVTALLTKGLDGVIGASFAVEPDPFKAADLMLEHIEGKRKALGLK", "text": "FUNCTION: CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH). SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family."}
{"protein": "MQPRLLLLAAFLALLVLPEATKAEEGSLLDKMQGYVKEATKTAKDALSSVQESQVAQQARDWMTESFSSLKDYWSSFKGKFTDFWESATSPTQSPP", "text": "FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C3 family."}
{"protein": "MKFYIKTFGCQMNVNDSEKMAGILQTLGYTPTENWEEADVILVNTCSVREKPDQKVLSALGEFKKVKKHNPNAVIGVCGCLAQRAGYEIYQKAPFIDIVFGTTNIHHLPNLLEEAKSGNKAIEILEEIDENENLLDQFPTVRENKYTAFVTVIRGCDKKCTYCIVPTTRGRERSRRIGDILREVQYLVEDGVKEIHLIGQNVTAYGKDFGDVKFWELLKAVAEVDGVERIRFTTGHPRDLDEDTIKVMADLPQICEALHLPIQAGSDRILQAMDRGYTQKEYLQKIELLKKYIPNIALSTDIIVGFPGETYEDYLETVKVIKEVEYDQVFAFKYSPRPGTPAADLPMTESPEELSKRLNDLINLQKDITFKKNLEYQDKIVEILVEEINQENKLVGRTRTNKLVYAEGSPEYLGKLVNVKIEKVNRFSLEGSIIGGD", "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": "MNISIISVGKIKEKFLRAAIDEYSKRLSKYCKLNIIEVTDEKTPDNASLKEENIIREKEGSLILKHIKDNNFVIAIDLKGKSIASEEFSDLIENCRLTGNSTIAFVIGGSLGLSQQVLSRANYKLSFSKMTFPHQLFRVMLLEQVYRAFRILCGEPYHK", "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": "MKKKMRLKVLLASTATALLLLSGCQSNQTDQTVATYSGGKVTESSFYKELKQSPTTKTMLANMLIYRALNHAYGKSVSTKTVNDAYDSYKQQYGENFDAFLSQNGFSRSSFKESLRTNFLSEVALKKLKKVSESQLKAAWKTYQPKVTVQHILTSDEDTAKQVISDLAAGKDFAMLAKTDSIDTATKDNGGKISFELNNKTLDATFKDAAYKLKNGDYTQTPVKVTDGYEVIKMINHPAKGTFTSSKKALTASVYAKWSRDSSIMQRVISQVLKNQHVTIKDKDLADALDSYKKLATTN", "text": "FUNCTION: This protein is essential for production of active forms of the serine proteinase located in or secreted from the cell envelope. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the PrsA family."}
{"protein": "MSQKKSFQGLILTLQEFWAAQGCVILQPYDMEVGAGTFHPATTLRALGPKPWKAAYVQPSRRPKDGRYGENPNRLQHYYQFQVILKPNPPNLQELYLASLAAIGVDLKLHDIRFVEDDWESPTLGAWGLGWECWCDGMEVSQFTYFQQVAGFECAPVAGELTYGLERLAMYVQGVENVYDLDFNGAEGPDRITYGDVFLQAEQEYSRHNFEAADTAMLFRQFTDAEAACRSYLAAGAPDAEGARHRMAQPAYDQCIKASHVFNLLDARGVISVTERQSYILRVRELAKACGAAWLKTAAGGAP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MAIEMLGLILAGGQGTRLGKLTKDVAKPAVPFGGRYRIIDFALSNCANSNVKNVGVITQYQPLTLNAHIGNGAPWGLNGINRGVTILQPYFSQEGSKWFEGTSHAVYQNISYIDQQNPEYVLILSGDHIYKMDYEAMLESHKEREASLTVSVMEVPLEEASRFGIMNTDDNDRIIEFEEKPKEPKSNLASMGIYIFNWKRLREVLVNGYSKGNPMEDFGGDVIPAYIEAGENVFAYRFKGYWKDVGTIDSLHQSSMEFLDLNNELNITDKSWRIYSHNDISAPQFITEKSKVKNALVGDGCYVDGTVIHSILSQNVHVQEGTTIEDSFIMSGTFIGENVTIKNAIIGENAKIGDNVEIIGEDEVAVIGHGEIKGENKNEQ", "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": "MRRSPPKPWENNSGGGGSTSMTGSGGISRPMSGPQRTTSPGGGSSTTTQTSTLNNTGSPSTSVGGPLVTRPRTPMRPWESGGAGSSSIDSFGGGVGGSSGYRSSYGGGYRDSYSSGGYGSSGYGSSYGSGGSGGYGSSLYGGGGYSSGGYGGSGYGSSYGGGYGSSYGSGYGSSYGGSGYGSSYGGGYGSSYGGGYGGGYGGGYGQRGYDNMDGKGGALQSVVSSGHSWMEALHSIVDTFSRFSRLLDANFDAVHGSFSSIIRLCQSMSHFSYEIMAIIKTYSLFRMFQSVASRFLRVFRYLLGKKSKSNSSNNNTSSKFGSNAITESLRQANMDVSDFRNFQNEKKQSVGTLILIIAATFIGVPMVIGQLLNLRRRGQASRLDKGWEEQQGGGYGQVKAIYEFNPETTRDLPLRVGDIVNVIDKPHDNWWVGECNGLSGFFPVDFTEKISPNDINNNNNNNNNNNNNINTSVQIYDNNNGFNRNNSNNNLNNSEYSDYSSSNNNNNNNNNNNNNSNYQLQSNFSSNNDGISKNIIYNNNNDNQRPISPSKTSQQLSRSELMDKPYVEES", "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 (By similarity). 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 (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peroxin-13 family."}
{"protein": "MLNEPNALLRRDANSTIATVTELFPNEYSNADIAYVLLSTVVVFTVTPGIALYYAGMVRKNSALSILTQSFLVTAVVFIQWYLFGYSLACSSGSSFYGTLWQGGMNHLWLEPYIPGSTIPAIVYFPFGGLFAVATAQLFAGAMAERGRLIPSLVISFLYITLVYCPQAYWTWAPNGWLYTLGALDFAGGGPVHISSGFAALAYSLCLGRRIVVDEPDRPDSIRSTDNADLPSSSQNNCKANWKRWFGFKSVSWKNSFGRGKIAHNPPHDAGMVYIGVVLIWFAWLCFNSGTLLTVNIRTAYIMTNTLISSSFGALTWAIIDYIRYRKFSTIGICEGAIAGLVGITPACGFVFPWGAAAGGIVPALVCNFLHDLNEWIGVDETLRVFNLHGIGGIVGSIVLGVVAHPDVAASDGATVIDGGWAVHHWKQMGYQFAGFTSVAAWSFVITAIICLLVDLVPGLHIRASFEEELRGMDFVELEEQLPGQTLESKPMIIYAQEMDEPVTQGSNIKQEKQDEF", "text": "FUNCTION: Transporter for ammonium to use as a nitrogen source. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family."}
{"protein": "MFIISSKNMLQKAQHAGYAVPAFNIHNLETLQVVVETAAEMRSPLIVAGTPGTFSYAGMGNIVAIAGDLAREYNLPLAIHLDHHESLADIESKVMAGIRSVMIDGSHFPFEENVALVKSVVDFCHRYDTSVEAELGRLGGIEDDLVVDSKDALYTNPQQAREFVARTGIDSLAVAIGTAHCMYAAEPKLDFERLAEIRALVDIPLVLHGASGLPESDIRQAISLGVCKVNVATELKIAFSDALKEYFLQNPKANDPRHYMQPAKQAMKEVVRKVIHVCGCEGQL", "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": "MKKTPRSTARELALLALSQLPKKSGSLEKKQLQEVVLAAVRTLRIEAQDILETAAAELQRGSDRLLNSQIDTTDIESARVMLYEAIELGQTAINRIGTAVELPEMLQLTNQLEVRSYAMEVLTKVNGNRKEVDKLLQESIVDWQIERLPRIDLDILRIAVAEMMFIGIQKQVAISEAVELAKRYSGEDGYKFINGVLRRVFDKINVI", "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": "MSFLWGSTKSKKGKNKKAAGSLPSGVVPQQRVKPTRKNVPIDYPRTLEKVHGESLIFRTSLLSELVSTGKSGIGPPDLIHCTELDKFHDEKIGEFFYITGIDASSVSMPIAFLKLIKWNDGKKLKSASLKNDDITTYCTFNIFQKLDIRLRYESEDVYQVNIVDCLNGNNEIPLSDLIWEETFVSCCIRSVIINSDFERKIPGLVELPFVFENRCASDYKRVIDSLCKFLPRFLECGWDSTKSVYATILNNYLTESLLVFLSITPEFITDYAIQVLDNLMTNDPSNSRYYAIVIISIMERSNDRDVEMIKRIHEILDLLLPVLYGLPSDEPYISDLINCITDVLSIQARFLLNNNDYELSLSISTLATNLSSDNFESWYLLSKGYIFSQQYDKALLSINSMPCLAEYDIVKQAQINAFKFYMNYYKAPLCHSREHCTMTSHELNHLMNIMHYENELELKTIIFGRTVMPNESKYGCIEEIWNKSCLELGPICGPQSDNLINFVSQQEVNTVGDMLLLKRSKETRQESWFIKQVRLLLMELVARIGWNALLQLRSDVFVMESKFKMIESSDKLSTELRQKRLCQRWFDAMFLDVYEDLSISTSSQENKATAKYSGLEWELLGLTLLRVSDLPDAVACLRTSILARFDPISCHHLLNFYLTMDFNDEFMRRFDVDIILDLLVKLISFRIRFYDRFQIFSLQVLRKLEGQLGSEIIKNKIINSPYGQAGITSVIDYMLECLSKNRNEACLAYERPLPDLPSTIKPLAD", "text": "FUNCTION: Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Note=Trans-Golgi network location requires interaction with CHS5 and with myristoylated GTP-bound ARF1 for the recruitment to the membranes. SIMILARITY: Belongs to the CHAPS family."}
{"protein": "MPRKGPAPKRPLVNDPVYGSQLVTQLVNKVLLKGKKSLAERIVYGALENAREKTGTDPVITLKRALDNVKPALEVRSRRVGGATYQVPVEVRPDRSTTLALRWLVSFSRQRREKTMVERLANEILDASNGLGASVKRREDTHKMAEANRAFAHYRW", "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": "MSKITTTNLLKMKQEGQRITAITAYDATFAKLFDDEGAHVLLIGDSLGMVLQGGQDTLGVSMDEMVYHTRCVVRGTTNALVVTDMPFMSYATPEQTYQNAARLMAAGARMVKMEGGDWLCDSIRHLTRNGVPVCGHLGLTPQSVHVFGGFKVQGRDEFQAQEIYRQALELQAAGIQLLVLECVPTSLAERISKALRIPVIGIGAGPATDGQILVMHDAFGITSGYVPKFTKNFLAETGDMRAAIRLYVKQVSEGTFPGPEHCFN", "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": "MTTGIRVPTLGESVTEATIGKWFKKLGEAVAVDEPLVELETDKVTVEVPSPVMGKLTEIIAKEGDIVEVNAVLGFVESGAAGISQSFSPSATSIPEAPSELEQSPSSSATPSGTMPPAPSAAKLMAENNIAKSDISGSGKRGQILKEDVLGALAQGTKASTSVATLTASSSSAAPIQEMREERVRMTKLRQTIARRLKDAQNTAAMLTTFNEVDMSAVMDLRKRYKDLFEKKHGVKLGFMGFFTKAVCHALKEFPTVNAEIDGTDIVYKNYVNAGIAVGTDKGLVVPVVRDADQMSLAEIEKEISRLGRLARDGKLAVSDMQGGTFTITNGGVYGSLMSTPILNAPQSGILGMHAIKERAMVVGGQIIICPMMYLALSYDHRIVDGQEAVTFLVRVKESLEDPERLVLDL", "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": "MSLSIFKDLPEEHPRHLIPSLCRQFYHLGWVTGTGGGMSIKHNDEIYIAPSGVQKERMQPEDLFVQDITGKDLQLPPEIRGLKKSQCTPLFMLAYQHRGAGAVIHTHSQHAVMATLLWPGKTFRCTHLEMIKGVYDEADKRYLRYDEELVVPIIENTPFERDLADSMYAAMMEYPGCSAILVRRHGVYVWGQTWEKAKTMSECYDYLFSIAVEMKKAGIDPEKFEST", "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": "MKLFGWMQNKLNGKQGNKKPNTVPITTHPAKQEPREEFSDWPHGLLAIGTFGNNDLKENAAESQDIQEDPTSSEEILDNFTPEEVGKLHKELTKLLTRKPNIEKEIADLPLDRFLNCPSSLEVDRRNSNALCSDSADDHKDEDIEKTISVILGRCKEICGDKNKKAIGKKSISFLLKKMFVCRSGFAPQPSLRDTLQESRMEKLLRVMLNKKIINPQGSSRAASMKKYLEDRQIPTKKESNTEDDTKEKINNGCKWVKTDSEYIVLEI", "text": "FUNCTION: Involved in the development of the root system architecture by influencing lateral root angles and primary root length. SIMILARITY: Belongs to the LAZY family."}
{"protein": "MEEIEELIYKYALQNAYKHGGKAQDKAVVSKIFVERPDLRSRAKEISEIAKKIVEKVNSMSIQDQERELKEKYPDLLEEKKKEEPEKKTLPPIKVEGKFVTRFAPNPDGPIHLGNARAAIISYKYAEMYKGEFILRFDDTDPKVKKPIKEAYDWIRKDLKWLGIKWDKEVKASERLEFYYSMAKELISKGFAYVDTCSEEEFKKMRDASKPCPNRLKSAEDNLYLFEKMLNGEFKEGEAVVRIKTDLSLPDPSQRDWVLLRIIDVKKNPHPITGDKYWIWPTYNFASALDDHDLGITHIFRGKEHEVNAEKQKWIYNYMGWKYPYVEEFGRLRLEGFMMSKSKIRTVLEKGVSIDDPRLPTLAGLRRRGILPETIIETIITVGLKVSDATISFDNLAALNRKKLDPIAKRLMFVQQPKEFIIELSEPIRAKIPYNPSKPSEYREILVNPGDKILLDAKDAEEGAVVRLMELCNVTISGNKLIFHSKTLEDAKKLNAKIIQWVKKDEASNVEVIIPDPNEEKPPISGYGEKEIGNLKINEIVQFIRFGFVRVDNKIDNKVTVIFSHE", "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": "MTITRAITLRTILDSRGRKTVEAEVRTEHGFGRAAAPGGASTGIHEAAVRDPLLAIADAQGQVIPHLIGIDSSDQIGVDSLLHEIDGTDNFSGIGANVAVALSLAMAKAAADATNIPLWQHIGGIFVDSAPRPLGNIIGGGAHASHATQFQEFLVVPTGCERVRDGIFANAQVHKTVYDLLKKRGIRAGKGDEGAWAPPISDPEAFRILAEAISLVSDETGFEISPGIDAAASQLYDPESGMYRYRDGTVRSPEDQVTYIADLIDEFDLIYVEDPLYEEDYEGFAALNREAGNRCLICGDDLFVTNTKRIQEGISHGSANCVLIKPNQIGTLTDTHEAIHLAKRHGMETVISHRSGETEDTTIAHLGCAFQCIFIKTGVVGGERTAKLNELIRIEESIYERK", "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": "MPRFVDRVVIHTRAGSGGNGCASVHREKFKPLGGPDGGNGGRGGSVVFVVDPQVHTLLDFHFRPHVTAASGKQGMGSNRDGAAGADLEVKVPDGTVVLDDNGRLLADLVGAGTRFEAAAGGRGGLGNAALASRARKAPGFALLGEPGQARDLTLELKTVADVGLVGFPSAGKSSLVSVISAAKPKIADYPFTTLVPNLGVVAAGGHSFTVADVPGLIPGASQGRGLGLDFLRHIERCAVLVHVVNCATAEPGRDPISDIDALEAELAAYQPTLQGDAVLDDLAERPRAVVLNKIDVPEARELAEFVEDELAQRGWPVFLVSTVTRENLQPLIFGLWQMVSEYNAARPQAAPRRPVIRPVPVDDSGFDVQADGHGGFVVTGARPERWIGQTNFDNDEAVGYLADRLVRLGVEEELLRLGAKPGCAVTIGEMTFDWEPQTPAGGHVAMSGRGTDVRLERSDRVGAAERKAARRQRRERDDD", "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": "MQFSTTPTLEGQPIVEYCGVVTGEAILGANIFRDFFAGIRDIVGGRSGAYEKELRKAREIAFKELGEQAKALGADAVVGIDIDYETVGKDASMLMVSVSGTAVKTRR", "text": "SIMILARITY: Belongs to the UPF0145 family."}
{"protein": "MNWLLVIAGAAAGAPLRYLTDRAVQTRHDTVFPWGTFTVNVTASLLLGLVAGAAGAGAPPAWVASEQVVSLVGTGLCGALSTYSTFSYETLRLAEDGARLLAAANVAGSVLAAFGAAALGAALARAVWG", "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": "MPKLEMMLLVLLILPLSSFSAAGEQVVQGDRRSDGLARYLQRGGRDVQECQVVTPGSKWGRCCLNRVCGPMCCPASHCYCIYHRGKGHGCSC", "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": "GGADVFADNCSTCHVNGGNVISAGKVLSKTAIEEYLDGGYTKEAIEYQVRNGKGPMPAWEGVLSEDEIVAVTDYVYTQAGGAWANVS", "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": "MGNQKLKWTAEEEEALLAGIRKHGPGKWKNILRDPEFADQLIHRSNIDLKDKWRNLSVPPGTQSLTNKARPAKVKEEGDTPAADANDAVTIPRPIPTIPPPPGRRTLPSELIPDENTKNAPRYDGVIFEALSALADGNGSDVSSIYHFIEPRHEVPPNFRRILSTRLRRLAAQSKLEKVSTFKSIQNFYKIPDPSGTKIGVPKPKETHTKLRQANNQTSADSQQMIEEAAITAACKVVEAENKIDVAKLAAEEFEKMTKIAEENRKLLVIATEMHELCSCGETMLLA", "text": "FUNCTION: Binds preferentially double-stranded telomeric repeats. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H1/H5 family. SMH subfamily."}
{"protein": "MVTMKDLLECGVHFGHQTRRWNPKMKKFIFGVRKNIYIIDLQKTLRYFRYTYNVVRDRAAEGQTMIFVGTKKQASETIKKAAISCGMPYVNHRWLGGMLTNFGTIKKSIRKLEIIKKMREEGQLDLLTKKEALMLTRKEEKLELYLGGIKEMNKLPDMMFVLDAVKEKIAIQEARRLGITVVAPLDTNCDPDVVDLPIPGNDDAIRSIHLFCNEMAAAMNEGKAALADETGVEVEPISAEEKEELIAEAVAEGEEFNFAEEGENA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MTDLNIPHTHAHLVDAFQALGIRAGQALMLHASVKAVGAVMGGPNVILQALMDALTPDGTLMMYAGWQDIPDFIDSLPDALKAVYLEQHPPFDPATARAVRENSVLAEFLRTWPCVHRSANPEASMVAVGRQAALLTANHALDYGYGVESPLAKLVAIEGYVLMLGAPLDTITLLHHAEYLAKMRHKNVVRYPCPILRDGRKVWVTVEDYDTGDPHDDYSFEQIARDYVAQGGGTRGKVGDADAYLFAAQDLTRFAVQWLESRFGDSASYG", "text": "FUNCTION: Resistance to antibiotics containing the 2-deoxy-streptamine ring including dibekacin, gentamicin, kanamycin, sisomicin, tobramycin and neomycin, but not to amikacin or netilmicin (PubMed:1649572). Acetylates a broad range of both 4,5- and 4,6-disubstituted aminoglycosides, including neomycin, paromomycin, ribostamycin, sisomicin, gentamicin, tobramycin and kanamycin, with no preference of one disubstitution over the other. Acetylates sisomicin and kanamycin most and least efficiently, respectively. Does not modify plazomicin (PubMed:35921328). SIMILARITY: Belongs to the antibiotic N-acetyltransferase family."}
{"protein": "MLKIFNTLSRQKEEFKPIHAGQVGMYVCGITVYDLCHIGHGRTFVAFDVVARYLRYLGYSLKYVRNVTDIDDKIIKRAAENGETSDQLTTRMIAEMHADFDALNILRPDAEPRATHHITDIIEMVETLIARRHAYVASNGDVMFSVDTAPGYGVLSRQDLDQLQAGARVEITEVKRNPMDFVLWKMSKPGEPHWSSPWGEGRPGWHIECSAMNCKQLGEHFDIHGGGSDLMFPHHENEIAQSSCAHDGPYVNYWMHSGMVMVDREKMSKSLNNFFTVRDVLAYYDPETVRYFLMSGHYRSQLNYSEDNLKQARAALERLYTALRGTDPDAAAQGGDEFEGRFREAMDDDFNTPEAYSVLFDMAREVNRLKTEDAQAANQLASALRKLSGVLGLLEQDPEQFLQNGAQVDNDEVKEIEALIQQRKDARAAKDWALADQARDRLNEMGIVLEDGPQGTIWRRK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MTMTKQSSLSPGSRLYDYTTQDGAAWRVSALKEVSYDVVVQPRLLDPANPALADALSSGTTPARRLIVIDATVRSLYGEQLAAYLAGHDVEFHLCVIDAHESAKVMETVFEVVDAMDAFGVPRRHAPVLAMGGGVLTDIVGLAASLYRRATPYVRIPTTLIGMIDAGIGAKTGVNFREHKNRLGTYHPSSLTLIDPGFLATLDARHLRNGLAEILKVALVKDAELFDLLEGHGASLVEQRMQPGEGGTGGAALTVLRRAVQGMLEELQPNLWEHQLRRLVDFGHSFSPSVEMAALPELLHGEAVCIDMALSSVLAHHRGLLTEAELGRVLDVMRLLHLPVLHPVCTPDLMRAALADTVKHRDGWQHMPLPRGIGDAVFVNDVTQREIEAALLTLAERDRVPRWRALHGAVDMGV", "text": "FUNCTION: Catalyzes the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone. Involved in validamycin biosynthesis. SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EEVS family."}
{"protein": "MEARAQSGNGSQPLLQTPRDGGRQRGEPDPRDALTQQVHVLSLDQIRAIRNTNEYTEGPTVVPRPGLKPAPRPSTQHKHERLHGLPEHRQPPRLQHSQVHSSARAPLSRSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPVADGIIRVQPKSELKPGELKPLSKEDLGLHAYRCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT", "text": "FUNCTION: Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity). Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity). Inhibits TGFB- induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity). Inhibits CBL/C-CBL-mediated EGFR ubiquitination (PubMed:17974561). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, ruffle membrane Note=Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated ith EGF (epidermal growth factor). SIMILARITY: Belongs to the sprouty family."}
{"protein": "MINAQEISALLKQQIEGFQPDFDYTETGVVTYIGDGIARAQGLDNAMSGELLVFENGTIGMAQNLETNDVGIIILGQFTDIREGSVVRRTGKIMEVPVGSALIGRVINPLGQPVDGLGEIRTSKTRPIEYPAPGVMQRKSVNEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRQYGALDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYEGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDELGGGSITALPFIETQAGDISAYIATNVISITDGQIFLKDDLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTQFGSDLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVLILYALTNGFLDSVPIDDILAFEEELYAYFDLHYDGLLDVIRTTKDLPDTDELNAAIQAFKDQSVFK", "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": "MSNNKKLTSLFGAPVSDRENSMTAGPRGPLVMQDWYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTNDITQYTSASIFSEVGKQTEMFARFSTVAGERGAADAERDIRGFALKFYTDEGNWDLVGNNTPVFFFRDPKLFASLNHAVKRDPRTNMRSAQNNWDFWTSLPEALHQVTILMSDRGIPKGYRNMHGFGSHTYSMYNDKGERVWVKFHHRTQQGIENLQPDEAAKIIADDRESSQRDLFEAIENKDYPKWKTYIQVMTEEQARNHKDNPFDLTKVWYKGDYPLIEVGEWELNRNPDNYFQDVEQAAFAPTNIVPGIDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNQPKGVGVENICPFSRDGQMRILDNNQGGGTHYYPNSDGSFEDQPEFKKPGLKVEGEAYEYDFRQDDDNYFEQPGRLFRLQSKEQQERIFENTANEMQGTTLEVQHRHIRHCYKADSEYGKGVARALGVDINDVDLEIKD", "text": "FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. SIMILARITY: Belongs to the catalase family."}
{"protein": "MSERIFIEGESCKSAWHNATAGYDDTDTHLEILGKPVMERWETPYMHSLASVAASKGGRVLEIGFGMAIAATKLEEYNIEEHWIIECNDGVFKRLQEWATKQPHKIVPLKGLWEDVVPTLPDGHFDGILYDTYPLSEETWHTHQFNFIKGHAYRLLKPGGVLTYCNLTSWGELLKAKYNDIEKMFQETQIPQLVDAGFKSENISTTVMDLIPPEDCRYYSFKKMITPTIIKV", "text": "FUNCTION: Converts guanidinoacetate to creatine, using S- adenosylmethionine as the methyl donor. Important in nervous system development. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family."}
{"protein": "MNRATITSNKSNAPSFLSIPLLAHNNNINNNNNNINNNNNNNNINSNNNGTTTTTTTTTITTISYKNNISELITIIDKIIKDLNNFKSKTVLNDQEFSELNNTIQFTKTSLVNYIHYENENKINFNLSDSKIICSEIKIIEYGIESFIFSICKLYQDLIQFQQLLLKLSSPPTTITFNTTINSTNSFTSNLIINNLLKVDSILKQSIDQLLALFPPSSSSLNNENNNNNNNNYNPYELLSNEAKVLWNQFGGNKITFVPWSIFFKGFQKFFNKEILAYESSLRYTLDFTRDGYVTPFKLSVFIKWFGALPVSLGIFQDVINSKIFSGFISGIEATQLLSRQQVGYYLLRCSKTIVGAFAITFVDSTNHIRHCLLYPVTSSINGGLTLQKPPDIFKSILSFILSFSSKLKYPIGPLDNDLLPPLSIINNNPILILPDENNNNQNNNQNNNNNNINTFSTSPSSFFTIDSSNSSDTNKSPTKSRKSSFKNDKDKKEKEKEKGKDKEKEKERVSDENFDNLPTFLNSEDENDNNNNNNNNNNNNNNNNNNNNNNNNNNSSNNNNCNIKETHQTTSNGSSGNNNNNNNNNNNNNNNNNNNNSSSTTKRNNNNNGSDESKDLCTVCMDNEINTVFLECGHLSCCSLCSVKLKKCPICRSRITRVINIFKS", "text": "FUNCTION: Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Up-regulates STATc tyrosine phosphorylation via an inhibitory effect on ptpC accumulation. Recognizes activated receptor tyrosine kinases, RTKs and terminates signaling. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=A very small proportion appears to be nuclear but this may reflect cytoplasmic contamination of the nuclei."}
{"protein": "MNEETSMDEGEQEKIELIMGLRRQGIRDKRVLSALERVPREKFISATFRKQAYEDHALPIECGQTISQPYIVAYMTEQLHVGERMKVLEVGTGSGYQAAVLSRLCRRVYTIERYRTLLKDAVKRLEDLHIHNVTAKVGDGAQGWPEQAPFDRIIVTAAAPSVPQKLVDQLKEGGLMIVPVAVSGARGEQKLVRIERTGDGVKREELLPVRFVPLVEGVAKES", "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": "MLDNTRLRIAIQKSGRLSDDSRELLARCGIKINLHTQRLIAMAENMPIDILRVRDDDIPGLVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYLTLRRLDFGGCRLSLATPVDEAWDGPAALDGKRIATSYPHLLKRYLDQKGVSFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRDGEMAQSKQQLIDKLLTRIQGVIQARESKYIMMHAPSERLEEVIALLPGAERPTILPLAGEQQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME", "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": "MIAIIDYGSGNLRSIANAFRKIGADALVTSDPQILEAADALVLPGVGAFGSAMAKLEGLRETLLGNIMDGKPFLGICLGLQVLLSESQESPGVHGLDLIPGRVIRIPPGNKVPHMGWNQLIIVEDSQLLEGAEDEYFYFVHSYYAEPSNDVVVARTDYGVEMTAAIESDNIHATQFHPEKSGEAGLDVLRNFVEIIRA", "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": "MVGRRKALLFSLCFFFLSLPSFSSLPSFQTLFPNSHSLPCASPVSFQPDSDSESLLESEFESGSDSESSSSITLNLDHIDALSSNKTPDELFSSRLQRDSRRVKSIATLAAQIPGRNVTHAPRPGGFSSSVVSGLSQGSGEYFTRLGVGTPARYVYMVLDTGSDIVWLQCAPCRRCYSQSDPIFDPRKSKTYATIPCSSPHCRRLDSAGCNTRRKTCLYQVSYGDGSFTVGDFSTETLTFRRNRVKGVALGCGHDNEGLFVGAAGLLGLGKGKLSFPGQTGHRFNQKFSYCLVDRSASSKPSSVVFGNAAVSRIARFTPLLSNPKLDTFYYVGLLGISVGGTRVPGVTASLFKLDQIGNGGVIIDSGTSVTRLIRPAYIAMRDAFRVGAKTLKRAPDFSLFDTCFDLSNMNEVKVPTVVLHFRGADVSLPATNYLIPVDTNGKFCFAFAGTMGGLSIIGNIQQQGFRVVYDLASSRVGFAPGGCA", "text": "FUNCTION: Aspartyl protease. Not able to cleave BAG6. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MNIHEYQGKEIFRSMGVAVPEGRVAFTAEEAVEKAKELNSDVYVVKAQIHAGGRGKAGGVKIAKSLSEVETYAKELLGKTLVTHQTGPEGKEIKRLYIEEGCAIQKEYYVGFVIDRATDQVTLMASEEGGTEIEEVAAKTPEKIFKETIDPVIGLSPFQARRIAFNINIPKESVNKAAKFLLALYNVFIEKDCSIVEINPLVTTADGDVLALDAKINFDDNALFRHKDVVELRDLEEEDPKEIEASKHDLSYIALDGDIGCMVNGAGLAMATMDTINHFGGNPANFLDAGGSATREKVTEAFKIILGDENVKGIFVNIFGGIMKCDVIAEGIVEAVKEVDLTLPLVVRLEGTNVELGKKILKDSGLAIEPAATMAEGAQKIVKLVKEA", "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": "MLNRYPLWKYIMLVVVIIVGLLYALPNLYGEDPAVQITGVRGVAASEQTLIQVQKTLQEEKIPAKSVALEEGAILARFDTTDTQLRAREALMSVLGDKYVVALNLAPATPRWLAAIHADPMKLGLDLRGGVHFLMEVDMDTALGKLQEQNIDSLRSDLREKGIPYTTVRKENNYGLSITFRDSKARDEAIAYLTPRHRDLVISSQSGNQLRAVMTDARLSEAREYAVQQNINILRNRVNQLGVAEPVVQRQGADRIVVELPGIQDTARAKEILGATATLEFRLVNTNVDQAAAAAGRVPGDSEVKQTREGQPVVLYKRVILTGDHITDSTSSQDEYNQPQVNISLDSAGGNIMSNFTKDNIGKPMATLFVEYKDSGKKDANGRAVLVKQEEVINIANIQSRLGNSFRITGISNPNEARQLSLLLRAGALIAPIQIVEERTIGPTLGMQNIKQGLEACLAGLVVSILFMIFFYKKFGLIATSALVANLVLIVGIMSLLPGATLSMPGIAGIVLTLAVAVDANVLINERIKEELSNGRTVQQAINEGYAGAFSSIFDANITTLIKVIILYAVGTGAIKGFAITTGIGVATSMFTAIIGTRAIVNLLYGGKRVTKLSI", "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": "MFSHLLKPAARSAGLLGHVNRRYLATVHTNTAREIPKPSRKPTPISLENATFTIKNGPIFSGKSFGAKANISGEAVFTTSLVGYPESMTDPSYRGQILVFTQPLIGNYGVPSSARDEHGLLRYFESPNIQASGIVVQDYALKHSHWTAVESLAQWCAREGVPAISGVDTREVVTYLREQGSSLARITVGEEYDADEDEAYIDPEAINLVRRVSTKAPFHVSSSLGDMHVALIDCGVKENILRSLVSRGASVTCFPFDYPIHKVAHHFDGVFISNGPGDPTHCTSTVYNLRKLFETSQLPVMGICMGHQLIALAAGAKTIKLKYGNRAHNIPALDLTTGKCHITSQNHGYAVDPTTLTSEWKEYFTNLNDQSNEGLIHASRPIFSAQFHPEAKGGPMDSSYLFDKYIQNVQRYKDHQSSFSEKSNKPSPLLVDLLSKERVGVHPAQPDFEMHVPGRVEQVDVGGPVAPPYQPITAAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CarA family."}
{"protein": "MQITREKWSKNFSEWFDWVLREGEFYDYGRYPVKGMGVWMPYGFKLRQNIISIIRNLLDSTGHEEVLFPLLIPEDLLSRESTHIKGFEEEVFWVTKGGSEDLDVKLALRPTSEVAITTMENLWLKSYKQLPKKYYQIVSVFRYETKATRPMIRLREITTFKEAHTVHETYDDAQRQVEEAIEIYKKIFNNLTIPYVLSERPEWDRFAGALHTYAFDTIMPDGKVMQIGTVHHLGQNFSRALDFKIQKKDGSLDYPHQTSYGISDRAIASVIAIHGDDHGPILPPSVAPIKVVVVPIPAKNEEGTQQVMKYSIEICEMLNKNNITCVTDQDTEKTPGEKFYIWEIKGVPIRLEIGPRELASSTVFIKRRDNLKSYTVKKEEVVNKVKEVLNEIQEDLRKRAWESLKSRIEYANDIEKAKNILENNSGIVEVPWCGSKECGLKIEELTNARVLGYPIEDRKVNDKCVICKMNAKTVLRVAKTY", "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": "MMTGNLNGGGRGGEGPCGACKFLRRKCVKGCVFAPYFDAEQGTARFAAVHKVFGASNASKMLLRLPLHKRLDAVVTLCYEAMARIRDPVYGSVGHLFSLQHQVMNLQAELAHVQARLSTIQRFPLQSPQQMQPPSFDPAHNNEYAMEPSNLDSVWGEEHLLQDGTGDGDFQELASQFVSRYLPAVKLPACT", "text": "SIMILARITY: Belongs to the LOB domain-containing protein family."}
{"protein": "EWCGTNSDCGEGECCTGGSFNRH", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the u-CNTX family."}
{"protein": "VVGGDECNINEHPFLV", "text": "FUNCTION: Snake venom serine protease homolog that may act in the hemostasis system of the prey. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MSWLFGVNKGPKGEGAGPPPPLPPAQPGAEGGGDRGLGDRPAPKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDLPQQEERERLVRLHFDNCVLKPATEGKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASKDGVLTEAMMDACVQDAVQQYRQKMRWLKAEGPGRGVEHPLSGVQGETLTSWSLATDPSYPCLAGPCTFRICSWMGTGLCPGPLSPRMSCGGGRPFCPPGHPLL", "text": "FUNCTION: May play a role in a mitochondrial network organization typical for stem cells, characterized by reduced mitochondrial metabolism, low mtDNA copies and fragmentated mitochondrial network. may act by suppressing ATAD3A function, interfering with ATAD3A interaction with matrix nucleoid complexes. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein Note=Has been found to co-purify with nucleoids (PubMed:22453275). Since it does not face the mitochondrial matrix, the association with nucleoids could be mediated by ATAD3A. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MEIILFDNKINSRFNKVTSTNYAAKLDQTSEIWLFNCIENTQHIFLKSQLKLSQITKIFISGTSFKYAAGLPGLLSSLTLSGKINTVSIYGPNSLKAYLQACTKYSQTNFSFSVNFHAVSYGKLVSGQSYTVICLPLSSNKLLYGFTILKKQQQGVFNLKKAITLNISQGPIYGELKGKHNFLSPDGYYLHGEDFSSSTTLGNKISIPVVLKYSRIISEMHWLSSYTVKSNTYPHQQATKYLLSNIETNVMNYQVSQDNNLIE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AtsA family."}
{"protein": "MNKTITPSLETIERNWFLVDAKDKTLGRLATEIATVLRGKNKPTFTPHLDTGDFVIVVNAEKVEVTGKKASQKLYRRHSGRPGGMKIEKFESLQERIPERIIEQAVKGMLPHNSLGRQQFKKLKVYKGADHPHAAQNPVLLNS", "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": "MSTQPSKDLETFPNPRPERDFVLHMRIPEFTCLCPKTGQPDFATIHLDYVPDERCVELKSLKLYMWSFRDQGAFHEAITNEILDDLVRATEPRYMKVTAEFYVRGGIYTTVVAEHRKPGWAPAPKVELA", "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": "MSFDRSRIPTWRQGYRYQYEPAQKGHVLLYPEGMIKLNDSAALIGGLIDGERDVAAIIAELDKQFPGVPELGEDIEQFMEVARAEHWITLA", "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": "MAKAKFERTKPHCNIGTIGHVDHGKTSLTAAITKVLAESGGATFRAYDSIDAAPEERARGITIATAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPALVVFLNKMDMADPDLVELVEMEVRDLLSKYEFPGDDIPIIKGSALCALEDSNAELGREAILKLMEAVDSYIPQPERPKDKPFLMPVEDVFSISGRGTVVTGRVERGIIKVGDEVEIVGLKATVKTTVTGVEMFRKLLDQGEAGDNIGALLRGTKREDVERGQVLAAPGSITPHTNFSGSVYILNKEEGGRHTPFFTNYRPQFYFRTTDVTGVVTLPEGVEMVMPGDNVTVSVELIAPIAMDEGLRFAIREGGRTVGSGVVASITK", "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": "MAVGSTTTRAGEAALERLRQWPGEHRVAIGLSGGVDSSLTAALLVEAGWEVEGLTLWLMSGKGACCAEGLVDAAGICEQLGIPHHVVDMRETFQQEIVQRLVDGYRDGITPLPCSQCNRSVKFGPMLDWALQERKLPRIATGHYARIRHGGDRGRHQLLRGLDTRKDQSYFLYDLPQEVLGRIVFPLGELTKPDTRLEAARHGLRTAEKPESQDLCLADHHGSMRAFLDAYLPPRQGEIVLADGTVVGEHDGIEHFTVGQRKGLGVAWGEPLHVIRLDAAMNRVVVAPRAEAGRDSCVVGAVNWVSIDPIEAPRTVEVQVRYRSTPVRAELSPLPAIEADQQRERPHRCRLSFEEEQFSITPGQAAVFYDGETVLGGGLIQRE", "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": "MSKQADSLGFEQDAKPENVVWHRHAVDKAQRATLKQQRPAVLWFTGLSGAGKSTVAGALENRLAALGYHTYLLDGDNVRHGLCSDLGFSEQDRRENIRRIGELAKLMSDAGLIVLTAFISPHRAERQMVRDLLPNGEFLEVYVNTSLDVCEARDPKGLYKKARAGEIRQFTGIDSAYEAPLNPDIDLPAGEKSVDELVAQCLQALAERHIIQRWV", "text": "FUNCTION: Catalyzes the synthesis of activated sulfate. SIMILARITY: Belongs to the APS kinase family."}
{"protein": "MSIPEITQTLLQAKKDKGLSFADLEATLGRDEVCIAALFYRQASASEEEAKLLVEALGLDSSYIKHLTEYPVKGLGPVVPTDPLIYRFYEIMQVYGFPIKEVIQEKFGDGIMSAIDFTLDVEKEADPKGDRVKITMSGKFLPYKKW", "text": "FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family."}
{"protein": "MLKLVIIENMAEIMLFSLDLLLFSTDILCFNFPSKMIKLPGFITIQIFFYPQASFGISANTILLLFHIFTFVFSHRSKSIDMIISHLSLIHILLLFTQAILVSLDFFGSQNTQDDLRYKVIVFLNKVMRGLSICTPCLLSVLQAIISPSIFSLAKLKHPSASHILGFFLFSWVLNMFIGVIFCCTLRLPPVKRGQSSVCHTALFLFAHELHPQETVFHTNDFEGCHLYRVHGPLKRLHGDYFIQTIRGYLSAFTQPACPRVSPVKRASQAILLLVSFVFTYWVDFTFSFSGGVTWINDSLLVWLQVIVANSYAAISPLMLIYADNQIFKTLQMLWFKYLSPPKLMLKFNRQCGSTKK", "text": "FUNCTION: Putative pheromone receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGEKPNRIGRANISYINHDHIFLPSFQPSYPSRQLHPLISSQNKVHSSIVHLPKVASPSSPETQQHSQAPLFITHIMSGLPQALASGFAARVREGGTTLYINTTPMLRSARHNTAVNYAEFEEDFDANDFEDDDDDDQSQRESRDGSEEAEGDEDGTKKEEQDKFAGLKAPLVSNEPKRAAPPVRPVMYPQEVLEELSQVKEPTLIPIRVAVENIDVFRVQDFFLWDADEKILTPEQFATLTCADLDVPIGYSAQMSAQIKKQLAEYTAAPALPKDVEVHVIVELAVTVDKIVYEDKFEWDLSGEYATPQEFARTVVQDLGLGQEFYPAITYQLYETLGKLQKAWLERSIPLDVDNRAAFGLEAGLRVDQDNLGESWVPRVEEMTPEEMQKREMERDRSSRRLKRESARMAEVPYVDLDSLYSRKRRRRFDEDSRSGSPMW", "text": "FUNCTION: Part of the chromatin structure-remodeling complex (RSC) which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and required for cell cycle progression (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNF5 family."}
{"protein": "MANPFLLSLSLCLVLLYTSACLGEGLDRFNECQLDRLNALEPDNRIESEGGVTETWNSNKPELRCAGVAFEKHTIEPKGLHLPSYTNYPQIIMIVQGEGALGISVPGCTETFEEAQQSQSRQERRRGQRSQSQEQEDSHQKIRHFREGDILVIPPGTPYWTYNYGDEQLVAINLLDTTSLSNQLDPNPRRFYLAGNPEEEYPETQQQRQQRQQHQRPSGRRHGQHQKEEEQEGKNNILSGFDPQFLSQALNIDEDTVHKLQNPNERIKQIIRVEEGLGVISPKWQEQEEEEEEKEEPRQRRRRERREEREEEEKEEEDEPRESRRHRGGHEEEEVEEERGRGRGGSEWKRTTRRRHTRGDEGQEEEETTTTTEERRRRRGGRGSRQEEEEEQSPPRSRNGLEETICTAILRENIADPTRADLYNPTAGRISTANSLTLPILGWFQLSAEYVNLYRNGIYAPHWNINANSVIYVIRGRGRVQVVNSQGNSVFNDDLRRGQLLVVPQNFVVAHQAGDEGFEFIAFKTNDQATTSPLKQVFRGIPAEVLANAFRLSLNQVSELKYNGNHNPLVTPQSQSQDHNLVKVA", "text": "FUNCTION: Sulfur-rich seed storage protein. This protein found in the seeds of many leguminous and non-leguminous plants is the source of sulfur-containing amino acids in seed meals. SIMILARITY: Belongs to the 11S seed storage protein (globulins) family."}
{"protein": "MEKVYVAGAIPEVGLKLLQEHFEVEMYEGKGLVDKDTLIKGVKNATALISLLSTNVDKDVIDAGKDLKIIANYGAGFNNIDIEYAREKSIDVTNTPKASTNATADLTIGLVLAIARRIVEGDQLSRTTGFDGWAPLFFRGREVSGKTIGIIGLGEIGSAVARRARAFDMDVLYTGPNRKEEKEREIGAKYVDLDTLLKNADFITINAAYNPKMHHLIDTEQFKMMKSTAYLINASRGPIVHEQALVQALKDNEIEGAALDVYEFEPDITDDLKSLNNVVLTPHIGNATFEARDMMSKIVANAAISAVQGEKPQFVVN", "text": "SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
{"protein": "MASLREIQMRINSTKSTKQITKAMNMVSASKLNRAQAHSAKFQPYMLKMQEVLGTIANGTTGASHPMLEKRPVKKTGYIVITSDRGLAGAYNANVLREVYREINEKHTTDSYVLFVVGKVGVQFFRSRGITVTDAITGLNDSPSYVDVAEIVKRTVSAFTLGEIDELKLCYNHFMSVISQEVKVETLLPLGEIEASSSTTYEYEPSEEQILAELLPRYAESLIFGALLDAKVAEHASRMTAMQSATDNADDLIGRLTLVYNRARQAAITQEITEIVSGAAAQQ", "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": "MKSFLVDQDGYYGEFGGAYVPEILHKCVEELQNTYLDVIESEDFKKEFDQLLRDYVGRPSPLYPARRLSEKYGCKMYLKREDLNHTGAHKINNTIGQILLARRMGKKRIIAETGAGQHGVATATVCALMNMECIVYMGKTDVERQHINVEKMKMLGATVVPVTSGNMTLKDATNEAIRDWCCHPSDTYYIIGSTVGPHPYPDMVARLQSVISEEIKKQLQEKEGRDYPDYLIACVGGGSNAAGTIYHYIDDERVRIVLAEAGGKGIETGMTAATIQLGKMGIIHGARTFVIQNEDGQIEEPYSISAGLDYPGIGPMHANLADKKRAMVLAVNDDEAIRAAYELTRLEGIIPALESAHALGALEKITFKPEDVVVLTVSGRGDKDIETYLG", "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": "MSDNKPSEGDNKLQLKAPRRIVLKKTVEGSSIKQNFAHGRSKSVAVEVRRKKTFLKPGSKEGGFLIDQEKPEEIEEKKEAPKSPKRGEERHILRPLTPEEIEAKQKELEAKRQAEEEAARQKAEQEAARQKQEAEAARRKAEQEAARQKQEAEAARRKAEEEAARAAAAAPAAPVAAPAEAAPAVPVAVAEPVVVAQPAPEAPAPVVEEEMVEAKPLPAAAPAAPSAPVRLLHQPVEEEPKRKLSKAQREEMARRKTEDLVSKRLNQLEELREQKRKEDARKEAEVALAKKEKPVVAATAAAAAEVVAGRTPREDSAGEPFSAGRRKNKKYQDNEDRLQQPRGKSRRRKPFKSEMQAPAPVYREVTIPETITVGELANRMAVKSSEVIKLLFAQGMLVTINQTLDQDTAVLVVEEMGHKPKSVSESAAIEAELDAGEDAAEDMETRPPVITVMGHVDHGKTSLLDAIRSTDVTSREHGGITQHIGAYQVTLASGDKITFLDTPGHSAFTAMRARGAQVTDIVVLVVAADDGVMPQTVEAINHAKSAKVPIVVAVNKIDKPGSNPDRVMQQLSDHGLVPEAWGGDTIFVHVSAKSGEGISTLEEMLLLQAEMLNLQSNPTKKRARGTIIEANLDRGRGAVATCLVQNGTLRVGDICVVGNEWCRVRALNDDRGNQVSEASPSMPVEIIGLSGVPQAGDDLVAVNDERRAREIAQFRQQKDKEAIQAKQQPATRLEDMFEHIEQGEVEELNVVLKADVQGSVEAVAEALRKIKHEQIEVRVIHTGVGGINESDVMLAVASGAITVGFNVRADAKARDLAKREQIDLRFYNVIYDLVDDISLALEGRLAPTVREKVLGHAQVREVFRITKIGNVCGCLVTDGIIQRNGKLRILRQNVVVYEGPVSALKRFKDDVKEVREGFECGISIEKFNDVKVDDVLECYVEEQVKQTLS", "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": "MSKSGNGNGDKVLYCSFCGKSQHEVKKLIAGPSVFVCDECVELCNDIIREETHETHEETEARLPTPKEISNFLDEYVIGQQHAKKVLSVAVYNHYKRLQHKSEDGVELGKSNILLIGPTGSGKTLLAQTLARILNVPFAMADATTLTEAGYVGEDVENIIQKLLQKCDYDVDKAQQGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTSNILFICGGAFAGLDKVIRERSDKSSIGFSAQLKSKKSSNDEASKVLGQLESDDLIKYGLIPEFVGRLPVVTTLQELDEAALIDILTRPKNALTKQFQSLFKMEGSELEFRDEALIAIAKKALERKMGARGLRSILENILLDTMYDLPSLEGVNKIVIDESVVNGLSKPILIYEQDEKKSASGSKD", "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": "MDVTRLLLATLLVFLCFFTAYSHLPPEEKLRDDRSLRSNSSVNLLDFPSVSIVALNKKSKQMSRKEAEKKRSSKKEASMKKVARPRTPLSAPCVATRDSCKPPAPACCDPCASCQCRFFRSACSCRVLSLNC", "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": "MAFLEDGNHTAVTGFILLGLTDDPVLRVVLFVIILCIYLVTVSGNLSTILLIRVSSQLHHPMYFFLSHLASADIGYSSSVTPNMLVNFLVERNTISYLGCGIQLGSAVFFGTVECFLLAAMAYDRFIAICSPLLYSNKMSTQVCVQLLVGSYIGGFLNASSFTLSFFSLVFCGPNRVNHFFCDFAPLVKLSCSDVSVPAVVPSFTAGSIIIVTIFVIAVSYIYILITILKMRSTEGRQKAFSTCTSHLTAVTLFYGTITFIYVMPKSSYSTDQNKVVSVFYMVVVPMLNPLIYSLRNKEIKGALKRQLAKNTFS", "text": "FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MMRIVIFLLTNLAVMVVFGILLTCVGTHSSNTVRLMIISGLFGFCGAFISLLMSKFIALRSVGGKVISQPQNETEHWLLNIILNQAQKIGITMPQVAIYNAPDMNAFATGPSRNNSLVAVSTGLLQNMPRTEIEAVIAHEISHISNGDMVTITLISGIVNTFVIFISRFLAQLTAGFIGSNNEESNNGNKLVYMIVSTILELAFGILASIIVLWFSRYREFYADAGSANIVGCDKMIAALQRLKTSYEPKVTNNIKIFCINGYQKSLSEFFMSHPPLNKRIEALRYGTYMK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
{"protein": "MDKYTSRYHKFYDEVVVPKLMKELEIKNIMECPKLEKIIVNMGVGEATQNSKLIDAAMADLTIITGQKPLLRKAKKSEAGFKLREGMPIGAKVTLRKERMYDFLDRLVNVVLPRVRDFEGVPSNSFDGRGNYSVGLRDQLVFPEIDFDKVEKLLGMSITMVSSAKTDEEGRALLKAFGMPFKK", "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": "MSTLAILGAGAKAVAVAAKASVLRDMGVEVPDVVAVERIGVAANWQASGGWTDGAHRLGTSPEKDVGFPYRSALVPRRNAELDERMTRYSWQSYLIATASFAEWIDRGRPAPTHRRWSQYLSWVADHVGMTVVHGEVEQLAVTGDRWALHTHETTVHADALMITGPGQAEKSLLPGNPRMLSIAQFWDRAANHDRISAERVAVIGGGETAAAMLNELFRHRVSSITVISPQATLFTRGEGYFENSLFSDPTNWPALTLAERRDALARTDRGVFSSSVQEALLADDRIHHLRGRVTHAVGVQGQIRLTLSTNRGSENLETVHGFDLVIDGSGADSLWFAPLFSQEALDLLELGLGGPLSSERLQEAIGYDLAVTDVTPKLFLPNLSGLTQGPGFPNLSCLGLLSDRVLGSTLGPTNYPARRRHDERQPL", "text": "FUNCTION: Flavoprotein monooxygenase required for N-hydroxylation of the two acylated lysine residues during mycobactin assembly, thus producing the hydroxamate groups necessary for iron sequestration. Is also able, but less efficiently, to hydroxylate L-lysine (non acylated) in vitro (By similarity). SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)- oxygenase family."}
{"protein": "MSRSLSIIWLFGLISGFNIMITGNTLNYWLAKENIALQTIGLLSLITLPYSINFLFAPIFDSLKIKYLDKIFGHRLSWICLTSIALVFFVYILSFLNPFDNLLLFASISLIISFFSSMQDTILSAFRTEIVNKESLGFASGIYIFGYRFGMLLANSGAIYLSIYLTFNEIYKIFAILIFIYLILLIVGVKYCRFDQNNDIEQTTNNNDDIFAFIKNILKPIGSISFIILILIFLILYRLPDNFINVMINPFLLHLNYDAFEIASVGKFWGVMGAIVGGLLGGFIMKKKNILDSILLFGIIHALAHILFIILKIHGKNSTLLFITIGAESITGGMTMTAYIAFISSLCQGKFRATQYSFFSSMMGISRSIFPIISGYIVVNFGWQNFFLFTTIITIPSLLVLLKIKNKLQQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MEGLKDKTLQELEEMQNDPEAIARLALESPEVQDLQLEREMALATNRSLAEQNLEFQGPLEISRSNLSDKYQELRKLVERCQEQKAKLEKFSSALQPGTLLDLLQIEGMKIEEESEAMAEKFLEGEVPLETFLESFSSMRTLLHLRRVRVEKLQDVVRRPRALPELAGDVPPKRPPPPRPVPQATPPETEEQPPQPSVVTPYPLPYSPSPGLPVGPTAQGALQPAPFPVVAQPSSYGGPLGPYPSPHPGPRAMVGYSWSPQRSGPPQPGYPTAPTSTSGPGYPLVGGRTPGPGYPQQSPYLPSGNKPPYPTQPQLPGFPGQPQPPVPPQPPYPPGTTPSYGFHPPGPAWPRY", "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": "SIPCGESCVFIPCTVTALLGCSCKSKVCYKN", "text": "FUNCTION: Probably participates in a plant defense mechanism. Has antibiotic activity. Inhibits the cytopathic effects and replication of the human immunodeficiency virus. Active against both Gram-positive and Gram-negative bacteria. SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
{"protein": "MPSVGVKLYSVFFKFLLKHRLQNRIQSSGDESSSDPFGVTTRPEESVAAPNPLFTDGVATKDIHIDPLTSLSVRIFLPESALTPLEPSTSACVYSGKARTLNNIAGSDLLSRRNSLGSSNSLLSHKVESRRNSYGYTTGSSSPEAGSSDVYRGYAPSSSGGNSRKLPVMLQFHGGGWVSGSNDSVANDFFCRRMAKHCDIIVLAVGYRLAPENRYPAACEDGFKVLKWLGKQANLAECNKSMGNSRRPGGEVKKSEVNKHIVDAFGASLVEPWLANHADPSRCVLLGVSCGANIADYVARKAIEVGQNLDPVKVVAQVLMYPFFIGSVPTQSEIKQANSYFYDKPMCILAWKLFLPEEEFSLDHQAANPLVPGRSPPLKFMPPTLTIVAEHDWMRDRAIAYSEELRKVNVDAPVLEYKDAVHEFATLDMLLRTPQAQACAEDIAIWAKKYISLRGHEFSY", "text": "FUNCTION: Carboxylesterase acting on esters with varying acyl chain length. SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family."}
{"protein": "MNFKYIIAVSFFIASAYARSEEKDVQSLSQRDVLEEESLREIRGIGGVLLSAGKAALKGLAKVLAEKYANGKRTAEDHEVMKRLEAVMRDLDSLDHPEEASERETRGFNQEEIANLFTKKEKRILGPVLGLVGNALGGLIKKIG", "text": "FUNCTION: Maximin-H3 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity. FUNCTION: Maximin-4 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 does not possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
{"protein": "MEKANASTSAKTIDQLCKECNLCMHSLQILCVFCRKTLSTAEVYAFQYKDLNIVWQGNFPFAACACCLEIQGKVNQYRHFDFAAYAVTVEEEINKSIFDVRIRCYLCHKPLCDVEKLRHILEKARFIKLNCEWKGRCFHCWTSCMENILP", "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": "MKSGVIPSSAVGQKINEWYRYIRTFSVPDAEVLKAEIQQELKHMQHDSNLLLYYSLMEFRHQLMLDYLEPLEKLNIEDQPSLSELSRNIDSNQADLKGLLDYYVNFFRGMYEFDKREFISAITYYKQAEKKLSFVADHIERAEFYFKIAEAYYYMKQTYFSLINIKNAYEIYVEQETYNVRIIQCHFVFGVNLMDERNFEQAARHFKLALNMAQAEQKAQLVGRAYYNLGLCYYNQDLLDPAIDYFEKAVSTFESSRIVNSLPQAYFLITLIYYKQGKHDKASEYHKRGYEYAKETDDADYAVKFEFLQSLYLDQPNEEGIERCFQYLKNKNMYADIEDLALEVAKYYYEQKWFKLSASYFLQVEEARKQIQRSEGLYEIEI", "text": "FUNCTION: Involved in the regulation of genetic competence development (PubMed:12950917, PubMed:16816200). Inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:12950917, PubMed:16816200). Acts by binding to ComA, independently of its phosphorylation state, leading to the inhibition of ComA DNA-binding activity (PubMed:12950917). Does not dephosphorylate phospho-ComA and does not affect the phosphorylation level of the ComP-ComA system (PubMed:12950917). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rap family."}
{"protein": "MSDKLIIFDTTLRDGEQSPGASMTREEKIRIAKQLERLKVDVIEAGFAASSNGDYEAIRSIAQVVKDSTICSLARANDKDIARAAEALKPANSFRIHTFIATSALHMEKKLRMTPDQVYEQARLAVRFARQFTDDIEFSPEDGSRSDMDFLCRVLEGVIAEGATTINLPDTVGYAVPEGYADLIRSVRERIPNSDKAVWSVHCHNDLGMAVANSLAAVKLGGARQIECTINGLGERAGNTSLEEVVMAVKTRRDYFNLDVGVDTSQIVPASKLVSQITGFVVQPNKAVVGANAFAHASGIHQDGVLKARDTYEIMRAEDVGWTANKIVLGKLSGRNAFKQRLQELGVELESEAEVNAAFGRFKELADQKAEIFDEDIMAIVSNEAQHDANEHYRFISLSQRSETGERPHARVVFNMDGQEHSGEGEGNGPVDATLHAIESQVNSGAEMVLYSVNAITGGTEAQGEVTVRLSKAGRIVNGVGTDPDIVAASAKAYLAALNKLHDKAVQKINPQI", "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": "MPANLSSALETFKQQRDAAEAHYLKANRVSVFFREYTAAVETLLAALWAEYFQNSALCLMAVGGFGRGELYPCSDVDLAVVSPAPLSDGIQEQIARFVQTLWDCKLMPSVKSGSVDELCESVRNDITGDTAFLEARFLFGNRQTADKLAEKMNAQRNVAAFVEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLATDLPDLLKQRILTRAEAGMLSHGYRRLAHIRIHLHLNAKRAEDRLLFDLQPQVAESMGYEGLNLRRQSEELMRVFYRAIKTVKQLSGILTPMLRSRVSSAPMRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRHRFAGFFRNGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILTVVRNVRRLALDMHSHELPYASALMQSFEKQDILYLAAFFHDIAKGRGGDHAIQGIADARQFAADHFLTGEESDLLAWLVENHLLMSAVAQKEDIQDPDVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRYLTGNGGNPHTLFGRRRQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFETPIVRSRILFKSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAETQSHSRRISRRSRYMPIAPSITITPEEDYPDWYSVEITAVNRPFLLADMAEVFFAHNVSLRYAKISTLDERAEDSFTVFSLDLKNPKIQSSLKQTLLEQLS", "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": "MILLLTNSKIIYPYSEALFSIAKDQEKFEVIKNDMELFVTFTKNLNGFKKFLETPLINKNKKIKVVKDVFSKILNSTTLNFISILINKNRIMFVSNISEKYNQLVLKDKSVKLVKIACARQLSEKQAQALSEVLKHKFKCLSVKLIFNIEPELIAGFKIFIESQVIDVSLQGELKEFEWYLTK", "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": "MFFTVRNLSNRTSQVVNYAYIQYRLLSSTTKTKGLPRLIKAIQGSSKDQLADDHLHMIDDHRYGEDSWFVSSTPKAETMGVADGVGGWRRLGIDSGLFAQELMTNCSEFAEQPQYDGSDPRQLLIDSFDQMKKMSGKVCGSSTACLVTLHRRDCTLHSANLGDSGFMVLRNGKVLHRSDEQLHGFNTPYQLTVAPEPGMDCILCDSPQQAVTSHINVQQGDLVLLATDGLFDNVPESMLVRHLQPLHGETRMEHLQHAVNRLVDMAKTLSLSNTFQSPFALKAKASNMNYGVGGKPDDITVILASVDVPDKD", "text": "SIMILARITY: Belongs to the PP2C family."}
{"protein": "MTKALAAIVGSGNIGTDLLYKLLRSEIIEPRWMIGVDPDSEGLKRAADRGVIASAEGVDWLLAQDERPDIVFEATSAYVHRANAPRYRELGIQAVDLTPAALGPAVVPAVNMGEHRTAPNVNLITCGGQATIPMVYAVSRITEVAYAEIVASVASPSAGPGTRANIDEFTITTSRGIETIGGAKKGKAIIILNPAEPPMFMKDTVFCSIPADADRDAITASIHDVAASVQAYVPGYRLRAEPQFDDPTPISGGLARVGIFLEVEGAGDFLPPYSGNLDIMTAAATKVGESFATQILGASV", "text": "SIMILARITY: Belongs to the acetaldehyde dehydrogenase family."}
{"protein": "MTMQQPIPVPPPDETPAPQAEAAARVTPMMEQYLEIKAAHQGLLLFYRMGDFYELFFEDAEIASKTLGIVLTKRGKHQGADIPMCGVPVERAEDYLHRLISAGHRVAVCEQTEDPAAAKARGNKSVVRRGVVRLVTPGTLTEDTLLDARANNYLLAIARARSSTGGDRFGLAWIDISTAEFMVTECSGGELAATLARINPNEAIVTDALYNDNELGQTLRELPAVTPLTRDVFDGATAEKRLCDYFAVATMDGLAQLTRLEATAASAAVTYVDRTQVGRHPPLSPPAREASGATMAIDPATRANLELTRTLAGERRGSLLDAIDCTVTSAGSRLLAQRLAAPLTDAPAIARRLDAVGAFVADSAAREDIRSILRGAPDMSRALARLSVGRGGPRDLAGLRDGIIAADQVLARLGELDQPPQEIAAVMAALTRPSRELAAEFATALDEQLPLIKRDGGFVRQGYEPALDEARNLRDASRLVVASMQARYADDTGVKGLKIRHNNVLGYFVEVTAQHGDKLMSAPLNATFIHRQTLAGQIRFTTSELGEIEAKIANAGDRALGLELEIFERLCAKALEISDDLRAAAQGFALLDVATSLAKLAVDENYVRPEVDSSLGFAIEAGRHPVVEQALKRNGEPFIANACDLSPAPAQKSGQLWLLTGPNMAGKSTFLRQNALIALLAQIGSFVPATRARIGIIDRLFSRVGAADDLARGRSTFMVEMVETAAILNQAGERALVILDEIGRGTATFDGLSIAWAAIEHLHESNRCRTLFATHYHELTALSAKLPRMFNATVRVKEWQGNVVFLHEVLPGSADRSYGIQVAKLAGLPPAVITRAKSVLAKLEAQDRGQTARALADDLPLFAVPSRAAAEAAPPSEAELLMDAVKALHPDEMSPREALDALYALKAKLPKQ", "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": "MAALASFTRNSRSYGQQPIDVTQQGQRDRSVMSLDAQGRSKMSNINYTRPAALSTSDSTIGVFRRAPSSFSGASSSSSNHHHPVYHSHNSLPPTLIGGSPHSASSNSLAQGHRNPALGSGNTLTRSYHQPSSTNSSTSNLHGPLGTYSRDLKQAIRDISPPVINSSANPHLVNYIHTSSFDNGSYEFPSGQAQQQRRLGGSQQHLAPLQQTSSSLYSNPQSSSSQLLGQQAVRSNYAYQQSLPRQQHINSHQTQAFFGTIRAPGNSTNIVTPLRASKTMIDVLAPVRDSVAAQATTGALPSVGTSSSNGSSNSSSGVGSGGSGSLMTQSIGGPNKHLSASHSTLNTASTHDSMMHTKIPKSPSNESLSRSHTSSSGGSQGGHNSNSGSNSGFRPEDAVQTFGAKLVPYEKNEIYNYTRVFFVGSHAKKQPGVIGGANNGGYDDENGSYQLVVHDHIAYRYEVLKVIGKGSFGQVIKAFDHKYQQYVALKLVRNEKRFHRQADEEIRILDHLRRQDSDGTHNIIHMLDYFNFRNHKCITFELLSINLYELIKRNKFQGFSLMLVRKFAYSMLLCLDLLQKNRLIHCDLKPENVLLKQQGRSGIKVIDFGSSCFDDQRIYTYIQSRFYRAPEVILGTKYGMPIDMWSLGCILAELLTGYPLLPGEDENDQLALIIELLGMPPPKSLETAKRARTFITSKGYPRYCTATSMPDGSVVLAGARSKRGKMRGPPESRSWSTALKNMGDELFVDFLKRCLDWDPETRMTPAQALKHKWLRRRLPNPPRDGMDSMGGLADHDKKADLPNIDSNANILMRKKF", "text": "FUNCTION: Required for oocyte-to-zygote transition in which it phosphorylates oocyte proteins, including mei-1, oma-1, oma-2, mex-5, and mex-6, modifying their activity and/or stability following meiosis. Through phosphorylation of P granule components including meg-1, promotes the disassembly of zygotic P granules in the anterior cytoplasm during zygote polarization, and thus plays a role in P granule distribution and segregation in early stage embryos following meiosis (By similarity). Functions in both spindle positioning and in the posterior localization of cytoplasmic determinants, including pie- 1, pos-1, and pgl-1, in early embryos. Involved in the asymmetric distribution of plk-1 at the 2-cell embryonic stage. SUBCELLULAR LOCATION: Cytoplasm, cell cortex Note=Maintained at the cortex by the cortical anchor egg-3 before meiotic divisions. During anaphase of meiosis I, egg-3 translocates into the cytoplasm on vesicles and is slowly degraded, releasing mbk-2 (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily."}
{"protein": "MTKRTASIKRQTTETTISLSLNLDGSGQAEMCTGVRLFDHMLSQLAKHGLFDINVSANGDDIHHLVEDVALTLGKAFNEALGERKGIVRMADATVPMDDSLATVALDLSGRGYAVVDLPFSKNDLTGFPTDLVRHFLETFAIEGRLNLHARILYGSNDHHKAEALFKALARALDKATSLDPRREGIAPSTKGMLEN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MTITPQHLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNQEEFYLLVLIAALGGILLANANHLAALFLGIELISLPLFGLIGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGNLSFVALGKSLGDGMLHEPLLLAGFGLMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAVRIVLGVIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQSGEMSMEAVGVYLAGYLFSSLGAFGVVSLMSSPFRGPDADSLFSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQASLWWLVAAVVVGSAIGLYYYLRVAVSLYLSAPQQLNRDAPSNWQYSAGGIVVLISALLVLVLGIYPQPLISIVQLATPLM", "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": "MTTETHTLHIEEILELLPHRYPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMVMEVTFEKTRRGVTRFKGVALVDGKVVCEATMMCARSREA", "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": "MKLVLLERVENLGVIGDVVSVRPGFARNFLLPQGKALRATEANMARFEVERELLEKRNAERAAEAAESGKTIDGESFVMIRQAGESGQLYGSVTSRDIAEIVSESGTKVVRSQIALNAPIKTLGLHELKIKLHADVSVTVTINIARSQDEAERQAAGEDVIAAQADEDRAIADAQAAELFEASEEGQELAAQREATEDAGADESEETEA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MTIKLHHLRPAPGAKTEKTRVGRGEGSKGKTAGRGTKGTKARKNVPAAFEGGQMPLHMRLPKLKGFTNPFRTEYQVVNVGDIARLFPEGGQVTVEDLVAKGAVRKNQLVKVLGDGDLTVAVQVTVDKFTGSAKEKIAAAGGTATEL", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MAADPIHQFQITKLFTLGHVGGQEIAFTNSSAYMFGTVALIAILMLVPGRQLVPGRLQSIAELSYEFVANMIRSTAGKEGLKFFPLVFSLFMFIAVSNLIGIVPYTFTVSSHLIVTVALALLVFFTVLIYGFSKNGLKFFKLFVPSGVPIYILPLVVFIEVISFFLKPVSHSVRLFANMLAGHIALKVFASFVAMLGALGVVGWFGAVLPLGLTIALTALELLVAFLQAYVFAILTCIYLNDAIHPGH", "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": "MKPPIFIIIMTTVISGTMMVLISSHWLLIWIGFEMNMLAIIPILMKKFNPRAMEASTKYFLTQATASMILMLGIIINLLYSGQWTMLHTPNPMASNMMTIALTMKLGLSPFHFWVPEVTQGISLSSGMILLTWQKIAPLSVLYQMAPSINPNLLMSMAIMSMLVAGWGGLNQTQLRKILAYSSIGHMGWMTSITVYNPTLMHLNLVMYIMMTLGTFMLFMYNSSLTTLSLSYSWNKFPLTTLLILMLMLSLGGLPPLSGFIPKWMIIQELTKNNMIIIPTFMAIAALLSLYFYMRLTYTTALTMFPSMNNMKMKWQFENTKKITLLPPLIIMSTMLLPMTPMMLILY", "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": "MNVIDLFKKLLSFKSVTPDDDGGMEFIKEYLKGFEVIESEKEGVKNLFIYKKFGEGDHLCFGGHIDVVPPGEGWNTDPFTPTEKEGFIYARGAQDMKSGLAAFLWAMKNAKNFKGTLSALITSDEEGDAVWGTKYMLEILKDKNLIPDYAIVAEPTCEKVFGDAIKIGRRGSINGVLKKIGLQGHAAYPEKSINPIHKVAQVLHKIAGVDLDDGDEFFAPSKFVVTDIRAGMEVTNVTPGELKMMFNVRNNTHTDKEKIKNFIHEHFKDMNYTLELKQSAEPFVTNPDTKVVKALDRAIKNHTNITPQHSTAGGTSDARFFAKHGVKVVEFGVKNDTIHAPNERTTPEEVNKLADIFKEVIEEWN", "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": "MYAIFQSGGKQHRVSEGQVVRLEKLELATGEKVEFDSVLMVVNGEDIKIGAPVVAGAKVMAEVVAQGRGDKIKIVKFRRRKHSRKQQGHRQWFTEVKITGIQA", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MKLLSKVFVTALGLTSIVNAAPTSSSSAEEAQKTVPVELSIGVKQLPNIHNDSAVDANAVAKGYSLVNVSLTARGLTGILKLKEATNIYGYDFEYLNLSVEYQSDTRLNVHIEPTDLTDVFVLPEELVVKPKLEGDAKTFNFENSDLVFEYDEEDFGFEVLRSSTREVLFSTKGNPLVFSNQFIQFNTTLPKGHSITGLGESIHGSLNEPGVVKTLYANDIADPIDGNIYGVHPVYYDQRYNTNTTHAVYWRTSAIQEVVVGETSLTWRALSGVIDLYFFSGPDPKDVIQQYVSEIGLPAMQPYWALGYHQCRWGYDTVESLETVVENFKKFDIPLETIWSDIDYMDGYKDFTNDPYRFPTDKFRKFLDDLHNNSQHYVPIFDAAIYVPNPNNATDNDYEPFHLGNESDVFLKNPDGSLYIGAVWPGYTVFPDFLANNTQEYWNKMFKDWYERIPFDGIWTDMNEVSSFCVGSCGTGRYFDNPVHPPFEVGYSGSDYPLGFDKSNASEWKSISEAAAATKTTTTTSSSTSTSIDGKNTLAPGKGNINYPPYAINNNQGDHDLATHAISPNATHADGTVEYDIHNIYGLIQERAIYEALLEIHPNKRPFIIGRSSFAGSGKYMGHWGGDNYADYYMMYFSIPQALSMGLSGIPFFGVDACGFNGNTDMELCSRWMQLASFFPFYRNHNVLGAIPQEPYVWEGVMNATKTSINVRYSLLPYYYTLLHESHVTGIPIMRAFNWQFPYSKELAGVDTQFFVGDALLVTPVLEPGVNHTKGVFPGENAVYYDFYTHKKQKFTAGKNETLAAPLGHIPLHIKGGNIIPTQEPGYTTTESRKNPFGLLVALDAEGTASGKLYLDDGESVDVEEALYVDFVASKNKLVASVFGEYEVRQPLANVTILGVDSEPKKVLFNNETVSHNYENGAVYLTDLEKFTKEGAFAEEFSIQW", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 31 family."}
{"protein": "MAPAGLSLGATILCLLAWAGLAAGDRVYIHPFHLLVHSKSNCDQLEKPSVETPADPTLTPVPIQTKSSPVDEEALWEQLVRATEKLEAEDRLRASEVGLLLNFMGFHVYKTLSETWSVASGLVFSPVALFSTLTSFYTGALDPTASRLQAFLGVPGEGQGCTSRLDGRKVLSSLQTIQGLLVAPGGASSQARLLLSTVVGLFTAPGLHLKQPFVQGLSSFAPITLPRSLDLSTDPNLAAEKINRFMHSATGWNMGRPLAAASPDSTLLFNAYVHFQGKMKGFSLLPGLTEFWVDNTTSVPVPMLSGSGTFHYWSDNQNHLSMTRVPLSANGYLLLIQPHHTLDLRKVEALIFQHNFLTRMKNLSPRAIHLTVPQLTLKASYDLQDLLAQAKLPTLLGAEANLGKISDANLRVGKVLNSVLFELKADGEQAPESVPQPAGPEALEVTLNSPFLLAVLERSSGALHFLGRVSRPLSAE", "text": "FUNCTION: [Angiotensin 1-7]: Is a ligand for the G-protein coupled receptor MAS1. Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets. FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone. Acts by binding to angiotensin receptors AGTR1 and AGTR2. Also binds the DEAR/FBXW7-AS1 receptor. FUNCTION: [Angiotensin-3]: Stimulates aldosterone release. FUNCTION: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
{"protein": "MPSVFLLFDIGNTNVKIGIADHDGVVASYVLPTDTHQTGDSLGLRLADVVRHAGFAPGDVTACVASSVVPSFNPLMRQACGRYFDRRLLLAPEDIAIPLENRYERPQEVGADRLVAAFAARRLWPAPRSIVSVDYGTATTFDCVQGEAYLGGLICPGVHSAAGALAAGTARLPRISLDVREDLPVVGRSTSMSLNHGFVFGFASMTEGLCHRLSAVLEAPMQVVATGGFASAIARVSNCFDHVRPDLLLEGLRILYMESGIKG", "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": "MLIGEYKHVVDNKGRVTLPSKFREELGEKFILTKGLDNCLFGYSLKEWAVLEEKLKKLPLTSKDARAFLRFFFAGACECEVDKQGRILIPQNLREYANLQKEVFIIGVMTRIEIWSEENWQREMADESLSVEKIAQKMEELGI", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family."}
{"protein": "MQTAYWVMVMMMVWITAPLSEGGKLNNVIRGLVPDDVTPKRISQSLISRRRFDSRIMFVPSCIWKTCPSYLHGDNYDLKEKDK", "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": "MDKLLSLLGVSILAGLLLEAFAQTDLTGKVFVFPRQSETDYVKLIPRLDKPLQNFTVCFRAYSDLSRPHSLFSYNAEYGENELLIYKERIGEYELYIGNQGTKVHGVEEFASPVHFCTSWESSSGIAEFWVNGKPWVKKGLQKGYTVKNKPSIILGQEQDNYGGGFDNYQSFVGEIGDLNMWDSVLTPEEIKSVYQGVPLEPNILDWQALNYEMNGYAVIRPRCVALSSYNKIS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pentraxin family."}
{"protein": "MGDFGYSFEGYDPTRHVRASLREKQISHKHAREISLHIRGMTVEKARDFLQAVIEKKRAVPFRRFKRQVGHRSDPGVMAGRYPEKSAAEFIKLLDNLESNAEYKGMDLDRLTIVGAVAHKGILIKRFIPRAMGRSTPKNNVLTHVELVAREA", "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": "MITTQEIQQIREQIRTWRTKGETIAFVPTMGNLHLGHITLIKEAAKRADHVVASIFVNPMQFGANEDLDAYPRTLEADKLALSDAGAELLFTPTPDIIYPKGMEQQTYVEVPKIGDQLCGASRPGHFRGVATVVCKLFNIVQPDIALFGRKDFQQLMIIKTMVEDLSLPIEIVGIDTIRETSGLAMSSRNGYLSTAQKSQAAVLKQTMDQISSAVKQGASLDLAIENGKQALIDSGFTPDYLELRNAKDLSLVTDGQDELVILAAAYMGNTRLIDNLCFTR", "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": "MWTFGRRAVAGLLASPSPAQAQTLARAPRLAELAQLCSRRGLRTGINATCTTHHTSSNLRGLNQIRNVKRQSVYLMNLRKSGTLGHPGSLDDTTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLGAELTKALKTKLDLSSLAYSGKDA", "text": "FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation. May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity). FUNCTION: [Extramitochondrial frataxin]: Modulates the RNA-binding activity of ACO1. May be involved in the cytoplasmic iron-sulfur protein biogenesis. May contribute to oxidative stress resistance and overall cell survival. SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion. SIMILARITY: Belongs to the frataxin family."}
{"protein": "MYLENLVLHDFRNYADLTINFSQGVNVLLGENAQGKTNLLEAIYVLALTRSHRTANDKELIRWQTTTATLQGRLHKSTGAVPLELELGRRGKRAKVNHLEQAKLSQYVGNLNVIVFAPEDLSIVKGAPAVRRRFMDMEFGQMSPKYLYNLSQYRTILKQRNQYLRQLNRQQAKDKVYLGVLSDQLAAFGAEIIHKRLQLLQQLEKWAQAVHSEITQEQEQLTFHYVTQVPTADQTSVDHIYQTLQALYQQQQAKEIFQGTTLLGPHRDDLQFGVNGKNVQTFGSQGQQRTTALSVKLAEIDLMKAETGEYPVLLLDDVLSELDAARQTHLLTAIQDKVQTFLTTPSLDGVARKLINAPKVFEVSHGTLHEEEPH", "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": "MPHLAELVAQAKAAIEEAQDVAALDSVRVEYLGKKGHLTLQMSTLRDLPAEERPAAGAVINQAKQEVQQALNARKEQMESALLNERLAAEKIDVSLPGRRIENGGLHPVTRTIERIETFFGELGFSVESGPEIEDDYHNFDALNIPAHHPARADHDTFWFDAKRLLRTQTSGVQIRTMQNKQPPIRIIAPGRVYRNDYDQTHTPMFHQVEGLIVDKDISFTNLKGTLHDFLKNFFEEDMEIRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDLRFLKQFK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MPNFRLKLPSRNWMIFLTVTGSFTAALVYDRKQKKRAQQKWCDLVAHLSKESLPVDQTRRKLTVFLSAPPGDGLRVAREHFKEYVKPILVAAALDYQVIEGRREGEIRAGLAERIRKFRRKSGEPSTVVEETGIEEVVADAREKIGVVEEPVPKGDLIIGRNTWKEYIRGLHEGWLGPLDPPQPPLSTDVPSPSEGAETNGSPDDTPTAENSEKKEEPEKKDEKPSKPTGPTPAYITPADYSSQSLPRSLPQSLDGSVPIQFPHILGFLNTPIRIYRYLNQRYLADSVGREVAGIVLASTTRPYSDGSFSTDSELTPAGIDGAPASDNLLGGNYEQKTLLEEEEKDWHKSAHKKDEANPDKEREWVDSVVLDPRIAARMQRYVLSPEDEARSQRIAEGAEYILGEERPTPVPFWQRMWIKYGYGEDEETLKRKPIIGNIDGEDDQ", "text": "FUNCTION: Essential 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; Single-pass membrane protein. SIMILARITY: Belongs to the TIM54 family."}
{"protein": "MVPDQDGELRHDVCSLSTSLRLTAHVTSSIVHEQSSNIRYGENRKHGQRYAYHEPLPPEIVARCNGHDGKHLTLVTRNSKPVNVRLEKRGQSFYISKGWKKFVELTDLRVGQCVRFSVSSPSTLDLLILDKHGTSLAIPPSKRDLKLKSKRSTHQDSKGHPSNTDPGPSRIINRRVTKSESSANTQLLVQYFSKRYPIDHLEQLMTGRTEDIEVQTLVGPSVNMVLHTSTDHRCNLKKGWTDFALSNGIKLNTVCIFHFYKTTHLGVIVDIF", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MELNSIKPADGAKHAARRVGRGIGSGLGKTAGRGHKGQKSRSGGYHKVGFEGGQMPLQRRLPKRGFKSHLLKFNAEISLTALENLGLAEVDVLALKNAGLVGELAKVVKVIKSGEISKAVKLSGITATAGAKAAIEAAGGSLA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MTTHRKPSQEQGFLNGQFLLAMPGMSDERFARSVVYICAHSDEGAMGFIINQLQPVQFPDLLRQIGVIGEEDLIILPDRAQHMVVRNGGPVDRTRGFVLHSDDYMVDSTMPVSDDVCLTATVDILRAIYGGGGPERALMALGYSGWAPGQLEMEVAENGWLTCDAPLDMLFDSDIEGKYSRLMLHMGIDMSRLVFDAGHA", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
{"protein": "MARADDPDERKTQGGHGDRRRREFRGGEQVVRAGTLLLAATDLTEPTFRRSVVYIMEHNDSGSLGVVINRPSETSLADVLPRWSALAADPGTLYFGGPVKRDAALCLGTLKVGASTAGVPGLRRIDGRVVLVDLAADPERIAPLVEGIRVFAGYAGWTFGQLEGELDNEDWIVLSALPTDPISAARPDLWADVLRRQPLPMSLLATHPIEVERN", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
{"protein": "MKFERARPFIAIVFIQCLYALMSIVAKLALNKGMSPHVLVAYRMAVASALITPFALILERNTRPKLTFKILLQIAILSLFEPVVEQNLYYSGMKLTTATFTSALCNALPAMTFIMACVFKLEKVTIERRHSQAKLVGTMVAIGGAMLMTFVKGNVIELPWTSNSRGLNGHTHAMRIPKQADIARGSIMLVASCFSWSCYIILQAKILAQYKAELSLTALMCIMGMLEATVMGLIWERKNMSVWKINPDVTLLASIYGGLVSGLAYYVIGWASKERGPVFVSAFNPLSMVLVAILSTFVFLEKVYVGRVIGSVVIVIGIYLVLWGKSKDKGGMLQPNAGCAETVVKIDQQKVPTPDNNQVVSISYHLMIPKAAARSQE", "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": "MAPGLRGLPRCGLWLLLAHHLFMVTACRDPDYGTLIQELCLSRFKENMETIGKTLWCDWGKTIQSYGELTYCTKHVAHTIGCFWPNPEVDRFFIAVHHRYFSKCPISGRALRDPPNSILCPFIALPITVTLLMTALVVWRSKRTEGIV", "text": "FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the RAMP family."}
{"protein": "MTQYTPMIQQYLKVKADYQDAFLFFRLGDFYEMFFEDAVKAAHELEITLTSRDGGSSERIPMCGVPYHAAKNYIEQLVEKGYKVAVCEQVEDPKTAKGVVRREVVQLITPGTMMEGRTIDEKENNFLAALTHFEDGSYALACNDLTTGQNTVTLLTGSVEDILLEVYATGSKEIVVDSSFSKDELNKLTETLKMTISYEDATAIPEGLEHLVKNVSQAKLIKAVGRLFNYVIRTQKRSLDHLQPVEIYYTNQFMKIDVHSKRNLELTETLRTKEKTGSLLWLLDKTKTAMGGRMLKQWMERPLIQKERIEERLEMVETFVNDYFLREDLKEKLKEVYDLERLAGKVAFGNVNARDLLQLRRSLLQVPAILEAISLLDNAYAARLIQGADPCESLTELLGRSIQENPPLSIKDGDIIKDGYNDKLDQYRYVSKNGKTWIAELEKRERDITGIKSLKIGYNRIFGYYIEVTKANLGALPEGRYERKQTLANAERFITDELKEKETLILEAEEKIVQLEYDLFTALREEVKVFIPKLQHLAKVISELDVLQSFATVSEEEQFVKPVLTTKREIFIKDGRHPVVEKVLNGKLYVPNDCIMPENMDVFLITGPNMSGKSTYMRQLALVTVMSQIGCFVPATEAVLPVFDQIFTRIGAADDLISGQSTFMVEMLEAKNAIANASERSLILFDEIGRGTSTYDGMALAQAIIEHIHDQIGAKTLFSTHYHELTVLEDSLDQLKNVHVSAIEENGKVVFLHKIQDGAADKSYGIHVAQLAELPDSLIARAKEVLAQLEGQEEIVIPKRVEVKAQEQEVIPEPIVVKEEPIEIEETKVDNEEESQLSFFGAEQSSKKQAKPALDAKETAVLTQIKKIDLLDMTPLEAMNELYRLQKKLKKG", "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": "MNSKFIVIEGLEGAGKTTARDTVVAVLRAQGINDIVFTREPGGTPLAEKLRDLIKQGIDGEVLTDKAEVLMLYAARVQLVENVIKPALARGSWVVGDRHDLSSQAYQGGGRGIDSQLMASLRDTVLGEFRPDLTLYLDLPPAVGLARARARGELDRIEQESLAFFERTRARYLELAASDASIKTIDASQPIEQVSASISQALAQWLTNQEPV", "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": "MALKIRLRQQGRRNHVVYRLVLADVESPRDGRYIELLGWYDPHSAVNYQLKGDRIFHWLSQGAELTEKAAVLIKQGAPGVYSELMAKQAARKAAVCQKRRAYRQRRSLKRAEAAKAAAK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MSAAQARHLTTLATGRYGFELQTLMERAGESLAGLAAHLAPDGPVLVVAGRGHNGGVGLAAAHCLARARRAVWVVPTHEAENYSGVPKELLERLAELPNVRLRSSLPKMKFSCALDAAVGMRLEGPPRGRTLDVITVLNNLGCKVLSLDVPTGLAADSGEVPGDVVRASATLALALPKPGTPPGGVVGDLYLASFDLPEALFHDVGLEPFVAPSPWARIV", "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": "MSDSFDRAPEQTKPQRAPPSSQDKIPQQNSESAMAKPQVVVAPVLMSKLSANAPEFYPSGYSSNYTESYEDGCEDYPTLSEYVQDFLNHLTEQPGSFETEIEQFAETLNGWVTTDDALQELVELIYQQATSIPNFSYMGARLCNYLSHHLTISPQSGNFRQLLLQRCRTEYEAKDQAAKGDEVTRKRFHAFVLFLGELYLNLEIKGTNGQVTRADILQVGLRELLNALFSNPMDDNLICAVKLLKLTGSVLEDTWKEKGKTDMEEIIQRIENVVLDANCSRDVKQMLLKLVELRSSNWGRVHATSTYREATPENDPNYFMNEPTFYTSDGVPFTAADPDYQEKYQELLEREDFFPDYEENGTDLSGAGDPYLDDIDDEMDPEIEEAYEKFCLESERKRKQ", "text": "FUNCTION: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA- binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MISAIEPKNLLRPHSQPVVTTSTLQPDDECNIELRIEDTTVDKYPAKQHARRVAAEIHRDRGLVYLMGQKSTLYEDSDQERTFRQRRYFFYMSGVDEPDCDLTYDINADKLTLYVPDFDLKRTIWMGPTLGREEALQRFDIDEVKYQSSLDEDVKQWAQNQGRGSTLYLLHESQKPAEKVPNVFIDSKTLKQAMDTSRAIKDEHEIGLIRRANEVSAAAHIDVLRGIRKMSNERDIEASFLNTSVSLGAHKQAYHIIAASGSNAATLHYSKNNEPLKGRQFVCLDAGAEWNCYASDVTRTFPMTSQWPSAEAKHIYKLVEHMQESCMVRVKEGVRYLDLHILAHRSLIRGFLTLGIFKGGTLEEIQNSGASNLFFPHGLGHHIGLEVHDVSPESIMAQDNGDYSDNVLISPNNLSPCTTSSPTLKSGMVVTIEPGIYFSQIALDNAKPEQVKYVDLELVKTYMPVGGVRIEDDILVTKTGYENLTTAPKGDGMLEIIRQGDGSCNI", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MSMFLDTAKISVQAGRGGDGMVAFRREKYVPNGGPWGGDGGKGGSVIFRVDEGLRTLMDFRYNRKFKAKSGEKGMTKGMHGRGAEDLIVFVPQGTTVRDAETGKVITDLVEHGQEVVIAKGGRGGRGNIRFATPRNPAPEIAENGEPGEERQLELELKILADVGLVGFPSVGKSTLLSVVSSAKPKIGAYHFTTIVPNLGMVRTKSGDSFAMADLPGLIEGASQGVGLGTQFLRHIERTRVILHVIDMSASEGRDPYEDYVSINNELETYNLRLMERPQIIVANKMDMPEAQDNLKAFKKKLATQYDEFNDLPMIFSISSLAHQGLENLLEATAELLAKTDEFLLYDESDLVDEEAYYGFAEAEKEFEITRDDDATWVLSGEKLERLFVMTNMERDESIMKFARQLRGMGVDEALRERGAKDGDLVRIGKFEFEFVD", "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": "MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAEK", "text": "FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. SIMILARITY: Belongs to the biotin--protein ligase family."}
{"protein": "MTNAFVYPNVEFIAGVDEVGRGPLVGAVVTAAVILDPHNPIEGLKDSKKLSEKKRLLLAEEIKQKALAWSLGRAEPAEIDKLNILHATMLAMQRAVENLKIQPHFVLVDGNRIPQLPMSAQAVIKGDSLVAEISAASILAKVARDQEMIELDRRYPEYAFAQHKGYPTKLHLERLAQFGVLPEYRRSFAPVKKLLSTLLSKNHEYVFKIQK", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MGTGEKTLKSFQLHRKQSVKVKDVPKGCLAIKVGSQGEEQQRFIVPVLYFNHPLFMQLLKEAEDEYGFDQKGTITIPCHVEEFRYVQALIDGERSVYNGNNHHHRHGGRDQYHHLVGCFRA", "text": "FUNCTION: May play a role in the apical hook development (Ref.6). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Primarily localized in the nucleus. SIMILARITY: Belongs to the ARG7 family."}
{"protein": "MFNHDWKYSINSKTFADLNIELFRNHKFKTVLNYIIGVVGWNGLKLALFVSDIYTCIKLLAFNSWSNNIIKPYLPFKISKWLFSGCILASIVLLIWEAIAGMRIYKTGNISLTYVNNFSRNLNSVLNYSKFCVYNMIERKGFRQKMTFFTFFQLKDCIRLIFTDTPRQVINGLTLWSVLVTVNKNEDLGDLESFTGLINKIKNIGQTNHEEAVILSLMLFSFIIWALFVFKFLLAVICSIFVYYKIINDQEYSGLREYICVTVSENVDELVERQRKKENDDTIYKTGLLESQTFDDFKEVENKIETSFNDTSYASNNDSMIELIERRPEYKSQDVCGPIPTMKKTETMESFVDNGNPQYTTRFSAILDSPYINSYESNDIKKAKIQSRSVNTPKYEDLSSSDIFNKIHSAGQLKSTTSMEFHGPLDSMPNTTNNIRNFNSNSSRPRPPPLQTKSSINSKADSNDNGRIYTPMKAYFREPDLPRKGLLEDEDRTYNYT", "text": "FUNCTION: Low affinity potassium transporter that, with PRM6/KCH2, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone (PubMed:21252230, PubMed:23204190). Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx (PubMed:23204190). KCH1 and KCH2 act at the apex of the calcium signaling pathway that is used for survival during prolonged exposures to mating pheromones (PubMed:23204190). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KCH1 low affinity K(+) transporter family."}
{"protein": "MRHLHHQTSQTKLWAVIPAAGSGSRFSKTELKQYQYIQDATVIEHTVKRLSQLPLTGYVLAIGKQDTFASTLSFQDKHKAHFCNGGVERVHSVLNALNYLSQIADEDDWVLVHDAARPCVTFECLNTLVKNAIETNQSAILAIPVRDTLKQVNQEQQIEKTVSRELLWQAQTPQIAKIGILKKAIETALKNNLTITDEASALESIGESVQVVMGRSDNIKITYPDDLELARLILQSQN", "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": "MATLSAARCLVVKIGSALLVDQASGALRQDWLTGLAQDVAEIRARGADVILVSSGSIALGRRVLGLGTGALPLEQAQAAAAVGQIRLARAYEEVLAPHKITTAQVLVTLEDSTDRRRYLNTRATLGTLLSLGVTPIVNENDTIATDEIRYGDNDRLAAQVAVMAGADQLVLLSDVDGLYTANPATDPTATRFDRVDEITPEIEAMAGDAVSGLSKGGMKTKLMAARTAMDAGCAMAITEGARPRPLKALMDGAPATWFVPRTDPLAARKHWIAAMKPRGEITVDAGACAALKRGKSLLPAGITEVSGAFGRGDPVIILAPDGTALGRGLTRYTAVEARAIRGHRSAEIEAVLGYPGRAVLIHRDDMVL", "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": "MKDYLVKALAFDGEVRAYSVRTTNTVSEAQRRHDTWRTASAALGRSLTAGTMMGAMLKGDQKLTIKVEGNGPIGPILVDAHANGDVRGYVTNPHVDFEGTEQGKLRVYQAVGTEGFVTVIKDIGMREPFIGQSPIVSGELGEDFTYYFAVSEQTPSSVGVGVLVNGDDSILAAGGFILQIMPGAQEETISFIEERLQKIPPVSTLIEQGLSPEELLYAVLGEDKVKVLETMDVQFNCTCSRERIESVLISLGKTELEQVREEEEETEVHCHFCNERYKFSKEDITNLIENL", "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": "MKHADPLRADTLGTAPLSQAIEAHHHGKEREAHRQSLSSVPGDTVVEAPEKVVDLEINSVDNDKEHHRAPTRDEIQTLRKVPGSIPATAYLLCFVDFAERASWFGARSVSSNFMQFPLPEGGNGAGAPPSGSELPAGALGHGQRFSVALGLVFSFLSYVIPIFGAWLAEAKVGRYRTILIGVLIGGVAHIIMIAGAVPSILQAGKGTAPFLVSLFLLALGAGLFRPNVSPTVLDQHRHYQPFVKELPSGENVIIDPEATMQRIMLIFYALINVGAFYSLATVYSEKLVGYWLAFLLPGIIYLLLPLMLWYLNDKLIKVPPDGGALTKFWKILTVSLVENKGMVWKKGFFDRVQPGALLQKYPSSGPVKWTSKDVEDVKRTLVACEIFLYFPIYHLNDGGVGTILPSQGAAMLKKGVPNDLLGNFNPITIMITVPVLTYIVYPALRKSNIKFGRISRITLGFWLAVISGLVSSLVQWRIYKTSPCGYHATTCPEVAPVSIWWQLPSYVLGALSECFSNVTGYELAYARSPPGMRSLVVSLFLFSTALSSALGLILTPAIVDPHLVWVWAGPTIALAVQTVIFWVRHRKYNDDEFMIEGDE", "text": "FUNCTION: MFS-type transporter; 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). 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": "MRTAYHEQLSELSERLGEMCGLAGIAMERATQALLQADLVLAEQVISDHEKIATLSARAEESAFVLLALQAPVAGDLRAIVSAIQMVADIDRMGALALHVAKIARRRHPQHALPEEVNGYFAEMGRVAVELGNSAQEVVLSHDPEKAAQIREEDDAMDDLHRHLFTVLMDREWKHGVAAAVDVTLLSRFYERFADHAVEVARRVIFQATGAFP", "text": "FUNCTION: Plays a role in the regulation of phosphate uptake. In this role, it may bind, possibly as a chaperone, to PhoR, PhoP or a PhoR- PhoP complex to promote dephosphorylation of phospho-PhoP, or inhibit formation of the PhoR-PhoP transitory complex (By similarity). Important for tolerance to antibiotics. FUNCTION: Plays a role in the regulation of phosphate uptake. In this role, it may bind, possibly as a chaperone, to PhoR, PhoP or a PhoR- PhoP complex to promote dephosphorylation of phospho-PhoP, or inhibit formation of the PhoR-PhoP transitory complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PhoU family."}
{"protein": "MDVLSAVLLALLLIGANAFFVGAEFALISARRDRLEALAEQGKATAVTVIRAGEQLPAMLTGAQLGVTVSSILLGRVGEPAVVKLLQLSFGLSGVPPALLHTLSLAIVVALHVLLGEMVPKNIALAGPERTAMLLVPPYLVYVRLARPFIAFYNNCANAILRLVGVQPKDELDIAVSTAELSEMIAESLSEGLLDHEEHTRLTRALRIRTRLVADVAVPLVNIRAVQVSAVGSGPTIGGVEQALAQTGYSRFPVVDRGGRFIGYLHIKDVLTLGDNPQTVIDLAVVRPLPRVPQSLPLADALSRMRRINSHLALVTADNGSVVGMVALEDVVEDLVGTMRDGTHR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TerC family."}
{"protein": "MRNLIFFVIPFHFWLPAEGFKLNTNLLETNLINLGVVLGLLVYFGKGVLNNLLDKRKQTILSTIRDAEERYKEATDKLKQAQIRLQQAELKANEIRVNGLSEMEKEKQDLINIADEDSKRLEDSKNATIRFEEQRAIEQVRQQVSRLALERASEVLNNCLNSELHSRMIDYHIGLLKTMGSTTE", "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": "MRRIDKIYHQLKHNFHDSTLDHLLKIQGNSAKEIAEQLKMERSNVSFELNNLVRSKKVIKIKTFPVRYIPVEIAEKLFNKKWDTEMMEVKDLQAFSGNSKQNHQHISTNPLELMIGAKGSLKKAISQAKAAVFYPPNGLHMLLLGPTGSGKSLFANRIYQFAIYSDILKAGAPFITFNCADYYNNPQLLLSQLFGHKKGSFTGAAEDKAGLVEQANGGILFMDEIHRLPPEGQEMLFYFIDSGSYNRLGESEHKRTSNVLFICATTENPSSALLKTFLRRIPMTIHIPSLEERSLNERVDLTTFLLGKEAERIKKNLSVHIDVYNALIHSAKFGNVGQLKSNVQLVCAHGFLHNLDRNEVIELTVRDLPDEIKQEWMSSSKNMQRSKAISEYVNITTIISPIVEDETTKIDEDLSFNLYHLIEEKVKTLMKEGLSKKDINQYILTDVHLHVRSFFHHQAFQKDNLLTFVEDDVIQMTKQLKEIAEHELDCTFDRKFIYFLSMHIDAFLKRGKQIDVLNTQETDEIRDTHVKEYRVAMIFKDKIQEYFKVAIPEIEVIYLTMLIHSIKSLKENKRVGIIVAAHGNSTASSMVEVATELLGSTPIAAVDMPLTVSPSDILECVAEKMKQVDEGEGVLMLVDMGSLAMLESRLEEKTGISIKTISNVTTSMVLDAVRKVNYLNLNLHAIYQSVTKDFIELWERQPAASGKKKALVSICTTGSGTAKKLEDILTTIVNKASDTPIHILTVSSIKLANSIKEIEKEYEILATVGTKDPKINAPHVSLEVLIEGEGEKLIQQAITKGSISLSNGLNEANIIVRELCEDSLKKYLVFLNPHHVIDMLLEWLQTVQDELGVIFNNAVLIKVIMHTAFAFERVIKQNPIAFSEEEEINDQLKEMVYVTERTLAPYEEKLGLRISDDEKLFIAAIFAEEVHGQLF", "text": "FUNCTION: Involved in positive regulation of the levanase operon which comprises the levDEFG genes for a fructose PTS system, and sacA for levanase. SIMILARITY: Belongs to the transcriptional antiterminator BglG family."}
{"protein": "MLKILRAKLHGIRVTECVLDYHGSITLDPEICGLAGIMPLEFVYIWNKHSGQRISTYVIYGEAGSRCCILNGAAARTCQKGDEVIISAFEYVAGPGDISQRSPVVLTFDAHNRVQERLRYIVEQKDGGMSFNIADDPLPEA", "text": "FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family."}
{"protein": "MLQTWAKLAYEANLGIVYGSTLIILLLPLIGSFMPPNLVSSISKLNAFTLLESYLLPVLSNFGIFGGLALGVGSAIAFSVLNSIASSFLNLSFNQQQALTIVVALLVSQFIFGGWATFALFLTSMLGSVPPVPGLAVIMSFITPFIDGLIATLGGLMVVLSILYELSEIGLVTLP", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein."}
{"protein": "MSKDIKFSSDARTAMMRGIDILADTVKTTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVREGLKNVTAGANPVGIRRGIELAAETAVASIKEMAIPVHDKSAIAQVATVSSRSEKVGEYISDAMERVGSDGVITIEESKGMQTELDVVEGMQFDRGYLSQYMVSNTEKMVAELDNPYILITDKKISNIQEILPLLEQILKTNRPLLIVADDVDGEALPTLVLNKIKGVFNVVAVKAPGFGDRRKAQLEDLAILTGGTVITEELGLDLKDATLEALGQAAKATVDKDHTTIVEGAGSADAISDRVAIIKAQIEKTTSDFDREKLQERLAKLAGGVAVVKVGAATETELKAMKLLIEDALNATRAAVEEGIVSGGGTALVNAIAALDKLSEEGDIQTGINIVRRALEEPVRQIAANAGYEGSVIIDKLRSEEVGTGFNAATGQWVNMIEEGIVDPAKVTRSALQNAASVAGLILTTEAVVANKPEPAAPAMPPMDPSMGMGGMM", "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": "MAKNAPAPRGARRKPVKKVGVPLRERVATAVPWMLVGSVAMVSLLAVIYLPAALDGYPIRKVGVDGVTDVRRQQQIETALAALVREENYFSVPLEEIYQQSQGLSWVEEVSVRRQWPDTVVLTVEERRPVAVWNESVLVSDSGQPFKALKQYDLDDLPHLNGPEQRLEEVMGFYHSMGKTLADVDLSIRSMEVNARLTARLTLNNDMELVVDREHYTTKLRRFVRLYRGVLNTDSRQVARVDLRYADGMAVTWREQQS", "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": "MENNRAGRPKSCRRVKEMPKVRCFKPQGIPGIKLEEMVLSVDEMESLRLADLEGLYQSEAARRMDVSRQTFGRIIDSAHRKVADAIIHGKSIVIEGGVVMKREEQVHNAKPGCVCQHCGHEESHRSGLPCRDMICPECGHHMIRKGGCGTGQEDI", "text": "SIMILARITY: Belongs to the UPF0251 family."}
{"protein": "MRLNTLSPAEGSKKAGKRLGRGIGSGLGKTGGRGHKGQKSRSGGGVRRGFEGGQMPLYRRLPKFGFTSRKAMITAEIRLSDLAHVEGDVVDLNALKAANIIGVQIEFAKVILSGEVTRPVTVRGLRVTKGARAAIEAAGGKIEE", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MSQQGTIYRVAGPVVTAVGLNARMYDVVKVGNEGLMGEVIEIDNDKAIIQVYEDTSGVRPGEPVENTGMPLSVELGPGLLTSIYDGIQRPLEVLKEKMGNFITRGVSAPGLSRTKKWKFVPVVKAGDKVKGGIVIGTVQETKTIVHKIMVPPNVGETTIKDIKEGEFTVEDVIGHLENGTELKLMHKWPVRVPRPYVEKLRPDIPLITGQRVLDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLAEFPHLTDPKTGNPLMDRTVLIANTSNMPVAAREASCYTGITIAEYYRDMGYGVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLAARLSEFYERAGRVITPIGKEGSVTVIGAVSPAGGDISEPVTQNTLRIVKVFWALDAKLAQRRHFPSINWLNSYSLYQDSLKDWYDKNISPEWNQLKAESMELLQRESELQEIVQLVGSDALPEDQQLTIEIARMIREIFLQQNAYHEVDTYCSLDKQLKMLKSIMQFGAYARTALASGVPMSKILNLNSKNDLAKVKFEANYDAYLTKVNDDMKKEFKSLEAA", "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": "MKRKVDEFMERHGLGVGDLVRVVKREGDERITFEGLVMPPYELSPGETLTIKLDNGYNIGILIDAIEGIEILEKAKEAPKMEFREVLPRKEGLPSVTILGTGGTIASRIDYKTGAVHAAFTAEELAKAVPEIFDIANITPKLLFNIMSEDMKPEYWKKIAHEAAKALNSDEDGVVIAHGTDTMGYTAAALSFMLRNLTKPVVLVGSQRSSDRPSSDAAMNLICATRMAVSDAAEVMVVMHGETSDTYCLAHRGTKVRKMHTSRRDTFRSINDVPIAKVWPDGKIEYLRDDYRKRGEGEVEVDDKFEEKVAILKIYPGVTSELLEFLVDRGYKGIVIEGTGLGHTPNDMIPAIERAVENGVAVCMTSQCLYGRVNLNVYSTGRRLLKAGVIPCEDMLPETAYVKLGWVLGHTDDLKEVRRMMLTNYAGEITPYTRFDTFLR", "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": "MAKIFYDNDADLSLIQSKKVAIVGYGSQGHAHALNLRDSGVTVIVALPEGSKSRPKAQAAGLQVATVSEAAKAADVIMILAPDTSQARIYNEQIAPHLGPGKTLMFAHGFNIRFNTITPPPSVDVSMIAPKGPGHRVRETFEAGGGVPALLAVHQDASGKAEAQALAYAKGIGATRAGVLLTTFAEETETDLFGEQAVLCGGASELVKAGFETLVNAGYQPEIAYFECLHELKLIVDLMYRGGLNYMRYSISDTAEHGDYVSGPRVITDKTREEMKRILAEIQSGEFARKWIAENEAGRPKFEATRAKEREQRLEIVGANLRKMMPFIDPVTIKPGD", "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": "MYWLLFLFFVHFLRHGLCDTSTRSNGSGTMNPAGINITNSTYMNATWQSNSLSHELAVRSQRDIMSNITIDQVPFPGINLNSVLFHKAFIVNNNGSHLPFNESIAFEYFQNIMVYGAQSFVVDIEVGMNYSWVLKETDVLLSDLLIQMRNFISATNNNLYGNVLMLLLRVDPTIKLASARNKTIYNSRLNFTDDLFNKFPNLNITGILDNTIGRSFIYTPSDFLGTYDPPYSIDNSTNFWPTLGALMYGRRKRLLAMEITNSFDALESNYIFTNHNLTYDVGNVSISCPYNRDQFISASETTFKFLEARYTKSEVEMYSGCGYSPMIANRFDSANITALIDLLAPAVVWSWAVGQPILTVSVPRKTSDLVAENCAAFNFAYNNFSANWFVENCYSKKRALCRSDKQIFNWTATNVKDSYFEMDGYRGETKCPNTYSFSIPRTPLEQRSILLQFEASQFNDDTLWIDLNSISVSNCWVSGGSYASCPYQRAVSTRNFVAMMVPVTVCSFVLLMMALYFSLFRIPIYDNRYNWRRVVNNYSKTEVDGVPS", "text": "FUNCTION: May be involved in telomere capping. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MTC6 family."}
{"protein": "MLRVLTSTLRFPRPWKPLETRGCSSNPGAAGREIQVCALAGPNQGIAEILMNRPSARNALGNVFVSQLLEALAQLREDRQVRVLIFRSGVKGVFCAGADLKEREQMSEAEVGLFVQRLRGLMTEIAAFPAPTIAAMDGFALGGGLELALACDLRVAASSAVMGLIETTRGLLPGAGGTQRLPRCLGVALAKELIFTGRRLSGAQAQALGLVNHAVAQNEEGNAAYHRARALAQEILPQAPIAVRLSKVAIDRGIEVDIASGMAIEGICYAQNIPTRDRLEGMAAFREKRLPRFVGE", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MALKHFKPVTPSLRQLVIVDRSGLYKGKPVKTLTEGKSSSGGRNNNGRITVRFRGGGHKQTYRLVDFKRTKRGVPAVVDRIEYDPNRSAFIALIKYEDGDLAYILAPQRLAVGDQVIAGEQVDVKPGNAGPLSSLPVGTIVHNVELKVGKGGQIARSAGTYAQIVGRDQGYVIVRLNSGEQRLVLGACYATVGAVSNPDHMNISLGKAGRNRWLGRKPHNRGVTMNPVDHPHGGGEGRTSGGRNPVTPWGFPTKGKKTRNNKATDKFIVSSRHKRKK", "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": "MARVTVQEAADKIGNRFDLILTAARRARQLQLHVREPLVPEENDKPTVIALREIEKGLINGQIMDQLENNDAIQQEVAEQEAISFLADVQANA", "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": "MREALNQGLIDFLKASPTPFHATAALAQRLEAAGYQRLDERETWTTEPNGRYYVTRNDSSIIAFKLGRHSPLQGGIRLVGAHTDSPCLRVKPQPELQRQGFWQLGVEVYGGALLAPWFDRDLSLAGRVTFRRDGKVESQLIDFKLPIAIIPNLAIHLNREANQGWAINAQTELPPILAQFAGDERVDFRAVLTDQLAREHGLNADVVLDYELSFYDTQSAAVIGLNGDFIAGARLDNLLSCYAGLQALLTSETDETCVLVCNDHEEVGSCSACGADGPMLEQTLRRLLPEGDEFVRTIQKSLLVSADNAHGVHPNYAEKHDANHGPKLNAGPVIKVNSNQRYATNSETAGFFRHLCMAQEVPVQSFVVRSDMGCGSTIGPITASHLGVRTVDIGLPTFAMHSIRELCGSHDLAHLVKVLGAFYASHDLP", "text": "SIMILARITY: Belongs to the peptidase M18 family."}
{"protein": "MAYTLDRGSYAAMFGPTVGDRVRLADTELIIEVEQDYTTYGEEVKFGGGKVIRDGMGQSQHSRQEGAVDTVITNALIVDHWGIVKADVGIKDGRICAIGKAGNPDVQPNVDIIIGPGTEAIAGEGRILTAGGIDAHIHWICPQQIEDALHSGITTMLGGGTGPAEGTNATTCTPGPWHIARMLQAAEGLPMNMGFFGKGNASRPQGLEEQLRAGACGLKLHEDWGTTPSAIDVCLSVAEKWDVQVAIHTDTLNESGFVENTTAAFKGRTIHAFHTEGAGGGHAPDIIKLCGEANVLPSSTNPTRPFTRNTLDEHLDMLMVCHHLDSRIPEDVAFAESRIRRETIAAEDILHDLGAFSMIASDSQAMGRVGEVIIRTWQTADKMKRQRGALPEERGQNDNQRVKRYIAKYTINPAITHGIAHYVGSVAVGKLADLVLWKPMFFGVKPDLVLKCGTIASAAMGDPNASIPTPQPVHYRPMFGAFGGALTHSAVNFVSQAGLDGEIAQQFGLRKTLLPVVGCRTIGKADMVHNSATPHMEVDPETYEVRADGRLLTCEPATVLPLAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "MLPYPQIDPVALAIGPLKIHWYGLMYLIGIGGAWLLASRRLNRFDPTWSKEKLSDMVFWMSMGVIVGGRLGYVLFYDLSAYLANPTLIFEVWKGGMSFHGGFIGVMLAAWWFGKRNNKTFFELMDFVAPMVPIGLGAGRIGNFINAELWGKPTDLPWAMVFPPFSDPAQLPRHPSQLYQFALEGVALFLILWLFSRKPRPTMAVSGMFALFYGIFRFIVEFVRVPDAQLGYLAWNWLTMGQVLCVPMILGGLGLIWLAYHRAPAKSAAQ", "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": "MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP", "text": "FUNCTION: Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria, with highest activity against Gram-negative bacteria (PubMed:9202117, PubMed:10837369). Antimicrobial activity against P.aruginosa seems to be salt-sensitive and is reduced with high salt concentrations greater than 25 mM (PubMed:10837369). Also exhibits antimicrobial activity against the yeast C.albicans (PubMed:9202117, PubMed:10837369, PubMed:30050988). Permeabilizes C.albicans cell membranes via targeting plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), thereby leading to cell fragmentation and cell death (PubMed:30050988). Acts as a ligand for C- C chemokine receptor CCR6 (PubMed:10521347, PubMed:20068036). Binds to CCR6 and induces chemotactic activity of CCR6-expressing cells, such as immature dendritic cells and memory T cells (PubMed:10521347, PubMed:20068036). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family. LAP/TAP subfamily."}
{"protein": "MSHLVKMENGQSQTIQEMLGCIERYNPDHLKTLESYVQDQAKNNTYDLEANLAVLKLYQFNPHMLNFDITYTILLKSLTSLPHTDFVMAKCLLLPQQMKDENVQTIIDLADILERADFTLFWQRAEVNRNMFRHIAGFHDSIRKFVSHVVGTTFQTIRKDLLKELLGGIEDSTLESWIKRNGWKNQGQGLVIVAMQDDKIKTKNITEKIEFDNVGALMAQCL", "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": "MSDNQICDISNEVLEELKKFRFSKSKNNAALILKVDREKQTVVLDEFIDDISVDELQDTLPGHQPRYVIYTYKMVHDDQRISYPMCFIFYTPRDSQIELQMMYACTKSALQREVDLTRVYEIRELDELTEEWLKAKLK", "text": "FUNCTION: Inhibits Arp2/3-mediated actin nucleation (PubMed:25308079). Together with flr, promotes Arp2/3-nucleated actin filament array disassembly (PubMed:25308079). Promotes debranching (PubMed:25308079). Regulates lamellipodial protrusion dynamics possibly by facilitating lamellipodial retraction (PubMed:25308079). In egg chambers, enhances the retraction dynamics of cellular extensions in border cells and thus together with flr plays an important role in directional migration of border cell clusters (PubMed:25308079). SUBCELLULAR LOCATION: Cell projection, lamellipodium Cytoplasm, perinuclear region Nucleus Cytoplasm, cell cortex Note=Colocalizes with F-actin and Arp2/3-nucleated actin arrays. SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF subfamily."}
{"protein": "MAAIEDSPTFSSVVTPAAFEIGSLPTTEIPVDPVENDSTAPPKPVRITCPTVAGTYPVVLFFHGFYLRNYFYSDVLNHIASHGYILVAPQLCKLLPPGGQVEVDDAGSVINWASENLKAHLPTSVNANGKYTSLVGHSRGGKTAFAVALGHAATLDPSITFSALIGIDPVAGTNKYIRTDPHILTYKPESFELDIPVAVVGTGLGPKWNNVMPPCAPTDLNHEEFYKECKATKAHFVAADYGHMDMLDDDLPGFVGFMAGCMCKNGQRKKSEMRSFVGGIVVAFLKYSLWGEKAEIRLIVKDPSVSPAKLDPSPELEEASGIFV", "text": "FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to yield chlorophyllide and phytol (PubMed:10611389, PubMed:11950974). Shows a preferential activity toward chlorophyll a (PubMed:11950974). Does not seem to be required for chlorophyll degradation during senescence (PubMed:17996203, PubMed:18349515, PubMed:31779896). May modulate the balance between different plant defense pathways (PubMed:15598807). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MAKKVVTDLDLKNKKVLVRVDFNVPMKDGKITNDNRIVAALPTIEYILEQNGKAILFSHLGKVKTEEDKEGKSLRPVAARLSELLGKEVKFVPTTRGPELEKAVDELKDGEVLLFENTRFEDIDGKKESKNDPELGKYWASLGDVFVNDAFGTAHRAHASNVGIASNLESAAGFLMEKEIKFIGGVVDNPARPLVAILGGAKVSDKIGVIENLLTKADKVLVGGGMTFTFMAAQGQEIGKSLLEADKVELAKGLLEKAGDKLVLPVDAVVSKEFSNDAPFHTVSADSIPADEMGLDIGQATIDLFTKELQGAKTVVWNGPMGVFELSNFAKGTIGVCEAIANLTDATTIIGGGDSAAAAMDLGFADKFTHISTGGGASLEYLEGKELPGVASISDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MSSVVVVGTQWGDEGKGKITDFLSQNAEVVARYQGGNNAGHTIKFDDVTYKLHLIPSGIFFEDKICVLGNGMVIDPKAFVEEVAYLHERNVSTDNLRISNRAHVILPYHLKLDILQEEDKGANKIGTTKKGIGPAYMDKAARVGIRVADLMDKDAFREKLVQNLKEKNRLFEKVYEADPIQVEEILDEYYAYGQKMAPYVTDTSVVLNDAIDEGKRVLFEGAQGVMLDIDQGTYPFVTSSNPIAGGVTIGSGVGPTKINHVVGVSKAYTTRVGDGPFPTELHDEIGNQIREVGREYGTTTGRARRVGWFDSVVVRHARRVSGITDLSLNSIDVLTGIETLKICVAYRYKGEIMKEFPASLKVLAECEPVYEEMPGWQEDITGAKSLDDLPENARHYLERVSQLTEIPLSIFSVGPDRSQTNVVRSVYRP", "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": "MLKMSGWQRQSQNQSWNLRRECSRRKCIFIHHHT", "text": "FUNCTION: [Isoform AltDDIT3]: Product of the upstream open reading frame (uORF) of DDIT3/CHOP that is specifically produced in absence of stress, thereby preventing translation of downstream stress effector DDIT3/CHOP. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MDIGRKIELITKRPTEELLTVENLRHLLEIGAPMQHYIGFEISGYIHLGTGLMAGAKIADLQKAGIKTRIFLADWHSWINDKLGGDLEIIQKVALTYFKEGMKQSIKVMGGDPDKVEFVLASEILEKGDYWQTVIDISKNVTLARMMRSITIMGRQMGEAIDFAKLIYPAMQVADIFYQGVTIAHAGMDQRKAHVIAIEVAQKLKYHAIEHNGEKLKPVALHHHLLLGLQEPPVWPIESEEQYKELKTQMKMSKSKPYSAVFIHDTPEEIKQKLRKAFCPAREVKYNPVLDWAEYIIFREEPTEFTIHRPAKFGGDVTYTTFEELKRDFAEGKLHPLDLKNAVAEYLIELLKPVRDYFEKHPEPLELMREIKITR", "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": "MPPLRWQACLFITINAVALSMLLFDAPVGASERPAAVKELGELLTGFGDSAWLICISILLFFQGKAGYKLLKTARSKAQALYVSWIGAYLFTTVVFSGLLANLLKRAIGRARPDHFHDYGMFSFTPFSGHAAFESFPSGHSTTVGAFFAAFALLFPRYRVAFIACAIWLGMTRVMVGAHYPSDVIAGLAFGGWFSLLTAIVYARCGLLFKLAPDGWPLAKRLFPDIEKPGAL", "text": "FUNCTION: Probably removes the 1-phosphate moiety from lipid A species. Does not seem to act on other membrane components, nor does it dephosphorylate the 4'-phosphate group of lipid A and/or lipid A precursors. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the lipid A LpxE 1-phosphatase family."}
{"protein": "MIQTISADGIGYGATLQNHFLIAMPGMRDERFARSVIYMCAHNAEGAMGIIINRGQQLGFTDILVELGILERSQSIRLPARARNIAVRSGGPVDRSRGFVLHSDDYVVESSMAVSEKICLTATVDILRAISTGRGPSQALMALGYSGWGAGQLEAEIADNGWLACPASPELLFDAEIDTIYDRILAANGIDPLHLSQVAGHA", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
{"protein": "MKFGKDFVRQMIPEWQQAYMDYAGLKSILQEIQTSRKRSERPGILKRKLSGSRNFSGLTKRYSRTASTREPEIQDILVHATTGDDGFERYETTILEVAEAGRESELAFFKTLDLEFDKVNHFYRSKVEEMVKEAVVLNKQMDALIAFRIKVERPSSSWSCSETVSVDMNALDSNDQRNTLAEEMGIRVEGNGSNGGDSTKESVPQVLSVLERIRLNKTQETPLSTIKNVLKLSNQEELKFTRENLKKIEERLKNVFIEFYRKLRHLKNYSFLNTLAISKIMKKYDKIASRSAAKPYMEMVDKSYLTSSDEINKLMLRVESTFVEHFAGLNRSKGMNLLRPKVKKEKHRITFSTGFFVGCTVSLVVALVMFIHARNIMGAVGHKVYMETMFPLYSLFAFVVLHMIMYASNIYFWKRYRVNYPFIFGFKEGTELGYRHVLLLSFGLGTLALCAVLINLDMEMDPNTNDYKTMTELLPMFILALVVAILFCPFNIFYRSSRVFFLMVVFRCIAAPLYKVNLPDFFLADQLTSQVQALRSLEFYICYYGWGDFKHRQNTCRSSDVYSTFYFIVAVIPYWSRFLQCVRRLIEENDSSQGYNALKYLLTVVAVCLRTAYSFNRGNIWKISAWVFSALATFYGTYWDIVFDWGLLHRPSKHLLREKLLVPHKAVYYVAIVLNIVLRMAWLQTVLDFNLSFLHRETMIALLAALEIIRRGIWNFFRLENEHLNNVGKFRAFKSVPLPFNYNEEEDRDS", "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": "MGKYRKKAREIVFRTLYTYDIKGGDLFEIMEDHIKDIRGKLSKKTVDYIYSILKGIDEHLPEIDDILRENLKNWRLERLGYPERALLRLGVYELLFSDIEDKGRVFMDILDLTKCYIDNPDTVKFINGVLSTVYKNRQKVNQ", "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": "MPQAINLKDLPQAKLKDLLEFPCAFTFKVVGIHREDLVEDVVAITQVHAKGDCNPRQQRSSKGTYNSVSIDIIAEHIDQIETLYLELAKITGVRMVL", "text": "SIMILARITY: Belongs to the UPF0250 family."}
{"protein": "MAGMKTATGDYIDSSWELRVFIGEEDPEAESLTLRVTGESHIGGVLLKIVEEIKRKQDWSDHAIWWEQKRQWLLQTHWTLDKYGILADARLFFGPQHRPVILRLPNRRALRLRASFSQPLFQAMVAICRLLSIRHPEEMSLLRAPEKEKKKKKEKEPEEEVYDLTKVVLVGGVAPASFRGMPAHFSDSAQTEACYHMLSRPQPPPDPLLLQRLPRPSSLLDKTQLHSRWLDSSRCLMQQGIKAGDTLWLRFKYYSFFDLDPKTDPVRLTQLYEQARWDLLLEEIDCTEEEMMVFAALQYHINKLSQSGEVDEPAGTDSGLDDLDLALSNLEVKLEGSAPTDMLDSLTTIPELKDHLRIFRPRKLTLKGYRQHWVVFKETTLSYYKSQDEAPGEPIQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYARWMAGCRLASKGRTMADSSYSSEVQAILAFLSLQRTGGGGGGSGNHPQGPDASAEGLNPYGLVAPRFQRKFKAKQLTPRILEAHQNVAQLSLSEAQLRFIQAWQSLPDFGISYVVVRFKGSRKDEILGIANNRLIRIDLSVGDVVKTWRFSNMRQWNVNWDIRQVAIEFDEHINVAFSCVSASCRIVHEYIGGYIFLSTRERARGEELDEDLFLQLTGGHEAF", "text": "FUNCTION: Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs). SUBCELLULAR LOCATION: Cell projection, podosome Note=Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells. SIMILARITY: Belongs to the kindlin family."}
{"protein": "MGKLQDWSITTCLFLFFLHASQTHCTSQSHVRNRLYRSKRGIGSSIDTSHLNAIRRLSVSLSLQNISGVNQQEQKERDLIENLPGQPSVNFKQYGGYVTVNESAGRSLYYYFVEATNTKNSSPLVLWLNGGPGCSSLYGAFQELGPFRVHSDNKTLYTNPYSWNNVANMLFLESPAGTGFSYTNTTTDMENPGDMKTAADNYVFLVKWLERFPEYKGRDFYIAGESYAGHYVQWRHGCGDFGDSYNVRTEDDESNGCYGMASVV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MIPIQLSVFFMIIYVLESLTIIVQSSLIVAVLGREWLQIRRLMPVDMILISLGISRFCLQWTSMLNDFCFYFNFNYVLCNLTITWTFFNVLTFWLNSLLTVFYCIKVSSFTHPIVLWLRWRILRWLPWLLLGCLMITCVTIIPSAIGNYIQIQFLTMEHPPRNSTVIDRLQKFHQYLHQAHTVALVIPFILFLASTILLMASLTKQIQHHGTGHCNPSMKAHFTALRSLAILFIVFTSYFLTILITMIGTLFDKRCWLWVWEAFVYAFIFMHSTSLMLSSPTLKRILNGKC", "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: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
{"protein": "MASQGTKRSYEQMETGGERQNATEIRASVGRMVGGIGRFYIQMCTELKLSDHEGRLIQNSITIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRRDGKWMRELILYDKEEIRRIWRQRNNGDDATAGLTHLMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGLAVAGGYDFEREGYSLVGIDPFRLLQNSQVFSLIRPNENPAHKSQLVWMACHSAAFEDLRVSNFIRGTRVVPRGKLSTRGVQIASNENMETMDSSTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERATIMAAFTGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKATNPIVPSFDMSNEGSYFFGDNAEEYDN", "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": "MGGKTVTRADLAEAVYRKVGLSRTESAALVEMILDEVCDAIVNGETVKLSSFATFQVRDKNERIGRNPKTGEEVPILPRRVMTFKASNVLKQRILQEHQKRETKSQK", "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": "MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDPSKDSGEGSCSDSEENILEEELNEDIQVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATVSDSAAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVSEPKKWNLRRNRPLLDFVSMEELNAMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDDDEGSGSEEDENDEGNDEDHSSPASEAGGKKKRSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCGVSPSCELCPNQDGIFKETDAGRWVHIVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHADRLDRKWKRKNYLALQSYCKMSLQEREKQLSPEAQARINARLQQYRAKAELARSTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDNSDTSSSVDGRRKHKQPALTADFVNYYFERNMRMIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSEGQGIWALLGRITGQKLNVPAILRAPKERKPSKKEGGTQKTSALPTVLYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQAGSSDMEAEMAMETLPDGTKRSRRQIKEPVKFVPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKPKAEDLRTECSTCKGTGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDSSSSKEDENEAEKKNASQELSMEQKTPKK", "text": "FUNCTION: Histone-binding protein (By similarity). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (PubMed:22730381). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (PubMed:33035772). SUBCELLULAR LOCATION: [Isoform 1]: Nucleus Chromosome Note=Mainly localized in the nucleus of interphase cells. In mitotic cells, colocalizes with condensed chromatin during metaphase and anaphase. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm."}
{"protein": "MTTTKRPIALLILDGWGYRENTHMNAVYHANTPVLDRLNAQYAHGLISGSGLDVGLPDGQMGNSEVGHINLGSGRIVYQELTRISKAIADHEFEQNPALCDAVDAAVKTGGAVHIMGLLSPGGVHSHEEHIEAMCRMAVARGATKVYLHAFLDGRDTPPRSAKSSLSHFDDLFTTLGHGRIASIIGRYFAMDRDNRWDRVSQAYDLITQGKSKFQYDNAVTALEAAYSRDENDEFVSSSAITDANGQVATLQDGDALIFMNFRADRARQITRSFINPEFDGFARAVTPKVNFVTLTEYAADIKAPIAYPSDNLVNTLGEVLQNRGRTQLRISETEKYAHVTFFFNGGKEEPFNGEDRILINSPKVATYDLQPEMSSTELTDKLVAAIESTKYDVIICNYPNGDMVGHTGNFDAAVKACEAVDACIGRVVEALAKVGGECIITADHGNAEQMTDETTGQAHTAHTSELVPFVFVGRDATIDKGGKLSDVAPTILHLMGESIPAEMTGKPLIHVKE", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family."}
{"protein": "MKEAKIENIDFGNALSERYLAYALSTIMSRSLPDVRDGLKPVHRRLLYAMLQLRLEPNSGYKKCARVVGDVIGKYHPHGDVAVYDTLVRLAQHFSLRYPLIDGQGNFGSIDGDNAAAMRYTESRMTEICMLLMEDIDKDTVDFRSTYDDSDLEPVIMPASFPNLLANGSEGIAVGMATNIPPHNLHELCDALLYLIDNPQAGINDIMNFIKGPDFPTGGIIIDKAEVINAAYTTGRGSFRVRSRWEKEELSYGTYQIVVTEIPYQIQKSKLIEQIAILLKDKKIPLISSIRDESTDIIRVVIEPRDRSCDPQIVMESLFKLTNLESRIQLNMNVIGSNNVPRVMNILEILQEFLVHRKNIIIRRSTYLLNKIKQRLEILKVLRIVYLNLDEIIEIIREEDEPKTIIMERFKISAIQVEVILNTRLRSLQKLEEHAIIDEHSNLQKQQAILEKILKNHKELWQIVKKEIKAVQTKFGLNTIIGARRTSFEEVDLTNQVVDITAFITKEPITIICSKMGWVRSLKGHNTDLSTIKYKEGDTEKFIIEAYTTDKILIISSKGRFFTLLADNISKGKGTGGVSIKLLVDIGNNDITNILVYKPNQLLLLASSIGKGFLVNSNEVIAQTKTGKQIMNIPEGYSCIACLPVNGDSIACIGESRRLLVFNIDEIPEMKKGQGVVLQRFKNAKLLDIKIFNKQDGLSWNDGTKIQLEKNIVAFLGKRGGFGTFPPIGFPKNNRFSP", "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": "MKVFLGLLLGFSIILILTYQSPTTQHPPKEELAYWCTYAKSCDFCWDCQNDTCINKVINESISITSIVNCRVTRDSQSCFYDISVKIPNHHSMECSYPRLYEHEMFMEKWRDEYWPIIIKQCCFYLVFSFAFAGCVAFAICKNLRLRTTIKLLILLSILVWLSQPILNN", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the asfivirus MGF 110 family."}
{"protein": "MDPEEQLESTEGVPAKSLSLIKHILLVLSGKGGVGKSSVTTQTALTLCGMGYNVGVLDIDLTGPSLPRMFGIEDSSIYQSADGWMPIPVETNGKGKLCVVSLGFLLGSRGTSVVWRGPKKTSMIRQFIKDVTWGELDYLLIDTPPGTSDEHISIAEELRFTNPDGAIVVTTPQGVATADVKKEINFCRKVNLRILGVIENMSGFVCPYCTECTNIFSKGGGESLAKQFDVPYLGNIPIDPKFVDLIENQKKMEGTLVELYEKSSLYPIYLEIMKKVQEESSKPQE", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily."}
{"protein": "MSGGSTGERPFSDIITSIRYWVIHSITIPSLFVAGWLFVSTGLAYDVFGTPRPNEYFTQDRQQVPLVNDRFSAKQELEDLTKGI", "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": "MIPPKQQTALKITPEGRIAAVSSPLPSLQDNELLVCVKSIALNPFDAKSAEMSPTIGATLGCDFAGKIVATGSNANDFNFSIGDRVCGCVFGNNPNRLDNGAFAEYVAVPADLLLRIPEHMDYNEAATLGVGLATVGMSLYHCLRLPMKPEQAGKSPSGYAAITTCSPHNFNLVKSLGATAAFDYHSPTCGRQIRDFSSGNLWYALDCITDTRSMAVCYEAIGPSGGRYLSLDPFPIRGHTRRSVKPNWVLSVTMYNQPIPWKRPFKRDACPQDLEFAKSWFQIAQRMIDAGEIRPHTSDVKAGGWNGIPGGLELLQKGEVSGRKLVYEVASH", "text": "FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821, PubMed:20828130, Ref.5). The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit (PubMed:20828130). The growing polyketide chain then elongates into a tetraketide (PubMed:20828130). The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:17369821, PubMed:20828130). Alpha- methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules (PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl- thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130). The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps (PubMed:20828130). A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A (PubMed:17369821). The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD- dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (PubMed:17369821) (Probable). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MTRLSVNVNKIATLRNARGGNVPDVLRVALDCERFGAQGITVHPRPDERHIRRSDVYDLKKALTTEFNIEGNPDERFIRLIEEIRPEQVTMVPDAPDVLTSNAGWDVARNYDHLCRLVEQFHAWGIRTSIFIDTDLDNISWAAKTGTDRIELYTEPYAAAYHKDMAAAVQPYVKASAHAHSLGLGINAGHDLNLDNLRYFAERLPYLDEVSIGHALIADALYLGLEETIRQYRDQLAL", "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": "MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF", "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 and the reversible oxidation of (S)-malate to oxaloacetate. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
{"protein": "MARVTVQDAVEKIGNRFDLVLVAARRARQLQVGAKDPLVPEENDKMTVIALREIEEGLINGKILDARERQEQQEQEAAELQAVSAIAEGRR", "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": "MTIRKVLNKYWGWTFLIVPLILQVVFFYFPMFQGAFYSFTNWTGLTYNFDFVGINNYKILMTDGKFMKAIGFTLVLTLALIVGEIVLGIIIARALNAKIKGKTFFRAWFFFPAVLSGLTVSLIFKQVFNYGLPAVGSALGIKFLETSMLGTANGAVIASIFVLLWQGVAMPIILFLSGLQSIPSEIVEAAAIDGADSKQTFWSVELPYLLPSISMVFIMALKAGLTAFDQIFALTGGGPNNSTTSLGLLVYNYAFKSNQYGYANAIALILFIIIGIVSVLQIKLSKKFEV", "text": "FUNCTION: Involved in a binding protein-dependent transport system responsible for the uptake of melibiose, raffinose and isomaltotriose. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. MalFG subfamily."}
{"protein": "MEVKSAKELKRISKELQENFLNRWKLLNLEQDKDRLKSLTEKAEDPNLWNNPEEARLVSQKKNELEKKLNPWFTIQQDILDFPDLVDLTLDEKGENGVGELSSEYNRLQEKFEELELLGALKNPEDLKPAFLNIHPGAGGTESQDWAEMLLRMYTRYFEKKGYQYSLIDVQAGDGAGIKNATLHVIGDFAFGFLKGENGVHRLVRISPFDANKRRHTSFVSVHVSPEIDDDIDIKIEEKDIRVDVYRSSGAGGQHVNTTDSAVRITHMPSGIVVACQNERSQIKNRDTAFKMLKARLYELEQEKAKEELEKKSGEKKDITWGSQIRSYVFHPYNLVKDHRTDHETGNVAAVMDGDIEPFILAYLKTL", "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": "MMMIMGRKCEDCGNQAKKDCVYMRCRTCCKSKAFHCQTHIKSTWVPAYRRSHHKHQSQPLSTSIPKGVQIHTTPGHFPAELSSLADFRCVKVSSIDDGKEQYAYQTTVNIGGHVFRGILHDQGLHKVMVDHHYNKNSNNHQELLTPSTSSCPLKITSPFTDFMFGTRFSSVLRR", "text": "FUNCTION: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influences vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHI protein family."}
{"protein": "MLTIGVLGLQGAVREHIRSIEACGAAGKVIKWPEELKEIDGLILPGGESTTMRRLIDTYQFMKPLQEFAASGKPVFGTCAGLIILAKNIAGTNDAHLGVLDVTVERNSFGRQVDSFEADLTVKGLEGPFTGVFIRAPHILEAGADVEVLSEHNGRIVAAKQGNLLGCSFHPELTDDHRMTKLFVEMVEKHKREAVV", "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": "MPAIPPKLILASSSRYRRELLSRLRLPFTAISPDVDETPQPGEAPADLALRLSVAKAMAVAATHPGSVVIGSDQVATVDGDPIGKPGGFERAREQLRRLSGRAVEFHSAMAVTDGVHTETADIVTLCRFRTLTDAAIDAYLRAEEPYDTAGSAKAESLGIALMDSIRSDDPTAIIGLPLIALTRMLGRFGLDPLTGHPA", "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": "MEDLLTNPLIIAAIIGIISAIFGKKSKEEKQNSQKRKKPQHVQSASPQKKQSKEDAPAPIPNRMEQARREAEERRRETARNLKGLERDLAAAKQKTVYTKQKMLQVNKDTVVQGIVLGEVFGPPRAKKPHRTMRPARKN", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MATFKKFNKDKRPKRNTQSLLFKRKRFCRFTVAGVEEIDYKDIDTLRDFISENGKIIPARLTGTRAIYQRQLNTAIKRARFLAMVPYSDQHRV", "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": "MGSATREARARSVSALAGLGSKADLATAEDLFAAGRVVADSVQLRAVLSDPAADRSGKDVLVKRVFGALSAPAVELLGVIAGERWSGQDDVLDAIEELGIRSIAASAPRTVDIPAELLAFGGAVTSDAELELALRSKLADPSAKAALVERLLVGKAAGQTVAITRQLVLQPRGRSVRQALREAARIVAAQDGQTIATVVTATPLPAAQAERLRASLAAKYGDLKLNQVVDPSILGGMRVQIGGDVIDGSVSSRLSKLRLQLAG", "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": "MHIIIAGIDTEVGKTFVSAILATLFQAEYWKPIQSGSLDRSDSTIVRELSGAVCHRETYRLTHPLAAHQAARVDNIPIHAENFSLPVTEAPLIIETSGGFLSPCSQDSLQGDVFSKWPCQWVLVSKAYLGSINHTCLTVEAMRTRNLNILGMVLNQYPKEEEDWLLNMTGIPYLGRLNYENIISKETVKNYANLWKETWEDREAKLCS", "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": "MEERENSEEGDDGAGEEEEEDQGSGEDGGEVGAEREQEAELKDSLRPSVLDLQLALARLCEDEYQDQPSKMPVLGLQIKDHQFERSFSGNGKVPSPGKIVNELFKEAKEHGAIPIDDTSKSSGAFYRARTFTGRGYKLGDSSKREFEYMQGEDPFEQGQEIQILLKLWSNGFSLDDGELRSYSDPINAEFLESVKKGEIPVELQRLVHGGQVNLDMEDHQDQEYIKPRLKFKAFSGEGKKLGSVTPEIISTPSSPEEEHKRFLNAEVDLDEHVPTTKIQIRLADGTRLIQRFNLSHRIMDVRQFIIHARSDFAQCDFALLTTFPNVELTDETQTLEEADILNTVILQRLK", "text": "FUNCTION: Adapter protein required for Golgi and endoplasmic reticulum biogenesis. Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis. Regulates the centrosomal levels of kinase aurka-a/Aurora A during mitotic progression by promoting aurka-a removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Endoplasmic reticulum Golgi apparatus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to centrosome during mitotic prophase and metaphase. SIMILARITY: Belongs to the NSFL1C family."}
{"protein": "MDSVLSGKIVQILVGYLKENIYSEQMIKLRMKRICSYEEFLPTYSLIERITEESKEIAIKVYEKNIIVEIVKDFKNKDLIELFELKEELFDEALSYLKKYNADKFLESYTLYCFSEYSDPDSFIKENKSILTKLLRNQYEEVPEEYINELLKSKIKYSTKDLIILDWDNGIILDKNEDFWEEVDIIELACIRVLNLRVFDSMLSEAIQYFTRLQWEKLGYFKLKKLSKDLYLQRISYISYFDSIENVLMLYGDRYYAELYERLCKIFYVSEWIKRVEKKMEMISDIYTMTRQHLTEFYGLLLEGTIVALILLEIILALAKIV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MSFSFGFTSNDFDDDELVAQPETFVESSKENENTTAYINPLDSDFLSQAGVVQPNVEDLGTILESLKDVRLTFEEFQSPIYRKPLIKRELFDVKHQLMLETDAQSNNNSTELDILLGDTSEDLRKNIYEGGLKSWECSYDLVDLLSENVDRISNDIDAVVEIGCGTALPSEFLFRSALLRNDRSKGLKFVLTDYNASVLRLVTIPNLVITWAKTVLTKEQWYALQKDECEDIPINNEELLLTSKLLAAFYDDVQSRNISVTLISGSWGRKFSNLIHEVLSGSQKVLSLSSETIYQPDNLPVIAETILDIHNLPQTDVKTYVAAKDIYFGVGGSITEFEAYLDDKINSEHLPIHSERFKVNSGLKRSIICIETNKAIR", "text": "FUNCTION: Protein-histidine N-methyltransferase that mediates methylation of RPL3 at 'His-243' (PubMed:20864530, PubMed:24865971). Methylates ribosome-associated RPL3, but not free RPL3, thereby regulating 60S subunit assembly (PubMed:24865971, PubMed:26826131). In addition to RPL3, mediates His methylation of other proteins (PubMed:26826131). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the methyltransferase superfamily. METTL18 family."}
{"protein": "MAAADDAQFPPPKVLTYPASTPPTLITQGAEGRLYKTTHLTRDRPCALKYRPPKPYRHPVLDARLTKARLSSEAKVLERCWREGVPVPAVYAMDPAAGWMMMEWIEGIPVRVGINEWLGDRPEEGAEIPQVADETPIVDLMKRIGAAIGALHKTGVVHGDLTTSNMMLRPRGFNPVDGAPGDEGKAGSVEGDVVLIDFGLATQSMSDEDRAVDLYVLERAFASTHPRAERLFATLLESYKSTFKKASSVLIKLEDVRMRGRKRSMLG", "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": "MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL", "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. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis. SUBCELLULAR LOCATION: [Isoform p46Shc]: Mitochondrion matrix Note=Localized to the mitochondria matrix. Targeting of isoform p46Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization. SUBCELLULAR LOCATION: [Isoform p66Shc]: Mitochondrion Note=In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation. SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion."}
{"protein": "MSDVLRPYRDLFPQIGQRVMIDDSSVVIGDVRLADDVGIWPLVVIRGDVHYVQIGARTNIQDGSMLHVTHKSSYNPDGNPLTIGEDVTVGHKVMLHGCTIGNRVLVGMGSILLDGAIVEDDVMIGAGSLVPQNKRLESGYLYLGSPVKQIRPLSDEEKAGLRYSANNYVKWKDEYLDQGNQTQP", "text": "SIMILARITY: Belongs to the gamma-class carbonic anhydrase family."}
{"protein": "MPELPEVETVRKGLEKLLNDFYIERIEVLKERSIASNGGSKSFIVSVKNSYLGSWERRGKYLIGSLLTKEKFSKGFLVVHLRMTGQFKLLEKEVLACKHTRVRFFDERGRELRFIDIRNFGQMWHVPSSRSIPEIVSGIKRLGPEPFSDDFNSHYLEEYLKKKTRSIKSALLDQETVAGVGNIYADETLFDAGINPKKESRNLKSTELKRLCNSLVKILNISIGEGGTTFSDFRDLEGINGNYGGQAWVYRRSGKNCKKCGEKILREKICGRSTHWCPNCQK", "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": "MNPPGTFHITATDGSARTGVLYTAHGIVNTPIFMPVGTVGSVKAIAPDDLEAISAEIILGNTYHLYLRPGDELIARRGGLHVFNAWEKPILTDSGGFQIFSLSSLRKLHKDGVIFRSHIDGSKHVFTPERVITIQRNLNSDIMMVLDECVAANADYTYTAQSLDLTIHWAKRSRDVYPKGEGDNLLFGIVQGGMFKSLRHSSVSQLIDLDFDGYAIGGLSVGEPKEIMMELLYDTAPLLPKTKPRYLMGVGTPLDILKGIEAGVDMFDCVLPTRNARNGTLYTSQGKLNIKRKEYAEDDLPLDENCSCYTCQTFSRAYLRHLFHSQELLAFRLNSIHNLTYFLNIIFGARKAIHGGYFFNYKQQVEQLYCN", "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": "MDYVSLLNQFWQKQIKSYKETPSQYHYLYPPRFFYKPVLGNLQHPTKWCCTIKFYEYSAQATECTKASAKQDAARLICEQLQAAGLLNGMELRFRSSASDIFGQNRYDASKSYFFSKTA", "text": "FUNCTION: Induces host cell G0/G1 arrest and apoptosis. SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host mitochondrion."}
{"protein": "MSLKHFIQITKPGIIFGNVLSVAGGFFLASKGHVDLAVFLAAMIGTSLVVASGCVFNNCIDRDIDLKMERTKNRVLVQGLISLKLALVYATVLGVAGVALLYKVANPLAALFAVIGFIIYVGFYSLYLKRKSVHGTLVGSLSGAMPPVIGYVAVTNSFDMAALTLLVMFSLWQMPHSYAIAIFRFNDYLAASIPVLPVKRGIQVAKKHILIYILAFLVATLMLTFSGYAGMSYLAVAAAMGMYWLYMAWTGYKAVDDTVWARKLFVFSIFTITALSVMMSLDFKVPTELLLTYAP", "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": "MSTVNQSSTRSELAGNWERLRKSCDTCQEAKVKCSQHKPSCHRCLRHRQPCVYSPQRRSGRPPKRPSPSSRLGPESNNSGDDIHNENTIQRTNLNANDSAMTDAGAVDPRVLTGDFAASTGIDPVDDIFQTSFESFLAASLSPKGGLLPGSHSNPTTPNGFSMNSPSITDPFGAFPFLITDHNLPIAALSSHVPPIDQLPVLSTGASNTSSECGDCGAKCYSSLLQHLLFLRQTLPESTRPSIDVIMQAEGHVRALLDRVLGCNACLGNRSSILLISAITERIVQMLDWIIEEKTLLDTENMRYNRRTFSSWGRPPRLPPHGLNGMRRNVCHVSLRVGNTELDEDAKQYFLKNFILLRLKKLAVKVQEVRRTATTRPGDCIYRAAELVLADSIQRLDYLRGQCQLWE", "text": "FUNCTION: Transcriptional regulator involved in the positive regulation of the expression of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSQLPFWQQKTLAEMSDSEWESLCDGCGQCCLNKLIDEDTDEIYFTNVACDQLNLKTCQCRNYERRFELEEDCIKLTRENLVTFEWLPPTCAYRLIGEGHDLPKWHPLLAGSKSAMHGERISVRHIAVRESEVIDWQDHILNKPQWAR", "text": "SIMILARITY: Belongs to the UPF0260 family."}
{"protein": "MRADTADYPQLFLEDVPMMDTRAPVEFAGGAFPNVLNLPLMTDSERQKVGTCYKQHGQRAAIELGHRLVSGRTKELRIQAWADFARAHPEGYLYCFRGGLRSQIVQQWLRDEAGIDYPRVTGGYKAMRNFLLDTTRQATAQCAFVLVGGLTGTGKTEVIAALGNALDLEGHANHRGSSFGKRATPQPAQIDFENRLAIDILRKRAAGVGRFVLEDESRLVGSCSLPLELHQGMQRYPLVWLEDSFEGRVERILRDYVVDLCAEFVAVEGPQAGFAAFAARLTQSLANIVKRLGGERYQRLSTLMARALAEQEAGRGVALHRDWIVGLLREYYDPMYAYQRESKAERIVFSGDREAVLAYLRECAAGAVDG", "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": "MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGENIYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLIFASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLCSWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWTPLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWGTFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEFRFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQKVCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNPLNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVYERKLKGKFNMKMKF", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2- GlcN-acyl-PI during GPI precursor assembly. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB subfamily."}
{"protein": "MRTATIKRKTKETDIEVTVNLDGAGVSNAATGIGFFDHMLDLLAKHSRIDITVKAVGDLHVDFHHTTEDVGIALGQAVRQALGNMAGIIRYASMLMPMDETLTRVVIDVSGRPFLVFKAEFPRDKIGEFDTELVREWFQAFAMNAGVTLHVETLYGENSHHIAESCFKGLARALRAAVAIDPQAAGEVPSTKGQLGG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MNNLSLANEKTKIQVRGLEFFYNNQKSLKSIDMTIPEKRITAIIGPSGCGKSTLLRVFNRIYAMYPKQEARGEVLLNGENILAPGYSMNRLRSHVGMVFQKPVPFPMSIYDNISYAIKHHEKLSRREMEDRVEQALRGAALWDEVKDKLKQSATGLSGGQQQRLCIARTIALRPQVLLLDEPTSALDPISTGRIEQLITELKEQFTVIIVTHNMQQAARCSDYTAFMFMGELIEHGDTDTIFTKPSKTQTEDYITGRFG", "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": "MSAAELASSYAALILADEGLEITADKLQALISAAKVPEIEPIWTSLFAKALEGKDVKDLLLNVGSGGGAAPAAGGAAAGGAAAVLDAPAEEKAEEEKEESDDDMGFGLFD", "text": "FUNCTION: Plays an important role in the elongation step of protein synthesis. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family."}
{"protein": "MASTSDIRNGLCIKFNHDIYKIIEFLHVKPGKGPAFVRTKLKSLTSGKVLDNTFSAGHKIDVIRVETHTFQFLYPEGDEFHFMNAETFEQISLNKNILDAPDLLKEGTNVMVQINTETDLPLSVDMPASVILEVTYAEPGVKGNTATNATKNATVETGANVNVPLFINEGDKIKIDTASGSYMERVKE", "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": "MIIVAHVLLILLGATEILQADLLPDEKISLLPPVNFTIKVTGLAQVLLQWKPNPDQEQRNVNLEYQVKINAPKEDDYETRITESKCVTILHKGFSASVRTILQNDHSLLASSWASAELHAPPGSPGTSIVNLTCTTNTTEDNYSRLRSYQVSLHCTWLVGTDAPEDTQYFLYYRYGSWTEECQEYSKDTLGRNIACWFPRTFILSKGRDWLAVLVNGSSKHSAIRPFDQLFALHAIDQINPPLNVTAEIEGTRLSIQWEKPVSAFPIHCFDYEVKIHNTRNGYLQIEKLMTNAFISIIDDLSKYDVQVRAAVSSMCREAGLWSEWSQPIYVGNDEHKPLREWFVIVIMATICFILLILSLICKICHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVICYIEKPGVETLEDSVF", "text": "FUNCTION: Cell surface receptor that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:9378992). Acts by forming an heterodimeric receptor with CSF2RB subunit and subsequently binding to interleukin-5 (PubMed:1495999, PubMed:22528658). In unstimulated conditions, interacts constitutively with JAK2. Heterodimeric receptor activation leads to JAK2 stimulation and subsequent activation of the JAK-STAT pathway (PubMed:9516124). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 5 subfamily."}
{"protein": "MANTTSAKKATRKIARRTAINKSRRTRVRNFVRKVEEAIASGDQALAAAALKAAQPELHRAASKGVVHANTASRKISRLASRVKALAA", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
{"protein": "MRQENDSLGIVLVPEDKLFGAQTGRSQEFFSYGKESMPLEIIHALVKIKKCAAKANGDLGCLDAKRRDMIVAATDEILSGEFDEHFPLKVWQTGSGTQSNMNVNEVIANLAIQRHGGELGSKHPVHPNDHVNKSQSSNDVFPTAMHIAAVQSIKGSLIPALEHLKKVIDAKALEFARDIKIGRTHLMDAVPMTLGQEFSGYSCQLHNCLERIGFSLTHLYELAIGGTAIGTGLNVPEGFVEKVIQYLRRETGEPFVPASNYFAALSNHDALVQAHGSLTVLACALVKIATDLSFLGSGPRCGLGEIFFPENEPGSSIMPGKINPTQSEALQMVCSQVIGNNQSIIFSGTKGNFELNVMKPVIIYDFLQSVNLLAGAMRSFADYFVCGLKVNKGQLQQNVERSLMLVTALAPVLGYDKCSKIALKAFHENLSLKEACVSLGFLSEKEFDEHVIPGLMVGNRGHE", "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": "MISRDDITGLILAGGRGSRMGGTDKGLQPLRGVPMAMHTLMRLSAQTGAVLINANRNLAAYESFGVPVVTDSVPDFAGPLAGMLAGLEQCQTGWMVTAPCDSPFLPTDLVQRLAQAIETEDAELAIPVTIDADGRRQTQPVFCLMPASAIDSLVAYLNGGGRKIETWAASHRLVEVPFDDAAAFANINTLDELHMHESEKRAG", "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": "MASNLRELRERRNSVATTKKITRAMELIASSRIIKAQNTVKAAGPYSLELTRALSAVAAHTHEEHPLTSMNPDPKRSAVLVITSDRGLAGAYSSNVIRTAEELTTALQPKQEIATYLCGRKAVQYFEFRGRKVDHLWSGFSDSPSYRDAKDIADHLIEDFLRPTEEGGVDEIHMVYTEFESMLTQTPKVIRLLPLAVVDPQDTPEGQLAEGDPGVGANAEEIFHEYRFEPNPVSVLDELLPLYVANRVHYALLQSAASELASRQRAMKAATDNAEQLIQTLTRQANQARQAAITQEITEIVGGAAALAESAPQE", "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": "MARIAGVNIPDNKHTVISLTYIYGVGRTTAQKICAATGVNPAAKIKDLTDEQIEQLRGEVAKVNTEGDLRREVNMKIKRLMDLGCYRGLRHRKGLPVRGQRTKTNARTRKGPRKPIRK", "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": "MAVRPVLAVGSYLPHAPWPWGVIDQAARVLLPASTTVRAAVSLPNASAQLVRASGVLPADGTRRAVLYLHGGAFLTCGANSHGRLVELLSKFADSPVLVVDYRLIPKHSIGMALDDCHDGYRWLRLLGYEPEQIVLAGDSAGGYLALALAQRLQEVGEEPAALVAISPLLQLAKEHKQAHPNIKTDAMFPARAFDALDALVASAAARNQVDGEPEELYEPLEHITPGLPRTLIHVSGSEVLLHDAQLAAAKLAAAGVPAEVRVWPGQVHDFQVAASMLPEAIRSLRQIGEYIREATG", "text": "FUNCTION: Esterase that shows preference for short chain fatty acids (PubMed:26398213, PubMed:28164792, PubMed:28327423). Contributes to the growth of M.tuberculosis during the nutritive stress (PubMed:28164792). Elicits strong humoral response in both extrapulmonary and relapsed cases of tuberculosis patients (PubMed:28327423). SUBCELLULAR LOCATION: Secreted Note=Extracellular. SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family."}
{"protein": "MKINTKSKKVNKAWFNDHIHDTYVKLAHKEGYRSRAAYKIKEIDETCGLIRPGQVVVDLGAVPGAWSQYVRRRFAPREAGVGGAAAGELNGRIIALDLLPFEPLEGVAFLQGDFCEEAVLAQLVGLLDGRAVDVVLSDMAPNLSGVEVTDAARIANLVELALEFAQSHLKPQGALVCKVFHGSGYSQLVDQFKRTFRVVKAVKPKASRDRSAETFLVGIGLKSTGMPNADAV", "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": "MDLKKLEGIFEGMLFASGDKVSIEKLSSITGIDKKTVKLVINNMIVKYNNDPSRGITIREINNGYQLCSKPEYYDYIKQLFEPKQRSGLSQAALETLAIIAYNRPITKAKIEQIRGVNSDSAITKLLEKNLIREAGRLDAPGKPVLYETTDEFFRSFGFKSDADLPIFELNDIHETVEINQNSEQEKADTELEKQEKA", "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": "MAKKIEAYIKLQVAAGAANPSPPVGPALGQKGVNIMEFCKAFNARTEKFEKGMPIPVVITVYNDRSFTFETKTPPASFLLLKAVGLKSGSGRPNTQKVGTIKRSAVQEIAETKAADMTGADIEAMTRSIEGTARSMGLVVED", "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": "MKTKFIFVTGGVVSSIGKGLAAASLGALLEARGLRVTHQKLDPYINVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERYTSARLSKKSNFTTGQVYFSVIEKERRGDYLGGTVQVIPHITDEIKSKILDNAKGSDIAIIEIGGTVGDIESLPFLEAIRQFKADRGAGNVLYLHVTLVPFIKTADELKTKPTQHSVKELREIGIQPDILLCRCEQDLPREMKAKIALFCNVEEKAVITSMDAEHIYAVPLALHKEGLDEQVVEKLNIWAKAPDLTPWQQVVDKLMHPGHGKVRIAIVGKYVNLTESYKSLAEALTHGGIANDCRVHLSYLDSEKIEQEGIDGLLDGVDGILVPGGFGERGTEGKIKAIEYARTRKIPFFGICLGMQMAVVEYARNVCHLDDAFSSEFKQDCANPIIHLMEEQKGVSRKGGTMRLGAYPCTLAKGSFAQKAYGTLDISERHRHRYEFNNDYRDLLVSNGLILSGIYKEGDLVEIVEIPDHPWFVGCQFHPEFKSKPLNPHPLFRAFIAAALHNIKA", "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": "MGRSNEQDLLSTEIVNRGIEPSGPNAGSPTFSVRVRRRLPDFLQSVNLKYVKLGYHYLINHAVYLATIPVLVLVFSAEVGSLSREEIWKKLWDYDLATVIGFFGVFVLTACVYFMSRPRSVYLIDFACYKPSDEHKVTKEEFIELARKSGKFDEETLGFKKRILQASGIGDETYVPRSISSSENITTMKEGREEASTVIFGALDELFEKTRVKPKDVGVLVVNCSIFNPTPSLSAMVINHYKMRGNILSYNLGGMGCSAGIIAIDLARDMLQSNPNSYAVVVSTEMVGYNWYVGSDKSMVIPNCFFRMGCSAVMLSNRRRDFRHAKYRLEHIVRTHKAADDRSFRSVYQEEDEQGFKGLKISRDLMEVGGEALKTNITTLGPLVLPFSEQLLFFAALLRRTFSPAAKTSTTTSFSTSATAKTNGIKSSSSDLSKPYIPDYKLAFEHFCFHAASKVVLEELQKNLGLSEENMEASRMTLHRFGNTSSSGIWYELAYMEAKESVRRGDRVWQIAFGSGFKCNSVVWKAMRKVKKPTRNNPWVDCINRYPVPL", "text": "FUNCTION: Contributes to cuticular wax and suberin biosynthesis. Prevents the postgenital fusion of epiderm cells in organs in contact, as well as ectopic pollen hydration and germination. Required during ovules formation. May regulate an epidermis-specific developmental program during gynoecial ontogeny. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
{"protein": "MGWITEDLIRRNAEHNDCVIFSLEELSLHQQEIERLEHIDKWCRDLKILYLQNNLIGKIENVSKLKKLEYLNLALNNIEKIENLEGCEELAKLDLTVNFIGELSSIKTLKHNIHLKELFLMGNPCAFFDHYREFVVATLPQLKWLDGKGIEPSERIKALQEYSIIEPQIREQEKDHCLKRAKLKEEAQRKHQEEDKNEDKRSNAGFDGRWYTDINATLSSLESKDHLQAPDTEEHNTKKLDNSEDDLEFWNKPCLFTPESRLETLRHMEKQRKNQEKLSERKKKVKPPRTLITEDGKALNVNEPKIDFSLKDNEKQIILDLAVYRYMDTSLINVDVQPTYVRVMIKGKPFQLVLPAEVKPDSSSAKRSQTTGHLVICMPKVGEVITGGQRAFTSVKTTSDRSREHINTRSKHMEKLEVDPSKHSFPDVTNIVQGKKHTPRRRPEPKIIPSEEDPTFEDNPEVPPLI", "text": "FUNCTION: May play a role in dynein arm assembly, hence essential for proper axoneme building for cilia motility. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium. SIMILARITY: Belongs to the tilB family."}
{"protein": "MVWEVKTNQRPHAVQRLLLVMDERATGVSDSLELLQCNENVPSSPGYNSCDEHMELDDLPELQAVQSDPTQSAIYQLSSDVSHQEYPRPSWSQNTSDIPENTHREDEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSAKSGPAFPHDHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTVWHCFLKGTRLCFHKESKKEWQDVEDFARAASCDEEEIQMGTHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEIHIGDVCLPPGHPDAINFDDSGVFDTFKSYDFTPMDSSAVYVLSSMARQRRASLSCGGPGTGQEFAGSEFSKSCGSPGSSQLSSSSLYTKAVKSHSSGTVSATSPNKCKRPMNAFMLFAKKYRVEYTQMYPGKDNRAISVILGDRWKKMKNEERRMYTLEAKALAEEQKRLNPDCWKRKRTNSGSQQH", "text": "FUNCTION: Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'- TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4 (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAMKAVCVLKGDSPVQGIINFEQKESNGPVKVYGRITGLTEGLHGFHVHQFGDNTQGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVAKVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MGRADKVVLAYSGGVDTSVCIPYLKNEWGVKEVITLAADLGQGDELGPIQAKALRCGAVESLVTNAQEEFVTEYAFRAIKANALYENRYPLSTALARPLIAKLLVEAAEKYGADAVAHGCTAKGNDQVRFDLGILALNPNLKVLAPAREWNMSREETIAYGERCGVESPVKKSSPFSIDRNLLGRSIEAGPLEDPMTEPPEEIYLMTKAIADTPDTPEYVDIGFEKGIPVSLNGQTLDPVSLISQLNEKVGNHGVGRLDMIENRVVGIKSREIYEAPALLVLIDAHRDLESLTLTADVTQYKHGVGDTYSQLIYRGLWYSPLKTALDALIDQTQERVTGMVRVKLFKGNAVIVGRQSENSIYSANLSTYGSDDAFDHKAAEGFIYIWGLPTRVWAQKTK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
{"protein": "MAKKTRRVVKRKKKIAVDHGVVHIKSSYNNTIITLTDPDGKVITWGSGGTAGFQGTRKGTPYAAQLAADQVAKEAVKLGIKKVDILVKGPGSGREAAIRTFQAAGLEIGTIKDVTPIPFNGCRPKKKRV", "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": "MTKEQILAEHIIDAVGGIDNMDNIINCMTRVRIKVLDEDKIDYEQLKSIKGVMGVVKDDRVQVVVGPGTVNKVASHMSELSGAPLGETIKHKSKDYRANAEAQAQANKSEFQSKQKRGKFNKLLKTIANIFIPLIPAFIGAGLIGGIAAVLSNLLAAGQISGEWVTQLVTVFNVIKDGMLAYLAIFTGINAAKEFGATPGLGGVIGGTTLLTGLTDKNMITNIFTGEPLQPGQGGIIGVIFAVWLLSIIEKRLHKIVPNSIDIIVTPTITLFIIGLLTIFIFMPLAGFVSDGLVTVINGIIDIGGVFSGFIIGAFFLPLVMLGLHHMFTPIHIEMINQTGATYLLPIAAMAGAGQVGAALALWVRCRKNTTLRDTLKGALPVGFLGIGEPLIYGVTLPLGKPFITACIGGGIGGAVIGGIGHIGATAIGPSGISLLPLISDHMYLGYIAGLLVAYAGGFIFTYFFGTTKAMRESDTLGD", "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 the uptake and phosphorylation of MurNAc-GlcNAc, the principle peptidoglycan turnover product of S.aureus, yielding cytoplasmic MurNAc 6P-GlcNAc. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTNLQDQTQQIVPFIRSLLMPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTLQSNGNLKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQPGGVTITLFSANIDAITSLSVGGELVFQTSVQGLVLGATIYFIGFDGTTVITRAVAADNGLTAGTDNLMPFNLVIPTNEITQPITSIKLEVVTSKSGGQAGDQMSWSASGSLAVTIHGGNYPGALRPVTLVAYERVATGSVVTVAGVSNFELIPNPELAKNLVTEYGRFDPGAMNYTKLILSERDRLGIKTVWPTREYTDFREYFMEVADLNSPLKIAGAFGFKDIIRAIRRIAVPVVSTLFPPAAPLAHAIGEGVDYLLGDEAQAASGTARAASGKARAASGRIRQLTLAADKGYEVVANLFQVPQNPVVDGILASPGVLRGAHNLDCVLREGATLFPVVITTVEDAMTPKALNSKIFAVIEGVREDLQPPSQRGSFIRTLSGHRVYGYAPDGVLPLETGRDYTVVPIDDVWDDSIMLSKDPIPPIVGNSGNLAIAYMDVFRPKVPIHVAMTGALNAFGEIEKVSFRSTKLATAHRLGLKLAGPGAFDVNTGPNWATFIKRFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAANVDPLFQSALSVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQRAKDTRISKKMETMGIYFATPEWVALNGHRGPSPAQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQILKAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMELKHRNPRRAPPKPKPKPNAPTQRPPGRLGRWIRTVSDEDLE", "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": "MQNQKHSHILTAITIVLLFAMAAKINAIDVHDAMCYRSECTSVCDQICLSHGYTNGWYCGTFRLHTGCCCLKKKELNQIISPSKN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MIDQYKHQQLQIGLVSPQQIKAWANKNLPNGEVVGEVTRPSTFHYKTDKPEKDGLFCERIFGPIKSGICACGNSRPSGAENEDERFCQKCGVEFVDSRIRRYQMGYIKLACPVTHVWYLKGLPSYIANLLDKPLKKLEGLVYGDFSFARPSTKKPTFLRLRGLFEEEISSCNHSISPFFSTPGFATFRNREIATGAGAIREQLADLDLRIIIENSLVEWKELEDEGYSGDEWEDRKRRIRKVFLIRRMQLAKHFIQTNVEPEWMVLCLLPVLPPELRPIVYRSGDKVVTSDINELYKRVIRRNNNLAYLLKRSELAPADLVMCQEKLVQEAVDTLLDSGSRGQPIRDGHNKVYKSLSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHQCGLPLEIAIKLFQLFVIRDLITKRATSNVRIAKRKIWEKEPIVWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPTLVEGRTISLHPLVCKGFNADFDGDQMAVHLPLSLEAQAEARLLMFSHMNLLSPAIGDPICVPTQDMLIGLYVLTIGNHRGIYANRYNSCENYPNQKVNYNNNNSKYTKDKEPHFSSSYDAMGAYRQKLISLDSPLWLRWKLDQRVIGSREVPIEVQYESLGTYHEIYAHYLIVGNRKKEIRSIYIRTTLGHISFYREIEEAIQGFSQAYSYTI", "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": "MSWQQRVDDALTARRATDTLRRRYVVSQGAGRWLVANGRQYLNFSSNDYLGLSQHPQIIRAWQQAATRFGVGSGGSGHISGYSVAHRALEEELAQWLGYPRALLFISGFAANQAVITALMKKNDRIVADRLSHASLLEAANLSPAQLRRFIHNDTQHLSRLLQSPCVGQQLVVTEGVYSMDGDSAPLAEIQHIARRHHAWLLVDDAHGIGVTGDEGRGTCCQRGVKPELLVVTFGKGFGVSGAAVLCSESVADYLLQFARHLVYSTSMPPAQAQALSASLAVIRSDEGRERREKLAALVQRFRAGVNASRFTLLNAHSAIQPLIVGDNSRALRLAEALRQQGCWATAIRPPTVPVGTARLRLTLTQAHEACDIDRLLEVLHGAGE", "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": "MNRIERILEGFDPVSNGLDEDFVLTKLTGMKGCGCKVPRNVLLQLLQTFKTDLVINNDEVDIGLDSCVIPLRHPGLRLVQTTDFFYPLIDDPYIMGRVTCANVLSDLYAMGVSECDNMLMLLAVAIDLNEKQRDIVVPLFIQGFKDAADEAGTKIRGGQTVRCPWLLLGGVATSVAHESEIIKVDQAVPGDVLILTKPIGGQVAVNSYEWIKKKNGKIEELNLEIPKIEKAFKQVCEQMSRLNRNAAKLLHKYDAHSSTDVTGFGLLGHAENLARVQKQPMEFIIEKLPIIEYMDEIADKMIAKGGEGFKLYQGTSAETSGGLLIAMSEENAKKYIAELSSLDNAPAWIIGKVTAKTTDSSIARILPDAVRISVPSHI", "text": "FUNCTION: Synthesizes selenophosphate from selenide and ATP. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily."}
{"protein": "MFDGGVPEQIHRFIASPPPPPPLPPHQPAAERSLPFPVSFSSFNTNHQPQHMLSLDSRKIIHHHHHHHHHDIKDGGATTGEWIGQTDHDDSDNHHQHHHHHPWCSDEVLALLRFRSTVENWFPEFTWEHTSRKLAEVGFKRSPQECKEKFEEEERRYFNSNNNNNNNTNDHQHIGNYNNKGNNYRIFSEVEEFYHHGHDNEHVSSEVGDNQNKRTNLVEGKGNVGETVQDLMAEDKLRDQDQGQVEEASMENQRNSIEVGKVGNVEDDAKSSSSSSLMMIMKEKKRKKRKKEKERFGVLKGFCEGLVRNMIAQQEEMHKKLLEDMVKKEEEKIAREEAWKKQEIERVNKEVEIRAQEQAMASDRNTNIIKFISKFTDHDLDVVQNPTSPSQDSSSLALRKTQGRRKFQTSSSLLPQTLTPHNLLTIDKSLEPFSTKTLKPKNQNPKPPKSDDKSDLGKRWPKDEVLALINIRRSISNMNDDDHKDENSLSTSSKAVPLWERISKKMLEIGYKRSAKRCKEKWENINKYFRKTKDVNKKRPLDSRTCPYFHQLTALYSQPPTGTTATTATTATSARDLDTRPEENRVGSQDPDISVPMHVDGDGAGDKSNVQFSGFDLEF", "text": "FUNCTION: Probable transcription factor that binds specific DNA sequence. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRKRISAIIMTLFMVLVSCNNGGPKLKSDEVAKSDGTVLALAKISKKIKDASDFATSVKEVHTLVKSIDELAKAIGKKIHNDGSLTTEDGKNGSLLAGVHSVISAVKTKLGSLEQKAIGEFAGMKVQVVAIKTASIDLLNKFKDKNAELGKNEVSNDDAKAAILVSNTTKDKGASELEALNTAIDGLLKAANGAVEAAITELTVPVKVEKPSQNN", "text": "FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable small protein (Vsp) family."}
{"protein": "MSSHSQEPVGEENFDDSEYDRPSKSQVKREMHALLDLGKELVELSPERLRQLPLEERLYEAIREAQRTTGREGRRRQIHFVGKLMRSAPAEAIRAQLDTWRNGSREETAAMHRLEALRERLLKDDDALTAVLQRNPDADIQHLRALIRAARKEAAANAALSQGQEPQRKQYRALFQALKNLSA", "text": "SIMILARITY: Belongs to the UPF0307 family."}
{"protein": "MSHTTITNFLAGVIARPQGGNITSDETFRRYRTIVRTSATIGGNEDSRTTSIFHEIGRAVNTKGKALAVAGMEAPLVEASYPTNAVLVEDFIGLAKKYTNFSATFEYSSLAGVVERLARGLAACSVFEDVTSTDLRGNNPLAVHALATYDGPVNSLTSAVFIPRLVNNALTGDVFAVLCNCVAGEGGTVVTDTIELDANTRQPIVPEVGPLGVPGAIVDALRLLGSNMIASDQGPLFALALTRGIHRVLSVVGHTDEGGIVRDLLRCGGFGLPFGGIHYGLEEYSGLPALQFNSAAATAAYVDGIALVTAAVVAHADPGERYNGEWFPTFFDGTTHADTMRRSGDSTEGTAAMADRNRAQLLARQQLFWRPYITALGACFSTAGDISVAERFQCAASHSLGADPRHLRLPSVAPYFWIEPTGLIPHDFLGSVAEEEGFASYCWRDTTRTRPAWDSIVLSGARDTTFSAYHIRMKGARTAWFLAHWLGHPENGLGATRVRQLDPNAVLHPGPCEGNEQVRDRVEADLPLTDYLWRRGQSPFPAAGELLNLTSEWGILFRHVTFTDDGDLNPEHLPAAHEMADTTVTMTVGRPIGIAPGRSNAGDNQARRARTRASVELSAASRRARVFGRPDVGEMPTLTSAPAPIPASPAYDGNRGGEAGGVTGRGNNRSAAPGHASWSERQADGVPVNVTPHHNALRAPPFPRQQGALGGGGNVPLPPAPGAAPPPPPGPPNGPPAGPPPSDDGSSNPAAPVPTAIHAPPAAAQADRAEGQ", "text": "FUNCTION: Binds and removes 5' cap structures from cellular mRNA. FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains 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 the virion and are extruded into the cytoplasm (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the totivirus major capsid protein family."}
{"protein": "MKLFVGLGNPGARYAGNRHNIGYMAVEAIAADHGFGPWRARFQGLTSEGRLGSEQVLLLKPETFMNLSGQSVGEAMRFYKLTPADVIVFHDELDLAPGKLRLKQGGGHAGHNGLRSIHAHVGEAYGRVRLGIGHPGHKDAVAPYVLSDFAKADQDWLADLLRGIADGAEALARGDGAKFQNAVALRMQPPKPEKPKPAAKAPEAQAPEAAPDERSALQKLADRFR", "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": "MQVTETLSEGLKHEFQVSVPAADLDAKADAKLVDLKDKVRINGFRPGKVPVAHLKKIYGKSVMAETIDQTIRDTNTQIFTERGFRLATEPKVTMPTEEAEVEKILSGQSDLTYTVAVEVVPAITLADFKTFSVEKPVADITDADVDEAIKRLADANRSYAAKAEGAKAESGDRVKVNFKGTIDGVAFDGGTGEGIDVVIGSNTFIPGFEDQLIGIGVGETRTLKVAFPKNYLNNDLAGKDAEFETTATAIETPEEKVVDDEFAKTLGLESLDKLKQLMRDRLAGEFNQATRQRVKRALLDRLDETHKFDAPPSLIDEEFNLMWNSVKAEMDSSGKTFADENTTEEKAKEEYRTIADRRVRLGLVLSEIGEKNKITVTDDEVSRAVIERARSMPGREKEVWDFYRSNPQALAQLRAPIYEDKVVDFILELANVTEKKVSKDELFKDDENDKAA", "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": "MKAIILAGGQSERFGAPKAFAEIDGKMFYEQIITVLDSMNMFNEIIISSNETLASEFKGARVIVDDSEHKNKGPLSGIYSVMKQDFESELFFVISVDTPLITAKAISQLYQFMVEHVIEDQLDIAGFKEGNHPIPTIAFYSPNCLPIIARALESDDYSMRHVYQQTASDWIDVSSVDDDTEWYKNINYPQDLESIKK", "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": "MSSQFLLAFFLVLLVLGYEVQGAQGLQQDDPGSPALFGKVQESISSYWDTAKAAAQELYQKTYLTSVDEKLRDMYSKSSAAMSTYAGIFTDQLFTLLKGE", "text": "FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C2 family."}
{"protein": "MTGPSVHDRALGAFLGLAVGDALGATVEFMTKGEIAQQYGIHRKMTGGGWLRLKPGQITDDTEMSLALGRSLAAKGTLDVADICEEFALWLKSRPVDVGNTCRRGIRRYMHEGTTTAPYSEGDAGNGAAMRCLPAALATLGHPADLEPWVLAQARITHNHPLSDAACLTLGRMVHHLIGGRGMKACREEANRLVHQHRDFHFEPYKGQSSAYIVDTMQTVLHYYFVTDTFKSCLIQTVNQGGDADTTGALAGMLAGATYGVDDIPSGWLSKLDMKVEREIRRQVDALLALAGLD", "text": "FUNCTION: Involved in the regulation of nitrogen fixation activity by the reversible ADP-ribosylation of one subunit of the homodimeric dinitrogenase reductase component of the nitrogenase enzyme complex. The ADP-ribosyltransferase (DraT) transfers the ADP-ribose group from NAD to dinitrogenase reductase. The ADP-ribose group is removed through the action of the ADP-ribosylglycohydrolase (DraG, this entry). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family."}
{"protein": "MGGEALTLPKDLLDFSGYGPKELQALLDLAERLKRERYRGEDLKGKVLALLFEKPSLRTRTTLEVAMVHLGGHAVYLDQKQVGIGEREPVRDVAKNLERFVEGIAARVFRHETVEALARHAKVPVVNALSDRAHPLQALADLLTLKEVFGGLAGLEVAWVGDGNNVLNSLLEVAPLAGLKVRVATPKGYEPDPGLLKRANAFFTHDPKEAALGAHALYTDVWTSMGQEAERAKRLRDFQGFQVNGELLKLLRPEGVFLHCLPAHYGEETTEEAVHGPRSRVFDQAENRLHTAKAVLLTLLK", "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": "MSMHDPIADMLTRIRNGQQAKHQQVTLVSSKLKEEIARVLKEEGYIQDFFIETLPNGLKSITLKLKYYHGRPVIEFIKRISRPGLRVYKSYKDLHSIPGFGVAILSTSKGIMTHVSAKVKGVGGEVICEVA", "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": "MSEQKRTPIFTEYASHGAKTIDFGGWDLPVQFSSIKHEHEVTRTKAGLFDVSHMGEISVKGPKSESFLQYVLTNDISKLEPGKAQYTIMCYEDGGTVDDLIVYKLDDEDYLLVVNAANTEKDANWIKQKNTYSNDEIVIEDVSNQYVQLAIQGPKAVEILQKCTDENVQEIKFFRFKNNVALKGIEAKALISRTGYTGEDGFEIYIDASSGVALWKLLLEKGEANGLEPIGLGARDTLRFEANLALYGQELSKDISPIEAGLGFAVKVNKGPDFIGKEVLKNQVENGTDRKLVGIEMIDKGIPRHEYEVLKDNKEIGFITSGTQSPTLNKNVGLALINISYTEIGTEVDVKVRKRILKAKIVPTPFYKRGR", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. SIMILARITY: Belongs to the GcvT family."}
{"protein": "MSENNNDKITVKKTLTLKRSVLETSTVKQNFSHGRTKAVVVETKRRKITRTDEKAETSQPITKPHVAPQRSKPRFEEAKPSESSMAKSNLSSAEMEARLRALEEAHIQERITREKVEEQARRIKEREESLRQAVQETEIHQEEQKEEKNPPVQTSPLSSAHSSIEPIDIAITPKNITVTEKRKADEIKNDDRHSRRANPAKSEVRTPKVVKGANERRRGKLTLNSALDEEGSVRGRSMAAMRRRQEKFKRAQNQEPKEKISREVVIPETITIQELAQRMAERSVDVIKFLMKQEQMMKPGDVIDADVAELIAVEFGHTVKRVLESDVEEGIFNIADNPQKMQPRPPVVTIMGHVDHGKTSLLDAIRKANVVSGEAGGITQHIGAYQVEQNGQKITFIDTPGHAAFTAMRARGARVTDIAVLVVAADDSVMPQTVESINHAKAAGVPIIVAINKIDKPAADAQKVRTELLQHEVFVETMGGETLEVEVSAKTGQNLVKLLEAILLQAELLDLKADPKRTAEGVVIEAKLDRGRGSVATVLVQKGTLHPSDIIVAGNEWGRVRALIDDHGRHVKEAVPSTPIEILGMQGTPQAGDRFAVVTHEAKAREIAEYRQRLARDKAVARQTGSRSSLEQMMTKLQTTGIKEFPLIVKGDVQGSIEAIASALEKLGNEEVRARIVHSGAGGITESDISLAEASNSAVIGFNVRANKQACALAKTQGIEIRYYNIIYDLVDDIKAAMSGLLSPEQRETFLGNAEILEVFNITKIGKVAGCRVIEGKIERGAGVRLIRDNIVIHEGKLKTLKRFKDEVNEVQSGQECGIAFENYEDIRAGDTIEIFRIEHINRTL", "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": "MASATAAAAPGEAEETTRLRKPRFSFEENQILIREVRAHYPQLYGAQSRRVSVAERRRVWDSIATKINGITSWKRTGQEVQKRWNDFKRRTKEKLARVPHSTQGAGPAAEDAFSAEEETIFAILGPGVAGPGAGSGAEESRAAASSQPQASTASTQRYVLSEDRRQDRRADTPAQSKGGSSSPESWARPSCNPQEAKERESTSPAAMQPVQLPRLALSPPLPAPPPPPTALAQVAPSSPSPTPPRPTSAPEQSLDFLRAQQETANAIRELAGTLRQGLAKLSEALSALLPLLPGTPADPLPPPPPPPPPPPPKPVLPPSAPKVELAPEPVSVVAAVVDGAVVAARGVIISPRSEEGVPKPLPPAPPLPLHDSPPHKRRKGFPTRKRRGRWKSP", "text": "FUNCTION: Transcriptional repressor; DNA-binding protein that specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization with PFN1 reduces its DNA-binding capacity. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "LHMIHLHWYQYPPMNPIMYPLLLVFMLITGILCLAGNFVTIWVFMNTKSLRTPANLLVVNLAMSDFLMMFTMFPPMMITCYYHTWTLGATFCQVYAFLGNLCGCASIWTMVFITFDRYNVIVKGVAGEPLSTKKATLWILTIWILSTTWCVAPFFGWNRYVPEGNLTGCGTDYLSQDILSRSYLYIYSTWVYFLPLAITIYCYVVIIKAVAAHEKGMRDQAKKMGIKSLRNEEAQKTSAECRLAKIAMTTVALWFIAWTPYLLINWVGMFARSYLSPVYTIWGYVFAKANAVYNPIVYAIS", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Can use both retinal and 3-dehydroretinal as visual pigment. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Signaling via GNAQ probably mediates the activation of phospholipase C. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Note=Detected on the rhabdomere membrane in the photoreceptor outer segment. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MTVTTFSELELDESLLEALQDKGFTRPTAIQAAAIPPALDGRDVLGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVSDHARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIEHIAGETRWRKQTLLFSATLEGDAIQDFAERLLEDPVEVSANPSTRERKKIHQWYYRADDLEHKTALLVHLLKQPEATRSIVFVRKRERVHELANWLREAGINNCYLEGEMVQGKRNEAIKRLTEGRVNVLVATDVAARGIDIPDVSHVFNFDMPRSGDTYLHRIGRTARAGRKGTAISLVEAHDHLLLGKVGRYIEEPIKARVIDELRPKTRAPSEKQTGKPSKKVLAKRAEKKKAKEKEKPRVKKRHRDTKNIGKRRKPSGTGVPPQTTEE", "text": "FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. Acts before DeaD. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. SrmB subfamily."}
{"protein": "MAKGGFPGGFGGGNMNNLMKQAQKLQKQMEDMQKDLETKEFETSVGGGAVSVTVTGKKEVKSINIKPEVVDPDDVEMLEDLVLTAVNEALRKAEEETASKMGKLTGGMPGGLF", "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": "MPDSLRIVFAGTPEFAAEHLKALLASQHEVIAVYTQPDRPAGRGQKLMPSPVKQLAVEHGIPVHQPASLRNEEAQAELAALKPDLMVVVAYGLILPQVVLDTPRLGCINSHASLLPRWRGAAPIQRAVQAGDLESGVTVMQMEAGLDTGPMLLKVSTPISAEDTGGSLHDRLARLGPQAVLQAIDGLAAGTLIGELQDDAQANYAHKLNKDEARLDFSRPAVELERLIRAFHPWPICHTTLNGDALKVHAAELGEGSGAPGTILAADKNGLTVACGEGALRLTRLQLPGGKPLAFSDLYNSRREQFAPGLVLGQ", "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": "MADFTRIPLWLIGTIVGILVIGLIGIYFYGSYSGLGSSL", "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": "MVKEPNGVTRTMRRIRRIHFVGIGGAGMCGIAEVLLNLGYEVSGSDLKASAVTERLEKFGAQIFIGHQAENADGADVLVVSSAINRANPEVASALERRIPVVPRAEMLAELMRYRHGIAVAGTHGKTTTTSLIASVFAAGGLDPTFVIGGRLNAAGTNAQLGASRYLVAEADESDASFLHLQPMVAVVTNIDADHMATYGGDFNKLKKTFVEFLHNLPFYGLAVMCVDDPVVREILPQIARPTVTYGLSEDADVRAINIRQEGMRTWFTVLRPEREPLDVSVNMPGLHNVLNSLATIVIATDEGISDEAIVQGLSGFQGVGRRFQVYGELQVEGGSVMLVDDYGHHPREVAAVIKAIRGGWPERRLVMVYQPHRYTRTRDLYEDFVQVLGEANVLLLMEVYPAGEEPIPGADSRQLCHSIRQRGQLDPIYFERDADLAPLVKPLLRAGDILLCQGAGDVGGLAPQLIRNPLFAGKGGKGA", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family."}
{"protein": "MATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE", "text": "FUNCTION: Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (PubMed:22170058, PubMed:21395585). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). May be involved in keratinocyte differentiation (PubMed:8092987). SUBCELLULAR LOCATION: Cytoplasm Nucleus Synapse Postsynaptic density Secreted Note=Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (PubMed:24692551). Secreted by astrocytes, but not by neurons (By similarity). SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MSLYDYWVQFVSYIIGANAPEFLYVISFVLFIVLFFGMFFKLIQKMWSF", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein."}
{"protein": "MAATQEEIIAGLAEIIEEVTGIEPSEVTPEKSFVDDLDIDSLSMVEIAVQTEDKYGVKIPDEDLAGLRTVGDVVAYIQKLEEENPEAAAALREKFAADQ", "text": "FUNCTION: Acyl carrier protein involved in meromycolate extension. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acyl carrier protein (ACP) family."}
{"protein": "MPALMVVGCTSHAGKSLITAAICRLLRRQGWRVAPFKGQNMALNAYVTASGGEIGYAQAFQAWAAGVEPTIEMNPILLKPQGDMTSQVVLKGRAVGRTLAERYYQDYFEVGWEAICEALEQLQADYDWIVCEGAGSPAEINLKHRDLTNLRVAKHLQAPTLLLVDIDRGGSFAHLIGTLELLDPDERSLIRGFVFNKFRGRRELLQSGLDWLEERTGIPVLGVIPWIDRAFPSEDSLDLMERRRRKTQAEVTIAVIRLPRIANFTDFDPLESEPSVQVRYVGLQDELGYPDAVILPGSKTTISDLLDLQRSGLAQAIRDYAAAGGTVLGICGGFQMMGQHILDLEGTEGIEGQFEGLHLFPTQTWFTAEKTLRQRQTTARSPQAGLPITGYEIHQGQTRLDSDSEEFLPIFDDPKLGLCDRNGNLWGTYLHGIFDNGAWRRAWLNSLRHRRGLKALPTSIGHYQAQRDDLIDALADAVEPYLNLSPLLTAL", "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": "MPRKGSVAKRDVLPDPVYNSKLVTRLINHLMIDGKRGKASTILYDAFDMIKKQTGNEPLDVFEEAMKNVMPVLEVKARRIGGSNYQVPIEVRPDRRTTLGLRWIVQYSRQRGEHTMDERLAKEIMDAANNTGAAVKKREDTHKMADANRAFAHYRW", "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": "MNVSFITQYTSSIDADAAILLQVEKFEKTFGLELVDPNRIIKKGYLIENFQGSFGSQIKFLYLEGSPFAFVKVVGLGKEQSINDETWLKAGGLCVSEIKNYPKKVVVFADALGIDVSTTQIMNFVLGALLKQYSFECYYTDKKKSKQKNKNILELVIITKNAENCQKELKQVQAICEGVNLTKELVNEPANILGTEEFVEKIKKLEKLNVKVQVLDKEKLKELGMNALLSVAQGSSRPPYLVIMQWNGSDNKEEEPLAFVGKGVVFDSGGISIKHSSGMEDMKADMGGAGTVVGLMHTLATRKAKINVTGVVGLVENMPSCHAQRPGDIVTSMSGQTIEVINTDAEGRMVLADVLWYCKTKIQPKLIVDLATLTGAIRIALGEQHAGLFSNNEALAKQIIKSGEATSEKVWQLPLGLEYDKLIDSKFADMKNSSGGSAGSITAAQFLKRFVDEKTPWAHIDIAAVCMGNKLNEFNNSWASGFGVRLLNYLIKNYYEQK", "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": "MLSIKEATKNISQQLTTVSKTPRLDAELLLECVLKKSRADLFAYPEIQLNSSQQKTLSAYVKRRLKGEPIAYILGQKEFWSLNLKVTPDVLIPRPETEMLVEWILKNLPKDEKLRIADLGTGSGAVALAIAVERPHWTIDATDNSQAALKIAEINAKQHEIKNCNFYHGEWCQALPRRDYHAIVGNPPYIPDKDQHLQQLKHEPREALAAGSDGLSAIKIIIHEAKSYLVNGGWLLLEHGYDQAEKIMTLMQADGYREITDRRDLAGLSRMMVARRG", "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": "MPTIQQLIRKPRQPKVKRSKSQHLEQCPQKRGVCTRVYTTTPKKPNSAMRKVAKVRLTNGYEVISYIPGESHNLQEHSVVLIRGGRVKDLPGVRYHILRGVLDTQGVKDRKQRRSKYGAKRPK", "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": "MNKDLKGLYAALLVPFDENGQVNEQGLKQIAQNTIETEELDGLYVNGSSGENFLLNTEQKKQVFKVAKEAVGDKVKLIAQVGSLDLNEAIELGKYATEIGYDALSAVTPFYYPFTFEEIRDYYFDIIEATQNNMIIYAIPDLTGVNISIEQFSELFNHEKIVGVKYTAPNFFLLERIRKAFPDKLILSGFDEMLVQATISGVDGAIGSTYNVNGRRARKIFDLARQGQIQEAYQLQHDSNDIIETVLSMGIYPTLKEILRHRGIDAGLPKRPFKPFNEAHRQTLDQLIAKYDL", "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": "MSNRKYFGTDGIRGRVGNAPITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDDVEEAIEAEMEKEITCVDSAELGKASRIVDAAGRYIEFCKGTFPNELSLNGLKVVVDCANGATYHIAPNVLRELGATVIAIGCEPNGVNINEEVGATDVRALQARVLAEKADLGIALDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKLQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMVRNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLENEAVKAVTADVEATLGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTAFAHRIADAVKAV", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MTATAQQLEFLKNSIQSIPDYPKPGILFRDVTSLLEDPKAYALSIELLVERYRHAGITKVVGTEARGFLFGAPVALGLGVGFVPVRKPGKLPRKTFAEDYALEYGTDTLELHCDAIQPGDVVLVVDDLLATGGTIEATVNLIRRAGGSVKDAAFIINLFDLSGEARLKALGVESYSLVSFPGH", "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": "MSELKDCPLQFHDFKSVDHLKVCPRYTAVLARSEDDGIGIEELDTLQLELETLLSSASRRLRVLEAETQILTDWQDKKGDRRFLKLGRDHELGAPPKHGKPKKQKLEGKTGHGPGPGPGRPKSKNVQPKIQEYEFTDDPIDVPRIPKNDAPNRFWASVEPYCADITSEEVRTLEELLKPPEDEAEHYKIPPLGKHYSQRWAQEDLLEEQKDGARAAAVADKKKGLIGPLTELDTKDVDALLKKSEAQHEQPEDGCPFGALTQRLLQALVEENIISPMEDSPIPDMSGKESGADGASTSPRNQNKPFSVPHTKSLESRIKEELIAQGLLESEDRPAEDSEDEVLAELRKRQAELKALSAHNRTKKHDLLRLAKEEVSRQELRQRVRMADNEVMDAFRKIMAARQKKRTPTKKEKDQAWKTLKERESILKLLDG", "text": "FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53- dependent transcriptional activation (By similarity). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NGG1 family."}
{"protein": "MDKFNPVDMSVWQGRQDPEDGELALRWHDKVQPWPQAGRAAPGVALVGFACDEGVRRNKGRVGAAGAPLAVRKLLANSAWHLGRPVYDRGDVNCEDGDLDAAHGRLAERVARLLDEGHFPLVLGGGHEVAFGSWSGLNRHLAGRGRVGIINFDAHFDLRMKLEQASSGTPFFQIAEQCAIQGTPFTYACLGVAETANTQALFARAEALGVWHVLDEAMTPAELPALLSGLDAFIARCDHLYLTIDLDVLPAAVMPGVSAPAARGVELAVIEPLIAHIRASGKLRLADLAEYNPSLDQDNRSARVAARLVHQLIK", "text": "FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L- glutamate and formamide. SIMILARITY: Belongs to the arginase family."}
{"protein": "MKLLVEKTNEKAIIPFQAHEGDAGMDLFSVEEITLKPMERKLIHTGIKIQLPKDTEAQIRPRSGLALKHGITVLNTPGTIDEGYRGEIGIILINLGSEEFKVEEGMKIAQMVIKPTLTLKVEEVVELTETTRGENGFGSTGV", "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": "MSEHDMHLLDSAPFGRILPAMVTPMKSDGSVDFAAAQKLAKYLVADGADGLVVNGTTGESPVTHMDEKVELVRAVKEVVDVPVISGAGSNDTAHTVRMVEQTQEAGADAVLVVMPYYSRPSQDGIVGHYKAVDESAEKPIIVYDVPGRTGLKVKVGTYDRLAELEHVKAVKDATGDLAAAVEKQQRTGLAWYSGDDGLFLPFLSIGAVGIISVIAHVASNPMQQLVQAFDRGDITTARRLANQLAPLVHALNGDGYQAVMAKAALKVKGVIPSTTMRLPNIGPDATQLDKAEEGMRAAGLL", "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": "MDVNSRAKIRPLDQLVINKIAAGEIIERPENAIKELIENSLDAGSTSIDVLLKDGGLKLLQITDNGSGIQYDDLPYLCQRFSTSKIDNFNDLQHLQTFGFRGEALASISHVAKVTVVTKLSSDIHAWKAFYVDGALAPISPGMSPAPQPCAGKQGTVITAEDLFYNVRSRKSALKNGSEEFRRIMILVQKYAIHNDQVSFNCKKVGDTVASLSLSSRLSKADKIRHIYGPRVASHLRDFSLGEGQSSIVGFSANGFISNADFQDKKSNLILFINNRLVESVELRHALEETYAKYLHKGASYFVYLSLNMSPEQLDVNVHPSKRIVHFLYDQEIATSICDKLGEILERTDTERSYPLQAMIPSISNTKNAESSSQKAVRTYENYLVRTDPRERSIKSMLSDNFLQRSSNNYDNEIIEKVDSANSNKNATNDIKDLQTEEIVEEGNSIDLESIKSLQKQVINSMHVLATNILTEHKYVGLVCPTRRIAAVQHNIGLYVVDYGKLSYHLFYQICLTEFGNYGEFVLETPLSISDLFEIVNGDEDKSESEKFTRLLVSRRDMLKDYFSISVTSGGLLTAVPMLSPKYHPPFEQLPLLISSLTPKFFDWLDEKSCLNGIMKAIAKFYVPLPLSYEESDVKSIRSLESCLEDYLFPEFRRRVICPKKVFEEKCIYQITSLPRLYNVFERC", "text": "FUNCTION: This protein is involved in the repair of mismatches in DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family."}
{"protein": "MSTESMIRDVELAEGPLPKKAGGPQGSKRCLCLSLFSFLLVAGATTLFCLLHFRVIGPQEEEQSPNNLHLVNPVAQMVTLRSASRALSDKPLAHVVANPQVEGQLQWLSQRANALLANGMKLTDNQLVVPADGLYLIYSQVLFSGQGCRSYVLLTHTVSRFAVSYPNKVNLLSAIKSPCHRETPEEAEPMAWYEPIYLGGVFQLEKGDRLSTEVNQPEYLDLAESGQVYFGIIAL", "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": "MALYLSSSRLITFLSFILLLSNGFSSSSSRPSIHHRHHLDNHNYKDALSKSILFFEGQRSGKLPPNQRMTWRSNSGLSDGSALNVDLVGGYYDAGDNMKFGFPMAFTTTMLSWSLIEFGGLMKSELPNAKDAIRWATDFLLKATSHPDTIYVQVGDPNMDHACWERPEDMDTPRSVFKVDKNNPGSDIAGEIAAALAAASIVFRKCDPSYSNHLLQRAITVFTFADKYRGPYSAGLAPEVCPFYCSYSGYQDELLWGAAWLQKATNNPTYLNYIKANGQILGADEFDNMFSWDNKHVGARILLSKEFLIQKVKSLEEYKEHADSFICSVLPGASSSQYTPGGLLFKMGESNMQYVTSTSFLLLTYAKYLTSARTVAYCGGSVVTPARLRSIAKKQVDYLLGGNPLKMSYMVGYGLKYPRRIHHRGSSLPSVAVHPTRIQCHDGFSLFTSQSPNPNDLVGAVVGGPDQNDQFPDERSDYGRSEPATYINAPLVGALAYLARS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family."}
{"protein": "MSFHPQTPQSPSHFSPSSSDQSTSMSGSIVSTTTTLPTPAHSVNGSSLANDMSFTDIVMGENSPQKRKRTSDDVGDREQKKVHIEDRKLGIDDLHLDVGEKYLLCRSQHQPPRPHLSEDLFEMYGLADLAAEYARIKDGQKNALRKTYKGHIKKLGVQGHFDSVKTDEKDPERLEYLMGCPQEEWNAHFVRGKEITRGLSSDMKSKISRAVTMSRGAVPSTLWNNSVLGDIAASSMKAHLNQPPSARPTAPNTPLAYGGPAMQRVKPQTPGFQDNRPRRNIKKRGYGDSSFEGYGEGFEDDGGLETGYSTGEGDMASGLKRRKKAQPGTQSYAQARQQSSYGHHGVSGI", "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": "MDEILKTRVKDLCEKIRSGQIKSIEIVKACFKRIKETDPKVKAFLKLNEERSLKQAAQSDDKIKTGAECGSLEGVPIGIKDNIMIKGESMTSASKYLENYISPYDAAVIEKLKEAGVIFVGRTNMDEFAMGGSTETSVYQKTANPWNIDYIPGGSSGGSAAAVSSGMVPFALGSDTGGSIRQPAGFCGIVGYKPSYGLISRYGACALASSFDQIGVFSKTVKDASLLTSFIAVGDYRDPVCETGEQTNYAHGIYNPDILKTVRIGIPKQLSNYKADEEITKYFGDAVNKLKLEGAATVEIDVPAYKYVPALYEVIMCAEVSANIATFDGIRYGYRSSNGRNLNDEYAKSRAESLGYEVKKRILFGTYVLGAKNYYRCYHQAQRVRTLLINQITDAYKKCDFIFSPATLQMPVKFGEKLSEECDIFLTAANLAGLPGITVPCTFTSSGMPMGVHFMGSRFSDAKLFQIADAFERISGFDINKYPNL", "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": "MARAVGIDLGTTNSVVAVLEGGEPTVIANAEGARTTPSVVAFAKSGEVLVGEVAKRQAVTNVDRTIRSVKRHMGTDWLTKIDDKDFTPQQISAFVLQKLKRDAEAYLGEPVTDAVITVPAYFSDAQRQATKEAGEIAGLNVSRIVNEPTAAALAYGLDKGDDQTILVFDLGGGTFDVSLLEIGEGVVEVKATSGDNHLGGDDWDARIVDWMVKKFKDNNGVDLAADKIAKQRLQEAAEKAKIELSSSSETTIHLPYITHGESGPLHFEEKLTRSEFQRLTTDLLDRTKGPFQSVLKDGGVAIKDIDHVVLVGGSTRMPAVTEVVKELLGGKEPNKGVNPDEVVAVGAALQAGVLKGEVKDVLLLDVTPLSLGIETKGGVMTTLIERNTTIPTKRSEIFTTADDNQPSVEIKVAQGERQMWAQNQPLGNFELTGLPPAPRGIPKIEVTFDIDANGIVHVTAKDQASGKEQSMTISGGSALGKDEIDRMVREAEQYAEEDAKRREAVETRNQAEQLVYTTEKFLDENSDKLPDDVKTEVRADVDALKVTLEKEDASADDIRAGVTKLGESSQKMGAAMYAAAEADSAAAGGSAGATGESDDDVVDAEIVDEGGADDGAEGESK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MKQLAQRLFSLALVLALVLGISVQSAQALSLQSPLLAVAEAEIRNEADAQRIEAGGKLDLNNIGVRAFQQFPGMYPYLASKIVLGGPYDSVDDVLKLDLSDRQREVFEQYKENFTVTPPRDALNEGDDRINNGIYR", "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": "MFKVIKCNELNEKLINKKVEINAWVKKIRHHGKFIFLNIRDRYEKAQVLITEEHLLKIAEKIKLEYCIKIQGLLSKRPPNMINENMKTGSFEILAKNIEIISKCNELPFMIEDDNNASENSKLKYRYLDLRRDSLKNKIILRCQATHLIRNFLVKKKFLELETPTFVKSTPEGARDFVIPSRIHKGSFYALPQSPQLYKQLIMIAGFDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFVKKENIFKLIENMLFLIFKNCLNIKLPKKFKKITYKTAMNKYGSDKPDTRFELTLQDISRNLKNSEFNVFKETLKNKGSIKILIVKDEADKFSRAKINNLEEIAKLYKTQGLYFAKIENNKFSGGIAKFLKTEEQQLIKTYSLENNDIIFFTANKKWETACKAMGQIRIKIANDLGLIDENKFEFLWVYDFPLFEYDENTKTYTPAHHMFSLPKKRYIASLEKIPNKTIGEIYDLVLNGVELGSGSIRIHNKELQQRIFNIIGFQKEKSEDRFGFFLKALEYGAPNHGGIAIGIDRLIMLMTKSTSIKDVILFPKNSFATSPLDDSPSKISNEQLKELGINIVTDDA", "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": "MNERMVDQSMHSEETDFELSLRPTRLRQYIGQNSIKSNLEVFIKAAKLRHEPLDHVLLFGPPGLGKTTLSNIIANEMEVNIRTVSGPSLERPGDLAAILSGLQPGDVLFIDEIHRLSSVVEEVLYPAMEDFFLDIIIGKGDEARSIRIDLPPFTLVGATTRAGSLTGPLRDRFGVHLRLEYYNESDLKEIIIRTAEVLGTGIDEESAIELAKRSRGTPRVANRLLKRVRDFQQVNEDEQIYIETTKHALGLLQVDQHGLDYIDHKMMNCIIKQYNGGPVGLDTIAVTIGEERITIEDVYEPFLIQKGFLERTPRGRKATPLAYEHFAKSNEERE", "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": "MSATYTDLREKLQSLNRDSPKEVRKRKQPASDTEEEDEAGSEPEAEEEEARKVRSGIRQMRLFSPDECAAIESKIDEVVSRADKGLYQEHTVDRAPLRNKYFFGEGYTYGAQLQRRGPGQERLYPKGEVDEIPGWVHELVIRRLVERRIIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVFFLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVVILRKTRTEAPRLEMKSLSSSYQPERLQGSNRQHILKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPKQRRRSHFSSENYWRRSHDHVDTYTETGEDEGSPVRKVKMRRH", "text": "FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)-methyladenosine in single- stranded DNA (in vitro) (By similarity). Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Demethylation of m6A mRNA affects mRNA processing and export (By similarity). SUBCELLULAR LOCATION: Nucleus speckle. SIMILARITY: Belongs to the alkB family."}
{"protein": "MPKPTKGPRLGGSSSHQKALLANLATSLFEHGRIKTTEPKARALRPYAEKLITHAKKGELHNRREVMKKIRDKDVVHTLFAEIGPFFADREGGYTRIIKVEPRKGDNAPMAVIELVREKTVTSEANRARRVGASKQTAPVAAAAAPQAAVEPEATEGPDADDSSALPEAEDTTASEASRSTETDDPTQDSDADKS", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MTAAYLPSILVPLVGLIFPALGMALLFIYIERETIA", "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": "MAAATSSSPISLTAKPSSKSPLPISRFSLPFSLTPQKDSSRLHRPLAISAVLNSPVNVAPPSPEKTDKNKTFVSRYAPDEPRKGADILVEALERQGVETVFAYPGGASMEIHQALTRSSTIRNVLPRHEQGGVFAAEGYARSSGKPGICIATSGPGATNLVSGLADAMLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVDDIPRIVQEAFFLATSGRPGPVLVDVPKDIQQQLAIPNWDQPMRLPGYMSRLPQPPEVSQLGQIVRLISESKRPVLYVGGGSLNSSEELGRFVELTGIPVASTLMGLGSYPCNDELSLQMLGMHGTVYANYAVEHSDLLLAFGVRFDDRVTGKLEAFASRAKIVHIDIDSAEIGKNKTPHVSVCGDVKLALQGMNKVLENRAEELKLDFGVWRSELSEQKQKFPLSFKTFGEAIPPQYAIQILDELTEGKAIISTGVGQHQMWAAQFYKYRKPRQWLSSSGLGAMGFGLPAAIGASVANPDAIVVDIDGDGSFIMNVQELATIRVENLPVKILLLNNQHLGMVMQWEDRFYKANRAHTYLGDPARENEIFPNMLQFAGACGIPAARVTKKEELREAIQTMLDTPGPYLLDVICPHQEHVLPMIPSGGTFKDVITEGDGRTKY", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MIIYRDCISQDEMFSDIYKITEVANGLCLEVEGKMVSRKEGEIDDALIGGNASAEGPEGDGTEATVITGVDIVMNHHLQETSFTKESYKKYIKDYMKSIKARLEETKPERVKPFMTGAAEQVKHILGNFKNYQFFVGENMNPDGMVGLLDFREDGVTPYMIFFKDGLEMEKC", "text": "FUNCTION: Venom protein that causes edema, enhances vascular permeability and is likely related to the inflammatory activity of the venom. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TCTP family."}
{"protein": "MRIIGLTGGIGSGKSTVARIWQGCGAIVIDADAIARVLMEPGSTVLEEVSQVFGRDLLDAEGKLRRAELAARAFISEEKTAQLNSITHPAIRRQIRRGIECARAEGVQVLVLDHPLLFESGMSDLVDDVVVVDVPAELRVRRLVDLRGLKEEDARHRIMRQMSDEDRRMRADYVIDNSGSRDVLERLARELWQRFATQVE", "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": "MGKRILPQRMGRGTPTFRSPSHRRVGPAKYPPLKLDRTIKGKIIDLLHDPGRWVPLAKIVLEDGTTFLTPAVEGMYVGQIIEIGPDAHISNGNILPIGKIPEGTQIANIEKRPGDGGKFVRSSGTYALIVGRAGTKTQVQLPSGKIIEVPNNARATIGVIAGGGRDEKPLLKAGNAYHKWKVKAKKWPKVRGVAMNAVSHPHGGGSHQHVGKPSTVARETPPGRKVGHIAARRTGRRKG", "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": "WPPLHPLYRTDLSLEAAIEEEANRLDPLVQQANLLIDTAALSTHELAERLREFLSGHSDKELKIVVESFGFKYGIPLDADYVFDVRFLPNPHWNQGLRPLTGLDDEVANS", "text": "FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family."}
{"protein": "MKIRPLHDRVIVKRLEAERKTASGIVIPDSAGEKPDQGEVLAVGNGKILDDGKVRPMAVKVGDKVLFGKYAGQTVKVEGDELLVMREEDIMGVVEA", "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": "MEMGRLVFGLCLILIVGTFLEFSGGATAAKGVTYDGRSLIIDGQRKLLFSGSIHYPRSTPEMWPSLIKKTKEGGIDVIQTYVFWNLHEPKLGQYDFSGRNDLVKFIKEIRSQGLYVCLRIGPFIEAEWNYGGLPFWLRDVPGMVYRTDNEPFKFHMQKFTAKIVDLMKSEGLYASQGGPIILSQIENEYANVEGAFHEKGASYIKWAGQMAVGLKTGVPWIMCKSPDAPDPVINTCNGMKCGETFPGPNSPNKPKMWTEDWTSFFQVYGKEPYIRSAEDIAFHAALFVAKNGSYINYYMYHGGTNFGRTSSSYFITGYYDQAPLDEYGLLRQPKYGHLKELHAAIKSSANPLLQGKQTILSLGPMQQAYVFEDANNGCVAFLVNNDAKASQIQFRNNAYSLSPKSIGILQNCKNLIYETAKVNVKMNTRVTTPVQVFNVPDNWNLFRETIPAFPGTSLKTNALLEHTNLTKDKTDYLWYTSSFKLDSPCTNPSIYTESSGHVVHVFVNNALAGSGHGSRDIRVVKLQAPVSLINGQNNISILSGMVGLPDSGAYMERRSYGLTKVQISCGGTKPIDLSRSQWGYSVGLLGEKVRLYQWKNLNRVKWSMNKAGLIKNRPLAWYKTTFDGPNGDGPVGLHMSSMGKGEIWVNGESIGRYWVSFLTPAGQPSQSIYHIPRAFLKPSGNLLVVFEEEGGDPLGISLNTISVVGSSQAQSQFS", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
{"protein": "MLKLLLGDPNARKLKRYQPIVSDINLLEEEVSPLSDDDLRRRTAEFRQRLDNAGSLDQQRPVLDELLPEAFAVVREAGKRVLGMRHFDVQLIGGMVLHEGQIAEMKTGEGKTLVATLPSFLNALTGRGVHVVTVNDYLARRDAEWMGQVHRFLGLSVGLIQQDMTPAERRRNYGCDITYATNSELGFDYLRDNMAADINEVVQREFQYCVIDEVDSILIDEARTPLIISGQVERPQEKYQKAAEVAAALTRAAEMGKDGIDPEGDYEVDEKQRSCTLTDEGFAKAEQMIGVADLYDPQDPWAHYITNALKAKDLFTRDVNYIVRDGEAVIVDEFTGRVMPGRRWSDGQHQAIEAKEALAIQPETQTLASITYQNFFLLYPRLAGMTGTAKTEETEFEKTYKLETTIVPTNRVRARQDWVDQVYKTEEAKWRAVAKETAEVHQQGRPVLVGTTSVEKSELLSALLAEEDIPHNLLNAKPENVEREAEIVAQAGRSGAVTIATNMAGRGTDIILGGNSDYMARLKLREVLLSRLVRPEEGHRPPVPLQRSGAEGGGGFAAKAAPASGPHGHAPSEARAIGSLYPCQLTEDTDQALADLAKDLVKAWGDRALTVIELEDHIATAAEKAPTDDPAIAALRAAIARVKGEYDDVVKQEEQRVREAGGLHVIGTERHESRRVDNQLRGRAGRQGDPGSTRFFLSLGDNLLRIFGGDRVAGLMNAFRVEEDMPIESGMLTRSLEGAQKKVETYYYDIRKQVFEYDEVMNNQRKAVYSERRRVLEGRELKKQVVGYGERTMNEIVEAYVNPDLPPEEWDVTQLVSKVQEFVYLLDDLQADQLQGLSMDELKAFLQEQLRNAYDLKEGQIEDQRPGLMREAERFFILQQIDTLWREHLQSMDALRESVGLRGYGQKDPLIEYKNEGYDMFLDMMTNMRRNVIYSMFMFQPAPPAGQSAGQRTTA", "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": "MLILTRRVGETLMVGDDVTVTVLGVKGNQVRIGVNAPKEVAVHREEIYQRIQKEKDQEPSH", "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": "MARIAGINVPDHKHAVIGLTAIYGIGKTRSKAILAATGIAETTKIGELSDETLDVLRDAVGKYTVEGDLRREVTLNIKRLMDLGCYRGLRHRRSLPLRGQRTKTNARTRKGPRKPIKR", "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": "MRKIKRLNSSLAEFRREFDELLLRGNVDMDTVIPVVSGLIKEIRTQGDAALLAHVAKFDRWNPKSAMELKIDPSLMKRAYEGLEASLREALHSAYNRIHSFHSKQKPQSWLDFEENGTILGQKVTPMDRAGLYIPGGKAAYPSSLLMNAIPAIVAGVKEIVVCTPTPENEPNELLLAACHLCGIKEVYKVGGASAIAAMAYGTESLGRVDVITGPGNIYVATAKKLVFGQVNIDMVAGPSEIGILADESAKAPWVALDLLSQAEHDEMASSILVTPSVELADAVDVEVERALERLDRKEISSKSIYTRGAIIIAKDMNEAVSLMNEIAPEHLEVLVENPFGWLPEIRHAGAIFLGENTPEPIGDYIAGPNHTLPTGGTARFYSPLSTEHFMKKSSILSFSERGIRELGHHCAKLAQTEGLDAHKESVLARLV", "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": "MALEKDEKTAIIADYQMHSTDTGSPQVQVALLTERINGLIEHLKVHPHDHHSRRGLLKLVGRRRRLLAYLASRDKEAYRKLIDTLGLRR", "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": "MLDLRLIREHPDLVREALRKLNTEAPLDEILELDERRRQLVAEVEQLKAQRNAESKRIGQLPAGPEREATIAAMRALGDRIEALDRELAAIEERLQALLLEVPNLPDPDVPVGPDESGNVVVRHWGEPRPFDFPVKPHWELAEELGLIDFARGVKIAGSRFYVLRGDLARLQRALIAWMIDLHVNEHGYLEVYPPFLVRREAMIGTGNLPKFGDNLYHDEETDLWLIPTAEVPVTNLFRDEILPPGSLPIYLVAATPCFRKERVSAGRDVRGIKRVHQFEKVEMVKFVEPDRSDEELQRLVADAEDVLRRLELPYRVVQMCTGDLSFTAAKKFDLEVWAPGSQEWLEVSSCSNFRDFQARRANIRYRPSEGARPQFVHTLNGSGLALPRTLIAIMENYQQPDGTIEIPAVLRPYMGGQQRIGRQPAYWEPAQARRAREQARAGDS", "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": "MSIRDEIKKRRTFAIISHPDAGKTTITEQLLYFGGEIREAGTVKGKKTGNFAKSDWMDIEKQRGISVTSSVMQFDYAGKRVNILDTPGHEDFSEDTYRTLMAVDAAVMVVDSAKGIEAQTKKLFEVVKHRGIPVFTFMNKLDRDGREPLDLLEELEEVLGIASYPMNWPIGMGKAFEGLYDLYNERLELYKGNERFAKIEDGDTLFANNPFYEQAKEDIELLTEAGNEFSEEAILAGELTPVFFGSALTNFGVQTFLDTFLKFAPEPHGHKTVDGDEIDPLNKDFSGFVFKIQANMDPRHRDRIAFVRIVSGEFERGMSVNLTRTGKGAKLSNVTQFMAESRENVENAVAGDIIGVYDTGTYQVGDTLTVGKNKFEFEPLPTFTPELFMKVSAKNVMKQKSFHKGIEQLVQEGAIQLYTNYQTGEYMLGAVGQLQFEVFKHRMENEYNAEVVMTPMGKKTVRWIQPEDLDERMSSSRNILAKDRFDQPVFLFENDFALRWFADKYPDVTLEEKM", "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": "MGIKGLSQLIADLAPFAVKEGEIKNFFGRKVAIDASMCLYQFLIAVRAEGAQLTSVDGETTSHLMGTFYRTIRLLENGIKPVYVFDGKPPDLKSGELTKRAEKREEAQKALDKATEAGVTEDIDKFNRRLVKVTKQHSNEAKELLKLMGVPYVDAPCEAEAQCAALVKGGKVYATATEDMDALTFGSNILLRHLTFSEARKMPVQEFNYDKILQGLELTRDEFIDLCILLGCDYCDSIRGIGPKKAVELINKHRTIEKILENLDTKKYVVPENWNYQQARVLFKEPEVANPEEVELKWGEPDEEGLVKYLCGDRQFNEDRIRAGAKKILKTKSTATQGRLDSFFKVLPSTPNPKRKIEDKKTPASKKAKTTGGKPGRKPK", "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": "VLIIAVLFLTACQLTTAETYSRGRQKHRARRSTDKNSKWTRECTRSGGACNSHTQCCDHFCSTATSTCI", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
{"protein": "MTLEMSPEQIQESKIYREWGLTDEEYLKIKDEILGGRLPNFTETGMYAVMWSEHCCYKNSKPVLKKFPTTGPQVLMGPGEGAGVVDIGDDLAVVFKAESHNHPSYVEPYEGAATGSGGIIRDIFSMGARPIAILDSLRFGPIDNGKTRHIVDQVTAGIAGYGNCIGIPTVGGEVAFDESYAGNPLVNVMCVGLIEHKHIQKGQAKGVGNSIFYVGAKTGRDGIHGASFASKEFGSGSETQRSAVQVGDPFMEKLLLEACIEVIQNHGDILVGIQDMGAAGLVSSTSEMASKAGSGLRLNLDNVPQRETEMIPYEMMLSESQERMVLCVKKGHEQEIIDLFKKYDLDAVNIGEVTDDGFYTLYHKGQMVAHVPVDSLAEDAPTYYREAKVPERIQKFTDSEKYLPEITDSAVSEIFKKLLAQPTIASKKSIYETYDSRVMTNTVVAPGSDAAVLRVRGTNKALAMTTDCNARYLYLDPEKGGAIAVAEAARNIVASGGKPLAITDCLNFGNPEKPEQFWELTTAADGISRSCLALDTPVISGNVSLYNETNGSAILPTPMIGMVGLIEDVKNITTQEFKKAGDLIVLVGQIFDDFSGSELQKMLTGEISGKIDFDLETEKVNQDFVLKAITDGLINSAHDLSEGGLAIALAESAFANGLGIDVEVDLSNAQLFSETQGRFVLSISPENQAAFEKLLTESSASSEVIGKVTDNGILKINELSISTDEAVSIYEGALPCLMK", "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": "MPIKIVTDSSITIEPGIARELDITIVPLSVTIDGTMYSDDDLKFEDFMVKMAASKNLPKTSQPPVGVFAEVYEKIAAEDDEIISIHLTEALSGTVEAARQGGMLSGRNVTVIDSDFTDQAQKFQVVEAARLAKAGASKEEILEKIKYIRENTELFIGFSTLENLVKGGRVSRMTGLFGSLLQVRVIGTLKDRELNTLLRGRGSKTFYKWLEELSDSISSSGRKIREIGISHAQGLEFSQKAKEVLQKFVEKPISILDTNTTIATHTGPGAWAIMIDYE", "text": "FUNCTION: May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism."}
{"protein": "MAKLTKRMRVIREKVDGTKLYEINDAVALLKELATAKFVESVDVAVNLGIDPRKSDQNVRGATVLPHGTGREVRVAVFTQGANAEAAKAAGAELVGMDDLAEQIKAGEMNFDVVIASPDAMRVVGMLGQILGPRGLMPNPKTGTVTPNVAEAVKNAKAGQVRYRNDKNGIIHTTIGKVDFTPVQLKENLEALISALKKAKPAVAKGVYVKKVSISTTMGAGVAIDQATLDTAN", "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": "MFKAELSDSSILKTSFDAISSIVDEVQIQTDSEGMRLDALDRSHITFVHLELKASLFDEYVCDVPEKINIDTGEFMSVLKRAKSQDRVIMSLDEGNFIITFEGDATRTFKIRLIDIEYDNPTPPELEHPASFKVHFGILKDAINDIDIFSDKIALQVDEDYFRASADGEFGDASVKYLHGENINTQEKSLFSLDKIREMLKADKFSEEAEIGLGTDMPLKLTLNMVTGDGKLSFLLAPRLESDE", "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": "MRPATKIYGLIGRAVDYSYSPLIHNTAFEQLSLPCRYTIFNITEEHLVADALKGARALGLAGFSVTIPYKKTVVPLLDSLSEEAKSIQAVNTIVNHEGTLVGHNTDIAGFASPLLPHARSIQGRPVAILGSGGASLAAIEAFRTLFMPSEITLFMRNPAKETRMTDPAIKRCALGDLRESGSESSALLRDAAVVINATPVGTLGRPDAHMSPVPAESNLLHQGQIIYDMVYNPLDTPLLLAARKAGAVTIPGMEMLLAQGAAAFRLWTNLEMPMDAVRSALLNEIGASAI", "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": "MPSCDPGPGPACLPTKTFRSYLPRCHRTYSCVHCRAHLAKHDELISKSFQGSHGRAYLFNSVVNVGCGPAEQRLLLTGLHSVADIFCESCKTTLGWKYEQAFETSQKYKEGKYIIEMSHMVKDNGWD", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the yippee family."}
{"protein": "MSFKFNEESFLDNSFNETLREKLTKMLNSRKSMDIKIDDHLSYANNRGSTSCSNNFDNSSSIKARDSKLDILKSDVKVCEVNFPTIPNLEILDLDVSGQPRALAKGICKISCRDALLQIQTEIEANSLLLYTNISPDFTTPLMIANDTFTIPITMTFSQIQLEAITNVFVKNSGVGISFNDVSLDFQFDCSIKLLQPHIAKRLRKSMQLVFKDVLPSALFNMSRSWFTHDGSSSQTTTDHSQEEGSRLIRLHRLTVEDLDLQDLSPVNMLKLSTLTSSRQTLSLHSTMPKYFSTIPGCLDRQNFRNFTSRMPCLSNYGGGSDDGDKHVPHIHNLQNKNLLPEEALEENDIDLKAILSIQTKIYERGISTNNDVIRPRRRKIRIKRAKKSIVNKATETSSNLNADSEITPVSSSHNATSSVNTITSLTTSSLGSTAGSSNSKNTNRSSSFTSSIMPITPLAQSSMNKKDGNLITLRQDSKVLDSMKYFTKIQDLHNIHASFNSSRETQDSNNRFRIASEMLPTKREISPIPTLNSFIEPNRRFSFVGLNHKTSHDNSWSVDEQPPPYY", "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": "MNGQLIIDRYMEELNAELANMPDVERENAIDELKGHITAFVQDRIKAGLSEEELQEAVESEFSHPKELAELMMGDGGETKRRRSLLGKSWISVLLIVTIIALPLLPSDFRHLPLAVYLMVLAGYVWKRKKLVMFAGVRKNKMRSQKEIVKISRVGAVYLLFLAVVLLLSPFLNALVVLLLIAVSCAAFFLFLNIK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MLALRLLNVVAPAYFLCISLVTFVLQLFLFLPSMREDPTATPLFSPAVLHGALFLFLSANALGNYILVVQNSPDDLGACQGTSSQRPQRPPPSTHFCRVCARVTLRHDHHCFFTGNCIGSRNMRNFILFCLYTSLACLYSMVAGVAYISAVLSISFAHPLAFLTLLPTSISQFFSGAVLGSDMFVILMLYLWFAVGLACAGFCCHQLLLILRGQTRYQVRKGVAVRARPWRKNLQEVFGKRWLLGLLVPMFNVGTESSKQQDK", "text": "FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (By similarity). Catalyzes the palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane (By similarity). Might also mediate palmitoylation of CNN3 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MMFCKLLRCQNGIASKRAALSLKGFKTSSINLVEKKLNKYSETITGPKSQGASQAMLYATGLNEEDMKKPQVGIASCWYEGNPCNMHLLDLGRRVKEGVKKAGLTGFQFNTIGVSDGISMGTTGMRYSLQSREIIADSIETVMQGQWYDANVSIPGCDKNMPGCLIAMGRFNRPSIMVYGGSIRAGHSPCQNNAPIDIVSAFQSYGEFITGKIDEPTRHDIIRHACPGGGACGGMYTANTMASCAEAMGMTLPGSSSYLAGSPEKFAECEAAGSAIKRLLVDDIKPRDIMTRSAFENAMVLTMTLGGSTNSVLHLIAIAKSVGITLTLDDFQAVSNRTPFIADMKPSGKYVMEDLFAIGGIPSVLKYLHAEGLIDGSNITVTGKTLAENLRGFKDLAEGQKIIRPLSNPIKTEGHLRVLRGSLAPEGSVAKITGKEGLNFTGKARVFDAENDFIAALERGEFKKGEKTVVIIRFEGPKGGPGMPEMLKPSSAIMGAGLGKDVALLTDGRFSGGSHGFLIGHVDPEAQVGGPIALVQDGDVIEINAVKNTLDLMVDEKEMARRRSVWKAPPLKYQQGTLLKYARNVSTASKGAVTDSLE", "text": "FUNCTION: Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3- methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3- methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3- methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L- valine, respectively. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the IlvD/Edd family."}
{"protein": "MAKKYVVALDQGTTSSRAIIFDHDANIVSVSQREFPQIYPQAGWVEHDPMEIWASQSSTLIELLARSGIHGSEVAAIGITNQRETTVIWDKLTGKPVYNAIVWQCRRSSHICDELKAQGLEDYVRETTGLLLDPYFSGTKIKWILDNVAGVRERAEKGELLFGTIDTWLVWKLTEGKVHVTDPTNASRTLLFNIHTQQWDSKLLEALNIPESLLPEVKPSCAVYGKTRIAGEGGEISIAGIAGDQQSALFGQLCIDEGMAKNTYGTGCFLLMNTGKQAVKSTHGLLTTVAIGADCEVNYALEGAVFMGGATIQWLRDELGLIRDAQDTEYFASKVEDTNGVYLVPAFVGLGAPYWDPNARGALVGLTRGSNRNHIIRAALEAIAYQSRDLLDAMAKDSGVMLKQLKVDGGAVSNDFLMQFQADITNVEVQRPAITETTAMGAAFLAGLAVGFWSSTSELKHKADIERTFIPSISAEKCDELYCGWNRAVTQTIKS", "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": "MVHSSMGAPEIRMSKPLEAEKQGLDSPSEHTDTERNGPDTNHQNPQNKTSPFSVSPTGPSTKIKAEDPSGDSAPAGPPPPQAVQAHLSQVQLMLTGRQLAGDIQQILQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQAVTRPTLSDPHLSHPQPPKCLEPPSHPEEASDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSRPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPASYSPHLVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGAAGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLSGLNPSTGPGLWNPAPYQP", "text": "FUNCTION: Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates IL6 expression in B cells with POU2AF1. Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-2 subfamily."}
{"protein": "MRIKRGFKARHRRKKILKLAKGFRGGHSKLFKTAKNTVDKALGYAYRDRKQRKRDFRRLWIARINAAVRMHSLSYSRFMHGLKKAGVELDRKVLAELAISDPSGFSKVVAVAAEQQ", "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": "MLKIEKQAKAIKITEVKESNYKGQFIVEPLYRGYGNTLGNALRRVLLSSIPGAAIKGMRIEGVLSEFTVMDGVKEAVTEIILNVKEIVVKAESSGERRMSLSIKGPKVVKAADIVADIGLEIVNPEQVICTVTTDRTLDIEFIVDTGEGFVVSEEIDKKDWPVDYIAVDAIYTPIRKVSYEIQDTMFGRMTDFDKLTLNVETDGSIEIRDALSYAVELLKLHLDPFLEIGNKMENLRDDIEEMIEEPMDIQVIDDKSHDMKIEELDLTVRSFNCLKKAGIEEVSQLASLSLNELLKIKNLGKKSLDEILEKMKDLGYDLEKNGSPE", "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": "MASRDSANADITPEVLLRAYACGIFPMAESIDDPTLFWVEPELRGIIPLGGFRVASRLARTVRSDVFTVTVNRDFRGVIDGCASPQPGRDDTWINRRIRELYIGLHGIGHCHSVEVWQDDDLVGGLYGVSLGRAFFGESMFHRARDASKVALVHLVARLLAGGYELLDTQFVTEHLRSFGAIEVPRQRYRALLDDALHGVADFGALPVDQPVSGAQALEIIAKN", "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": "MDKRIPVGADTLRIRNLGLQDYDTVWQAMRDFTVRRDSATVDELWWVEHPPVFTLGLNGQECHLRDVGDIPVVRCDRGGQVTYHGPGQSIVYILVDLRRRALGVRQLVDALELSVVDLLQSYEIETERRANAPGVYVQGRKIASLGLRVRKGCCYHGLSLNVAMDLSPFYRIDPCGYSGMEVIDLKRLGMELPLADVQQNLSRYLVRRLGYSAPFYGEENRMIK", "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": "MNYLVMISLALLFMTGVESLKDGYIVNDINCTYFCGRNAYCNELCIKLKGESGYCQWASPYGNSCYCYKLPDHVRTKGPGRCNDR", "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 (PubMed:12911331). The toxin principally slows the inactivation process of TTX-sensitive sodium channels (PubMed:23685008). It discriminates neuronal versus muscular sodium channel, as it is more potent on rat brain Nav1.2/SCN2A (EC(50)=29 nM) than on rat skeletal muscle Nav1.4/SCN4A (EC(50)=416 nM) (PubMed:12911331). It also shows a weak activity on Nav1.7/SCN9A (EC(50)=1.76 uM) (PubMed:23685008). In vivo, the toxin produces pain hypersensibility to mechanical and thermal stimuli.(PubMed:23685008). It also exhibits potent analgesic activity (when injected intraperitoneally), increasing hot plate and tail flick withdrawal latencies in a dose-dependent fashion (PubMed:20619318). This paradoxical analgesic action, is significantly suppressed by opioid receptor antagonists, suggesting a pain-induced analgesia mechanism that involves an endogenous opioid system (PubMed:20619318). This led to hypothesis that pain relief induced by peripheral administration of Amm VIII may result from sensitization of primary afferent neurons and subsequent activation of an opioid-dependent noxious inhibitory control (PubMed:20619318). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MNSIKNHLMCEEINKRFNLHPKVREAMESIEREVFVPAPFKHFAYTLNALSMQAQQYISSPLTVAKMTQYLEIDHVDSVLEIGCGSGYQAAVLSQIFRRVFSIERIESLYIEARLRLKTLGLDNVHVKFADGNKGWEQYAPYDRILFSACAKNIPQALIDQLEEGGILVAPIQENNEQVIKRFVKQNNALRVQKVLEKCLFVPVVDGVQ", "text": "FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. L- isoaspartyl/D-aspartyl protein methyltransferase family."}
{"protein": "MASIPPDDDAAAAAAAGAAENGYGNGKGNGNGPAPRPPPAKRPRSVISAAQIRAEFEHHEAGVARVNNGSFGCCPSSLLDAQARWQRLFIAQPDDFYFHALQPGLRRSRAAVAGLVNAGDVAEVSLVDNATTAAAIVLQHAAWSFAEGRFSRGDAVLMLHYAYGAVKKSIHAYVARAGATVVEVPLPFPVASADAIIAEFRAALDVAKAGGRKVRLAVIDHITSMPSVVIPVKELVAICREEGVDKVFIDAAHSIGQVPVDVRDIGADFYTSNLHKWFFCPPAVAFLHTRKDDPIASQLHHPVVSHEYGNGLPMESGWIGTRDYSAQLVVPESIDFVNRFEGGIEGIRSRNHEKVIEMGKMLAEAWGTFLGTPPELCGSMVMVGLPGCLGVESDDDVMRMRTMLRKDFMVEVPIYYNSRRVEAQEMAKDKNGDAVTGYVRISHQVYNVTEDYEKLRDAVNKLVADGFTSSKLRPSQKQETMA", "text": "FUNCTION: Catalyzes the production of hydrogen sulfide (H2S) from cysteine. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MTVQVQDHDITTAADTAKLPQPMQPPLKQATYKTHTTDFIVNELLPLEFTGEGEHLWLHIQKSGMNTAYLAKLLSEWAEIPLRDVGFSGLKDRHALTTQWFSLRIPKKQLPDSEFAPVDISANESVTILEQQWHNKKLNRGTHRANQFIITLRDIEFASFEASLSLQISASEQPMSAKQAVEQHLTTISQSGVPNYFGPQRFGRSGNNIREALSLFARPVPESRPQPNKGKRKRVPREQNSMELSAARSLIFNEILAARVRDGSWNTGLAGEVFNLDGSGSIFASDEIDHTLRARLETGDIHPTAVLWGTSNEKVSGKAAAMETDIVAQSPLLMQLAVGLEQRDIKAQRRALRLPIEALSWEWEDKEDGQILVLNFTLTTGSFATSVLASLVQELITSSYSRS", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
{"protein": "MLTLKKSMLLLFFLGMVSFSLADDKREDEAEEGEDKRADEGEEKRAAEKKRFLEGLLNTVTGLLG", "text": "FUNCTION: Induces contraction of smooth muscle in isolated guinea pig urinary bladder (EC50=4.66 nM). Has no antimicrobial activity against the Gram-positive bacterium S.aureus, the Gram-negative bacterium E.coli and the yeast C.albicans. Elicits histamine release from rat peritoneal mast cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MNYNPFQWTFKSEQTANEFNEHVEKSVPFYKEIHKIVKIIGGFFVEENTNVYDIGSSTGNLLKGMSNILKRNANYIGIDNSIYMNQVAMNDADSDNIKIISEDVQDFKFTNASYITSILTLQFINIEDREKTIKNVYQGLNKGGAFILVEKVNGEFVQSHEIMNQIYHDFKLENGLTYEEVIKKSQSIRGVLKPLTLKQNKRMLEKAGFKDIDTWFKWNNFVGIIAVK", "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": "MTEFQGYLELDRSWQHDLLYPLIFREYIYTFVHDHGLNRNKSNLLENVGYDNKSSLLIVKRLISRMYQQNHLIISANDSNQNPVFGYNKFFFSQMISEGFAVVVEIPFSLRLVSSLKGTELVKYYNLQSIHSTFPFFEDKFPHLNYVSDVLIPYPIHLEILVQTLRYWVKDVSSLHLLRLFLHEYYSWNRFRIPKKSISFFSKSNPRFFLFLYNSYVCEYESILLFLRNQSSHLRLTSSEGFFERIYFYGKMKHPVKEVFADDFPTNLWFFQDLVIHYVRYQGKSILASKDMPLLMNKWKFYLVHLWQCHFYVWSQAGSISINQLSKHAFGFLGYLSSMRINLSVVRSQMLENSFLMDNAMKKIDTLISISPLIGSLAKMKFCNVVGQPLSKSTWADLSDFDIIDRFARICRNLFHYYSGASKKKSLYRVKYILRLSCVKTLARKHKSTVRTFLKRLGSELLDEFFTEEEEVLSLIFPRTYSTLRRLYKGRIWYLDIFCINDLVNYE", "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": "MLSITPEIIKEIVQGEYHDVFAVLGPHAQKNGYVIRAFFPAAKTLQVKSKLDGSVLAEAVMRNEEGFFEANCNCSEKPSYYFTVGYGDKEFDVEDMYRFGSTIPEGDLYLFGEGTYEQAYRLFGAHPTEVDGVPGCRFTVWAPNAKTVAVVGDFNFWQGRAHVMRKHIPSGIWELFIPYLGEGALYKYEIRNHSGDCLPHKADPYGFAAQKPPEQASVVSVLDRYEWNDAEWFAKANNWTQRDRPISIYEVHLGSWKRVVEEDNRYLSYKELAADLIPYVKSMGFTHIQLMPISEFPFDGSWGYQPVGLYAPTSRFGSPEDFKYFVDCCHQNDLAVLIDWVPGHFPTDSHGLGLFDGTPLYEHADSRQGFHPDWNTYIYNYGRHEVKSFLMANALFWLEQYHIDGLRVDAVASMLYLDYSRKDGEWLPNSYGGRENLEAIDFLRLVNERVYKRFPHAMMVAEESTAWPGVSSPTSCGGLGFGYKWNMGWMNDSLQYISKEPIHRQYHHHDMTFSLHYAFSENFVLPLSHDEVVHGKRSLLGRMPGDAWQQFANLRAYYAFMWTHPGKKLLFMGGEFAQGMEWNHDTSLSWHQLEIDYHSGIQTLVKSLNRLYTDVPALYKEDCMSSGFEWVEADDRHNSIFAFLRKAKDEKPVLVVANFTPVAREGYRVGVNQPGYYRELLNTDSELFGGSNLGNEGGVHSEEIAWHQRPQSVSINIPALAAVVFQLDS", "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": "MKKVYIKTFGCQMNEYDSDKMADVLGSAEGMVKTDNPEEADVILFNTCSVREKAQEKVFSDLGRIRPLKEANPDLIIGVGGCVASQEGDAIVKRAPFVDVVFGPQTLHRLPDLIESRKQSGRSQVDISFPEIEKFDHIPPAKVDGGAAFVSIMEGCSKYCSFCVVPYTRGEEVSRPFEDVLTEIAGLAAQGVKEITLLGQNVNAYRGLMSDGEIADFALLLEYVHEVPGVERIRFTTSHPREFSQRIIDCYAKLPKLVSHLHLPVQSGSDRVLMAMKRGYTGLEYKSIIRKLRAIRPDLCLSSDFIIGFPGETEADFEQTLKLVRDCEFDFSFVFIYSPRPGTPAANLPDDTPHAEKVRRLEALNEVIEAKGYAINQSMVGTVQRVLVENVSKKDATMLAARTANNRVVNFAGHPRLLGRMIEVKITAAFPHSLAGEALTSESA", "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": "MKLQLIAVGTRMPDWVTRGFEEYQRRFPRDMALELIEIPAGKRGKNADIVRILQKEGEQMLAAIPKGNHIVTLDLPGKNWTTPELATAMNKWQLDGRDVSLLVGGPEGLAPACKEAAHQSWCLSALTLPHPLVRIVVAESLYRAWSVNTNHPYHRE", "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": "MNKDHTLYCSVYIRNAFFSEIGIGISANSCLLLFHTFMFIRGHRPRLTDLPIGFVALIHLVMLLLAAYITEDFFMSSGGWDDITCKLVIFLHRFFRSLSVCATCLLSVFQAIILCPQSSHLAKLKQNSPHQLSYFFIFLSIFYTSISSHILIAAIPTQNITFVNLIYITNSCSFLPLSSSMQHTFSTLLAFRNVFVIGLMGLSTCYMATLLCRHKTRSQRLQNSKLSPKATPEQRALRTILMLMSFFLLMSTFDSIISYSRTILQGNPLPFCFQILVAHSYAAVSPLLVLSNEKRITNLLISMYEKIVL", "text": "FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MASTIERKTLEANEEPVDEVLQMPPSLLTCGGCQQSIGDRFFLKAIEQYWHEDCLSCDLCGCRLGEVGRRLYYKLGRKLCRRDYLRLFGQDGLCASCEKRIRAFEMTMRVRDKVYHLECFKCAACQKHFCVGDRYLLINSDIVCEQDIFEWTKLNGSIV", "text": "FUNCTION: Transcription factor that acts synergistically with tal1/scl in primitive and definitive hematopoiesis, and in endothelial development. Specifies mesodermal precursors to a hemangioblast cell fate. Hemangioblasts are bipotential precursors of blood and endothelium, and in the absence of hematopoietic induction cues such as gata1, tal1/scl-lmo2-induced haemangioblasts differentiate into endothelial cells. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKLLCLVAVVGCLLVPPAQANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARTMATAAASIGGPRANTVLERVEGAQQRWKLQVQEQRKTVFDRHKMLS", "text": "FUNCTION: Transmembrane protein that binds to and facilitates the assembly of lysosomal proton-transporting V-type ATPase (v-ATPase), resulting in enhanced lysosomal acidification and trafficking (By similarity). By bringing the v-ATPase accessory protein ATP6AP2 and the v-ATPase subunit ATP6V0D1 together, allows v-ATPase complex formation and activation (By similarity). TMEM9-controlled vesicular acidification induces hyperactivation of Wnt/beta-catenin signaling, involved in development, tissue homeostasis and tissue regeneration, through lysosomal degradation of adenomatous polyposis coli/APC (PubMed:30374053, PubMed:32380568). In the liver, involved in hepatic regeneration (PubMed:32380568). SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Endosome, multivesicular body membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TMEM9 family."}
{"protein": "MAGESTNSVGNDITSLIQPGLDQVIQDEGVQVTLINSILGWCRIHIINPVKSSKIVKSRAFQITMIVLGIILLIAGLALTFVLQGQLGNNAFLFLIPAVIGLVKLLATSVFMEKPCTPEKWRLCKRLLATTEDILDDGQINQSNTIFTMDSSESTNAAAS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MFESTRKNIQPSDATLVITQTRGVTGSKQNHRDTLRSLGLKRIGHQVTRKADAVTVGMVNTVPHLVSVEEVNNG", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MASSSTRKYETRKRDPNSKIAALLVIDMQNHFSSMAKPILNNVLTTIDICRRASVPVFFTRHNHKSPTDHGMLGEWCNGDVILDGTTDSEIIQEIQGQVTGPDEMVEKNTYSAFNKTRLQENLEKIGVKEVIVIGVMTNLCCETTAREAFIKGFRVFFSTDATATFNEELHEATLMNLAFGFAYLVDCDKLRRSLLGN", "text": "FUNCTION: Catalyzes the deamidation of nicotinamide, an early step in the NAD(+) salvage pathway. Prevents the accumulation of intracellular nicotinamide, a known inhibitor of poly(ADP-ribose) polymerases (PARP enzymes). SIMILARITY: Belongs to the isochorismatase family."}
{"protein": "MYSFIRNCLFKLDAEVSHELSLDWLGAFERLHMLKPFALKVTPSPINVMGIDFPNRVGLAAGLDKNGDFVNALGQLGFGFVEIGTITPLAQSGNPKPRLFRLPEHQAIINRMGFNNKGVDHLVAQVQKRRYPGVLGINIGKNKITPEENALDDYVKCMDKVYAHADYITVNISSPNTPGLRNLQFGETLANLIAGIKQAQDRLAQTHDKYVPVAVKIAPDMTAEEIHSVADTLVNGNIDGVIATNTTISREAVQGHINADEAGGLSGLPVRDKSTEVIATLSAHLQGAMPIIGVGGIVEGADAQAKIAAGASLVQIYSGFIYKGPKLIAEAADAIASAG", "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": "MTSSDPQSHNVFVYGSILEPAVAAVILDRTADTVPAVLHGYHRYKLKGLPYPCIVSSDSGKVNGKVITGVSDAELNNFDVIEGNDYERVTVEVVRMDNSEKVKVETYVWVNKDDPRMYGEWDFEEWRVVHAEKFVETFRKMLEWNKNPNGKSMEEAVGSLLSSGD", "text": "FUNCTION: Putative gamma-glutamylcyclotransferase. SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family."}
{"protein": "MRYPMSKLAYHRVLLKLSGEALMGSADYGIDPKVINRLAGEVIEAQNAGAELALVIGGGNIFRGAGLAAKGMDRVTGDHMGMLATIINALAMQDALEKLGTKVRVMSAIKINNVCEDFIRRRAIRHLEKSRITIFAAGTGNPFFTTDSGAALRAIEIGADLLLKATKVDGIYNKDPQKHCDAVKYSTLSYDEVISQNLEVMDTAAFALARDSNLPLRIFDIEQPGVLLRILHGEEIGTLVKERNSKS", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MTDIFARRATLARSVRLLSQFRYERSEPARFYGALAADTAAMVDDLWRAGHGESAAGRTLLDVGGGPGYFAAAFADAGVRYLGVEPDPGEMHAAGPVVAADTGTFVRASGMALPFADDSVDICLSSNVAEHVPRPWQLGAEMLRVTRPGGLAVLSYTVWLGPFGGHEMGLTHYLGGSRAAARYARKHGHPAKNNYGSSLFEVSVADGLAWAACTGAELAAFPRYHPRWAWWLTSVPVLREFLVSNLVLVLQPQ", "text": "SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MSLAEFDADVVINAQNCIVGRVASEVAQRALGGETVAIVNVEDAVITGSEEDVMSVYETRSELGSDQGPAYPSRPDGIFKRAVRGMLPYKSDRGREALSNVRTYVGNPYDDDGEAIDGTTLDRLSNIKFLSLGEVSANLGATVTW", "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": "MRILGIDPGIAIVGFGVVDKEGSQLRPVQYGSIQTEAGLPVPLRLKQIFEAMQSLLETYRPDEMSVEKLFFNKNVTTAFTVGQARGVIILAAELAGVPVYEYTPMQVKQAVTGYGGAEKKQIQEMTKLLLRLKEVPKPDDVADALGIAITHAQFRAFISISEGVKK", "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": "MEALKVEKFTTANRGNGLRAVAPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEKLMRCSQCRIAKYCSAKCQKKAWPDHRRECSCLKSCKPRYPPDSVRLLGRVIVKLMDEKPSESEKLYSFYDLESNISKLTEDKKEGLRQLAMTFQHFMREEIQDASQLPPSFDLFEAFAKVICNSFTICNAEMQEVGVGLYPSMSLLNHSCDPNCSIVFNGPHLLLRAVREIEAGEELTICYLDMLMTSEERRKQLRDQYCFECDCIRCQTQDKDADMLTGDEQIWKEVQESLKKIEELKAHWKWEQVLALCQAIINSNSNRLPDINIYQLKVLDCAMDACINLGMLEEALFYAMRTMEPYRIFFPGSHPVRGVQVMKVGKLQLHQGMFPQAMKNLRLAFDIMKVTHGREHSLIEDLILLLEECDANIRAS", "text": "FUNCTION: Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family."}
{"protein": "MRHRKSGRQLNRNSSHRQAMFRNMAGSLVRHEIIKTTLPKAKELRRVVEPLITLAKTDSVANRRLAFARTRDNEIVAKLFNELGPRFASRAGGYTRILKCGFRAGDNAPMAYIELVDRSESKAEATAE", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MKIFIDTANVEEIKRISKWGILDGATTNPSLIAKEGRQLKEVVEEICSIVDGPISAEVISLNCDAMVKEARDLAKIHKNIVIKIPMCEEGIKAVNILSKEGIRTNVTLIFSPQQALIAAKAGASFVSPFVGRLDDIGMDGVSSIKDIAEIFKIYDIKTEIIAASIRHPMHVLEVAKAGSHIATVPYKVLMQMIKHPLTDIGIEKFLEDYNKSK", "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": "MERNGGHYTDKTRVLDIKPLRTLRPVFPSGNQAPPFVCAPPFGPFPPGFSSFYPFSSSQANQHTPDLNQAQYPPQHQQPQNPPPVYQQQPPQHASEPSLVTPLRSFRSPDVSNGNAELEGSTVKRRIPKKRPISRPENMNFESGINVADRENGNRELVLSVLMRFDALRRRFAQLEDAKEAVSGIIKRPDLKSGSTCMGRGVRTNTKKRPGIVPGVEIGDVFFFRFEMCLVGLHSPSMAGIDYLVVKGETEEEPIATSIVSSGYYDNDEGNPDVLIYTGQGGNADKDKQSSDQKLERGNLALEKSLRRDSAVRVIRGLKEASHNAKIYIYDGLYEIKESWVEKGKSGHNTFKYKLVRAPGQPPAFASWTAIQKWKTGVPSRQGLILPDMTSGVESIPVSLVNEVDTDNGPAYFTYSTTVKYSESFKLMQPSFGCDCANLCKPGNLDCHCIRKNGGDFPYTGNGILVSRKPMIYECSPSCPCSTCKNKVTQMGVKVRLEVFKTANRGWGLRSWDAIRAGSFICIYVGEAKDKSKVQQTMANDDYTFDTTNVYNPFKWNYEPGLADEDACEEMSEESEIPLPLIISAKNVGNVARFMNHSCSPNVFWQPVSYENNSQLFVHVAFFAISHIPPMTELTYDYGVSRPSGTQNGNPLYGKRKCFCGSAYCRGSFG", "text": "FUNCTION: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. 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": "MKERYPTKKIYVGDVAVGGDAPISVQSMTYSDTRDVAATVEQINRLHFAGADMVRVAVPEMEDALALKAIKEQISLPLIADIHFNYRLALEAAKWVDCIRFNPGNIGEKSRIKEIVKACQERNLPIRVGVNAGSLEKEFDQKYGATAEGMVASAEYNIKFLEDLGFTDIKVSLKASDVDRTVDAYRMLRPKNAYPFHLGVTEAGTIFHATVKSAIGLGALLLDGIGDTMRVSITGELEEEIKVGKAILKDSGRVQEGLNIISCPTCGRIEADLVSAVAEVEKRTAHIKTPMDVSVMGCVVNAIGEAKHADVAIAYGKGSGLVMVKGEVVAKLPEGELVERFVAEVEKFAGENG", "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": "MSAFTPASEVLLRHSDDFEQSRILFAGDLQDDLPARLDTAASRAHTQQFHHWQVLSRQMGDNARFSLVATADDVADCDTLIYYWPKNKPEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEQMLADYAPLNKVDSARRCGLYFGRLEKQPVFDADKFWGEYSVDGLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSVAFARHSPKIRLTLCDVSAPAVEASRATLAANCVEGEVFASNVFSEVKGRFDMIISNPPFHDGMQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDVLDETFGFHEVIAQTGRFKVYRAIMTRQAKKG", "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": "MGTPGSGRKRTPVKDRFSAEDEALSNIAREAEARLAAKRAARAEARDIRMRELERQQREGVEDTLSLRSLGSHRLDEKSDKQYAENYTRPSSRNSASATTPLSGQSSRRGSGDTSSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ", "text": "FUNCTION: May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity). SIMILARITY: Belongs to the LRRFIP family."}
{"protein": "MNKRRANGSSHSTRPVRTGSPKWVRFSREEVEMLIEELAKKGYTPSMIGIVLRDQYGIPLAKPIIGKKVNQFLKDKGLASQIPEDLFNLIRRAVNVRRHLNEYPGDKTAKKGLEEIESKIRRLSRYYKRVEKLPQDWTYDPAKAELLVSASS", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MGGARDVGWVAAGLVLGAGACYCIYRLTRGPRRGGRRLRPSRSAEDLTEGSYDAILSAEQLEKLLYLLESTDDPIITEKALVTLGNNAAFSTNQAIIRELGGIPIVGSKINSLNQSIKEKALNALNNLSVNVENQTKIKIYVRQVCEDVFADPLNSAVQLAALRLLTNMTVTNDYQHLLSNYITGLLHLLLIGNGSTKVQVLKLLLNLSENPAMTEGLLSAQVDSSFLSLYDGQMANEILLRALTLFQNINNCLRVEGRLANQLPFAKGSLFFLLYGEECAQKMKALACHPDVDVKEKALAIKPKF", "text": "FUNCTION: May play a role in cell survival and cell growth. May suppress the transcriptional activity of p53/TP53 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Mitochondrion outer membrane; Single-pass membrane protein."}
{"protein": "MSDINATRLPIIIVLGLIIPLCVSDIEMILTRGER", "text": "FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24613547). SIMILARITY: Belongs to the MSDIN fungal toxin family."}
{"protein": "MGQKINPLGLRLGTNQDHYSIWFSQPKAYSKSLQEDQKIRSFIRKYIQNMKISPSGVEGLARISIYKRIDLIELRIFLGFPKLLLENRPQGLEKLQITLQKELNCGNRRLNIVITKVEKPYSNPNILAEFIAGQLKNRVSVRQAMKKAIELAEEADTKGIQVQVAGRLNGQDIARVQWIREGRVPRQTIRATFDYCSYPVRTIYGILGIKIWIFVGEAK", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MVNIPKARKTHCVKCNKHTPHKVTQYKAGKPSLFAQGKRRYDRKQSGFGGQTKPVFHKKAKTTKKIVLRMECSCGYKKQQVLKRCKRFELGGEKKSKNEAIKM", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family."}
{"protein": "MAAKDVKFGNDARVKMLNGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDETVGKLIAEAMEKVGKEGVITVEEGTGLQDELDVVEGMQFDRGYLSPYFINKPETGSVELESPFILLADKKVSNIRELLPVLEAVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGMELEKATLEDLGQAKRVVINKDTTIIIDGIGDEATIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKIAELKGDNEDQNVGIKVALRAMEAPLRQIVINAGEEASVIANSVKAGEGSYGYNAYSEEYGDMIGMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKEDKADMGAAGMGG", "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": "MADENQTPEQNDQQADANQNRFGIKRIYMKDMSFETPMGVQAFQVQWQPKVNQDLNTQVNKLDENHYEVVLKLTITVKMNDDKTAFLAEVHQAGLFEVAGLEAPQLQRLLSSACPEILFPYAREALDSLATRGGFPPLQLPPINFDALFSQAMNQAQQQAEQGQQPN", "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": "MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPIQETPSGQDQPTSGLMHQTFGQQKLYQVPNPHSAPRDTIYQVPPSYQHQGIYQVPTSHGIQEQDVYQVPPSVQRSIGAANGPHLSKKVVTPVRTGQGYVYEYPSRHQKDIYDIPPSHTTQGVYDIPPSSVKVPVFSLPVGEIKPQGVYDIPPTKGLYAIPPSACRDEAGLREKEYDFPPPMRQAGRLDVRPEGVYDIPPTSTKPTGKDLHIKYNCDAPGAAELATRRHQSVLLNHAPSQLGQSPGAQNDAYDVPRGVQFLEPPAETSEKANPEERDGVYDVPLHNPPDAKGSQDVVDGMNRLSFSSTGSTRSNMSTSSTTSKESSVSASPSQDKRLLLDPDTAIERLHRLQQTLEVGVSSLMALVTTDWRCYGYMDRHINEIRTSVDKVELFVRDYLHFARGAVANASCLPELTLHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAVNKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSSHVKSGSENIMNSTEYPHAASQMPLLHPGDHKAQGLNKPLPPSLGKDQPPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIIKQNKLQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSSVGAQDRQLLCFYYDQCETHYISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVAAQDICHKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF", "text": "FUNCTION: Negatively regulates embryonic fibroblast migration (By similarity). May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRKl and SHPTP2 to the tyrosine phosphorylated form (By similarity). Promotes adhesion and migration of lymphocytes; as a result required for the correct migration of lymphocytes to the spleen and other secondary lymphoid organs (By similarity). Plays a role in the organization of T-cell F-actin cortical cytoskeleton and the centralization of T-cell receptor microclusters at the immunological synapse (By similarity). Negatively regulates cilia outgrowth in polarized cysts (PubMed:27926875). Modulates cilia disassembly via activation of AURKA-mediated phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). In conjunction with NKX2-5, positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia (By similarity). Positively regulates RANKL-induced osteoclastogenesis (By similarity). Required for the maintenance of hippocampal dendritic spines in the dentate gyrus and CA1 regions, thereby involved in spatial learning and memory (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cell cortex Nucleus Golgi apparatus Cell projection, lamellipodium Cytoplasm Cell junction, focal adhesion Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Basolateral cell membrane. SIMILARITY: Belongs to the CAS family."}
{"protein": "VAVDACLEQDSDSKVACETCTKTNLVMVFGEITTKANVDYEKIVRNTCRNIGFVSADVGLDADNCKVLVNIEQQSPDIAQGVHGHFTKKPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCAWLRPDGNTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDSKTICHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRRGAYIVRQAAKSIVASGLARRAIVQLLRAIGVPEPLSVFVDTYGTGKIPDREILKIVKETFDFRPGMISINLDLLRGGNGRFLKTAAYGHFGREDPDFTWEVVKPLKWEKA", "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": "MKIGHQFHTVALVGRSNTPGIAEPLASLAACIAKRGFEVVFEADTAQAIGSAGYPALTPAEIGARADVAVVLGGDGTMLGMGRQLAPYKTPLIGINHGRLGFITDIPASDMREVVPMMLAGSYEREERTLLEARIVRNGEPIYHALAFNDVVVNRSGFSGMAELRVSVDGRFMYNQRSDGLIVATPTGSTAYALSSQGPILHPQLQGIVLVPIAPHALSNRPIVLPDDSKIAIQIIGGRDVNVNFDMQSFTALELNDTIEVRRSKHTVPFLHPVGYSYYATLRKKLHWNEHPSSEDDDDA", "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": "MGNKQTIFTEEQLDNYQDCTFFNKKDILKLHSRFYELAPNLVPMDYRKSPIVHVPMSLIIQMPELRENPFKERIVAAFSEDGEGNLTFNDFVDMFSVLCESAPRELKANYAFKIYDFNTDNFICKEDLELTLARLTKSELDEEEVVLVCDKVIEEADLDGDGKLGFADFEDMIAKAPDFLSTFHIRI", "text": "FUNCTION: Calcium- and integrin-binding protein that plays a role in intracellular calcium homeostasis (By similarity). Acts as a auxiliary subunit of the sensory mechanoelectrical transduction (MET) channel in hair cells (By similarity). Essential for mechanoelectrical transduction (MET) currents in auditory hair cells and thereby required for hearing (By similarity). Regulates the function of hair cell mechanotransduction by controlling the distribution of transmembrane channel-like proteins TMC1 and TMC2, and by regulating the function of the MET channels in hair cells (By similarity). Required for the maintenance of auditory hair cell stereocilia bundle morphology and function and for hair-cell survival in the cochlea (By similarity). Critical for proper photoreceptor cell maintenance and function (By similarity). Plays a role in intracellular calcium homeostasis by decreasing ATP-induced calcium release (PubMed:23023331, PubMed:26173970, PubMed:26426422). SUBCELLULAR LOCATION: Cytoplasm Cell projection, stereocilium Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Cell membrane, sarcolemma Note=Colocalizes with ITGA7 at the myotendinous junctions (MTJ) and at the neuromuscular junctions (NMJ) (By similarity). Located mainly in stereocilia and at the apical surface of hair cells of the cochlea (By similarity). Localizes in the cuticular plate along and at the tip of the stereocilia of vestibular sensory hair cells (PubMed:26173970, PubMed:26426422)."}
{"protein": "MQTQSLNQTSYVFRTENLNVYYGSNLAVKNVTLDIPARQITAFIGPSGCGKSTILRCFNRTNDLIPGARVEGKLTYHGKDLYAKEVDPVAVRRRIGMVFQKPNPFPKSIYDNVAYGPRVLGMKVDLDEVVETSLKRAALWDEVKDKLKENGQSLSGGQQQRLCIARALAVQPDVILMDEPCSALDPISTRRIEELMKELVQDYTIIIVTHNLQQAGRVSDMTAFFSVELVGSNRVGELIEFDRTEVIFNSPTKQATRDYVEGRFG", "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": "MFSPQSRLRHAVADTFAMVVYCSVVNMLIEIFLSGMSVEQSLSSRLVAIPVNILIAWPYGVYRDLIMRVARKASPAGWAKNLADVLAYVTFQSPVYIIILLTVGADWHQIMAAVSSNIVVSMLMGAVYGYFLDYCRRLFKVSNYHQAKA", "text": "FUNCTION: Exports L-alanine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AlaE exporter family."}
{"protein": "MSTIYRESDSLESEPSPTPTTIPIQINMEEEKKDAFVKNIDEDVNNLTATTDEEDRDPESQKFDRHSIQEEGLVWKGDPTYLPNSPYPEVRSAVSIEDDPTIRLNHWRTWFLTTVFVVVFAGVNQFFSLRYPSLEINFLVAQVVCYPIGRILALLPDWKCSKVPFFDLNPGPFTKKEHAVVTIAVALTSSTAYAMYILNAQGSFYNMKLNVGYQFLLVWTSQMIGYGAAGLTRRWVVNPASSIWPQTLISVSLFDSLHSRKVEKTVANGWTMPRYRFFLIVLIGSFIWYWVPGFLFTGLSYFNVILWGSKTRHNFIANTIFGTQSGLGALPITFDYTQVSQAMSGSVFATPFYVSANTYASVLIFFVIVLPCLYFTNTWYAKYMPVISGSTYDNTQNKYNVTKILNEDYSINLEKYKEYSPVFVPFSYLLSYALNFAAVIAVFVHCILYHGKDIVAKFKDRKNGGTDIHMRIYSKNYKDCPDWWYLLLQIVMIGLGFVAVCCFDTKFPAWAFVIAILISLVNFIPQGILEAMTNQHVGLNIITELICGYMLPLRPMANLLFKLYGFIVMRQGLNLSRDLKLAMYMKVSPRLIFAVQIYATIISGMVNVGVQEWMMHNIDGLCTTDQPNGFTCANGRTVFNASIIWSLPKYLFSSGRIYNPLMWFFLIGLLFPLAVYAVQWKFPKFKFAKHIHTPVFFTGPGNIPPSTPYNYSLFFAMSFCLNLIRKRWRAWFNKYNFVMGAGVEAGVAISVVIIFLCVQYPGGKLSWWGNNVWKRTYDNDYKKFYTLKKGETFGYDKWW", "text": "FUNCTION: High affinity transporter for glutathione. Also transports tetra- and pentapeptides like the opioids leucine enkephalin (Tyr-Gly- Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly_Phe-Met) across the cell membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the oligopeptide OPT transporter family."}
{"protein": "MRILKPYLRSTSIQCYLCLLLNSHFLTEAGIHVFILGCISAGLPKTEANWQYVINDLKTIEHLIQSIHMDATLYTEGDAHPNCKVTAMQCFLLELRVILHESKNAAIYEIIENLTMLANSNLSSIENKTELGCKECEELEEKSIKEFLKSFVHIVKMFINTS", "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": "MLDIQLLRKDLDGVAKRLADRGYTLDVAAFSALEAERRAIQTHTEELQARRNSLSKQIGAMKGKGEDTSAVMAEVSGIGDDMKASEAKLGEIQARLSDLMLGMPNVAHESVPVGKDEADNVEVRRWGTPRQFDFEVKDHVDVGTPLGLDFETGAKLAGARFTMLRGPIARLHRALAQFMIDTHTQQHGYTETYTPYIVNPEILYGTGQLPKFADDMFRVEKGGAENTVTQYLISTSEISLTNTVRESIVDGAALPIKLTAHSPCFRSEAGSYGRDTRGMIRQHQFDKVEMVQVVAPETSYAALDEMVGHAEAILQKLGLPYRVITLCTGDMGFSAAKTFDLEVWLPAQNTYREISSCSNTEAFQARRMQARFRNAQGKPELVHTLNGSGLAVGRTLVAVLENYQNADGSVTVPEVLRPYMGGMERIDAPAQTS", "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": "MSIEINNESAIEVDEPVIQRLVTYALDTLHVHPDAELAIVMVDEGAMEQLHVQWMDEPGPTDVLSFPMDELRPGTEDRPTPAGLLGDIVVCPQVAAEQAVTAGHSTMEEILLLTAHGILHLLGFDHAEPDEEREMFGLQRDILIGFAMSERGR", "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": "MGEQSHEKDHDEAHSYNPFVRSAVEYDADTRLQMAENAASARKLFVSSALKDIIVNPENFYHDFQQSAQMAEDANQRRQVSYNTKREAHIHQLKAQGLPLPSNIPMIEINPTRVTLNMEFESQYYSLMTSDNGDHENVASIMAETNTLIQLPDRSVGGTTPDPFAQQVTITGYFGDVDRARMLMRRNCHFTVFMALSKMKMPLHELQAHVRQNPIQNVEMSFVDAPEKNGIVTTYLRITAREKNQHELIEAAKRLNEILFRESPAPENNFTLHFTLSTYYVDQVLGSSSTAQLMPVIERETTTIISYPCYNNRNETRGNIYEIKVVGNIDNVLKARRYIMDLLPISMCFNIKNTDMAEPSRVSDRNIHMIIDESGIILKMTPSVYEPADLLSGEVPLNCASLRSKEFNIKKLYTAYQKVLSKKFDFIAPQPNDYDNSIWHHSLPANFLKNFNMPCRGELSDGSNGRRHRSSSIASSRSKHSYMSKGKQFSESSGGPSRSHTRVSSFSENSSTVPIMQFPTPHFAPPMLTPHHHMLKYVYLQQHQQAQTFLKGAAGLHPGTHIMFPPPIIVDGSFVSALPFADPVVFDGFPYVHGLFPVNEAEQHRNHRESSPSLRSTQEIRKPSRNMGNRPSSSTGSYYPSTTPRQRVYEQVREDDLRSHIGSRRTSVNGDDQNVESMHDQGYERQYPRQHQRLQKDDQQRWKTGSRGDIHSSRTINVHRDVRNSNEYDFHVGNSGPAKRSPSLEQVQLQMTHHLKLKSNDVDLDHEKLYMHESPHNDSDTTVSASGFGNDLMDGDFVQRFLSNANINESGRRPRTVSCFTEKDGQSARYIDSDGAYSVVDHASTHQSRSYDSFRKVGDNGVTKTILEPRARVEKDYGKISLEHKTKYSNEYGDEEKSAENDTSSLGSRQYRIDPMKLIASVRESSEQLPRIHERQFSDVLNEKEKEIADKSIESTVTQDLSLDETSTY", "text": "FUNCTION: Required maternally for germline survival and embryogenesis. Forms a complex with gls-1 which promotes the oogenic cell fate by freeing the translational repressor fbf to repress sperm promoting factors. Promotes maturation of primary spermatocytes to mature sperm. Required during hermaphrodite development to promote sperm fate, which is critical for determining the normal number of sperm. Promotion of sperm fate is at the expense of oogenesis, possibly through the negative regulation of fbf. Required during male development for the continued production of sperm and inhibition of oogenesis. Together with gld-2, promotes the transition from mitosis to meiosis. Required for polyadenylation of neg-1 mRNA during embryogenesis (PubMed:26096734). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic granule Cytoplasm, perinuclear region Note=Localizes to P granules. Found also in particles near but not coincident with P granules."}
{"protein": "MSDRVIIFDTTLRDGEQALAASLTVKEKLQIAQALERLGVDVMEVGFPVSSPGDFQSVQTIARHIKQSRVCALARALPKDIDAAGEALRVAEAFRIHTFISTSSIHVESKLKKSFEDVLEMGVSAIKHARRYTDDVEFSCEDAGRTPIDNLCRMVEAAIKAGARTINIPDTVGYTVPTEFSGIIQTLFNRVPNIDQAIISVHCHDDLGLSVANSIGAVQMGARQIECTINGIGERAGNCSLEEVAMILKTRADLLGVHTNIRHSEIHRTSALVSQLCNMPVQPNKAIVGANAFSHSSGIHQDGVLKAKNTYEIITPESIGLTQNNLNMTSRSGRHVIKHRMESMGYAESSYDLDDLYGKFLTLADKKGQVFDYDLEALAFFSQIHEEPEHFKLEYLGVQSGSSVMATASVKLKVGQEIVSEAATGNGPVDAVYQCINRITGYEISIDKYELKGKGEGKNALGQVDIVAQYKGRKFHGMGLATDIIESSAQALIHVINSIWRADQVAEQMERNVAKTDKINTESV", "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": "MSVTNVSNETNATKAVFDPPMGITAPPIDELLDKVTSKYALVIFAAKRARQINSYYQQADEGVFEFIGPLVTPQPGEKPLSIALREINVGLLDHEEG", "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": "MNYRKIWIDANGPIPKDSDGRTDEIHHKDGNRENNDLDNLMCLSIQEHYDIHLAQKDYQACHAIKLRMKYSPEEISELASKAAKSREIQIFNIPEVRAKNIASIKSKIENGTFHLLDGEIQRKSNLNRVALGIHNFQQAEHIAKVKERNIAAIKEGTHVFCGGKMQSETQSKRVNDGSHHFLSEDHKKRTSAKTLEMVKNGTHPAQKEITCDFCGHIGKGPGFYLKHNDRCKLNPNRIQLNCPYCDKKDLSPSTYKRWHGDNCKARFND", "text": "FUNCTION: This endonuclease is specific to the nrdB gene splice junction and is involved in intron homing."}
{"protein": "MTLAAQPILLTPGPLTTSDTTRDAMLRDWGSWDSDFNAITARLRERLLQIVHGEGTHECVPLQGSGTFSVEAAIGTLVPRDGHVLVPNNGAYCQRIAKICRVLGRQLTTIDYSEDRRVDPADVERALAADPTITHVALVHCETGAGVLNPLHDIAQVVAKHGRALIVDAMSSFGAIDIDARTTPFDAVIAASGKCLEGVPGLGFVIAKRSTLERCEGNSHSLAMDLYDQWVYMQRTTQWRFTPPTHVVAALDAAVGQYVDEGGLAARGGRYQRNYRALIDGMLALGFRPFLDPAIQAPIIVTFHAPDDPNYDFKRFYQEVKKRGYILYPGKLTEVETFRVGCIGHFGEAGIPGAVAAIADTLRAMGVRRVSAEAAA", "text": "FUNCTION: Involved in phosphonate degradation. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. PhnW subfamily."}
{"protein": "MSAQKPGLHPRNRHQHRYDLAALCQTTPELTSFLIRTPAGEQSVDFANPQAVKALNKALLAHFYAVTHWDIPPGFLCPPVPGRADYIHHLADLLGETTGSIPAQATILDVGVGANCIYPLIGVHEYGWRFTGSEVSDAAMSSAQAIIQANTGLSRAIRLRRQKDPAAIFTGIIHKNEFYDATLCNPPFHDSAAAARAGSERKRRNLGQNKDDALNFGGQQQELWCEGGEVAFIKKMIAESQTFRRQVLWFTTLVSRGENLPPLYRALTEAGAVKVVKKEMAQGQKQSRFIAWTFMGDDQRRRFITRKR", "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": "MSGKRVLACDICKSRNYSVTSAKKSDTRLTVKKFCKRCNGHTLHVETR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MQQLIDNLKKRGILDNSSAGLESLTVPVSAYLGFDPTAPSLHIGHWIGICFLRRLAAYGITPVALVGGATGMIGDPSGKSVERSLLDQAQVLDNSKKIAAALASYLPGIRIVNNADWLGSLSMVDFLRDVGKHFRLGSMLAKDVVKQRVYSEEGISYTEFSYLLLQSYDFAHLFKEHNVVLQCGGSDQWGNITSGIDYIRRRGLGQAYGLTYPLLTDSKGKKIGKTESGTIWLDPALTPPYELFQYFLRLPDQEISKVMRTLTLLDNEEIFALDERLTSDPQAVKKYIAEVIVKDVHGSEGLAQAQAATESFFASKGKSITEAELVALVESGVGVKVARADLIGKRWLDIVVELGFCSSRGQARRLIQQRGLYINQEPLADEQSILDGTQLCFDRYVLLSQGKRKKQVIDLN", "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": "MNFKYIVAVSFLIASAYARSVQNDEQSLSQRDVLEEEESLREIRGIGGKILSGLKTALKGAAKELASTYLHRKRIAEDHEVMKRLEAVMRDLDSLDHPEEASERETRGFNQEEIANLFTKKEKRILGPVLGLVGNALGGLIKKIG", "text": "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. FUNCTION: Maximin-H3 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
{"protein": "MSSNQIYSAKYSGVDVYEFIHPTGSIMKRKADNWVNATHILKAAKFPKAKRTRILEKEVITDTHEKVQGGFGKYQGTWIPLELASKLAEKFEVLDELKPLFDFTQQEGSASPPQAPKHHHASRSDSTRKKATKSASVPSGKVSEKASSQQQQPVSQQQQQQPGSAPKRRGRPPRNKATVTLQRSQSEMVFPKPSIPSSSIQSTKLPSLQPQFGRSATSLSPIMDVKSPLDQASPQFKELDIEDGLSSDVEPNSIMGTKHEDNTHLMNTKDEPVSSSSSLPSSPSEFSQSVAFGSRSNMQTPLQLNGTTSMNMILPKFSSSQNGPSDSNQRANEYLSKLVNYFISNDTQNESEIPMELLNPPLHCSPFIDTWIDPEHHTAFHWACAMGTLPIVEALLKAGSSIRSLNNVGETPLIRSSIFHNCYTKRTYPQIFEILKDTVFDLDAKSRNVIHRIVSRKSHTPSAVYYLDVVLSKIKDFTPQYRIDVLINQQDNDGNSPLHYAATNKDDQFYQLLLQNGALTTVQNNSGMTPNGIISGRYSMDEITKGQRLDDPYEFNKMYPSQAATRTNRIIPEVINMMKEMANSYQNAYQKRQNEVLQMERTVKSMKKTITSVEMKLLEALNLKETDNVDIVLNDRKEKIDELQRRIATDKRVLINRLEEGQVKLIRKFVDEETKNVEGKTTDGEESEDIEALLKELVLIQLKRKRKLNQIIDVITDNSKVYKYRKMISQGTDIDVSDVDECLDVIYQTLSKEG", "text": "FUNCTION: Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MVKVGVNGFGRIGRLVTRAAILSAKVQVVAINDPFIDLNYMVYMFKYDSTHGHFRGTVKAENGKLVINGNAITIFQERDPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILAYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEYGYSNRVVDLMVHMASKE", "text": "FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a 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 (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MLRLPRITRRALSSGALAPHFDRPLPPPPPAPPAPLCALPPLTAPDALAPLTRRTVRHADALVARIAAAPAHPDPAELRRVVKNLDRLSDVLCGVIDMCELVRNVHPDPHWVAAAEKTYETLCSFMNQLNTSTGLYDALVATVSHTFPGNPLSPAELRVAQTFLSDFERSGIQLPPGVRAKFVRHSDNILSLGRTFLSFAAAGPSADTPIEIPEPEVLLAGLSSKFVASLPRKKRKGPALLAPGSWEAQMIGRYADNEEARRLVYIGSMREDKDRVYVLETMLKERAELAHVLGKETWADVALSDKMAKTPQNVLQFLTSLATHHRPSAAADVAALQRLKALSTVSRTSSQLPTVHAWDRDHYAEQYAASLLPNGSLPSITPYFSVGTAMSGLSHMLSRLYGISFKPVSVAHGEVWHPSVRRLDVMDEHGKRIGVIYCDLFSRPGKPSAGAAHYTVRCSRRVDDDPSEGDGLPPGWDQHLGKGMEVQGEALHGKEGKYQLPIVVLTTDFGTVEESGPALLGWNDLETLFHEMGHAIHSMIGQTEFHNVSGTRCATDFVELPSILMEHFISSPAVLSTFATHYTTNEPLPIPLIQAHLQLDQSLKALETHSQILMALLDQKYHSIKHGEQLDSTRVWNELQSQVGVIPPVRGTAWQTQFGHLYGYGATYYSYLFDRAIAGKIWSSLFARGRTGPAAANHDPAAAEDILSREGGEAFKEKVLKWGGGRDPWEMVGDVIGGAEGEQVAKGDEKAMELVGRWMIK", "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": "MFKDFFNRTKKKKYLTVQDSKNNDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIALTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDGMKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQMGKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTINEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AccD/PCCB family."}
{"protein": "MGIDPGLTRCGLSVVQAGKGRAVYPVAVGVVRTPSDMPVEQRLNKLFDAVEQWFDDYQPHVVALERVFERSNVSTVMNTAHASGVLMLAAARRGVDVHMYTPSEVKKSISGNGRADKAQMTRMITRILGLSEAPKPPDAADALALAVCHCWRAPLNHLVKGKL", "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": "MSRIGYKTVNVPAGVEVKRDGDQVTVKGPKGELTRTFSSVISMKISDGAVDFDRPDNNNKTRALHGTQRANLNNMVEGVVSGFAKTLKLVGVGYRVQAKGKTLILSVGYSNPVEMAIPETLEVKVPDNTTINISGISKQEVGDFAAEVRAVRSPEPYKGKGIRYENEYVRIREGKTGK", "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": "MGDVILSPVSTEKTALLAEKENKLTLIVDRKATKEDIKREVESRFSVKVEGINILITKKGKKAIVKLAKEYSAEEIAERIGVF", "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": "MNEINESYDTDSVREFTVSDADAGPYALAEGPDGALWFTLVHRGAVARRDPDDGRVTVHPVGDGPTVIAPGPDGALWFTEYRAHRIGRITPEGHYASFAPLTPEGGPFGITAGPDGAMWFTLSSADRVGRVTMDGEVTEHPAPGAFPSALTAGPDGALWCTLNQGNAIGRLTPDGHGTAYPLPTPGAAPVGIAAGPDGALWFTEIGAGRIGRITVTGDLTEYPLSDPAARPHAVTAGPNGALWFTEWGSGRVGRITVDGRVTSYPLSRTDCEPHGIAVHDGALWCALETGSLARIQVPA", "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": "MRLSYRLVSGLLVLASIVGMSFALYLEHVKGLEPCPLCIFQRVGLMAMGFVALIAFLHNPVSNAIKRFYAFLAGVAILWSVGVAGRHVWLQHLPPDQVPSCGPGLNYLIDALPMKTVLQEVLSGSGECAAIDWTFLGQSLPVWSLAYFLLLLLVCLWQLFRFYPVFKTAKK", "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": "MNITIISVGKLKEKYLKHAIDEYSKRLSRYCKLNILELQDEQTPDNASEKDELIIKDKEGNKILNSIKDNMYVITLDLKGKMMSSEELSKFIDNCGVRGNSNLCFVIGGSLGLSEAVLKRSNHSLCFSKMTFPHQLFRVMLLEQIYRAFRISNGEPYHK", "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": "MGSGCRIECIFFSEFHPTLGPKITYQVPEDFISRELFDTVQVYIITKPELQNKLITVTAMEKKLIGCPVCIEHKKYSRNALLFNLGFVCDAQAKTCALEPIVKKLAGYLTTLELESSFVSMEESKQKLVPIMTILLEELNASGRCTLPIDESNTIHLKVIEQRPDPPVAQEYDVPVFTKDKEDFFNSQWDLTTQQILPYIDGFRHIQKISAEADVELNLVRIAIQNLLYYGVVTLVSILQYSNVYCPTPKVQDLVDDKSLQEACLSYVTKQGHKRASLRDVFQLYCSLSPGTTVRDLIGRHPQQLQHVDERKLIQFGLMKNLIRRLQKYPVRVTREEQSHPARLYTGCHSYDEICCKTGMSYHELDERLENDPNIIICWK", "text": "FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. FUNCTION: Suppresses Src-dependent tyrosine phosphorylation and activation of PDPK1 and its downstream signaling. Down-regulates PDPK1 kinase activity by interfering with tyrosine phosphorylation at 'Tyr- 9', 'Tyr-373' and 'Tyr-376' residues. May act as a tumor suppressor. Suppresses cell growth and enhances sensitivity to various anticancer drugs. SUBCELLULAR LOCATION: Lysosome membrane Note=Localization to lysosomes is amino acid-independent. SIMILARITY: Belongs to the NPR2 family."}
{"protein": "MAKLHDYYKSSVVAELTKQFSYTSVMQVPRIEKITLNMGVGEAINDKKLLENAASDMATISGQKPLITKARKSVAGFKIREGYPIGCKVTLRGERMWDFLERLINIALPRVRDFRGVSAKSFDGRGNYSMGVREQIIFPEIDFDKVDRVRGLDITITTSAGTDEEGRALLAAFNFPFRK", "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": "MIDPVLLREHPDVLRRSQEARGDSVQLVDEALQVDIERRAAITAFEELRAEQNAFGKRVAQAPKQEKKELVAQAQQLAGRVKEAQQVAAAAEARFESVLRKIGNPVVAGVPSGGEDDYAVLKEVGGIPAFGFEPRDHLALGELLGAIDMARGAKVSGARFSFLRGLGARLEIALMNLALDKALANGFVPLITPTLVKPEVMQGTGFLGEHSDEVYHLETDDLYLTGTSEVALAGYHADEILDVTEPLRYAGWSTCYRREAGSAGKDTRGIIRVHQFTKLEMFVYTLPEHAEAEHARLLAWQEEMMQALGLSYRVIDTAAGDLGSSAARKYDVEAWIPTQGRYRELTSTSNCGTFQARRLETRYRTESGKTAPVATLNGTLATTRWIVAILETHQREDGSVLVPETLRPYLGGLEILEPIGK", "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": "MSETHFGFEKVDESEKAGKVAGVFHSVASKYDVMNDLMSGGMHRLWKVFTIAQANVRPGQKVLDIAGGTGDLAKAFAKQAGPTGEVWLTDINESMLRVGRDRLLNKGVVTPVALCDAERIPFPDNYFDLVTVAFGLRNMTHKDAALAEMRRVIKPGGKVMVLEFSKVWKPLEKFYDVYSFKVLPWLGERVAGDAPSYRYLAESIRMHPDQGSLVRMMEQVGLEQVEYFNLTAGVVALHVGRKY", "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": "MSPLASKALRPAATDPASIRNFCIIAHIDHGKSTLADRMLQMTGVVDSRSMRAQYLDRMDIERERGITIKSQAVRMPWELDGQTYALNMIDTPGHVDFSYEVSRSLAACEGAILLVDAAQGIEAQTLANLYLALENDLTIIPVLNKIDLPAADPDKYAAELASLIGGDPSDVLRVSGKTGAGVEDLLDRVSRTIPAPVGDPDAAARAMIFDSVYDAYRGVVTYVRMIDGKLSPREKISMMSTRATHEILEIGVSSPEPTPSDGLGVGEVGYLITGVKDVRQSKVGDTVTTAARPATEALPGYTEPLPMVFSGLYPIDGSDYPDLRDALDKLKLSDAALVYEPETSVALGFGFRCGFLGLLHLEIITERLSREFGLDLITTAPSVIYEVTSEDKKTVTVTNPSEFPGGKIVSVSEPVVKAAILAPKDYVGTIMELCQSRRGILLGMEYLGEDRVEVRYTMPLGEIVFDFFDNLKSKTAGYASLDYEPAGSQDSDLVKVDILLQGEQVDAFSAIVHRDKAYAYGVLMTGRLRELIPRQQFEVPIQAAIGARIIARESIRAMRKDVLAKCYGGDITRKRKLLEKQKEGKKRMKMVGRVEVPQEAFIAALSGDTEKKAK", "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": "MDERLSLLRSPPPPSARHRAHPPQRPASSGGAHTLVNHGYAEPAAGRELPPDMTVVPGDHLLEPEVADGGGAPPQGGCGGGGCDRYEPLPPSLPAAGEQDCCGERVVINISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASTSQDSFEAAGNSTSGSRAGASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAERQGNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADDPTSGFSSIPDAFWWAVVTMTTVGYGDMHPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQSQYMHVGSCQHLSSSAEELRKARSNSTLSKSEYMVIEEGGMNHSAFPQTPFKTGNSTATCTTNNNPNSCVNIKKIFTDV", "text": "FUNCTION: Mediates the 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. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.3/KCNA3 sub-subfamily."}
{"protein": "MGIGRVTQVMGPVIDVRFEHNEVPKINNALVIDVPKEEGTIQLTLEVALQLGDDVVRTIAMDSTDGVQRGMDVKDTGKEISVPVGDETLGRVFNVLGETIDLKEEISDSVRRDPIHRQAPAFDELSTEVQILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYFEMSDSGVIKKTAMVFGQMNEPPGARMRVALSGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTTKGSVTSIQAVFVPADDYTDPAPATAFAHLDATTNLERKLTEMGIYPAVDPLASTSRALEPSIVGQEHYEVARDVQSTLQKYRELQDIIAILGMDELSDEDKQTVERARRIQFFLSQNFHVAEQFTGQKGSYVPVKTTVANFKDILDGKYDHIPEDAFRLVGSMDDVIAKAKDMGVEV", "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": "MIAAAASMSALGLGLGYLLGAAARKFHVETPPIVEEIAKILPGTNCGACGFPGCNGLAEAMAEGNAPVTACTPGGRDVALALAEIVTVEAGADAGPIAEIEPMVAFVFEDHCTGCQKCFKRCPTDAIVGGAKQIHTVVMDACIGCDACIEVCPTEAIVSRVKPKTLKTWYWDKPQPGLVAASAETAA", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required for nitrogen fixation. Stabilizes RnfC (PubMed:9154934). FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required for nitrogen fixation. Involved in electron transfer to nitrogenase (PubMed:8264535). SUBCELLULAR LOCATION: Cellular chromatophore membrane; Peripheral membrane protein; Cytoplasmic side. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily."}
{"protein": "MNRGRGVRKRNAPEKASILETCDEEIRAEVAQLFNKVRSYVPPAGEKWTLPDPNVVLCDPHVSHPRLQALKHSLNEVKNQLSDKDLSVWHQHTCFTNRAGTVTSHLRSTTNAELCTQAWAKFYEILGTFQLLPDSALKTGELNSIHLCEAPGAFISALNHFLKTSSLHCDWNWIANTLNPYYEANGRGCTITDDRLIVHTLPWWFFGSDNTGDIMLQKHLLELPRFVSNMRSVDLVTADGSFDCQGDPGEQERLVAPLQHCEAICALLLLGTGGSFVLKMFTLFEHSSVCLLYLLACCFRSVNIFKPGTSKSGNSELYIVCLDYQAKEQIRPLLSKLIRNYGPDLASTASLFPRRCIPDSFLSQHEEICTFFQALQVNTIQENLRLFVCMSTEQRRRLEQLREYAAEFYTKRFSVQYLPRKSWVCRGGVVRWVKVCERKQMGSLNQRKEMELQGWKQRLAQGNYGPFIEKHLVAAEGCEVVLNGPLDECDLGAWFALEGAALPKVCSSIFCDQEMLDFLNEALEGNLRVKTVNWSLKALPTCSSCSSDSPVSILSEICSHPDVTSCLVLGSQSWCDDKLTGVRIQPEFLQGPSYCGVQNVTMHDGQPDYQLELLNAVLFALQKQDQGSTLVIPLSSALTRFTSGLVFTLHLCFRYITFRCLSGWPPAALVCMGFSPPSALPSLLDFLQNVMEKMKKVELGRQVLQFVPLEELLRGELPHFLSSFNTAVIRQQLHMLIQLDQST", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG- capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYEEPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP", "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) (By similarity). 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 (PubMed:30842659). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842659). 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 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). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (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 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": "MDKTKALEGALSQIERAFGKGSIMRMGQRPKVETNVISTGSIGLDIALGIGGMPRGRIVEIYGPESSGKTTLALHVLAEAQKKGGTVAFIDAEHALDPGYARKLGVNIDDLLLSQPDAGEQALEIADTLVRSGAVDVLVVDSVAALVPRAELEGDMGDSHVGLHARLMSQALRKLTGTVSRSNTLVIFLNQIRMKIGVMFGNPETTTGGNALKFYSSIRLDIRRIGSIKDKDEVVGNQTRVKVVKNKMAPPFRQVEFDIMYGEGISKMGELLDLGVKGNIVEKSGAWFSFDSQRIGQGRENAKQFLREHPEMASEIERRIRAEAGVLSDALMTDPEPDADGTPED", "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": "MTVPKFKKFKIEAYKPGKSNIAKIRNIIKLSANESALGVSPRVKKILQNKKLLISKYPDGKAKNLRKEISKKFKCDFERIICGAGSDEIIQMICQLYLKPSDEVIVPQYSFLMYRIYAQIVGAKVVFSKEKNFKVSINEIIKKVTRKTKLVFIANPNNPTGTYLTRAELIDLRKKLNKNILLVLDDAYFEYMKNKDYKSGLDLFKNKDNVVVIRTFSKIYGLASLRVGWGHGPKKIISAMNLIRPPFNVNQVAQMAAIEALKDRKFINNSVKHNIREANKVRNALQKLKILSNEVTANFLLLNFDRCKFSANYIFNKLQSKGIILRSTEDGYNIKNKLRLTIGSTKENMRFITTIKAIFN", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
{"protein": "MKLGFEIQRALQGLLNKAAVDGGAYGHLIQHFTRHRLPLHVLQLHARIVVFSIKPDNFLASKLISFYTRQDRFRQALHVFDEITVRNAFSYNALLIAYTSREMYFDAFSLFLSWIGSSCYSSDAARPDSISISCVLKALSGCDDFWLGSLARQVHGFVIRGGFDSDVFVGNGMITYYTKCDNIESARKVFDEMSERDVVSWNSMISGYSQSGSFEDCKKMYKAMLACSDFKPNGVTVISVFQACGQSSDLIFGLEVHKKMIENHIQMDLSLCNAVIGFYAKCGSLDYARALFDEMSEKDSVTYGAIISGYMAHGLVKEAMALFSEMESIGLSTWNAMISGLMQNNHHEEVINSFREMIRCGSRPNTVTLSSLLPSLTYSSNLKGGKEIHAFAIRNGADNNIYVTTSIIDNYAKLGFLLGAQRVFDNCKDRSLIAWTAIITAYAVHGDSDSACSLFDQMQCLGTKPDDVTLTAVLSAFAHSGDSDMAQHIFDSMLTKYDIEPGVEHYACMVSVLSRAGKLSDAMEFISKMPIDPIAKVWGALLNGASVLGDLEIARFACDRLFEMEPENTGNYTIMANLYTQAGRWEEAEMVRNKMKRIGLKKIPGTSWIETEKGLRSFIAKDSSCERSKEMYEIIEGLVESMSDKEYIRKQELDEAY", "text": "SIMILARITY: Belongs to the PPR family. PCMP-E subfamily."}
{"protein": "MRLNTLSPAAGSNPSKKRVGRGIGSGLGKTGGRGHKGQKSRSGGKVRVGFEGGQMPLKQRLPKFGFTSRKSLVTAEVRLSELAKVEGNVIDLNSLKAANVITKNIVFAKVVLSGEIATAVTVKGLRVTKGAKAAIEAAGGKIEE", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKAEPMDTDDNSNCPGQNEQQRESSGHRRDQIIEKDAALCVLIDEMNERP", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 7 family."}
{"protein": "MSLVVMATGGTGGHIYPAVATAKELRGRGYEVALMGQKGGMEEGIAEREGLTFYGVDAGKLARSGQGRPDPRQLLKAGQGLAQARRTLAGLNPAAVVGYGGFASLPGVLAAQSLGIPTILHEQNARLGLTQRLAVRRARAVGTAYDKVIGLDPRKATLVGMPVREERMPRAEALAALGLRDGPITIMVMGGSQGSLYLNQQVPGILWRLFGKVGKLRGKGDSVPPIDLDLRGPHLIENARSREVQVLHATGPRWLAEVQPKVENLPWYHVTGYVDAVAAWSVADLGITRAGTGTLAEAAFHGVPLVMVPLPESAENHQYHNAVAVEQAGAGRVVEQKVLPETLEKVVLECAAPGKRAAMRDAAQKRARPGAAARFADLIEVQLRRAPSPTAHAPTAHD", "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": "MKYVLVSGGVISGIGKGVIASSTGLLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGEVFVLNDGGEVDLDLGNYERYLNVTLTHDNNITTGKVYSNVIQKERRGDYLGKTVQIVPHVTNEIQDWVERVARIPVDQSGEEPDVCIVELGGTVGDIESAAFVEAMRQFQFRVGHENFVSIHVSLVPVINGEQKTKPTQQAIRDLRSLGITPDLIACRCKQPLEKSVIDKISLFCHVGPEQVLAVHDVSSTYHVPQLLEDKLLEYLKIRFALDKISVSRELALAGENMWSSWKHLTQGYDHLFKKVTIVLVGKYTHLQDSYISVIKALEHSAMRCGRKLDLQWVEASHLEASTNTSDPLSYHKAWHLVCSANGILVPGGFGSRGVEGMIAAAKWARENNTPYLGICLGMQVAVIEFARSVCGIEGAFSEEFDKECENNVVVYMPEIDKDKLGGTMRLGLRPTFFQPNSEWSKLRKLHKMVDEVLERHRHRYEINPAFVSRLEQGGISFIGKDERGERMEIIEKRDHPYFVGVQYHPEYLSKPLKPSPPIFGLVAASAGLLDEFIQSGEEVEWSNFSHFNAESALADMNDSVEVTEEATVVTIS", "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": "MGVHPQLNKNGELQHLLTTEGLPAVILRHILDTAESFTGVTERDVKKIPLLRGKSVFNLFFEPSTRTRTTFEIAAKRLSADVINLNMAVSSQTKGETLLDTVDNLSAMHADMFIVRHNQSGAAHLIARHVRPEIHVINAGDGWHAHPTQALLDMFTIRRYKQDFHALRVAIIGDILHSRVARSQIHALTTLGVPEIRVIAPKTLLPAKVERLGVHVYHNMVQGLQDVDVLMMLRLQHERMESAHLPSTEEYFKYYGLTPEKLALARSDAIVMHPGPMNRGVEIDSEVADGTQSVILPQVNFGIAVRMAVMSILAGN", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
{"protein": "MNPTKRNSHAIVEFVDVLLRDGAVIQADAIVTVAGVPLLGISLRAAIAGMTTMTEYGIFDGWDADHRRRNAQP", "text": "FUNCTION: Gas vesicles are small, hollow, gas filled protein structures that are found in several microbial planktonic microorganisms. They allow the positioning of the organism at the favorable depth for growth. This protein could be important for the shape determination of the gas vesicle. SUBCELLULAR LOCATION: Gas vesicle. SIMILARITY: Belongs to the gas vesicle protein type A family."}
{"protein": "MTSPIVTLKSVEQQQDLIITPPTTGLSLTGKITIPGDKSISHRALMLGAIAQGETIIKGLLLGEDPHSTAKCFRAMGAEISPLNTDKIIVKGIGLGNLQEPVDVLDAGNSGTTMRLMLGLLASHPERFFTVTGDSSLRSRPMSRVIKPLQQMGAQIWGRKQNSLAPLAISGQSLQPIHYHSPIASAQVKSCILLAGLSVEGKTTVTEPALSRDHSERMLKAFGANLEIDPQTHSVTVMGPSRLTGQTVIVPGDISSAAFWLVAGSIVPGSDLLIENVGINPTRTGILEVLEMMGADLTLLNQREITGEPVADIRVKHSQLKACTISGDIVPRLIDEIPILAVAAVFAQGTTVIRDAQELRVKESDRLAVMACELNQMGAKITELPDGLEITGPVSLKGSQVDSYTDHRIAMSLAIAALNASHSTTIHRAQAAAVSYPEFITTLQQLCQ", "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": "MMDKRLVKISKTLSMLLRHHPEKLGLVLDQYGRTDWKTLVRRFNAHYQMHLDRQVLQAIMAQSTKKRFALEGTTIRAVYGHSVPVMPLTPATEPPQWLYHGTSHQAATVIAKEGLLPMNRDFVHLSEDVATARQVGARHDTHPVIYRIAARDAAKNGILFYPTSSRVWLVSELPARFLHHLTSYFRRP", "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": "MSEKLIIIVGPTAVGKSALGIKVAKKINGEIISGDSMQVYKYMDIGTAKVLPEEREGVPHHLIDILEPFQKYSVALFQKEARRLIKEINERGKIPIIVGGTGLYIRSVIDPYDFTDFSFDPVFRGKLEQAAKEKGSSYLHQMLEKIDPVAAQKIHSNDLRRIIRALEVYEHTGKPISYYWERGKQSKPQYRLLYYGLTMDRALLYQRINERVDKMIEKGLIAEVKRLLQMGFKESTAMQALGYKEIVQYLEGKITLDEAIYLIKRDTRRFAKRQLTWFRRDPRIKWFDSGKESLEKITEKIITEAGVNNFL", "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": "MAVPKKRTSKSKTNLRKTVWKKKALKQAIQAYFIASRASKKLNLEKAITKDLNTES", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "MAGEIPDLVAQERTGTGKGAARQARRDGMVPGIVFGGDVDPLPINIPFNVLIKKLREGRFKSTLFNMKVEGHDDVRVICRDVQRHVVKDLPTHIDFMRLKRTTKINLFIAVEVEGEDVAPGLKKGGVLTLIRPEVELIVTAGDIPDHVTIDISEMEIGDNITISSVNLPEGAKPTIDRDFVIAQLSAPAGLVSSDDEEEEDGAEEAIEATEE", "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": "MARIAGVDIPKNKRGVIALTYIFGVGRSRAIEVLEKAQVSQDKKVQDWNDDEIGGIREAVSFYKIEGELRSEVSLNIKRLMDIGCYRGIRHRSGLPLRGQRTKNNSRTRKGKRKTVANKKKATK", "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": "MSAVMITRKITRKWEKLPGKNTFCCDGRVMMARQKGVFYLTLFLIVGTCSLFFAFECPYLAVHLSPAIPVFAVLLFVFVMAMLLRTSFSDPGVLPRALPEEANFIEMEIEAANGNVLAGQRPPPRIKNVQINNQIVKLKYCYTCKIFRPPRASHCSICDNCVDRFDHHCPWVGNCVGKRNYRYFYLFTLSLSLLTIYIFAFDIVHVVLRSVDSGFVNTLKETPGTVLEVLVCFFTLWSVVGLTGFHTYLISLNQTTNEDIKGSWSGKNRVQNPYSHKNIIKNCCEVLCGPTYPSVLDRRGLMLEDSCSSAPSNGATTVPVNKSSNPATQTTKSSAPLIPNEHTPDEAKPSICSGTQKSSSSPKEEKPSSPISPNAVAPAVIKESTH", "text": "FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily."}
{"protein": "MSSATDFDPKPRRSSVAVDVGGVIVGGGAPVVVQSMTNTDTADIDSTVAQVAALFKAGSELVRITVDRDESAAAVPKIRERLLRLGMDVPLIGDFHYIGHKLLADHPACAEALAKYRINPGNVGFKDKKDKQFAEIIEMAIRYDKPVRIGVNWGSLDQDLLTALMDQNSAAGSPLSARQVTRETIVQSALISADLAEEIGLPRNRIILSAKVSQVQDLIAVYSMLSERSNHALHLGLTEAGMGSKGIVASSAAMGYVLQHGIGDTVRVSLTPEPNGDRTREVQVAQELLQVMGFRQFVPVVAACPGCGRTTSTVFQELAQNIQNDLRKNMPVWRDKYPGVEALNVAVMGCIVNGPGESKHADIGISLPGTGESPAAPVFIDGQKAMTLRGPNIASDFEALVADYIEKRFGQKSVAAE", "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": "MSKDFILAVDQGTTSSRAIIFDKKGNIRKIAQKEFTQIYPKSGWVEHDAMEIWGTQSGVMREALEFGRVKPDQIAAIGITNQRETVVVWDKETGDPVYNAIVWQCRRTSSICDEIKRDPQFVKYIKENTGLVVDAYFSGTKVKWILDNVEGAREKANAGKLLMGTIDTWLIWNLTRGKVHATDYSNASRTMLFNINSLEWDKKILDYLNIPESMLPEVKNSSEVFGVTDSHTLGGAEIPIAGVAGDQHAALFGHCCFEKGMAKNTYGTGCFALMNVGDKPVYSDEGLLTTIAWAENGKPTYALEGSVFIAGAVIQWIRDGLGLVRSAEDSEYYATKIDSTNGVYLVPAFVGLGTPYWDMYARGTIVGITRDTKREHIIRAALEAIAYQAKDVLECMKEDTGLDLAGLRVDGGAVQNNFLMQFQSDILQSEISKPKVNEITGLGAVFLAGLAVGFWKDKQELKSILTTEKVFEPQKDSQAVAHDYRGWKKAVERSKAWAECYS", "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": "MTKSKPATKKNEWTVKDSCSLYGLDLWGEEYFSINDSGNVTVSPQGKEGNSLELTHLLEELKGRNLNTPLLLRFDDILEDRLKKLHQAFENAINQYGYNNDYQGVFPIKCNQQRHVVEEIVTIGRKWHFGLEAGSKAELLIALALVNDPKAFLICNGYKDNRYIETTILARQLGRQPIVVIEQSDEVGRIIKASQKLGAAPLIGIRAKLSNQSSGRWGNSVGEKSKFGLSIPEILKAVQELTAAGLLNELILLHFHVGSQINDIAILKNALQEASQIYVELNRLGAPMGHLDVGGGLGVDYDGSRTATSASTNYSLQNYANDVVATIQECCKAKKVKVPKLISESGRFLSSHFSILIFNVLGTSSVPTQIAIETSNECLSVKNLRETLMILHQICEEKKIDVSKLQEAWNDALKFKEDALNAFRLGFIDLTERATAEQLTWACAKQIAAHLPNDLKIPKELLAINKGLTETYYANISIFRSAPDTWAIQQLFPLLPIHRLQEKPDQLGHFADLTCDSDGKLARFINNGQEKFLLELHTVKANENYWIGMFLGGAYQEVMGNLHNLFGSTNAIHIRLTKNGKYKLDHVVRGNSKSDVLQAMEHDSEQLLERIRMASESAIQQGSLKINDAQRLIEHVETSLRQSTYLQE", "text": "FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily."}
{"protein": "MHPSSRANGPAPHKPYNPFYLQLYFWVIIAIILGALLGHCYPAVGQQLKPLGDAFIKLVKMIISPVIFLTIVTGIASVAHVGTVARVFGKAMVYFLFFSTLALLLGLVVAHVVHPGAGMNINPVDLHQGEIANYVEKSHDLTLVGFLMDIIPKTLLSPFVGDNILQVLFVAVLFGIALALAGERGKPVLNLLDALTVPVFKLVQMLMKMAPIGAFGAIAFTIGKYGVDSLVNLGWLVGSFYLTSLLFVLVILGAVSWLCGFSILKLIRYLKAELLLVLGTSSSESALPSLMEKMVQAGCRKSVVGLVVPTGYSFNLDGTNIYMTLAALFIAQATNTELTPAHQLALFLVAMLSSKGAAGVSGAGFITLAATLAVVPEVPIAGMALILGVDRFMSECRSLTNFIGNAVATLVVSRWENALNHEQLKIALDGNEAAYQSLHAKDAEPSLSR", "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": "MGKNKTAYVCQECGYKSVKWLGKCPSCGEWNTLVEEFEPQSFSLVKKEPSLVLPVTDWEKEEHERETTGFESLDNALGGGLVKGQVILIAGEPGIGKSTLLLQISDRVANGKKVLYVSGEESGTQIALRAKRLGINNENLLVYPEVNLEKILQTLEKEKPSLLVLDSVQTIFSERLESSAGSVSQVREVTYRITEFCKEKNVPAFIVGQITKEGSIAGPKVLEHIVDTVLQFEGERFNFYRIVKVIKNRFGSTGEIAVFKMTDKGLEEVPEPSAFFISEKANAPGSVVFPHTEGSKPVLLEVQALVIPALYTTPQRRTQGFDPNRLALILAVLEKEAKIFTRDQDVFVNVAGGMSVKEPAADLAVAMAVVSSKKEKEVPKDFVIFGEVGLSGEIRAVHFGDLRLKEAKRFGFKKALIPKSLEIEIDGMEIYPVSHIQEAIEVLF", "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": "MRVKGIMRNCQHLWIWGTMLFGMWMICSAVEQLWVTVYYGVPVWKEATTTLFCASDAKAYSTEAHNVWATHACVPTDPNPQEVILGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDKNITDWKNTTIIGGGEVKNCSFNITTSRRDKVHKEYALFYKLDVVPIKGDNNSSRYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENFTDNAKTIIVHLNESVEINCTRPYNNVRRSLSIGPGRAFRTREIIGIIRQAHCNISRAKWNNTLKQIVEKLREQFKNKTIVFNHSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWNGTDIKGDNKNSTLITLPCRIKQIINMWQGVGKAMYAPPIQGQIRCSSNITGLLLTRDGGNSSSREEIFRPGGGNMRDNWRSELYKYKVVRIEPLGVAPTKAKRRVVQREKRAVGTIGAMFLGFLGAAGSTMGAGSLTLTVQARQLLSGIVQQQNNLLRAIDAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNASWSNKSMNQIWDNLTWMEWEREIDNYTSIIYSLIEESQNQQGKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLIGLRIVFTVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSVRLVHGFLALIWDDLRSLCLFSYHRLRDLLLIVKRIVELLGRRGWEALKYWWNLLQYWSKELKNSAVGLLNAIAIAVAEGTDRVIEVVQRICRAIIHIPRRIRQGLERALL", "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": "MTKLTVLLLAILVLLPLATSNSAADEALASLSGLLRRAKRCVPQNSCTSNADCCGSYTCSCVSQPSCKGMNPRRRCM", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MQEFMNFEECSKQNTNNCKQHEKNIDENNCSCKEKKVQSKKVSSDHSSSEDNASSDINSNKAETLTLNCGDQSDNKNSISDIESNKFIPNENDFQMLKKQLNDLKAENVNLKRDLQEAHQQRTNDNLKYLADFDNFKKRITVQTNREIKYALTDFIKNILIPLEQFEKVLEMPKVDDSVKSFLLGFKMIHKQVKDILQKEGVEEIKALGVKFDPNFHYALEKISDLKQPNGINVLVLQKGFLYKDLVIKPAMVKVNEWSDKNND", "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": "MLTYQVKQGDTLNSIAADFRISTAALLQANPSLQAGLTAGQSIVIPGLPDPYTIPYHIAVSIGAKTLTLSLNNRVMKTYPIAVGKILTQTPTGEFYIINRQRNPGGPFGAYWLSLSKQHYGIHGTNNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTINR", "text": "FUNCTION: Probable enzyme that may play an important role in cell wall biology. SUBCELLULAR LOCATION: Spore wall Note=Probably localized either on the surface of the outer spore membrane and/or in the inner spore coat. SIMILARITY: Belongs to the YkuD family."}
{"protein": "MRVILLGAPGAGKGTQAQFIKEQFNIPQISTGDMLRAAVKAGTPLGLEAKKVMDAGGLVSDDIILGLVKERITENDCANGFLFDGFPRTIPQAQSLVEQGVDIDFVVEIDVDDEEIIERLSGRRVHPASGRVYHTKYNPPKVEGKDDETGDELVQRDDDQEETVRKRLEVYQAQTRPLVDFYQDLATQGESNAPRYVRVAGVGSVDDIRDRVLSALKG", "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": "MKRIAMLAAACVIAVPAFAQNVATVNGKPITQKSLDEFVKLVVSQGATDSPQLREQIKQEMINRQVFVQAAEKDGVAKQADVQTEIELARQGILVRALMADYLQKHPVTDAQVKAEYEKIKKEQAGKMEYKVRHILVEDEKTANDLLAQVKSNKSKFDDLAKKNSKDPGSAERGGDLGWAPATNYVQPFAEAVTKLKKGQLVDKPVQTQFGWHVIQVDDTRPVEFPAMDQVRPQLEEMLRQQTLANYQKQLREQAKIQ", "text": "SIMILARITY: Belongs to the PpiC/parvulin rotamase family."}
{"protein": "MSTIAESARIHPMAVVEDGAVIGEGVKIGPFCHVGPHVVLHENVELLSHAVVAGRTVIGKGTRIFPMAVIGGDPQSVHHGGEETTLSVGANCTMREGVTMNTGTADFGGQTIVGDNNLFLANSHVAHDCKVGNHVIMSNNVMLAGHVVIEDRVILGGGSAVHQFTRVGRQAFVGGLSAVSYDVIPYGMLNGNPGLLSGLNVVGMTRAGVDRAVIHRVRRAYKSIFEGTGSVRENAAAIRDEYADCEQAVQILDFIAADSDRALSSPTRGQKG", "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": "MKASELQGKDQAALTKELNDLLKAQFGLRMQIATQQLNNTSQLKKVRRDIARVKTVMNQKDAK", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MSSALDEDTQQTIAAGRETAGAMLRAAQKDLQKVFIVFLVGFLGTFYALRLYVWEFFRGVTKAQMDASVSGNVSIIAQTPFDVILLQAKIGLVVGVLFALPPFIYVSRGALKARDAWPKSPVAPWKLALIGLTMVALFAAGVAYGYFVFFPFTFAFLAQNAISAGFTPSYSIVKWAQFIFLLTLSFGLASQLPLAMTGLSYAEVVPYELFRDKWRHAIVGIFAFGALFTPPDPFTQIMWAVPVILLYAFSLYLARVVVTAKRGSEKIDVKSTATTHWNLLAGVGVVVGLLVYAFYEYGGVELANDGLAAIGSDYVFLAPGSGVALGAFVVAGGFVGLAFGLAYLVYRDIERLERTEIGVGDPTKLDLSALDVAGVRAAPPEAFADLEEDEVMALASAAIDDGDKAKAQALIDRFDEAEADREAEAADAEDEPGELEDRTTRAGGAFVSELTEGETDEDDIGGYYTDIAFIVDSLTSRAFWVVGWFMLVLATTFGWLYTGGIRDVYDDFLGRLPAAVRPEEVLNVVALHPMEALIFEVKFSTILAVLATLPLVAYFVWPALRERNIIRKRRRTVFVWTGALAGGLLGGFALGYTYVAPTVITFLVEDALAANMIITYRITNFFWLIFFTTAGIGLLADVPILMVLLNTAGISYRMMRNRWREVTVFILAISAVFTPASITTMFMVTLPLMAAYGVGLGVLFVLTVGGRRDLSPARGAAE", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family."}
{"protein": "MGMRPPSGLPSLSRRSRVLLVAAVVLAALLLLGPRFTDAYTNWLWFGEVGFREVFLTVVVTRIILFAAVALFVGATVWLALLLAYRTRPVFVPMAGPNDPIARYRTTVMSRLKTFGIGIPVLLGLLAGLVAQSNWVTVQLFLNGGDFGEQDPQFHLDVGFYAFDLPFYRMVLNWMFVAVVIAFFASLVTHYIFGGLRLSGREGTLTRPARIQLAVIAGLFVLLKAVAYWFDRYDLLSSSRKEPTFYGGSFTDINAVLPAKLILLAIAVICAVAFFAGVVLRDLRVPAMAAALLVLSSVLVGAVYPLVVEQFSVRPNAADKESEYIERNIAATRQAFGITSDKIEYKDYKGESDKNPLDVPVDAATIGNARLLDPNILSPTFTQLRQLKNFYGFPESLDIDRYNLDGNLQDYIVAARELSPAALTGNQTDWINKHTVYTHGNGFVAAPANRVNKPQSEDVAAGGSSDSGYPIFLVSDLFTPKDRQRIPVEQPRIYFGELISQSDPDYAIVGGAEGQAPREYDSDTAQYTYTGKGGVPIGNWFNRLAFAAKYAERNILFSSAIGDDSKIIFNRSPRERVQKVAPWLTTDGNAYPAVVDERIVWIVDAYTTLDNYPYAQKTSLEGAVEDSIDKKTGRLLPRKEVSYIRNSVKATVDAYDGTVTLYEVDSTDPVLKAWRGVFPGAVKPESEISPELRAHFRYPEDLFKVQREMLTKYHVDNPREFFTNNAFWSVPSDPTIEGGSFNQPPYYVLLGDPKTNRPVFNLTSAMVGYNRQFLSAYISVRSDPDDYGKFTILRLPTDTQTQGPQQTQNTMTTAPQVSQEKTLLSNSNKIRYGNLLTLPIADGGILYVEPFYNERNTGPNTATFPQLLRVLVSYRDQAGSVKVGYASTLAEALNQVLPGAGSLATPFGGDPATRPQPGTAPPVVDSTQPPADGGTPQPQTTPPPTGSAAKDAAAAELDRKIEAVRNAMRSGNFQDFGKALEELEAAVKTYQDAGR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0182 family."}
{"protein": "MAELSSDFDLAPYIEHSLLDPAATLEQIDQLCQEADRYHFAAVCLFPWVVRQAREWLNGRSPRLCTVIDFPNGASTAASKVYAAQEAVENGAQELNVVVNLGWLRSDRADLVHQELAEIVEATGVPIKAILEATRLNPSELEQLTDLCLDAGVTMLQTSTGWFGGATPALVQQLRQLTRNRVGIHAAGGIRTWDQAAALVEAGAIRLGTSYGPMILQQRLAASTPAPA", "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": "MKKIRWVILIIVLIACVILWTQTINVMCDQDVQFFSGICAINQFIPW", "text": "FUNCTION: PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing. MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Represses PhoP/PhoQ signaling, possibly by binding to the periplasmic domain of PhoQ, altering its activity and that of downstream effector PhoP. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MgrB family."}
{"protein": "MGRGRVEMKRIENKINRQVTFSKRRAGLLKKAHEISILCDAEVSLIVFSHKGKLFEYSSESCMEKVLERYERYSYAEKQLKAPDSHVNAQTNWSMEYSRLKAKIELWERNQRHYLGEDLESISIKELQNLEQQLDTSLKHIPSRKVCK", "text": "FUNCTION: Probable transcription factor that promotes early floral meristem identity in synergy with APETALA1, FRUITFULL and LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Seems to be partially redundant to the function of APETALA1 (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MALLGTYNHTLDDKGRLTIPSKMREQFKDDKVFISLGFDGCVDVRNEAEWLKWTEKVASTGQATAEGRALTRKIMSMSDETTFDNAGRIKISSILQNKANITKDVVIIGNNDHLELWDLKVWEVYIEQAPGIEEAAKNFEEKI", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family."}
{"protein": "MQPSGWAAAREAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELLQSSGDNHKRAWDLVSWILSSKVLTIHSAGKAEFEKIQKLTGAPHTPVPAPDFLFEIEYFDPANAKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSLFGEGTYLTSDLSLALIYSPHGHGWQHSLLGPILSCVAVCEVIDHPDVKCQTKKKDSKEIDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQKPPKRASSQLSWFSSHWFTVMISLYLLLLLIVSVINSSAFQHFWNRAKR", "text": "FUNCTION: Intracellular mono-ADP-ribosyltransferase that plays a role in different processes, such as protein translation and unfolded protein response (UPR), through the mono-ADP-ribosylation of proteins involved in those processes (PubMed:22701565, PubMed:23103912, PubMed:25043379, PubMed:34314702). Acts as an inhibitor of protein translation by catalyzing mono-ADP-ribosylation of ribosomal subunits, such as RPL14 and RPS6, thereby inhibiting polysome assembly and mRNA loading (PubMed:34314702). Mono-ADP-ribosylation of ribosomal subunits is promoted by NMNAT2 (PubMed:34314702). Involved in the unfolded protein response (UPR) by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors (PubMed:23103912). May also mediate mono-ADP-ribosylation of karyopherin KPNB1 a nuclear import factor (PubMed:22701565). May not modify proteins on arginine or cysteine residues compared to other mono-ADP-ribosyltransferases (PubMed:22701565). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the ARTD/PARP family."}
{"protein": "GLPICGETCVGGTCNTPGCSCSWPVCTRN", "text": "FUNCTION: Probably participates in a plant defense mechanism. FUNCTION: Probably participates in a plant defense mechanism. Has cytotoxic activity against human lymphoma U-937 GTB and human myeloma RPMI-8226/s cell lines. SIMILARITY: Belongs to the cyclotide family. Moebius subfamily."}
{"protein": "MSQIDENIRYGGAANETDGEDAQRKAQEREAKKAEVRKRLEEAGQKKQKKGFLTPERKKKLRKLLMNKAAEDLKTQQLRKEQERVKVLAERTVALPNVDSIDDHAKLEAIYNDLFSRLCNLEEEKYDINHITTETETTINQLNIEVNDLRGKFVKPSLKKVSKYDNKFKKMAEAKKEDGSKNLRNNLKTVKKESVFTQIANKKKSDKPEWSKKKEEKKEESAPEPVIEPVEEEETAASEGEEEEEEADEE", "text": "FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to muscle actomyosin ATPase activity. SIMILARITY: Belongs to the troponin I family."}
{"protein": "MSQQMTLSVQKREGLGKGANRKLRTAKKVPGIFYNSEGKNIPVAIDGTQLEKLYETAGKTTVFNLDIEGETAPCLIWQIERHPYKPFFTHVDLFGVDMEKPIKARIPLKITGVAKGTKIGGRMEVYRDFVDVFTKPGSMPKVIDINVSNMEMGDAVHVADLKLEDGHCIYDSNYVIVRVSAPRGGKGEEGEDA", "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": "MKNESTFIDVPADSSSAMKGKAPLIGVAKDHTASGSGGYNRGLSIFDFLLRLAAIVAASVAAGTMFTSDETLPFFTQFLQFEAGYDDLPTFQFFVIAMSLVSGYIVLSLPISVVTIVRPLAAAPRLLLLVLDTAVMGLTMAAASSAAAISYVAHNGNQNTNWLPICQQFFDFCQKTSGAVVSSFVAVVFFMILVVLSGVALERH", "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": "MRHGKKINHLSRQTGHRKAMLANMACSLIEHKRINTTVAKAKALKQFVEPLITKSKEDTTHNRRIVFAYLRSKYAVTDLFRDVAAKVGDRPGGYTRIIKVGNRLGDNADMAMIELVDFNELYNGGKKEVKKAKSRRGGKAKKAEGTAPEAPAAESESTTEASE", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MNNRRFDCIGIVGHPRHPAALATHEILYHWLKARGYAVMVEQQIAHDLNLTDAITGSLADIGQKADLAVVVGGDGNMLGAARVLARYDIKVIGVNRGNLGFLTDLDPDNALQQLSDVLEGEYLSEQRFLLETHVRRTNQQSRISTAINEVVLHPGKVAHMIEFEVYIDDRFAFSQRSDGLIIATPTGSTAYSLSAGGPILTPTLDAIVLVPMFPHTLTARPLVISSSSTIRLKFSHITSDLEISCDSQIALPIQEGEEVLIRRSDFHLNLIHPKDYSYFNTLSTKLGWSKKLF", "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": "MLTSWRTISLLQKTTSRFIKRSKTYADVRYNSQALQNHGVPGNKRKWMKRFVFVGAAGIGVYAWDRVYNAHALTRSIRTVYTASIIAADYKLNFSEKKADKIDALHQRVAQRLFKTIYKNGGLYIKMGQIIAMQSNNLPEAYGKAFQGMFDNAPQVEWEELQDIFKEQYGRPVEEVFASIEKRAAASASIAQVHRAVLPSGEKVAVKIQKPDVAKQMSWDLLVYKYMMYVYDKWIFHIPLYFTVDYVSERLRSEVDFTTEANNSEHAREGVEETDYLRDKIYIPKVYKEISGKRVMVTEWADGIPLYDQTALSEAGMSKKEILTNLFRFLAFQMFHSKQVHCDPHPGNILVRKNQAGLCQTVILDHGLYVFESEKFRKEFALLFTAAYSLDKKSILQVMDAWGIGQPELFANRMLNIPMDEEQPHTGEKIISKKEAFQQQLAERKKFIGFLQDCTRLPKELLMLGRCLMLIQKNNQNFGYPVNSIAVMAKVADKYTTDKPSPTWYQRLLSPIFWVFQHLFYPGNFRLPELTNDKK", "text": "SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein kinase family."}
{"protein": "MGQKINPIGLRVGIIRDWEAKWYAEKDFASLLHEDLKIRKFIDNELKEASVSHVEIERAANRINIAIHTGKPGMVIGKGGSEIEKLRNKLNALTDKKVHINVIEIKKVDLDARLVAENIARQLENRASFRRVQKQAITRAMKLGAKGIKTQVSGRLGGADIARAEQYSEGTVPLHTLRADIDYAHAEADTTYGKLGVKVWIYRGEVLPTKNTSGGGK", "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": "MAEAITYADLRFVKAPLKKSISSRLGQDPGADDDGEITYENVQVPAVLGVPSSLASSVLGDKAAVKSEQPTASWRAVTSPAVGRILPCRTTCLRYLLLGLLLTCLLLGVTAICLGVRYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQQRRALEQKLSNMENRLKPFFTCGSADTCCPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATFSEIYPQSHSYYFLNSLLPNGGSGNSYWTGLSSNKDWKLTDDTQRTRTYAQSSKCNKVHKTWSWWTLESESCRSSLPYICEMTAFRFPD", "text": "FUNCTION: Plays a role in B-cell proliferation and differentiation. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein."}
{"protein": "MNSLDFDRKPEDTRVVVAMSGGVDSSVVAGLLKREGYDVLGITLQLYDHGAAVHRAGSCCAGQDIDDARRVCETIGIPHYVLDYEARFRETVINPFAESYIAGETPIPCVACNQTVKFADLLATAKELGADALATGHYIRSRPSPKPRYAGQRALYRPADAERDQSYFLFATTQEQIDYLRFPLGGLPKSETRALAEEMGLVVAKKADSQDICFVPQGKYSDIVSKLKPNAALAGEIVHLDGRVLGAHEGILHYTIGQRRGIGVATGEPLYVVYLDSRSRRVIVGPKEALETRRVYLRDVNWLGDEELEAAAGQGFECFAKVRSTRRPAPAVLKSDAEGLYVELVEGEAGVAPGQACALYSGTGEDARVYGGGFIRRSEREPAAEAALKALLQAPAAA", "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": "MARAVGIDLGTTNSCIATLEGGEPTVIVNAEGARTTPSVVAFSKSGEILVGEVAKRQAVTNVDRTISSVKRHMGTDWTVDIDGKKWTPQEISAQILMKLKRDAEAYLGEPVTDAVITCPAYFNDAQRQATKDAGKIAGLNVLRIINEPTAAALAYGLEKGKEDERILVFDLGGGTFDVSLLEIGKDDDGFSTIQVQATNGDNHLGGDDWDQKIIDWLVSEVKNKYGVDLSKDKIALQRLKEAAEQAKKELSSSTSTSISMQYLAMTPDGTPVHLDETLTRAHFEEMTSDLLGRCRTPFNNVLHDAGISVSDIDHVVLVGGSTRMPAVKDLVKELTGGKEANQSVNPDEVVAVGAAVQSGVIKGDRKDVLLIDVTPLSLGIETKGGIMTKLIDRNTAIPTKRSEVFSTAEDNQPSVLIQVYQGEREFARDNKPLGTFELTGIAPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSMTITGGSGLPKDEIDRMVKEAEAHEAEDKQRKEDAETRNQAEAFAYSTEKLVNDNKDKLSDDIVKEVTDKVNALKEALKGDDTEKVKTAQTELMTAAQKIGQVLYAQQGAEGAAAGAGAAGAAGAGASAGSASGSDDDTVEAEVVDDDDDKDNK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MKPSIILYKALPDDLLHRLEEHFTVTQVPNLRPETVEQHAQAFASAEGLLGSSETVNSALLEKMPKLRAASTVSVGYDNFDVAALNARSVLLMHTPTVLTETVADTVMALVLSTARRVVEVAERVKVGEWTKSIGPDWFGTDVHHKTLGIVGMGRIGLALAQRAHFGFNMPILYNARRHHPEAEERFNARYCDLDTLLQAADFVCLILPLTEETHHLFGAAQFAKMKSSAIFINAGRGPVVDETALIAALQSGEIHAAGLDVFEQEPLPVDSPLLSLPNVVALPHIGSATHETRYNMAACAVDNLIDALQGKVEKNCVNPQVAG", "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": "MNQETKALFQTLTQLPGAPGNEHQVRAFMKQELAKYADDIVQDRLGSVFGVRRGAEDAPRIMVAGHMDEVGFMVTSITDNGLLRFQTLGGWWSQVLLAQRVEIQTDNGPVPGVISSIPPHLLTDAQRNRPMDIKNMMIDIGADDKEDAIKIGIRPGQQIVPVCPFTTMANEKKILSKAWDNRYGCGLSIELLKELHGKELPNTLYAGATVQEEVGLRGAQTASHMIKPDLFFALDASPANDMSGDKNEFGQLGKGFLLRILDRTTVMHRGMREFVLDMAETHDIPYQYFVSGGGTDAGKVHISNSGVPSAVIGICSRYIHTNATIIHIDDYAAAKEMLIKLVTACDKQTVDAIKENM", "text": "SIMILARITY: Belongs to the peptidase M42 family."}
{"protein": "MTTVLLDSHVAYWWSAEPQRLSMAASQAIEHADELAVAAISWFELAWLAEQERIQLAIPVLSWLQQLAEHVRTVGITPSVAATAVALPSSFPGDPADRLIYATAIEHGWRLVTKDRRLRSHRHPRPVTVW", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits translation and colony formation. Its toxic effect on colony formation is neutralized by coexpression with cognate antitoxin VapB22; the effect on translation has not been tested but is probably neutralized also. SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient starvation. SIMILARITY: Belongs to the PINc/VapC protein family."}
{"protein": "MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAIAEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGNSNGGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLAPCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIELSMIVCVIASTIPGISMNPIIAIAQDTLF", "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": "MAKEKFERNKPHCNIGTIGHVDHGKTTLTAAITIILAKSGGATAKNYADIDAAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPALVVYMNKVDLVDDEELLELVEMEVRELLSSYDFPGDDIPITKGSAKVAIDGGDPVIGEQSILALMTTVDAYIPQPDRPIDLPFLMPVEDVFSISGRGTVVTGRIEKGVVKVGEEVEIVGIRAVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQFYFRTTDVTGIIKLREGVEMIMPGDNAELDVELITPIAMDQGLRFAIREGGRTVGAGVVAKIVE", "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": "MPLEMDQKVNKLTFGCQRSSTSDDDSGCAMEEYTWVPPGLRPEQVQLYFACLPEEKIPYVNSIGEKYRIKQLLYQLPPHDNEVRYCQSLCEEEKKELQMFSGQRKKEALGRGNIKMLSRAVMHAMCEKCGEKINGGEIAIFVSRAGPGVCWHPSCFVCSTCNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMNHFCCYECETVLGGQRYIMKDGRPFCCGCFESHYAEYCESCGDHIGVDHAQMTYDGQHWHATETCFSCAQCKVSLLGCPFLPKKGRIYCSKACSLGEDVHASDSSDSAFQSARSRESRRSVRMGKSSRSADQCRQSLLLSPALNYKFPGMSGNADDTLSRKMDDLGISRQGAGFDNDFWKARDEQETPEDHEEWAEHDDYMTQLLLKFGEKGLFQQPSEDNRSTEHWMSENIKGKNDLQRNNRNKSLASKKYQSDMYWTQSQDGLGDSAYGSHPGPASSRKLQELDMDHGASAYMHEKMPWYKRSLECLSDNLKPQNENIRDSMDSLALSNITGASVDGENKSRPSLFCYQNFQDLNTRDCEKMSNMGTLNSSMLNRSTESLKSLTSEICQEKPPPEEKPMHTSALRRSKSQTRPQVKFSDDVIDNGDYGSIEIRQPPMSERSRRRVYNFEERSQRPHHHRRRKSRKSRSENALHLATDSKPSGKERNRFYTAEDYERLFHNKSAHQVQAYIQNADLFGQYSNAASNVGLPSKVAGKFLGLYGEDEDSWCSTCSSSSSDSEEEGYFLGQPIPKPRPQRYQYFSDDLCSPTNALSSSQFSQRTTKSKKKKGHKGKNCIIS", "text": "FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization along the apical/basal axis of epithelial cells. Regulates the polarized assembly of fibronectrin on the surface of the mesoderm during gastrulation. Essential for gastrulation cell movements, cooperating with dvl2/dsh to activate jnk. Acts together with tes to control axial elongation. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the prickle / espinas / testin family."}
{"protein": "MISPFIVNDKNLFLSRFPVSQVNRSLQAWDSADEYLINHVHDQNLINAQTKVAIFNDAFGALAVNFCQSTSENPEVISINDSYISSEGASYNIEQNSLDDSHFTQLNSLDSLPNNIDVILYKIPKSKSLLIEQLIQIKKSVNENCIFIAADRAKEIHSSTLKVFEKHLGTTKTSLAVKKARLVFCQFDNKQVHQSPFPTVWSIPHKSTNDLPSRELTISNHANVYAREKLDIGARYFIENLPTVAANSTVIDLGCGNGVIGLTVLANQPEAHVQFIDESTMAISSAKQNIMTNLPDVIEQCEFTLNDSLTDIEGGSVDLILCNPPFHQNTATTDHIAWQMFKDSHRVLKKGGELRIIGNQKLAYHIKLQRLFGNETLIASNDKFVTQSAIKR", "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": "MENDAGENVDLYVPRKCSASNRIIHAKDHASVQLSIVDVDPETGRQTDGSKTYAICGEIRRMGESDDCIVRLAKKDGLITKNF", "text": "FUNCTION: May be an associated component of the ribosome rather than a core structural subunit. May act as a translation initiation factor. Has a role in regulation of cell proliferation in the hematopoietic organs and the imaginal disks of larva (By similarity). 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": "MPREIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINSIQNSEYRNLYNHENVFVADHGGGAGNNWASGYHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNQMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHIPNPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLVASLIPTPRCHFLMTGYTPLTVERQANAIRKTTVLDVMRRLLQAKNIMVSSYARTKEASQAKYISILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPYVQTAHRVSGLMLASHTSIRHLFSKCISQYEKLRKKQAFLDNYRKFPMFADNDLSEFDESREIVQNLVDEYKACESADYIKWGMEDRGKQVSGEGNTSGTVDSRVGAS", "text": "FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles, suggesting that it is involved in the minus-end nucleation of microtubule assembly. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center. SIMILARITY: Belongs to the tubulin family."}
{"protein": "MCEHNLLNSGYVGSLLNFTSPEPFYFANLRPNGTQLATLSPALSYTRRDVCSLPWTSSPCASPPQSRAFSGYSQSYLSNSVSISINRHVSDKAAAGEEPNKYYFQDSSRKVEERCRHNQSYPSDASIPSSVNINPAKYEYPNVETSLHGSSLHNQGFELNSNSPTVNDGIKQSVSLSMSLQSSVTPVCNRSSDGLPWCPTQVRSRRKRKPYTKQQIAELENEFLANEFINRQKRKELSDRLNLSDQQVKIWFQNRRMKKKRLVMREQTLSLF", "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": "MSDFVDRVTVHVKGGDGGNGSAGIRREKYKPLAGPNGGNGGDGGSVVFVADRNATSLLDYRFMPHRVAGSGTMGLGDNKDGSKGEDLILPVPCGTVVFEARGEQGKAKHPGAQLADLRHEGDRCVVAQGGAGGLGNIALANKTRRAPGFALLGELGEERDVILELKSIADVALVGFPSAGKSSLIAAMSSAKPKIADYPFTTLVPNLGVVIAGDSRYTIADVPGLIPGASEGKGLGLEFLRHIERTEIIAHVIDCATLEPDRDPMSDYHALENELALYADKLELPLGAIPIPERPRIVILNKIDVPEAKELAEFVRPEFERLGLKVFEISTASHEGLKELNFALSALVHEMREEVANREQAEEEARVVIKPLETKGRRPRRADEGGSALEFTVERRELGNGEVFFEVRGVKPERWVMQTNFDNDEAVGYLADRLAKLGVEDELRRKGAHPGDEVRIGRGARMVEFDWDPTISAGAEMLDGSNLGARGKDLRLEEQDPRTHRRSNAERRAQYHEMMDARAAVRDAMMAERKAGHWADPTVDDDRHDENSLFGHGESSEDGETEE", "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": "MTLIHMNILMAFSMSLVGLLMYRSHLMSALLCLEGMMLSLFVLATLTILSSHFTLANMMPIILLVFAACEAAIGLALLVMVSNTYGTDYVQNLNLLQC", "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": "MLPRNATDKIQGNVSKPCFWKSLSPGQNWKSKSMRSFPEEFVKSTPGAFEHRVVFSVRWGNSWQLWLEREEKDLFMIEEDWDEFVDDNHLGPNDNVFFRHDDKMFLEVQIFKNDGNEIIDAPPEVEPETEPFHPTTPKNSHKETTTASASASASEFSDNWRETHGCADIKNPELYLLNPKNPYFVKTLTKGNDVLYVPKTVIKKYGLKFGPHLSPMHYLLPGDKINGSTKIYGGGSAPCFNGWVDLCRKYNLKTGDSMVCELERSGELVTAVRVHFINKT", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAVQIENLGSLDRKMTLEFARADLAKAREARLAKVGKSMKMAGFRPGKVPKNLVEKQHGMQVDFELQFDKAAELFYELAQKEGVALAGQPRLEPKSEIDAEKVVFDAFFEVLPEVKIGDFSKAEVTKYTTDIGEAEIDRALDALRKQQVHYHPRGEAGPHGDGGSNTAAQNGDQVVINFVGKIDGVEFAGGKAENFECVLGEGRMLPEFEAATLGLKVGESKSFPLSFPADYHGKDVAGKTAEFTITVKSVNWAHLPVVDDAFALSLGVTEGGVTKMRAEVKENLDREVKRRVTTLLKSEVMDKLNSLCELDVPKSLVASEQERLVEGARQDLMQRGVPNAKDAPIPAEIFAEQATKRVRLGLILSELVKNQNLIATADQIKAEIDEQATTYEDPKEVIRWFYRNPGRLKDIENLVLEDNVIKYFTSQAKVNDKSVTFEELSKLN", "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": "AKSGRASCKKCGDNIAKESLGLAIMVQSPMFDGKVPHWHHYSCFWKRARVLSQGDIYGYTELRWEDQEMIKKAIETGGAAAGAGGDSKGGKGEMTLNDFAAEYAKSNRSACKGCEQKIEKGQIRISKKSVDVERPQLGMIDRWYHPDCFVSSREELDFLPSYSASQLKGFTILSAEDKDSLKKKLPAVKNEGKRKADEVDGHSAATKKKIKKEKEKESKLEKLLKEQTELIWHIKDELKKVCSTNDLKELLIANKQQVPSGETNIVDRVSDGMAFGALLPCEECSGQFVFKGDAYYCTGDLSAWTKCVAKTQTPNRKDWVTPKEFHEIPYLKKFKFKRHDRAFPPCAAPTPISPPAAPEPKPTVEETFPEGKPLTNTKVLLIGKLSKNKDEVKTLIEGLGGKVAGSAHKANLCISTNKEVKKMSKKMEEVKAANVRVVSDDFLKEVESGKSVQELLSQFGISSWGAEIKQEAVQPTEKQPSSGPVAGKSSGKVKEEKGSNKSEKKMKLTVKGGAAIDPDSELEDSCHVLETGGKIFSATLGLVDITRGTNSYYKLQLIEHDRDSRYWVFRSWGRVGTVIGSKKLEEMSSKEDAIEHFLNLYQDKTGNAWHSPNFTKYPKKFYPLEIDYGQEEDVVKKLSVGAGTKSKLAKPVQELIKLIFDVESMKKAMVEFEIDLQKMPLGKLSKRQIQSAYSILSQVQQAVSESLSEARLLDLSNQFYTLIPHDFGMKKPPLLNNLEYIQAKVQMLDNLLDIEVAYSLLRGGADDGEKDPIDVKYEKIKTDIKVVAKDSEESRIICDYVKNTHADTHNAYDLEVLEIFKIDREGEYQRYKPFKQLHNRQLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHAMPGSPIGLILLGEVALGNMHELKAASQITKLPKGKHSVKGLGRTAPDPSATVQLDGVDVPLGKGTSANISDTSLLYNEYIVYDIAQVNLKYLLKLKFNYKGGMMW", "text": "FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP- ribosylation of proteins and plays a key role in DNA repair (By similarity). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Specificity for the different amino acids is conferred by interacting factors, such as hpf1 and nmnat1 (By similarity). Following interaction with hpf1, catalyzes serine ADP-ribosylation of target proteins; hpf1 confers serine specificity by completing the parp1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with hpf1 (By similarity). Following interaction with nmnat1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; nmnat1 confers glutamate and aspartate specificity (By similarity). Parp1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits hpf1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair. Mediates the poly-ADP-ribosylation of a number of proteins. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (By similarity). Parp1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (By similarity). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II. Acts both as a positive and negative regulator of transcription elongation, depending on the context (By similarity). Poly-ADP-ribose chains generated by parp1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos. Also acts as a negative regulator of the cGAS-STING pathway by mediating poly-ADP-ribosylation and inactivation of cgas. Acts as a negative regulator of adipogenesis by catalyzing poly ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) (By similarity). SUBCELLULAR LOCATION: Chromosome Nucleus Nucleus, nucleolus Cytoplasm, cytosol Note=Localizes to sites of DNA damage. Recognizes (via PARP-type zinc-fingers) and binds DNA strand breaks. Also binds normal/undamaged chromatin. Auto poly-ADP-ribosylation promotes dissociation from chromatin. SIMILARITY: Belongs to the ARTD/PARP family."}
{"protein": "MREVVSIHVGQAGVQIGNACWELYTIEHGLSPDGRLSDDSPSKHDDGFSTFFSETSSGKYVPRSLYVDLEPNVIDEVRNGPYRSLFHPETMITGKEDAASNYARGHYTIGKEQIDVVMDKVRRLVDNCNGLQGFFVFHSFGGGTGSGFGALILERLSTDYGKKSKLEFSVYPAPTLASSVVEPYNSVLTTHTTLEHSDCSFMVDNEAIYDICKKNLNIAQPGLTNLNRLIAQVVSSITASLRFDGSLNVDLNEFQTNLVPFPRIHFPLATLAPIVSVDKAGHESNSVAEMTYSCFEPGNQMVKCDPRDGKYMACALLYRGDVVPKDTNAAVALIKTKRTIQFVDWCPTGFKLGICNEPPAHVPGGDLAKVKRSMCMLSNTTAISSAWSRLDHKFDLLYSKRAFVHWYVGEGMEEGEFSEARQDLAALEKDYEEVGMDSADAEEEAAEY", "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": "MTQISRQQYADLYGPTIGDKIRLGDSDLYVEIEKDLRATYGDELQYGGGKTLRDGMGSENFLTQEAGCLDLVITNVTVIDAIQGVVKADVGIRNGRIVGLGKAGNPSTMDGVTRGLVTGASTDAISGEHLILTAGGMDTHVHYIAPQQVEAALSNGITTLWGGGIGPVDGTNGVTTTNGPWNLEMMLRSIEGLPINFGIQGKGNSTGIAPLIEHLEAGAAGFKVHEDYGATPAAIRACLSVADEYDVSVAVHTDTLNESGYVEDTIAAFDGRSVHTYHSEGAGGGHAPDLLKVVGQNNILPSSTNPTLPCGKNSVAELFDMIMVCHNLNPKIPSDVAFAESRVRAETIVAESVLHDMGAISMIGSDSQAMGRIGETFLRAIQTADAMKKARGPLPEDAPGNDNFRVLRYIAKVTINPALTAGVGDVIGSIESGKFADLVLWEPAFFGVKPKLVLKGGLVAWANMGDPNASLPTPQPMYYRPMFAAYGSALQKTSITFVSRAAYDKGVADRFGLQRLVMPVSGTRVIGKAHMVRNSYLPNIEVDPQTFAVKVDGVHATVKPPQSISLNQLYFFS", "text": "FUNCTION: Disrupting the ure2 operon has no effect on urease activity, or pathogen survival in BALB/c mice when inoculated by gavage, but confers slightly enhanced resistance to low pH killing in vitro. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "MSKPPSDPPRRPPAAFTYEDEATERHDNGRQAERRRKPESFSENIVVTADEDDPFLNPDKDLSAVPVATPLRRRTSFGKIAAGAFGILLSLGIGLWTDSLIRDLFTRADWLGYLALAVLAVGVLAVLALVIRETSGMMRLAAVQAIKAEAEAAMVETRPAKARAVVARLVTLLSANPETSKGRATLKATEGEVIDPPHLIALAERELLTPLDRKARALIVNASKRVSLVTAVSPRAVVDLLYVLYEAVRLIRAMAELYGGRPGTLGMFRLLRDVLAHLAVTGSIAVGDSLVQQVLGHGLASKLSARLGEGVINGLMTARIGIAAMDLCRPLAFHALKRPGIGDFIGDLTPSMSPRGNTP", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0283 family."}
{"protein": "MFFSKDLPSPTSVFTAYASMAGYMMMIRSMAHELIPAPLQDFIYRTLRSLFFRSSSSTLTLTIDDDNMGMNNEIYRAAQTYLSTKISPDAVRLRISKGHKDKHVNLYLSDGEIVNDVYEDVQLVWRFVTDGGDKKGGGGGVGGRGGGGGRRGGMDDDGKSEYFELSFDKKHKDLILNSYVPYIESKAKEIRDERRILMLHSLNSLRWESVILEHPSTFETMAMEDDLKRDVIEDLDRFIRRKEFYKRVGKAWKRGYLLYGPPGTGKSSLVAAMANYLKFDVYDLQLASVMRDSDLRRLLLATRNRSILVIEDIDCAVDLPNRIEQPVEGKNRGESQGPLTLSGLLNFIDGLWSSCGDERIIIFTTNHKDRLDPALLRPGRMDMHIYMGHCSFQGFKTLASNYLGLSDAAMPHRLFPEIERLIDGEVMTPAQVAEELMKSEDADVALEGLVNVLEKMRLKSKESNPVMMKQKESRLEMEEMRLKSDTEGSPRKNSKRFKKLVLFWT", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily."}
{"protein": "MSKEPNFPPSEKLEKVEAPADLRSIAGFEWWRRTFEYKTGLGLTPEAKVQYEKDYQYVLQREQCKQCYDNRDWLLKYSPTVVFMTQQIAKLNRRRTGDDSLHFDTSKIICDVCPEWKSGGFNPSLGILLCQNRIRDKWQMEDTLSHELVHQFDELKFEVDWMNLKHHACSEVRASNLSGECRLSQEFFRRGFNGSFGRGHQECVRRRAVLSVMGNPKCKDKAEAEQIVDEVWQSCFNDTRPFEEIYR", "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": "MEAKAILRTARISPQKARLVADQVRGLSAERAVNLLKFSDKKAAHLIKKVVESAIANAENNQGADVDELKVKTIMVDEGPSLKRFMARAKGRGTRILKRTSHITVIVGAAK", "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": "MNALLSNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASQPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTAEQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDTMLYSDALDQRLAMFKSGKNGPRIKGSY", "text": "FUNCTION: Catalyzes the reversible retro-aldol cleavage of 2-keto-3- deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde. 2-keto-3-deoxy- L-mannonate, 2-keto-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7- dioate (HKHD) are also reasonably good substrates, although 2-keto-3- deoxy-L-rhamnonate is likely to be the physiological substrate. 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. SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDR aldolase subfamily."}
{"protein": "MKKVRIGAVVAEFNYDITHMMLELAKEHARFLDAEITRVIAVPGVFDMPLAVKKLLLEDEIDAVITLGAVIEGATDHDQIVVQHASRKIADLALDYDKPVALGISGPGMTRLEAHQRVDYAKRAVEAAVKMYRRLKEDI", "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": "MSRRRAHDTEDESYDHRRNKRRRVSENQEIEDRLESLILRVGERSTSSVESNLEGLVSVLEADLGTFRLKILRILSDCAVRMPEKCTVYTTLVGLLNAKNYKFGGEFVDHMVKTFKESLKLCRWDAARYSLRFLADLVNCHVISATSLLQLLDTMIDVSNEDTVPQVRRDWFVFAVLSTLPWVGRDLYEKKESSLESLLLRIEVYLNKRSKKHHNALRVWTSDAPHPQEEYLDCLWAQIRKLRQDNWAEKHIPRPYLVFDSILCEALQHNLPQITPPPHHDNFEYPMPWVVYRMFDYTDCPDGPNLPGAHSIERFLIEEHLHHIIETHHRERKDCAAQLLNFPFKHKIPLEYCIVEVIFAELFHMPTPRYLDICYGSILIELCKLQPGTLPQVLAQATEILFMRIDSMNTSCFDRFVNWFSYHLSNFKFTWSWDEWDSCLLLDAEHPRPKFIQEVLLKCLRLSYHQRITEMMPTTYAKLIPVTPVPNYKYTSEEAANLPGTTVALQLVGAIRQKCTPEEVVNILKEIPSSGYSGEEMSDGSFNALKIDVFVQTLLNLGSKSFSHSFAAISKFHVVFRALAETEEAQICILHNIFELWSSHQQMMVVLIDKLLKLQIVDCSAVATWIFSKEMTGEFTKMYLWEILHLTIKKMNKHVIKLNVELSDAKEKLSKADSSSSDTDEDTPHKRKKPITHADKPSEEVVERMEEKLEAANVNQKRLFLIVFQRFIMILSEHLLRSDTDGRDPDTDWYRWTIGRLQQVFLMHHEQVQKYSSTLETLLFTSDLDTHILEVFQQFVALRA", "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": "MIVTQDKALANVFRQMATGAFPPVVETFERNKTIFFPGDPAERVYFLLKGAVKLSRVYEAGEEITVALLRENSVFGVLSLLTGNKSDRFYHAVAFTPVELLSAPIEQVEQALKENPELSMLMLRGLSSRILQTEMMIETLAHRDMGSRLVSFLLILCRDFGVPCADGITIDLKLSHQAIAEAIGSTRVTVTRLLGDLREKKMISIHKKKITVHKPVTLSRQFT", "text": "FUNCTION: Has affinity for the xisA upstream region. Binds to a 66 bp region containing three repeats of the consensus recognition sequence 5'-ACATT-3'. FUNCTION: Required for full expression of proteins subject to ammonium repression. Transcriptional activator of genes subject to nitrogen control."}
{"protein": "MKCLLLALGLALMCGIQATNIPQTMQDLDLQEVAGKWHSVAMAASDISLLDSESAPLRVYIEKLRPTPEDNLEIILREGENKGCAEKKIFAEKTESPAEFKINYLDEDTVFALDTDYKNYLFLCMKNAATPGQSLVCQYLARTQMVDEEIMEKFRRALQPLPGRVQIVPDLTRMAERCRI", "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": "MSEKQVFSTEWAGKTLSVEVGQLAKQASGAALIRYGDTVVLTAAVGSKKPRPGDFFPLTVNYEEKMYSVGKVPGGFLKREGRPSDRATLTARLIDRPIRPLFAEGFRNEVQITSTVFSVDQDCSPEMAAMLGSSVALVISDIPFEGPIAGVDVGRIDGKYVINPTIEQAEKSDISLTVAGTYDAINMVEAGAKEVSEEAMLEAIMFGHEEIKRLCEFQQQIIAAVGKEKREIELFVSDPELEAEVKAASEGKMKAAIKTEEKKAREAAIEDVKEEILESYKAKELENEAEILSEVAHILEMIEKDEMRRLISQDKIRPDGRKVNEIRPLSSEVGMLPRVHGSGLFTRGQTQALSVCTLAPLREHQIIDGLGTEEYKRFMHHYNFPQFSVGETGPRRAPGRREIGHGALGERALQYVIPSEEEFPYTIRLVSEVLESNGSSSQASICGSTLAMLDAGVPIKAPVAGIAMGLVKLGDDYTILSDIQGMEDHFGDMDFKVAGTKDGITALQMDIKIDGLSRQILDEALTQAKEGRLHILEHLTSTISAPREELSAYAPKIITLNIKPEKIKDVIGPGGKQINAIIDETGVKIDIEQDGTVYIASQDQAMNRKAIAIIEDIVREVEVGEVYTGKVRRIEKFGAFVELFKGTDGLVHISELAHERVGKVEDILKLGDEVTVKVIEVDQQGRVNLSRKALLEKKEQPEGDKKPQAEKKFYPKTKKPESK", "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": "MGKIIGIDLGTTNSCVAVMDGDKARVIENAEGARTTPSIIAYTDNETLVGQPAKRQAITNPKNTLFAIKRLIGRRFESEEVQRDIKIMPFEITRADNGDAWVNVKGDKLAPPQISAEVLKKMKKTAEDFLGEAVTEAVITVPAYFNDAQRQATIDAGRIAGLDVKRIINEPTAAALAFGLGSTKENQVIAVYDLGGGTFDISIIEIDNFDGEQTFEVLATGGNTHLGGEDFDNRVIDYIIDEFKKEQGVDLRNDPMALQRVKEAAEKAKIELSSAQSTEVNLPYITADATGPKHLAINVTRAKLEALVEDLVASSIESLKTVLKDAGKSVNEINDIILVGGQTRMPLVQQKVAEFFGKEARKDVNPDEAVAIGAAVQGGVLKGDVKDVLLLDVTPLSLGIETMGGVMTVLIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKQASANKSLGQFNLEGINPAPRGMPQIEVTFDIDANGVINVSAKDKNTGKEQQIRIQASSGLSDEEIEQMVRDAEANAEADKKFEELVQARNQADGIAHATRKQIEEAGDALNADDKAKIEAAIADLEKAAKGDDKAEIDAKTEALIKASEPLMQAAQAKAQQAGGEQPQAKKDDGVVDAEFEEVKDNK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MTLPSGHPKSRLIKKFTALGPYIREGKCEDNRFFFDCLAVCVNVKPAPEVREFWGWWMELEAQESRFTYSYQFGLFDKAGDWTSVRIKDAEVVERLEHTLREFHEKLRELLATLNLKLEPADDFRDEPVKLTA", "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": "VGCEECPAHCKGKNAIPTCDDGVCNCNV", "text": "FUNCTION: Calcium channel activator. Rapidly and reversibly activates ryanodine receptor 1 (RYR1). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 09 subfamily."}
{"protein": "MARIAGINIPDKKHAVIALTSIYGIGRTTALDICAKTGVSAAVKISELSEKQIEELREQVAKYTVEGDLRREVTLNIKRLMDIGTYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK", "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": "MVEWTDSERAIINSIFSNLDYEEIGRKSLCRCLIVYPWTQRYFGGFGNLYNAETILCNPLIAAHGTKILHGLDRALKNMDDIKNTYAELSLLHSDKLHVDPDNFRLLADCLTGVIAAKMVPAFTVDTQVGWQKFRSFVVSALGREYH", "text": "FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
{"protein": "MFDRLSVLEDRYMQLNEMLADPEVLSDSTKLRQYSKEQAQLEETVQMYRQYKETSQAFKEAKSMLEDRTLDAEMRELAKEEMNLLEPEVKELEAKLRILLLPKDPNDEKNVIVEVRGAAGGDEAALFAGDLYKMYTRFAERQNWKVELIDANYTELGGFKEVTFMINGAGAYSKLKFENGAHRVQRVPSTESGGRIHTSTATVAVLPEAEDVEVHIDMKDVRVDTFTSSGPGGQSVNTTQSAVRLTHIPSGLVVSCQDEKSQHKNKDKAMKVLRARLYDKMQSEHMEELSAQRKSAVGTGDRSERIRTYNFPQSRVTDHRIGLTLQKLDRVLAGELEDIIDALIMDEQARLMEDAE", "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": "MTNRLALSGTVCRAPLRKVSPSGIPHCQFVLEHRSVQEEAGFHRQAWCQMPVIVSGHENQAITHSITVGSRITVQGFISCHKAKNGLSKMVLHAEQIELIDSGD", "text": "FUNCTION: Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT. SIMILARITY: Belongs to the PriB family."}
{"protein": "MISTEGIKDLEAVDIEKLLSILPHRYPFLLIDRIVNIDGEQEAIGIKNITINEPHFTGHFPTKPVMPGVLILEAMAQTAGAIALLNLGNKRTNLVYLMTVDNAKFRKPVMPGDQLKIHVQLLKKRSGMRRFSCVAKVENVRVAEAEIAAMIVEEE", "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": "MLSPCLAAPATECRDPADAPAAPARHTGPARPRKRRPRNWKPHLPRERLLERGPAALTDAELIALLLGTGGGGRDVFASARALLARFGDSLRDMLDAEPDVFATHPGIGTARSAVLIAVTEIVRRALVEKARERLQIDSPGAVEDYLRLRIGTRPHEVFVTLYLDARHGLIDVEESARGSLTRMAVYPREIVRRALVLNAAALIIAHNHPSGAVQPSAEDRRLTRVLHEALALIDAKLLDHVVVGTADTFSFARAGWL", "text": "SIMILARITY: Belongs to the UPF0758 family."}
{"protein": "MLKINVKKQLGQLALEANLQIPARGVTALFGLSGSGKTSLINLVSGLVHPDEGYISLNERVLVDQSKAVCIPAYQRHIGYVFQDARLFPHYTVKGNLCYGIKKIDLAKFDDIVSLLGIGHLLKRYPITLSGGEKQRVAIGRALLTQPEILLMDEPLSALDLPRKRELMSYLETLSKKIDIPILYVTHSIEELLRLAEYVVLLDEGKVRAFDRLESIWENPLFLPWKLEDEQSAVLSLPILHNNTGYQVTALGLQQQQIWIKAQQAEVGENIRICIKGSDVSLSLTQPEKTSIRNILHGKVKRIVERENRVDVQIEIDEKPIWATISKWALEDLALQLGQPVFAQIKAVSVL", "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": "MKKSYRVKKEKDFKALFDAGHSVANRKFVVYCLDRNLPHFRVGLSVSKRLGNAVTRNRVKRRLRHALMDMSSQLENQDFVVIARKGVEDLSYQDIYSNLVHVLKIAKLYKD", "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": "MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN", "text": "FUNCTION: Isoform 4 acts as a translational repressor for GLI1. FUNCTION: Isoform 1 is involved in regulation of mRNA splicing of MAG pre-mRNA by acting as a negative regulator of MAG exon 12 alternative splicing. FUNCTION: Isoform 3 can induce apoptosis, while heterodimerization with other isoforms results in nuclear translocation of isoform 3 and suppression of apoptosis. FUNCTION: RNA-binding protein that plays a central role in myelinization (PubMed:16641098). Binds to the 5'-NACUAAY-N(1,20)-UAAY- 3' RNA core sequence. Regulates target mRNA stability (PubMed:23630077). In addition, acts by regulating pre-mRNA splicing, mRNA export and protein translation. Required to protect and promote stability of mRNAs such as MBP and CDKN1B. Regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia (PubMed:16641098). Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor (By similarity). FUNCTION: RNA-binding protein that plays a central role in myelinization (PubMed:10864952, PubMed:11917126). Also required for visceral endoderm function and blood vessel development (PubMed:11892011, PubMed:16470614). Binds to the 5'-NACUAAY-N(1,20)- UAAY-3' RNA core sequence (PubMed:16041388). Acts by regulating pre- mRNA splicing, mRNA export, mRNA stability and protein translation, as well as cellular processes including apoptosis, cell cycle, glial cell fate and development (PubMed:10535969, PubMed:12467586, PubMed:11297509, PubMed:11917126, PubMed:15568022). Required to protect and promote stability of mRNAs such as MBP and CDKN1B which promotes oligodendrocyte differentiation (PubMed:10535969, PubMed:15568022). Participates in mRNA transport by regulating the nuclear export of MBP mRNA (PubMed:12467586). May also play a role in smooth muscle development (PubMed:14706070). FUNCTION: RNA-binding protein that plays a central role in myelinization. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Acts by regulating pre-mRNA splicing, mRNA export, mRNA stability and protein translation. Required to protect and promote stability of mRNAs such as MBP and CDKN1B which promotes oligodendrocyte differentiation. Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. Note=Isoform 1 localizes predominantly in the nucleus and at lower levels in cytoplasm. It shuttles between the cytoplasm and the nucleus. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus. Note=Isoform 3 localizes predominantly in the cytoplasm and at much lower levels in nucleus. SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=Isoform 4 localizes both in the cytoplasm and nucleus. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MANSVYVKFEVPKEIADKVYEALEIARDTGKIGKGTNEVTKNIERNNVALAVIAEDIEPAEIVAHLPILAEEKEIPYVYLPTKEELGEAAGLNVGTASACIIDAGEGQELVDEIVEKVAELKN", "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": "MKNTQRQLSSSFMKFLEEKNRDLEAVFAYMDANRDGRISAEELKKSFKTLGEQMSDEEAEAAVKLSDIDGDGMLDINEFALLIKGNDEFTEEEKKRKIMEAFRMYIADGEDCITPGSLKMMLMKLGESRTTDDCKVMIQAFDLNADGVLSFDEFALMMR", "text": "FUNCTION: Potential calcium sensor that binds calcium in vitro."}
{"protein": "MNNEILTLQVGKTGILTGNEFWKSLVREKNLLSDFSLGKNSPTNDNVFFEESNESFFIPRTIIFDLSERDFNYIMKSNYSKMYDKNRHFILNKNTGNSWLKGYYEGISNCNLVDNILRKRIEKMNSVKYFNVFNSINGGTGAGLSSYLIEYIRNNYPKSFINCCSIFPDLYGNTQVTFQPYNSVLSIAWQGLYCDSNIFFQNHAIENLLTKNQINNELSFRKVNYIIGKTISIIMNTLNHNFTLETLISPLIVNPYLNLFFSTINIDILLSKLRKKRPSMIENKTNQLNEISMNLDLKSGNYLSSIELSNRNFYKLFANSIYDKIFYDQTRFYSQLLNQYDSVIINNNVKKENYSSLTYLLNHTSFNPVIKKIIQNFELLKKRNAFLEYYCGEILLDEANTLFRESKDYILDIINNYDNILSYY", "text": "FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. SIMILARITY: Belongs to the tubulin family."}
{"protein": "MVMTDPIADLLTRIRNANKARHPKVDMPSSKLKLEILKVMKQEGFIKDFSVNKDKFPKITVTLKYSDTNERVIKGLKRISKPGLRVYASIDNLPRVLNGLGVALVSTSKGILTDREARQQQIGGEVLAYVW", "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": "MAITVYYDKDCDLNLIKSKKVAIIGFGSQGHAHAMNLRDNGVNVIIGLREGSVSAVKAKNAGFEVMSVSEASKTADVVMILAPDEIQADIFNVEIKPNLSEGKAIAFAHGFNIHYGQIVAPKGIDVIMIAPKAPGHTVRNEFTLGGGTPCLIAIHQDESKNAKNLALSYASAIGGGRTGIIETTFKAETETDLFGEQAVLCGGLSALIQAGFETLVEAGYEPEMAYFECLHEMKLIVDLIYQGGIADMRYSISNTAEYGDYITGPKIVTEETKKAMKGVLKDIQNGVFAKDFILERRAGFARMHAERKNMNDSLIEKTGRNLRAMMPWISAKKLVDKDKN", "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": "MNVTLLIPARYGSSRFPGKPLAPINGKPMIQHVYERASLAKGLTNIYVATDDDRIKAAVEGFGGKVVMTSPDAASGTDRINDAINQLGLKDDDLVINLQGDQPLIDPTSIEQVISLFERHPGEFEMATLGFEIVNKAELDDPMHVKMVFDNNNYALYFSRSRIPFGRDTQDYPVYKHLGVYAYTRKFVQAFAALPLGRLEDLEKLEQLRALEYGHKIKIAISAFDSIEVDTPEDIRKCEQRLAVD", "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": "MTPAELKRLYHIIKVQLEYGLDELMPEHQLTKAPLLARKSLFWLKNKHQDKELGHRLRLALQELGPVWIKFGQMMSTRRDLFPPHIADQLALLQDQVAPFDGQLAKRDMEKALGGRLDNWFTDFDIEPLASASIAQVHTAKLKESGREIVLKVIRPDIRPVIDADLKLMHRMARIVAKSLPEARRLKPVEVVHEYEKTLLDELDLRREAANAIQLRRNFEGSEELYVPEVIPDLSSETLMVSERIYGIQVSDIETLEANGTNMKLLAERGVTVFFTQVFRDSFFHADMHPGNVFVNPENPDNPQWIGLDCGIVGTLNSEDKRYLAENLLAFFNRDYRKVAELHVDSGWVPHDTNVNDFEFAIRMVCEPIFAKPLGEISFGHVLLNLFNTARRFNMEVQPQLVLLQKTLLYVEGLGRQLYPQLDLWATAKPFLETWMMNQVGPQAVINAVKERAPFWAEKLPELPELLYDSLRQGKAMNHRMDQLYQGYRDSKRQQATGKFLFGVGATLVVCSAILVSSPYEQLSMGCGIAGVTFWLLSWRAYRR", "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": "MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQFGQ", "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. FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane (PubMed:8809774, PubMed:9575204, PubMed:12119303, PubMed:15304478, PubMed:28869968). Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:12119303). Shows ATPase activity (PubMed:12119303, PubMed:18024585, PubMed:18344567, PubMed:19132955, PubMed:20412049, PubMed:21462989). May transport glycerophospholipids (PubMed:9575204). In proteoliposomes, mediates the ATP-dependent flipping of a variety of phospholipid and glycolipid derivatives (PubMed:20412049). May also function as a multidrug transporter (PubMed:19132955). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. 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": "MESDEAAAVSPQATTPSGGTGASGPKKRGRKPKTKEDSQTPSSQQQSDVKMKESGKKTQQSPSVDEKYSQWKGLVPILYDWLANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVKPRVAAAEHISQFNEEARSPFVKKYKTIIHPGEVNRIRELPQNSKIVATHTDSPDVLIWDVETQPNRHAVLGAANSRPDLILTGHQDNAEFALAMCPTEPFVLSGGKDKSVVLWSIQDHITTIGTDSKSSGSIIKQTGEGTDKNESPTVGPRGVYHGHEDTVEDVAFSPTSAQEFCSVGDDSCLILWDARTGTNPVTKVEKAHDADLHCVDWNPHDDNLILTGSADNTVRLFDRRKLTANGVGSPIYKFEGHKAAVLCVQWSPDKSSVFGSSAEDGLLNIWDYDRVSKKSDRAAKSPAGLFFQHAGHRDKVVDFHWNASDPWTIVSVSDDCETTGGGGTLQIWRMSDLIYRPEEEVVAELEKFKSHVMTCASKP", "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 the flowering autonomous pathway which positively regulates flowering by promoting transcriptional repression of the flowering repressor FLC. May promote histone deacetylation at the FLC locus leading to the formation of repressive chromatin structures. Forms a histone deacetylase complex with HDA5, HDA6 and FLD that represses FLC gene expression to control flowering time (PubMed:25922987). Also negatively regulates cold-responsive genes. Acts together with PDP1 and MSI5 to regulate the function of the PRC2 complex on FLC (PubMed:29314758). Required for systemic acquired resistance (SAR) toward pathogenic bacteria (e.g. Pseudomonas syringae pv tomato DC3000 (avrPto)) (PubMed:32392578). Together with FLD and MSI4/FVE, contributes to dehydroabietinal-dependent (DA, a diterpenoid tricyclic diterpene) activation of flowering ans SAR (PubMed:32392578). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
{"protein": "MSIMMLPMEQKIQWVPTSLQDITAVLGTEAYTEEDKSMVSHAQKSQHSCLSHSRWLRSPQVTGGSWDLRIRPSKDSSSFRQAQCLRKDPGANNHLESQGVRGTAGDADRELRGPSEKATAGQPRVTLLPTPHVSGLSQEFESHWPEIAERSPCVAGVIPVIYYSVLLGLGLPVSLLTAVALARLATRTRRPSYYYLLALTASDIIIQVVIVFAGFLLQGAVLARQVPQAVVRTANILEFAANHASVWIAILLTVDRYTALCHPLHHRAASSPGRTRRAIAAVLSAALLTGIPFYWWLDMWRDTDSPRTLDEVLKWAHCLTVYFIPCGVFLVTNSAIIHRLRRRGRSGLQPRVGKSTAILLGITTLFTLLWAPRVFVMLYHMYVAPVHRDWRVHLALDVANMVAMLHTAANFGLYCFVSKTFRATVRQVIHDAYLPCTLASQPEGMAAKPVMEPPGLPTGAEV", "text": "FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MIDADGFRPNVGIILTDDQGRLLWARRVGGQDAWQFPQGGIKHNESPENALYRELEEEVGLCKADVEVLGVTQGWLRYRLPRRLVRDKEPKCVGQKQKWYLLRLVSNDSAIRLDASSPAEFDTWNWVSYWYPLGKVVAFKRDVYRRALKELSPVYNQYFLSTLGEGRALC", "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": "MAPNSSVTVGNVVFDNNAALALIAGPCQFESRQHAFDMAGALKELTARLGIGLVYKTSYDKANRTSLSATRGAGMDAALPVFDELRKEFSLPVLTDVHTEEQCAIVAPHVDVLQIPAFLSRQTDMLVAAAKTGKVINVKKGQFLAPWDMKNVVAKITGSGNPNVLTTERGASFGYNTLVSDMRALPVMAEIGAPVIFDATHSVQQPGGQGGSSGGERRFVETLARAAVAVGVAGVFIETHQDPDNSTSSDGPNMLPLKDMPALLERLMAFDRIAKGR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsA family."}
{"protein": "MAELISIDDTIDTAYDIFLEMAPDNLEPADVILFTAQFDDRGAAELVDVGDDWDDQVGFEVDKEIYAEVRIGLVNEENDVLDDVFARMLISRDPDQKFCHMLWKRD", "text": "SIMILARITY: Belongs to the UPF0263 family."}
{"protein": "MRLILWLPVLVVVLLMVLEGPAPAQGAPAIASTFSNIPNSLKEFGNNLKDAFESIPEATRKLMTSFAEGLKNLRLPLL", "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": "MLTLGVNIDHVATIRQARRTVEPDPVAAAVLAEIGGADGITVHLREDRRHIQDRDVRILRQTVRTHLNLEMAPTEEMIAIALDIKPDYVTLVPEKRQEVTTEGGIDMLGNFDRFCRVVERLQAANIPVSWFIDADFAQIQAAANTGAKFIELHTGQYAEAQQESDRQALLTILKEGCEYASSLGLRVNAGHGLTYGNVYAVACLPNMEELNIGHTIISRAVLVGLERAVREMKLAMRGQL", "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": "MATTHAQGHQPVLGNDTLREHYDYVGKLAGRLRDPPEGGTLITTILFLVTCSFIVLENLMVLIAIWKNNKFHNRMYFFIGNLALCDLLAGIAYKVNILMSGRKTFSLSPTVWFLREGSMFVALGASTCSLLAIAIERHLTMIKMRPYDANKKHRVFLLIGMCWLIAFSLGALPILGWNCLENFPDCSTILPLYSKKYIAFLISIFTAILVTIVILYARIYCLVKSSSRRVANHNSERSMALLRTVVIVVSVFIACWSPLFILFLIDVACRAKECSILFKSQWFIMLAVLNSAMNPVIYTLASKEMRRAFFRLVCGCLVKGKGTQASPMQPALDPSRSKSSSSNNSSHSPKVKEDLPRVATSSCIIDKNRSFQNGVLCK", "text": "FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MHGLVVLLVCLAVGSAFAGTIGVSNADPFEREGRIVGGEDTTIRAHPYQVSLQNKKGSHFCGGSLINEDTVVTAAHCLVGKKIAKVFVRLGSTLYNEGGIVVAVRALTYNADYSSKTMENDVGILKLAEKVKETDDIRYIELATETPPTGTTAVVTGWGSKCYFWCMTLPKTLQAVYVNIVDWKTCASDEYKYGEVIYDTMVCAYEKKKDACQGDSGGPLAIGNTLVGIVSWGYACASNLLPGVYSDVPALRKWILNASQTL", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MAKKITAKVKLQLPAGSANPSPPVGPALGQHGVNIMEFCKAFNAKTMEQKGTIIPALITIYADRSFTFITKTPPASVLLVKAAKIDKGSGEPNKNKVGKVTAAQIEEIAKLKMVDMTAKDLEAACRTISGTARSMGIEIV", "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": "MTKQDQRAERHIPVLLQPVLAGLMPLVGAKVIDGTFGAGGYTRALLKAGAQVIALDRDPHAIAAGQSLVDEFFPRLRLVHMEFSQLDRVVEEKVDAVILDIGVSSMQLDEAERGFSFQKDGPLDMRMAQTGFSASDVVNHLKAKDLARIFKILGEERYAGRIARMIEKRRAVQPFLRTGDLAYAIEALVGRKPGDRIHPATRVFQALRIYVNDEIGELARGLFAAERVLKAGGRLGVVSFHSLEDRMVKRFFVSRSGEGMRSRHLPEIKHSPATFFPLFKGGITANKEELQQNPRSRSARLRMGVRTNAEALAEDMKLFGLAEIASFEGGKK", "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": "MEREKQWIVRVVWRVSERQISRWRGIVTYKIRNKQLPWEYRHHWQVQWQFWTYSQFIIPLSKDDYIEVNIYHNLTPERGWLSSHGVGLSYYHQKGYKTEVDPGTADRMIHLYYFNCFTDRAIQQAIRGEKYTWCTFKEGHKGQVQSLQLLALVAYTNGIRKRSKRTFTRMAGNLGSRQGAMGRMATRHAQGSKRRSQKALWNEHANPSMELLCRGGKET", "text": "FUNCTION: Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity). SUBCELLULAR LOCATION: Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Virion Note=Seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor (By similarity). SIMILARITY: Belongs to the primate lentivirus group Vif protein family."}
{"protein": "MRAVVQRISEGKVVVDDAVTGAIKKGLLVFLGVTKEDTMEDVQYMAEKIVNLRIFEDQEEKMNLSVKDVGGKILAVSQFTLLGDCRKGRRPSFTEAARPETADKLYEAFIEQCEKLDIKVEKGVFQAHMMVHLVNDGPVTMLIDSKKVF", "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": "MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMREFVKLLK", "text": "FUNCTION: Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins 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 advanced glycation endproducts (AGE) that cause irreversible damage. Also displays proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C56 family."}
{"protein": "ALWKTLLKNVGKAAGKAALNAVTDMVNQ", "text": "FUNCTION: Has antibacterial activity against the Gram-positive bacteria S.aureus and E.faecalis, and the Gram-negative bacteria P.aeruginosa and E.coli. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=10.9 uM), C.guilliermondii (MIC=21.8 uM), C.albicans (MIC=21.8 uM) and C.albicans ATCC 1023 (MIC=10.9 uM). Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MSTQLASNIYAPLYAPFFGFAGCAAAMVLSCLGAAIGTAKSGIGIAGIGTFKPELIMKSLIPVVMSGILAIYGLVVAVLIAGNLSPTEDYTLFNGFMHLSCGLCVGFACLSSGYAIGMVGDVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIVALILNTRGSE", "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 (PubMed:1837023, PubMed:9030535). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1837023, PubMed:9030535). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
{"protein": "MAHGVDRTRRIGEQMRRDLAQALVDIVHHPHASLLSFTAVHLTRDLSFAKVYVTHVLDNEEERSELVAELNAKAGQFRHYLAKNLSIRKVPELQFYYDQSVEYGARMEQLLTHLVKDSEHKD", "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": "MSSVDQIVKTFANLPEGERNAAVNAILAMMPPGPGPVRQIPEPVPQAPAPKKKVNGFMGFRSYYSSLFSQFPQKARSPFMTILWQHDPFHNEWDFMCSVYSSIRNYLEQLNAQREKKITLQYWLHFAVPVMGVLGRENYLPTLGWDLVTMPNGTIDLMRIAMPLFRKNLQPMDGLCLFTKCQEGGLQVDNQHFVIAKLSDPSHDMIWFNKRPHYQQRHAAQTDSSEAGVSALFPRNHAVAAEADGVATVQLPHWMQQGDFGTESGYSPQFETLLGSILENGNATSNDSYNMALAMDVPMMG", "text": "FUNCTION: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in fungal differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional activator that induces the transcription of alpha- specific genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MATALPHA1 family."}
{"protein": "MRLGVSLLGSTGSIGRQTLEVVAAHPDRFRVVALAARSQIDALQEQVRIFRPELVAIAQESLGISFPDTRVVSGPGGLVEAATYETADIVVIALSGNSGIEPTLAAAAAGKTIALANKESVVCAGPLLRDIQSRTGCQVRPVDSEHSALWQLLQLPHRPAEIARVILTASGGPFRDRPLEHLNQVTPDEALAHPTWRMGPKITIDSATLLNKGLELIEAHWLFDLPFERLDVVIHPQSIVHALLAFVDGTTVAHAAYPDMRLPIQYALFYPERVASTVPPLDLARIGPLEFFPPDTERFPALPLAREVGIAGSTYPTVLCAADEIAVEAFLAGQIRFTEIVPLIRSVLDRHQPASEPLTLEAILAADRWARSVARELVGRAIRHA", "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": "GSFELTILHTNDVHARLEQTSRDSGKCTGEDCYGGVARRATKIRQIRASHRNVLLLDAGDQYQGTIWFNYYKGREVVHFMNSLRYDAMALGNHEFDNGLNGLLDPLLKNVKFPILSANIRPKGPIASNISGYILPYKIINVGSEKVGIIGYTTKETPVLSNPGPYLEFRDEVEELQKHADKLTTLGVNKIIALGHSGFMEDCRIAQKVKGVDVVVGGHTNTFLYTGSPPSNEVAAGNYPFMQLSDDGRQVPVVQAYAFGKYLGYLNVTFDDKGKVIKASGNPILLNKSIQEDPAVKAEISRMKVQLQNYSSQEIGRTIVYLNGTTHACRFHECNLGNLICDAVVYNNLRHPDDNEWNHVSMCIVNGGGIRSPIDEQANNGIITLEELTAVLPFGGTFDLLQIKGSTLRQAFEHSVHRHGQGTGELLQVSGIKVVYDLSQKPGKRVVSLNVLCTECRVPTYVPLEMEKTYKVLLPSFLAAGGDGYYMLKGDSSNHSSGDLDISIVGDYIKRMGKVFPAMEGRMVFSAGSL", "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": "MIEADRLVSAGVISEEEVIDRAIRPKMLAEYVGQPVVREQMEIFIKAAMMRGDALDHLLIFGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAALLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYRVEDLQHIVGRSAACLGLPLSDEGALEIARRARGTPRIANRLLRRVRDFAEVRAGGEMSGDVASRALDMLSVDSEGFDYMDRKLLLAIIDKFTGGPVGLDNLAAAIGEERETIEDVLEPYLIQQGFIQRTPRGRMATQHAYKHFGITREG", "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": "MRTLTIEPLTKEAFAPFGDVIETEGSDYFMINNGSTRRYHKLATVETAAPEDQAIISIFAAEALEMPLVIRMLERHPLGSQAFIPLLGHPFLVVVAPLGDAPVPGHVRAFRSNGRQGVNYHRGVWHHPVLTIEKRDEFLVVDRSGSGNNCDEYFFTEDQQLLLDPQQVSR", "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": "MSRIGRKPIDIPSGVDVKIDGNVITVKGPKGTLTREIHPEMIVKIENNQIIVQRPSDERFHKALHGLTRTLIANMVEGVTKGYEKVLEVVGIGYRAQKQGKKLVLNVGYSHPVEIEEPAGITIEVPDQNRIVVKGIDKQQVGNFAANIRKVREPDPYLGKGIKYADEVLRLKEGKAGKGGKK", "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": "MGKKRKITDEKDAQHVPAEKREKVENWLKKSTEKPTSSQSDAEKKKKRPWRNKVRKLAAKKAAADKKSENPEEPPLILEPKSSSDENTKKKRKRGPKKKKFKPEVAGKAAETENDDVAAAPEEADPIAEAKKRLDAGRFRFLNEKLYTCTGSEAFDFFKEDPTAFDLYHKGFADQVKKWPNHPLREIIRWLQSKPDQQSVFDLGCGEAKIAEAVGEKHKIRSFDLVAVNDRVESCDMSKLPAEDSSADIVIYCLSLMGTNLYDFIREARRVLKIGGILKIAEVTSRFVSIKQFCEAITKMGFEQSHRRELTDYFMMMEFKKVEKVEQKRPYGLKLKPCLYKKR", "text": "FUNCTION: Probable methyltransferase required to silence rDNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family."}
{"protein": "MRNKIFSSLYFQVLLAITLGVFLGHVYPDLGADMKPLGDGFVKLIKMIIAPVIFCTVVTGIAGMESMKAVGKTGAIALLYFEVVSTIALVIGLCVVNLLQPGVGMNVDPATLDASAISAYAEQAKSQGIIAFLLDVIPGSVIGAFASGNILQVLLFAVLFGFSLHHIGEKGKLIFNVIDSFSQVIFGIINMIMRLAPVGAFGAMAFTIGKYGIGSLVQLGQLIACFYVTCLLFIFMVLGSIARANGFSILRFISYIKEELLIVLGTSSSESVLPRMLVKMEALGCKKSVVGLVIPTGYSFNLDGTSIYLTMAAIFIAQATNTPLDLFQQITLLVVLLISSKGAAGVTGSGFIVLAATISAVGHLPLAGLALILGIDRFMSEARALTNLIGNGVATVVVARYCDQLDEQQMNEVLANPAAVQKVDQHG", "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": "MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPEPSPAPGPGRRGGRGELARQIRARYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLPRPRPPWARPLSDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYMGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGVRRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEDIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVDGELKVTDLDDARVEETPCAGSTDCILEFPARNFTLPCSAQGWCEGMNEKRNLYNAYRFFFTYLLPHSAPPSLRPLLDSIVNATGELAWGVDETLAQLEKVLHLYRSGQYLQNSTASSSTEYQCIPDSTIPQEDYRCWPSYHHGSCLLSVFNLAEAVDVCESHAQCRAFVVTNQTTWTGRQLVFFKTGWSQVVPDPNKTTYVKASG", "text": "FUNCTION: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29 (PubMed:25171405). Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation (PubMed:25171405). May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane (By similarity). SUBCELLULAR LOCATION: Secreted Golgi apparatus. SIMILARITY: Belongs to the protein kinase superfamily."}
{"protein": "MKQYLDLMKKVLEEGTTKDDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELLWFLNGDTNIGYLKENNVSIWDEWADENGDLGPVYGKQWRAWGAADGRQIDQLSKVVQQLKQDPNSRRIIVSAWNVGELDQMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLAVGDFVWTGGDTHLYSNHIEQTHLQLSREPRALPKLIIKSKPASLFDYRFEDFEIEGYDPHPGIKAPIAI", "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": "MAADGDWQDFYEFQEPAGSVRDQENCNASPEAGAGAHAGGDSFPALASSLEEKLSLCFRPTSDADPPRAAVRPITERSLLQGDEIWNALTDNYGNVMPVDWKSSHTRTLHLLTLNLTEKGMSDGLPFDTSDEEELREQLDMHSIIVSCVNEEPLFTADQVIEEIEEMMQESPDLEDDETPTQSDRLSMLSQEIQTLKSSSMSSCEERVKRLSVSELNELLEEIETAIKEYSEELVQQLALRDELEFEKEVENSFISALIEVQNKQKEHKETAKKKKKLKNGSSQNGRNERSHMPGTRFSMEGISNVIQNGLRHTFGNSGGEKQYLTTVIPYEKKNGPPSVEDLQILTKILHAMKEDSEKVPSLLTDYILKVLCPT", "text": "FUNCTION: Involved in axonal outgrowth and fasciculation. SIMILARITY: Belongs to the zygin family."}
{"protein": "MKDPNTIPPWRCTDFNAWCIAVDKSTNVKNKEELLSTLTYFINYEIEMGQTYPIDIKMTRNEAEDFFFKFCTVICVPVESETSPAPDLATASIDWKTSLLGAFYIKPNYPGRCSHICNGGFLVSPSHRSKGIGRNLANAYLYFAPRIGFKSSVFNLVFATNIKSIRLWERLNFTRAGIIKDAGRLKGHEGYVDAYIYQYHFPSLEDALK", "text": "FUNCTION: N-acetyltransferase involved in oxidative stress resistance. Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5- carboxylate (P5C), or more likely its spontaneously forming tautomer glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis in the mitochondria. P5C has been shown to increase the levels of reactive oxigen species (ROS) in the cell by inhibiting the function of the respiratory chain in the mitochondria. The enzyme is able to reduce intracellular ROS levels under P5C-induced oxidative stress and protects cells from damage by oxidative stress (By similarity). Also acetylates and thereby detoxifies the proline analog azetidine-2- carboxylate (AZC), however it is unlikely that AZC is a natural substrate as it occurs only in plants belonging to the Lilaceae family (PubMed:12761200). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MARYTGPRGRRDRRAGVMLSSMRKNPLEKKPYPPGEHGRDRQRQTEYGLRLMEKQKARWYYGVSERQFRRAYEEAIRQPGVSGENLLRLMELRMDNVVYRMGFATSRPQARQLVVHGHFLLNGRKHNIPSATLKPGDVITVRDKSRRLQPIQEAVEQVVAVPAWLEADHENFTGRVLHTPSRDEIDAPVEEQLIIEFYSR", "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": "MTNIWHTAPVSALSGEITICGDKSMSHRALLLAALAEGQTEIRGFLPCADCLATAQALRALWVDIQREKEIVTIRGVGFLGLQPPKAPLNMQNSGTSMRLLAGILAAQRFESVLCGDESLEKRPMQRIITPLVQMGAKIVSHSNFTAPLHISGRPLTGIDYALPLPSAQLKSCLILAGLLADGTTRLHTCGISRDHTERMLPLFGGALETQKEQIIVTGGQKLHGCVLEIVGDLSAAAFFMVAALIAPRAEVVIRNVGINPTRSAIITLLQKMGGRIELHHQRFWGAEPVADIVVYHSKLRGITVAPEWIANAIDELPIFFIAAACAEGTTFVGNLSELRVKESDRLAAMAQNLQTLGVACDVGADFIHIYGRSDRQFLPARVNSFGDHRIAMSLAVAGVRAAGELLIDDGAVAAVSMPQFRDFAAAIGMNVGEKDAKNCHD", "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": "MKIVWYGHACFLIKTKGVSILIDPYPDVDEDRMEKVDYILITHEHMDHYGKTPLIAKLNDAEVIGPKTVYLMAISDGLTKVREIEAGQEIQLGDVTVKAFYTEHPTSQYPLGYLIIGDKRVAHLGDTYYSPSFKNLRGQVDILLVPIGGRSTASEREAVDIVDIIRPRIAVPMHYGTYGGGSAEGFKRELQRRRVWVLVKDLKPYEGFEV", "text": "SIMILARITY: Belongs to the UPF0173 family."}
{"protein": "MKNKTTIRWLKQALVLSSIVNILLLLLIYSTVFRKDIYKLQVFPGHLIAKSARIGKIPEDILERLEAASLADLIILLREERLVFGHPLKLWALSMGIQKYSLDITPMLTHPLTFIKLKSPEQTWLLPDINDQEFSRINQYLHTERFPFSSKGFFRIMARDWEAGIVNEDILYRFCHIPEFLYVRSLLFGAEIEAASVASLARMVIQGGEDLFFSLCCLENLQTAISDQQRRVFLKAYVDRQEPLAALLLLVHDADWVLHEFSDTDLKYFVQLLPKEVSYTKQFLDQVGHSCRQEILSILQ", "text": "SIMILARITY: Belongs to the chlamydial CPn_0593/CT_474/TC_0759 family."}
{"protein": "MIPKEEIMGIFEKYNKDEITIATVGSHTSLHILKGAKLEGFSTAVITTKDRDVPYKRFGVADKFIYVDKFSDISSEEIQEQLREMNAIVVPHGSFIAYCGLDNVESTFKVPMFGNRAILRWEAERDLEGQLLGGSGLRLPKKYNSPDEIDGPVMVKFPGARGGRGYFPCSSTEEFWRKINDFKAKGVLSEEDVKKAHIEEYVVGANYCIHYFYSPLKDRVELMGIDRRYESSIDGLVRVPSKDQLELDIDPSYVITGNFPVVIRESLLPQVFDMGDKLCKKAEELVKPGMLGPFCLQSLCTENLELVVFEMSARSDGGNNTFMNGSPYSYLYNAEPLSMGQRIAKEIKLALELKMIEKVIS", "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": "MRSQLSLMGKKEGMIHVFDKDGNLVACSVISMSPNVVSQIKVDSTDGYNAIQMGADEISVPEKTLQKRVNKPILGHFKKSGSRVFRTLKEVRVSEDAVNEASLGSEFGLEVFEDVSSVDISGVSKGKGFQGVMKKFGFRGGPKTHGSGFHRHAGSIGMRSTPGRCFPGSKRPSHMGAVNVTIKNLEVIKIDLEKKVLLVKGAIPGPRGSVVVVRRSSRAKA", "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": "MMMFNEMGMYGNMDFFSSSTSLDVCPLPQAEQEPVVEDVDYTDDEMDVDELEKRMWRDKMRLKRLKEQQSKCKEGVDGSKQRQSQEQARRKKMSRAQDGILKYMLKMMEVCKAQGFVYGIIPEKGKPVTGASDNLREWWKDKVRFDRNGPAAIAKYQSENNISGGSNDCNSLVGPTPHTLQELQDTTLGSLLSALMQHCDPPQRRFPLEKGVSPPWWPNGNEEWWPQLGLPNEQGPPPYKKPHDLKKAWKVGVLTAVIKHMSPDIAKIRKLVRQSKCLQDKMTAKESATWLAIINQEEVVARELYPESCPPLSSSSSLGSGSLLINDCSEYDVEGFEKEQHGFDVEERKPEIVMMHPLASFGVAKMQHFPIKEEVATTVNLEFTRKRKQNNDMNVMVMDRSAGYTCENGQCPHSKMNLGFQDRSSRDNHQMVCPYRDNRLAYGASKFHMGGMKLVVPQQPVQPIDLSGVGVPENGQKMITELMAMYDRNVQSNQTPPTLMENQSMVIDAKAAQNQQLNFNSGNQMFMQQGTNNGVNNRFQMVFDSTPFDMAAFDYRDDWQTGAMEGMGKQQQQQQQQQDVSIWF", "text": "FUNCTION: Probable transcription factor acting as a positive regulator in the ethylene response pathway. Could bind the primary ethylene response element present in the ETHYLENE-RESPONSE-FACTOR1 promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EIN3 family."}
{"protein": "MKWTALVIVAVLQTQFPVTAAQSFGLLDPKLCYLLDGILFIYGVIVTALFLRAKFSRSADAPAYQHGQNPVYNELNVGRREEYAVLDRRGGFDPEMGGKPQRKKNPHEVVYNELRKDKMAEAYSEIGMKSDNQRRRGKGHDGVYQGLSTATKDTYDALHMQALPPR", "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. CD3Z ITAMs phosphorylation creates multiple docking sites for the protein kinase ZAP70 leading to ZAP70 phosphorylation and its conversion into a catalytically active enzyme. Plays an important role in intrathymic T-cell differentiation. Additionally, participates in the activity-dependent synapse formation of retinal ganglion cells (RGCs) in both the retina and dorsal lateral geniculate nucleus (dLGN). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the CD3Z/FCER1G family."}
{"protein": "MTETRTTCPYCGVGCGVIASRAPHGQVSVRGDEQHPANFGRLCVKGAALGETVGLEGRMLFPEVDGERATWPQALAAAGSRLREIIDRHGPQAVAFYASGQLLTEDYYAANKLMKGFIGAANIDTNSRLCMSSAVTGYKRALGADVVPCSYEDVENSDLVVLVGSNAAWAHPVLYQRLAQAKRDNPQMRVVVIDPRRTATCDIADRHLALAPGSDGGLFVGLLNAIAASGAISDDFNDAQRALTIAQDWDLDKVAQFCGLPRQQIADFYREFIAAPRAITLYTMGINQSASGSDKCNAIINVHLACGKYGRPGCGPFSLTGQPNAMGGREVGGLATMLAAHMNFEPDDLRRLARFWGSERLAQTPGLTGVELFAAIGRGEVKAVWIMGTNPVVSLPDSHAVSEALARCPLVIISDVVADTDTGRFAHIRFPALAWGEKSGTVTNSERRISRQRAFMPPPGEARADWWIVARVAEALGFGSAFAWQHPHEVFSEHAALSGYENDGQRAFDIGGLADLSREAWDALEPVRWPVSRSEAAWSVHKGWHRDGKLRMVPVAPQPTRATTDAFYPLILNSGRIRDQWHTMTRTGAVPRLMQHINEPVVEVAPADAQRYHLLEGELARVRSPKGVMVAKVTIGDGQRPGSLFVPMHWNNQFARQGRVNNLLAAVTDPHSGQPESKQTAVAIATWLPAWKGELFSRQPVPLPASLHWRRRAAQGIIHLSLAGDTRSRDWLVEWCQRQGWQMQVAEGGKVWNLLAWRAGELMLGWWSDASEPAIDADWIHAAFRVPPQNAARRHALLSGRKGGVEMPRGRIICSCFSVGERAIGEAIAGGCRTPGALGGKLKCGTNCGSCIPELKALLAAKLAQA", "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 prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily."}
{"protein": "MSIGVQSSGINISHAELSRLVDAGKSEQGDKAVRDDGRALARADAALAAVVGERVAARRDAVAGSGAQRVELARPKPDAQTRATDRRTVSGLEREHKRLAASQTPRVTGMHDALVQRHVSLDGAKAAHGEGVKRAAGDAPRAAADAPQRFAFADDKAFDAMLALGAAMQKNVQSDLAMQGKLTMLAHDAMMSAAAQDRSIGAAQMTAAIAGGALQATTSLGGAMQQMKSLSTKSMSIEKELKPQAELKQFHAEQALELRGINKPVLSNDEVSHVKIKRDTGETVRHEIDHGGERMSDEHASVLAQEAPARQHRIDMHGMRHEENLVKAGRQQMKGDLLQSGGQIGKNQIDGASAQQQGADRAEQKEDENAQQTAMAAASTRDEAAHRSREAAQKAIDAAKSQVANDNAVAAQVAGNLRT", "text": "SUBCELLULAR LOCATION: Secreted Note=Secreted via the bsa type III secretion system. SUBCELLULAR LOCATION: Secreted Note=Secreted via the bsa type III secretion system. SIMILARITY: Belongs to the invasin protein C family."}
{"protein": "MKITIFGGGAWGQALAFAFAQKNEVQIVSRRNISTALMPLNEILNKNSHRIILQSSLEESLNSELFVIAISVQALREWFIRARLNQNSKILIASKGIEEKTGIFVSQIAKKFISLENLCFLAGPSFAKEIILGLPCALAIHSCNPILAQKFANQMPSFIKPYIEDDIIGGEVASAYKNVIAIAGGICDGLNLGQNAKASLLSRGLVEMCKFGEYFGAKMQTFLGLSGAGDLFLTANSLLSRNYRVGLGLAQNNRLEDILRDLGEVAEGIKTSQAITQISEKEGIYTPIATEIQKIIQGKSPLESMSTLMKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MSRLFMILLVICVITLGTDASQAEDSGTEKKSWPMPDADLKAFQSWPLTDPDLKSAFKQYNWQRMPYGTRK", "text": "FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin NSf-1 superfamily."}
{"protein": "MNIDYVRSILPHRYPFLLVDGVIEESEDRIVAFKNISISDPVFQGHFPEYPIYPGVLIIEGLAQTAGILLLKDLEGIPLFLGIDEARFKKEVRPGDKLIYEVKKIGEKLGTVQVEGVAKVENTIVAKAKLLLGVKKK", "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": "MAEVTAALVKELREKSGVGMMDCKKALVENNGDIDASIDWLRAKGLSKAAKKADRVAAEGLVGIVVRAEGAGMIAAAVEVNAETDFLSRNELFQTAVRKIARAGLDNEGVEAISAAKTPDGEVVSDLLTHLIATIGENMVLRRSARFAVAHGAVASYIHNATAPDLGRIGVLVAIEGAGDQTKILELGRKIAMHVAATAPLSLSPDDLDQAAIEKERQIFTEQALESGKPPAVVEKMVEGRIRKFLEEVVLLKQAFVMNPDQTVEQLVAEAGKELGSPLTVKGFVRLALGEGVEKGPEGDFAAEVAAMTGQA", "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": "MLDTKFDELMDFPCAFPFKVVGDAHEALTDRVVAVVQKHAPGDYAPTTKASSKGSYYSITIRVTVTSKDHIETLYTELAAIEGVRRVL", "text": "SIMILARITY: Belongs to the UPF0250 family."}
{"protein": "MRQLFVLDPLSQIRPEKDSTAALMQAAQRAGDDIWSCTPSDLIARGDEPMAVALPVTPDPWIAVGAPERQSLAGFDVIWMRKDPPVDEAYLYATHLLEVAERAGVRVLNRPSALRAWNEKLGALRFSRWMAPTLVAGRVSELMAFAREQGDVVLKPLGGRAGLGVIRVQAEAPGLKALLELVTEQERLPVMAQRFLPDVTEGDKRILLVDGDPLGAVNRRPSEGEFRSNLAVGGQAEATELSEPERQICAALAPALRAEGLFFVGIDVIGGMLSEINVTSPTGVREVERLMQEPLADQTIERLRSLV", "text": "SIMILARITY: Belongs to the prokaryotic GSH synthase family."}
{"protein": "MSDEVEAGFVRVRLDLSYDGSEFSGWAKQAGGRRTVQGEIEDALRTVTRSRETYELTVAGRTDAGVHARGQVAHVDLPREVWAEHHVKLLKRLAGRLPRDVRVWALREAPSGFNARFSAVWRRYAYRVTDNPGGVDPLLRGHVLWHDWPLDVDAMNAAARGLLGEHDFAAYCKKREGATTIRTLQELSLVRGEDGIVTATVRADAFCHNMVRSLIGALLFVGDGHRGPEWPAKVLAAGVRDSAVHVVRPHGLTLEEVGYPADELLAARNKEARNKRSLPGAGCC", "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": "MQQKMLRILEFDKVKEQLAEHASSALGLEKIAALVPSSDLDEVAVWLEETDEAAAVLRLRGYVPLDGVVDIRSHLKRAAIGGVLSPIELLEVAATAAASRQMKQLIMSLHDEHGGLARLADYADELAEVPALEEDIRRSIDDHGEVLDTASDRLRSLRGQIRAAEARIREKLESIIRSPSAQKRLSDAIITIRNDRYVIPVKQEYRSAYGGIVHDQSASGATLFIEPQVVVELNNALREARAKEKQEIERILRELSAKVAEHDEPLKRAVEALAHFDFLFAKAKYARRLQAAKPAVNNRGYLRFLQARHPLIDQDKAVPNDIVLGGDYTTIVITGPNTGGKTVTLKTVGLLTIMAQAGLFIPAADGSEAAVFRSVFADIGDEQSIEQSLSTFSSHMVNIVDILRHVDEESLVLFDELGAGTDPQEGAALAIAILDEVHGRGARTVATTHYPELKAYGYNRPGVVNASVEFDTETLRPTYKLLIGIPGRSNAFDISRRLGLDERIIERAKVQVSAESHSVENMIASLERSKKQAEEDEARAHSAREEAERLRAEWEQKLEELEDKKAEQLAEAAQKATDIIRAAEREAERIINELRRLQKEKQAEVKEHELIAAKQRLAAAVPVVEKRKKTKKATARHAFQSGDEVKVTSLNQKGYLLEKVSEDEWQVQLGILKMKIHERDLEYIGSAPAKEVTPIATVKGKDAHVSLELDLRGERYEDALVRLEKYIDDAVLAGYPRVSIIHGKGTGALRQGVQQFLKQHRAVKSFRFGAANEGGTGVTVVELK", "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": "MTGSDQTRAKLIDIELDESIGRSTPDVEHERAVAIFDLIEENSFQPVNDSGAGPYRLKLSLAEQRLVFAVAREDGTAVVTHILSLTPLRRIVKDYYMICESYYDAIRSSTPSHIEAIDMGRRGLHNEGSQTLMDRLSGKIDIDFDTARRLFTLVCVLHWRG", "text": "SIMILARITY: Belongs to the UPF0262 family."}
{"protein": "MSSMEKHLFNLKFAAKELQRNSKKCDKEEKAEKVKVKKAIQKGNMEVARIHAENAIRQKNQSVNFLRMSARVDAVAARVQTAVTMNQVTKSMAGVVKGMDATLKSMNLEKISGLMEKFERQFETLDVQTAQMEDSMSSTTTLTTPQGQVDTLMMEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLAKLRDQV", "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. SUBCELLULAR LOCATION: Cytoplasm, cytosol Endosome Late endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family."}
{"protein": "MTSFKIVIVCLALLVAVASARSRDMMSDDERDYHFSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ", "text": "FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity for arthropod over mammalian channels (PubMed:18538344). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Also causes paralysis of cherry shrimps immediately after injection at very low doses (PubMed:29424690). Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes (PubMed:22048953). It has also been observed to cause death of zebrafish larvae within 1 hour (PubMed:31134275). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type II subfamily."}
{"protein": "MIVSFSTVYFFIYLLLFVSIGLTSSLFIVPLLGASFAFASGVVIFGFLSNVTFKSAQTIYIKVDKRLKFILAKMSSFTNGNESEKNVDVPLLQQTKKRHSQIQSKLKNSFNTNINNNNLTNNDNIVTSTTRGIDVPLDTNNSVTSAIARSLETRADSKIATN", "text": "FUNCTION: Involved in spore wall assembly. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OSW5 family."}
{"protein": "MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVRDFVAQNNTVQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESSKFDLVGFIPLLRERIYSNNQYARQFIISWILVLVSVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDEPDEPKSVAQKQTEPNPEDSLPKQEGTASGGASGPCDSSFGSGISVFTSASTDRAPVTLHLDGIVQVLNCHLSDTTIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVVLKDLEVLAEIASSPAGQTDDPGAPDGPDLQVNHSELQVPTSGRANLLNPPNTKGLECSPSTPTMNSYFYKFMINLLQTFSSERKLLEARGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHTLNTILLTSTELFQLRNQLKDLKTLESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLTEVDKLVQLIECPIFTYLRLQLLDVKNNPYLMKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDCLKAAPKSQKGDSPSIDYTELLQHFEKVQKQHLEVRHQRSGRGDHLDRRVVL", "text": "FUNCTION: Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3- phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. SUBCELLULAR LOCATION: Endosome membrane Microsome membrane Note=Mainly associated with membranes of the late endocytic pathway. SIMILARITY: Belongs to the VAC14 family."}
{"protein": "MHIKTLTVSQLNRYVKNTLDADFILNNASVKGEISNLKIHSSGHIYFSLKDGGSKINCVMFKSYAYNLKFAPENGMDVVALGNVSVYEKEGSYQLYVKDMKREGIGDLYVAFEKLKEKLKEEGLFDDVHKKEIPKFSKKVGVITSPTGAALKDIINVTKRRNKGIELLIYPALVQGTDASRTLIEGIKILNKVEDVDIIILARGGGSIEELWAFNNEELAYAVYNSKKPIITGVGHETDFTIVDFVSDRRAPTPSAAAEIAVFDREVLINEILNYKYNIKNYMENIIKEKRNYLNLYKQKIEANSPTNIIVNEYKNIDNLKELLNMKIEGKLNKEKNNLSRLSSLLEAHNPLNVLKKGYTLIEDEGNNLITEKEALKELNKINIIFKDGRAKLSIEYIEEF", "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": "MARIAGINIPDHKHTVIALTSIFGIGKTRSQSICASTGIAEHVKISELSEEQIEQLREAVAKFTVEGDLRREVTLSIKRLMDLGTYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK", "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": "MLSDREVLSTLEMLKNEHLDVRTVTLGVSLFDCAGHDPEKFKENVQRKIFRLAGNLVKVCDEIGIRYGIPVVNKRVAVSPIAVAACSFSRPQMVEVARKLDETAADIGIDFIGGFGALVEKGFTEGDRALIAAIPEALASTRRVCSSVNVASTRAGINMDAVYLMGKTIKDAAELTREADGIACAKLCVFANIPEDVPFMAGAYLGVGEPDSVINVGVSGPGVVKKAIDRARAANPHLDLGALSDIIKRTSFKVTRVGELIGRQVAEKLGVPFGVVDLSLAPTPNVGDSVGEIFQSLGLQSIGVPGTTAALALLNDAVKKGGAFASSYVGGLSGAFIPVSEDLNIAAAASRGYLSMEKLEAMTSVCSVGLDMVALAGDTSAETLAGIIADEMAIGVINKKTTAARLIPVPGKKAGEKASFGGLLGEAVIIAVSSNFGSREFISLGGRIPAPIHSLIN", "text": "SIMILARITY: Belongs to the UPF0210 family."}
{"protein": "MANHKNLFFLCFLIGLGLCSARRALLSSSESEAEVAAYGVNSGLSAGLGVGIGGGPGGGSGYGGGSGEGGGAGGHGEGHIGGGGGGGHGGGAGGGGGGGPGGGYGGGSGEGGGAGYGGGEAGGHGGGGGGGAGGGGGGGGGAHGGGYGGGQGAGAGGGYGGGGAGGHGGGGGGGNGGGGGGGSGEGGAHGGGYGAGGGAGEGYGGGAGAGGHGGGGGGGGGSGGGGGGGGGYAAASGYGHGGGAGGGEGSGGYVP", "text": "FUNCTION: Involved in leaf vasculature patterning. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTAIKKSFQYGQHTVTFETGEIARQASGAVLVNMADTVVLVTAVGLKDVAQGRDFFPLTVNYQERTYAAGRIPGGFFKREGRPTEKETLTSRLIDRPIRPLFPKGFMNEVQVIATVMSMNPEVDPDVPAMLGASAALALSGLPFKGPIGAARVGYLNGAYVLNPSMSELKHSDLDLVVAGTEKAVLMVESEAKLLSEEVMLGAVMYGHEQMQAAIKVINELAAEAGKPAWDWVAPEENVALKEAVAAACEAELTAAYQIAEKQARNQQVNALRDAVVAKLATGEEGAPSAEKVKGAFGALEKRIVRSRVLKGEPRIDGRDTRTVRPITVKTGVLPRTHGSALFTRGETQAIVVATLGTDRDAQLIEAIEGERRERFMLHYNFPPFCTGETGMVGSPKRREIGHGRLAKRGVQAVMPGEAECPYVLRVVSEITESNGSSSMASVCGTSLALMDAGVPLKAPVAGIAMGLIKEGDAFAVISDILGDEDHLGDMDFKVAGSKDGVSALQMDIKIDGITREIMEKALAQAKEGRLHILEKMNAVLSEPRTEVSAYAPRFTTLKIHPDKIRDVIGKGGATIRALTEETGTSIDISDDGTVKIASVDKAAGDEARRRIEELTADVEVGRIYEGRVVKIMDFGAFVTILPGRDGLVHISQISEERVESVSDRLTEGDLVKVKVLEVDKQGRIRLSMKEVG", "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": "MQLQEIAQKLGCAYEGDPTLEIHSVASLAEARPGELSFLSEARYLPLLEQTQASAVIVEEGLALPCSIACLRGRDPRLLFAQAIELFYQPYRLPVGIHPTAVIDPSVELGEGVAIGPHAVVMEGVKIGDHTQIHPNVTIYPHVRIGSRCQLFANCVIHERTEIGDDCLIHSGAVIGDDGFGHIPLADGSWRRMLQAGRVVLEDNVEVGSNTTIDRAAVGETRIGRGTKIDNLVQIGHGVRTGSHCLIVAQVGIAGSTQLGHHVILAGQCGLAGHLHIGDGVRVAAQTGVTSDVPAGQTVAGYPHQPIAEWRKSMAVQRHLPELQRTLRKLEARVAKLEQNSTDRAPNAKMLEVGVDPETTCSS", "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": "MFYPVVQVLIGIILVIILILGFYHMKHKPPKKKCKTDTDCKDKGHHCVRGTCTDKSCLEAAKQDIKDIKLDPTIRSCDYAPGFYRFNATTADLQSPFGKTRIDLGRVWTTWSKEDEYCQSLCLQRKGSIGWEFDELSLGGVGNCYCYTNSHPVLKNSNNTTVMGIARNVL", "text": "SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. Host cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the asfivirus envelope protein p22 family."}
{"protein": "MEKYERIRVVGRGAFGIVHLCLRKADQKLVILKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNIHTDVGSVRMRRAEKSLTPGPPIASGSTGSRATSARCRGVPRGPVRPAIPPPLSSVYAWGGGLSSPLRLPMLNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGAGGGTLLPGAVELPQPQFVSRFLEGQSGVTIKHVACGDLFTACLTDRGIIMTFGSGSNGCLGHGNLTDISQPTIVEALLGYEMVQVACGASHVLALSTDGELFAWGRGDGGRLGLGTRESHNCPQQVPVAPGQEAQRVVCGIDSSMILTSPGRVLACGSNRFNKLGLDHLSLDEEPVPYQQVEEALSFTPLGSAPLDQEPLLCVDLGTAHSAAITASGDCYTFGSNQHGQLGTSSRRVSRAPCRVQGLEGIKMVMVACGDAFTVAVGAEGEVYSWGKGTRGRLGRRDEDAGLPRPVQLDETHPYMVTSVSCCHGNTLLAVRSVTDEPVPP", "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. 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": "MIISSSTDYRRAAQKRLPPFLFHYIDGGAYAEHTLRRNVDDLAEVALRQRVLKDMSQLDTSIDLFGEKLSMPVALSPVGLTGMYARRGEVQAARAADARGIPFTMSSVSVCPIEEVAPRLSRPMWFQLYVLKDRGFMRNALERAQAAGCSTLVFTVDMPVPGARYRDAHSGMSGPNAALRRYAQAVMHPRWAWDVGLLGRPHDLGNISRYLGKPTGLEDYMGYLGANFDPSISWKDLEWIREFWKGPMLIKGILDPDDARDAVRFGADGIIVSNHGGRQLDGVLSSARALPAIADAVKGQIKILADSGIRSGLDVVRMIALGADAAMLGRAYIYALAAAGQSGVDHLLGLIEKEIRVAMTLTSVSSISQITSELLVREP", "text": "FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "MLKLPKGLKKKKKKSKKDQELFTEEELEQYKRDLKAKQEAAATKSDAGESDGASSDVEAHHEPVAFNSGLGSGSSSSILNAQQQLSDQNQGAAGGDEEWAKFKALTSGVDSILHKTQDELDRIKKESFYQRLPSAAEKKKQKEEEAARLEAEQQEREKQRLGQIEAQRDKLAEAVVQLSESEEEAGDYEADDIFATDYIEAITSGELQLAVVPDSPVLAEDGPDPFDTAYAEKVIVGADRAKGNKKLVSLGAAVEVLSGRVDREHAVALANPKRKLRKGIQNLLLSESIELADSEAELLAATSNAEPQHNLLDDLDEELSESSVPIDLSVSLHLHLIKHKQPVEEEEELEQKGRENQLLNPDLSEFDSLKDEEDDEFAELAAESLTKKEEVTVVSQVVLPVAQLPTEAFEAGSWAEFEEQSGQEPGKPKRPPPPVRPPTGPHIVPGAIYVSEDEEENPEDDPFNTNYAEQVIKKTTVLEEDDDFDPRAEEHATEPPFLAAPQRDLLAGSATDLSQVVPAPLAPTLSVDQEAEDFDPFDTSAVSALVQPKSTELRFLERELLNYSGLDGVTLKHSLSDQDFDPRADQKEPAAPQVKLEQKETDFDTAQRKSSLSLNIQAKSVGFLVPASDLLGAGNELGASKKPLTPYYAPSDNRLQEREREAEDVDPFDTSHVPEAKLSDIELKHIEKDLISVPANLRHSLSDPDFDPRAPPTPVPAEVLLAVEENINIKVLTPAQDRKKLTNSGGSGKSEEDIDPFDTSIAANLQPGQTELKLLENELLPETKTLVTDVLDVQSDAQELGLGDKVLTPSTHSRPSLPAQDIDPFDTSIAENLAPGEAEIKLLESELIER", "text": "FUNCTION: Adapter protein involved in endocytic recycling of synaptic vesicles membranes. May act by mediating the retrieval of synaptotagmin protein Syt from the plasma membrane, thereby facilitating the internalization of multiple synaptic vesicles from the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm. Synapse. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Colocalizes with synaptic vesicle pools. Colocalizes with the endocytic network within synaptic boutons."}
{"protein": "MAEVIKGKVVQVIGPVVDVEFEGVKELPKIKDGLKTIRRAIDDRGNWFEEVLFMEVAQHIGEHRVRAIAMGPTDGLVRGQEVEYLGGPIKIPVGKEVLGRIFNVAGQPIDEQGPVEAKEYWPMFRNPPELVEQSTKVEILETGIKVIDLLQPIIKGGKVGLFGGAGVGKTVLMQELIHNIARFHEGYSVVVGVGERTREGNDLWLEMKESGVLPYTVMVYGQMNEPPGVRFRVAHTGLTMAEYFRDVEGQDVLIFIDNIFRFVQAGAEVSTLLGRLPSAVGYQPTLNTDVGEVQERITSTKKGSITAIQAVYVPADDITDPAPWSIFAHLDATTVLTRRLAELGIYPAIDPLESTSKYLAPEYVGEEHYEVAMEVKRILQRYKELQEIIAILGMEELSDEDKAIVNRARRIQKFLSQPFHVAEQFTGMPGKYVKLEDTIRSFKEVLTGKYDHLPENAFYMVGTIEDVIEKAKQMGAKV", "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": "MYAVVRTGGKQYKVSEGDFLKVEKLEGAVGDTVELSEVLMVGGDKVAIGTPLVPSASVVGKIVEQGKDKKILVFKSKRRKDSRKLNGHRQLRTILKIEKINA", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MNTFSQVWVFSDTPSRLPELMNGAQALANQINTFVLNDADGAQAIQLGANHVWKLNGKPNDRMIEDYAGVIADTIRQHGADGLVLLPNTRRGKLLAAKLGYRLNAAVSNDASTVSVQDGKATVKHMVYGGLAIGEERIATPYAVLTISSGTFDVAQPDASRTGETHTVEWQAPAVAITRTATQARQSNSVDLDKARLVVSVGRGIGSKENIALAEQLCKAIGAELACSRPVAENEKWMEHERYVGISNLMLKPELYLAVGISGQIQHMVGANASQTIFAINKDKNAPIFQYADYGIVGDAVKILPALTAALAR", "text": "FUNCTION: Required for anaerobic carnitine reduction. May bring reductant to CaiA. SIMILARITY: Belongs to the ETF alpha-subunit/FixB family."}
{"protein": "MPIQPFDQREWNEPMHSLRISVGGLPVLASMTKATDPRFRPRWRVILTSFVGAALLWLLYSHHQGPVPGRPPTHNAHNWRLSQQRISHYNDTYPLSPPQRTPGGIRYRIAVIADLDTGSRAQEENTWFSYLKKGYLTLSDSGDRVSVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVIYQIEGTKAVPWVILSDGDGTVEKGFKAEWLAVKDEHLYVGGLGKEWTTTTGEVMNENPEWVKVVGHRGSVDHENWVSSYNALRAAAGIRPPGYLIHESACWSDTLQRWFFLPRRASHERYSEKDDERKGSNLLLSAAQDFRDISVRQVGTLIPTHGFSSFKFIPNTDDQIIVALKSEEDNGRIATYVMAFTLDGRFLLPETKIGTVKYEGIEFI", "text": "FUNCTION: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > IDP >> UTP > CDP = GTP = ITP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Note=Processed form: Secreted. SIMILARITY: Belongs to the apyrase family."}
{"protein": "MGTIKSGDIEKGTFLLFKGMPHIVLEREFSKMGRGGSIVRLKLKNLKNKSVVKETLKGADTVEEIEVLEVASQYLYRENENLIFMDLETYDQFDVNLREISNIEDKVMFLQEAGIYSLVKWDNEVIDLRLPPKVAFEVVDAEIAVKGDTVTNAMKNVTLHTGLVVKAPLFINVGDKILVNSETKEYAERVKE", "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": "MQRLCAYVLIHVLALAACSEASWKPGFQLQDASSGPGANRGKEPHELDRLGPASHHRRQLGLQGPPHLVADLAKKQGPWMEEEEEAYGWMDFGRRSAEEGDQRP", "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": "MKIKIQKIHPNALIPKYQTEGSSGFDLHAVEEVTIKPHSVGLVKIGICLSLEVGYELQVRTRSGLALNHQVMVLNSPGTVDNDYRGEIKVILANLSDKDFKVQVGDRIAQGVVQKTYKAEFIECEQLDETSRGSGGFGSTGVSKA", "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": "MRGGKKGQQTAQKNRINEEITAQEVRLIDIDGEQAGIQSLKDAQTMADAAGVDLVEISPNAEPPVCRIMDYGKFIFEKSKELKEQKKKQKQIQIKEIKFRPGTDEGDYQVKLRNLRKFLEAGDKAKITIRFRGREMAHQEIGIELLNRIKGDLEELAVVESFPNRVEGRQMVMMMAPVAKK", "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": "MSINTDESTWRTFKRLWTFIRLYKSGLAVAVVALIINAVSDTYMVSLLKPLLDEGFGSAESDFLRTLPLLVFGLMFIRGISSFVSTYCLSWVSGNVVMQVRRMVFNHYMQMPVSYFDKEKSGSLLSRITYDSEQVSAATSQALVSIVREGTSIIGLLVLMFYNSWQLSLVLILVAPVVAWAIGFVSKRFRKISKNMQTTMGIVTSSAEQMLKGHKVVLSYGGQEVEKSRFDVVSNQMRQQSMKLITAQAAANPIIQMIASIAIVVVLYLASVDTIKDQLTPGTFTVVFSAMFGLMRPLKALTNVTSQFQRGMAAAQTLFALVDLEPEKNTGTYSVERAKGEVNVKDISFTYEGAEKPALSHVSFDIPRGKTVALVGRSGSGKSTIANLFTRFYDVDSGEIQLDGVDVRDYELKNLRTQFALVSQNVHLFNDTIANNIAYAAGDKYSREDIERAAELAHAMEFISKMENGLDTVVGENGASLSGGQRQRVAIARALLRDAPVLILDEATSALDTESERAIQSALDELQKNKTVLVIAHRLSTIEKADQILVIDDGAVVERGSHSELIEKDGAYAQLHRIQFGEG", "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": "MDFPSQSEKKKYITKKRTTLFSYDDDDDDDDFDQNREFIHMSSYEESKDQQNSFNTLLLSELSNCEDQKQQQQQQSSSPTQSDCDSSPTNNNNNNNTNNNIVHHLNNSNSIPISGSNNNNNNNNNNNNNNNNNNNNNNNSHHHHLRKGRRLFHDDNDDQPIYPASASLSSTKTNMFPSSPILYSSPSSQQQQQQQQQQSQSQQTNEFKVPSFTPLSFINNSSTNSMNIRPINNNRIYNNLNNNNNNNNNNNNNINNINNNNINNINNNYNNNNNNEEDQIFSSSLPTSPVSWSANGSMMNGHNINNITGNHSRFLSNGSYNKGNTFPSTEVKRVRPDQRAFNENSFSMSPTPSPPPTPSLKRNNYSSPKFEPVFIRLAEERTNRKRSTSMTSNVNNNNNNNANNNNVNNNNNNNNGPNSISSLIANVNPFTEEGRLQSLNKPCPSFQLVNNNNNNNNASNNNNDNNNNNNNNNNNNNNNDDTCNNNNNNSQNIDNNLITKFSLYKHTFQELDLIGEGSFGHVYKVRHRIDGCLYAIKKTKKPLKGQKDRDIVLREVYGLSAIKDHTNIVRYFNAWEEDSHIFIQMEHCNGGNIYKWVTEHIKQSESNLLLLAKQILTGIVYIHSLGLVHLDIKPENIYIIYKCNQNQIITNNNNTCSINNSSNGSDSYFKSKIKTTENDLDNFITTTNSVNNNNCNNNNNNNVDNQNNNNQNNYLIIDGNKINFNSITFKIGDLGLLNEATNTKIYSEGDSRYLSRELLHDDMSALKKSDIFSLGCTLYELARCKPLPKSGMEWDSIRNGILSFEKEDSIYDDNKNDFSTEFWQLIKSMIHPDPSVRPSAEQLLEHPLIKYGVIEIDDFENEIETLKNLLAEKEKVLIIQKEKQKLRQNQLQQKMQQPNFIELKQQPQQQQEKQQMLHQQKQQYLEQHNNNNDNNNNEFDESEKEYQIQLEQFKIQKMQFQLQQEQLQYQHQHKHQNFFTKQICTASQIEGGIKNMAL", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily."}
{"protein": "MAAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSNPASQIYVASKRKACDEVGFVSRSYDLPETTSEAELLALIDTLNADNTIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKDLRHHVEHADLLIVAVGKPGFIPGEWIKEGAIVIDVGINRLENGKIVGDVVFDEAAARASYITPVPGGVGPMTVATLIENTLQACIEYHDPQGK", "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": "MSTGSLPLGLPSRDSLDGLRNSVDLPLLAAAALLLGLGLIMVASASMDLGERYYGNTWHFFQRQVLFAAIGLALATVMWAIPLERWERAGPWLLILVMVLLIAVLLPGVGRTVNGATRWIPIGMFNLQVAEPVKLLVVMYLAGYIVRHYSALRLHLRGFVRPLVVLGFGTVLLLLQPDFGGAAIMLAIGMGMLFLAGAKLWQFAALGATIAVGMAFVAVAAPYRVARLTAFLDPWQDPFATGFQLTQSLIAIGSGGWFGTGLGNSVQKLFYLPEAHNDFLFAVFAEEFGFIGVLALIALFAVVVWRCVKIGLWAERAGHAFGSHLAFGVAIWLALQSALNLAVNMGLLPTKGMTLPFLSYGGSSLIVTLMAIGLVMRVYREAQIPAPRQSTPPRRKRGQA", "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": "MEGIFNSKSLYEYLEEQKQAGISKTKEISLYYKATSKSVGDDEYSLRIWLDYIRLLMDGTKDVTEARETFKMIKMRFCKFYNYWEAYVRFEIEAGNGSLCKILQHSIDFVKVKEFTEKKRVLEYLECVMSYARNGEDLSVFCRGPETSFKPGAQVLSPFEARIGEQSKNKVLKKEHEESGPGHRDDGKNLLSRSGRAHLAPDECKENDNKNRAREDGASLSPSFAAKSKNCGATFGTIPIRFEKEDYSQGITMEINAALGRTSPEGSNSSPRSGAVRSRERIIIKGREIEILKQIGKGGSSKVYKVLFGSNVYALKRVELIGDEKMLSSYINEINLLYKFKGTSEIVEIIDHEVGEDYLHILLEYGETDLSKIIRKGGLSMNFIKDVWEQMLLIVKRVHIERIIHCDLKPANFLFVKGRVKLIDFGISKVIRNDTTSILSEEQCGTVNYMSPEAVTQNKSKVARSSDIWSLGCILYEMVHSNPPLHEYPNLIQKIQRLQEYSEFKYTSKNKAAVMVMKECLARDPKKRPTIDNLLNHRFLTGEMCLESLRELVEKILKIDGGDRVDPEHVDRIAEQLHSTHRQDQA", "text": "FUNCTION: Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication. Dual specificity kinase that can phosphorylate serine, threonine and tyrosine residues (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MKVLLIGGGAREHAIAMALKKNELVELYTLMKNKNPGIYAISDEVSFNSETDVPAIKEFAEKIKPELAVIGPEAPLGVGAADLLIEMGIPTVGPKKLPAQIETSKEFMRNLFKKYEIDGSLRYAAFNEYGNDLETFIDEMTSLGKDVVVKPAGLTGGKGVKVVGEQLKDNEEAKIYAKEVFDKSIGGGNIIIEEKLVGVEFTLHGFVDGENIVFMPAVQDHPHAYNNDEGPITGGMGSYSCPNHGLPFLSAEMLDRAEKIMEKTVSSINSEVGPYNGFLYGQFMLTADGPKIIEYNARFGDPEAMNLLPILKTDFLDVCFAIAEGKLDKINLEFENKATVCKYVVPNGYPIDPVRNKELTVDEKAIENADAILFYASINEKNGKLYITGSRSAAVVGISENIEEAEKIAQMAIENFKGEVYYRSDIGTLGLIKKRIERVKQLAK", "text": "SIMILARITY: Belongs to the GARS family."}
{"protein": "MFLKTGDKVRVITGKDKGQEGTIKKTFAKENRVIVEGVNKIKKHQKPSNMNPNGGIIDTEAPINASNVMLLDPSTNEPTRVGFEVVDGKKVRVAKKSGKQID", "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": "MRFFCFGMLLPFTFVLANEGLQLPLETYITLSPEYQAAPQVGFTHNQNQDLAIVGNHNDFILDYKYYRSNGGALTCKNLLISENIGNVFFEKNVCPNSGGAIYAAQNCTISKNQNYAFTTNLVSDNPTATAGSLLGGALFAINCSITNNLGQGTFVDNLALNKGGALYTETNLSIKDNKGPIIIKQNRALNSDSLGGGIYSGNSLNIEGNSGAIQITSNSSGSGGGIFSTQTLTISSNKKLIEISENSAFANNYGSNFNPGGGGLTTTFCTILNNREGVLFNNNQSQSNGGAIHAKSIIIKENGPVYFLNNTATRGGALLNLSAGSGNGSFILSADNGDIIFNNNTASKHALNPPYRNAIHSTPNMNLQIGARPGYRVLFYDPIEHELPSSFPILFNFETGHTGTVLFSGEHVHQNFTDEMNFFSYLRNTSELRQGVLAVEDGAGLACYKFFQRGGTLLLGQGAVITTAGTIPTPSSTPTTVGSTITLNHIAIDLPSILSFQAQAPKIWIYPTKTGSTYTEDSNPTITISGTLTLRNSNNEDPYDSLDLSHSLEKVPLLYIVDVAAQKINSSQLDLSTLNSGEHYGYQGIWSTYWVETTTITNPTSLLGANTKHKLLYANWSPLGYRPHPERRGEFITNALWQSAYTALAGLHSLSSWDEEKGHAASLQGIGLLVHQKDKNGFKGFRSHMTGYSATTEATSSQSPNFSLGFAQFFSKAKEHESQNSTSSHHYFSGMCIENTLFKEWIRLSVSLAYMFTSEHTHTMYQGLLEGNSQGSFHNHTLAGALSCVFLPQPHGESLQIYPFITALAIRGNLAAFQESGDHAREFSLHRPLTDVSLPVGIRASWKNHHRVPLVWLTEISYRSTLYRQDPELHSKLLISQGTWTTQATPVTYNALGIKVKNTMQVFPKVTLSLDYSADISSSTLSHYLNVASRMRF", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Cell outer membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the PMP outer membrane protein family."}
{"protein": "MGFYMLLTVALLLTSLMNVEATPVNQAERSALEKSGLGNRIQPRYDNCGDAEADCYQSKCMDEETYDEECEASCNYVVANCI", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MLINFVKMHGLGNDFMMVDNLAGDITFNAEQIANLANRHLGIGFDQLLLVETSNTKNVDFRYVIYNADGLEVEQCGNGARCFAFFVSKKGLSNNNPIVVETRSGIINLYLNDDNTVRVDMGKPSFNPADILLLVPQQSTYYQIEGFDLGAVSIGNPHCVMLVEDVNTVDVSSIALRIQQSELLPNQANIGFMQILNTHEINLRVYERGSGETLACGSGACAAVVYGVEQGLLKENVVAHLNGGDTLIEYIQGGHVFLSGPVQFVFEGKVEI", "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": "MNPTVELRDIEALVTNLHADPFAILGPHRAEDGGAWVVRTYQPGASRVVLLGESGELAMENRRHPDLFECAVPTAPGAYRLRVEDAWGERLIEDAYRFRGSLLSDLDGHLFAEGNHHRIYEKLGAHPAVFEGVAGVYFAVWAPSARNVSVLGDFNRWDGRFHQMRRVERSTGIWELFIPELGEGTVYKFEIKNGFGHIYEKSDPYAFQQELRPKSGSVVADLDRYSWNDGEWLKRRALSNPLKQPLAIYEVHLGSWMRVPEEGDRFLSYTELADKLIPYVKDLGFTHIELLPILEHPFDGSWGYQVLGYYAPTSRFGNPTEFMAFVDRCHQSGIGVILDWVPAHFPKDGHGLALFDGTHLYEHADSRQGEHKEWGTLVFNYGRNEVRNFLIANALFWFERYHIDGIRVDAVAAMLYLDYSRHDGEWVANRYGGRENLEAIGFLRQLNELIFLYYPGALSIAEESTAWPLVTRPPYLGGLGFNLKWHMGWMHDTLAYFRTDPLFRRYRHNDITFSITYTFYENFVLALSHDEVVHMKGSIIGKMPGDGWQKFANLRALFTFMYGHPGKKTLFMGMEFAHGREWNAYQSLDWHLLDYPQHRQMQQFVRALNRLYTGQPALYEEDCNPAGFFWVDCHDVLNSVFTFVRRGKDPSEQLLFVCNFTPTYHPHYRVGVLETGFWQEIFNSDSGIYGGSNKGNLGGLWSENWAIHGQPYSLGLQLPPLGCLVFKRRKEQD", "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": "TICYSHTTTSRAILKDCGENSCYRKSRRHPPKMVLGRGCGCPPGDDYLEVKCCTSPDKCNY", "text": "FUNCTION: Inhibits acetylcholinesterase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Acn-esterase inhibitor sub-subfamily."}
{"protein": "MISGIRVNDNCVTEFNNMKIRKTCGWIIFVIQNCEIIIHSKGASTTLTELVQSIDKNNEIQCAYVVFDAVSKIHFFMYARESSNSRDRMTYASSKQAILKKIEGVNVLTSVIESAQDVADLK", "text": "FUNCTION: Not involved in actin polymerisation, instead functions to stimulate nucleotide exchange on monomeric actin and influence turnover of the small amount of cytosolic actin microfilaments. Essential for erythrocytic schizogony (By similarity). FUNCTION: Not involved in actin polymerisation, instead functions to stimulate nucleotide exchange on monomeric actin and influence turnover of the small amount of cytosolic actin microfilaments. Essential for erythrocytic schizogony. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MVISDYFEIERAYAKLNLYLDVLSKRPDGYHNITGLFQTIDLHDELEISQIDKRGEVRIETNIEIQGTNLIEKAFRTVEKFYNVGFGIKVRLKKNIPMGSGLGGGSSDAAAVLRFLGRKLKISIKDLLILAAEVGSDVPFLIVGGTAIVEGRGEKVTFLNPISDYRVDLFCPTISVSTKFAYQMIHESTYAKKPDFALKLYEAYLKRDHNQIKALSYNVFQEIMTSKYPQIQDALDKAQRCNPIVAMMTGSGSCIFAVQADKGKYRFIEDVFQHL", "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": "MDSKKHKIINGYYHKNCISCKSWLPATEENFYSVKKNKDGLHSYCKACVLKKAKESMLKNYDKQLERMRERNLLPGMKEAKKKYNSSLKKKKTQQIWQEKNKLKLKNYRLQRDAHKKHNITDVQWQKCKDYFNNKCSYCGLKIEDHKILFKGTYIQSDFHKEHVDHKGANDISNCIPACKSCNSSKHDFAFEEWYNSSNKNFSSERLLKIKEWLNRFKEERQDSEWRTKG", "text": "SIMILARITY: Belongs to the HNH nuclease family."}
{"protein": "MVTIKKDFIPVSNDNRPGYAMAPAYITVHNTANTAKGADAKMHAKFVKNPNTSESWHFTVDDSVIYQHLPIDENGWHAGDGTNGTGNRKSIGIEICENADGDFEKATSNAQWLIRKLMKENNIPLNRVVPHKKWSGKECPRKLLDHWNSFLNGISSSDTPPKETSPSYPLPSGVIKLTSPYRKGTNILQLQKALAVLHFYPDKGAKNNGIDGVYGPKTANAVKRFQLMNGLTADGIYGPKTKAKLKSKLK", "text": "FUNCTION: Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Could play a role in mother cell lysis with CwlC. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family."}
{"protein": "MIENRRGLDIFCHVMLIIGVLLILFPLYVAFVAASLDDTQVFQVPMTLIPGPHLWQNISHIWHAGVGNNSAPFGLMLFNSFVMAFAITVGKITVSMLSAYAIVYFRFPLRNLFFWLIFLTLMLPVEVRIFPTIQVIANLNMLDSYTGLTLPLMASATATFLFRQFFMTLPDELLEAARIDGAGAMRFFWDIVLPLSKTNLAALFVITFIYGWNQYLWPILITSDASMGTAVAGIRSMISSSGAPTQWNQVMAAMILTLIPPVAVVLLMQRWFVRGLVDSEK", "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": "MAETKDQNVLNIIIISDAAGDTAFSNATAAAAEFPNAEINYRRYPFITNLEKLDEVLKEIEKYPNLVIIFSLVKDEMQIPVIKFARDHNIQCVDIFSPVVEAIQQTTHMIPDQKIGAQHSLNQKYFDRISAMEFAVMYDDGKDPKGFLEADVVLLGVSRTSKTPLSLFLANKNLKVANLPLVPETHIPKEIYEIDPKKIIGLTNDPSVLNEIRRQRMIAYGLNPDTTYSSMDSINKELESAQALYKKLGCYVINVAHRSIEETAALILEHLGIDDYAK", "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": "MSVESSSAPGSVPTTSTVRKPRPGRETTREKSGTSPIEACVEAAPRANVSSGSGARTMANWAKETCDAVCHGGGARRRTPLERISEADEDAEECGNSANLPTRYEFANMLARGMPTAELVRAVVAHVIPRFFFEIRTAPGMPVVFAADSVSAILVGRDGSEMELELVSGTSMTMEDYFDAYLEMDNHLGFVFSVLTGAEDRVGSVALTWTELIDRMYVIQPNTSVDFSLCVLCMYLENVAEEDVTLSHCVMLKAALDKLKRKITFHAKVAALLANGCEWLLNTLMAMHDLPAFDRELILPHYGVAKPLMSVESEGLEELIRGLYDTHTITVINMPEPGHSDVQIMLEARKSTLNRVYENGNYYSRVLRLWWNTPLKRKNAYAMYHVYK", "text": "FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm. SUBCELLULAR LOCATION: Virion Virion tegument Host cytoplasm Host Golgi apparatus. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 1 family."}
{"protein": "MHYVDPNQSGSKIHFKDQYENFIGGQWVAPVKGVYFDNISPVDGKSFTRIPRSSAEDIELALDAAHKAKKEWNKSSPTTRSNLLLKIADRMEANLEMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMAAWKLAPALAAGNCVVIKPAEQTPVGILLVAELIQDLLPAGVLNIVNGYGAEVGRPLATSPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNVFFADVMDHDDDFLDKTLEGFAMFALNQGEVCTCPSRALIQESIADQFMEKAIERVKRIKLGHPLDTDTMVGAQASLEQQEKILRCIDTGRQEGAEVLLGGHGRQEVGNGYYIEPTIFKGHNNMQVFQEEIFGPVLSVTTFKDFDEAIQIANDTMYGLGAGVWSRSTHTAYRAGRAIEAGRVWTNCYHIYPAHAAFGGYKKSGVGRENHKMMLDHYQQTKNLLVSYSTKAMGFF", "text": "FUNCTION: Aldehyde dehydrogenase that shows activity toward n-alkanals (C(4) to C(14)), with a preference for longer carbon chains. The best substrate is tetradecanal. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MTHEAVDTTPLHGTGWSFRSAMYDPKYRSIFYQILTIVILVGFVWWVAHNTAVNLARSNTASGFGFLRGRAGFEIGQSLITFSSDSTYARALLVGILNTLLVAVTGIFTATIIGFLIGIGRLSRNWLIAKLCTVYVEVFRNIPPLLVIFFWYLGVLSVLPQPRESVGLPFSMYLNNRGLAFPKPIFDTGMIAVGIALVIAIVASIIIARWAHKRQAATGQPFHTVWTAIALIVGLPLLVFVVSGFPLTFDVPVAGKFNLTGGSVVGPEFMSLFLALSFYTASFIAEIVRGGIRGVPKGQSEAAGALGLHPSSVTRLVVVPQALRIIIPPLTSQYLNLTKNSSLAIAIGFSDLVAVGGTILNQSGQAIEIVCIWGIVYLSLSILTSLFMNWFNAKMALVER", "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": "MSYFEHIPAIRYEGPQSDNPLAYHHYDPDKRVLGKTLAEHLRIAVCYWHTFVWPGHDIFGQAAFRRPWQQPGDALERARMKADAAFEFFTKLGTPFYTFHDTDVAPEGDSLREYAANFARMVDYLGERQQASGVRLLWGTANLFSHPRFAAGAATNPNPDVFAWAATQVCHALDATHRLGGENYVLWGGREGYETLLNTDLKRERDQFARFLSMVVEHKHRIGFKGALLIEPKPQEPTKHQYDYDVATVHGFLVQYGLQNEIRVNIEANHATLAGHSFHHEIANAFALGVFGSVDANRGDPQNGWDTDQFPNSVEELTLAFYEILRHGGFTTGGMNFDAKVRRQSIDPEDLFYGHVGAIDVLALALERAAVLVENDRLDALRRQRYAQWDDAFGRKILAGGYTLESLAADALARGVDPQHASGAQERLENIVNQAIYGLR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family."}
{"protein": "MAAPWWRVVLNGSRNWRGFSTSAALSRRAAPLGPMPNEDIDVSNLERLKKYRSFDRYRRRAEREARDPHWWRTYREHFGEESDPKDTVDIGLPPPKVCRTQQLLERKRVLRELRTSVEEERASRLRTASIPLEAVRAEWERTCGPYHKQRLAEYYGLYRDLFHGATFVPRVPLHVAYAIGEDDLVPVYYGNEVTPTEAAQPPEVTYEADEGSMWTLLLTNLDGHLLEPDAEYVHWLVTNIPGSRVAEGEETCPYLPPFPARGSGFHRFAFLLFKQDKPVDFSGDTRPSPCYQLAQRTFHTFDFYKKHQDAMTPAGLAFFQCRWDDSVTHIFHQLLDMREPVFEFVRPPPYHPKQKCFPHRQPLRYLDRYRDSHEPTYGFY", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family. Mitochondrion-specific ribosomal protein mL38 subfamily."}
{"protein": "MILEDLLMVLSCLALHILWKVQAVPILPLSLVPDTFDDAYVGCSEEMEEKAGLLLKEEMARHALLRESWEAAQEAWAHGRHKLTLPPGFKAQHGVAVMVYTNSSNTLYWELNQAVRTGGRSRELYMRHFPFKALHFYLTRALQLLRGTGGCSREAGEVVFRGVSSLHFEPKRLGDSVRLGQFASSSVDERVARRFGNATFFNLRTCFGAPIQALSVFPEEREVLIPPHEVFLVTGFSQDGAQSIVTLWSYNQTCSHFNCAYLGGEKRRGCVSSRAGQPESFSTEALALQSGKTLLLAPGELQLSRAGP", "text": "SUBCELLULAR LOCATION: Secreted Membrane Note=Membrane-associated. SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family."}
{"protein": "MTVSPSSQTGRGEIGRDELVRWLGEYLRIGAYPDPSLNGLQIQGTDKIRRIAASVDTSLQTLQAAAESGADLLLVHHGLFWGRPLAITGPHYERVRTAIQADLNLYAAHIPLDAHPEVGNNAMIARALSLTDLQPFGDWQGHKIGVAGTLPRELGLQDFADRIQKLTGEICLVHGGGSPNIHRVGVTSGSGAGAIAEAAAMGLDTLLTGEPEHKYFHDSFEYGVNVIFAGHYETEVFGVRALAARIEDEFGIPWQFLNFPTGL", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family."}
{"protein": "MNCPVPENQLPINEYNKLTSAWDFSWACKIGKLYYKFLLKMQLCLFLFFCICLNFLDSKYETGLYSLILSTLFICLICLRTYLGFRYIYVRLLKSALPYEESSWYDGQVWVKNINYLIKDRLVADYTVLPILSRLKISFTINFSFLICLLLRFIF", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf36 family."}
{"protein": "MADNIDLELSLQTNHSMIINKRLTQSDVDYNNRLHLPKREFEQFILPEMEWELVMNLRNSVEVIVKDVNGNEYHVTLVKYQNGHYYFMGKWMDIVRAKGYKRDDEISLLWDKSNEVFYII", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAKRYLLDFEKPLVELEKQIEQIKELARDSEVDVSQQLLQLETLATRRREEIFKSLTPAQKIQVARHPQRPSTLDFVQMFCDDWIELHGDRNGGDDMALIGGIGSINNRPVLMLGHQKGRDTKENVVRNFGMAKPGGYRKALRLMQHADRFSLPILTFIDTPGAYAGLTAEEQGQGEAIARNLREMFGLTVPIVATVIGEGGSGGALGIGVADRLLMFEHSVYTVASPEACASILWRDAAKAPEAASALKITGKDLLKLGIIDEVLPEPSGGNNWAPLDAGNTLKEAIEKHLDTLLQMTKDELIEERYKKFRVLGKFIEANNIEEIYSEIPPQSE", "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": "MIDQYKHKQLQIGLVSPQQIKAWAKKILPNGEVVGEVTRPSTFHYKTDKPEKDGLFCERIFGPIKSGICACGNSRASVRENEDERFCQKCGVEFVDSRIRRYQMGYIKLACPVTHVWYLKGLPSYIANLLDKPLKKLEGLVYGDFSFARPSAKKPTFLRLRGLFEDEISSCNHSISPFFSTPGFATFRNREIATGAGAIREQLADLDLRIIIENSLVEWKELEDEGYSGDEWEDRKRRIRKVFLIRRMQLAKHFIQTNVEPEWMVLCLLPVLPPELRPIVYRSGDKVVTSDINELYKRVIRRNNNLAYLLKRSELAPADLVMCQEKLVQEAVDTLLDSGSRGQPTRDGHNKVYKSLSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHQCGLPLEIAIKLFQLFVIRDLITKRATSNVRIAKRKIWEKEPIVWEILQEVMRGHPVLLNRAPTLHRLGIQAFQPTLVEGRTICLHPLVCKGFNADFDGDQMAVHLPLSLEAQAEARLLMFSHMNLLSPAIGDPICVPTQDMLIGLYVLTIGNRLGICANRYNSCGNSPNKKVNYNNNNYYKYTKDKEPHFSSSYDALGAYRQKRIGLNSPLWLRWKLDQRIVGSREVPIEVQYESFGTYHEIYAHYLVVGNRKKEIRSIYIRTTLGHISFYREIEEAIQGFSRAYSYTI", "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": "MRSNYCTELDSGDIGKIVDVCGWVNSYRDHGGVIFIDLRDRSGLIQLVCDPKHSQEAYTIANSVRDEFVLRAHGKIRARGKDLINPKLKTGEIEVVVENLIVENPSKPLPFVIGDKNVSEETRLKYRFLDLRTNENFNKFFTRSKAAIAARNALDRLGFVEVETPILTRATPEGARDYLVPSRVYNGQFYALPQSPQLFKQLLMCSCFDKYFQIARCFRDEDLRADRQPEFTQIDIEMSFCDQKDVMKVGEAVLKDIFKSCGKDIKTPFRVMQYKDAMENYGSDKPDLRFGMKFIDVADIFEKSSNEIFANIAKDKKKNRVKAIKVEGGDLKFSKRQMQRFEEYVRKFGAQGLAFIQVKEEGLKGPLVKFFEKSEIDELVKRCELKVGDVVFFGAGKKKIVLDYMGRFRIFLANELELINPDALEFLWVVDFPMFEQNEDGTYSAMHHPFTMPNNVDEPDIEEITSIAYDVVLNGIELGGGSIRIHKEDIQEKVFKLLKIEPAEQREKFGFLLDALSFGAPPHGGIAIGFDRLMMLVTRSSSIRDVIAFPKTQRAQCLLTKAPSGISNEQLRELGLKINKKEQK", "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": "MILNFIIDSSSFEKGLGNIAIWSKLNDPKLTINAYLPLFTIQELDFQRFKRKSVVAKRALHFIDLLQDSTSFKLHLEYPELNEAISWNETVKLCQQNSHTSLSQHQISVIPIRFKKLLKSCYYKCHYKSHDLDEDIDHTNEKSDPDDKGWVLVTEDDTVRSLATQFQIPFISVVEADAIINACIKDKSYVVNEKFSKTVIKKANKVKEQEDGKKVFVTDFKNDFLAPRAKSGELWTPTSAKNKS", "text": "FUNCTION: Involved in nonsense-mediated decay of mRNAs containing premature stop codons. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSDKQINLVIVTGMSGAGKTVAIQSFEDLGYFTVDNMPPALVPKFLELLERTNETQKVALVVDMRSRRFFKEINSILDHIELNANLKLRILFLDATDSELVSRYKETRRSHPLAADGRVLDGIRRERELLVPLKSMSQHVVNTTDLTPRQLRKVISDQFSSESDQASFRIEVMSFGFKYGLPLDADLVFDVRFLPNPYYQVALREQTGLDQAVFDYVMTHQESEAFYNHLLGLIVPILPAYQKEGKSVLTIAIGCTGGQHRSVAFAHRLAQDLTADWPLHESHRDINRRKETVNRS", "text": "FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family."}
{"protein": "MPHTSPETEAQRDSNAPLVVVLLGPTASGKTALALELAERFDLEIINVDSRQLYQEMSVGTAKPSPEQQARIRHHLLDLRPPDQPITLQEFQEEALQAVNQSLAKRGAAFLVGGSGLYLKALTAGLRPPAVAPQPALRRQLAQLGQPLCHQLLNTADPEAAVRIASADALRTQRALEVLYATGAPMSRQTSASPPPWRVLELGLNPLDLRQRISARTQALYSQGLVEETRQLRERYGPELPLLQTIGYGEALQVLAGDLSRPAAIAHTTRRTQQFAKRQRTWFRRQHQPHWLPDDNPLNEAGRLIEAGLG", "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": "MISYIKGELAEILPDVIVVEANGIGYNIYVPGSVPGELPSVGSEVKIYTYMNVKEDECSLFGFLTRDDLSMFKMLICVNGIGPKAALGALSNITADDLRFAVLADDVAAIKALPGIGPKTAQKIIIELKDKLKLDEVFESALSKNKKADNNSNVSNVMMIRNDAVEALVSLGYSSKDALVAVKEVEDIENKDSETVLKEALKKLVKF", "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": "MNRHLTGKQKFAFGFGAIGKDAIFNIVSVFLMFYITDIVGLSPAFVGVMLFVARIWDAINDPIMGMIVDNTRNNFGKFKTWLVIGTLINAVVTVLLFTNFDLSQTAMYIYISIIYISWGMTYTMMDIPYWSWLPNLTHDPREREELSVIPRFFASLAAFTVGTFGLFFIHKLGDIFGGGSDSTGIFVFAIICSLIFIFTIGVTVFKVPEDQEMEKLIGIKVKFKDIGRILFKNKELLAIMGVLLTFNLCLQTLNGSIIYYFKYVVNAEHLFAIFNSMILCEMVGLLLLPRFIKWVGRTAAFNTSIICIISGLLIILISGYIAPQSMTLIIIGAGILRIGSGFMVGITTVSLADVIDYGEVKFGQRNESIITSTNTFLTKTSQAVAALIVGLGLSILGYTPNEAQSVVTINGLRIMILVSPLVFICLAAFLYHKAFNLKGDFLTDIEKTLQYKRQREFRERIK", "text": "FUNCTION: Responsible for transport of beta-galactosides into the cell, with the concomitant uptake of protons (symport system), and also for transport of homologous and heterologous exchange of beta-galactosides. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:galactoside symporter (TC 2.A.2) family."}
{"protein": "MKKQEQNQFLKEFGISLIKMFPKYIDKAIYSKGELTLHVKPTNLIALMKILKNHTNCQFKSLSDLCAVDFPEKKERFEIVYNLLSVRYNSRIRVKTFVDELTPVPSVTCLFQAAGWFEREVWDLFGVYFTNHPDLRRILTDYGFEGHPMRKDFPLTGYVEVRYDDEQKRVVTESLEMTQEFRSFNFTSPWEQIEISKPNIKEKK", "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 30 kDa subunit family."}
{"protein": "MDYSSRDDLLFHYNSLPFNVNDTQDMLLYNLVAEGSSQETVNSSSSYGIKEEEVTSYEEERKDKNYRGVRKRPWGKYAAEIRDSTRNGVRVWLGTFDNAEEAALAYDQAAFAMRGSMAILNFPVEIVKESLNEMKCRFDGNCSPVIELKKRYSMRRKSVSRKNRARKDVVVFEDLGAEYLEELLISSESITNW", "text": "FUNCTION: Transcription activator that binds to the GCC-box cis-acting elements found in the promoter regions of ethylene-responsive genes (PubMed:23057995). Acts downstream of MYC2 in the jasmonate-mediated response to Botrytis cinerea infection (PubMed:28733419). With MYC2 forms a transcription module that regulates pathogen-responsive genes (PubMed:28733419). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MAKLIVDDLDVKGKKVLVRVDFNVPIKDGVIGDDNRIVAALPTIKYIIEHGGKAILLSHLGRVKSDADKKELSLKPVAERLSELLKKPVTFVPSNEGKEVEDAINNMKDGDVVVLENTRFQDIDNDFGKRESGNDPKLGEYWASLGDMFVNDAFGTAHRSHASNVGIATAMKGNGKLAAAGYLLEKEIKYLGDAVDNPVHPFVTILGGAKVSDKIGVINNLIPKSDHILIGGGMAYTFLAAQGHEIGKSLFEADKVDLAKELLEKAGDKIVLPVDNVAATEFSNDASREVVGDDIPDNMMGLDIGPKTIAKFKDILKDAKTVVWNGPMGAFEMPNFAEGTLEIGRALANLTDATTIIGGGDSTAAAKQLGIAPKISHISTGGGASLNYLEGKVLPGIACVQDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MSKNDLVKTLRMNYLFDFYQALLTKKQRNYLELFYLQDYSLSEIADTFDVSRQAVYDNIRRTGDLVEDYETKLELYSKFEQRREIYNQMKASIEDPDALKRYIEELEELE", "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": "MEVNTYLNAIILVLVVTIIAVISTSLVRTEPCVIKITGESITVLACKLDAETIKAIADLKPLSVERLSFH", "text": "FUNCTION: Plays a role in viral cell-to-cell propagation, by facilitating genome transport to neighboring plant cells through plasmosdesmata. May induce the formation of granular vesicles derived from the endoplasmic reticulum, which align on actin filaments. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the Tymovirales TGBp3 protein family."}
{"protein": "MNKGYPITDLVILAGGQARRMNGLNKLLQQFDGDTQLLKIHQKLKSSVSEIWVNSHRDYSIYQSIVPDIKCFQDDASGFFGPLMGMKSAWSHVRADYVLFIPCDVTYIPTQVVAKLHSALRKNKQAQAAYVSINGDALYPFCLLKRESLEVLEQQIDKQQLSLKNCFKLLHAQVAIFQKQNLFFHSINSLDELQQYKQIKAFKEIFSTN", "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": "MSPLKKTYVLKLYVAGNTPNSVRALKTLKEILEQEFQGVYALKVIDVLKNPQLAEEDKILATPTLSKILPPPVRKIIGDLSDREKVLIGLDLLYEELNEDEYNL", "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": "MSSSSGPLSPQSTTATSSLAAKAANPLSSKVTTVLSSSYADTEFREALALLDERGVQNTAETRRQLRLDLQKEVIDSNGEIIDEFAKVAEQLRRIGTTIGRLNETFNEMKTQIGSAQKTTSSTLIEASQLMIQRRQVEQKQALLGAFNTNFVLSEDETAALTLTSEPVDDLFFAVLAKAKRISKDCEILLGFENQTLGLEIMEQTSKNLNLGFQKLYKWVQREFKTLNLENPQIGSSIRHALRVLAERPSLFQNCLDFLAEAREHVLSNSFHTALTGSSPSGIEDQSVKPIELVAHDTLRYVGDMLAWAHSAAVGEREALEGLFIGEGDEIAKGIQAGRDNEIWRLVAEDGEVSDTFDAVETLNELVDRDLSGAARLLRQRVEQVIQTNEETILAYKLANLLNFYKSTFSRLLSVGSALVETLGALESEALRQFRSLARDHVAAIQGDFQHTPADLRPPEFLLGALEQLAAIMKTYETSFTSSSDREEEFEPVLAEAFDPFISGSANMAKPLRAPSNSIFLINCLLTAERSLSRFDFTQRRAARLQAQIQEERARLVETQYRFFRGESGLDSLIVQLEPLGESKEDIQKALLLESLQSPALSQASQKLDDFLPSALMDAMENLKNLQDSRLVQSITEEAAEKFCVDFEHVEEMLILVDEATEQKQNEQDDIQGPRTLFPRTSGEIRVLLS", "text": "FUNCTION: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COG6 family."}
{"protein": "MLYIFRLIVTVIYSILVCVFGSIYCLFSPRNPKHVATFGHMFGRLAPLFGLKVECRKPADAENYGNAIYIANHQNNYDMVTAANIVQPPTVTVGKKSLLWIPFFGQLYWLTGNLLIDRNNRAKAHSTIAAVVNHFKKRRISIWMFPEGTRSRGRGLLPFKTGAFHAAIAAGVPIIPVCVSNTSNKVNLNRLNNGLVIVEMLPPVDVSEYGKDQVRELAAHCRALMEQKIAELDKEVAEREATGKV", "text": "FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-acyl-carrier-protein as the fatty acyl donor. FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-acyl-carrier-protein as the fatty acyl donor (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
{"protein": "MDLNLDAPHSMGTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSANLIRMLAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAVSLAIARDGASGGVVRTVIINSEGVTRNFYPGDKLQLWHEELEPQNSLLDILNAAGPEPMAM", "text": "FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MSEFGAGAELPGWVTESRSRGEFFSPEESHAAAPAGFLQELPSYRSVLWRRAAAGDVQERWGNLRGIASAERREPQPDGGERGAIPLWELPFSIAEKRDSQQGDIKYSSGWNHWKRTSSKSWKKALKDIKELSSYMQLWRHDIHSIEGKFGTGIQSYFSFLRFLVLLNFLMFILMFSFVTLPAVISNYGIFNSSSTKISPNNTEPYCTVYTPSGNKGLVYFYTYLKDLLTGTGFLEVTVLFYGYYTIDAAWFSVLRYNLPLAYLLTTFAYLALSFVWIIKRSVERFRQHLVDDEDQFQSYCNKVFAGWDFCITDLNAARLKHRSLLYELQTNLEEERLKQKIAERTMKEKLQIYSLRIFINIIVIAVLSGCFYSIYRATVFSQENSSVSIRRNVMIANLLVQYLPSIVITSANFIAPQIFSFLIRFEDYSAAFEIRLTLIRCVFVRLANVGVLLFSLWSQIHCDNDQCKACGYDYELYPCWESAVGQEMYKLLIFDFMIIIAMTLFVDFPRKLLVTYCSWKLVQWWGLQEFGISDNVLEIIYGQTICWIGTFFSPLLPAIATIKYFIIFYIKKISLIHTRKPASRPIRASSSNFFFLAVLLIGLILAFVPLGVSIALISSSKACGPFRNFNTSWAIVPYTILEFPIGLQKFLYGIASEAFAVPFFVIACLFMFYFIALAGAHKRVVEQLREQLVTESRDKLFLLEKLSEAQKNSGKPQKARKLTSSWLLEPLDKG", "text": "FUNCTION: Probable ion channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMC family."}
{"protein": "MNLNNLENIRYNEIKEFSDKIKKEFTFSQKKQVMDIIEKLNKDSRKNVIKLGQALEKFLNKYEEELKRTNNMYNFDRRYGNNYLIAGVDEVGRGPLAGPIVAAAVVLDLNVEEMQRIFNIKDSKKLSEKKREELDIIIREKAISYNIALVDNKTIDERGISWSNNEVLKRAVEGLKVKPDLVLSDGYAVKNLNIRNEFIIKGDSKSISIASSSIIAKVYRDSMMKEYSKGLNMYGFNHNAGYGTEEHVQAIKKHGPSKIHRMSFLTNIL", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MAAYLTNRVLMSSLMFFVMTGSLNAQVADIKAICGKAKNQSFCTSYMKSNPKTSGADLQTLANITFGSAQTSASEGFRKIQSLVKTATNPTMKKAYTSCVQHYKSAISSLNDAKQSLASGDGKGLNIKVSAAMEGPSTCEQDMADFKVDPSAVKNSGDFQNICGIVLVISNMM", "text": "FUNCTION: Inhibits pectin methylesterase (PME) from flowers, siliques and pollen tube. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the PMEI family."}
{"protein": "MQVIEGGINAAGKKFAIIVSRFNHFMVESLLDGAVQTLKHYGEVADDDITVVRVPGAYEMPVTAKRLASSGKYDAIIAVGAVIRGGTPHFEFVAGECNSGLGRVATEFDLPVAFGVITTDTLEQAIERSGSKAGNKGSEAALSALEMVNVLKQL", "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": "MALSPRESAAKRAQRVRTRLKSLANGRPRLSVFRSSKNIYAQVIDDERGVTLASASTLEAEGKGADKDAAAAVGKLVAERAIEKGVKDVVFDRGSYIFHGRVKALADAAREAGLNF", "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": "MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGSLNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNAIAAAL", "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": "MQFDYIIIGAGSAGNVLATRLTEDPNTTVLLLEAGGPDYRFDFRTQMPAALAYPLQGKRYNWAYETEPEPYMNHRRMECGRGKGLGGSSLINGMCYIRGNAMDLDNWAKEPGLEHWSYLDCLPYYRKAETRDIGPNDYHGGDGPVSVTTPKPGNNPLFEAMVTAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPQGRRASTARGYLDQARGRPNLTIRTHALTDHIIFAGKRAVGVEWLEGESTIPSKATANKEVLLCAGAIASPQILQRSGVGNPELLRQFDIPVVHDLPGVGENLQDHLEMYLQYECKEPVSLYPALQWWNQPKIGAEWLFGGTGIGASNQFEAGGFIRSRAEFAWPNIQYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRLKSRDPHAHPAILFNYMSHEQDWQEFRDAIRITREIMNQPALDKYRGREISPGTECQSDAELDEFVRNHAETAFHPCGTCKMGYDEMAVVDGEGRVHGLEGVRVVDASIMPQIITGNLNATTIMIGEKMADAIRGRQPLPRSTAAYYVAGGAPVRR", "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": "MKVQPSVKKICDKCKVIRRHGRVMVICDNPRHKQRQG", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MALAVLRVLDPFPTETPPLAVLLPPGGPWPATGLGLVLALRPASESPAKPALLVAAVEGSGAQGEQRGPGPPPLLVSRALLRVLALGPGARVRARLVRRPPALGWALLATAPGPGLGPRVGPLLVRRGETLPVPGSRVLETRPALQGLLGPGTRLAVTELRGRAKLGQESRDHSHPPPPPVVSSFAASHSVRRLRGVLGGTGDALGVSRSCLRSLGLFQGEWVWVAQVAELPNSSQPRLAQVQVLEPRWELSERLGPNSGQQPGEPLADGLVFLPATLAFNLGCDPLEVGELRIQRYLEGSIAPENKGSCSPLPGPPFARELHIEILSSPHYSANGNYDHVLYRHFQTPRVVQEGDVLCVSTAGQVEILEGSLERLPRWREMFFKVKKTVGEAPEGPASAFLADTTHTSLYLAGTALSHVPSLPSGRSPPWDSLSPPGLEALVNELCAILKPHLQPGGTLLTGTSCVLLQGPPGSGKTTAVTAACSRLGLHLLKVPCSSLCADSSRAVETKLQATFSRARRCRPAVLLLTAVDLLGRDRDGLGEDARVAATLRHLLLDEDALSRCPPLMVVATTSRVQDLPTDVQTAFPHELEVPVLSEAQRLSILQALTAHLPLGQEVNLPQLARRCAGFVVGDLYALLTHTCRAACTRIRASGSAGGLSEEDEGDLCVAGFPLLAEDFGQALDQLQTAHSQAVGAPRIPSVSWHDVGGLQDVKKEILETIQLPLEHPELLSLGLRRSGLLLHGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENVREVFARARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSTQDVFVIGATNRPDLLDPALLRPGRFDKLVFVGASEDRASQLRVLSAITRKFKLEASVSLANVLDCCPPQLTGADLYSLCSDAMMTALKRRVRDLEEGLELRSSALLLTMEDLLQAAARLQPSVSEQELLRYKRIQRKFAAC", "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. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome membrane Cell projection, cilium, photoreceptor outer segment Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes (By similarity). Localized at the base of the outer segment of photoreceptor cells (PubMed:26593283). SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MGQNLSDEQPQRRSHEELTHELAERFRSKCFTSLEFYSLKDVFKSLADQQDSIRYMKEDTIARYLEIPDILGASPVIFQMVSYLGAFPFLQDAPVVLELPRMIMVIVIMTERYRTVLARGSADRTKLLFRSLAVFDRKPSESDALIPDAAQLDEPNGKDEKVQENSHVAGFAVDQAGDEVDDDDDEDDDLVLTAFELLDVKEAVDQGHAPKFHSATIPTDNFRKLLMLLLLAAPLDPQESLSLYSPHVVGEQLEGLRATAECILASFVNAETSTGIKYSHFKSIIPVICPNLFRGFNGLFEHFLFSKNLDFSKHQNDIPITKVAQPLLTDSGEILNHNTLCQISLFLPGSDLFRRVRLLYSGNDAGFSMGSFQTKVFNWQAPTLLLVSGTRLSDIPEGGQEVAFAASLPTKRFPHGSKSDQLTFGVYVREPWKHTHRECFGDADTVLFQLEPIHDVFPASTINKDYVTFTKAPAHHPMLSFGCPHPHPSQAHRKADMLHLGPVSLTLDDSFEFAVFNHDFTSRGGAFRSSSVRKFDFQERFQIESLEVWGCGGDAEARAQAERWAWEEREAEARRKINLGTGDIEADRALLEMAGLIGGARSGGSMG", "text": "FUNCTION: May be involved in a process influencing telomere capping. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RTC5 family."}
{"protein": "MPTTIQAISAEAINLPLTEPFAIASGAQAVAANVLVKVQLADGTLGLGEAAPFPAVSGETQTGTSAAIERLQSHLLGADVRGWRKLAAMLDHAEHEAAAARCGLEMAMLDALTRHYHMPLHVFFGGVSKQLETDMTITAGDEVHAAASAKAILARGIKSIKVKTAGVDVAYDLARLRAIHQAAPTAPLIVDGNCGYDVERALAFCAACKAESIPMVLFEQPLPREDWAGMAQVTAQSGFAVAADESARSAHDVLRIAREGTASVINIKLMKAGVAEGLKMIAIAQAAGLGLMIGGMVESILAMSFSANLAAGNGGFDFIDLDTPLFIAEHPFIGGFAQTGGTLQLADVAGHGVNLA", "text": "FUNCTION: Has epimerase activity with a variety of hydrophobic dipeptides (in vitro). Enzyme activity is highest with L-Phe-L-Tyr, but is still relatively low, suggesting that L-Phe-L-Tyr is not the physiological substrate. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
{"protein": "MVIRVYIASSSGSTAIKKKQQDVLGFLEANKIGFEEKDIAANEENRKWMRENVPENSRPATGYPLPPQIFNESQYRGDYDAFFEARENNAVYAFLGLTAPPGSKEAEVQAKQQA", "text": "FUNCTION: Appears to function as an adapter protein that bridges proteins together or proteins with mRNAs. May function as a ubiquitin ligase-substrate adapter. Additionally, associates with translating cytoplasmic ribosomes and may promote the expression of specific mRNAs. FUNCTION: Appears to function as an adapter protein that bridges proteins together or proteins with mRNAs (PubMed:34331014). May function as a ubiquitin ligase-substrate adapter (PubMed:34331014, PubMed:34870550). Additionally, associates with translating cytoplasmic ribosomes and may promote the expression of specific mRNAs (PubMed:34331014, PubMed:34870550). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane. SIMILARITY: Belongs to the SH3BGR family."}
{"protein": "MELPANVQNQLMQFQQLQQQLQMIMYQKQQFETQLKEMEKAIEEMEKSGSDEVFKMAGGILIKRNKAEVKEELSERVETLQLRVTTFEKQEEKMQKRYTELQENLQKAMGQGQ", "text": "FUNCTION: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit beta family."}
{"protein": "MARIAGINIPPQQHAEIGLTAIFGIGRTRARKICEAAGVPVTKKVKDLTDAELERIREHIGVFAVEGDLRREVQLSIKRLIDLGTYRGMRHKRGLPVRGQRTRTNARTRKGPRRAAASLKK", "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": "MVTVLMHDMFHAGVHFGHQTRYWNPRMKPFIFGVRNKIHIINLEQTAPMFNNALFELNKIASRKGKILFVGTKRAASEAIKEAARSCDQFFVNHRWLGGMLTNWKTVRQSIKHLKELETQSQDGTLDKLTKKEAIICNRKLEKLEKSLGGIKDLGGLPDALFVIDAEREKIAVKEANNLGIPVFAVVDTNTDPNGIDFIIPGNDDAIRAINLYLTAVAHAISEGHQKNALEI", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MSLVAIGINHKTATVDLREKVAFSPDKIHDAMKSLASRTKTGEAVIISTCNRTELYTNTGDEAEVIRWLEEYHQLSHEDVEPCLYKFEGQAVAQHLMRVSSGLDSLILGEPQILGQVKQSFVKAKEAGSVAITMDRLFQNTFSVAKKIRTETEIGAAAVSVAFAAVSMAKHIFSSLSTTKVLLVGAGETIELVARHLKDNGVDSMVVANRTLSRAEGMCEEFGATAITLEQIPDYLPQADIVISSTASPLPILGKGMVEKALKQRRHQPMLLVDIAVPRDIEAEVAELDDAFLYTVDDLQSIIEQNMASRREAAEQAEVIAEEQSHLFMEWVRSLESVDSIREYRTASMAIKDELVERAINKLAQGGDSEKLLLELANKLTNKLIHAPTQALTVASRQGDLNSIGQLRTALGLDKN", "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": "MNIVVLAGGRSAERQVSWVTGKACKRALEDLGHRVKVIDPDEDLPLRLWQERQAGCDFVWIALHGPGGEDGVVQGMLDWLGLPYQGSGPLASALAMDKLVSKQIFRAAGIPTPDWQVWDDQNPLTWADCAAELGSPLVIKPSNNGSTVGISIVRDERSFAQGLELARSVSSRIFLERYVPGKEITLSILSGQVLPAIEIIPAQGDFYDYEAKYAPGGSRHLIPCSLSPAGLARCEAAGLKAYQALGCEGLARVDLRVDPEENPWVLEVNTLPGMTPTSLCPDAAAALGWTFTELVERMLQDALQKAQLTGSRHPQSSSATLGNAP", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MPDRNIVVLTAPSGAGKTTIAHRVLEAMPDMQFSVSATTRAARPDETDGVDYHFLSPEEFRARIDAGDLLEYEEVYPDQFYGTLRSEVEDRAEDGPVLLDIDVKGALNVKRIFGDDALILFVAPPSLDELQRRLEGRGTEDRESLQDRLDRVEQEMDRADDCDAVVVNDDLDPAVEETLTRIRQFLSS", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family."}
{"protein": "MKYLLDLILLLPLLIVFSIESLVKLFIPKKKKSVAGEIVLITGAGHGIGRLTAYEFAKLNTKLVLWDINKNGIEETAAKCRKLGAQAHPFVVDCSQREEIYSAAKKVKEEVGDVSILVNNAGVVYTADLFATQDPQIEKTFEVNVLAHFWTTKAFLPVMMKNNHGHIVTVASAAGHTVVPFLLAYCSSKFAAVGFHRALTDELAALGRTGVRTSCLCPNFINTGFIKNPSTNLGPTLEPEEVVEHLMHGILTEKQMIFVPSSIALLTVLERIVPERFLQVLKHRINVKFDAVVGYKDK", "text": "FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A- dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet Note=Redistributed from the endoplasmic reticulum to lipids droplets in the cell upon induction of lipids droplet formation. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily."}
{"protein": "MNFKKGEVLFFNKPLGWTSFKVVGHVRYHICRRIGVKKLKVGHAGTLDPLATGVMILCTGKATKRIEEFQYHTKEYVATLRLGATTPSYDLEHEIDATYPTGHITRELVEETLTHFLGAIEQVPPAFSACMVDGKRAYELARKGEEVELKAKQLVIDEIELLECRLDDPEPTIRIRVVCSKGTYIRALARDIGEALQSGAHLTELIRTRVGDVRLEDCLDPEHFKEWIDRQEIENDEDNN", "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": "MLQLVNDNGLVVNVILWLFVLFFLLIISITFVQLVNLCFTCHRLCNSAVYTPIGRLYRVYKSYMRIDPLPSTVIDV", "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 (By similarity). Counteracts the production of type I interferon by interacting with host IRF3 component and preventing its translocation to the host nucleus. SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass type III membrane protein Host endoplasmic reticulum Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. SIMILARITY: Belongs to the alphacoronaviruses E protein family."}
{"protein": "MAESQSQGADQAQDLNNELKTRREKLVALRETGIAFPNDFRRDSTSDRLHAEFDGKENEELEELGVEVTVAGRMMTRRIMGKASFVTLQDVGGRIQLYVSRDDLAEGIYNEQFKKWDLGDILGARGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLADQETRYRQRYLDLIANDESRNTFRIRSKVMAAIRSFMVDHGFMEVETPMMQVIPGGASARPFITHHNALDIDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGVSPRHNPEFTMMELYMAYADYKDLIVLTENLFRTLTQDVLGSTTVEYGDQTFDFGKPFEKLTMREAICKYRPETNVADLDDLEKATAIAQSLGIKIEKSWGLGRIVTEIFEETAESSLIQPTFITEYPAEVSPLARRNDQNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFAQQVNAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMRPQK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MKPLRFAVTPGEPAGIGPDLCLLLAADAQPHPLIAITSRDLLAERATQLGLAVSLLPVAPGQWPDLPAPAGSLYVWDTPLAAPVVPGQLDKANAAFVLETLTRAGQGCLDGHFAGMITAPVHKGVINESGIAFSGHTEFLAELTRTAQVVMMLATRGLRVALVTTHLPLRDVADAITAERVERVTRILHADMRDKFGIANPRILVCGLNPHAGEGGHLGREEIDIIEPTLARLRTEGMDLRGPLPADTLFTPKYLEHCDAVLAMYHDQGLPVLKYKGFGAAVNVTLGLPIIRTSVDHGTALDLAGTGKVDTGSLRVALETAYQMAENRP", "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": "MSQEIVDRVRNYLSPNIPVTPISQGAEAVVFTTSVHPYLPENCNSNEKYIIKYRSPKRYRHPVIDKSLTKHRTLGEARLLSKLYTIEGLHVPKLIACDAYNGYLWLEFLGEDLPENFGYSNLKNFLWMYDAKNDPYCEVVKRALIEVGEQIGKLHWNDYCHGDLTSSNIVMVHSDTDSHHWVPHLIDFGLGSTTTMVEDKGVDIYVLERAILSTHSQHAEQYIEWMLDGFKSVYEKNGKLGKKKLDELLKRFAEVRLRGRKRSMIG", "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": "MNDQPETGITPGGTSGAFRDVLSKDHARRGKPPLHFADMSEEERIGKAKELGLPKFRVKQLANHYYGHFDVNAEEFSDFPAARRSDAAEAFFPELIHEVTRQVADGGTTIKTLWRLFDGSLIESVLMRYPTRTTLCISSQVGCGMGCPFCATGQLGLTRNMSAGEIVEQVRVAAKAMRDGEVAGGSGRLSNIVFMGMGEPMGNYKSVLSAVRQISSMPPEGFGISARNITVSTVGVVPGIRKLAEEGIPVRLAVSLHAPSDELRDELVPMNKRFNTKQVLDAAHDYYLASKRRVSIEYALMRGINDQAEHAKLLAKRLNHYGDDWAHVNPIPLNPIEGSKWTASKPEDERRFLEILHNAGITATLRDTRGQDIDGACGQLAAKERD", "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": "MPVSRYAVFGHPVAHSLSPAIHADFGKQTGIALDYTAIDAAPEEFTAALERFAADGGKGANVTLPLKEAAFALSASLSDRARVAGAVNTLVRNDGQWQGDNTDGAGLVRDLTERHGLDLRGRRVLLLGAGGAARGVAPALLEAGITEMVVVNRSPERADALCDALGEPGRVVSRYLEDLRELGDFELIVNATAAGRDRDAGAFALPLGLVNSLTAAVDLNYGATAIAFLAWARSAQCRYAIDGLGMLVEQAAESFALWHGVRPQTDPVYDALRARDAVLVSAD", "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": "MDYLTMFYDGWRDLMDNKSDPRTRDYPLMSSPFPTIAISLTYAYIVKVLGPKLMENRKPFELRKVLIVYNAAQVIFSAWLFYESCIGGWLNGYNLRCEPVNYSYSPKAIRTAEGCWWYYFSKFTEFFDTFFFVMRKRYDQVSTLHVIHHGIMPVSVWWGVKFTPGGHSTFFGFLNTFVHIFMYAYYMLAAMGPKVQKYLWWKKYLTVMQMIQFVLVMVHSFQLFFKNDCNYPIGFAYFIGAHAVMFYFLFSNFYKRAYVKRDGKDKASVKANGHANGHVKALKDGDVAPTSNGQANGFHNTFSKFTTDMCNPALNSSTRQRVLVNAGNK", "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. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ELO family."}
{"protein": "MHSPRKLFHARSSLATRRSTALVVLTSLAIGIAGFTFGLAVILIPGLRLTGRNCLTNTPPKTVRVVWDVAGNSNGVVSGEKKRHKVMGFVGIQTGFGSAGRRRSLRKTWMPSDPEGLRRLEESTGLAIRFMIGKTKSEEKMAQLRREIAEYDDFVLLDIEEEYSKLPYKTLAFFKAAYALYDSEFYVKADDDIYLRPDRLSLLLAKERSHSQTYLGCLKKGPVFTDPKLKWYEPLSHLLGKEYFLHAYGPIYALSADVVASLVALKNNSFRMFNNEDVTIGAWMLAMNVNHENHHILCEPECSPSSVAVWDIPKCSGLCNPEKRMLELHKQESCSKSPTLPSDDE", "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": "MNLRDKLDVYLRLARMDRPIGTLLLLWPCLMALLLAAGGMPDLKVLTIFIFGVVVMRACGCIINDYADRDLDAHVDRTKSRPLASGEVTGREALILFAVMGLFAFGLVLMLNPLVVKLSVVGIILTIIYPFTKRFTNMPQMFLGVVWSWSIPMAYAAQTGEVPAEAWWLFAANWCWTVAYDTMYAMVDREDDLKVGIKSTAILFGKYDRQIIGLFQLAALACFITAGWAADRGLVYGLGIITFVGFSMYQQKLIHERERAPCFKAFLNNNWAGLSLFIALGVDYLI", "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": "MSAHAAPSSEALSRRAEFKAAKADMLERFRSAANVASLMHALSKLTDDALKRVWDDCGLPATLALIAVGGYGRGELAPYSDVDILVLLPDAHDPALDARIERFIGMAWDLGLEIGSSVRTVAQCIEEASQDVTVQTSLLEARRIVGSTALFERFTVRYHEALDARAFFTAKVLEMRQRHAKFQDTPYSLEPNVKESPGGLRDLQTILWIARAAGFGSSWRELDTRGLITEREARELRRNEGFLKTLRARLHVIAGRRQDMLVFDLQTQAAESFGYRPTQAKRASEQLMRRYYWAAKAVTQLATILIQNIEAQLFPATSGITRVLSPDRFVEKQGMLEIVDDGVFERHPDAILEAFLLYEVTRGVKGLSARTLRALYNSREIMNNTWRRDPQNRRTFMQILQQPEGITHAFRLMNQTSVLGRYLLNFRRIVGQMQHDLYHVYTVDQHILMVLRNLRRFAVAEHAHEYPFCSQLIGNFERPWVLYVAALFHDIAKGRGGDHSTLGMADARRFCREHGITGDDAALIVWLVQHHLTMSQVAQKQDTSDPEVIKRFAEVVGNERYLTALYLLTVADIRGTSPKVWNTWKGKLLEDLYRITLAVLGGANPDAHSELKSRQEQALALLRLETVPDDAHRALWDQLDVGFFLRHDAADIAWQTRVLYRHVNAETAIVRARPSPIGDALQVLVYVKDRPDLFAGICAYFDRNGLSVLDARVSTTRHGYALDNFIVTQTERDVRYRDIANLVEQQLATRLAETAPLPEPSKGRLSRLSRTFPITPRVDLRADERGQYYILSVSANDRPGLLYSIARVLAEHQVGVHAARINTLGERVEDIFLLDGAGLSDNRLQIQLETELLRAIAV", "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": "MTPSAISPVAAGWIRRWLILMALMVYAIILVGGATRLTDSGLSITEWRPVSGALPPMSEAAWLVEFEKYRATTQYQLTNAGMALSEFQFIYWWEWGHRQIGRLIGLVAVAGFAFFAWRRWLGQGLGWKLVGLIALGGLQGAIGWWMVSSGIGETERVSVAPYRLMTHFTLALLILAVIAWLWLDLGRQQRAGAPRAAQRAAMALMGLIFVQMAAGALVAGLDAGRTYTDWPLMAGEVFPAHYIHAELGVRSFFEGREATQFNHRLLAYGLWAGSLAAAWAFRKTDVHREFAFLAVLVSAQAVWGILTLVNAAPMGLALVHQGLGVVTTLWAVYTVWRAGGPKTVAEINPPA", "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": "MDTVVFEDVVVDFTLEEWALLNPAQRKLYRDVMLETFKHLASVDNEAQLKASGSISQQDTSGEKLSLKQKIEKFTRKNIWASLLGKNWEEHSVKDKHNTKERHLSRNPRVERPCKSSKGNKRGRTFRKTRNCNRHLRKNCCTSVRRYECSQCGKLFTHSSSLIRHKRAHSGQKLYKCKECGKAFSRPSYLQTHEKTHSGEKPYACQSCGKTFLRSHSLTEHVRTHTGEKPYECGQCGKGFSCPKSFRAHVMMHAGGRPYECKHCGKAFRCQKSFRVHMIMHAGGRPYECKQCGKAYCWATSFQRHVRIHNGEKPYKCGKCGKAFGWPSSLHKHARTHAKKKPVSGGSVGKSSARPRPSTDVKSQTREKVYKCETCGKTYGWSSSLHKHERKHTGEKPVNAASVGKPSGGLCSSKNVRTQIGQKPSKCEKCGKAFSCPKAFQGHVRSHTGKKSCTSK", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MTKPTIAGNRTGRKLGQRVKKKKLKASSREWLHRHINDPYVQRAQLEGYRARAAFKLLEIDEKHQILKGARRIIDLGAAPGSWSQIAAKVTGSTEDDIRVAAIDFLEMAHLPGVTILQLDFLDPDAPQRLVDAVGGEPDLVMSDMAAPTTGHHRTDHLRTMHLCEVAAHFAIEVLAEGGHFLAKTFQGGTERDLLNLLKQNFRQVVHVKPGASRAESVEMFLLAKGFKGRNVEHGTISA", "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": "MTSHSPKLTPMFEQYMNIKAEYPDALLFYRMGDFYELFFEDAEVAARELQIALTCRNPNAENKVPMCGVPHHSARSYISQLVDKGYKVAICEQMEDPREAKGLVKRGVIRVLTSGTALEDENLSPKAHTYLGALCWDKSEGAGGFAWVDFSTGEWSGLQSRKEQELWQWVQKMAPRELLLADTLTPPASLELTETQFSKVPERAYFDYKRSAEKIMSAQQVAELGALGLENRKELVRACGALLTYLSQTQKQDLNHLCQFKPLNLNRHLLLDEITERNLELFRRLDGRKGKGTLWHVLDHTVTPMGGRLLQERLKHPWREQAPIDETQEAVSHFFAHNTLRRQLREALDTVYDIERLSTRIFLNRATPRDYVALRQSLKALPAVRELLEAPQTGDGRYATPEEQLGAALPPFLHRMLKSWDDLADYHDLLEKALVDNPPHVITEGGLFRQGFHPALDELMDLSEHGASKLHDLLAEVQQTTGISKIKLGNNRVFGYYFEVPKSVSEELPDTFVRRQTLANAERYTSERLKELEEKLFSAADKRKTMELKLFQQLREHVAQARPRVLFMADLLATLDHWQGLAEAARHWNWVRPVLHDGQDIVIREGRHPVVEAVQGPAGFIPNDLRIDDQRRLLLITGPNMAGKSTVLRQAAIICILAQIGSFVPAREARIGLCDRIFSRVGASDNLAQGQSTFMVEMMETARILRQATRRSLVILDEIGRGTSTFDGLALAWAVVEELMKKQQAGIRTLFATHYHELTSLEGTIPGVHNMNIAIKEWGGEIVFLRRLVPGPSDRSYGVEVAKLAGVPQNVVQRARQILELLEQKSKADGTRRPASYHEAQPLLPGMPEPPSTASAEPPQTVTPPEPPVLTALRDLDTDNLTPLEALTVLTEWKTLWGAGKNEC", "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": "MRVIMGTASLGSIWAVFLLPLVFGVPTEEPTFGESVASHLPKNCQRCCDPEDPLSPADTVNAVPPYVLPEVRPYINITILKGDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPGSSCQTHYSAFSVGRKTGLHSSENFLSLLFDRVFVNTDGHFDMATGRFVAPLRGLYFFSLNVHSWNYKETYVHIVHNEQAVVILYAQPSERSIMQSQSVMLPLVPGDYVWVRLFKRERENGIYSDDMDTYITFSGHLIKAEDN", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MRALLDVNVLLALLDRDHVDHERARAWITGQIERGWASCAITQNGFVRVISQPRYPSPISVAHAIDLLARATHTRYHEFWSCTVSILDSKVIDRSRLHSPKQVTDAYLLALAVAHDGRFVTFDQSIALTAVPGATKQHLATL", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. Its cognate antitoxin is VapB44 (By similarity). SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient starvation. SIMILARITY: Belongs to the PINc/VapC protein family."}
{"protein": "MAHKKGTGSTRNGRDSNAQRLGVKRFGGQAVIAGNILVRQRGTKFHAGNNVGIGKDDTLFALVDGVVTFERKGKSRKKVSVYPAAAAEAVAS", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MNIQALLSEKVRQAMIAAGAPADCEPQVRQSAKVQFGDYQANGMMAVAKKLGMAPRQLAEQVLTHLDLNGIASKVEIAGPGFINIFLDPTFLAENVQQALKSDRLGVATPEKQTIVVDYSAPNVAKEMHVGHLRSTIIGDAAVRTLEFLGHKVIRANHVGDWGTQFGMLIAWLEKQQQENAGEMALADLEGFYRDAKKHYDEDEEFAERARNYVVKLQSGDEYFREMWRKLVDITMTQNQITYDRLNVTLTRDDVMGESLYNPMLPGIVADLKAKGLAVESEGATVVFLDEFKNKEGDPMGVIIQKKDGGYLYTTTDIACAKYRYETLHADRVLYYIDSRQHQHLMQAWAIVRKAGYVPESVPLEHHMFGMMLGKDGKPFKTRAGGTVKLADLLDEALERARRLVAEKNPDMPADELEKLANAVGIGAVKYADLSKNRTTDYVFDWDNMLAFEGNTAPYMQYAYTRVLSVFRKAEIAEEELAAAPVIIREDREAQLAARLLQFEETLTVVAREGTPHVMCAYLYDLAGLFSSFYEHCPILSAENEEVRNSRLKLALLTAKTLKLGLDTLGIETVERM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MVTQALLPSGLVASAVVAASSANLGPGFDSVGLALSLYDEIIVETTDSGLTVTVDGEGGDQVPLGPEHLVVRAVQHGLQAAGVSAAGLAVRCRNAIPHSRGLGSSAAAVVGGLAAVNGLVVQTDSSPSSDAELIQLASEFEGHPDNAAAAVLGGAVVSWTDHSGDRPNYSAVSLRLHPDIRLFTAIPEQRSSTAETRVLLPAQVSHDDARFNVSRAALLVVALTERPDLLMAATEDLLHQPQRAAAMTASAEYLRLLRRHNVAAALSGAGPSLIALSTDSELPTDAVEFGAAKGFAVTELTVGEAVRWSPTVRVPG", "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": "VFINAKCRGSPECLPKCKQAIGKAAGKCMNGKCKCYP", "text": "FUNCTION: Blocks potassium channels Kv1.2/KCNA2 and Kv1.3/KCNA3 with high affinity (K(d)=1.9 nM and 10.7 nM, respectively). The voltage- dependent steady-state parameters of potassium channel gating are unaffected by the toxin in both channels, but due to the fast association and dissociation kinetics the toxin slows the rate of inactivation of Kv1.3/KCNA3 channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 04 subfamily."}
{"protein": "MKKRFIFITGGVVSSLGKGITTAALAAVLEARNLNVTIIKLDPYINIDPGTISPEQHGEVFVTEDGAETDLDLGHYERFIRTKMTRKNNFTTGSIYSEVLNKERKGEYLGATIQIIPHITNTIKKRIISCAHNVDIVFVEVGGTVGDIESLPFLEAIRQIAIDIGRENTIYIHLTLVPYISITKEIKTKPTQHSVKELLSIGIQPDILICRSQYTIPIQARSKIALFCNVLKESVISLINVDSIYKIPKLLNLQKVDQIICHHFKLKVPPADLSEWDEVIYNELNTNNVVTIGIIGKYIKSPDAYKSVIEALKHGGIKNKTVVKIKLINSEKIEKNGTNRLNCLHGILIPGGFGHRGITGKLITVEYARINNVPFFGICLGMQIALIEFFRNVIGLKDANSTEFSQNCQHPIISLIPKGNRNLPNINNNVKKKLGGTMRLGNQTCYLKQDSISHKLYGKNIISERHRHRYEVNNKFINKIEKYGLKITGKSKKNKLVEIIELSNHLWFIACQFHPEFTSTPRDGHPLFIDFIKAAIQYKKIKQK", "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": "MAAARGRGGQVGTKAKVSLGLPVGAVMNCADNSGAKNLYTIACFGIKGHLSKLPSASIGDMILCSVKKGSPKLRKKVLQAIVIRQRRPWRRRDGVFIYFEDNAGVIANPKGEMKGSQITGPVAKECADIWPKVASNAGSVV", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
{"protein": "MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSGTIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK", "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": "MKPTTVSTLRQWKQQGEKFASITAYDFSFARLFADEGIQVMLVGDSLGMVVQGHDSTLPVTLADIVYHTEVVRRGAPAALLLADLPFMSYATPEQTFDSAARLMRAGANMVKLEGGKWLAETVKQLTERAVPVCGHLGLTPQSVNIFGGYKVQGRDAEAADLLLEDALALEAAGMQLLVLECVPVALAKRVTEALSIPVIGIGAGNATDGQILVMHDAFGITGGHIPKFAKNFLAETGDIRAAVRQYVEEVKAGSYPAEQHSFQ", "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": "MLVWLFSWLGHYYAPFYAVSSLTLRALLAVVTALAFSMVFGNRVIRRLRALKYGQAIRNDGPQSHLVKTGTPTMGGVLILSAIGVSTLLWARLNNPYVWILLIVMIIFGAVGWADDWLKIKYKNPKGLIARKKYFWLSMGALFVGISLYYIATLQPDIATTREMQDLLIPIFKDWMIPFSAVPFGIGFIIFTYFVINGASNAVNLTDGLDGLAILPVVLVAAGLGAMAYVSGDVRFADYLHVPYIAYNSEVIIVCGAMIGAGLGFLWFNAHPAQVFMGDVGALSLGAMLGTIAVMTRQEIAFAIMGGLFVAEALSVMLQVGSYKLRKKRVFRMAPLHHHFEEIGWKETQVVARFWIIAIILVILGLMTLKLR", "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": "MAKAKGARIIITLECTECRTNVNKRSPGVNRYTTTKNRRNTTARLELKKFCPKCNRHTVHKEIK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MHYLPVAIVTGATRGIGKAICQKLFQKGLSCIILGSTKESIERTAIDRGQLQSGLSYQRQCAIAIDFKKWPHWLDYESYDGIEYFKDRPPLKQKYSTLFDPCNKWSNNERRYYVNLLINCAGLTQESLSVRTTASQIQDIMNVNFMSPVTMTNICIKYMMKSQRRWPELSGQSARPTIVNISSILHSGKMKVPGTSVYSASKAALSRFTEVLAAEMEPRNIRCFTISPGLVKGTDMIQNLPVEAKEMLERTIGASGTSAPAEIAEEVWSLYSRTALET", "text": "FUNCTION: Involved in biosynthesis of fatty acids in mitochondria. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGVETVV", "text": "FUNCTION: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MANIKSAIKRAELNVKQNEKNSAQKSALRTVIKAFKANPTEEAFRAASASIDKAASKGLIHKNKASRDKSRLAAKLAN", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
{"protein": "MSERTKRSVGVLGAPFSKGQARGGVEEGPIYIRRAGLIEKLEELEYEVRDYGDLHFPELPCDEPFQNVKNPRTVGQAAEKVANAVSEVKRSGRVCLTLGGDHSLAVGTITGHAKVHPDLCVVWVDAHADINTPITSPSGNLHGQPVSFLIRELQTKVPAIPGFSWVQPSLSAKDIVYIGLRDVDPGEHYILKTLGIKSYSMSDVDRLTINKVMEETIEFLVGKKKRPIHLSFDIDGLDPSVAPATGTPVPGGLTYREGMYITEQLYNTGLLSAVDMMEVNPSRGETERESKLTVNTSLNMILSCFGKAREGFHASSLRVPDLI", "text": "SIMILARITY: Belongs to the arginase family."}
{"protein": "MNTLDEIERAVKDTAHYVSGNLANYANRAAGENPSGEQQVGGDVWADDLFFDALAYIDGIGAYASEERSDVVDCGEGYSIAIDPLDGSSNLASNNSVGTIIGVYDAELPAAGREMVASLMVLYGPYTTLTIARSDRDVVQEHLLRDGHSERWGQFELPAEATVVGLAGKTGERSDAFNDIAQSFERDLKLRYGGATVADLAQVLEYGGLFGYPVTSGYPNGKLRVHFESAPLAYLVEAAGGASSDGSQSLLDVEPDGIHDRTPTFLGNAELVDELEAALSET", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
{"protein": "MAQEADGIRLDQRHGKARVRVGRVWRHAHDGSHHFVEWNVSISLLSHCLSSYRLDDNSDIVATDTIKNTVYVKAKECGDRLSVEEFAILIGKHFCSFYPQVFTAIVNIIEKPWERVSIDGKPHLHGFKLGSENHTTEARVEKSGALNLTSGIGGLALLKTTQSGFERFVRDKYTILPETRERMLATEVNASWRYSYESVASIPTKGLYFSEKFMDVKKVLMDTFFGPPETGVYSPSVQRTLYLMGSAVLKRFADVSSIHLKMPNIHFLPVNLSTKENPSMVKFKDDVYLPTDEPHGSIEATLSRITSKL", "text": "FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the uricase family."}
{"protein": "MTDILIDNTATEAVRALIQAFSLVPVSQPPEQGSYLLAEHDTVSLRLVGEKSSVIVDFASGAAQYRRTKGGGELIAKAVNHTAHPTVWDATAGLGRDSFVLASLGLAVTAFEQHPAVACLLSDGIRRALLNPETQDTAARITLHFGNAAVQMPALVQTQGKPDIVYLDPMYPERRKSAAVKKEMTYFHRLVGEAQDEAALLHTARQTAKKRVVVKRPRLGEHLAGQAPAYQYTGKSTRFDVYLPYGTDKG", "text": "FUNCTION: Specifically methylates the guanosine in position 1516 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family."}
{"protein": "MVSMTASSGRRVLLAAPRGYCAGVDRAVIAVEKALEQYGAPIYVRHEIVHNKYVVQTLERKGAIFVERTAEVPEGAIVMFSAHGVAPVVHEEAARGKLATIDATCPLVTKVHKEAVRFANEDFDILLIGHEGHEEVIGTSGEAPEHITLVDGPGDVAKVEVRDPSKVVWLSQTTLSVDETMETVDALKEKFPQLISPPSDDICYATQNRQLAVKQMGEEADLVIVVGSRNSSNSVRLVEVAKLAGARDAYLVDFADEIDEAWLEGVSTVGVTSGASVPEILVEQVLEWLSQRGFEDVEIVKAAEESITFSLPKELRRDLRAEAAALVEQRTGNGPSAE", "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": "MAGLRNSGNSDKAQNDGKGVPSAYRGVRKRKWGKWVSEIREPGTKNRIWLGSFETPEMAATAYDVAAFHFRGREARLNFPELASSLPRPADSSSDSIRMAVHEATLCRTTEGTESAMQVDSSSSSNVAPTMVRLSPREIQAINESTLGSPTTMMHSTYDPMEFANDVEMNAWETYQSDFLWDP", "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": "MTLGITEVKKGMVLKVEGDLYSVVKTEFVNPGKGSAFIRTKLKNLTKNSSIERTFKAAEKLESVELEKRNMTICYTEGNDIIFMDSNDFEQMPVSKEYVEDILPFLKEETPMEVTFYEGKPIGVIPPNFSILEVTYAEEGLKGDTSGTAQKRVTVETGGEINVPIFVKQGDVIKIDLRDLTYVERVSR", "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": "MSWQTYVDEHLMCEIEGHHLASAAILGHDGTVWAQSADFPQFKPEEITGIMKDFDEPGHLAPTGMFVAGAKYMVIQGEPGAVIRGKKGAGGITIKKTGQALVVGIYDEPMTPGQCNMVVERLGDYLVEQGM", "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": "MSKLKTLNRQFISNLETHKVTTDAKRNLILSILKSTTTKREAKNYLTKYQNQFDFNDDLDFNKNIKIKNEQLSLTNRDSQRELFINRFLNQSNPFINIYDREDVKLQKVPLRLAIFKIKFTKITIKQWKGIAETFKRLITLGISPIIMLDYDHLPSNSFKNNELYMINQGNKMLNYLGRPEEESDLKVTLLRSLFTSHKGVPTLDSLESILIPLYQGIIPIIQPIVYNADASKQEFLESDKLLLGLSSALIEKRTTDLLSIEKIVMIDPMGGIPSIERRQTSHVFINLSQEYSDILSELFIGHIEPKYRDTHVNNLNTMNNVLSFINEKSGNDETTGIITTPEIMSINIDQLNPIIYNVLTDRAIISSSLPSTTNRTPHLSTTIIKKGVDVQIFDIDNYDKDLTMQNLFDDKLVNKEKLINLLNDSFGKSLDVDPYLDRINDNIATVVIVGDYDGAAIITWEYSKGEKIAYLDKFAIAKKNQGLPGLADVIFKIILQSHPFELIWRSRKNNPVNKWYFERCCGCMSAPDSQWKIFYTGEVFDKKIDRFKRNPRHKNGVVNIDRKLQQYSEICEGITPSFK", "text": "FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MIGKWRMGLWALAILTVPMYFIVTEGRKTSWGLENEALIVRCPQRGGAINPVEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLNVTIYKRPPNCKIPDYMMYSTVDGSDKNSKITCPTIALYNWTAPVQWFKNCKALQGPRFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNYIVTATRSFTVEEKGFSTFPVITNPPHNYTVEVEIGKTANIACSACFGTASQFVAVLWQINKTRIGSFGKARIQEEKGPNKSSSNGMICLTSLLRITGVTDKDFSLKYDCVAMNHHGVIRHPVRLRRKQPIDHQSTYYIVAGCSLLLMFINVLVIVLKVFWIEVALFWRDIMAPYKTQNDGKLYDAYIIYPRVFRGSAAGTGSVEYFVHYTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFAYEQEIALHSALIQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLVKMQGTIKWREDHVADKQSLSSKFWKHVRYQMPVPKRPPKMASVAAPLSGKVCLDLKHF", "text": "FUNCTION: [Isoform B]: Inhibits IL-33 signaling. FUNCTION: Receptor for interleukin-33 (IL-33), its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function (By similarity). Upon tissue injury, induces UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3- dependent differentiation of inflammation-resolving alternatively activated macrophages. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform B]: Secreted. SIMILARITY: Belongs to the interleukin-1 receptor family."}
{"protein": "MYYPEPIARLIESFSKLPGIGQKTATRLAFYTIGMEDQDVNEFAKNLLSAKRDLSFCSICGNLTESDPCAICTDPTRDRTTILVVEESKDVLAMEKIREYRGLYHVLHGTISPMNGISPDEINVKTLITRLMDSEVKEVIIATNATSDGEATAMYLARMIKPAGIKVTRLARGLAVGSDIEYADEITLSKAVENRLEI", "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": "MTKYIFVTGGVVSSLGKGIVAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKFSNVTTGKIYSTVLKKERRGDYLGGTVQVIPHITNELKDRVYRAGKETNADVVITEIGGTVGDIESLPFLEAIRQMKSDIGRENVMYIHCTLVPYIKAAGELKTKPTQHSVKELRSLGIQPNIIVVRTEMPISQDMKDKIALFCDIDTKAVIECEDADNLYSIPLELQKQGLDKLVCEHMKLACKEAEMSEWKELVNKVSNLSQTITIGLVGKYVELPDAYISVVESLRHAGYAFDTDVKVKWINAEEVTENNIAELTSGTDGIIVPGGFGDRGVEGKIVATKYARENNIPFLGICLGMQVASIEYARNVLGLKGAHSAEIDPSTQYPIIDLLPEQKDVEDLGGTLRLGLYPCKLEEGTKAFEVYQDEVVYERHRHRYEFNNEFRQQMEEQGFVFSGTSPDGRLVEIIELKDHPWFVASQFHPEFKSRPTRPQPLFKGFIGASVEAANQK", "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": "MKTIIALSYIFCQVFAQNLPGNDNSTATLCLGHHAVPNGTLVKTITNDQIEVTNATELVQSSSTGRICDNPHRILDGKNCTLIDALLGDPHCDGFQNEKWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFFNEGFNWTGVTQNGGSYACKRGPDNSFFSRLNWLYKSESTYPVLNVTMPNNDNFDKLYIWGVHHPSTDKEQTNLYVQASGRVTVSTKRSQQTIIPNVGPRPWVRGLSSRISIYWTIVKPGDVLLINSNGNLIAPRGYFKIRTGKSSIMRSDAPIGTCSSECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGIFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEDMGNGCFKIYHKCDNACIGSIRNGTYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWACQKGNIRCNICI", "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": "MMNAKALYKKKALRDRRKLRIKSKLLGDALRPRVSVFRSNRYFYAQAIDDVKQSTITHIDGRKMGFKNTQEDAKKLGALFAEELKKAGIERAVYDRNGYLYHGVVAAFAESLRENGIAL", "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": "MSDALIRLEKVAVRFAGQNVLDNIHLSVEPGQIVTLIGPNGAGKTTLVRAVLGLLKPDSGSVWRKPKLRVGYMPQKLHVDPTLPLSVLRFLRLVPGVDRPRALAALKEVGAEHVIDSPVQSVSGGEMQRVLLARALLREPELLVLDEPVQGVDVAGQAELYSLITRLRDRHGCGVLMVSHDLHLVMSTTDQVVCLNRHVCCSGHPEQVSGDPAFVELFGNNAPSLAIYHHHHDHAHDLHGSVVKGPVTGQPHVHGDSCKHG", "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": "MMDSDDDMLDAHDMDSVDYDFDSGGTDDDNDIDETDYVFGEADTDDAAIIAYHRSQINYVVLKEEDIRRHQKDDVGRVSVVLSITDVQASLLLLHYHWSVSKVNDEWFADEDRVRRTVGILEGPAPDGREFTCGICFESYPLEETISVSCGHPFCATCWTGYISTSINDGPGCLMLKCPYPCCPAAIGRDMIDNLCSKEDKERYYRYFLRSYVEVNREMKCCPAPGCEHAISFAAGTESNYDVSCLCSHSFCWNCSEEAHRPVDCDTVGKWILKNSTESENMNWILANSKPCPKCKRPIEKNHGCMHMTCTPPCKFEFCWLCLNAWTEHGESSGGYYACNRYEAAKKQGLYDEAERRREMAKNSLEKYTHYYKRWASNQVSRQKAMGDLQKMQSEKLRKLSDIQCTSESQLKFIAEAWLQIIECRRVLKWTYAYGYYVPDDHTKKQFFEYLQGEAESGLERLHECIENDIEVFEFGEGPSEEFNHFRTKLTDLTSITKTFFQNLVKALENGLADVDSHAASSKPANCKPSSNTKDGGKGKKEALTMAGSAET", "text": "FUNCTION: Might act 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. SIMILARITY: Belongs to the RBR family. Ariadne subfamily."}
{"protein": "MAAGVLPQNEDPYSTLVNSSGHAAHMDENSGRPAPKYTKVGERLRHVIPGHMACSMACGGRACKYENPARWSEQEQAIKGVYSSWVTDNILAMARPSSELLEKYRIIEQFLGQGIKTIINLQRPGEHASCGSALEQESGFTYLPEAFMEAGIYFYNFGWKDYGVASLTAILDMVKVMTFALQEGKVAVHCHAGLGRTGVLIACYLVFATRMTADQAIIFVRAKRPNSIQTRGQLLCVREFTQFLAPLRNIFSCCDPKAHAVTLAQYLIRQRHLLHGYEARLLKYVPKIIHLVCKLLLDLAENRPVVMKSMLEGPVLSAEIEKTVSEMVTLQLDQELLRQNSDVPDPFNPTAEVAEFENQDVILSTEQEFDPLWKRRDIECLQPLTHLKRQLSYSDSDLKRAKAILEQGETPWTVPAQELLDHSLQHQKPTSHCYMPPTPELGFNKEALVQNTFSFWTPSKCGGLEGLKDEGSLLLCRKDIPKEVQRSRTFSVGVSCSHNPGEPVPPNFTSIHKDPEQVTHCRCEAPGGWVPGPVHEMVRSPCSPLNCGSSPKAQFPHGQETQDSTDLSEAVPHAGLQPELSAEARRILAAKALANLNEFVEKEEVKRKVEMWQKELNSREEAWERICGERDPFILCSLMWSWVEQLKEPVITKEDVDMLVDRQADAAEALFLLEKGQYQTILCVLHCIVSLQTLPMEVEEACLLHAIKAFTKVNFDSENGPIVYDTLKKIFKHTLEEKRKMAKDSLS", "text": "FUNCTION: May play roles in cilia formation and/or maintenance. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class PTPDC1 subfamily."}
{"protein": "MLICLTASHHNASFEVLEKLSVAAPSVAGALMEQNDFIAGAVVLATCNRFEAYLDVEEPLTAARALAVEATVDVVSGASGIARDDVRGSVDVKCGDAVAEHLFAVSSGLESVVVGEGEIAGQVRRALEGARTGGTTSTGLERLFQTASNTSRGVKTRTGLQSAGRSMVRLALDLAESRIADWSATRVLLVGTGAYAGASLAALRDRGVVDVHVYSPSGRAQKFAGPHGIPAVEGRDLLRALAASDMVVTCSTAPTAVLAAHHMQGAAAVSGDGRRRLVIDLGLPRNVDPDVVTVDGVELLDLETISLHAPLRDLTATDDAREIVSTAAAEFRAASAEDEVAPAVVALRTHIFDVLEGELERVRKRGDSSDATEKALRHLVSVLVHQPSVRARELARQGEGARVVDAVQALFGLDVEMPAAVSSPVAVALSRTAEAGQAS", "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": "MYHLLIIITTLSFSSINITFAVDEAFPSIPTTFSVATKQHYDVKPIHHEVYDGERKIYDISHQYTPELPVWESSEGLGNFLRLAVSMKNGSDANISKMELSVHSGTHVDAPGHFHDHYYESGFDTDSLDLQILNGPALLVDVPRDKNISAEVMKSLHIPRGIRRVLFKTLNTDRRLMFKKEFDSSFVGFMVDGAKWLVENTDIKLVGLDYLSFAAYDEAPATHRFILERRDIIPVEALKLDDVEVGMYTLHCLPLRLVGAEGAPTRCILIK", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Cyclase 1 superfamily."}
{"protein": "MSRKLFGTDGVRGRANTHPMTAEMALRLGAAAGRYFRRSGEDHHRVVIGKDTRLSGYMLENALTAGLTSTGMNVLLLGPVPTPAVGYLTRSMRADVGIMISASHNPAHDNGIKFFGPDGFKLSDEAEARIEAIVAGEIIPAQPQNIGRAKRIDDGRGRYVEYAKTTFPSGQRLEGLKVVVDCANGAAYRAAPDVLWELGAEVIPLGVSPNGHNINDGLGSTHPEACARAVLEHGADMGISLDGDADRVMIVDEKGQVADGDQIMALLAARWAAQGRLRGGALVATVMSNLGLERFLQGRGLRLERTAVGDRYVVERMRGAGFNLGGEQSGHIVMTDYATTGDGLIASLQFLAALSDSGQRASELVAQFEPVPQLLKNVRYAVGADPLSKDSVQAEIARAEARLNGSGRVLIRKSGTEPLIRVMAEAEDETVLREVVEDIVAAVEKAA", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MALKIRLSRGGSKKRPYYHIVVADARSPRDGRFLERVGAWDPMLPKDGPRVKLNEERIQYWLGQGAQPTDRVLRFLDAVGLKKRPNRNNPHKGQPGKKAQERISAAKQVAEAESAPV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MKITHHYKSLLSAIISVALFYSAAPHADILDGGEIQFNGFVTDDAPKWTWQISSPDQTWAVDTADARTENGQLVFDLSDKGPLPFLEGYLYEVAERGGPGFTPFITFSSNGRPFAVKEGSDTSVQRFRASVPVRDPETGNVSGQLSFTLNQGMAVSTGKQEEGASTPSGMSLVSGQSVTDVQSGSLPQGLKNRLSALLLMNKGFGNGMSAVDNGQVITQGVLADGRVMNLAAAYASAVSDFELRLPAEGTPARWQAGLNVTVTVQ", "text": "FUNCTION: K88 minor fimbrial subunit, plays an essential role in the biogenesis of the K88 fimbriae. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs. SUBCELLULAR LOCATION: Fimbrium. Note=Located in or along the K88 fimbrial structure. SIMILARITY: Belongs to the fimbrial K88 protein family."}
{"protein": "MARVVALVLLGLLSLTGLEAVPRVPKVQVYSRHPAENGKPNFLNCYVSGFHPPEIEIDLLKNGEKMKVDRSDLSFSKDWSFYLLVHTDFTPNGVDEYSCRVQHSTLKDPLIVKWDRDL", "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": "MAAAQISAEEMEELREAFTKVDVDGNGHISTDELNALFKAANLPLPGYRVREIIQEISRTMDLNQDGKITFDEFAKVVHDLKSSEVAKTFRKAINKKEGICSVAGTSEQSGTQHSYSEEEKVAFVNWVNKALEKDPDCQHVLPMDPSTDDLFTAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGRQHLVLGLLWQVIKIGLFADIEISRNEALIALLRDGESLEDLVKLSPEELLLRWANYHLEEAGCPKINNFSSDIKDSKAYYNILNQVAPKRDEEGIPAIPIDISGIREKDDLKRAECMLEQADRLGCRQFVTATDVVRGNPKLNLAYVANLFNKYPALKKPENQDIDWSSIEGETREERTFRNWMNSLGVNPRVNHLYVDLADALVIFQLYEKIKVPVDWDKVNKPPYPKLGSNMKKLENCNYAVELGKKEAKFSLVGIAGQDLNEGNRTLTLALLWQLMRRYTLNILEDLGDGQKIIDETIVQWVNETLTQAGKGTISGFKDGSISSSMPVLDLIDAIQPGSIRYDLLKAEDLTDEKKLNNAKYAISMARKIGARVYALPEDLVEVKPKMVMTVFACLMARGMRRI", "text": "FUNCTION: Actin-binding protein. Plays a role in the activation of T- cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell junction Cell projection Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MTGINSQQEDIKIETLTQEEALELATALKQKLSHGELPNSDLESINKMVAGLGDNRGELRLTFAKSLGSIGEDAIPILCEALKNSSNVVIRRASAKTLNIIGNKKALPNLIEAFESDEDPVVQGSSAGAMATIGEPAIEPLLRILTESNCTAFQIGLINLALGFIGSKGPMGFNSAISSKNPEIRIAALNALAEQAQKSENKDVQALILNALKDQDSEVRAEAAIIVGKSMDQEEGAHQLHELLKDKNDQVRKNAALSLMKMEAVISIDFLDRAIRQESDEQVKGVMIVARNQLMKH", "text": "FUNCTION: An enzyme involved in the biosynthesis of bilin. SIMILARITY: Belongs to the CpcE/RpcE/PecE family."}
{"protein": "MRFLLVAVVAMMALVSSSTAAVAETSNDINTMNNNQEFARSLRNTEERSIAAILAEAGEEDRAAWRINYRAWYKAKLTPTQVKTVLGVSQAEMNNVAKQLQRLYLGYYSFYTAMEKKKEEKKRLATP", "text": "FUNCTION: Effector that suppresses flg22-induced post-translational MAP kinase activation in potato and 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, PubMed:30536576). Does not suppress programmed cell death triggered by the P.infestans elicitin infestin-1 (INF1), or by co-expression of tomato Cf4 with Cladosporium fulvum Avr4 (PubMed:30536576). Suppresses early pattern-triggered immunity (PTI) via interaction with the U-box-kinase protein UBK, a positive regulator of specific PTI pathways in both potato and Nicotiana benthamiana (PubMed:30536576). SUBCELLULAR LOCATION: Secreted Host nucleus, host nucleolus Host nucleus Note=Forms a ring around the nucleolus. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MTLLFDKTGPIDSPTLAPASVDNHCRSPDRSAAARVIEIGLVNNMSDAALRATERQFMRLLRAGSGEHLVRLHCFALPSVQRSPATRQRIDSLYADIADLRHTRLDALIVTGAEPRAATLQSEPYWDEMRALVDWAEANTRSTIWSCLAAHAAVLHLDGIERERLPQKCSGVFAGEQVNDDALLSDLPSPLKVPHSRLNDLAADRLAARGYEVLTHAPNAGVDIFARQGRSRFVFFQGHPEYDATSLQREYLRDIGRFLTGERHDYPEFPVDYFDADIEDALDAFRAEAEAARDPAIIARLPHLALRQGTAEGIETTANALFRNWLISLASEP", "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": "MAVSIYDSLRTPGPKHYKYKICDGIDLGDGLVIDPLNLDSLVVYAKNVKWSSFCDYGVPLYLAADTMDTPYEYPPIIMNDWRWFIFNDHYFGKYWGYGLYTILMVYSTIFVITVALTVLSFLTVNKGPYKITSLLLKLSSVLASTSIIYFLTSALSTISRQQEHYGVANGNVFGTLLNSNLVIATLNLLSMFFYKLCQVSIVARLFERKLEWRIVVFVGGIMSIVSFIISAIVSYTDRVGIRNDNLVTLSPFGLLFDIALETCFAFIIVTNVWGTRKTWVSHLQMWYLALLTIAIVLLSPAMFLADVGTGLLSAYAATVSPLLYTMSTFVAWEWLERIHILKKAAQVKSLLGQKIYEDEQEGYNFAYYSVNNESNLDTNSDSHISLYNDMFRNSEQFSNVGSNLSSKESSSLPAQMNSTGISFPTAVNQVEFQKRKSFLDHLTNFTYSRPYKIYKKSKSIIQLRKRNSETVKNERSNEELSIEKVRRRLGLTNERREYVYNTKDIVFASDDDTESECESNNILNESIDSHFPENGAGSV", "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": "MDSPSLRELQQPLLEGTECETPAQKPGRHELGSPLREIAFAESLRGLQFLSPPLPSVSAGLGEPRPPDVEDMSSSDSDSDWDGGSRLSPFLPHDHLGLAVFSMLCCFWPVGIAAFCLAQKTNKAWAKGDIQGAGAASRRAFLLGVLAVGLGVCTYAAALVTLAAYLASRDPP", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CD225/Dispanin family."}
{"protein": "MAIYGIGTDIVQVSRVAAVMQRTNGRFAEKVLGPDELRVYHARHARSQARGLAFLATRFSVKEAFSKAIGLGMRWPMTWRALQTLNEPSGRPTCVASGELADWLAERGITSRVTLSDERDYAVSFVIAETPDTAD", "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": "MLNEGLCCGAWAMKGTLLLVSSVGLLLPGVGSCPMKCLCHPSSNSVDCSGQGLSKVPRDLPPWTVTLLLQDNRIHWLPALAFQSVSLLSTLNLSNNSLSNLAAEAFYGLPHLRVLNVTQNSLLSIESSFAHALPGLRELDLSSNSLRILPTSLGKPWENLTVFAVQQNHLLHLDRELLEAMPKVRLVLLKDNPWICDCHLLGLKLWLERFTFQGGETDGAICRLPEPWQGKALLSIPHELYQPCSLPSQDLAPSLVQQPGSAPQDAQKSHENSSGQQDPLECEAKPKPKPTNLRHAVATVVITGVVCGIVCLMMLAAAIYGCTYAAITAQYQGRPLASARKSEKMGSKELMDSSSA", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MKILVTGFDPFGGDKINPAIEAVKRLPDEINGAEIIKLEIPTVFNKSAEVVKEAIEKENPDYVLNVGQAGGRFGLTPERVAININDGRIPDNEGYQPLGEPIHEDGETAYFTQLPIKAEAKAIRDAGLPASISNTAGTYVCNHIMYQVQYMRDKEFPNIKAGFIHIPFLPEQVVNRPNTPSMALDDIVKGLTAALGAIVERDGKGDIKAVEGANH", "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": "MIQQESRLRVADNTGAKEILTIRVLGGSGRRYAGIGDVIVATVKDAIPGGNVKKGDVVKAVIVRTVKERRRQDGSYIRFDENAAVILKNDGDPRGTRIFGPVGRELREKKFMKIISLAPEVL", "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": "MNTPRIPIASHQAVMRCLRDKLQQANLTLQTDYTEPAVSYQQRGATAGTAWLQHWEIRLNPVLLQENQQTFIDEVVPHELAHLLVYARFGRVAPHGKEWRWMMENVLHVPAKRTHRFAVQSVQGKTFTYLCDCQRHELTIRRHNRVLRGETEYRCRRCGKTLRHDVKSSI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SprT family."}
{"protein": "MDMVASDNVYAPLYAPFFGFAGCALAMILSCLGAAIGTAKSGIGIAGIGTFKPELIMKSLIPVVMSGILAIYGLVVAVLIAGNLSPTEEYTLFNGFMHLSCGLCVGFACLSSGYAIGIVGDVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIIALILNTKGSE", "text": "FUNCTION: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
{"protein": "MFKDIFKKNKKKKYVTVKNMTDTEVPEGIMAKCPKCQKIMYTKELQENLNVCFNCDHHMAMNAYDRIDALMDKGTFKELDKHVEPVNPLNFPNYEEKIEKDRAKTEIDEAVVTGWGTINGYKTGIAVMDSRFRMGSMGTVVGEKITRAIEYATKQQMPFIIFTASGGARMQEGILSLMQMAKVSVALNRHRETGLLYIAFMTHPTTGGVSASFASVGDINLAEPESLIGFAGRRIIEQTINEKLPDDFQTAEFLLDHGQLDKVVHRKEMKEVLTTILKLHQRGEN", "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": "MFAKATRNFLKEVDAGGDLISVSHLNDSDKLQLLSLVTKKKRYWCWQRPKYQILSATLEDVLTEGHCLSPVVVESDFVKYESKCENHKSGAIGTVVGKVKLNVGGKGVVESHSSFGTLRKQEVDVQQLIQDAVKRTVNMDNLVLQQVLESRNEVLCVLTQKIMTTQKCVISEHVQSEETCGGMVGIQTKTIQVSATEDGTVTTDTNVVLEIPAATTIAYGIMELFVKQDGQFEFCLLQGKHGGFEHERKLDSVYLDPLAYREFAFLDMLDGGQGISSQDGPLRVVKQATLHLERSFHPFAVLPAQQQRALFCVLQKILFDEELLRALEQVCDDVAGGLWSSQAVLAMEELTDSQQQDLTAFLQLVGYRIQGEHPGPQDEVSNQKLFATAYFLVSALAEMPDNATVFLGTCCKLHVISSLCCLLHALSDDSVCDFHNPTLAPLRDTERFGIVQRLFASADIALERMQFSAKATILKDSCIFPLILHITLSGLSTLSKEHEEELCQSGHATGQD", "text": "FUNCTION: [Gasdermin-E, N-terminal]: Pore-forming protein produced by cleavage by CASP3 or granzyme B (GZMB), which converts non-inflammatory apoptosis to pyroptosis or promotes granzyme-mediated pyroptosis, respectively (PubMed:32188940). After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature interleukins (IL1B and IL16) and triggering pyroptosis (PubMed:33852854). Binds to inner leaflet lipids, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate (By similarity). Cleavage by CASP3 switches CASP3-mediated apoptosis induced by TNF or danger signals, such as chemotherapy drugs, to pyroptosis (PubMed:32188940). Mediates secondary necrosis downstream of the mitochondrial apoptotic pathway and CASP3 activation as well as in response to viral agents (PubMed:28045099). Exhibits bactericidal activity (By similarity). Cleavage by GZMB promotes tumor suppressor activity by triggering robust anti-tumor immunity (PubMed:32188940). Suppresses tumors by mediating granzyme-mediated pyroptosis in target cells of natural killer (NK) cells: cleavage by granzyme B (GZMB), delivered to target cells from NK-cells, triggers pyroptosis of tumor cells and tumor suppression (By similarity). May play a role in the p53/TP53-regulated cellular response to DNA damage (By similarity). FUNCTION: [Gasdermin-E]: Precursor of a pore-forming protein that converts non-inflammatory apoptosis to pyroptosis. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-E, N-terminal) binds to membranes and forms pores, triggering pyroptosis. SUBCELLULAR LOCATION: [Gasdermin-E]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Gasdermin-E, N-terminal]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the gasdermin family."}
{"protein": "MKLSTLFTLATTISTLTTFTIASPVVVVEKRAINETALAEDIPTTKNNHAQASYGKPFAIYQPKAFIISMFSLERDPWLKAMDFVHNITIPGLSPVYPDIHCTTNYTICQITTGEGEINAASSISALTLNPLFDLTKTYFLVGGIAGGEPNYTTIGGVTFAKYAVQVGLEYQLAYEDYHKTNPDWISGYIPYGTDDQNTYPGNVYGTEVFEVNEKLRDRAVELASKVHLNNGTEGNAKFRKLYNETAAQGLPKVVKCDSLTSDNYFTGNVLNDYFANFTLLMTNGSATYCSTAQEDNATLEVMTRLAKHGLVDYDRIMIMRTISDFSRPPPSMSAYEYFFNRSDGGISASLENLVIAGTPIIHDIVQNWDKIYKSGEKYSSKNYVGDIFATLGGKPDFGKESFDTA", "text": "FUNCTION: Nucleoside permease that transports adenosine and guanosine. Does not show any transport activities towards cytidine, adenine, guanine, uridine, and uracil. SIMILARITY: Belongs to the NUP family."}
{"protein": "MTSSEGPGIPAIKTPPVKLRGSCHACALSKLKCSQDKPTCSRCVKRGTACQYLASKRAGRKQGSKTGSFKSFYNMKTDYSTSINKDDDRRELMEVSTELMQYALQQDRSLEVYRRNQYHQRTPSYPESIPSLLSSTGPGTSATSPLTLGPPDYDGYLASPISLSLLDVPDMDYFPGADMSANVMDGFPDPPSFFPSGEPIPTLQENILKTSFADSPVPANSPSVPPTPDVTSVGTPRQCFCFPRALTLLRELFPNPSLSCVTPSSESGSASPPTVQQVITKNEQTLRDITEIIECSCSEDGYTITIITLAAFKVLAWYSAVAHISPISEDSQALEEIDRTPAVVRGYNIDGEDQGRMAAQLVLSELHRVQRLVGNLYQRLKDQVSGGKPARLSTTGVNDSNHYSLPFHLLERLAVDLGAQLRSLSSEIVDRLRRG", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSRRHAAEKREVLPDAKFGDRVLTKFMNNLMIDGKKSVAERIVYNAFDRVESKIKRAPVEVFHEALDNVKPSVEVRSRRVGGATYQVPVEVRPERREALAIRWLITAARGRNENTMEERLAGELLDAVQSRGTAVKKREDTHKMAEANKAFSHYRW", "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": "MLGSAGTLLLLLLAWGARALSQPDDNRITTGRNQDLNAIQQDLLLKLLSGWTDSRESNLVEVERNVPDPPEPKIPPSVKFPRLSLRERKAPCKNFFWKTFTMC", "text": "FUNCTION: Somatostatin inhibits the release of somatotropin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatostatin family."}
{"protein": "MISIDQRAMQAKPIDLEHLSAQDTALEIRNLDLSYGDKQALFNVSMKIPKKQVTAFIGPSGCGKSTLLRCINRMNDLVDSCKIKGEILLHGQNIYDKKVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGLNNRRDLDEAAERSLRGAAIWDEVKDRLHDNAFGLSGGQQQRLVIARAIAIEPEVLLLDEPTSALDPISTLTIEELITELKDKYTVVIVTHNMQQAARVSDQTAFMYMGELVEYADTNTIFTTPRKRKTEDYITGRYG", "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": "MLSLSHYLILGAVLFAISVVGIFLNRKNLIVLLMAIELMLLAVNLNFIAFSHYLGDIAGQVFVFFILTVAAAESAIGLAILVVMFRNLRTIHVDDLDSLKG", "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": "MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGATLLSLGLIFLLYTMFVWWRDVLRESTLEGHHTKAVQLGPRYGSILFIVSEVMFLFAFFWASSHSSLAPTVEIGGIWPPKGIGVLDPWEIPLLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVSTGFQGMEYYQAPSTISDSIYGSTFFLATGFHGFHVIIGTLFLIVCGIRQYLGHLTKKHHVGFEAAAWYWHFVDVVRLFPFVSIYWWGGI", "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": "MAEAKYEPRLKKEYVERIRKAMQEKFSYANEMMIPKLDKIVINMGVGEATADSKKPTVAAADLAAIAGQKPVITRARNSIAGFKVRENMPIGAKVTLRGARMYEFLDRLVNIALPRVRDFRGLNPKSFDGRGNFAMGIKEHIVFPEINYDKVDQMWGMDIIVCTTATTDDEARTLLKEFSFPFRQ", "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": "MDSDSCAAAFHPEEYSPSCKRRRTVEDFNKFCTFVLAYAGYIPYPKEELPLRSSPSPANSTAGTIDSDGWDAGFSDIASSVPLPVSDRCFSHLQPTLLQRAKPSNFLLDRKKTDKLKKKKKRKRRDSDAPGKEGYRGGLLKLEAADPYVETPTSPTLQDIPQAPSDPCSGWDSDTPSSGSCATVSPDQVKEIKTEGKRTIVRQGKQVVFRDEDSTGNDEDIMVDSDDDSWDLVTCFCMKPFAGRPMIECNECHTWIHLSCAKIRKSNVPEVFVCQKCRDSKFDIRRSNRSRTGSRKLFLD", "text": "FUNCTION: Modulates chromatin structure. Required for normal chromosome condensation during the early stages of mitosis. Required for normal chromosome separation during mitosis. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Note=Predominantly bound to chromatin, but a minor proportion is also detected in the nucleoplasm."}
{"protein": "MSWRTTTAILCLYGAVKEFRPATPFLTPFLASPEKNITLDELYSQVYPYWTYSYMLALIPMFILTDILRYKPIVMIEAIGLVATWALLVFGKGVWQMQIMQVSFGVASAAEIAYYSYIYSIVDRKHYKRATSYIRAAALMGKLVAFGLGQTLISTHTSDYLVLNQISLGAVCLVTIIAIFLPRVKSEKAKVSMRAHEIVEQQTVESVESVQTPKAVKMSYTREYFKKISEELQICSKNQELLKWSLWWALASCGVYQVQNYTQSLWKELQNNPDDVANGVVEFVNTALGAFLSLFIHHLSIDWTRHGQMILFITSAIVAVLLYLCSQTTTVLVAYSSYVVITSIYHMLITAASANVAKELSSNNHGLIFGCNTFVAVCLQSLLTLVVVDSRFLHLDIRTQFVIYSGYFALVASIFAFFFMISLFSKSSNAHTAQTTYEATNEIQEETVFLDQN", "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": "MRHSVLSISFAVALFLECYTPSTAIPIGKMDDVALEQDTLDSLLRVEVSENSPDSVRGRSSKIVLLADSGLWMNLNRGLPLYKLIAAAAGPDRALTLDRREAGQDLSPSISIVRRDTMRCMVGRVYRPCWEV", "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": "MAKSNEEPNSNLNTNKPPLKRTKTLAQQPSLNLRVSIAAADNGIGNSSSSSTKTDFEQQQRNYPSFLGIGSTSRKRRPPPPPKPSNITPNVKPPASDFQTKPHSEPKTSPSSSSPPSLPIAITKQQQQQHSISSPIFYLFVITCVIFVPYSAFLQYKLAKLKDMKLQLCCQIDFCSGNGKTSLQKDVVDDGSFSYYILNADSRTISLYIVLFTLVLPFILYKYIDYLPQMINFSRRTNSNKEDVPLKKRVAYMVDVFFSIYPYAKLLALLFATLFLIAFGGLALYAVTGGSMAEALWHSWTYVADAGNHAETEGMGQRIVSVSISAGGMLIFAMMLGLVSDAISEKVDSLRKGKSEVIERNHVLILGWSDKLGSLLKQLAIANKSVGGGVIVVLAEKEKEEMEMDIAKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEALRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDGLLFKDILISFPDAIPCGVKVSADGGKIVINPDDNYVLRDGDEVLVIAEDDDTYAPGPLPEVRKGYFPRIRDPPKYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMFNEVPEKQRERKLAAGELDVFGLENIKLVHREGNAVIRRHLESLPLETFDSILILADESVEDSVAHSDSRSLATLLLIRDIQSRRLPYRDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDSRTRNLVSVSRISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIKPAEFYLFDQEELCFYDIMIRGRTRKEIVIGYRLASQERALINPSEKSMTRKWSLDDVFVVIASGE", "text": "FUNCTION: Required for both rhizobial and mycorrhizal symbiosis. Involved in Nod-factor-induced calcium spiking. May induce a change in membrane polarization that activates the opening of a calcium channel required for calcium spiking. Might be calcium gated. SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the castor/pollux (TC 1.A.1.23) family."}
{"protein": "EDNHSTVEDDAANYDFDLFVIGAGSGGVRAARFSANLGAKVGICELPFHPISSEVIGGVGGTCVIRGCVPKKILVYGASFGGELEDAKNYGWELNEKIDFNWKKLLQKKTDEIIRLNNIYKRLLSNAGVKLYEGEGKIVGPNEVQVTQLDGTKLSYSAKHILIATGSRAQRPNIPGQELAITSDEALSLEEFPKRVVILGGGYISVEFASIWRGMGADVNLCFRKELPLRGFDDEMRAAVARNLEGRGVNVHPRTTLTELVKTDGGVVARTDHGEEIEADVVLFATGRSPNTKRLNLEALGVELDRTGAVKVDEYSRTSVPSIWAIGDVTNRMNLTPVALMEGTCFAKTVFGGQNSKPDYSNIACAVFSIPPLAVVGLSEEQAIEQASGDILVFTSSFNPMKNTISGRQEKTIMKLVVDAETDKVLGASMCGPDAAEIMQGIAIALKFGATKAQFDSTVGIHPSAAEEFVTMREPSRRVPGAGKPKTNL", "text": "FUNCTION: Maintains high levels of reduced glutathione in the chloroplast. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MISIKVLFFGEACQLVGKREEAIDFPEETDYEEIRKTILENYPALQKIEKVMMLAVDQEYANPGDRFELVRFTEIAVIPPLSGG", "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": "MSLFGTSPEDSSAGNSAHRSKSSLFADEPSLGTGSNANLGSSSLFADDDDLSSGSPWNSNVNKRTARHKLVKTLLSDSDAPESYIDAYDLVLSAGDRVGAGIGLTSVREILSGSGISASDQEKILNIVVSGDIDSANGLGRGEFNVLLALVGLAQEGEDLTLDAVDDRRKKLPAPKSLYLDALRANQESGTPAPSQERPITPPRPASPQQAPNSAHSRRESMTGLESDPWGSPELHRGHAHAQLESDHPVLNGYGSVRSATNAWSSRVGEDNNPNEISNSNRANSQTDSAPSHGSGFGWGESLGNTPSDGGLGGTARAGLGGFGPPSSVHSDSNPRRRSLGIGRVASPPVEEHVTVTLLPEKEGMFMFQHRNYEVKSARRGSTVVRRYSDFVWLLDCLQKRYPFRQLPLLPPKRLSADSNAFLEKRRRGLVRFTNALVRHPVLSQEQLVIMFLTVPTELSVWRKQATISVQDEFTGRDLPPDLEDSLPSTLPDTFETVRGGVKRSAEIYINLCTLLERLAKRNEGLAADHLRFSLALQSLTEVTRDTYAIDTNDVPLLNEGIRATANHLSVSQSLLEDEARAWEEGVLEDLKRQRDCLVSVREMFDRRDRYARNNIPQLERRIENNERKLQDLRSRPQGTVKPGEIEKVEDAIIKDKESIVQQHARGVFIKECIRDEIVYFQQSQYHISRLHQEWSQERVKYAELQADNWRSLSDQVESMPLSG", "text": "FUNCTION: Required for vacuolar protein sorting. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family."}
{"protein": "MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPECAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL", "text": "FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:6509022, PubMed:9078368). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:9078368). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (By similarity). FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (By similarity). Important for normal progress through mitosis and normal cytokinesis (By similarity). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (By similarity). SUBCELLULAR LOCATION: Nucleus matrix Cytoplasm, cytoskeleton Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium Cell projection, growth cone Cell projection, axon Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. SUBCELLULAR LOCATION: Nucleus matrix Cytoplasm, cytoskeleton Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium Cell projection, growth cone Cell projection, axon Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. SUBCELLULAR LOCATION: Nucleus matrix Cytoplasm, cytoskeleton Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium Cell projection, growth cone Cell projection, axon Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MNLDSSASALSYQSGFGNEFASEALPGALPVGQNSPQKAPYGLYAELFSGTAFTMTRSEARRTWMYRIQPSAKHPAFAKLARQLAGGPLGEVTPNRLRWSPLQIPSEPTDFIDGLVAMVANSAAQKPAGISVYHYRANRSMERVFFNADGELLLVPELGRLRIVTELGMLDLEPLEIAVLPRGLKFRIELLDPQARGYVAENHGAPLRLPDLGPIGSNGLANPRDFLAPVAHYEDLRQPTTLVQKYLGELWGCELDHSPLNVVAWHGNNVPYKYDLRRFNTIGTVSFDHPDPSIFTVLTSPTSVPGLANLDFVIFPPRWMVAENTFRPPWFHRNLMNEFMGLIQGAYDAKAEGFLPGGASLHSCMSAHGPDGETCTKAINAQLQPAKIDNTMAFMFETSQVLRPSQFALECPELQNDYDACWASLPVTFNPNRR", "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": "PMTKVLKADDINKAISAFKDPGTFDYKRFFHLVGLKGKTDAQVKEVFEILDKDQSGFIEEEELKGVLKGFSAHGRDLNDTETKALLAAGDSDHDGKIGADEFAKMVAQA", "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": "MANDYVSTVLLLLSLLIFLSQRTDSASIVKSLPGFDGPLPFELETGYIGVGEEEEVQLFYYFIKSERNPQEDPLLLWLSGGPGCSSISGLLYENGPVNVKIEVYNGTLPSLVSTTYSWTKVSSIIYLDQPVGTGFSYSRTKLVNKPSDSGEAKRIHEFLHKWLGKHQEFSSNPFYVGGDSYCGMVIPALVQEISKGNYVCCKPPINLQGYILGNPSTENEVDINYRIPYAHGMALISDELYESMKRICKGKYENVDPRNTKCLKLVGEYQKCTKRINKALIITPECVDTSPDCYMYRYLLTTYWANDENVQRALHVNKGSIGEWVRCYFEIPYNHDIKSSVPYHMNNSIDGYASLIFSGDHDMEVPYLGTQAWIRSLNYSLIDDWRPWMIGDQIAGYTRTYANKMAFATIKGGGHTPEYKPEESYIMFQRWISGQPL", "text": "FUNCTION: Probable carboxypeptidase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MGGFTSIWHWVIVLLVIVLLFGAKKIPELAKGLGSGIKNFKKAVKDDEEEAKNEPKTLDAQATQTKVHETSEIKSKQES", "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": "METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKTELSLAEKMKESSIDNLMKSLDKNSDQEIDFKEYSVFLTTLCMAYNDFFLEDNK", "text": "FUNCTION: Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites (By similarity). FUNCTION: Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites. SIMILARITY: Belongs to the S-100 family."}
{"protein": "MKLTPRQQEILDFIKSTLEVLGAPPTRMEISSAFGFASPNAAEDHLKALAKKGAIVLEPGSARGIRLVEQLGLPLIGSVAAGSPILAVENMQGRYALDASLFAPKADFLLKVRGLSMIDVGIFDGDLLAVHKTNQARDGQIVVARLDEEVTVKRLERSGGQIRLIAENPDFEPIIVDPEAVDFAIEGIAVGLIRGAVSKLS", "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": "MAYPVQLGFQDAASPIMEELLYFHDHTLMIMFLISSLVLYIISLMLTTELIHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEISTPSLTLKTMGHQWYWSYEYTDYENLCFDSYMAPPSDLKPGELRLLEVDNRVVLPTELPIRMLISSEDVLHSWTIPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELVPLKHFEEWLLSML", "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": "MLQPTLTSWVILAGGQASRMGGKDKGLIALNNKPLIEYVIDRLTPQTSNILINANRNQDDYQQYGPVFGDHFQNFPGPMGGIHAGLLHASTDWVGFVPCDCPRINEDLVERFCRAVTDETDILVAHDGDHQQPVFTLYHKRVLPKLTAFLERGDRKIILLYKECHTQYVDFSDSPDCFVNLNTPEELTQFGQLES", "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": "MITIPYLTAVSTYFSYGLLFAFGQLRDYSRLIFDWWRTNNLQGYAPICLAHEDFYIRRLYHRIQDCFGRPISSAPDAWIDVVERVSDDNNKTLKRTTKTSRCLNLGSYNYLGFGSFDEYCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEDCVAKYVGQPAAVIFGMGYATNSAIIPVLIGKGGLIISDSLNHTSIVNGARGSGATIRVFQHNTPGHLEKVLKEQIAEGQPRTHRPWKKIIVVVEGIYSMEGEICHLPEIVSICKKYKAYVYLDEAHSIGAIGKTGRGVCELLGVDTSDVDIMMGTFTKSFGSCGGYIAGSKDLIQYLKHQCPAHLYATSISTPSATQIISAIKVILGEDGSNRGAQKLARIRENSNFFRAELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLRENLAVVVVGFPATPLLLARARICISASHSREDLIKALQVISKAGDLTGIKYFPAAPKKQEVEKNGIKLD", "text": "FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1 constitutes the catalytic core. Plays an important role during male gametogenesis and embryogenesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MESTQEFQVPLKTIRLTDGTEYQSYHTEGSLSDKKPSDYKNGIPKIRKEWIRTRLDRGDTNHSQMYYAKKGIITEEMRYVALRENMNPEFVRLEIACGRAILPSNRNHPELEPMIIGRNFLVKINANIGNSALGSSIEEEVEKLHWAVKWGADTVMDLSTGKNIHETREWILRNSPVPIGTVPIYQALEKVKGKAGNLNIQVFLDTLEERAEQGVDYFTIHAGVLLRYIPFTANRVTGIVSRGGSILAKWCLAHHKENFLYTHFDEIIKVMKKYGVSFSLGDGLRPGSIADANDKAQFGELETLGELTKRAWEEDIQVMIEGPGHVPMHLIKENVDLQMKLCQEAPFYTLGPLVTDIAPGYDHITSAIGAAMIGWFGMAMLCYVTPKEHLGLPDKEDVKQGVIAYKIAAHAADLAKGHPGAIKRDNLLSKARFEFRWEDQFALSLDPETAKSFHDETLPQDRMKTAHFCSMCGPHFCSMNLTQELRKFAQEKGMEEKSEVTICNRKKESGK", "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": "MEDFVAQSFNPMIVELAEKAMKEYGEDPKIETNKFAAICTHLEVCFMYSDFHFIDERGESIIVESGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGVEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRRLADQSLPPNFSSLENFRAYVDGFEPNGCIEGKLSQMSKEVNARIEPFLKTTPRPLRLPDGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMKTFFGWKEPNIIKPHEKGINPNYLLAWKQVLAELQDVENEEKIPKTKNMKKTSQLKWALGENMAPEKVDFEDCKDVSDLKQYDSDEPEPRSLASWIQSEFNKACELTDSSWIELDEIGEDVAPIEHIASMRRNYFTAEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVTFVSMEFSLTDPRLEPHKWERSCVLEIGDMLLRTAIGQAPRPTFLYVRTNGTSKIKMKWGMETRRCLPHLLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEEGSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFNLGGLYEAIEECLINDPWVLLNASWFNSFLTHALK", "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": "MTKVGLRIDVDTFRGTREGVPRLLEILSKHNIQASIFFSVGPDNMGRHLWRLVKPQFLWKMLRSNAASLYGWDILLAGTAWPGKEIGHANADIIREAAKYHEVGLHAWDHHAWQAHSGNWDRQTMVDDIARGLRTLEEIIGQPITCSAAAGWRADQQVIEAKEGFHLRYNSDCRGVMPFRPLLDSGKPGTAQIPVTLPTWDEVIGRDVKAEDFNGWLLNRILRDKGTPVYTIHAEVEGCAYQHNFVDLLKRAAQEGVTFCPLSELLSGMLPLGQVVRGNIAGREGWLGCQQIAGSR", "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": "AASPQKRAASPRKSPKKSPRKSPKKKSPRKRKARSAAHPPVIDMITAAIAAQKERRGSSVAKIQSYIAAKYRCDINALNPHIRRALKNQVKSGALKQVSGVGATGRFRVGAVKRSAASANKLKATREKARARAKAKKAKAAARRKAAAAKRKAAAAKRRAAKKARKAKAKP", "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": "MASQKPHLNLITIGHVDHGKSTLVGRLLFEHGEIPAHIIEEYRKEAEQKGKATFEFAWVMDRFKEERERGVTIDLAHRKFETDKYYFTLIDAPGHRDFVKNMITGTSQADAAILVISAREGEGVMEQTREHAFLARTLGVPQIVVAINKMDATEPPFSEKRFNEVKADAEKLLKTIGYKDATFVPISGYKGDNVTKPSPNMPWYKGPSLLQALDAFKVPEKPINKPLRVPVEDVYSITGIGTVPVGRVETGVLKPGDKVIFLPADKQGDVKSIEMHHEPLQQAEPGDNIGFNVRGIAKNDIKRGDVCGHLDSPPTVVRAFTAQIVVLNHPSVIAPGYKPVFHVHTAQVACKIDEIVRTLNPKDGTTLKDKPDFIKTGDIAIVKVIPDKPLVIEKVSEIPQLGRFAVRDMGQTVAAGQCIDLEKR", "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": "MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVELVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK", "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": "MMKLVLLSVIVILFSLIGSIHGANVPGNYPLDSSGNKYPCTVLGDNQSCIDVCKKHGVKYGYCYGFKCWCEYLKDKNVSL", "text": "FUNCTION: Probable neurotoxin that inhibits ion channels (By similarity). Is toxic to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium/Potassium channel inhibitor family."}
{"protein": "MAFAGLKKQINKANQYMTEKMGGAEGTKLDMDFMEMERKTDVTVELVEELQLKTKEFLQPNPTARAKMAAVKGISKLSGQAKSNTYPQPEGLLAECMLTYGKKLGEDNSVFAQALVEFGEALKQMADVKYSLDDNIKQNFLEPLHHMQTKDLKEVMHHRKKLQGRRLDFDCKRRRQAKDDEIRGAEDKFGESLQLAQVGMFNLLENDTEHVSQLVTFAEALYDFHSQCADVLRGLQETLQEKRSEAESRPRNEFVPKTLLDLNLDGGGGGLNEDGTPSHISSSASPLPSPMRSPAKSMAVTPQRQQQPCCQALYDFDPENPGELGFKENDIITLLNRVDDNWYEGSVNGRTGYFPQSYVQVQVPLP", "text": "FUNCTION: Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Note=Associated with internal membranes. Expressed presynaptically at NMJs. SIMILARITY: Belongs to the endophilin family."}
{"protein": "MNTDTFMCSSDEKQTRSPLSLYSEYQRMEIEFRAPHIMPTSHWHGQVEVNVPFDGDVEYLINNEKVNINQGHITLFWACTPHQLTDTGTCQSMAIFNLPMHLFLSWPLDKDLINHVTHGMVIKSLATQQLSPFEVRRWQQELNSPNEQIRQLAIDEIGLMLKRFSLSGWEPILVNKTSRTHKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQQRRQTFPG", "text": "FUNCTION: Transcription activator for the expression of the melAB operon. MelR binds at two sites located upstream of the melAB transcription site. FUNCTION: Transcription activator for the expression of the melAB operon. MelR binds at two sites located upstream of the melAB transcription site (By similarity)."}
{"protein": "MTKNCLNQENCIPIFSENSSGDFFSCNPWLLFFNRNKINYQIFSLKKNDTLLFNSSSRLYIILIGSLIITKVLRNTHKVTLNLLTTGDTFGQIELVDDNFYYEAEAIDKTEVACINYTTIIKACSNCAPFNLFFVNHLVFCSAKAYHFIEIISHKSITSRLASLLLLLAEQNGTQVNNGIMLNFTITHKILAQIIGSNRVSVTRILANLLKTKLISIQKKRIIVHSPVLLSQRILNQ", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MHHPKETLLIDSSNPSYSHLTEYRFDNLKREESRSTSLFGDRRRVMKILSGFSLIIIVVFIFATSHEQALSTTGDLTSSTQSTTHGGVVFTYPTTRKSPGKGCVLNSQRSTPKNLKQYTGNISDACLAGIKSSNCKTWLMTNAVILKYSDDVVSNCPSILEFVNKTSLSCSGKSQIQYMYPQSDSASSDCNHSYDFNSNALNRAIYNFNYSKTLISTSYANTPGFAMYTFLLKIMNCVNKNGIKLDAGILNIFTDMTYIDLCESDVFMSSFPDTLNKLIEAGYIVKFYFLNQNLQDTQKNVENVLAGCKYMNSRSYCEIVDWSYHSENPNEFEICIPDSQPSGKKEDFNWHVTELLLIIGIPCISLTICCIAFFVCCLKCAKLKMAMMRMNVFSNDTHQNPDEMELKKRWIGMRKKFNKDVENGSCKELNTQKWSHFASANNYMDIQALANANKKDIWEIDTKNLLVQEDHLLGNGAFANVYKGIVKGKIPLLVVNNSLNMTVESENNGHYEAAIKKLPAHADEQNHLDFFHEIDFMKRLGHHPHVISMLGCVSNPYEPLIVVEYCARGDLLKFLRRHKDYVLMNKTDDCPIEADMCLRIKDLVSIAWQVADGMSYLASKNFIHRDLAARNILLTKSLTAKVSDFGLCRYMDSALYTAKGGRLPIKWMSVEALKLYEFSTKTDVWSFGVLLFEIFSMGDVPYPTIQQVDMLEHLLAGGRLSQPLKCPNEIFNIMQKCWAEKPEDRPEFNEMRGEITVMLNLDDESYGYLSVESQGGPKYTQLTMQDSKETAPCSTPGGSQDMDEDGDYDSGSEGHSQGTCAQLDQVLTERFGEEQKKEIKQIFCEITSKSMRGKRRQSNSTVSTYQS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
{"protein": "MSHIPVLLKETINALNIKKNGIYIDGTFGNGGHTKEILKYLGQSGKLYSIDQDIKSVNKGKKIKDKRFSIIFGKFSKKIPYIYKKNKKKKIDGILLDLGISSNQINQNDRGFSFMKNGLLDMRMNNTTGIPAWKWLKKSSQKEIEKVLRKYGEERYSKKISYAIYNRNKKKTITQTLDLVQIIKKAIPKIDKYKHPATRTFQAIRIHINNEIKELKKTLKISIKILKKKRRLVIICFHSLENRIVKNFFKKHGKTFFIPRGLPITEKKIKKIENKKIKIIKKIKPKKTEIQKNKRSRSAILRIAEML", "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": "MQARDPHANVFFVGLMGAGKTTVGRAVARRLDRTFFDSDHEIEARTGARIPVIFEMEGEAGFRDRETQVITDLTQRENIVLATGGGAVLRPENRDCLKNNGIVVYLRANPHDLWLRTRKDKNRPLLQTEDPKGRLEALYEVRDPLYRECADFVIETGRPSVNGLVNMVLMQLELAGVIAKPLQA", "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": "MTIITPITNDPTTALLRLMAWLSPVFPVGSFSYSHGLERAVHDGLVVDAAGLQDWLQWLVRRGSGWNDAVLCAESWRCAMKGEDLHEIAELAEALAGSRERHMETMLQGGAFFAAARSWPCEIFDRLPPDCAYPVAVGAVAGGHGVPLAQALAAFLQAFCINLLQASIRLSVTGQSGVTAIMAALEPVLGETAARAALSSMEDLGSATFIADIMAMKHETQHSRLFRS", "text": "FUNCTION: Disruption of the ure1 gene cluster suggests that it protects brucellae during their passage through the stomach. The major route of infection in human brucellosis is oral. 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": "MRAGQPKITGAKITGAIIAGGQSSRMQAGGVSGDKFLQPLGSAPVIAHVIARLQPQVDTLFINSKGDLSRFAAFGLPAVKDIAMNHGGPLVGLLTCLAHASPCRLLLTSAADTPFLPCDLASNLIRKQAETGARIILACSNERVHPIVGLWHTDLVPDLEKWLQYAEKASIFWFAKHIGFEVVNIPLAHAPRLAESYDPFFNINLPDDLLKAREINEALQA", "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": "MYKLMKNIQTTALNRTTLMFPLALVLFEFAVYIGNDLIQPAMLAITEDFGVSATWAPSSMSFYLLGGASVAWLLGPLSDRLGRKKVLLSGVLFFALCCFLILLTRQIEHFLTLRFLQGIGLSVISAVGYAAIQENFAERDAIKVMALMANISLLAPLLGPVLGAFLIDYVSWHWGFVAIALLALLSWVGLKKQMPSHKVSVTKQPFSYLFDDFKKVFSNRQFLGLTLALPLVGMPLMLWIALSPIILVDELKLTSVQYGLAQFPVFLGLIVGNIVLIKIIDRLALGKTVLIGLPIMLTGTLILILGVVWQAYLIPCLLIGMTLICFGEGISFSVLYRFALMSSEVSKGTVAAAVSMLLMTSFFAMIELVRYLYTQFHLWAFVLSAFAFIALWFTQPRLALKREMQERVAQDLH", "text": "FUNCTION: Efflux pump that mediates resistance to chloramphenicol. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MAKKVVGMIKLQLPAGKATPAPPVGPALGQHGVNIMAFCKEYNAKTANQAGMTIPVIISVYQDRSFSFILKTPPAAVLIKKAAGLDSGSGEPNKTKVGKITKAQLKEIAETKMPDLNAGSVESAMSMIAGTARSMGITVEE", "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": "MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGELFRPDNFVFGQSGAGNNWAKGHYTEGAELVDNVVDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAYSFRAVSVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGKVSMKEVEDQMRNIQSKNQSYFVEWIPNNIQTALCSIPPRGLKMSSTFIGNSTSIQELFKRVGDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDASISEGEEEYAEEEIMEGEE", "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": "MNHKVGFVSLGCPKALVDSERIITQLKAQGYELVPTYEDAGVVVINTCGFIDSAVQESLDTIKEAMAENGRVIVTGCLGAKADVIKNACPDVLHISGAHAYEEVVNAVHQHLPPPADPFTQLIPPQGIKLTPRHYAYLKISEGCNQKCTFCIIPTMRGKLQSYPMAQILTEAKKLKQAGVKELLVISQDTSAYGVDTRYQQVEWQGKTVNTRFYDLCEQLGELGIWVRLHYVYPYPHVDDIVPLMRDGLILPYLDIPLQHANSRILKAMKRPASSENTLLRIASWREICPDITLRSTFIVGFPGETEEEFSELLAFLKEAQLDRVGCFKYSPVEGAKANDLDNPVSEDIKEERYHRFMQVQAEISRNKLKNKIGSTQTVLIDEITEDQIIARSKSDAPEIDGLVYLPKISGITVGSFAEVVITDSDDYDLYASLV", "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": "MPTINQLIRKGREQVVYKSTAPALKECPQKRGVCTRVYTTTPKKPNSALRKVARVRLTNGIEVTSYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYHIVRGALDSAGVQNRNRGRSKYGTKRPKK", "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": "MLSRSHSNATMSTTRHRLLATASRFVETLESLDMDAMLAVRSSTCLHHMCCPSFRNYSITNDQTREALPQWKATIKKYKFGVLDDSQTLVDEQARKVMIRAETAAETTVGDYNNEYVFILRMTEDCNAVDEIWEFYDTIRLRDLRHRLEAGHVPIGVDAPAPFTTTASPAAL", "text": "FUNCTION: Part of the gene cluster B that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin (PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5- dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). 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 then modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O- acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:29076725). The cytochrome P450 monooxygenase then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:29076725). The hydroxylation catalyzed by ausR permits the second O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:29076725). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end product of the Penicillium brasilianum austinoid biosynthesis clusters is acetoxydehydroaustin (PubMed:29076725). SIMILARITY: Belongs to the trt14 isomerase family."}
{"protein": "MSNKKIEQWEIERYWEIFASLANGQPRLNNSQAASVLRNSRLRDEQLEKVWDLADVDGDGELDFEEFCVAMRLVFDLVNGELQTVPAVLPDWLVPESKSHLVHATRALSTQPEQFERIEDEDDTPGLKDGFEWYMKPADKSKYEEIYNANRNQRGEIAFESLQPLYDSLDVPDTDVRSAWNLVNPSASHTINKDATLAFLHILNYRHEGFRIPRTVPASLRASFENNKIDYQVDNARPAQKWGADGDTETPTGRKTKFGDTYLSRLGAGGKSSYTPKGTNFSDTIQDEEWEKVRLRRELAELETKLNSAQQASEGRRDQPRNDGRTSWGLVKKEALQLLEYKERELRELREGTGRSKEGQNLERLREDVKAVGEQVDGLKSHLANRNEVLADLRRQIDEEKVSR", "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": "MHSKPQWLRAKAPTGEVFNETLNIVKLHNLHTVCEEAACPNIGECWNKRHATVMILGSVCTRACAFCNVATGIPDKLDPHEPENLAKAIKKLNLKHVVITSVDRDDLPDGGANQFIQCIEEIRKITSETTIEILTPDFLNKKGAFEAIAVASPDVYNHNIETVPRLYAKIRPRARYFHSLYLLKMVKQINPKVFTKSGLMVGLGETKEEILQVMDDLRSAEVDFITIGQYLQPTPKHAKLDRYVTPEEFEHYKYIAYSKGFLVVASSPLTRSSYHAEEDFNRLKACR", "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": "MASAANSSREQLRKFLNKECLWVLSDASTPQMKVYTATTAVSAVYVPQIAGPPKTYMNVTLIVLKPKKKPTYVTVYINGTLATVARPEVLFTKAVQGPHSLTLMYFGVFSDAVGEAVPVEIRGNPVVTCTDLTTAHVFTTSTAVKTVEELQDITPSEIIPLGRGGAWYAEGALYMFFVNMDMLMCCPNMPTFPSLTHFINLLTRCDNGECVTCYGAGAHVNILRGWTEDDSPGTSGTCPCLLPCTALNNDYVPITGHRALLGLMFKPEDAPFVVGLRFNPPKMHPDMSRVLQGVLANGKEVPCTAQPWTLLRFSDLYSRAMLYNCQVLKRQVLHSY", "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. Activates the AP-1 pathway and enhances EBV reactivation and virus release. Inhibits type I IFN-induced TYK2, STAT1 and STAT3 phosphorylation, thereby impairing type I IFN signaling and counteracting the ability of IFN-alpha to suppress the reactivation of EBV. Recruits SHP1 phosphatase to dephosphorylate STAT1. Mediates STAT2 ubiquitination and proteasomal degradation. Also suppresses type II and type III IFN signaling. Contributes to G1/S arrest in the host cell. Acts as an miRNA regulator that interferes with the function of RISC in miRNA-mediated mRNA silencing. As a result, SUMOylation is increased. When encapsulated in the exosomes released by EBV-infected host cells, may facilitate the infection in recipient cells. 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. Activates the AP-1 pathway and enhances EBV reactivation and virus release (PubMed:29695622, PubMed:26559845). Inhibits type I IFN-induced TYK2, STAT1 and STAT3 phosphorylation, thereby impairing type I IFN signaling and counteracting the ability of type I IFN to suppress the reactivation of EBV (PubMed:32213613, PubMed:34319780). Recruits SHP1 phosphatase to dephosphorylate STAT1 (PubMed:34319780). Mediates STAT2 ubiquitination and proteasomal degradation (PubMed:34319780). Also suppresses type II and type III IFN signaling (PubMed:34319780). Contributes to G1/S arrest in the host cell (PubMed:24501404). Acts as an miRNA regulator that interferes with the function of RISC in miRNA-mediated mRNA silencing (PubMed:35007297). As a result, SUMOylation is increased (PubMed:35007297). When encapsulated in the exosomes released by EBV- infected host cells, may facilitate the infection in recipient cells (By similarity) (PubMed:35729616). SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Host Golgi apparatus, host trans-Golgi network Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. Associates with the capsid before the final envelopment. Recruited to the TGN via the interaction with BBLF1 (PubMed:32038519). Also found in the exosomes released by the host cell (PubMed:35729616). SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Host Golgi apparatus, host trans-Golgi network Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. Associates with the capsid before the final envelopment. Recruited to the TGN via the interaction with BBLF1. Also found in the exosomes released by the host cell. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 2 family."}
{"protein": "MPGNSFGELFRITTFGESHGPMVGVVIDGVPAGLPIKKEDIEFELSFRRPGRQFVTGRREKDEPEIVSGVYNGRTTGAPITILVKNTDVISSLYEEIHYKPRPGHADLPYIMKYGFENWDYRGGGRASARETVGRVAASAIAKKLLMLTDTWIAGHLKSLGYVELNEPVTFEEVLCSKYSPVRASKKWLEKKYEELVKQATVEGDSWGGIAEIIVRNPPIGLGEPVFDKLKADLAKALLSIPAVMGFEYGLGFNAAKMKGSEANDEIVKKGDKYRWKFNNSGGILGGLSTGEDILVRCAFKPTSSIRKPQKTIDLRTGEETTISVIGRHDPAVAIRGVSVAEAMVSLVIVDHAMRAGYIPTVRISDDQIKIIEERWNKYISLCKPTQVSQ", "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": "MKIVQETISTKTKKNIAIIISRYNNFINQHLLDGALDILKRIGQINQKNIPIIHVPGAYEIPIIASIISKQKKYNAIIALGTIIKGHTLHYSHISHAVNSGLTNISITNNIPISIGIITANNIEQAIERAGTKLGNKGSEAALTALEMINIINILAQNK", "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": "MSAKAAPQDYFVKDISLAEYGRKEIAIAETEMPGLMAAREEFGPSQPLKGARICGSLHMTIQTAVLIQTLEALGAQVRWVSCNIYSTQDHAAAAIADAGTAVFAYKGETLEEYWDYTDRMFQWPDGEGPNLILDDGGDATMYLILGEKAESDPSFLEKPTSEEEKYFFAQIKKRLTASPGWFKKTKAGVRGVSEETTTGVNRLYQLEKRGELPFPAINVNDSVTKSKFDNKYGCKESLVDAIRRGTDVMMAGKKAFVAGYGDVGKGSAASLAGSGARVGVSEVDPICALQAAMDGFEVLTMDEAAPKFDIFVTATGNKDILTVDHMRAMKDMAIVCNIGHFDNEIQVEGLRNFQWTNIKPQVDMITFPDGKRIILLSEGRLVNLGNATGHPSFVMSASFTNQTLAQIELHLRGNEYDNKVYTLPKHLDEKVARLHLDKLGVQLTKLSGEQAAYIGVEQTGPFKPEHYRY", "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": "MAAPEEKALQVAEWLKKVFGDHPIPQYEMNSRTTEILYHLSERNRVRDRDISLVIEDLKQKASEYESEAKRLEDFLMESVNFSPANLSKSGSRFLNALVDSAIALEIKDTSLASFIPAVNDLTSDLFRTKSKSEEMKLELGKLEKNLTATLVLEKCLREDLKKAELQLSAEKAKVDSRLQNMDFLKAKAAEFRFGIKAAEEQLSARGMDASLSHRSLAALSEKLSELKEQTIPLKKKLESYLDLMPSPSLAQLKIEEAKRELDAIEAELTKKVDMMGL", "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 Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=Localizes with the spindle poles in mitotic cells. In interphase, localized at the centrosome and diffusely in the cytoplasm. Localizes to mitotic spindle microtubules (By similarity). SIMILARITY: Belongs to the HAUS1 family."}
{"protein": "MKHLHVLLLCGGGGSEHEISLLSANYLESQLKELAEVSVTRVELFPDHWQTNDGRSCHLGMDRQLHFANEAKPVDFVVPCIHGFPGETGDIQSMLELIGLPYLGCGSEGSKLCFNKVSTKLWLSALDIPNTPFLFLSDNNEAAHAQAHTAFRNWGAVFVKAASQGSSVGCYKVTDAAKLSEAVNAAFGYSDQVLVEKAVRPRELEVAVYRYNDQLVATRPGEIATPSDSFYSYEEKYSSGSNSTTYLEAPGLSDAQISTIREYALKAFTQLGLKDLSRIDFFLTEDNEILLNEINTFPGMTPISMFPKLLEHHGDNFKQFLEGIIRSTVK", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MIITPYLNPRLVKPLKWLAIIILLYFLYFSLFSINKKPGKPRKPPKAVENYTCPFEKADFSNFKDKKLEFHKNNGTDPKILVILDSLFSRHGKSIIQILNSQKFAFKAEAISKNLPVLTSAKRGKYSLIIVENYYKYLNMARWNRQLLDKYCKEYRVPLFSFIASKPNDQLKRIRIKGSSLWMWQNQRINRLTVSPSPIHKISKIGAYRNLTTQESDWILFEISENFESILTGTVKNGYERAVVLRDLGREDGVEKVIFGRNLTDFQIKITFLDALWWAMGDEKLFGLDRFVQVDIDDVFVGAQSTRIVEEDVRHLISAQNHFRNFIENFKFLLGFSGSYFRNGDDFEDRGDEILIENAEKFVWFPHMWRHNHAHEHNFTYLESIMVQNRLFAQNMHLPIDYPYAIAPQHDGVFPVHEQMYEAWKKIWNVTVTATEEYPHLKPATGRKGFIHSGIHVLPRQTCGLYTHTQFFDEYPEGFQKVIKSIQGGDLFFTILLNPISIFMTHQQNYAHDRLALYTFENLFRFLNCWTNIRLKWQSPVESAKMYFEKFPEERIPLWTNPCSDPRHQAILPPSMSCSKKSLPDLLIIGPQKTGSTALASFLALHPNVSQNMEIPGSFEEIQFFSGQNYLKGVEWYMSKFPNETTVIFEKSATYFDNPSAARQAAAMVPHAKLVIILQNPTQRAYSWFQSLFQHLIAHKDPIAMSSESLDVILNSTSSESAKFKIRQRCLSGGRYVHHLDKWLEHFSLQQIQFIDSDELRKEPAKVLSSLSKWLDLPEFPFETHIRFSPSKGFHCRLINGKTECLGESKGRKYSEMSQELRQKLDGIFALDNSALFKFLRKNRLKIPDWLEEAVRIRV", "text": "FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily."}
{"protein": "SVYYGSIEAGGTKFVLAIADEHFNI", "text": "SIMILARITY: Belongs to the ROK (NagC/XylR) family."}
{"protein": "MKPVVALVGRPNVGKSTLFNRITRSRNALVDDFPGVTRDRHYVDAVWNERPFTLVDTGGFLLSDDDFFAREIRGHVELAIEDADIVALVLDGRAGISPFDRDLADILRRTSKPVFFLVNKVENHKQREELLEFYSLGIEKFYPMSAEHGIGVEPFLDDMVALFPAPEPVVEPQAGSEQGEPDASEQEICIAVAGRPNVGKSSLINRLFGKSRVVVSHVPGTTRDSVDLSIERNGRRFRLIDTAGIRRKGKVRERIEKYSILKSLKSLDQCDVALILIDADEGVTDQDITIAGYAQDRGCGALFLINKWDLLDEDRKDQRRFMEDLRTKSKFLSFAPAMTISALTGFRTHKILAMVEKIHAQYAYRINTGLLNRIVEDAIFRSEPPMHKGKRLKFFYATQVAVKPPTIVCFVNYPDAVHFSYHRYLVNQIREMAELEHTPIRLLFRAKTGKIDFSGKSKLAERIVEKKEKKTTRRKKERKEQSRRKRVRDLKG", "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": "MHLEVIVQSYKKSKYYFSHTFYLYKFIVVNSPDMLHISRLGLFLGLFAIVMHSVNLIKYTSDPLEAFKTVNRHNWSDEQREHFYDLRNLYTSFCQTNLSLDCFTQILTNVFSWDIRDSQCKSAVSLSPLQNLPRTEIKIVLSSTTANKSIIASSFSLFYLLFATLSTYTADPPCVELLPFKILGAQLFDIKLTEESLRMAMSKFSNSNLTRSLTSFTSKNFFNYTSFVYFLLYNTTSCVPSNDQYFKQSPKPINVTTSFGRAIVNFDSILTTTPSSTSASLTSPHIPSTNIPTPAPPPVTKNSTKLHTDTIKVTPNTPTITTQTTESIKKIVKRSDFPRPMYTPTDIPTLTIRLNATIKTEQNTENPKSPPKPTNFENTTIRIPKTLESATATTNATQKIESTTFTTIGIKEINGNTYSSPKNSIYLKSKSQQSTTKFTDAEHTTPILKFTTWQNTVRTYMSHNTEVQNMTDKFQRTTLKSSNELPTIQTLSVTPKQKLPSNVTAKTEVHITNNALPSSNSSYSITEVTKEVKHTRMSASTHEQINHTEIAQITPILNAHTSEKSTTPQRSFTAETFLTTSSKPNIITWSNLLTTTPKEPLTNTSLRWTDHITTQLTTSNRTQSAKLTKANISSQTTNIYPQTITGRSTEV", "text": "SUBCELLULAR LOCATION: [80 kDa Glycoprotein O]: Virion Host cell membrane Note=Expressed on the host cell surface as a part of the gH-gL-gO complex. SIMILARITY: Belongs to the herpesviridae U47 family."}
{"protein": "MSPESGHETISGTSDFVVVANRLPVDLERLPDGTTRWKRSPGGLVTALEPLLRKRRGSWIGWAGVADSDEEPIVQDGLQLHPVRLSADDVAKYYEGFSNATLWPLYHDLIVKPEYHREWWDRYVEVNRRFAEATARAAAEGATVWIQDYQLQLVPKMLRMLRPDVTIGFFLHIPFPPVELFMQMPWRTEIVEGLLGADLVGFHLPGGAQNFLVLSRRLVGANTSRASIGVRSRFGEVQVGFRTVKVGAFPISIDSAELDGKARNRAIRQRARQIRAELGNPRKIMLGVDRLDYTKGIDVRLRALSELLEEKRIKRDDTVLVQLATPSRERVESYIAMREDIERQVGHINGEYGEVGHPIVHYLHRPIPRDELIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRQAYLVNPHDLEGVKDKIEAAVNQNPEEGKRRMRALRRQVLAHDVDRWARSFLDALAATGETGDSGVTGESTPAPESDSGSF", "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 (Ref.4, PubMed:27513637). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P) to form trehalose-6-phosphate (Ref.4). ADP-Glc, CDP-Glc, GDP- Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as substrates, there is an absolute requirement for a high molecular weight polyanion for activity (Ref.4). SIMILARITY: Belongs to the glycosyltransferase 20 family."}
{"protein": "MSAPAVSQGRNVVVIGTQWGDEGKGKIVDWLTDHAQGVVRFQGGHNAGHTLIIGGKKTILRLIPSGIMRDGVACYIGNGVVLSPEALFKEIDELESAGVQVQNRLRISEATNLILPYHVAIDKAREAKRGAAKIGTTGRGIGPAYEDKVARRGLRVQDLFDPAYFAERLRENLDFHNFVLTQYLNHPALDFQQTLDEMLSYAGRLAPMVTDVSAELFAANAAGKNLMFEGAQGTLLDIDHGTYPFVTSSNCVAGNAAAGAGVGPGQLHYILGITKAYCTRVGSGPFPSELYDADNPARQDPIGVRLANVGKEFGSVTGRPRRTGWLDAAALRRAIQINGVSGLCMTKLDVLDGLETLKLCVGYMLDGKQIDILPRGSDAVARCQPIYEEFPGWNTSTFGLKEWDALPQTAQAYLKRVEEVAGIPIAMISTGPDRDETILLRHPYKD", "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": "MAIVLGIDPGSRVTGYGVIRQQGRQLTYLGSGCIRTVVDDMPTRLKLIYAGVTEIITQFQPDFFAIEQVFMAKNPDSALKLGQARGAAIVAAVNLNLPVSEYAARQVKQTVVGTGAAEKSQVQHMVRSLLKLPANPQADAADALAIAITHCHLSQNTLRLGNDQMTLSRGRIR", "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": "MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLSRAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE", "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": "MSGEDEQQEQTIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVIGVAQGTQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAKDAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTVENATSGETLEENGAGD", "text": "FUNCTION: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1- regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly (By similarity). Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). Together with PTBP1 is required for the translation initiation on the foot-and-mouth disease virus (FMDV) IRES. Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm Nucleus, nucleolus Note=Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization. SIMILARITY: Belongs to the peptidase M24 family."}
{"protein": "MRIQDYTKEMVDEKSFIDMAYTLLNEKNDTMNLYDIIDEFKALGHYEDDEIENRIVQFYTDLNTDGRFLNVGENIWGLRDWYSVADIEEKIAPTIQKFDILDDDDEEDKNLKLLGEDEADDDDDIPAVTDDQETLNDPEDPEDDDVDEDLNETDIVIDEDDEDLDEEDEEEEEFEDEEETEE", "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": "MAKGHRPRRGSLAYSPRKRSQSHIPRFRSWPESDAEPKLQGFAGYKVGMTHVIMIDDVKHSLTEGTEISVPVTIIETPAIRVAAIRAYGKDTYGEIAIAEAWTDVLDKDLSRRLKTAKNPDVNASLEKLETLVESGRANDIRLITYTLPSTLTGVPKKVPDVMETGVSGSDVKAKFEYAKTVLGTMVEISDVFDNGKIVDVAAITTGHGTQGPVKRWGINLMKNKHSRQGSLRQVGTLGPWTPAHVSWRVPQAGQMGYHQRTDYNKRILKMSSDVDEVNPAGGFVNYGLVRGNYILIKGSVPGPSKRLIRLREPTRSKVSSIGEPQIMHVSTQTLQG", "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": "MSSSSASQPSHDQLATKAQAWSALFSEPMSDLVKRYTSSVFFDKRLWQADIAGSLAHAEMLAAQGIISAQDHADIQKGMAQITQEIASGAFEWKLDLEDVHLNIEARLTQLVGDAGKRLHTGRSRNDQVATDVRLWLRGEIDLIEGLLSELQLSLVEVAEQNVEVILPGFTHLQVAQPVSFAHHLLAYVEMFARDAERMRDVRRRVNVLPLGSAALAGTTYPLDRERVAKTLGMEGVCQNSLDGVSDRDFAIEFTAAASLCMVHVSRLSEELIIWMSQNFGFIKIADRFTTGSSIMPQKKNPDVPELARGKTGRVVGHLMGLITLMKGQPLAYNKDNQEDKEPLFDTVDTLKDTLRIFAEMIGGQMNPATGCKDGGITVNAEAMRAAALKGYATATDLADYLVKKGLPFRDAHETVAHAVKAAVSHSVDLSELPLAVLQGFHPAIEKDVFDALSLQGSLNARNTLGGTAPAQVRTQLARHRARLSA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MFRRLLIATLIGILAALAVAAFRHAMQLLEWIFLSNDTGSLVNAAEGLSPWRRLITPALGGLAAGLLLWGWQKMNQQRPHAPTDYMEALQTDGQFDVGASLVKSLASLLVVVSGSAIGREGAMILLAALAASSFARRFTPREEWKLWIASGAAAGMAGAYHAPLAGSLFIAEILFGTLMLASLGPVVVSAVVALLTTHLLNGSDSLLYTVHLTVDLHAREYVMIVSTGLVAGLCGPLLMWLMTASHNSFLRLKLSPPWQLALGGLIVGLLSLLTPTVWGNGYSVVQSFLLSPPLFSLIGGIFACKILAVLASSGSGAPGGVFTPTLFVGLSIGMFLGRIWGFWLPGSDEIAILLGLAGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVVASVLSRTLRHDSIYRQHAAEH", "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": "MHFIAISINHRTADVALREQVTFRDDALRIAHEDLYETKSILENVILSTCNRTEVYAVVDQIHTGRYYIQRFLARAFGFEVDDIKAMSEVKVGDEAVEHLLRVTSGLDSIVLGETQILGQIRDAFFLAQSTGTTGTIFNHLFKQAITFAKRAHNETDIADNAVSVSYAAVELAKKVFGKLKSKQAIIIGAGEMSELSLLNLLGSGITDITVVNRTIENAMKLAAKHQVKYDELSSLPNLLESADIVISSTSAQSYIITNEMIERIAENRKQDSLVLIDIAVPRDIEPGISAITNIFNYDVDDLKGLVDANLRERQLAAATISEQIPTEIHAHNEWISMLGVVPVIRALREKAMAIQAETMDSIDRKLPGLSERERKIISKHTKSIINQMLKDPIKQAKELSSDKKSNEKLELFQNIFDIEAECPHEQAKQQKESKVKEISARRIFSFE", "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": "MDNVPIIRTVSGLRHFLRCFPGNLNTGASPSSTVIGQIGLVPTMGALHAGHLSLIQRARQENQCVIVSIFVNPLQFAAHEDLTEYPQTLNQDQALCQEQGVNTIFAPSTDTLLADAPLTQVIPPASLTEYLCGPHRPDHFTGVATIVLKLLNIVQPTRAYFGQKDAQQLAIIQRLVQDFNLDVTIVPCKLIRDATGLALSSRNQYLNAQEAQQATILHHSLQAARHTFQGGSCDRNSVLATVAQTLAKGPQVEVEYIDLVDPVTLQPLEQITTQGLVAIAARVGSARLIDNMLLDARLPILAIDGPAGAGKSTVTRRCAQAIGLQYLDTGAMYRAVAWLALDQQVEVSDPFAIADLVEDCQIELKPHADPQQQPQVWVNHQEVTQAIRTPDVTALVSAVAAQPPVREALVKQQQRLGRQGGLIAEGRDIGTNVFPDAGLKIFLTASIEERARRRQQDLKNQNLPPQTQSELEDLIASRDQQDSQREFAPLRKAYDAVEINTDGMTIEQVITRITTLYQERFPDRA", "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": "MLLCVSANHKKTSFTVLEQLARVSPDFASELVEAEDIDGAAILSTCNRFEVYIDAIQKGDQDDVCKTGLLVQNRIGELCNISPSTIIEQTSFLAGCEVSRHLFSVATGLESMIIGETEIAGQVKRALTYAQKCRTTSPELERLFQRASAVNRHIRQSTKINEVGQSLVSLSLDLASSRIGDWSGVRAIIVGTGKYASKALALLKERGVVDISVYSPSGHVNNICNTEGVRNIFNLQTALSGCDLVVGCSSVDKPVITKQDIETAQASGSRTSRVRPVGRPSTDLTAIEASNRSRHVLIDLGLPRNFDPAISDLPTADLIDLDMLRVHAPFDNLAAEKMAHELAIESSSQFVNDCKQHEATPVIVSFRNYLESLTQTSLRRTDNCKHAQHALKHFVNSLIHIPLTRCKQLAANGESHKFAESMEILFDVKTDCTEGTQYQSSCGKSFD", "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": "MSKPIQMEKGVKYRDADKMALIPVKNMPAEQKEVLRKPAWMKIKLPSDSHRIQEIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPEAEEPKKLAKTIKDMKLKYVVITSVDRDDLRDGGAQHFADCNREIREQNPNIRIETLVPDFRGRMDVALELMKDNPPDVFNHNLETAPRLYRKARPGANYKWSLDLLRKFKEQHPNIPTKSGVMMGLGETKEEIVQVLKDLREHGVTMLTLGQYLAPSRHHLPVERYVPPSEFDELKEIALELGFTHAACGPFVRSSYHADLQAQGMEIK", "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": "MDQKQIEEIVRSVMASMGQTAPAPSEAKCTTTTCAAPVTSESCALDLGSAEAKAWIGVENPHRADVLTELRRSTVARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWGKAQGLLEVRSEISDKNLYLTRPDMGRRLCAEAVEALKAQCVANPDVQVVISDGLSTDAITVNYEEILPPLMAGLKQAGLKVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRMATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR", "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": "MSWRSESIWIEFITGSRKTSNFCWAFILFLGSLGFLLVGTSSYLGRNFISLFASQQIIFFPQGIVMSFYGIAGLFISCYLWCTILWNVGSGYDLFDRKEGIVRIFRWGFPGKSRRIFLRFLMKDIQSIRIEVKEGVSARRVLYMEIRGQGAIPLIRTDENFTTREIEQKAAELAYFLRVPIEVF", "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": "MMKSIILIVLDGLGDRPGSDLQNRTPLQAAFRPNLNWLASHGINGIMHPISPGIRCGSDTSHMSLLGYDPKVYYPGRGPFEALGLGMDIRPGDLAFRANFATNRDGVIVDRRAGRENKGNEELADAISLDMGEYSFRVKSGVEHRAALVVSGPDLSDMIGDSDPHREGLPPEKIRPTDPSGDRTAEVMNAYLEEARRILSDHRVNKERVKNGRLPGNELLVRSAGKVPAIPSFTEKNRMKGACVVGSPWLKGLCRLLRMDVFDVPGATGTVGSNYRGKIEKAVDLTSSHDFVLVNIKATDVAGHDGNYPLKRDVIEDIDRAMEPLKSIGDHAVICVTGDHSTPCSFKDHSGDPVPIVFYTDGVMNDGVHLFDELSSASGSLRITSYNVMDILMQLAGRSDKFGS", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily."}
{"protein": "MSQKQTKPAAATKAAPAKTAVATTKSKKVVKKGEKKIKTRTLFNALYTKNVKNFGTGFGVQPKRDLTHFTHWPRYIKLQRQRRVLLKRLKVPPTINQFTRVFDKNTAVHLFKLLDKYRPEEASVKKARLLKIAEARAATPKGQAAPKAEKPVQHLRFGIDSVTKLIEKKKAKLVVIAHDVDPVELVLYLPTLCRRMDVPYCIVKSKSRLGELVHMRNASCVALTGVNSADSNELALLVESAKQMFNNNSEHRKTWGGNTLSGPARAILAKRQKAEAKESLAKSKI", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family."}
{"protein": "MKTSSLIAMRLIIFYLLSVVGRSTAAVEEAPASSLHIPRLNPLSSNLEYDEPSEKRAYAYISEYKRLPLYNFGIGKRWIDNSEDKRTRPFSFGIGKRLRDYRFGIGKRNSGYRPLGMDFSVDNMDFHSREDNLDDFIDDKRGGQPFSFGIGKRGWKLPMGEMAVSGRRLNDVVGPKYLLGLGKGLSENENLIQ", "text": "FUNCTION: May act as a neurotransmitter or neuromodulator. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the allatostatin family."}
{"protein": "MFDLEYQLKNLPDKPGVYLMKNNLGEIIYVGKAKILKNRVRQYFQKSQKHSEKVKAMVKNIEEFEYIITDSEIEALILECNLIKKYRPKYNILLKDDKHYPFIKVTLAEDFPRVVSTRKVTKDGSKYFGPYVDGSSVKDIIELIKKTFPIRTCKKNIVEGAKAIRPCLNYQIGLCKAPCAQYIKKSEYREIIDDVIKLLSGKHLDIVENFKLNMEKAAENLEFEKAAMLRDKINIIEKIGEKQKIILNNFDNEDYISLYSDGKDTCFQVFFLRNGKIVGREHFIIEDTFDTNSSTLISNFLKEFYGGTAYIPKTIYVPNIEDEALLEQWLTLKKESKSTIKIPIKGEKKNILVLVEKNAKTTLENFKLKYLQEKALYDNVLKDLKNILRLQEEPIRIEAFDISNIQGFDSVGSMVVFEKGRAKPSDYRRFKINTVKGADDYKSMKEILTRRFQHGLSEIKSIQDRKLEFSSGKFSVFPDLILMDGGKGQINIALEVLNTFNIDIPVCGMVKDNKHRTRGLIYNGEEIIINKYGSVMKFITRVQDEVHRFAISYHRSLRGKNSFHSLLDDIPNIGEKRKKDLLFNFKSIDNIKKATYEELLSIPSMDKKSAECVLEFFK", "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": "MRTSQYLFSTLKETPNDAQVISHQLMLRAGMIRPTAAGLYNWLPTGVKILKKVENIIREEMNKGGAIEILMPVVQPAELWQESSRWEQYGPELLRFADRGKRDFVLGPTHEEVITDLVRRELSSYKQLPLNLYQIQTKFRDEVRPRFGVMRSREFVMKDAYSFHTTPESLQQTYEVMYQVYHRIFTRLGLDFRTVQADTGSIGGSASHEFQVLASSGEDDIVFSTESDFAANIELAEAVAMGESKPATEAMVLIDTPNAKTIAELVAQFDLAIEKTVKTLIVKGANETAPLVALILRGDHELNEIKAQKHPLVAEPLAFADEDEIKAKIGVSVGYLGPVNLAIPAIVDRSVALMSDFVAGANIDGKHYLNINWQRDVVLPEVFDLRNVVVGDPSPDGRGILLIKRGIEVGHIFQLGQKYSAAMNATVQGEDGKPLVMTMGCYGIGVTRVVAAAIEQHHDERGIIWPTDEIAPFTVAIVPMNMFKSASVQAFAEQLYTDLMAQGVDVILDDRKERPGVMFADMELIGVPHMIVIGEKNLENGEVEYKNRRTGEKTMIAKDQLLAYLAQNVRA", "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": "MDGVTVIDHPLVQHKLTIMRRKETSTGSFRRLLREISTLLCYEVTRDLELTMETIETPLQTMESPILEGKKLVFASILRAGNGLLEGMLDLVPSARVSHIGVYRDHETLQPVEYYFKAPEDVAERLIIVVDPMLATGNSSIAAIDKLKERGAHNIRFLCLLAAPEGIRNFRAAHPDVPVFTASIDSHLNEKGYIMPGLGDAGDRMYGTK", "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": "MMNMKIVLFSLLLFVIRWNIISCNKNDKNQGVDMNVLNNYENLFKFVKCEYCNEHTYVKGKKAPSDPQCADIKEECKELLKEKQYTDSVTYLMDGFKSANNSANNGKKNNAEEMKNLVNFLQSHKKLIKALKKNIESIQNKKHLIYKNKSYNPLLLSCVKKMNMLKENVDYIQKNQNLFKELMNQKATYSFVNTKKKIISLKSQGHKKETSQNQNENNDNQKYQEVNDEDDVNDEEDTNDDEDTNDEEDTNDDEDTNDDEDTNDEEDTNDEEDHENNNATAYELGIVPVNDVLNVNMKNMITGNNFMDVVKNTLAQSGGLGSNDLINFLNQGKEIGENLLNITKMNLGDKNNLESFPLDELNMLKDNLINYEFILDNLKTSVLNKLKDLLLRLLYKAYVSYKKRKAQEKGLPEPTVTNEEYVEELKKGILDMGIKLLFSKVKSLLKKLKNKIFPKKKEDNQAVDTKSMEEPKVKAQPALRGVEPTEDSNIMNSINNVMDEIDFFEKELIENNNTPNVVPPTQSKKKNKNETVSGMDENFDNHPENYFKEEYYYDENDDMEVKVKKIGVTLKKFEPLKNGNVSETIKLIHLGNKDKKHIEAINNDIQIIKQELQAIYNELMNYTNGNKNIQQIFQQNILENDVLNQETEEEMEKQVEAITKQIEAEVDALAPKNKEEEEKEKEKEKEKEEKEKEEKEKEEKEKEKEEKEKEKEEKEEEKKEKEEEQEEEEEEIVPENLTTEESK", "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": "MALTLADVDKIARLSRLHLTAAEKEKSLQELNDIFAMVEQMQNINTDGIEPMAHPHEAALRLREDEVTETDRAAEYQAVAPEVRNRLYIVPQVIEE", "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": "MPTLTKLYSMEEAATHNKQDDCWVVIDGKVYDVSSYMDEHPGGDDVLLAVAGKDATDDFEDAGHSKDARELMEKYFIGELDESSLPEIPELKIYKKDQPQDSVQKLFDLTKQYWVVPVSIITISVAVSVLFSRKT", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Single-pass membrane protein Mitochondrion membrane; Single-pass membrane protein Note=Localizes preferentially on the chloroplast envelope. Localizes in stromule (stroma-filled tubular extensions of the plastid envelope membrane). SIMILARITY: Belongs to the cytochrome b5 family."}
{"protein": "MSALILDGKALAQKTEAELSERVAALKSKTGRTPILATILVGGDPASATYVRMKGNACTRIGMDSMKVELPETTTTDELLAKIAELNNNPDVHGILLQHPVPSQIDERACFDAIDLSKDVDGVTCLGFGRMAMGEEAYGCATPKGIMRLLEAYEIPLEGKHAVVVGRSPILGKPMALMLLNANATVTICHSRTKDLQSHIATADIVVGAVGIPEFIKADWIKPGAVVVDAGYHPGGVGDIELGPLADKASALTPVPGGVGPMTINTLIYQSVDSGEKKLA", "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": "MSKSRLTVFSFVRRFLLRLMVVLAIFWGGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEQALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILAVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSAPSGYVRSRQAWILRQMYQLGGEPFMQQHQLD", "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": "MKKILNGTDQVVEQMVEGLVKSHADVVHRVEGTRVIARNDKRPGKVGLVSGGGSGHEPAHAGYVGRGMLSAAVCGDVFTSPTPDQIYEGIKAADQGAGVLLIVKNYTGDVMNFEMAADLADADDIKVEQIVVDDDIAVEDSTFTTGRRGVAGTVLVHKIIGAAAEAGASLEELKALGEKVIASVKTLGVALSPCTVPEVGHPGFELGDDEIELGIGIHGEPGFTREKIMPSARLAKQLYERISSESKLLAGDKVVVLVNGMGATPLMEQYVFANDVHELLKNAGVQVEKTLVGDYMTSLEMAGLSLTILKLEDEKWVDMLKLPVDTIAW", "text": "FUNCTION: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)- dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAEEKQLFSTEISGKKFTVEVGELAKQANGACMIHYGDTSVLSVATASSEPKDLPFFPLTVNYEERLYAVGKIPGGFIKREGRPSEKAILSSRLIDRPIRPLFPDGFRNEVQVISTVMSVDQDCPSEIAAMIGSSIALSVSDIPFEQPIAGVNVGRVDGEFIINPTIEQEAKSDIELTVAGTKDAINMVEAGANEVPEDIMLEAIMFGHEEIKRLVAFQEELVKACGQDKFDVVLAESEEELVENVHSEAKDKIVNAIQVQEKHARDEAIKQAKNEIVAHYEEQEVEEDVIKQVKSILDSMVKEEVRRLITKEKIRPDGRKVDEIRPLSSRIHVLPRTHGSGLFTRGQTQALSVCTLGALGDVQILDGLDLEESKRFMHHYNFPQYSVGETGPIRGPGRREIGHGALGERALEKVIPDDKEFPYTIRLVSEVLESNGSTSQASICASTLAMMDAGVPIKAPVAGIAMGLVKSGDDYTILTDIQGMEDALGDMDFKVAGTANGVTALQMDIKIDGLSRDILEEALSQAKKGRMQILDSMLATIKEPKEELSEFAPKILTMAIEPDKIRDVIGPSGKQINQIIDETGVKIDIEQDGSIFISSTDNEMNKKAKQIIEDLVREVEVGQIYLGKVKRIEKFGAFVELFKGKDGLVHISELAEERTNKVEDVVSIDDQIMVKVKEIDRQGRVNLSRKAVIQDEKKAKEQAK", "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": "MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGIEVIAVDRYPDAPAMHVAHRSHVINMLDGEALRHVIAVEKPHYIVPEIEAIATDTLRDLEDEGLNVVPCARATQLTMNREGIRRLAAEELGLPTSTYRFADSEASFRDAVAAVGFPCIVKPVMSSSGKGQSFIRSPEQLAQAWKYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDGVYFCAPVGHRQQDGDYRESWQPQQMSELALKRAQEIARHVVLALGGHGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGAIRQYGPAASAVILPQLTSRNVTFDNVQAAVGAGLQVRFFGKPEIDGARRLGVALATGENVEEAVIRAKKAVSSVIVKE", "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": "MAPWPPGNSSLTPWPDIPTLAPNTANASGLPGVPWAVALAGALLALAVLATVGGNLLVIVAIARTPRLQTMTNVFVTSLATADLVVGLLVVPPGATLALTGHWPLGVTGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRRARAAVVLVWVVSAAVSFAPIMSKWWRVGADAEAQRCHSNPRCCTFASNMPYALLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRRELGRFPPEESPPAPSRSGSPGPAGPYASPAGVPSYGRRPARLLPLREHRALRTLGLIMGTFTLCWLPFFVVNVVRALGGPSLVSGPTFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCPPEEHLAAASPPRAPSGAPTVLTSPAGPRQPSPLDGASCGLS", "text": "FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta- 3 is involved in the regulation of lipolysis and thermogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB3 sub-subfamily."}
{"protein": "MAENSESNSKNVDVRPKTSRSRSADRKDGYVWSGKKLSWSKKSESCSDAETVSAIEKTEVPLRSQERKHSCSSIELDLDHSCGHRFLGRSLKQKLQDAVGQCFPIKNCSSRHSSGLPSKRKIHISELMLDKCPFPPRSDLAFRWHFIKRHTAPISPKSDEWVSTDLSQSELRDGQLKQRRNMEEVSCFSHTSVQPCVITSNNSSGRGGPGTDSIVNLASNNSIEDSDMDSDDEIITLCTSSRKRNKPKWEIDEEILQLETPPKYHTQIDYVHCLVPDLLQINNNPCYWGVMDKYAAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYSRSLHARIEQWNHNFSFDAHDPCVFHSPDITGLLEHYKDPSACMFFEPLLSTPLIRTFPFSLQHICRTVICNCTTYDGIDALPIPSSMKLYLKEYHYKSKVRVLRIDAPEQQC", "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": "MKNITILGATGSIGTQTLDVIRREKEELKLVAISANKSDKKVIEIIKEFKPKYAVLMEENAFKIVEDFCIDNKIDTKVLKGMEGMIYISTLEEVNTVVTSVVGMIGLVPTIKAIESGKDIALANKETLVVAGELVISKAKEHNVNILPVDSEHGAIFQCLRGNKKEEVKNIIVTASGGPFRGKKKEELIDVKPEHALKHPKWNMGRKISIDSATLMNKGLEVIEAHFLFGVDYENIKVVVHPQSIVHSMVEYKDGSVIAQMATPDMKLPIQYALNYPNRKESQIEPLDFYKISNLTFEKPDMDTFLPLKLAYEAGKKGGVMPAILNGANEVAVDLFLKGKIEFLQIGDLLQECMNKFYKSMEATLENVISVDKEVREYLGKKYDI", "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": "MATQDADIIIIGAGITGCALGAALGRQGRKVLVLERDMSEPDRIVGELLQPGGIEALEKIGIADAVEGIDGQWTSGYQIFYGDSNVSVPYPSKPNGGAYQGIGFHYGRFVMNLRKALTSTPNVTVTEATVNELLRDETGEVITGVVTSSKKSESPVEYKAPLTIVCDGCFSKFRKAFIDHPIQVTDHFLGLILTNPDYIAPGRGHVILSKVAPMVLYPISSTEARILINYPGKNLPPMETLKKYVLESCVPNMPEKLRPSLKAAVYNDRLRSMPNQFLPPTVNRTKGMILVGDSNNMRHPLTGGGMTVCFHDAYLLSRFISPSAVPDLLDYERILNQMNKFHWKRKGYSFVINVLSIALYKLFTPKNRYMKALESGCIDYFKRGGNCVEGPIRLLGGLDHSPSHLIGHFYAVCLYGIYQYVLSGPALLMPVRIIESLLIFLQASLVIIPYILSEMSS", "text": "FUNCTION: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:33223513). Erg1 catalyzes the epoxidation of squalene into 2,3- epoxysqualene (PubMed:33223513). 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: Microsome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the squalene monooxygenase family."}
{"protein": "MNKDIATPIRTKEILNKYGFSFKKSLGQNFLIDTNILDRIVDHAGVTERTGVIEIGPGIGALTEQLAKRAKKVTAFEIDQRLLPILEDTLSPYDNVTVIHQDVLKADVRAVMDEQFQDCDEVMVVANLPYYVTTPIIMKLLEENLPLKGIVVMLQKEVADRMAAKPSSKEYGSLSIAVQFYTEAKTVMNVPKTVFVPQPNVDSAVIRLTLRKEPAVAVQDAAFFFQVVKASFAQRRKTLFNNLVNNLPNGKENKSKIERALQDSHIDGKRRGESLSIEEFAVLSDRLREVLL", "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": "MRNLSGGHVEEFVLVGFPTTPPLQLLLFVLFFAIYLLTLLENALIVFTIWLAPSLHRPMYFFLGHLSFLELWYINVTIPRLLAAFLTQDGRVSYVGCMTQLYFFIALACTECVLLAVMAYDRYLAICGPLLYPSLMPSSLATRLAAASWGSGFFSSMMKLLFISQLSYCGPNIINHFFCDISPLLNLTCSDKEQAELVDFLLALVMILLPLLAVVSSYTAIIAAILRIPTSRGRHKAFSTCAAHLAVVVIYYSSTLFTYARPRAMYTFNHNKIISVLYTIIVPFFNPAIYCLRNKEVKEAFRKTVMGRCHYPRDVQD", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGMHHHRINFDKYHPGYFGKVGMRHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKNGVAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKGVGGACVLVA", "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 uL15 family."}
{"protein": "MGPSCLLFLCLLLCGGPELCYPQTQWLLPGGTPTPAGSSSPVEVECKEAELVVTVRRDLFGTGKLVQPGDLTLGSEGCQPLVAVDTDVVRLNAQLHECSSGVQVTEDALVYNTFLLHDPRPVNGLSILRTNRVEVPIECRYPRQGNVSSHPIQPTWVPFSATVSSEEKLAFSLRLMEEDWNTEKSSPTFHLGEVAHLQAEVQTGSHLPLQLFVDHCVATPSPLPGQNSSPHHFIVDSHGCLVDGLSESFSAFQVPRPRPETLQFTVDVFHFANSSRNTVYITCHLKVAPANQIPDKLNKACSFNKTSQSWLPVEGDADICDCCSNGNCSNSSSSEFETHEPAQWSTLVSRNRRHVTDEADVTVGPLIFLGKANDQAVEGWTSSAQTSVALGLGLATVAFLTLAAIVLGVTRKCHTSSYLVSLPQ", "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. ZP3 is essential for sperm binding and zona matrix formation. SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZP domain family. ZPC subfamily."}
{"protein": "MCTTLFLLSTLAMLWRRRFANRVQPEPSDVDGAARGSSLDADPQSSGREKEPLK", "text": "FUNCTION: Involved in vision. SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment Membrane; Lipid-anchor; Cytoplasmic side Endoplasmic reticulum Golgi apparatus Note=Localizes to photoreceptor disk membranes in the photoreceptor outer segment (PubMed:27613864). The secretion in media described in PubMed:24992209 is probably an experimental artifact (PubMed:24992209). SIMILARITY: Belongs to the PRCD family."}
{"protein": "MNRTFSLRRKVKKSEISTPSNFEHRIHAGFDARSGTYTGLPKQWQALLGPPRSISRPKPMVDPSCITPVDVAELKTVIRGPSSSFRYNSPLPFGMTNSPMPSVARSNSLRISATASPVVNVSSARHSFRPTLPPVSQRGYPFNDPSYAPLPLRNQKPPMSTTFGVEKPHQYQQIITIVAPSRTTTPQLQPKSPSTPQAMRQQPKCTEGVSDEEFRNALKFVVDGTDPRSDLTDYKQIGEGSTGVVEAAYKISTKQIVAVKRMNLRKQQRRELLFNEVSILRQYQHPNIVRFFSSHLVDDELWVVMEFMEGGSLTDIVTATRMTEPQIATISRQVLGALDFLHARKVIHRDIKSDSILLKRDGTVKLTDFGFCGQLSEEVPRRRSLVGTPYWTAAEVIAREPYDTRADIWSFGIMLIEMVEGEPPFFNDQPFQAMKRIRDEHEARFSRHAKVSVELSELLSHCIVKDVNKRWPAKDLLRHPFFAKAQHSSSIAPLLLQLQGNTINGNNPPTHHHSSQITTVIQ", "text": "FUNCTION: Serine/threonine-protein kinase which plays a redundant role with pak-1 in embryogenesis but, in contrast to pak-1, is not involved in commissural axon guidance of ventral cord motoneurons or in distal tip cell (DTC) migration. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MINMTKQVSKILAGLFTALFAGSLMASDAPAVGKDLTQAAENIPPAFHNAPRQGELPALNYVNQPPMVPHSVANYQVTKNVNQCLNCHSPENSRLSGATRISPTHFMDRDGKVGSSSSPRRYFCLQCHVSQANVDPIVPNDFKPMKGYGN", "text": "FUNCTION: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the NapB family."}
{"protein": "MRGIRSLPCWAPGLSTKRIPPRELFADLFPNACVISARHSARNGLIRQFSGCSGSISNSCNPRPYRSAITSLLSANVCSKGVSAVQPRFLSTVRLFSTSQRSLEPKSNVKSTGGQVVRPELHQDQEHEDIEKGFELSERAAQAAQVNLSAKLAKDGAAGKKAGFKEIWRLLLIARPEAKKLALAFLFLLVSSGITMSIPFSIGKIMDTSTKATTEGGNELFGLSLPMFYGALAGILTLGAAANYGRIIILRIVGERIVARLRSKLFRQTFVQDAEFFDANRVGDLISRLSSDTIIVGKSITQNLSDGLRAAVSGAAGFGLMAYVSLKLSSILALLLPPIGLGAFFYGRAIRNLSRQIQRNLGTLTKIAEERLGNVKTSQSFAGEVLEVRRYNNQVRKIFELGKKESLISATFFSSTGFAGNMTILALLYVGGGMVQSGAITIGELTSFLMYTAYAGSSMFGLSSFYSELMKGVGAASRLFELQDRQPTISPTKGEKVASARGPIRFENVTFSYPTRPAVPIFRDLNFEIPQGTNVAIVGPSGGGKSTIASILLRFYSPTEGRVLIGGKDITHMNAKSLRRKIGIVSQEPVLFSGTIAENIAYGKPQAKRSEIVAAARKANCQFISDFPDGLDTQVGPRGAQLSGGQKQRIAIARALIKDPDILILDEATSALDAESETLVNSALTALLRGNNTTISIAHRLSTIKRSDTIIVLGPDGRVAEQGSYEELSARPDGAFTKLMEWQMSGGEVMDQLANTPANPVAQETSWDLQSDDGTEISEDTNIPSEPRTID", "text": "FUNCTION: Pleiotropic ABC efflux transporter that may be involved in A.fumigatus adaptation to azoles. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. Mitochondrial peptide exporter (TC 3.A.1.212) subfamily."}
{"protein": "MANIVVSGEQLQEAFREVAAMVDSTVGATAGPRGNTIGISKPYGGPEVTKDGYKVMKGIKPEKPLHSAIVSTIAQSASQCNDKVGDGTTTCSILTSNMIMEASKSIAAGNDRICIKNGIQKAKDVILKEITSMSRTISLEKMDEVAQVAIISANGDKDIGNSIADAVKKVGKEGVITVEESKGSKELEVELTTGMQFDRGYLSPYFVTNNEKMSVELDDPYLLITEKKLNIIQPLLPILEAIFKSGKPLFIIAEDVEGEALSTLVINKLRGLKVAAVKAPGFGDRRKEMLEDIAALTGAKYVIKDELGIKMEDLTLEDLGTAKNVKITKDNTTIVSEDSDCDKQNRVNARINQIKSQIETSTSDYDKEKLRERLAKLSGGVAVLKVGGATEVEVKERRDRVEDALHATRAAIEEGIVPGGGVALLYAASALDKLKASSDEEQIGINIVKKVLSAPIKRLVKNAGLESAVIIDYLIKQNDKELIYNVEAMNYANASTAGVIDPAKVVRIAFETAVSVASALITTESMIVDLPNKEENASSPMGAGAMGGMGGF", "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": "MRVQRVQIMGAGALGSLVGALIQLAGYDVIFVARGKQLEALKKGLRVSGLKNAELKVYCTSQPEDADITFVTVKAYDTETVAKKLAEVDAGVVCSLQNGVGNEEILAKYCRKVLGGVTTYGANLKDYGHVVYAGEGYTYVGEMDGRVSGEAEMVAEVLRDAGMRAEAVNDIEFRIWAKAVVNAAINPITAICRVKNGEVVRNPHLWEVARAVADEGRQVMARMGYEFDAASEVRKVAEMTAENRSSMLQDLERGKRTEVEFINGAIVKKGEEFGIDCAVNRTLLNLVRGVESGL", "text": "FUNCTION: Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ketopantoate reductase family."}
{"protein": "MGSGWVPWVVALLVNLTRLDSSMTQGTDSPEDFVIQAKADCYFTNGTEKVQFVVRFIFNLEEYVRFDSDVGMFVALTKLGQPDAEQWNSRLDLLERSRQAVDGVCRHNYRLGAPFTVGRKVQPEVTVYPERTPLLHQHNLLHCSVTGFYPGDIKIKWFLNGQEERAGVMSTGPIRNGDWTFQTVVMLEMTPELGHVYTCLVDHSSLLSPVSVEWRAQSEYSWRKMLSGIAAFLLGLIFLLVGIVIQLRAQKGYVRTQMSGNEVSRAVLLPQSC", "text": "FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B- cells. Modifies peptide exchange activity of HLA-DM. SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Complexes with HLA-DM molecule during intracellular transport and in endosomal/lysosomal compartments. Heterotetramerization is necessary to exit the ER. SIMILARITY: Belongs to the MHC class II family."}
{"protein": "MSMMNRNIGFLSRTLKTSVPKRAGLLSFRAYSNEAKVNWLEEVQAEEEHAKRSSEFWKKVTYYIGGPALILASANAYYIYCKHQEHAKHVEDTDPGYSFENLRFKKYPWGDGSKTLFWNDKVNHLKKDDE", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family."}
{"protein": "MAQSSYSSGNSTSDLNKIVLDYLFKKGYSRTEAMLRLEISSVGAIPEEQQDWHIGASETYVQVYILLRDWIDGTLDLYKPKLQKVLYPIFVHSYLDLLQKNDPEMAIYFFESFRIEHEVLHGYDIRALAQLKIASDVEEIEIAQLYRKNKYRINFTRSTFDLLVQFLFENEVNGSGIIIRLLNQYIDIKITMPQVEGKEDPNVQAVYEMDEAKNEQTIISEQEGIPGHSEQLLDYNKQSIQLGLRPLSEEVVTTLKNLLEVKDKDVEGRNEALNKILHPAKNLVELLTEKENLINESTLESPSDPPLPPTKMKDIDYFVSLLESEQNSLILGKNATDPSVFMYTMHNTLSAVNCAAFSDDASMFALGCADSSIHLYSSTNNGPQPLVGSQNEPLQKSSLIGHTRPVFGVSISPQKEFILSCSEDGFTRLWSKDTKSTIVKYAGHNAPIWDVQFSPFGYYFATASHDQTARLWDVEHAAPLRVFVGHQNDVDCVSFHPNAAYLATGSSDHTTRMWDVRTGGTVRVFNAHHSPVSALCMSADGLSLASADESGIIKVWDLRSSNQHVSFVKHSSIVYSLSFSYDNKILVSGGADTDVNFWDLTYRNNLSDGEQSPLLFNFKTKNTIIQNLSFTRRNYCLALSSS", "text": "FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat TAF5 family."}
{"protein": "MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDNTPMFVKGANFDKYEGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK", "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": "LVRKRCERLYEGRMGVWNGSLKAELRPAEIVLAKKTRSFTAAPLDTLLGAKVCVDDFNNWFYSKNMECPWTVGMTKFYKGWDEFLRKFPDGWVYCDADGSQFDSSLTPYLLNAVLSIRLWAMEDWDIGEQMLKNLYGEITYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVLITMYYALRKAGYDTKTQEDMCVFYINGDDLCIAIHPDHEHVLDSFSSSFAELGLKYDFAQRHRNKQNLWFMSHRGILIDDIYIPKLEPERIVAILEWDKSKLPEHRLEAITAAMIESWGHGDLTHQIRRFYQWVLEQAPFNELAKQGRAPYVSEVGLRRLYTSERGSMDELEAYIDKYFERERGDSPELLVYHESRSTDDYQLVCSNNTHVFHQSKNEAVDAGLNEKLKEKENQKEKEKEKQKEKEKDGASDGNDVSTSTKTGERDRDVNVGTSGTFTVPRIKSFTDKMVLPRIKGKTVLNLNHLLQYNPQQIDISNTRATHSQFEKWYEGVRNDYGLNDNEMQVMLNGLMVWCIENGTSPDISGVWVMMDGETQVDYPIKPLIEHATPSFRQIMAHFSNAAEAYIAKRNATERYMPRYGIKRNLTDISLARYAFDFYEVNSKTPDRAREAHMQMKAAALRNTSRKMFGMDGSVSNKEENTERHTVEDVNRDMHSLLGMRN", "text": "FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to- cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. SUBCELLULAR LOCATION: [Capsid protein]: Virion. SIMILARITY: Belongs to the potyviridae genome polyprotein family."}
{"protein": "MSKLNAYFGEYGGQFVPQILVPALDQLEHEFIKAQADESFKQEFKELLQEYAGRPTALTKTRNIVKNTKTKLYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLDLKCRVYMGAKDVERQSPNVFRMKLMGAEVIPVHSGSATLKDACNEALRDWSANYNKAHYLLGTAAGPHPFPTIVREFQRMIGEETKQQILAKEGKLPDAVIACVGGGSNAIGMFADFIDETSVQLIGVEPAGKGIETGEHGAPLKHGKTGIFFGMKAPLMQNSDGQIEESYSISAGLDFPSVGPQHAHLLAIGRAEYASATDNEALDAFKLLCKKEGIIPALESSHALAYALKLAYENPDKEQLLVVNLSGRGDKDIFTVHDILKEKGEM", "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": "MKIRIGTRKSKLALWQANYVKDFLEKHWGVEVELVKITTTGDKITDVPLAKIGGKGLFVKEIEKALLEGSIDLAVHSLKDVPMVIPKGLKLGAITKRENPYDVLISRSGKKLYELPSGSVIGTSSLRRQVQIKKRRRDLKVEVLRGNVDTRMRKLKEGLYDAVILAYAGVKRMGYESEITEVLEDFIPAVGQGSLAIEIREGDKRIEELIKPLNNEESFLCAIAERTFLRRLEGGCQVPVGAFAKIENGTLKMKAFISDIEAERYIEGYREGNPEEAEKLGLSLAEELLKKGGEEILKEIYSSQ", "text": "FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SIMILARITY: Belongs to the HMBS family."}
{"protein": "MTKKIITLVGRPNVGKSTLFNRLSIRKKAIVHDLPGVTRDRKYTDGKIGSFEFLLIDTPGLEENPDNMGERLMGQTTQAILEADLICFMVDGKSGVLPDDKLLSNFVRKYNKHCILVVNKCEKAFDFDKEYYKLGFDSIVIISAEHGIGLIDLYDAIISKLSVEESIERNIADPFRGDCLQIVVSGRPNAGKSTFINAIINDERLLTGPEAGITRESIEVDWQYKNTHIKLIDTAGLRKKSTITASLEKLSTSDTINSIKFANTVILMIDALAHVKQQDFNIASHIVNEGRSIIIVVNKWDLVKESEKEAFQKEFYYQINTHLPQIKGVPVLFISAINKQNIEQVLDACLKIYKIWNKKITTNKLNKWLDFTTKIHPLPLQKCGRRVRIKYMTQIKTRPPTFKLFSNNPGKITDSYTRYLVNNMRDAFDMHGIPIRFTYVKNKNPYV", "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": "MRMFRITACLPSPSKIRTQRELQNTFFTKLVPYDAWFREQQRIQKLGGKIIKVELATGRPNTNTGLL", "text": "FUNCTION: Rod linker protein, associated with allophycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=This protein occurs in the rod, it is associated with allophycocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MTKLLVGLGNPGDKYFETKHNVGFMLIDQLAKKQNVTFTHDKIFQADLASFFLNGEKIYLVKPTTFMNESGKAVHALLTYYGLDIDDLLIIYDDLDMEVGKIRLRAKGSAGGHNGIKSIIQHIGTQVFNRVKIGIGRPKNGMSVVHHVLSKFDRDDYIGILQSIDKVDDSVNYYLQEKNFEKTMQRYNG", "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": "MNFTALLAAVAAALVGSANATACTATQQTAAYKTLVSILSDASFNQCSTDSGYSMLTAKALPTTAQYKLMCASTACNTMIKKIVTLNPPNCDLTVPTSGLVLNVYSYANGFSNKCSSL", "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": "MTDLRHYDVIVSPSITEKSTLVSDFNQVVFNVARTASKPEIKAAVEALFGVKVTAVNTLLRKGKTKRFRGFAGKQKDVKKAIVTLAEGQSIDVSTGL", "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": "MSDIISIKDIDLAKKKVFIRCDFNVPQDDFLNITDDRRIRSAIPTIRYCLDNGCSVILASHLGRPKEISSKYSLEPVAKRLARLLDKEIVMAKDVIGEDAKTKAMNLKAGEILLLENLRFEKGETKNDENLAKELASMVQVYINDAFGVCHRAHSSVEAITKFFDEKHKGAGFLLQKEIDFASNLIKHPARPFVAVVGGSKVSGKLQALTNLLPKVDKLIIGGGMAFTFLKALGYDIGNSLLEEELLEEANKILTKGKNLGVKIYLPVDVVAAPACSQDVPMKFVPAQEIPNGWMGLDIGPASVRLFKEVISDAQTIWWNGPMGVFEIDKFSKGSIKMSHYISEGHATSVVGGGDTADVVARAGDADEMTFISTGGGASLELIEGKELPGVKALRSKENE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MSFRAVITSSEHQAVWSRLILTLSTINQDIKFTIMSNELILWSMNSTDTTMYQVRLKASFFSEFSFDPGNIVFGEEGLQVIEDLQKQQHTLYSFVINGRHLSILSRKPEYDNIKEFSLSIDNSTAAPEAIINRLHIRVYTESLITKEFSPAFNPVKYDPIVIDLKYKKKFLDVYGTEESVNGEQADPRLLDFFRQVRKQLEEAKFNEGIIDAPRPAELRSEHEINFLSMDSLIWRNAIDLCTNNTEELKLDLTMNKMVITAFTKGVQNMKSSDVLKQAISISNSVSTEDVEHYCLFTTSGNPGMSKKDADSKQAVFKLRDFRNFFSANQAWKENATVNCWFCSPGDPILFEIDRGHVKLSLVQITDTAGKAVGAAPDLAIHPVLVSPRKPVSPLRAACTNTNAASNALHGVQLDAANMDAIKTLFVQDVEIGVSAAAMAHSPANRCTDENLRSMCSISQQGQHSCDGSPATNLRRVSRAGTTIAWGAGKDHVMCPDSDYGVAQDVNQLKRRKVGELAHASQSPESQDYGLGPTQQYQPKGIFD", "text": "FUNCTION: Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DDC1 family."}
{"protein": "MISKPDKNKIRQKRHRRVRGKLSGTADRPRLNVFRSNTGIYAQVIDDVAGVTLASASTLDKEVSKGTKTEQAVVVGKLVAERAVAKGISEVVFDRGGYLYHGRVKALADAARENGLKF", "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": "MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNRRDLNFERGGDITLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC", "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": "MADGWMARIDDALAQRRREQTYRERWALSGGNDRLIRDGDRQYLNFSSNDYLGLARHPEVIAAWQQGAAQAGVGAGGSGHVTGYGLHHQRLEQRLADWLGFPRALLFTSGFAANQALVGALTASGDHILADRLSHASLLEAAMHSPATLRRFAHNDADALQRLLRRDCAGNRLVITEGVFSMDGDRAPLPALAEITRAAGCWLMVDDAHGIGVVGEEGRGCAWAPAGRPDLLVVTFGKAVGVSGAAVLCATPVAEYLLQFARHLIYSTAPPPAQIAAIDAALTVVRRGDALRQRLWDNIVRFRRGAAALGFALAPSDTAIQPLVIGDNLRTLQLAQRLRERGVWLTAIRPPTVPPGSARLRITLTSAHLADDIDTLLEALSDAQLQNA", "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": "MSILQSVHNSFVPIHKEGYPFIVAFFVISLILGWIWSPLFWCGLILTVWCIYFFRDPDRVIPLNSNWVMSPADGRISFVESCVPPEELGLGKDEMIRISIFMDIFSCHINRIPISGTVESILYHPGRFTNAEFDKASQFNERNGVVIESKHGKIGIVQIAGMFARRIVCWSKENDAVITGERFGLIRFGSRLDIYIPTEMKLRVAVGQTAIAGETVLGSFDDKSATTDFRYD", "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": "MSGNTFGKAFRVTTWGESHGPAVGAVVDGCPPGIPLTEEAIQVMMDRRKPGSSAASTTRKEEDLVHILSGVFEGLTTGTPISLMIKNKDAKSSSYDQFKNLFRPGHGDLSYQRKYGIRDYKGGGRASARETAGRVAAGAVAGLLLERVGIKTFAYTLELGSVRAKNIDPEAVSKNPFACPDMEAAEKMEARVNEVRKDGDSLGGIVQVQAAGVPAGLGEPVFDKLDAQIAKAMMSIGAVKGVEIGAGFEAARLTGSVNNDPILEDGFETNNAGGTLSGVSSGQDIVVRVAVKPIPSISVPQQTIGLDGKADTIQVGGRHDISAIPRVNVVCEAMLNLVLADFVLRQAQVRALELFAKQ", "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": "MSIDLKKRKVEEDVRSRGKNSKIFSPFRIIGNVSNGVPFATGTLGSTFYIVTCVGKTFQIYDANTLHLLFVSEKETPSSIVALSAHFHYVYAAYENKVGIYKRGIEEHLLELETDANVEHLCIFGDYLCASTDDNSIFIYKKSDPQDKYPSEFYTKLTVTEIQGGEIVSLQHLATYLNKLTVVTKSNVLLFNVRTGKLVFTSNEFPDQITTAEPAPVLDIIALGTVTGEVIMFNMRKGKRIRTIKIPQSRISSLSFRTDGSSHLSVGTSSGDLIFYDLDRRSRIHVLKNIHRESYGGVTQATFLNGQPIIVTSGGDNSLKEYVFDPSLSQGSGDVVVQPPRYLRSRGGHSQPPSYIAFADSQSHFMLSASKDRSLWSFSLRKDAQSQEMSQRLHKKQDGGRVGGSTIKSKFPEIVALAIENARIGEWENIITAHKDEKFARTWDMRNKRVGRWTFDTTDDGFVKSVAMSQCGNFGFIGSSNGSITIYNMQSGILRKKYKLHKRAVTGISLDGMNRKMVSCGLDGIVGFYDFNKSTLLGKLKLDAPITAMVYHRSSDLFALALDDLSIVVIDAVTQRVVRQLWGHSNRITAFDFSPEGRWIVSASLDSTIRTWDLPTGGCIDGIIVDNVATNVKFSPNGDLLATTHVTGNGICIWTNRAQFKTVSTRTIDESEFARMALPSTSVRGNDSMLSGALESNGGEDLNDIDFNTYTSLEQIDKELLTLSIGPRSKMNTLLHLDVIRKRSKPKEAPKKSEKLPFFLQLSGEKVGDEASVREGIAHETPEEIHRRDQEAQKKLDAEEQMNKFKVTGRLGFESHFTKQLREGSQSKDYSSLLATLINFSPAAVDLEIRSLNSFEPFDEIVWFIDALTQGLKSNKNFELYETFMSLLFKAHGDVIHANNKNQDIASALQNWEDVHKKEDRLDDLVKFCMGVAAFVTTA", "text": "FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
{"protein": "MEGFSPPINTAQVDAKTKLDEKVDYSNLPCPVLYEELNREATMALKPELFEGFRLDYNKSLNQKFFLSHSILMGPTEVPNPTPSSEIIKIPTANYDFGAGFIDPKLYLIGRITTDGRLNARAKFDLTDNFSVKANALLTDEEDKSQGHLVIDYKGSDYRTQLQLGNNSVYAANYIQHVTPHLSLGGEAFWLGQQLMSGVGYAARYETDKTVASGQIASTGVAVMNYVHKVSEKLSFATDFIYNYLSRDVTASVGYDLITRQSRLRGKVDSNGVVAAYLEEQLPIGLRFLLSAEVDHVKKDYKFGFGVNAF", "text": "FUNCTION: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the translocation pore. Directly involved in the pore formation (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tom40 family."}
{"protein": "MRLFNQLKWYFIKEWKRYLGSIILLIIIAFLQLLPPKIIGILIDLIIKEKMSGFEILPWISIILLIAIIVYILRYLWRILLFGASYQLATELRVKFYSYLSKQSEIFFLKNRTGDLIARATNDVDRVVFAAGEGVLTLVDSSVMGISVLIVMITQISWLLTIISLIPMPIMAILIKKYGKKLHDTFRNAQSAFSLLNNQTQEILTSIRMIRAFGLEKNQLKKFNNIVNDTGKKNMEVAEIDARFDPVIYLSVAFSNLLAITAGGWLVWNNTITIGKLTSFIMYLGLMIWPMLALAWMFNIVERGSAAWDRIHSIINQNLYIEDGKKTIINMNGKLNINIDMFFYPKNKKPSLKNIYLSLNPGKTLGICGPTGAGKSTLLKLIQRQFKIHKGEILYNSSSLLELKIDYWRSKIGVVNQTSFLFSDSISNNISLGKPKASQKEIEKAAKLADIHKDIVCLPQGYNTQVGERGVMLSGGQKQRIAIARALLLNTEILILDDALSAVDGKTENNILKNLKKWKDKGYSLIIVAHRLSALIHADEIIVIKEGTIIQRGNHEKLIKEKNWYKSMYDHQKIQTEIENF", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Drug exporter-2 (TC 3.A.1.117) family."}
{"protein": "MAAVVLPPTAASQREGHTEGGELVNELLKSWLKGLVTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLGNQVDKPRLISQLEQEDKVMTEERGILSGTCPDVENPFKAKGLTPKLHVFRKEQSRNMKMERNHLGATLNECNQCFKVFSTKSSLTRHRKIHTGERPYGCSECGKSYSSRSYLAVHKRIHNGEKPYECNDCGKTFSSRSYLTVHKRIHNGEKPYECSDCGKTFSNSSYLRPHLRIHTGEKPYKCNQCFREFRTQSIFTRHKRVHTGEGHYVCNQCGKAFGTRSSLSSHYSIHTGEYPYECHDCGRTFRRRSNLTQHIRTHTGEKPYTCNECGKSFTNSFSLTIHRRIHNGEKSYECSDCGKSFNVLSSVKKHMRTHTGKKPYECNYCGKSFTSNSYLSVHTRMHNRQM", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MNENTKVIKGRTGDWEMVLGLEVHAQVASKSKLFSGAAVGFGAGPNEQVSLVDAAMPGMLPVLNRFCVEQAVKTGLGLRAQINLKSRFDRKNYFYPDLPQGYQISQFDQPIVGEGVVSVERDDGTTFDVRIERLHLEQDAGKSLHDQDPNATYVDLNRAGTALMEIVSKPDMRTSEEAAAYVKKLRTILVYLGTCDGDMEKGNLRADVNVSVCRPGDYEKFRATGDFKHLGTRCEIKNVNSYRYIQQAIEYEARRQIEILEDGGKVDQETRLFDPTKGETRSMRSKEEAHDYRYFPDPDLLPLVLDPAWVKSIEETLPELPDAKKARLQSQYGLSAYDAGVLIIDADRADYFEAAAKGRDAKLVANWVTNELLAKLSAAGTEFTNSPLPHTDIAQLVELIENGTISSKIAKEVFEHMWAGEGRPAEIVEKRGLVQINDTGAIEKAIDDLIAGNPDKAEAVKDKPQALGWFVGQVMKATGGKANPGTVNELLRKKLGVE", "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": "MARRYLFEFEKPLVELEQQIEQIRELARDSEVDVSQQLLQLETLAARRREEIFQALTPAEKIQVARHPHRPSTLDFIQMFCDDWVELHGDRRGSDDQALVGGVGRIGKRSVLLIGHQKGRDTKENVARNFGMATPGGYRKALRLMDHADRFRLPILTFIDTPGAYAGLLAEEQGQGEAIAVNLREMFRLRVPVIATVIGEGGSGGALGIGVADRLLMFEHSVYTVASPEACASILWRDAAKAPEAAAALKITGPDLLSLGVVDEVLPEPAGGNNWAPLQAGEVLREAIERHLDDLLGLKVNQLRESRYRKFRAMGRVLDPSSSETGLPA", "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": "MRLRALLLMVAALLSGAAFVTPAAAQIEVDINAGAVKPLPIAIPVFSGSTRGAEIAQVITGNLERSGLFQPLNVAGVPDKLADVNVQPRFPDWQSTGAQALINGQVTVGADGGLRVDFRLWDVFSQQQLLGLQFSSTPDNWRRVAHKISDAVYERLTGEKGYFDTRVAFVAESGPKLNRIKRLAIMDQDGANPQYLTDGSYIVMTPRFSSTSQELTYMALRPTGSSIYLLNLETSRQETVGKFPGMVFAPRFSPDGSKVAFSVERNGNSDIYVMDLRSRATTRITTDPAIDTSPSFSPDGTKIVFNSDRGGQAQIYVMNTDGSGVRRISYGGGRYTTPVWSPRGDFIAFTKQTGGEFHIGVMRADGGDERLLTTSYLDEGPTWAPNGRVLMFFREGPSGNPRLWTVDITGRILRPAAYSGSASDPAWSPLLD", "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": "MENRTPMQHHSGYEIVKSEPPSTPKTLIKSSYMENTPEMVFGSFPIHSGFCTQVVTHTDPMNNNNQPKTNANGRALAADRKRPYPCNLCSSKFGSKMELEEHQNSHTGQKPFECDTCNARFNRRSTLWNHKRIHSDAKPFVCTVCQMTFKWKNSLKCHKDMHQRKNETSAHLDNDLRQLTYATAAKRKLQMEQEENGGLPASSSASSVISHPLITTTSGNKKRSKAAKAKQTPSSLATTLSQVHLGAVQPLHASALVPPSDHQIDLDTTSLDSLMQSQNQNFLMQLYGYSDDGRHNGGMLSLDDTMLSNLSDSKSDSGSSSGGLSIQLPMQTINMLNFRNLGTQQLPPVHQLASSLPSVSSGMDYVNVNQHDSHYIVSQPDMMLGNQPLYHNGSFANIEKSNPHNNQFTIDSCVLLPSSRQDYPFDYTMVNQQYPMQEQVHDQTVGVSVVQQHYAEQAHAHGKTVPHEQW", "text": "FUNCTION: Probable transcription factor; required for proper organization of muscle myofilaments and for their recruitment to the M line. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MNINLTLIGQSLTFIAFILFCMKYVWPQLIAMMEEREKRIAEGLEAADRADKDLELAQKKAGKQLTEAKEQAATIVEQANKRGNQIVEEAKEAAVAEGERIKAAAQAEIERQVAQAREELRGKVAALAIQGAEKVLGTTVDAKAHSEMLDKLAAEL", "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": "MPDAVKVGFVPFSAAARGTLVVFCDDTLKFGSVTGKALGAAASTVKRAVAASQFKGKSGSALDLLAPEGLKVGRLIVIGTGKAAALKDNDIVKLGGAVAGKLSTGDSAVTVIAELPGGAMRPEQAAAVASGIRLRAYKFDRYKTKKKDDDADAANANVSIAVADVAAAKKAFAPDSHVVDGVILARELVNEPPNVLYPEEFAKRAAQLRKLGVQVEILDVKAMTRLKMGALLGVSQGSAHPGRTVIMRWNGGKRGAQPVAFVGKGVCFDTGGISIKPSASMEDMKGDMGGAACVVGLMHALAARKAKINVIGAIGLVENMPDGNAQRPGDIVTSMSGQTIEIINTDAEGRLVLADVLWYVAQKHKPKFMVDLATLTGAIMVALGTDHAGLFSNNDELAERLTAAGLSTGERVWRMPLGPEYDKQIDSQFADMKNTGSRNGGSITAAQFLQRFVDNTPWAHLDIAGTAMGAPKSDINHSWGSGYGVRLLNALVAEHYEAKK", "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": "MNVVLKQRIPLKIKRMGINGEGIGFYKKTLIFVPGALKGEEVFCQISSVRRNFAEAKLLKINKKSKNRVEPPCSIYKECGGCQIMHLQYDKQLEFKTDVIRQALMKFKPEGYENYEIRKTIGMSEPEHYRAKLQFQVRSFGGNVKAGLYAQGTHRLIDIKDCLVQDSLTQEMINRVAELLGKYKLPIYNERKIAGVRTVMIRRAQASGEVQLIFITSKRLDFDDVVIELVREFPELKTVAVNINASKTSDIYGQITEVIWGQESINEEVLDYGFSLSPRAFYQLNPKQTQILYSEAVKALDVKEDDDLIDAYCGVGTIGLAFAGKVKSVRGMDIIPEAIQDAKENALYMGFTNTHYEAGKAEDIIPRWYSEGFRANALIVDPPRTGLDDKLLNTILKMPPEKMVYVSCNTSTLARDLVTLTKVYHVHYIQSVDMFPHTARTEAVVKLQRKE", "text": "SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
{"protein": "MLDSIIKILFGSKHERDIKAMLPILHKINEKEAWALSLSEEEFKAKTDEFRERYQKGESLDSFIPEAFALAREAARRILGERPYDVQILGSLVLHSGKIVEMKTGEGKTLMSVAAAYLNSLTGKGVHIVTVNDYLAERDADWMRPVYSYLGVSVGVILSNMENDARRIEYNCDITYGTNNEFGFDYLRDNMQMRLKDKTQREFSFAIVDEIDSILIDEARTPLIISGAAEDDTQRFFEVDRLIGQLKEVEKNPETGEYPNELEGEEVIGDYTIDEKSKRVSFTDSGMLHIQDILQRQGLIKSGNLFDEENFEYIHYFTQSVRAHVLFHIDVDYVIQDGQVQIVDEFTGRVLEGRRYSDGLHQAIEAKEHIKIAQRNRTLATITFQNFFRMYDKLSGMTGTADTEAVEFTKIYNLDVVVIPTNLPVARKDEHDVIYLNENDKFEALCTEISEAYKRGQPVLVGTVSIEKSELISKLLTKRGVRHEVLNAKNHEREALIIAEAGAKGSVTIATNMAGRGTDIKLGGSPEMRAKKRTGTNPNPDYYEKVLAEEYAKWQSDYNEVKELGGLYVIGTERHESRRIDNQLRGRSGRQGDPGRSKFFLSLDDDLMRLFGGENLKNVMSKIGMRAGEPIEHPWINKSIEKAQTKVENRNFDIRKHLLEYDDVLNEQRSFIYEQRNAILEDENLIERIYATLEEFISEKFDEYSSSSKAEKEERARLIKDIFREKFSYTLTEEDFANIDKKNHEEEINEFVEHFTKELKEKEALAGKENLNMFIRYQYLQAIDKKWLDHLENLESLREAVYLRSYGQKNPLTEYKLEGFDIFYSMLDDIRIEIASRLVRVQISTEEEAHASRQMRSIQGNAQHNSMGSFSGSGHGMGPTALSARSRPENAQVVRTVPKVGRNDPCPCGSGKKYKYCCGKNG", "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": "MNLHEYQAKRLLAEEGVPVPRAIPAFSVREAVNQARELGGPAWVVKAQVHAGGRGKAGGVRMVDSIAQVEKAAQELLGKPLVTAQTGPQGQHVAALLIEEPSRIARELYLALMVDRGQARITFLATREGGVDIEELAASRPEALHRVVVEPSTGFLPFQARQLGFQFGLDAGQVQQLTRIMQGMYRLAQRLDALMVEINPLAITAEGRLLALDAKVVMDDNALYRHPESDELFDSTQQDGREITARQFGLNYISLEGNIGCMVNGAGLAMATMDLIKLHGGEPANFLDVGGGAAADKVNQAFKLILSDTRVKAILVNIFGGITRCDLLAEGIIQAAAEVGLHLPVVVRLEGTRKEEGMALLRESGLSLITADGLTDAAMKAVAAAQG", "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": "MSLEIEKIHAREILDSRGNPTVEVDVWTCCGFGRAAVPSGASTGTYEALELRDGGDRYDGKGVLKAVRNVNEVIGPKLIGMDVIDQRGVDQIMIEMDGTPNKSNLGANAILGVSLAVAKAAASSLGMPLYRYLGGVSATRLPVPSLNVLNGGKHAGNDLSIQEFMIEPWGADSFSEALRMAAETYHALGRILRGKYGNVATNVGFEGGYAPPISKTRDALDAIMAALDVTGYTEEIKLGLDSAASSFYLDGGYSVDDNRLSPGELIDFYVELVKTYPIVLIEDPFEENAFEEFAELTKKLPDTIIVGDDLYVTNMARIEKGIRMRSTNALLLKLNQIGTVSEAFDAATLAYRNSFKVMVSHRSAETEDSALADVSVAIGAELIKTGAPARSERNAKYNQLLRIQEALGSSASYAGRRRWS", "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": "MNKEQLEKMKNGKGFIAALDQSGGSTPKALKEYGVNEDQYSNEDEMFQLVHDMRTRVVTSPSFSPDKILGAILFEQTMDREVEGKYTADYLADKGVVPFLKVDKGLAEEQNGVQLMKPIDNLDSLLDRANERHIFGTKMRSNILELNEQGIKDVVEQQFEVAKQIIAKGLVPIIEPEVNINAKDKAEIEKVLKAELKKGLDSLNADQLVMLKLTIPTEANLYKDLAEHPNVVRIVVLSGGYSREKANELLKDNAELIASFSRALASDLRAGQSKEEFDKALGDAVESIYDASVNKN", "text": "SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family."}
{"protein": "MRLSYFHSPDRVPAEGMADAAVAIDVLRATTTMAWALHNGAEAIQAFADLAQLDAAASAWPDDQSLRAGERGGQKLEGFDLGNSPLAVTPERIGGRRIFMSTTNGTRALDRVRSAPMLLTAALVNRSAVAQRLLQHRPEQIWMVGSGWEGAYSLEDSLAAGALADALLEGSGASLLDLAGNDETCAAHALWQQWKDQPEALLRLASHGQRLQRLGDHDADLACCATVDSLTVVPSQDEPGVLRLS", "text": "SIMILARITY: Belongs to the ComB family."}
{"protein": "MYCPFCRHPDSRVVDSRVSDDGSSIRRRRQCPQCERRFTTVETTSLTVIKRSGIGEPFSRGKVINGVRKACQGRPVSEDDLAVLAQEVEENIRASGAAEIEAHEVGLAILGPLQKLDKIAYLRFASVYQAFESLDDFEHAIEILRHEADLDGSAESAKKQVRP", "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": "MANEITEQEEVKCSFCGKPQSQVKKIVAGNGVYICNECIDLSKKIIDDELKADSIKETKDLPKPMEIKKQLDEYVIGQDRAKKVLSVAVYNHYKRISQMDIDSTGTELQKSNIALIGPTGSGKTYLAQTLAKILNVPFAIADATTLTEAGYVGEDVENILLKLLQNADYDIERAQRGIIYIDEIDKISKKAENVSITRDVSGEGVQQSLLKILEGTIASVPPQGGRKHPQQQMIKIDTTNILFIVGGAFDGIENIVKNRLGKKTIGFGAENGLNQVDADDWQKNLTTGDLVKFGLIPEFIGRIPIIATLDKLSTEDLIRILTEPKNALVKQYKKLLSLDDVDLEFTDGALQAIADMAISRRMGARGLRSIVENSLMDVMYRTPSDDNIKEVQITKDVITKHAEPKITYKEDKAEKTSEATK", "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": "MINVGLLFGSKSVEHEISIITAHQVLSFVDKNKYNIIPIYITKDGKWLTGKILEDLENFKNLERLEKKSKQISSISAKDGKLILHSNIKKITIDVCLLTFHGSNGEDGSIQGMLEFLNVPYTGCGMYSSMYTMDKVITKLILKEKNIPVVDFLYTNKKNYTNDFLNHCKEVLEYPMIVKPARLGSSIGVKKVNDKCELEEAIETAFSFDDKVIVEKWIDSRELNCAVMGYKNIVVSEIEEIKKQKDFFDYNEKYVQKGKKFSNHIIPAPIDENLKNTIKSIARDTFNALECHGNIRIDFLLSKDNKIYVNEVNSIPGALSYYLWQMSGFTFSQVIDNMISIAFEAFKDKKSKIYSIDTNLFDLKVEK", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MQQAVEQALDCAEYIVESAQQRPPKRKYLSSGRKSIFQKLYDLYVEECEKEPEVKKLRRNVNLLEKLVMQETLSCLVVNLYPGNEGYSLMLRGKNGSDSETIRLPYEEGELLEYLDAEELPPILVDLLEKSQVNIFHCGCVIAEIRDYRQSSNMKSPGYQSRHILLRPTMQTLVCDVHSITSDNHKWTQEDKLLLESQLILATAEPLCLDPSVAVACTANRLLYNRQKMNTRPMKRCWKRYSRSSLNRQQDLSHGPPPPQLRLLDFLQKRKERKAGQHYDLKISKAGNCVDMWKRSPCNLAVPSEVDVEKYAKVEESIKSDDSQPTMWPAHDVKDDYVFECEGGNQYQKTKLTILQSLGDPLYYGKIQPWKADEENDSQMSPSHSSADDHSNWFVIGSKTDAERVVNQYQELVQNEAKCPVKMSHSSSGSAALSPGEEAEQAETSSIQSSVLGKGVKHRPPPIKLPSGSGNSSSGNYFTAQQASSFLKSPTPPPSCKPSLSRKSSVDLSQVSMLSPAALSPASSSQRHES", "text": "FUNCTION: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail. Required for starvation-induced ATG9A trafficking during autophagy. SIMILARITY: Belongs to the SPT20 family."}
{"protein": "MAKQGKNKVSKPRKPPTLKQKLKKESKVVKAKDLQWKLVDIPDNLGDYEGFYGLEEIDGVDVQIVNGKAEFIVRDNGKVENKSKKEETNENGENNMDVEDNETPEVEDEKPTEQEEEEEEEEEEEEEEEEEEEEEEFAGFEDDENNQEDANTSERVSNNDKDDKLAESNDELNAVSFANLDLPLPDDNEINLPNWQEGDLGSSISAYTLYGLSQLDFKKPTPIQKETIPIALSGKDVIGKATTGSGKTLAYGIPILEKYIQSLNLIKQNNKDKKINHPTGIIFAPTRELAHQVVDHLNKLAKYSPLSTRGIVSITGGLSIQKQQRLLRHGPGIIVATPGRMLELVQGDSELAKRLASIDIIVLDEADRLLQDGHFDEFEKILELFGKNRPKSKSIEWKWQTLVFSATFSRDLFRKLDRHQKGKSSSLMGNDEIVQLLNEKLKFKDKKPTLVDANPKEIVSGQITEALVECGPTERDLYLYYFLLMYKGSTLVFANSIDSVKRLVPLLNNLNIPAFSIHSSMIQKQRLRALEKFKEASQKNEVAVLVASDVAARGLDIPNIDHVVHYHLPRSADVYIHRSGRTARAGKEGVSVMFCSPQEASGPLRKLRRLVAGNSNKESRLNMHNDVKLLPIEMDLVSQIKPRVEISSKLADASISSTATRKEDSWVKQAAEDLGLDDLSGLEDFEDDIIKKQRKRKEGKMLSKDETKALKYELKTLLANPIKKNTRKSYITSGLQNLAHQMVTGAHHDDVLGHEKVNALSDLKGSKNKNKKIEKKRISKKK", "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": "MQTLTIIRPDDMHLHLRDGDALKAVAPYTARQMGRAVIMPNLKPPVVSVADALAYKARIMAALPEGSAFEPLMTLYLTDNATPELVREAKAAGIVAFKLYPAGATTNSDSGVTDLFKLIPVLEEMAKQGILFLVHGEVTDPEIDIFDREAAFIGRVMKPVLAQVPNLKVVFEHITTAEAARLVLEAGDNVAATVTPQHLLLNRNDLLVGGVRPHHFCLPVLKRETHRQALVAAVTGEKAHKFFLGTDSAPHAKSAKENACGCAGMFSAMTAIELYAEVFEKAGALDKLEAFASKNGARFYGIPENTDTITLVKQSQTVPASVPYGDGELVPMRAGGEIGWTVQY", "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": "MTDPAVTPLAFSIPQLYCPFPTAIHPEVDTLTRAGMDFMTHHGFCNTEADRLVVANIDAGAIVARWYPNPDFPVDRLQMVTDFLYLYFLIDDLRFEVINSDTGLAGPIALFAQHLDLWEYPQAHRREELDLFHQAIHDLASRMAELTTPTKAARMRRSINGWFLALLREIALFNDDHAVMAEEYLPIRVVTVASRLMIDVNGFICPAEVPGDEWYSLKVQAAAEAAMSVCLYDNELYSAGKEQWLKSRATAHDRRPRNLVALIQAQTGGSTEHALQEVAEYRNRTVCLYLNLRSQLEKTASPALLAYLSVLDGVISGNLDAHATSSRYHNPDGHHPHAIAFTPLRTTDECSARAHTPIAPPIAWWWEQLDQ", "text": "FUNCTION: Diterpene cyclases that can form multiple diterpene products. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MSCFSSRLGASCGVRAFSCASACGPRPGRCCISAAPYRGISCYRGLSGGFGSRSVCGPFRSGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKHEEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCESNMEPLFEGYIEALRREAECVEADSGRLAAELNHVQESMEGYKKRYEEEVALRATSENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRQLYEEETRLLHSHISDTSVVVKMDNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRLCEGVGSVNVCVSSSRGGVTCGGLTYGTTPGRQIASGPSVTGGSITVMAPDSCSPCQPRASSFTCGSSRSVRFA", "text": "SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MRKIVHVDMDAFYASVEQRDDPGLRGKPVVVAWRGARSVVCAASYEARTFGIRSAMPAVRAERLCPNAIFVPPDFVRYKAVSRQVREIFHRHTDLVEPLSLDEAYLDVTQAKTGMQLATEIAQLIRTQIREETELTASAGIAPNKFLAKIASDWRKPDGQFVIAPSRIDAFLLPLKVNRIPGVGKVMDGKLAALGIVTVADLRLRPLEELQAHFGSFGQSLYRRARGIDERPVEPDQDVQSVSSEDTFSEDLALDALDTHILRLAEKTWLATRRTERIGRTVVLKLKTSNFRILTRSCTPEQPPVSQEALAQIALALTRRVELPAQTRYRLVGVGLSGFSNVEEGAVQGQLFGEIPQAE", "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": "MSLVTTINWEKVDGLVPAVIQDNTSGQVLMLGYMNKEALNKTLETKQVTFWSRTKERLWTKGETSGNVLELKSINLDCDQDTLLVKVNPVGPTCHLGTPTCFDNDAEGKQEQPALVFLHQLEQVLANRKGADPESSYTASLYARGTKRISQKVGEEGVEVALAATSGDKAELVCESADLIYHLIVLLQDQGLSLSDVTEKLQERHNK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family."}
{"protein": "MSTNFEKHFEENVDDCNLEQLRDILVNKEGKSALANRFRALFNLKTAASEFEANPSDAEKAVQYMGETFGDNSELLKHEVAYVLGQTKNLKAAPLLRKTMLDLAQQPMVRHEAAEALGALGDKDSLEDLEKCLKNDPHVAVRETCELAIARINWQHSDAPTKESLQQSLYSSIDPAPPLALEKEYDLEELKKLLNDQEKPLFLRYRAMFRLRDIGTDEAVLALASGFNDPSALFKHEIAYVFGQMGSTAAVPSLTEVLGRKEEAPMVRHEAAEALGAIASEDALPILKQYLNDEVDVVRESAIVALDMWEYENSNELEYAPA", "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": "MSVRLPSSMSYGEEEEPDVLQKMWDKSKQQPFVPLGSLLTAGAVLLAARSMKRGEKLKTQRYFRYRIGFQLATLVALVGGGFYYGTETSQHKQTREDKLREKAKQREKLWIEELERRDAIIQARKQRLEESKKELRELAKQGFIEEKESNDKKED", "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": "MITRMSELFLRTLRDDPADAEVPSHKLLIRAGYVRPVGPGLYTWLPLGLRVFRKIEQIVRDEMTAIGGQEILFPALLPRAPYETTNRWTEYGDTLFRLKDRRDNDYLLGPTHEELFTLTVKGEYSSYKDFPLILFQIQTKYRDEARPRAGILRGREFVMKDSYSFDVDDDGLKTAYHLHREAYQRIFARLGVHYVIVSAVSGAMGGSASEEFLAESEVGEDTFVRCLQSGYAANVEAVLTRVPEPLPIEGQPEAVVYDTPDAPTIATLVDWANGADLPNFAGRAVTAADTLKNVLVKVREPGGEWELLAVGVPGDREVDDKRLGAALEPAEYALLDEADFARHPFLVKGYVGPKALLDNGVRYLVDPRVVDGTAWITGADAPNKHVVGLVAGRDFVADGTIEAAEVRDGDPSPDGAGPLVSARGIEIGHIFQLGRKYTEAFSADVLGEDGKPVRLTMGSYGIGVSRLVAVIAEQQHDELGLRWPAAVAPFDVHVVIANKDDGARTGATELAGELDRLGLEVLLDDRKSSPGVKFKDAELLGVPWIVVVGRGWGDGVVELRDRFSGEKREIGVDDAATEILATVR", "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": "MALIDAIHAREILDSRGNPTVEVEVLLTDGSLGRAAVPSGASTGEFEAVERRDGDKKRYGGKGVLDAVAAVEGIAEELEGEFAADQRAVDRAMRDLDGTPNKGKLGANAILGVSMAVAVAAAQASDLMLYKYLGGPNSHVLPVPMMNILNGGAHADSNVDIQEFMIAPIGAPSFREALRWGTEVYHALKTVLQEKGLSTGLGDEGGFAPSLESNRAALDLIAEAVTKAGYRLGEDIALALDVASSEFFDKGSYTFEGQQRSAEEMAAYYTELVDNYPIVSIEDPLDEDDWEGWQHLTAQLGDRVQLVGDDLFVTNVERLQRGIDEKAGNALLVKVNQIGSLTETFDAISLAQRHMFHCMISHRSGETEDTFIADLAVATNAGQIKTGAPARSDRVAKYNQLLRIEEDLADAAVYAGRSAFPRFRG", "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": "MEMERKFVHTITFGCQMNEFDSELMTGLLEGMGYEPAKSLREADLVLINTCCVRESAENRVWGLLGSLKRYKRDKPELIVAVSGCLPQQEGTAEEIIRRFPVVDLVLGTHNRHELPGLIEEVRAGRRPVLGVRQPDSAVPEGLPVRRKSGLRAWVPVIHGCNNFCTYCVVPYVRGRECSRRPDAVVDEVCGLAAAGYREVTLLGQNVNSYGRDLGEGIDFAALLARLDGVEGLWRIRFTTSHPRDFTDRLIEVVARAAKVCEHIHLPAQAGSNRVLQRMNRGYTREDYLDLVARIRAAVPDVSLTTDLMVGFPGETEEDFADTLDLVRRVGYDQAFTFVYNPRRGTPAAGWPDQVPEDVKSRRIQELIQVQKEIGLARNRAEEGKVLEVLVEGPSATRPDLLSGRSRTNKTVVFPGEPGLAGQLVRVRVEVGHLTYLAGRVED", "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": "MKIKTRFAPSPTGYLHVGGARTALYSWLFSRHLGGEFVLRIEDTDLERSTQEAIDAIMDGMNWLNLDWDEGPYFQTKRFDRYNAVIDQMLDAGTAYRCYCSKERLEALREAQMANGEKPRYDGHCRDSQCTHGADEPSVVRFRNPQEGSVIFDDKIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVIDDWDMEITHVIRGEDHINNTPRQINILKALGAPVPEYAHVSMILGDDGKKLSKRHGAVGVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFSIEEMTQLFTLDAVSKSASAFNTEKLQWLNHHYINSLPPEQVAVHLSWHVEQLGIDTRNGPELVEIVKLLGERCKTLKEMAESCRYFYEEFDAFDVDAAKKHLRPIARQPLEAVKVKLAAITEWTTENVHNAIQGTADELGVGMGKVGMPLRVAVTGVGQSPGMDVTVHAIGQARTLARIDKALAFISEREAQQ", "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": "MNHVGRKCSMSAIVGATNAGKSTLVNVLVGQKVAAVTPKVQTTRVRMHAVSNHENVQLIFIDTPGIFSPKTKLEKFLVKHAWMSLKGIENVIVLVDVKNYLNQHLKKIIDRIKHSNLNAILVLNKIDIVHQSIVSEVIEYMYSLYKFSKAFTISALYGIGIDKLVDYLCETSPYGPWLYNDDQISDAPLKFFMAEITREKLFITLRHELPYSLSVVTELVEEKEDNSLIIKQVIYVTKGSHKTIILGKKGEMVKKISMESKSDLENILQVKVHLFLFVKVREFWQNHLNECVGYAE", "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": "MRVKTGVVRRRRHKKVLKLARGFYSGRRKHFRKAKEQLERSMYYAFRDRKQKKRDFRSLWVVRINAACRMHNTSYSRFMHALKVANIELDRKVLADMAMNDMQAFTSVLESVKEHL", "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": "LTAAVAVAGGNSRYVLDGVPRMRERPIGDLVDGLKQLGAEVDCFLGTKCPPVRIVSKGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIIDKLISVLYVEMTLKLMERFGISVEHSSSWDRFVVRGGQKYKSPGKAYVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEQMGAEVTWTENSVTVKGPPRNSSAMKHLRAIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPEKLNVTEIDTYDDHRMAMAFSLAACADVPVTINDPGCTRKTFPNYFDVLQQYSKH", "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: Plastid, chloroplast. SIMILARITY: Belongs to the EPSP synthase family."}
{"protein": "MDQDYKAHFKVFCSEVREWEKIHVVGSLPVLGEWNPRKSFPLTKSTDEENTFHAIVSVPSSIKEFNFRYIRVMYLDPSENNTSEPIMVLSKWETFNNARTCLIGVESQDGVARKNITDQFGSYSGKTQITDGWILNEKESVVYFRIHGEALKFFAKSYANKEYRLKVEPFDVRYSEMFSYTRKDITDRRGVWRHSSVYASMSIDGDDVVNLPTPSLPCFSNTDLSVLTREDPIFGDQYFNGSVFRNDQDYLVFRTRTVSLQNLAFRIEFYHGEKRCALSYVLPSSMSGTHGATVSPVIGLSSAPVGHINVNYMIVKRNKYTDQNLDIDSMKTTFGRYWRKRNRMLQIGHRGMGSSYTKNIGQRENTIFSLNEAARRGADYVEMDVQLTKDLKTVVYHDFHVLVAVAGRDSPSSTPTAAGENKSLHEIAIKDLTLAQLNLLHFEHISRANGSSAESPVALSVTPSKTETDELHVPFPSLAQVLRHVDENVGLNIEIKYPMYMQDGSHECQGYFEQNKFVDIILAEVAEHAGNRRIIFSCFEPDICTMITKKQHKYPVSFLVVGATNRYMPFQDIRSDCSKIAANFAAGCELLGVNFHSEELLIDQKPIEIAEKYGLIKFVWGDDLNSKEVQKHFRDEMNVDGLIFDRIGEDEVLKQNVFVVENHNRSSLFARSQHNSRSPSMSRRCMSTVE", "text": "SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "MSSRIDRDVINALIAGHFADPFSVLGMHQTQAGLEVRALLPDATDVWVIEPKTGRKVGKLECLDARGFFCGVLPRRKNFFRYQLAVVWHGQQNLIDDPYRFGPLIQEMDAWLLSEGTHLRPYETLGAHADTMDGVTGTRFSVWAPNARRVSVVGQFNYWDGRRHPMRLRKESGIWELFIPGAHNGQLYKFELLDANGNLRIKADPYAFEAQMRPETASMICGLPEKVTQSEERQKANQFDAPISIYEVHLGSWRRHTDNNFWLSYRELADQLVPYAKWMGFTHLELLPVNEHPFDGSWGYQPTGLYAPTRRFGTRDDFRYFINAAHAAGLNVILDWVPGHFPSDDFSLAEFDGTHLYEHSDPREGYHQDWNTLIYNYGRREVSNYLVGNALYWMERFGIDALRVDAVASMIYRDYSRKEGEWIPNEFGGRENLEAIEFLRNTNRIIGEQVPGAVSMAEESTDFSGVTRPPETGGLGFWFKWNLGWMHDTLDYMKLDPVYRQYHHDKLTFGMLYNHTENFVLPLSHDEVVHGKKSILDRMPGDAWQKFANLRAYYGWMWAFPGKKLLFMGNEFAQGREWNHDASLDWHLLEGGDNWHHGVQRLVRDLNHTYRHHKALHELDFDAYGFEWLVVDDNERSVLIFVRRDKAGNEIIVASNFTPVPRYDYRFGVNQPGRWREILNTDSMHYHGSNTGNGGVVHSDEIESHGRQHSLRLTLPPLATIWLMREGE", "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": "MDDASPLSNPAKEPAALRSLLGRTNRDWWPNQLSLDILHQHGRHGNPMGDDFDYAEAFKTLDYFAVKRDLHALMTDSQPWWPADYGHYGPFFIRMAWHSAGTYRTGDGRGGANSGNQRFAPLNSWPDNANLDKARRLLWPVKKKYGAKLSWADLMIMAGNVAFESMGAPVFGFGGGRADIFEPEKDVYWGTEEQWVGKGAKTRIVEGKAFEDPLAAVQMGLIYVNPEGPDGSPDPWASARDIRMTFARMGMNDEETLALTAGGHTFGKCHGAGDAAKIGAEPEGADIAQQGLGWTSSHESGMGDHTITSGLEGPWTPTPIKWDMSYFHMLLDYKYELVRSPAGAKQWQPVNPKPEDLAPGAHSPDRRVPTMMTTADLAFAMDPEYRKIAERFRDNPDQFADAFARAWFKLCHRDMGPKSRYLGPEVPAEDLIWQDPIPPVDHPLAEAADIASLKAKLLDSGLSVADLVRTAWASAATYRGSDHRGGANGARIRLAPQKDWEVNEPEKLARVLGVLEKVKADFDASAGGGKKISLADLIVLGGCAGIEKAARDAGHAIEVPFAPGRTDASPEQTDVESFEVLEPKADGFRNYLQVRFSVPTEELLIDRSQLLGLSAPEMTVLVGGLRVLGVNHGGSKNGVFTDRPGQLTNDFFVNLLDMGTAWKQVDDKADDLFVGTCRRTHEEKWTATRTDLVFGSNSQLRALSEVYASDDAGERFVKDFVRAWTKVMNADRFDLPRAQRLARAA", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MPKRVLQGVVVSDKQDKTIVVKVERRFTHPVMKKTVRRSKNYHAHDENNAAKVGQTVFIEESRPFSKLKTWRLVEGEARDVAATEA", "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": "MDSNTVSSFQDILLRMSKMQLGSSSEDLNGMITQFESLKLYRDSLGEAVMRMGDLHSLQNRNGKWREQLGQKFEEIRWLIEEVRHRLKTTENSFEQITFMQALQLLFEVEQEIRTFSFQLI", "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": "MDVTIQHPWFRRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVLDDFVEIHGKHNERQDDHGYISREFHRRYRLPTAVDQSALSCSLSADGMLTFSGPKIVDPSHSERTIPVSREEKPSSAPSS", "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": "MEALKRKIEEEGVVLSDQVLKVDSFLNHQIDPLLMQRIGDEFASRFAKDGITKIVTIESSGIAPAVMTGLKLGVPVVFARKHKSLTLTDNLLTASVYSFTKQTESQIAVSGTHLSDQDHVLIIDDFLANGQAAHGLVSIVKQAGASIAGIGIVIEKSFQPGRDELVKLGYRVESLARIQSLEEGKVSFVQEVHS", "text": "FUNCTION: Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so that it can be reused for RNA or DNA synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Xpt subfamily."}
{"protein": "MSGLGTMVLTLLLLVFMVTSHQDGGKKQATQRNAVNIRRRKSITQRTTDEKCNEYCEERDRNCCGKANGEPRCARMCFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O3 superfamily."}
{"protein": "MWRGGRLGSRGVRLLETLGFGCPSAVAQPPRLTSRSAYSGTQLTRNLQIKPWELGEHGTMCFRSYRMALSCLSRVKTYRTPWKRLYSTSQTTVDSREVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKTSASHHPGKPLSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVLDKRIQYKVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNKTQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSLNYAAHAVRSRAQEHQEPAESALKGETGALHANTSGSPSVREEQRT", "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": "MGRTRKGRAISGWLVVDKPAGMTSTAVVNKVRWALEAQKAGHAGTLDPDATGVLAVALGEATKTVPYITDALKCYRFMVRLGLSTRTDDASGEVIATSEARPTDAEIEAALAAFRGEIQQVPPQFSAVKVEGERAYDLARDGERLDLAARPLWVESLEILSRPDADHVELEMVCGKGGYVRSIARDLGEALGCHGHVAWLRRTWSGPFEAEDGISVATIDELARSEALLSHVLPLAKGLADLPELPATPEGAARLRCGNPGMVIASDVEFGEEAWASFQGQPVAVGIYKSGELHPSRVFNL", "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": "MEIKLEQLGYCYQKNSPFEKRALLDVNVSFDSGSYSAIIGHTGSGKSTLLQHLNALLMPTEGKITVGEREIVAGVKQKKLRDLRKKVGIVFQFPEAQLFEETVEKDICFGPMNFGVSEEDAKLRAKKVIYEVGLTEEILSRSPFELSGGQMRRVAIAGVLAMDPEVLVLDEPTAGLDPHGREEIMEMFYNLHKEKGLTTVLVTHSMEDAARYAEKIVLMKAGTVLQIGSPREIFAKPDALVDLGLSVPDVVRFQGLFERKFNVKLTKTCLTIAELITEMAPYLAKGGA", "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": "MTAKDIIFDSDARAKLKVGVDKLANAVKVTLGPAGRNVLIDKKFGAPTSTKDGVTVAKEIELADAVENMGAQMVREVASKTSDVAGDGTTTATVLAQAIYREGLKNVAAGARPIDLKRGIDRAVKEVVLELRNISRSISGKKEIAQVGTISANNDPEIGELIAEAMDKVGKDGVITVEEAKGMDTELKVVEGMQFDRGYLSPYFVTNPENMEAELEDPLILIHDKKISNMKELLPILEKSAQSGRPLLIISEDIEGEALATLVVNRLRGTLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEEKGYKLENATLTYLGQAGRITVDKDNTTVVEGKGKPEEIKARINEIKGQIEKSTSDYDTEKLQERLAKLSGGVAVLNIGASTEVEMKEKKARVEDALHATRAAVQEGIVVGGGVALIRAIKGLDNAVADNEDQKTGIEIIRRALEEPLRQIVANTGTTDGAVVLEKVKNGEGDFGFNARTEQYENLVEAGVVDPTKVTRSALENAASVASILLTTEAAITDIKEEKSDMPAMPPGGMGGMGGMY", "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": "MDASGAATMAVLSSLLVFLALSSSLCSAGTLNARPAFPVQSGEIQPSGQNSKQAARRVMHPSFANAGRTPGLEIWRIENFEPVIYPKTNYGKFYTGDSFIVLNTIENKKDKKLSWDVHFWLGLETSTDEAGAAAILTVQLDDLLNGGPVQHREVQDHESQLFLSYFKNGIRYEQGGVGTGFKHVETNAQGETRLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFSTDADKQHFFDVLGSGSADQVPDESTADEDSAFERTDAAAVSLYKVSDASGKLKVDIIGQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKYPAWTQIHRIVEGSESAPFKQYFDTWRDAGMSHSRLIRSALGIGSDELLNDDEIDSVVTQLKKSGGRAFGFMPDHGQNVIETITQYVAKPGSDEIVVSTVPFDEKLPLLGFASYVLTYNYEANNGDTGSLTYVWHGVKASAAARKRAFEEGLVGSKDGLLVQTNQGHEPRHFYKIFKGKLLTSFTALPVTAQLFRIRGTVESDVHASEVAADSSSLASSDAFVLHSGKSHKIYIWNGLGASAFEKQAAVDRFSDYWDDVELEQVEEGAEPDEFWEELNGEGQYDRSLGDDGAPLLESRLFHCHLSSGGFLKVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPTARSFDTVSIIRVPQGKEPRVFKRMFPNWDDNYWQNQPSYEDMKQLVIDANNEV", "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. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SIMILARITY: Belongs to the villin/gelsolin family."}
{"protein": "MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGGGKG", "text": "FUNCTION: Conversion of dopamine to noradrenaline. SUBCELLULAR LOCATION: [Soluble dopamine beta-hydroxylase]: Cytoplasmic vesicle, secretory vesicle lumen Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen Secreted. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type II membrane protein Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the copper type II ascorbate-dependent monooxygenase family."}
{"protein": "MTKKVMDEQESHKEYLDEILQAGEVQEDTVPLVEWSQGQSSPEGECTEARIAELETELARQKEQAGKYRDELLRRAADFENFRKQKEREAMMASSRALENIIRELLPVIDDVKRLLDHAPLSAERSSEARPYIEGVEMVKKNLEKWLDEKGVKAIASIGTMLDVNFHEAISQIDSPDAEPDMIVDEYQTGYLLGERVIRHAKVIVAR", "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": "MSIEQAKKLDECFPTYKEEFEIPTFKSLGIQNDEYEDSTDSIYLCGNSLGLMPKITRTAINDELNAWSERGVESHFRHPGEEKGLTSWVDIDLPLLPLIAPIVGGKENEVAVMGTLTSNLNAMLMSFYKPSGKKTKILFEKQAFPSDYYAFLNAAKIFGYNEDHLIQIEIKEGKTYIETEDIIETITNHQDELALVCFSGIQYYTGQFFNIGEITECAKSFGITVGWDLAHAVGNVPLQLHDWDVDFAVWCSYKYLNSGPGGIAGIFVHEKHTKDNSIEQFKPRLAGWWGNNASDRFKMLEVFDPIKSALSYRQSNPSVIDVVAVKSSLELFKKVGGISELRKKSVELTGFLQALLTSSKYYIKQEETTDRLGFKILSPLNKGDRGCQLSVLFQPHYEEYSKNIMERVNKYLSDHAIVCDERRPDVIRLAPLPLYNTFSETFIAVQRLIEAMDKIAANEI", "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": "MTNTVTIELKIGYKYAAEVVKAVLGVILFHRQFSTVPARTIDVLDITVPTLVGAELNEQLATKAAEFIDTIRNEAGANGQMILLLYERSPKKSWFGKGNTIPWEQWILHTTILEEGDSYQESSLSLEAAVEQIVQAVNLRSLSYLPPVAMDSGNYPYEIVTPTSTEGWGSLLKRMIIENVSGGD", "text": "FUNCTION: Autophagy factor required for autophagosome formation (By similarity). Has a role in meiosis and sporulation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG101 family."}
{"protein": "MRRSVFCGVGAFLPAKVITNDDLSLMVDTTDEWVFRRTGIKRRHVVEEGDTVSCMATEAAKIALEDAGVSATEVDLIIVATATPDKTMPSCATMVQGSLGCKNAAAFDINAACSGFLYALSIVDSMIKAGQANIALIIGSEAMSKVVDWTDRSTCVLFGDGAGAFVFKGQDETEKPGAGVMSTLLCADGSLGNVLYTNGGVASTGKAGYICMKGTVLFEHAVVKLSSAISALLESSALDVDSIDWFIPHQANVRIIDLVINRLGLSRDKVILSIDEHANTSSASIPLAMYEAKRAGRIKKGNLVLFAAIGAGITWGVSLLRL", "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": "MESTSNPTVSFLGIDFDLTILAMSLLTITIIFILVFWASRKMTIKPKGKQNVLEYVYELVNNTISQNLGHYTKNYSLLMFILFSFVFIANNLGLMTSLKTHEHNFWTSPTANFGVDITLSLLVAFICHIEGIRKKGIGGYLKGFLSPTPAMLPMNLLEEVTNVASLALRLFGNIFSGEVVTGLLLQLAVLSPFTGPLAFALNIVWTAFSMFIGFIQAYVFIILSSSYIGHKVHGDEEE", "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": "MARMFYDADANLENLKGKTIAVMGFGSQGHAQAQNLKESGLNVIVGLRKPFDEASEKEWNAVIAAGITPMSVAEAAEAADVIQILLPDEVQARVYNAEIKPYLKAGNALGFSHGFNIHFGQIVPPAFVDVFMVAPKSPGHLVRRMYVKGAGVPGLVAVQQDYSGKAKDLALAYACGIGCTRAGVIETSFQEETETDLFGEQCVLCGGVTELVKAGFETLVEAGYQPEIAYFECMHELKLIVDLMYEGGMSYMRYSISDTAEWGDYTKGPEIIGEEARYAMYEALQDIQDGSFAKGWLLENMVGRPRFNALKRQNREHLIEEVGAELRGMMPWLKETK", "text": "FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate. SIMILARITY: Belongs to the ketol-acid reductoisomerase family."}
{"protein": "MKFYDLMCKAAQDVGLELSKEQYEKFIIYKNLLQEWNEKVNLTAITEDEDIIKKHFIDSIKAFKRDEFKEAKTLIDVGTGAGFPGIPVAIMNENIQVTLLDSLNKRVNFLNLVTEKLGLKNVVAIHSRAEDGARQKNLRESFDIATSRAVANMSVLSEFCLPYVKINGHFIALKGPAVEEEIKDSDKAITTLGGQLLDICEVEIEDTELKHNLVVVKKIKECPKVYPRKAGNVTKKPIK", "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": "MATVGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYTDGEYWHFMDPESFEQVQADKAGMGGAEKWLKGEEDCIVTLWNGAPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEVIKVDTRSGEYSARVK", "text": "FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the elongation factor P family."}
{"protein": "MAIVKVKPTSPGRRAMVKVVNKDLHQGKPHAALLDTQSSTAGRNNNGRITTRHKGGGHKHHYRIVDFRRTKDGIPAKVERLEYDPNRSANIALVLYADGERRYIIAPKGLTVGQQLMSGSEAPIRAGNTLPIRNIPVGTTIHCIEMLPGKGAQMARSAGTSAMLLAREGVYAQVRLRSGEIRRVHIECRATIGEVGNEEHSLRQIGKAGANRWRGIRPTVRGVAMNPVDHPHGGGEGKTAAGRDPVSPWGTPTKGYRTRSNKRTTTMIVQRRHKR", "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": "MSQSPRIAVVGAGLGGAAAAKLLLQEGFNVRVYEQAPSFSRLGAGIHVGPNVMKILRRIGIEDALNEQGSHPDYWYSRHWQTGDVLAQIPLGDYAVKEYGASYLTVHRGDFHALLVEALPDSVMAYGKFLTKVEDRGNVVVMHFADGTTEEADIVIGPDGVNSRIREELLGPELPKYAGYLAHRAVFPTPEVKAGMLPFDACVKWWSDDRHMMTYFVTGKADELYYVTGVPVEKWDLNDRWLESSKEEMREAFSGWHPTVQALIDATVEVTKWSLLERDPLPLWSRGRLVLLGDACHPMKPHMAQGAAMAIEDGAMLARCLKEVGAHNHELAFALYEANRAERASKVQRISHDNTWLRTNEDPSWCFGYDVFNVPLVEPKVKAAA", "text": "FUNCTION: Flavin-dependent monooxygenase (FMO) that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH, a step in the aerobic nicotinate degradation pathway. Uses NADH in preference to NADPH as an electron donor. SIMILARITY: Belongs to the 6-hydroxynicotinate 3-monooxygenase family."}
{"protein": "MRVAVDAMGGDNAPAVEVEGAVVAAREFGIPITLVGDTEKLRLELAKHNVQGLDIAIHHASEVVGMHDAASDAVRRKKDSSIRVAFDLVKSGEAEAVVSAGNSGATMAAGMFVLKRLKGIDRPAIAQIFPTLRGKTLVLDVGGNVDCKPIHLVQFAIMGEVYARHVIGVEQPRIGLLSNGEEDSKGNELTRETNAILKNISFDYEGYVEGRDIFNGMVDVVVCDGFVGNVVLKLSEGLAETVGKMLREEIASSLLSKLGYLFVRKAFKNFKKKVDYAEYGGAPLIGINGVAMICHGGSNVKAIKNAIHFAHEYVRKGVNQRLAEKMETEFTAYMQQFDAVKEAVAG", "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": "TLHDKQIRVCHLFEQLSSATVIGDGDKHKHSDRLKNVGKLQPGAIFSCFHPDHLEEARHLYEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPPVQEIFPDKFIPSAAINEAFKKAHVRPEFDESPILVDVQDTGNILDPEYRLAYYREDVGINAHHWHWHLVYPSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRMLPFNNFDEPLAGYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMVRMRERILDSIHLGYVISEDGSHKTLDELHGTDILGALVESSYESVNHEYYGNLHNWGHVTMARIHDPDGRFHEEPGVMSDTSTSLRDPIFYNWHRFIDNIFHEYKNTLKPYDHDVLNFPDIQVQDVTLHARVDNVVHFTMREQELELKHGINPGNARSIKARYYHLDHEPFSYAVNVQNNSASDKHATVRIFLAPKYDELGNEIKADELRRTAIELDKFKTDLHPGKNTVVRHSLDSSVTLSHQPTFEDLLHGVGLNEHKSEYCSCGWPSHLLVPKGNIKGMEYHLFVMLTDWDKDKVDGSESVACVDAVSYCGARDHKYPDKKPMGFPFDRPIHTEHISDFLTNNMFIKDIKIKFHE", "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": "MNNTAPGLLHQPKPFFMIFFVELWERFGYYGVQGILAVFFVKQLGFSQEQAFITFGAFAALVYGLISIGGYVGDHLLGTKRTMVLGAIVLALGYFMTGMSLLKPEMIFIALGTIAVGNGLFKANPASLLSKCYPPKDPRLDGAFTLFYMSINIGSLLSLSLAPIIAERFGYAVTYNLCGLGLIIALLVYFACRGMVRSIGSAPDHQPLNYGKLLLVLAGAVVMIFLCAWLMHNVGVANIVLIAVSAVVLYFFFREAFKQDKTGRNRMFVAFILMIEAVLFYILYAQMPTSLNFFAINNVRHELLGFAINPVSFQALNPFWVVVASPILASIYTRLGSRGRDMTMPTKFTLGMLLCSLGFLTAAAAGMWFADAQGLTSPWFVVLVYLFQSLGELMISALGLAMVAALVPQYLMGFILGMWFLTQAAAFLLGGYVATFTAVPAGIHDPLQTLPIYTGVFGKIGIATLIVTLVMAAMVPWLNRMMNTPADGQKA", "text": "FUNCTION: Proton-dependent permease that transports di- and tripeptides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpB subfamily."}
{"protein": "MTSRRSVKSGPREVPRDEYEDLYYTPSSGMASPDSPPDTSRRGALQTRSRQRGEVRFVQYDESDYALYGGSSSEDDEHPEVPRTRRPVSGAVLSGPGPARAPPPPAGSGGAGRTPTTAPRAPRTQRVATKAPAAPAAETTRGRKSAQPESAALPDAPASTAPTRSKTPAQGLARKLHFSTAPPNPDAPWTPRVAGFNKRVFCAAVGRLAAMHARMAAVQLWDMSRPRTDEDLNELLGITTIRVTVCEGKNLLQRANELVNPDVVQDVDAATATRGRSAASRPTERPRAPARSASRPRRPVE", "text": "FUNCTION: Tegument protein that plays different roles during the time course of infection (PubMed:22993164, PubMed:24131716, PubMed:9658087, PubMed:11967313). Participates in both the accumulation of viral mRNAs and viral protein translation at late time of infection (PubMed:22993164, PubMed:24131716, PubMed:9658087, PubMed:11967313). Modulates the RNase activity of the virion host shutoff protein UL41 probably to ensure necessary levels of key cellular mRNAs and proteins (PubMed:22951838). Plays a role in microtubule reorganization that occurs after viral infection by stabilizing microtubule network (PubMed:9658087, PubMed:11967313). Finally, may prevent nucleosomal deposition onto the viral genome by interacting with and inhibiting host SET (PubMed:12917472). Plays a role in the inhibition of host innate immune system by targeting the CGAS enzymatic activity which is the principal cytosolic DNA sensor that detects invading viral DNA (PubMed:29793952, PubMed:34015248). Acts by mediating disruption of liquid-like droplets in which CGAS is activated, thereby preventing CGAS activity (PubMed:34015248). SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Host Golgi apparatus Note=One of the most abundant tegument protein (about 2000 copies per virion). Localizes in the cytoplasm at 8 hours postinfection and in the nucleus at 16 hours postinfection. During virion morphogenesis, this protein probably accumulates at the trans-Golgi where secondary envelopment occurs. SIMILARITY: Belongs to the alphaherpesvirinae VP22 tegument protein family."}
{"protein": "MAGIRLHVIAPLALAAVSKCARDPAVYVRRCAANALPKLHDLRLEEHASAIEELVGILLNDHSPGVVGAAAAAFTSICPNNFKLIGKNYKKLCQILPDVEEWGQILLIGTLLRYVVARHGLVRESLMLSIHGTNSNGFCEKDGLGRDLTLDKEDGGKSDSFDVNLVSLVSKCYIQGPDEYLSRSSCTDTVSSAFDTKETTSIAHNEDVKILLQCTSPLLWSNNSAVVLAAAGVQWIMAPLEDVKKIVKPLLFLLRSSSASKYVVLCNILVFAKAVPSLFAPHFENFFICSSDAYQVKAYKLEMLSLIATTSSIASILREFEDYIKDPDRRFAADTVAAIGLCAKRLMTIPTTCLDGLLALVRQESFAGDFESADGEAGVLVQAVMSIQTMIERDPLRHEKVLIQLFRSLDSIKVAAARATIIWMVGVYCSLGHIIPRMLTTITKYLAWSFKSEASETKLQILNTIAKVLISAEAGDFHMLKRIVVYVFELGEYDLSYDIRDRTRFLKKLLSCKLASHEPAEDSVASQENIAAHVVEHVFGRKLKSVSPITLHNRFYLPGSLSQIVLHAAPGYEPLPKPCSFVYEEQDQLSDLDKQREAAADLDGSEESSETGDENGSSDYDSESSNGSDFSSEGDERTVSNDANDPAAPLIQISETSVSADQEELRSRRALDLWLDDQPSTSNQTPSALNSNQSSYAKISIGDVGSRVKPKSYSLVDPGNGSGLKVDYAFLSEVSNVSPLHVCVEVLFENSSAEPILEVNLEDEESMKVADSSEQTLVGKANASYNNIPTLIPMEEISCLEPHQSTKRLIQVRFHHHLLPMRLTLHYNEKKVPVKLRPDLGYLVKPFSMSIEEFLATESRLPGMFEYSRRCTFDDHVKDSRTENGKDKFLSICESITLKVLSNSNLHLVSVDLPVANSLEDATGLRLRFSSKILSSEIPLLITITVEGKCTEVLNLTVKINCEETVFGLNLLNRIANFMVEPSSSAT", "text": "FUNCTION: Part of the AP-3 complex, an adaptor-related complex which seems to be 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. It also function in maintaining the identity of lytic vacuoles and in regulating the transition between storage and lytic vacuoles. SUBCELLULAR LOCATION: Cytoplasm 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 large subunit family."}
{"protein": "MAKTASPGATPPGNGTEPLPDNYEMALAELETLVARMEGGALSLEDSLAAYRRGATLVAFCQQQLEKVEQQVRVLDGATLKPLSSGTAATDGEDDDL", "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": "MATLIYVDKENGEPGTRVAAKDGLKLGSAPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVRMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the securin family."}
{"protein": "MPYLYRVAYDGALFHGFTGHSNSVEAALRRVFGHLLGRGSRTDPGVSAVGNAVLAPSRLPLGYINSRLPRGVWTWAVAEVGEGFNPRRARRRRYLYVAPHWGEDVEAMREVAELFKGTHDFSSFIQFRGERGTPPVTTVDEVGVEVAGRLVYLYFVGKGFRNKQIRKMAWAILAAGRGVVSRRYVEELLERPRPGAVPSAPAEGLILLDIEYDVKFDVDRGELRKAYVYFLEKYRRLEALAAAYRAAGERLLFYDDL", "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": "MKDELFKQNPKKQFEFDKSVASVFDDMINRSVPFYRENLELCGNLLAKILPTNASICDLGCSSANFLIFLANLRKDFKLFGVDNSASMLEVAKSKAKAYGLDISFFEANLCEFDFFICDVFVANYTMQFIRPPKRQELLDKIYKNLNSKGILIMSEKILYEDAFLSKNIIELYADYKEKQGYSKFEIAAKREALENVLIPYSQKENLNMLEKAGFKKIESIFKWANFETFIAFKD", "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": "MEKQRLKAQLSSLRVPLFSVPWPGQCSNKAEVIEARMMKWADEHNLLVTDEYRNRVIRTRYGLLAARCYPNAGEVLLQAIADYLVWFFLADDLFVDRVEVATDETIRNLTAMVDVLDLNVAGSPPVFGELAWLDVCQRLRRLLQAETFERFAQGMRLWATTAALQILNHLRPTSVGIREYQTIRRHTSGMNPCASLADAANKGSVQACEFYDADVQTLVRQTNNIVCWANDIQSLRIEIHQPGQFRNIVTIYAQQGQSLQDAVETTATRVNKEIAGFCELADAVTARPISDELHGLIDGLKYWIRGYLDWVVHDTMRYADQFIESDADDRRFSAPDLSLLKKKLLVCD", "text": "FUNCTION: Terpene synthase that catalyzes the conversion of (2E,6E)- farnesyl diphosphate (FPP) into sesquiterpenes which are important for fungi-environment interactions (PubMed:31239482). Produces a mixture consisting of 8 sesquiterpenes including corvol ethers A and B, as well as traces of epizonarene, gamma-cadinene, delta-cadinene, alpha- cadinene, alpha-cadinol, and an unidentified sesquiterpene (PubMed:31239482). Produces both corvol ether A and corvol ether B in similar concentrations (PubMed:31239482). SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MIAIIDYGMGNIRSVEQALKYIGAAYIVTSDKEEIFRSDGVILPGVGAFPKAMDILEEKDLVRMLQEIGRSRKPLLGICLGMQLLFEKSEELQDCNGLSLLPGVIRKLKVPYKIPHMGWNELKKEGEIALWNGVEDGSFVYYVHSYYADCPNEIVYGISDYGVKVPGFVAKGNIYGAQFHPEKSGDIGMQMLKNFKGVVETWKSSQLSI", "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": "MDPQPGDQAQQPPPPTLTHPRFTLELEFVSSLANPYYLSHLAVNYPNLLGINKSGDDNDTNDSGDPDAQAFAAYLAYLYSYWKTPEYAQFLTHPGATLRALRLLQEDTFRRDIIRPQVIEGLAGTGIENEQGGTEANNPGEAEGEQTKGTADQQDGSSKT", "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": "MSRFCLLFVAFGFVLYFLHMEVTGKRTREDILKEAEQKGPEIKAMILENVQKCKTNCALHLKYEKCNELVPECCPKETPKCKSV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-10 family."}
{"protein": "MAELIIVYFSSKSNNTHRFVQKLGLPAQRIPVDNRPLEVSTHYLLIVPTYAAGGSDAKGAVPKQVIRFLNNPNNRKHCKGVISSGNTNFGDTFALAGPIISQKLQVPLLHQFELLGTATDVKKVQAIFARLKHHTHDKQKQINNLITERTHPCHKPMRHTSH", "text": "FUNCTION: Probably involved in ribonucleotide reductase function. SIMILARITY: Belongs to the NrdI family."}
{"protein": "MERLFCVPCGYGTTDPLTYPGPWRHCQQQNWPQNMGAPIFLARLRVPANVSQSCMNPYNRAQLQAVSTQMDPNLSLWLRSVHTTEVGVQVSLRVDKSVQCSQGSQTLHSSSLSDRTSSRKPTEAWEVGRRALIRRPQDGEDEESQEELTGPTEASQLLLPTWSRDREEQFPRLKELGEEYAHSPQDRKGKQFLELKYGYFHCKDCKRRWESAYVWCISGTNKVYFKQLCNKCQKSFNPYRVEEIQCQTCLRVCCSCSPKKRHIDVRRPHRQELCGHCKDKKFSCSVFFSLK", "text": "FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (PubMed:31598710). 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, inhibiting their translation (PubMed:31598710). SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule. SIMILARITY: Belongs to the ZAR1 family."}
{"protein": "MAAEEVTLSSHIQHHLTNAKMCSTDAGLAFNKACADSGFWTWHVDTLAWSIGLGLIFLWIFRSAAKKSTLGVPGKFQCFIEIIVEFVGDNVRDTFHGKSKLIAPLALTIFVWVFLMNLMDLIPVDFLPSFAGFVGETAFGMDSHDVYMKIVPTTDINMTSALALGVFILMVGFAIKIKGIGGFIKELTLHPFSSNNVFVQILLIPFNLLLELIALVSKPFSLALRLFGNLYAGELIFILIGAIGFMQLPLHFVWAVFHILVITLQAFLFMMLTIVYLSMASSDNH", "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": "MMSAMKTEFLCVLLLCGAVFTSPSQETYRRLRRGARSYKVTCRDGKTQMTYRQHDSWLRPLLRGNQVEHCWCDGGRAQCHSVPVRSCSEPWCFNGGTCRQALYSSDFVCQCPEGFMGKLCEIDATATCYKDQGVAYRGTWSTAESGAECANWNSSGLAMKPYSGRRPNAIRLGLGNHNYCRNPDQDSKPWCYVFKAGKYISEFCSTPACAKVAEEDGDCYTGNGLAYRGTRSHTKSGASCLPWNSVFLTSKIYTAWKSNAPALGLGKHNHCRNPDGDAQPWCHVWKDRQLTWEYCDVPQCVTCGLRQYKRPQFRIKGGLFADITSHPWQAAIFVKNRRSPGERFLCGGILISSCWVLSAAHCFQERYPPHHLKVFLGRTYRLVPGEEEQTFEVEKYIIHKEFDDDTYDNDIALLHLKSDSLTCARESASVRTICLPDASLQLPDWTECELSGYGKHESSSPFFSERLKEAHVRLYPSSRCTSQHLFNRTVTNNMLCAGDTRSGGDHTNLHDACQGDSGGPLVCMKDNHMTLVGIISWGLGCGRKDVPGVYTKVTNYLDWIRDNTRP", "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": "MALVKVKPTSAGRRGMVKVVSPNLHKGAPHAALLEKKTRGSGRNNNGHITIRHRGGGHKQHYRVVDFRRNKDGIPAKVERLEYDPNRTAHIALLCYADGERRYIIAPRGLEVGATLVSGIEAPIRAGNTLPIRNIPVGTTIHCIEMIPGKGAQMARSAGASAVLLAREGTYAQVRLRSGEVRRVHIECRATIGEVGNEEHSLRQIGKAGAMRWRGVRPTVRGVAMNPVDHPHGGGEGRTGEAREPVSPWGTPSKGFKTRRNKRTNNMIVQRRKRK", "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": "MAMVKEKEQNTKDKKLLVGVIWNFSAELKLTFMALLVLCTLATLLPFIPSSFSLSTSDFRFCISRFSSAVPLNTTTTVEESSSSPSPEKNLDRVLDNGVIKRTFTGYGSAAYNFVSMSAYRGGVNSFAVIGLSSKPLHVYGHPSYRCEWVSLDPTQDPISTTGFKILTDWGYGRIYTTVVVNCTFSSISAVNPQNSGGTLILHATTGDPTLNLTDSISVLTEPPKSVDFDLYNSTKKTKKYDYLYCGSSLYGNLSPQRVREWIAYHVRFFGERSHFVLHDAGGIHEEVFEVLKPWIELGRVTLHDIRDQERFDGYYHNQFMIVNDCLHRYRFMTKWMFFFDVDEFLHVPVKETISSVMESLEEYSQFTIEQMPMSSRICYSGDGPARTYRKWGIEKLAYRDVKKVPRRDRKYAVQPENVFATGVHMSQNLQGKTYHKAESKIRYFHYHGSISQRREPCRQLFNDSRVVFENTPYVLDTTICDVGLAVRTFELRTIGDRLLRTRQ", "text": "FUNCTION: Involved in the biosynthesis of beta-1,4-galactan. Beta-1,4- galactans are abundant polysaccharides in plant cell walls and are found as side-chain of rhamnogalacturonan I, which is a major component of pectin. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 92 family."}
{"protein": "MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGSGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAEAWLGKRLVTYQTDALGQPVHQILVEAATDIDKELYLGAVVDRASRRVVFMASTEGGVEIEKVAEETPELIHKMTIDPLAGPQPYQGRELAFKLGLTGKQVGQFAKIFMGLATLFLERDLAMVEINPLVVTKQGDLICLDGKLGADGNALFRQPELREMRDLSQEDERESRAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGSK", "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": "MAEVRVDSLEFFKSHWTAWRYLGVAHFRVENWKNLYVFYSIVSNLLVTLCYPVHLGISLFRNRTITEDILNLTTFATCTACSVKCLLYAYNIKDVLEMERLLRLLDERVVGPEQRSIYGQVRVQLRNVLYVFIGIYMPCALFAELSFLFKEERGLMYPAWFPFDWLHSTRNYYIANAYQIVGISFQLLQNYVSDCFPAVVLCLISSHIKMLYNRFEEVGLDPARDAEKDLEACITDHKHILEWAGGSLVRVLFTFQLFSRLFRRIEAFISLPMLIQFTVTALNVCIGLAALVFFVSEPMARMYFIFYSLAMPLQIFPSCFFGTDNEYWFGRLHYAAFSCNWHTQNRSFKRKMMLFVEQSLKKSTAVAGGMMRIHLDTFFSTLKGAYSLFTIIIRMRK", "text": "FUNCTION: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to ethyl acetate, anisole, hexanoic acid, and pyrazines. 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": "MTDTTPSADLGASSQQPAKAWSGRFSEPVSDLVKRYTASVFFDNRMAEQDIRGSLAHAKMLARQGIIGAQDLADIERGMAQIKGEIERGEFNWNLDDEDVHLNIEKRLTALVGDAGKRLHTGRSRNDQVATDIRLWLRDAIDQILALIGDFQKNLLDVAEANAATPMPGFTHLQVAQPVTFGHHLMAYFEMTRRDAERFADCRKRVNRLPLGSAALAGTSYPIDREFVARELGFDEVCYNSLDAVSDRDFAIEFCAASSLLMTHLSRFSEELILWMSPRFGFIDLADRFCTGSSIMPQKKNPDVPELVRGKTGRVNGSLIALLTLMKGQPLAYNKDNQEDKEPLFDTADTVIDTLRIYADMITGIRVKADNMRGALTQGYATATDLADYLVKKGLPFRDAHEAVALAVRAAEVRGCDLPQFSLDELRAAMAHVPGAADKLADDIFGVLTVEGSLDSRNHIGGTAPAQVLAAVAHARTRLG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MPKLVTWMNNQRVGELTKLANGAHTFKYAPEWLASRYARPLSLSLPLQRGNITSDAVFNFFDNLLPDSPIVRDRIVKRYHAKSRQPFDLLSEIGRDSVGAVTLIPEDETVTHPIMAWEKLTEARLEEVLTAYKADIPLGMIREENDFRISVAGAQEKTALLRIGNDWCIPKGITPTTHIIKLPIGEIRQPNATLDLSQSVDNEYYCLLLAKELGLNVPDAEIIKAGNVRALAVERFDRRWNAERTVLLRLPQEDMCQTFGLPSSVKYESDGGPGIARIMAFLMGSSEALKDRYDFMKFQVFQWLIGATDGHAKNFSVFIQAGGSYRLTPFYDIISAFPVLGGTGIHISDLKLAMGLNASKGKKTAIDKIYPRHFLATAKVLRFPEVQMHEILSDFARMIPAALDNVKTSLPTDFPENVVTAVESNVLRLHGRLSREYGSK", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system, first identified by mutations that increase production of persister cells, a fraction of cells that are phenotypic variants not killed by antibiotics, which lead to multidrug tolerance (PubMed:6348026, PubMed:8021189, PubMed:16707675, PubMed:26222023). Persistence may be ultimately due to global remodeling of the persister cell's ribosomes (PubMed:25425348). Phosphorylates Glu-tRNA-ligase (AC P04805, gltX, on 'Ser-239') in vivo (PubMed:24095282, PubMed:24343429). Phosphorylation of GltX prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance (PubMed:24095282, PubMed:24343429). Once the level of HipA exceeds a threshold cells become dormant, and the length of dormancy is determined by how much HipA levels exceed the threshold (PubMed:20616060). The hipA7 mutation (a double G22S D291A mutation) leads to increased generation of persister cells (cells that survive antibiotic treatment) probably by entering into a dormant state, as well as cold-sensitivity (PubMed:14622409, PubMed:16707675). Wild-type cells produce persisters at a frequency of 10(-6) to 10(-5) whereas hipA7 cells produce about 100-fold more persisters (PubMed:14622409, PubMed:16707675, PubMed:25425348). hipA7 decreases the affinity for antitoxin HipB, leading to increased HipA levels and persistence (PubMed:20616060); depending on the protein level, can be toxic enough to reduce cell growth or even kill cells. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7 (PubMed:14622409). The toxic effect of HipA is neutralized by its cognate antitoxin HipB (PubMed:20616060). Also neutralized by overexpression of gltX (PubMed:24343429, PubMed:28430938). With HipB acts as a corepressor for transcription of the hipBA promoter (PubMed:8021189); binding of HipA- HipB to DNA induces a 70 degree bend (PubMed:19150849, PubMed:26222023). This brings together and dimerizes 2 HipA molecules, which distorts the promoter region, preventing sigma-factor binding; additionally HipA and HipB would physically prevent RNA core polymerase from contacting the -35 promoter box (PubMed:26222023). May play a role in biofilm formation (PubMed:23329678). SIMILARITY: Belongs to the HipA Ser/Thr kinase family."}
{"protein": "MELKNSISDYTETEFKKIIEDIINCEGDEKKQDDNLEHFISVTEHPSGSDLIYYPEGNNDGSPEAVIKEIKEWRAANGKSGFKQG", "text": "FUNCTION: This protein is able to protect a cell, which harbors the plasmid ColE8 encoding colicin E8, against colicin E8, it binds specifically to the DNase-type colicin and inhibits its bactericidal activity. SIMILARITY: Belongs to the colicins ColE2/ColE8/ColE9 and pyocins S1/S2 family."}
{"protein": "MRHFVTFVVGFLLSWGFLSSLQDPPSCRCRPWEPCWPDSHQWTSLNASIDGNLVHVQPVGSVCHDPHYDAVACGDVLDLSRNSGWRASNPATLQDWIWETGSGDNESCLLVSSSERPQEIPCHQGRLPLYSAAVKSTAHVQGVIRFAKDHNLRLVIKNTGHDATGRSAAPDSLQIHTYFLKDIHYDDNFLVHGDATGSGPAVTLGAGVVHSEVYKHGIDHKYSVVGGECPTVGIVGGFLQGGGVSSWSGFTRGLAVDNVLEYQVVTANAELVIANEHQNQDLFWALRGGGGGTFGVVTQATVRAFPDDPTVVSTLVLSSTRADTSFWVKAISRLLSILRSCNQQNVHGQLIITRPSVDILNAGLTLHFSNMTNVLHAETLLQPHIASLSEDQISTTLTSKFVANINSELRLDADIHPRGIGTLQTSMMISNELFGSSEGPLTVAQVFGKLPIGPNDLLFTSNLGGCIAANKGLDTAIHPAWRSSAHLVTYVRSVEPSIEAKKLALKEITNKYMPILYSMQPSFKVSYRNLGDPNEKNYQEVFWGEKVYKRLASIKAKLDPDGLFISKLGVGSEDWDTEGMCYQPQNRVSQPLRSLKYFLSVLKDT", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L- methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). The presence of easA is not required to complete this reaction (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MLMPKRVKYRKTQRGRMKGNAGRGTSVAFGSFGLKAIEPAWITSRQIEAARVAMNRYMKRDGKIWIRIFPDKPVSKKAAETRMGSGKGSPEFWVAVVKPGRIMFEADGVPMEVATEAFRLAAKKLPIKTRFIVRPDYEA", "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": "MTEFSIGRSEIAGVVLAGGRSQRMGRDKAGAMLGAESLLRHVLTRLSQQVLPVAVNADAAAEDVPVIPDRFRGKAGPLAGIHAAMVYAAGLPGITHVVTVSVDCPFFPADLVARLAAALERQSQIAIAASEGRSHPVFGLWPVTLAADLEAWMVTDEKRRVRDFLLRHDVTEVTFPLHPTRASLLDPFFNINTPDDLAEAERWLEALRA", "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": "MSPVEISGADAVVSPPMRGRVPLPPPPPPPPPPMRRRAPLPPPPPPPMRRRAPLPPPPPPAMRRRVLPRPPPPPPPLPMFDAEVLCCCYPPTRVRREAPLPPPPLIFVGAPPPTCALKGIVCCFPCPSKKKSSLKRFNWVKITRALPGSLWDELQIQQVCHGDIEDEQILCAIELDVSEIETFFSLGAAKPEKDPLIDLRRATDTELTLMLLNIRLPADMMAAIMAMDESVLDDDEIRGLINLFPTKENMELLMSYTGGKWTLEKWEQYFQELRKVLRVESKLRVFYFKIQFSTKITQFKKRLNVVNSACEEVCSSQKLKEIMKKITCLGNTSNQGTGRGVTVGFNLDSLCVKSMHNFCKVLASEASDLLDVHKDLQSLESASKKQLKSLAEEMQDIIRDLEKLNQELTAAETDGPDSQVFRNVCWFCSYGYFDQPWI", "text": "SIMILARITY: Belongs to the formin-like family. Class-II subfamily."}
{"protein": "ANNFDLMYEQVKFYGEVTQQMLKVSVLEMDGQFDR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the phosphoribulokinase family."}
{"protein": "MSDSAVATSASPVIAQAASGEKKVSTKKGSSTPESKKSTAAPPSHPPTQQMVDASIKNLKERGGSSLLAIKKYIGATYKCDAQKLAPFIKKYLKNAVANGNVIQTKGKGASGSFKLSASANKDAKPKASAVEKKTKKVNASAARATKSKSSTSTTKKAAGAADKKLSKSAAAKKNVEKKKADKEKAKDAKKTGTIKAKPTTAKAKSSATKPKTPKPKTTSAKPKKVVSATTPKKTAVKKPKAKTASATKK", "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": "MKEKLKELQELAIKQIENSIKSNELEEIRVKFLGKKGELTTILRGMGGLSPEERPLVGKLVNEAKAKVEEKLESAIKKIKDKEKAEKLAGETIDISLPGKKQVIGKSHPLELTLKNMEDIFVSMGFTIEEGPEVEYDHYNFEALNIPKNHPARSEQDTLYINDNIVLRTQTSPVQVRTMENQKPPIKMISPGKVYRSDSVDATHSPIFYQMEGLVIDKGVTFADLKGTLELFAKKMFGDKVETKFRPHHFPFTEPSAEMDATCFVCGGEGCRVCKNSGWIELLGCGMVHPNVLRNCGIDPEVYSGFAFGFGVDRMVMLKYGIDDIRLLYESDMRFLNQF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MHSLQAKILDPRLGTDFPLPQYATPGSAGLDLRAMLEEDTVLGPGQTLLIPTGLSIHIADPGLAALVLPRSGLGHKHGIVLGNLVGLIDSDYQGELMVSCWNRGESPFTIAVGERIAQLVLVPVVQAHFELVEQFDESQRGAGGFGHSGSH", "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": "MVDSFVQSKLRDNKVTLFVKGSCPYCKNAIVLLKEFNFLPGCLEVVDITGMDDIQDYFQKTTGQRTVPRVFIGTKCIGGFSDLQKMEQQLPMMLRQIGALV", "text": "FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family."}
{"protein": "MDVQERLDAILDITDSKICPHCLGRRFSDVMEGPGNRLRGERLVEKFSLHLEGPCLVCGDVFERLDEAALRVREKVDDLNLEYSSVLVGTRLPDDVLRIDEEIDRRLGIQVEGIKREVNRELGKRVTSILRCPADFESPDLVITVDLRGQIRVHVQINPIFIEGRYRKLVRGIPQTKWPCRSCRGRGCSRCDYTGKMYPTSVEELISEPVLEATGGSDSKFHGSGREDVDVRMLGTGRPFVLEIKEPAIRTPDLRALEDEINRRARGMVEVADLRFSSRNRKVELKESSRKKYKVYRAIVELEGAVSDEDLVKLEKLDLIRQRTPLRVSHRRADRIRERRVLEISWKRLDDHLELIIKAEGGLYIKELISGDSGRTEPSVSSILGVPARCASLDVLEVGEPA", "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": "MKRTFQPSNLVRARRHGFRARMATKGGRLVLNARRAKGRKKLSA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
{"protein": "MGDAESTSKTSLLLPVERVENVTWRDLRDGLFTAELKRLICFAAPMAAVVIAQFMLQIISMVMVGHLGNLSLASASLASSFCNVTGFSFIVGLSCALDTLSGQAYGAKLYRKVGVQTYTAMFCLALVCLPLTLIWLNMETLLVFLGQDPSIAHEAGRYAACLIPGLFAYAVLQPLTRYFQNQSMITPLLITSCFVFCLHVPLCWLLVYKSGLGNLGGALALSFSNCLYTIILGSLMCFSSACSETRAPLSMEIFDGIGEFFRYALPSAAMICLEWWSYELIILLSGLLPNPQLETSVLSVCLQTTATVYSIHLAIAAAASTRISNELGAGNSRAANIVVYAAMSLAVVEILILSTSLLVGRNVFGHVFSSDKETIDYVAKMAPLVSISLILDGLQGVLSGIARGCGWQHIGAYINLGAFYLWGIPIAASLAFWIHLKGVGLWIGIQAGAVLQTLLLTLVTGCTNWESQADKARNRMALAYGT", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MTSPAALSPTPFGRVVTAMVTPFDDSGAVDLPLAGRLARHLVEQGSDGLVVSGTTGESPTLSWQEQLQLLQAVREAVGSDAQVLAGTGSNCTAEAVEATRQAAAAGADGALVVVPYYNKPPQDGLAAHFRAIAEAAPELPLMLYNIPGRTGCSMAPETVAQLMDCPNVVSFKAASGTTEEVTALRLACSSKLAIYSGDDGLTLPMISVGAVGVVSVASHVVGPQIRAMIDAYMQGDAAVALALHEQLQPVFKALFATTNPIPVKAALQLNGWSVGDPRPPLSPLPDDMRSTLAQTMAALRQT", "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": "MLSIILLLMQLVAADIAVVGPSLDQSFDASGGTAKIPIQWLFTPNTPSQDDFTSLTFSLCSGPNYKIEAFKVIGKLSDIGTTDFEAEVSQSVGANGYYYVQIYAATTDGYTIHYSPRFKLTGMTGSKLPDTLLITAPPTPETRVTTGDLGATIDSKSFDIPYGEQNGKAKFAPMQTQPGTKITATTWSRRYATSAVSFFTSLTATPVQHTTLTPGWSYYISSDYNYAPPAPFPSDNGGWYDPKKRQSFTTRKLNMDKLRKRRQTS", "text": "FUNCTION: Involved in cell wall beta(1->6) glucan synthesis. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the KRE9/KNH1 family."}
{"protein": "MRVTDFSFELPESLIAHYPMPERSSCRLLSLDGPTGALTHGTFTDLLDKLNPGDLLVFNNTRVIPARLFGRKASGGKIEVLVERMLDDKRILAHIRASKAPKPGAELLLGDDESINATMTARHGALFEVEFNDDRSVLDILNSIGHMPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPTAGLHFDEPLLEKLRAKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQDVVDAVLAAKARGNRVIAVGTTSVRSLESAAQAAKNDLIEPFFDDTQIFIYPGFQYKVVDALVTNFHLPESTLIMLVSAFAGYQHTMNAYKAAVEEKYRFFSYGDAMFITYNPQAINERVGE", "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": "MHLNTLSPAPGSHKARKRCGRGIGSGIGKTGGRGHKGQKSRSGGSVRPGFEGGQMPLKQRLPKFGFTSRKSLVRAEVRLHELNLITGDVVDIHALKDAGLITRNIVAVKVMLSGEITRPITLRGIAVTKGAQAAIEAAGGKVEE", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MTNIRKTHPLLKIVNSSFIDLPTPSSISSWWNFGSLLGVCLIMQIATGLFLAMHYTSDTTTAFSSVAHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGIYYGSYMFTETWNIGIILLFATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFTFHFILPFIITALAMVHLLFLHETGSNNPSGLNSDADKIPFHPYFTIKDVLGILVLLTILTAFTLFVPDLLGDPDNYISANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILAIFPLLHTSKQRSLMFRPITQVLYWILVADLFTLTWIGGQPVEHPFIIIGQLASILYFSIILIMMPISGIIENKILKLN", "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": "MAKDKDVRPIIKLKSTAGTGYTYVTRKNRRNDPDRMVLKKYDPKIRQHVEFREER", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MKLDSIDITHCQLVKSTRTARIYRSDTYAIKCLALDFDIPPHNAKFEVSILNKLGNKCKHILPLLESKATDNNDLLLLFPFEEMNLYEFMQMHYKRDRRKKNPYYDLLNPSIPIVADPPVQKYTNQLDVNRYSLSFFRQMVEGIAFLHENKIIHRDIKPQNIMLTNNTSTVSPKLYIIDFGISYDMANNSQTSAEPMDSKVTDISTGIYKAPEVLFGVKCYDGGVDVWSLLIIISQWFQRETSRMGHVPAMIDDGSDDMNSDGSDFRLICSIFEKLGIPSIQKWEEVAQHGSVDAFVGMFGADGDGKYVLDQEKDVQISIVERNMPRLDEIADVKVKQKFINCILGMVSFSPNERWSCQRILQELEKP", "text": "SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MTVLIHVLGSDIPHHNRTVLRFFNDALAATSEHAREFMVVGKDDGLSDSCPALSVQFFPGKKSLAEAVIAKAKANRQQRFFFHGQFNPTLWLALLSGGIKPSQFFWHIWGADLYELSSGLRYKLFYPLRRLAQKRVGCVFATRGDLSFFAKTHPKVRGELLYFPTRMDPSLNTMANDRQREGKMTILVGNSGDRSNEHVAALRAVHQQFGDTVKVVVPMGYPPNNEAYIEEVRQAGLELFSEENLQVLSEKLEFDAYLALLRQCDLGYFIFARQQGIGTLCLLIQAGIPCVLNRENPFWQDMTEQHLPVLFTTDDLNEDIVREAQRQLASVDKNTIAFFSPNYLQGWQRALAIAAGEVA", "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": "MSNFNSSPVPTIFMSFFQMTKRVRLSDSFNPVYPYEDESTSQHPFINPGFISPNGFTQSPDGVLTLKCLTPLTTTGGSLQLKVGGGLTIDDTDGFLKENISAATPLVKTGHSIGLSLGPGLGTNENKLCAKLGEGLTFNSNNICIDDNINTLWTGVNPTTANCQIMASSESNDCKLILTLVKTGGLVTAFVYVIGVSNDFNMLTTHKNINFTAELFFDSTGNLLTSLSSLKTPLNHKSGQNMATGALTNAKGFMPSTTAYPFNVNSREKENYIYGTCYYTASDHTAFPIDISVMLNQRALNNETSYCIRVTWSWNTGVAPEVQTSATTLVTSPFTFYYIREDD", "text": "FUNCTION: Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. SUBCELLULAR LOCATION: Virion Host nucleus Note=Anchored to the pentons, protrudes from the virion surface. SIMILARITY: Belongs to the adenoviridae fiber family."}
{"protein": "MAFKRKFTPKRKFCRFCADKNLPLDYKRPDILKDFVTERGKIIARRITGTCAKHQRRLTTEIKRSRQMALMHYTTVHSTDVKKKSI", "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": "MDRGIDLQGTFIQSLESLGLSPGLSKVLWMPLPMLLMIIAATVGVLVTVWLERKISAAVQQRIGPEYAGPLGVLQSAADGLKLILKEDIIPAKADAFLFTIGPALVVIPVFLSYLIVPFGQELIITNVGAGVFLWIALSSIQPIGLLMSGYASNNKYSLLGGLRAAAQSISYEIPLALAVLAVVMMSNSLSTIDIVDQQSGYGILGWNIWRQPVGFIIFWIAALAECERLPFDLPEAEEELVAGYQTEYAGMKFALFYVGSYVNLILSALLVSILYLGGWEFPIPLDRVADWIGVDPANPILQITTAALGITMTVLKAYLLVFTAILLRWTVPRVRIDQLLDLGWKFLLPISLVNLLVTAALKLTFPVAFGG", "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": "MPVHMMMSGIIIAGGRSRRFGTDKRRLRLWGEQGPCLLERAVALLQPLCSEVLVVLNDAHAWPDLPARLVADEQPGSGALGGVISGLQAMQTPTALVIAADMPVIVPALLAALAQWPFVGDALIPSSYPHPGQLQPLLAVYRHSALAPLRRVFAAGERRLQVAVTALHWVDPGPELWQMYDPTARSLLNLNTPDDLKLVQAYLGTTNI", "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": "MATAVASQVAVSAPAGSDRGLRSSGIQGSNNISFSNKSWVGTTLAWESKATRPRHANKVLCMSVQQASESKVAVKPLDLESANEPPLNTYKPKEPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGIIPPGENPKKPGAPHNVRLYSIASTRYGDSFDGRTTSLCVRRAVYYDPETGKEDPSKNGVCSNFLCNSKPGDKVKVTGPSGKIMLLPEEDPNATHIMIATGTGVAPFRGYLRRMFMEDVPKYRFGGLAWLFLGVANTDSLLYDEEFTSYLKQYPDNFRYDKALSREQKNKNAGKMYVQDKIEEYSDEIFKLLDGGAHIYFCGLKGMMPGIQDTLKKVAEQRGESWEQKLSQLKKNKQWHVEVY", "text": "FUNCTION: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family."}
{"protein": "MAAKRKAAAMNAVDDEPVDPSDELAFYCLGGGNEVGRSCHIIQYKGKTVMLDAGMHPAKEGFSALPFFDEFDLSTVDILLISHFHVDHSSALPYVLSKTNFKGRVFMTHATKAIYKWLIQDNVRVNNTASSSDQRTTLYTEHDHLSTLPLIETIDFNTTHTINSIRITPYPAGHVLGAAMFLISIAGLNILFTGDYSREEDRHLIPATVPRGVKIDVLITESTFGISSNPPRLEREAALMKSITGVLNRGGRVLMPVFALGRAQELLLILEEYWETHPELQKIPIYYIGNTARRCMVVYQTYIGAMNDNIKRLFRQRMAEAEASGDKSVSAGPWDFKYVRSLRSLERFDDVGGCVMLASPGMLQTGTSRELLERWAPNERNGVVMTGYSVEGTMAKQLLNEPDQIHAVMSRAATGMGRTRMNGNDEEQKIMIPRRCTVDEISFAAHVDGVENRNFIEEVSAPVVILVHGEKHQMMRLKSKLLSLNAEKTVKVKVYTPANCEEVRIPFRKDKIAKVVGKLAQTTLPTDNEDGDGPLMAGVLVQNGFDLSLMAPDDLREYAGLATTTITCKQHITLSSASMDLIKWALEGTFGAIEEIGTDEDAEKEDQQSESEEKQRMKEEADEEIPMEKPQAYLVMGCVVIRYHPRTREVELQWEGNMMNDGIADAVMAVLLTVESSPASVKQSAKHNKHHHHHHHDETDTLKFLNPHAAQDAEERFARLLMMLEAQFGSDIAPIERPRVPSSTESATTTTNGNGNSKSDSEQLSSLESKTDGATPQDPDTLSELEAAELSRLHALGIPVPGIEIKVDKHVARVWLEDLEVECANAVLRDRVRVVIERAVETVASMWSVGRSSKTITNGGGKEIAGTGADDVASKPGLEVAARA", "text": "FUNCTION: Component of the cleavage factor I (CF I) involved in pre- mRNA 3'-end processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily."}
{"protein": "MSSRGHSTLPRTLMAPRMISEGDLGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLLPYWGI", "text": "FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases. Plays a negative role in TCR signaling by dephosphorylating MAP3K7 adapter TAB1 leading to its inactivation. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "QQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPNGPGSIPPGTLTTLWALSVAIFSVGGMFSSFLLGIISQWLGRKKAMLFNNTLAVLAGALMGLAKAAASYEMLILGRFLIGAYSGLASGLVPMYVGEIAPTHLRGALGTLNQLA", "text": "FUNCTION: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endomembrane system; Multi-pass membrane protein Cytoplasm, perinuclear region Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (By similarity). The dileucine internalization motif is critical for intracellular sequestration (By similarity). Insulin stimulation induces translocation to the cell membrane (By similarity). SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily."}
{"protein": "MINKTTIKTVLITLGVLAAVNKVSALRSVKRLIS", "text": "FUNCTION: Exolysin that catalyzes the cleavage of the host peptidoglycans during virus entry. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Note=Part of the capsid inner membrane."}
{"protein": "MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFSFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNIIGDTEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ", "text": "FUNCTION: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). SUBCELLULAR LOCATION: Membrane; Lipid-anchor."}
{"protein": "MDLSEPIHDFLLVFLGSGLILGGLGVVLLPNPIYSAFSLGLVLVCTSLFYILSNSYFVAAAQLLIYVGAINVLIIFAVMFMNGSEYYKDFHLWTVGDGITSMVCISLFISLITTISDTSWYGIIWTTRSNQIIEQDFLSNSQQIGIHLSTDFFLPFELISIILLDALIGAIAVARQ", "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": "MIQSLLTQFGEPLTRVENAITALQQGQGVLVVDDENRENEGDFVFSAEHLTTAQMAEMIREGSGIVCLCMGEERIKQLDLPQMVTHNTSQNNTAYTITIEAKEGVTTGVSAADRVTTIKAATADNAKPEDLSRPGHVFGLKAKTGGVLVRRGHTEASVDLMQLAGLKPFGVICELTNPDGSMARLPEVSGYANKHNMPVVSIEDLVQYIQIAQQKVS", "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": "MIIRAPIRTKTKSFRGDQMDFKFPSNESLPRGTLEEYHLNNHHLLNDVFAAENGVSRDEDGNSQTLSDYTSTSNTNTNSGYSSNGYYSFANISDNTTSSPRIVINQNETARLTSSDSNKSDFFASHDFPGNDSLHYSSSNVVKNQLHSMEAIPEGNITGSISTAFQTIPTADNVSYDIAPSSASSLLPRKSTSKSAILPSTQEAKPMTKLNMEKDIKTIELNNSVVPKPKKKLNRVPTIRRVESSRFSNSRYSSSVSSKSSSSRCSLKRSKAIRCKGGLLYYFTSLGIKIKKKLRKLRLVLRRRLFSYNVQKVPSATNSKTTKSKANINNKSKKRGTNLVNKNSNSTPRQKKSQRYVSNLQRSISSKSLVPVLAPQKKTKPLTVDTKFKANHPQSEDSKVGSNTPRSPLVSYTPSLRRTNSSIRRAASILTASATMTPANNKNSFISVPDNVSHAVTRNSSMYSRSRLVRSKPSTALNAIARQPSIVVENKVIPLSMNRYSIKEEDEYVIDTSSMRELSPVNSVCSSDYDRESSESYSNYADAMETTEVDNKDRVECNNEIQNVDANNEETSNEESYNLMKHYLSTVIAQRIMLRVQIARIQNYKSNVVYMNKSAETNSTIYEDLVDSLLTEYEADGSSSQIFDGVTVRADEEEEEDEDDEDDEEEEEENDDEEDEEDEEDDEDDEEEEEKRKEGEGRNLAKEVDELAELSPMRKQSDLSITLRSPFAMLNPAYSNSIISLPTGVVKRSLTLPVGMKI", "text": "SUBCELLULAR LOCATION: Bud neck. SIMILARITY: Belongs to the AIM44 family."}
{"protein": "MPTGTIILIVSIVIILIIAYVACLIVRKRNDNLLVALEERKEELFNLPVNEEVETVKALHLIGQSQVSFREWNQKWVDLSLNSFADIENHIFEAEGYNNAFRFVSAKNAIDSIDSQIDLIEEDIASIRQGLMELKEQEEKNSGRVKHALNLFDSLQEAVRENPDSYGETLSELEKQLKNIEVEFSEFVMLNSSGDPIEASEILDKTEEHMIALNQIMDRIPSLIERVTKDFPEQLEDLESGYRKLVEQNYLFTEANIESQFQNIRVSIRENTALIVSFDLDAAEAENEGIQAKIDHLYKVFNREIEANKEAVKISKNLPKFLEHVVQNTQLLDEESQRLNATYLLADSKLSRINQLKARLESIEIVVTESVEDIENPQVAYSILEERLDHSLASLKEIEEEQLVLADYLKSQELSENTARKKATLYINKLHTLKRYMEKRNLPGIPAEFLTNFFRTSDHVEALIAELDYKRINIEVVNRLLENATYDMNQLEELAYLIVQNATLTEQLLQYSNRYRSFDESVQKAFNRSLSIFEKDFDYQAAFEEISFALETVEPGVTERFVRSYEKTREAIRY", "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": "MSDTVERVKKIIVEHLGVNADKVVENASFIDDLGADSLDTVELVMAFEEEFGVEIPDEAAETIFTVGDAVKFIDKASA", "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": "MKAPIEVSPLAWLDAVEQQRRAAGLRRSLRPRPPVATELDLASNDYLGLSQHPDVIDGGVAALRMWGAGATGSRLVTGDTELHQQFESELADYVGAASGLLFSSGYAANLGAVVGLSGRGALVVSDAYSHASLVDACRLSRARVVVTPHRDVDAVRAALQDRDEERAVVITESVFSTDGALAPLRELHEVCRRHRALLIVDEAHGLGVRGGGRGLVFEAGLAGAPDVVMTTTLSKALGSQGGAVLGPAAVRAHLIDAARTFIFDTGLAPAAVGAARAALGVLRAEPWRSGAVLRHAGVLAEVCRVREAPQSAVVSVILGDPDVAVAAATACLDGGVRVGCFRPPTVPAGTSRLRLTARASLDDAELEVARRVLTDVLAGLG", "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": "MRLLFLLFILLVCLAQTTSGRKRNSKFRPCEKMGGICKSQKTHGCSILPAECKSRYKHCCRL", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MSLNAEQTATILAEFGRSEGDTGSTEVQVALLTAQINHLQGHFKEHKHDHHSRRGLLRMVNTRRKLLAYLKRTENVRYQELIKKLGLRR", "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": "MNLTSPKVSTMFFDQIITVTDHNVTWEKIQNCLYNLYGEATYNSWLSSLKFVSSRNGEVLLSVSTRFIKEWITVHYMKKILSLWQSEDKSIRSIDIQVIEERNSNFNVILKNREESNHNLGSPLDPRFTFDNFVVGKPNELAFTAAKRVAESIDPILGSNPLFLYGGVGLGKTHLMHAIAWHIVNSPSAKRKVVYLSAEKFMYQYITALRSKDIMLFKEQFRSVDVLMVDDVQFISGKDSTQEEFFHTFNALIDQNKQLVISADRSPSDLDGVEERIKSRLGWGLVADINETTFELRLGILQAKVEQMNMYVPKDVLEFLARNIKSNIRELEGALNKVTHTSLIGRSMTVESASETLIDLLRSNHRSVTIEEIQKKVAEFFNIKVADMQSNRRLRSLARPRQIAMYFAKKFTQKSLPDIGRNFGGRDHATVIHAVKQVENFIKTDSKFADEINRLKKMFK", "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": "MEEIKVHIGKTVALMNDNIDTDQIIPKSFLKRIERTGFGEFLFDSWRYLPNRKPNPDFPLNAPDRQEATILITGDNFGCGSSREHAAWALLDYRFRVIIAGSYSDIFYMNCTKNGVLPIVLPREAREKLAKIAADENVTIDLPNQQVISSVGTYPFEIDATWKNKFINGLDDIAITFEHIDAIKAYEQKVDSI", "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": "MSDFKTIQFVSVVIPVYNEQDSLSELLKRTIAACDSMGKQYEIVLVDDGSSDRSAEILREAAQRPGSRVVAVLLNRNYGQHSAIMAGFNHIKGDLVITLDADLQNPPEEIPRLVEAADQGYDVVGTIRQDRQDSWFRRRASRLINGLIQRTTGKSMSDYGCMLRAYRSSVIKAMLHCHERSTFIPILANSFARRTIEIPVKHAEREHGESKYGLMKLINLMYDLVTCLTTTPLRALSIFGSVVALLGFAFAVLLILMRLTLGPQWAAEGVFTLFAVLFIFIGAQFVGMGLLGEYIGRIYNDVRARPRYFIQNVVRANQPDEEQEK", "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": "MLDLKQYEVWFITGSQHLYGPETLEQVAKHSQIIAAGLDQSSTIPVRVVFKPVLKTPDEIYNLVLEANAAKNCIGLVAWMHTFSPAKMWIAGLRSLQKPLAHLHTQFNSEIPWSEIDMDFMNLNQAAHGDREFGFIVSRMRLERKVIVGHWQDSEVHDRIAAWTRAAAAWHDAQGARFARFGDNMREVAVTEGDKVNAQMRLGYSVSGYGVGDLVRFVNEVSDADIDSTLQEYAEQYELAAGLQAGGEQHHSLREAARIELGLRYFLEHGNFKGFTTTFEDLHGLVQLPGLGPQRLMDRGYGFAGEGDWKTAALVRAMKVMSAGLNGGTSFMEDYTYHFGSNGMKVLGAHMLEICPSIAATKPRLEVHPLGIGGKADPVRMVFDAKTGPAVNASIVEMGNRLRLINSVVDAVETDQPLPKLPVARALWLPQPDLKTAAAAWIYAGGAHHTGFSFDLTSEHLADFAEIAGMEYLQIDRNTNVQQFKQELRWNDLYYHLAKGL", "text": "FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. SIMILARITY: Belongs to the arabinose isomerase family."}
{"protein": "MEKIVICLMVIFLGTVAHKSSFQEQDLLLIRMRQLIDIVDQLKNYVNDLDPESLPAPEDVKRHCERSAFSCFQKVQLKAANTGGNEQIINVLTKQLKRKLPPTNAGRRQKHRPACPSCDSYEKAPPKEFLERLKSLIQKMIHQHLS", "text": "FUNCTION: Cytokine with immunoregulatory activity. May promote the transition between innate and adaptive immunity. Induces the production of IgG(1) and IgG(3) in B-cells. Implicated in the generation and maintenance of T follicular helper (Tfh) cells and the formation of germinal-centers. Together with IL6, control the early generation of Tfh cells and are critical for an effective antibody response to acute viral infection (By similarity). May play a role in proliferation and maturation of natural killer (NK) cells in synergy with IL15. May regulate proliferation of mature B- and T-cells in response to activating stimuli. In synergy with IL15 and IL18 stimulates interferon gamma production in T-cells and NK cells (By similarity). During T-cell mediated immune response may inhibit dendritic cells (DC) activation and maturation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-15/IL-21 family."}
{"protein": "MQPLEVGLVPAPAGEPRLTRWLRRGSGILAHLVALGFTIFLTALSRPGTSLFSWHPVFMALAFCLCMAEAILLFSPEHSLFFFCSRKARIRLHWAGQTLAILCAALGLGFIISSRTRSELPHLVSWHSWVGALTLLATAVQALCGLCLLCPRAARVSRVARLKLYHLTCGLVVYLMATVTVLLGMYSVWFQAQIKGAAWYLCLALPVYPALVIMHQISRSYLPRKKMEM", "text": "FUNCTION: Probable transmembrane reductase that may use ascorbate as an electron donor and transfer electrons across membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in another cellular compartment. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MTSKLEQLKQYTTVVADTGDFDAIARLKPVDATTNPSLLLKAAALPRYAEHLRQATAGSGGDAGLACDRFAVAVGKDILGVIPGRISTEVDARLSFDSEATLARAHRLIELYDEQGIDRERVLIKIASTWEGIRAAEILEREGIQTNLTLLFSFAQAVACADAGVFLISPFVGRIYDWYKKSENRDYAGAEDPGVQSVSRIYRYYKANGYKTVVMGASFRNLGQIEQLAGCDRLTISPDLLQQLADAQGELPRLLLPGEGEPRQVLDESAFRWQMNEDAMATEKLAEGIRLFARDQEKLEYQLATRH", "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. SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily."}
{"protein": "MEKFTVHTGVVAPLDRENVDTDAIIPKQFLKSIKRTGFGPNAFDEWRYLDHGEPGQDNSKRPLNPDFVLNQPRYQGASVLLARKNFGCGSSREHAPWALQQYGFRAIIAPSFADIFFNNCYKNGLLPIVLTEQQVDHLFNETVAFNGFQLTIDLDAQVVRAGDGREYPFEIAAFRKYCLLNGFDDIGLTLRHADKIRQFEAERLVKQPWLNTKLVG", "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": "MVISMKSEKPLVGIIMGSDSDLPVMKEAARILEEFGVPYEITIISAHRTPERAYEYAKKAEERGIEVIIAGAGGAAHLPGIIASLTVLPVIGVPIKSKALNGLDSLLSIVQMPSGIPVATVAIDNAKNAALLALRILGIKYPEIKEKLRRYMKDMKRKVEEKAKRLEEMGWERYLSE", "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": "MTAATRQEVLCLYRSIFRLARKWQAASGQMEDTIEEKQYILKEARTLFQKNKNLTDPELIKQCIVECTARIEIGLHYQIPYPRPIHLPPMGLTARRGRGLQTQEKLRKLSKPVYLKSHDEVS", "text": "FUNCTION: May promote cell proliferation and inhibition of apoptosis of preadipocytes. SIMILARITY: Belongs to the complex I LYR family."}
{"protein": "MKFSPALQSATLILRYKRFLADVVTPAGEHLTLHCPNTGAMTGCATPGDTVWYSTSENLKRKYAHTWEITETQQGAFICVNTQRANQLVKEAIATHTIPELTGYGSIKGEVKYGEEGSRIDFMLQADDRPECYIEVKSVTLADRDNGYFPDAVTLRGQKHLRELMSVAATGKRAVLLFAVLHSAIERFSPARHIDPKYAQLLNEAQKQGVEILAYKAELSADNMTLKSTLPVVL", "text": "SIMILARITY: Belongs to the SfsA family."}
{"protein": "MTDPFTNPDKTLDAQGLRCPEPVMMVRKTVRQMETGQTLLIIADDPATTRDIPGFCVFMEHELLAQETEQLPYRYLLRKG", "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": "MSFASEVKKELTQIAITDHEMKAELAALARMNGAISFGLGRGLTLDISTENASIARRIYSLLKRAYAVHLDLLVRKKMRLKKNNVYIVRVKQQADKILQDLGILGEGFTMIRSISDSILKDERRARAYLRGAFLAGGSLNNPATSSYHLEIFSLYEEHNAALRSLTNQFDLNAKAIERKKGHILYIKESEKISDFLKLVGATYSMLRFEDVRILKDMRNSVNRLVNCETANLNKTVGAALRQVENIKFLERTVGLDVLPDKLKEIAILRVTHQDVTLQELGEMVESGSISKSGINHRLRKIDQIADKIRNGESMTGAL", "text": "FUNCTION: Involved in cell division and chromosome segregation. SIMILARITY: Belongs to the WhiA family."}
{"protein": "MNATVPSAAPADLPAHRPATAVILAAGMGTRMKSDRPKVMHPLAGQPMLRYLLDNAASVFDRIVVVVGPGMEQVAALAAPHAVVVQQDRLGTAHAAAQAADLFGTGDVAVLYGDNPLITADSMRRMLACRAGEGNSEGAGLALMAMRPRDPGRYGRVVTQDGLVRRIVEWADASDEERAITLCNAGVLCAGAEDFRRWLGAVRNDNAQGEYYLGDVVAMAVAEGRQVRAVEAPEDELRGINSRAELAEAEACVQRRLRAAALDGGATLVAPETVFLAADTVLEPDVLVQPHVVFGPGVTVRRGAEIRAFSHLEGCVVGPGALIGPYARLRPGSDVGAAAHVGNFVELKATTLGAGAKANHLSYLGDATIGPATNIGAGTITCNYDGVFKHRTDIGAGCFVGSNAILVAPVSIGDGALVAAGSVITQDVLPDAMALGRARQTNKDGRGASLQAALRRKKEQG", "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": "MEINATTLWRDILAVRTKAPLVHNITNYVVMNSTANALLSIGASPVMAHAEEEVIDMVTIAGSLVINIGTLSKAWVAAMHKAMKKAHELQKPIVFDPVGAGATPYRTQTILELIHETPPSIIRGNSSEIKALVEAGIKTKGVDSTESSESAIEAAKHLSQKYGAVICISGATDHILNQEEYVRVENGHPMMTKVTGLGCTATAVVAAFAAINPSMMEATAHGMAAMGIAGEIAAKNVAGPGSLQVNFLDTLYSLSEADVHSHLKICA", "text": "FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ). SIMILARITY: Belongs to the Thz kinase family."}
{"protein": "MPRPEKVQLVAELTDRFASSTAAVLTEYRGLSVAQLNELRRALNGDAEYTVVKNTLSKLAVRNAGLTELEPLLQGPSAVAFVRGDPVKAAKSLRDFARANNALVIKGGILEGKLLSAAEVAALADLESREVLLAKVAGAANAVLARAAGLFQAPLAQVARLAEALRAKQAES", "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": "MFELLGTTLPSRLLLGTAQYPSPAILADAVKASGTSVVTVSLRREMAGGRAGEKFWSLIRSLGVRILPNTAGCHSVKEAVTTAKMARDVFGTSWIKLEVIGSHDTLQPDVFGLVEGARILCEDGFSVFPYTTDDLVVAERLLEAGCRVLMPWCAPIGSALGPVNMTALRSMRGHFPDVPLIVDAGLGRPSHAATVMELGFDAVLLNTAVARAADPVGMARAFGKAVDAGREAFSSGLLEPREVAVPSTPIFGRAVFS", "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": "MSFRDVLERGDEFLEAYPRRSPLWRFLSYSTSLLTFGVSKLLLFTCYNVKLNGFEKLETALERSKRENRGLMTVMNHMSMVDDPLVWATLPYKLFTSLDNIRWSLGAHNICFQNKFLANFFSLGQVLSTERFGVGPFQGSIDASIRLLSPDDTLDLEWTPHSEVSSSLKKAYSPPIIRSKPSWVHVYPEGFVLQLYPPFENSMRYFKWGITRMILEATKPPIVVPIFATGFEKIASEAVTDSMFRQILPRNFGSEINVTIGDPLNDDLIDRYRKEWTHLVEKYYDPKNPNDLSDELKYGKEAQDLRSRLAAELRAHVAEIRNEVRKLPREDPRFKSPSWWKRFNTTEGKSDPDVKVIGENWAIRRMQKFLPPEGKPKGKDD", "text": "FUNCTION: Acyltransferase required to remodel newly synthesized phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]- glycerol or CL), a key component of the mitochondrial inner membrane, with tissue specific acyl chains necessary for adequate mitochondrial function (PubMed:14651618, PubMed:28202545, PubMed:29091407). Its role in cellular physiology is to improve mitochondrial performance (By similarity). CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms (PubMed:16135531). Catalyzes the transacylacion between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2- diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor (By similarity). CoA-independent, it can reshuffle molecular species within a single phospholipid class (PubMed:15588229). Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization (By similarity). Required for the initiation of mitophagy (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Intermembrane side Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Note=Imported into mitochondria by the TOM complex and is first imported into the mitochondrion outer membrane in a TIM9-TIM10-dependent manner followed by insertion into the mitochondrion inner membrane. SIMILARITY: Belongs to the taffazin family."}
{"protein": "MATTTATTPPSLTDIRALKYTSSTVSVASPAEIEAITKTWAETFKIPNDVLPLACWDLARAFADVGASSKSELTGDSAALAGVSRKQLAQAIKIHCTIRQFCMYFANVVWNIMLDTKTPPASWSKLGYKEESKFAGFDFFDGVNHPAALMPADGLIRGPSEAELLAHQTAKQVALHRDAKRRGTNVVNSVEITNGRSDPIGPLITYPQ", "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": "MKEQLNQLSAYQPGLSPRALKEKYGIEGDLYKLASNENLYGPSPKVKEAISAHLDELYYYPETGSPTLKAAISKHLNVDQSRILFGAGLDEVILMISRAVLTPGDTIVTSEATFGQYYHNAIVESANVIQVPLKDGGFDLDGILKEVNDDTSLVWLCNPNNPTGTYFNHESLDSFLSQVPSHVPVLIDEAYFEFVTAEDYPDTLALQQKYDNAFLLRTFSKAYGLAGLRVGYVVASEHAIEKWNIIRPPFNVTRISEYAAVAALEDQQYLKEVTHKNSVERERFYQLPQSEHFLPSQTNFIFVKTKRVNELYEALLNVGCITRPFPTGVRITIGFKEQNGKMLEVLSNFKYE", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
{"protein": "MKGIRLCGSGAAVPRLRISNDDLSGRVETSDEWIRTRTGIAARRVADESESLTSLAAAAGKQALERAGWDASSVDLILLATSSPDDLFGSAPKVQALIGAGSAVAFDLTAACSGFLFSLVTAAQYLRTGAMTRALVIGADQLSRWVDWDDRRSCVLFGDGAGAVAIEACPAENDGLLGFRLNSDGARGDCLTLAQTSERAELLPGMSHQRGGYAPIGMNGQEVYKFAVREVPAILKQLLADTNTEPASIDWLLLHQANQRILDAAAERLGIAADKVLSNLANYGNTSAGTIPLMLHEAVSDGRIQSGQLIASSGFGAGLSWGAALLRWDGPTS", "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": "MLQLCSTFRPQLLLPCQFRFTNGVLIPQINYVASNSVVNIRPMIRCQRASGGRGGANRSKPAKPQVKEGSNKTVIEGLVTESLPNGMFRVDLENGDNILGYICGKIRKNFIRILPGDKVKVEMSVYDSTKGRIIFRMSSRD", "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": "MGEFSTLLQQGNAWFFIPSAILLGVLHGLEPGHSKTMMAAFIIAIKGTIKQAVMLGLAATLSHTAVVWLIALGGMYVSRAFTAESVEPWLQLVSAIIILSTAFWMFWRTWKGERDGLANRLPAHTHHHHDHEHHHHDHDHDHHHDHQHVHISLKGLTDGSHAWQDAHERAHATDIQRRFHDREVTNGQILLFGLTGGLIPCPAAITVLLICIQLKAFTLGATMVLCFSIGLALTLVAVGVGAAISVQQAAKRWSGFNTLARKAPYFSSILIGLVGLYMGMHGYLGIIR", "text": "FUNCTION: Efflux system for nickel and cobalt. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family. RcnA subfamily."}
{"protein": "MIKETDLENIPDLLIKFNEPLSNYTYTKVGGPADILAFPATIEALTELSAKAKATDTPVTVLGNASNLIVRDGGIRGVVILLEKLDSVKVAGYTIEAQAGAKLKEVTQVAQANSLTGFEFACGIPGSIGGAVFMNAGAYGGEIYQVLVSCKVMDAAGNVSVLSASEMQFGYRHSVIRDKNLIVLSAKFELQAGDPTQIQNEMDRLNFLRESKQPLEYPSCGSVFKRPVGHFAGQLIQEAKLQGQRIGGVEVSKKHAGFMVNVADGNATDYEKLIALVIEKVKENSGVTLEPEVRIIGEK", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
{"protein": "MSSSNFSCILSISLTFFILLLNKVNSAETTSFSITKFVPDQKNLIFQGDAKTASTGKLELSKAVKNSIGRALYSAPIHIWDSKTGSVANFQTTFTFTITAPNTYNVADGLAFFIAPIDTKPKSIHHGGYLGVFDSKTYKKSIQTVAVEIDTFYNAQWDPNPGNISSTGRHIGIDVNSIKSISTVPWSLENNKKANVAIGFNGATNVLSVDVEYPLIRHYTLSHVVPLKDVVPEWVRIGFSSSTGAEYSAHDILSWSFDSKLNLGFENNINANVSSSTQAA", "text": "SIMILARITY: Belongs to the leguminous lectin family."}
{"protein": "MSRLWVTGYRSYELSIFSDQDPKLKVIQNALKRKLIEKVESGTTWIIAGPQLGTEQWSLELANELKMDYPELQTALMFPFSDFGKQWKEEKVEKLALIKAKVDFFANVSENPYQNPQQLRNYQNFMLNHTDEALLLYDDEHEGKTKFDLNAIRSFQEHNSYNVETIDFYDLEEESMLYEEKDE", "text": "SIMILARITY: Belongs to the UPF0398 family."}
{"protein": "MLDKTRLRIAMQKSGRLSDDSRELLARCGIKINLQQQRLIAFAENMPIDILRVRDDDIPGLVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYFTLRRLDFGGCRLSLAMPLDEDYTGPECLQNKRIATSYPHLLKQYLDRKSVSFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRDGEMPAEKQQLIDKLLTRMQGVIQARESKYIMLHAPSERLEEVISLLPGAERPTILPLAGDQSRVAMHMVSSETLFWETMEKLKSLGASSILVLPIEKMME", "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": "MSIRLQEAGLRHGQVQALNNVDLQIGKGERVAIIGPSGAGKSSLLHLMATAVRPSAGQLDLLGEQPWLLTSGARQRLRARVGLVHQAPPLPPRQRVVTAVLAGRLGQWGTLRGLLNLIHPSDVPGAREVLAELGMVDKLFVQCGQLSGGQLQRVGIARALYQQPEVLLTDEPVSAMDPVLADHSLALLNRHAQAHGVTLVASLHAVELALAHFPRIIGIRAGEVAFDCPAEAVTPTMLDALYANEQLGSPVVPTATVLVQIPRC", "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": "MEKAIQRQRVLLEHLQPIRHHTHDHSSSLTTSICAAGDSAAYQRTAAFGDDVVIVAAYRTAICKSKRGGFKDTLSDDLLAPVLKAVIEKTNLDPKEVGDIVVGTVLAPGSIRAMECRMAAFYAGFPETVPIRTVNRQCSSGLQAVADVAASIKAGFYDIGIGAGLELMTVDNIGRVQQRNTKVDTFAQARDCLLPMGITSENVAQRFGVTRLEQDQAAVNSHQRAAAATASGKFKDEIIPVLTKIVDPQTGKEKPVVISVDDGIRPNTNLTSLGKLKPAFKNDGTTTAGNASQVSDGAAAVLLMKRSVAMKKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPPAVKSAGLDLDDIDLYEINEAFASQFVYCQKKLNLDPEKVNVNGGAMALGHPLGATGARCVATLLHEMKRRGKDCRFGVISMCIGSGMGAAAVFERGDAVDDLCNARVSNNNSFLSKDAK", "text": "FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway (PubMed:19659733). Thiolase that catalyzes the conversion of 3-oxo-3-phenylpropionyl-CoA (benzoylacetyl-CoA) to benzoyl-CoA (PubMed:19659733). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MRVDIVPVGDVPAHVKRQASSSLRSVYDCEVVVASEQDVPTAAYDEARSQYRAAEFIDTATRATSGDKTIAITPHDLFYRRRNYVFGLAYLDGRGCVVSTYRLQTSSDGGFSNRSSSDVFDDRVRKEVVHELGHTLGLEHCDNNRCAMNFSPTVREVDRKEENLCGSCQRTVF", "text": "FUNCTION: Probable zinc metalloprotease whose natural substrate is unknown. SIMILARITY: Belongs to the peptidase M54 family."}
{"protein": "MAVSVKICGLTEAAGLAAAVDAGARYVGFVFFPKSPRHVTPGTAAELAAQVPLGVAKVGLFVNPDDAALDAVLAHVPLDVIQLHGAETPARVAEVKARTGLPVMKAVGVADPQDLDALWDYGLVADMLLIDAKPPKDAVLPGGNGLAFDWRLLAGRQILKPWLLAGGLTPENVHEAIRLTRAPGVDVSSGVESAPGVKDPDRIRSFIARATAPIL", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MIENQVPFYLLIFLVGIGLGVLTFWAYHRFALGGFKRISKDIISRAEQETSELRKTNELSLKQKQVEYQRELEQMWQQERKKLQQEEERLKQREDKLESRMNLVEKKLSDTEKREAILIGRKAQLDEEKKQTIESHSKLLSILEKASGLTSSEAKEILLSRLSNEVKTESANLIRRIRKEAEEEAEKIASTIIATSINRLAVSCASESTVCTVTIPNEDMKGRIIGREGRNIRALERETGVNFIIDDTPGAVVLSGFDPVRKHIAKMALTELVQDGRIHPTRIEEVVEKATINVHKQIKQYGEDAALRAGAMNLHPDLINLLGKLKFRFSYGQNVLDHSLEVSHLMGLMAAELGLDIRLAKRIGLLHDLGKAVTHEIEGSHAIIGHDLALKLGENKEVANGIGCHHHEMAPLTIEADLCSAADAISASREGARIEAVEEYIKRLRKLEEIALEFAGVDKAYAMQAGREIRIVVLPDQVDDAGVVNLARDLTKRIEQELSYPGKIKVTVIREKRVVEYAV", "text": "FUNCTION: Endoribonuclease that initiates mRNA decay. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RNase Y family."}
{"protein": "MKYSQNKSLNTFEIEYKIANKAVQIKSSGKMGVITKELKLKESVIQANNTYYLKNHGDSRIIIGTMKQQIQGVLAGFCIELKLVGLGYVVHKVGNTLVLDVGYSHYRSCVIPVDVVVKLEGSQIILYSINKEKVTTFASLLKTFKKVNMYKGTGILGINQIIKLKKGKVR", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL6 family."}
{"protein": "MSRIGRLPISVPAGVEVSVDGSAVSVKGPKGTLTHTVSAPITVVVEDGTVQVSRPNDERESRSLHGLTRSLIANMIQGVSEGYTKQLEIVGTGYRVQAKGADLEFALGYSHPVPFSAPDGITLSVEGNNKVTVSGIDKQQVGQVAAKIRSLRLPDPYKGKGVRYAGEQIRRKAGKAGK", "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": "MRIALGIEYDGSGYFGWQRQAEVDSVQGQLEQALSKVANEPISLFCAGRTDAGVHATGQVVHFETNAIRNEGAWTLGVNANLPDNIAVRWAKEVDDSFHARFSATARRYRYVIYNHNFRPGILRHGVSHYHGDIDADKMHVAAQALLGEQDFTSFRAIQCQSKTPFRNVHSVKVTRQGMYVIVDISANAFLHHMVRNIVGSLLEIGLGNQPLTWMADLLALKDRNQAAATAKPNGLYLVDVTYPEQYQLPKLALGPLFMLD", "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": "MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLILYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFRHLGLEYLPPEQRNA", "text": "FUNCTION: Gap-filling polymerase involved in repair of DNA double- strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA polymerase type-X family."}
{"protein": "MYYSNGNYEAFARPKKPEGVDNKSAYLVGSGLASLAAASFLIRDGQMKGENIHILEELDLPGGSLDGILNPERGYIMRGGREMENHFECLWDLFRSVPSLEVEDASVLDEFYWLNKEDPNYSKCRVIENRGQRLESDGKMTLTKKANKEIIQLCLMKEEQLNDVKISDVFSKDFLDSNFWIYWKTMFAFEPWHSAMEMRRYLMRFIHHIGGLADFSALKFTKFNQFESLVMPLIEHLKAKNVTFEYGVTVKNIQVECSKESKVAKAIDIVRRGNEESIPLTENDLVFVTNGSITESTTYGDNDTPAPPTSKPGGAWQLWENLSTQCEEFGNPAKFYKDLPEKSWFVSATATTNNKEVIDYIQKICKRDPLSGRTVTGGIVTVDDSNWQLSFTLNRQQQFKNQPDDQVSVWIYALYSDERGERTNKTIVECSGKEICEEWLYHMGVPEEKISALAAECNTIPSYMPYITAYFMPRKEGDRPLVVPHGSKNIAFIGNFAETERDTVFTTEYSVRTAMEAVYKLLEVDRGVPEVFASVYDVRILLHALSVLNDGKKLDEIDMPFYERLVEKRLLKKASGTFIEELLEEANLI", "text": "FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. Cannot catalyze the reverse reaction. Is not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis- 8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of unsaturated fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy fatty acids. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments. SIMILARITY: Belongs to the oleate hydratase family."}
{"protein": "MIKVLVIADTHGQNQRWIELKNYHNPDVIIHAGDHMTTKQFMDQNATFWVAGNNDSIGNEIEIFQLGQINFVLMHGHQAPRDNLKKWYQLLVLKAQQYPCDVLIFGHSHIEYTNKINMIQLINPGSLQLPRNQTNTPSYCTFIVNKDELTDLTIHYYQASKVS", "text": "SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE family."}
{"protein": "MPTINQLVRKGRRDKVAKTKTAALKGSPQRRGVCTRVYTTTPKKPNSALRKVARVRLTSQVEVTAYIPGEGHNLQEHSMVLVRGGRVKDLPGVRYKIIRGSLDTQGVKNRKQARSRYGAKKEKS", "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": "MAPGSRGERSSFRSRRGPGVPSPQPDVTMLSRLLKEHQAKQNERKELQEKRRREAITAATCLTEALVDHLNVGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQLQSAPS", "text": "FUNCTION: May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5F1A and NDUFA9. FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension (PubMed:17182842). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). FUNCTION: May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5F1A and NDUFA9. FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. The BORC complex is most probably associated with the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. SUBCELLULAR LOCATION: Mitochondrion intermembrane space Mitochondrion matrix Cytoplasm, cytosol Lysosome membrane. SUBCELLULAR LOCATION: Mitochondrion intermembrane space Mitochondrion matrix Cytoplasm, cytosol Lysosome membrane. SIMILARITY: Belongs to the BLOC1S1 family."}
{"protein": "METFPSVGSPGLWAGFIAFVIAMLALDLGVFHRKAHVVKFKEALGWSALWVSLALVFGAGVWWKFGPEPGLQFITGYLIEKSLSVDNIFVFVVIFSALRIPALYQHRVLFWGILSALALRAIMIFAGVAMLARFHWLIYVFGGFLIITGVKLFLQRNKEDNPEEGALMRLARRTIPSTPNFDGHHFFTVENGRKLATPLLMALLLVEASDILFALDSIPAIFAVTTDPFIVFTSNIFAILGLRSMFFMLAGAVEKFSYLKVGLSAVLVFVGTKMAIIDFVKMPPEVSLSVIAGLLGASIVASLIKSRHAPTSDADAPKV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TerC family."}
{"protein": "MNARENAIVQKYALSFVEKVSDHADIWDMYDQISDLISIIHDSKLNRILLSATVSREEKADFVRTVRQSSFWQINDLIEDVIRDGHADLLLETLERVQLQISKFKNEFEARVVSVYPLTEAQKERLRHLVEQRFSLRVRNITEELDQSLLGGFIVTVNHKVIDASVRTQLKDIRKKL", "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": "MQNSEGGADSPASVALRPSAAAPPVPASPQRVLVQAASSAPKGAQMQPISLPRVQQVPQQVQPVQHVYPAQVQYAEGGDAVYTNGAIRTAYTYNPEPQMYAPSSAASYFEAPGGAQVTVAASSPPAVPSHSMVGITMDVGGSPIVSSTGAYLIHGGMDSTRHSLAHTSRSSPATLEMAIENLQKSEGITSHKSGLLNSHLQWLLDNYETAEGVSLPRSSLYNHYLRHCQEHKLDPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGIRLKPDSPLNRLQEDTQYMAMRQQPMHQKPRYRPAQKTDSLGDSSSHSGLHSTPEQTTAAQNQHHQQYIDVSHVFPEFPAPDLGSVLLQDGVTLHDVKALQLVYRRHCEATVDVVMNLQFHYIEKLWLSFWNSKASSSDGPTSLPASDEDPEGAVLPKDKLISLCQCDPILRWMRSCDHILYQALVEILIPDVLRPVPSTLTQAIRNFAKSLEGWLTNAMSDFPQQVIQTKVGVVSAFAQTLRRYTSLNHLAQAARAVLQNTSQINQMLSDLNRVDFANVQEQASWVCQCEESVVQRLEQDFKLTLQQQSSLDQWASWLDSVVTQVLKQHAGSPSFPKAARQFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMFYLVEHRVAEATGETPIAVMGERLSQNVTSALWPGSEPGSSPGELCSSAWLATLC", "text": "FUNCTION: Transcription factor that acts as a key regulator of spermatogenesis. Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function. Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters. Probably activates transcription of the testis-specific histone gene H1-6. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly expressed in the nucleus and at lower level in cytoplasm. SIMILARITY: Belongs to the RFX family."}
{"protein": "MTASPSKLAQLRELSVVVADTGDYDAIKRLQPVDCTTNPTLVKKALDLPVYADLLERELTWGRAHGGDDRTTTVDEVADRLTIGVGVKLSALVPGRVSTEVDADLAHDTQATIAKARKFVAMYAERGVPKDKILIKIAATWEGIEAARQLQLEGIDCNLTLIFNRAQALACAEANVFLISPFVGRILDYYVAQGQTPASIDEDPGVVFVRTVYNAFKQRGSSTVVMGASFRSTAQIEALAGCDRLTISPDLLEKLDAEHGELPRKLSPGNANNAQITPIDSDSFASGLAADPMATEKLASGIDTFAKDLHALRKTIADKLAG", "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": "MAKSAQGRTKEPTPMMRQYLEVKERYPGYLLLFRVGDFYETFLDDAVTVSSALNIVLTRRSNGGAGEIPLAGFPHHASEGYIAKLVTKGFKVAVCDQVEDPALAKGIVKREITDIVTPGITYSDKILDDRHNNYLCAVAPVKRGREHMAGVAFVDVTTAEFRMTELPLGELKDFLQSLRPSEILISSRDKELRESLAKSLFSGALFTTLDEWMFTEEQAARVLENHFKTHSLKGFGIEGYEAGRIAAGVILQYLEEAKQGSLKYLVRIGLVESGETMTLDIQTCRNLEIISSMQDGSLNGSLLEVIDRTKNPMGARLLRRWLLHPLRKLEPVVRRHDAVGELLDAPEMREGIRGMLGGIIDLERALARIATSRAMPREVRQLGSSLAMIPQLKSLLEGSKSLRLRELALRLDPLPELAETIEKALDAEASGTLRDGGYIRAGYHAELDELRAISSGARDRLLEIQQQERQRTSISTLKVQYNKVFGYYIEVSRANSDKVPEYYEKKQTLVNAERYTIPALKEYEEKILTAEEKSQLLEHQLFQELCAMIAEQAASIQTTAAALAELDCLACFASCADEFGYCRPVMNEGTELSIRAGRHPVLERILGADEPYVANDCQVGSEQQLLIITGPNMAGKSSYLRQVGLVVLLAQVGCFVPAESAEIGLVDRIFTRVGASDNLTSGESTFLVEMNEAASILNNATERSLLLLDEIGRGTSTFDGMSIAWSMCEYIHDQLRSRTLFATHYHELAELESRFERIVNFNATVVETADTVIFLRKIVRGASDNSYGIEVAKMAGMPPEVIERAREILAGMERREVEVPVQRQALPLRVESRQISLFEEEESRLRKALSGIDINRLTPLDALMELKRLQEIALGKGA", "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": "MNKITLPIGMHDKLFKRARVTYEIERDISDFLMAQGFNRIDTPTLEHFEVFSDHVEPHHYHLFDKKGELLVLRPDVTSQIGRVIASTRVHTPTKFSYSGKVFHYQEELRGLANELSQAGIEIIGYPAREAVLEAIKTAKQSLDLAQVKSYQFEFSHAAILQTILESLVLDSQEEAQLLDYIRKKNRTGIFEFTQSRPSEFDDFLQELPYLFGPSQQVLARAREIVDNERILTALDDVEQVLRSLSDLLDQTTMDLGQVATMPYYTGLTFKVFGDRVPDAFLSGGRYDQLFKRFGATELTAIGWSLDIDSVYQAIHDDLPDEGGKEGDGR", "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": "MSNSSPETVSQPSQEVKYGEREIAEGQLITFPNPRVGRRYDINITLPEFTCKCPFSGYPDFATIYITYVPDERVVELKALKLYINSYRDRYISHEESANQILDDFVAACDPLEANVKADFTPRGNVHTVVEVRHTK", "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": "MMRYALGVEYDGSEFLGWQQLGEMGPSVQATLQQALASVADSSVRVVCAGRTDAGVHGQCQVVHFDSAVTRPPRAWILGTTTRLPSSVAVRWCVPTSEDFHARFSACARRYRYRLLNRQVRPALQHQFLSWERHPLDAQAMHVAAQMLLGENDFSAFRSAQCQALHARRELQAISVRRDAEVIEICVQANAFLHHMVRNIVGSLLMVGTGERPMEWIAELLAGRDRTMAGPTASARGLVFVGPLYPEKWHLPMEVSV", "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": "MSDDPEDRMLGWDESVFRDEHVFEIDWLPETFKHRDTQMETLKYALRPAVRGSRPLNVIARGPPGTGKTTAVQILFDELTAQTDVKTVRVNCQMDSTRYAVFSRLFAEIFDYEPPSSGISFKKLFSQITDKLVEEDEVLVVALDDVNYLFYESEASDTLYSLLRAHEAHSGAKIGVICVSSDLELDTIDALDTRVQSVFRPEEVYFNPYGQAEIADILGERADRGFNEGVVGPTVLDRVAELTEEQGGDLRVGIDLLRRAGMNAEMRASRSVETEDVEAAYDKSKYVHLSRRLRELSDSETALVEVIAAHDGQQAGDIYDAFSEQTDLGYTRYSEIINKLDQLDIIDADYTNVEGRGRSRELTLNYDADAVLERL", "text": "FUNCTION: Involved in regulation of DNA replication. SIMILARITY: Belongs to the CDC6/cdc18 family."}
{"protein": "MPEVADTCSLASPASVCRTQHLHLRCSVDFARRALTGTAALTVQSQEDNLRSLTLDTKDLTIEKVVINGQEVKYTLGESQGYKGSPMEISLPIALSKNQEVVIEISFETSPKSSALQWLTPEQTSGKQHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGEAPDPEDPSRKIYRFNQRVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFHALGGWGELQNTIKTFGESHPFTKLVVDLKDVDPDVAYSSIPYEKGFALLFYLEQLLGGPEVFLGFLKAYVEKFSYQSVTTDDWKSFLYAHFKDKVDLLNQVDWNAWLYAPGLPPVKPNYDVTLTNACIALSQRWVTAKEEDLNSFSIEDLKDLSSHQLNEFLAQVLQKAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEEAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKACMHPVTAMLVGKDLKVD", "text": "FUNCTION: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities (By similarity). Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro- inflammatory mediator leukotriene B4 (LTB4) (PubMed:1544505). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides. In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "MPRITQEISYNCDYGDNTFNLAIDIGGTLAKVVFSPIHSNRLMFYTIETEKIDKFMELLHSIIKEHNNGCYRMTHIIATGGGAFKFYDLLYENFPQIKGISRFEEMEGLIHGLDFFIHEIPDEVFTYNDQDGERIIPTSSGTMDSKAIYPYLLVNIGSGVSILKVTEPNNFSRVGGSSLGGGTLWGLLSLITGAQTYDQMLDWAQEGDNSSVDMLVGDIYGTDYNKIGLKSSAIASSFGKVFQNRMTSNKSLENNENKLYSSHESIEKNNGQMFKNPDICKSLLFAISNNIGQIAYLQAKINNIQNIYFGGSYTRGHLTTMNTLSYAINFWSQGSKQAFFLKHEGYLGAMGAFLSASRHSSTKKTST", "text": "FUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the type II pantothenate kinase family."}
{"protein": "MSKIIGIDLGTTNSCVAVLEGGEPKVIPNPEGNRTTPSVVAFKNGERLVGEVAKRQAITNPNTIISIKRHMGTDYKVEIEGKKYTPQEISAIILQYLKSYAEDYLGEPVTRAVITVPAYFNDAQRQATKDAGRIAGLEVERIINEPTAAALAYGLDKEEDQTILVYDLGGGTFDVSILELGDGVFEVKATAGDNHLGGDDFDQVIIDYLVEQFKQEHGIDLSKDKMALQRLKDAAEKAKKELSGVTQTQISLPFISANETGPLHLETTLTRAKFEELSAHLVERTMGPVRQALQDAGLTPSDIDKVILVGGSTRIPAVQEAIKRELGKEPHKGVNPDEVVAIGAAIQGGVIAGEVKDVVLLDVTPLSLGIETMGGVFTKLIERNTTIPTSKSQIFTTAADNQTTVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDANGIVHVRAKDLGTNKEQSITIKSSSGLSEEEIQRMIKEAEENAEADRKRKEAAELRNEADQLVFTTEKTLKEVEGKVDEAEVKKAQEAKDALKAALEKNDIDDIRKKKEALQEIVQQLSIKLYEQAAKQAQAQQQAGAGGAAKKDENVVDAEFEEVKDDK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MSCLPALDKFLQNYHQAYLTSLGELPRYYPQGEASVCIQGEFHADLDQAVSWQPVKREVEGSFANVEHALELTLWPEINHFYGQYFSAPLLFDSEWGTGELLQVWNEDDFTCLQQNLIGHLMMKKKLKQPPTWFIGLLDEGDKMLTINNSDGSVWIELPGEIPTQQLSPSLAEFIGALSPRIAPPVKHEELPMPALEHPGIFASFKRMWQNLFGKR", "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": "MTSTRGEAAGIPSVSLNDGHSIPVLGLGVGELSESEAERSVAAALEAGYRLIDTAAVYGNEAAVGRAVNASGIPREEIYVTTKLAVADQGFGTSQDAARASLERLGLDYVDLYLIHWPAGDHGKYIDSWGGLMKAKQDGVARSIGVCNFNAEHLSNIIDLSFFTPAINQIELHPLLNQAELREVNAGYGIVTEAYGPLGVGRLLDHAAVTGVAQAHDKTPAQVLLRWSIQLGNVVIARSANPDRITSNLEVFDFELTDDEMATLNGLDEGTRFRPDPETYTGP", "text": "SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MQENLKNDKLKIGKYEFDSRFILGSGKYSLELIKSAIEEAKAQIITLALRRANTGEIANILDYIPKNITLLPNTSGARNADEALRIARLSRELGCGELIKIEVISDSRYLLPDNYETIKACELLAKEGFTPLPYMHADLYAARAMRDAGAAAIMPLAAPIGSNKGLCAKEFIQILLNEIDLPIIVDAGIGSPSQACEAMQMGVSAVMVNTAIAEAKDIALMARAFSLAVNAGRVAFLAGVASVSEAKASSPLTGFLRD", "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": "MKILLDLLLLLPLLIVCCLESFVKLFIPKRRKSVAGEIVLITGAGHGIGRLTAYEFAKLKSKLVLWDINKHGLEETAAKCKGLGAKVYTFVVDCSNREDIYSSAKKVKAEIGDVSILVNNAGVVYTSDLFATQDAQIEKTFEVNILAHFWTTKAFLPAMMKNNHGHVVTVASAAGHISVPFLLAYCSSKFSAVGFHKALTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPALEPEEVVNRLMNGILTEQKMIFSPSSIAFLTILERILPERFLAVLKRKINIKFDAVIGYKMKAQ", "text": "FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A- dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet Note=Redistributed from the endoplasmic reticulum to lipids droplets in the cell upon induction of lipids droplet formation. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily."}
{"protein": "MAEFVRAQIFGTTFEITSRYTDLQPVGMGAFGLVCSAKDQLTSQAVAVKKIMKPFSTPVLSKRTYRELKLLKHLRHENIICLSDIFISPLEDMYVVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIATICSENTLRFVQSLPKRERQPLKNKFKNADPQAIELLERMLVFDPRKRVKAGEALADPYLAPYHDPTDEPEAQEKFDWSFNDADLPVDTWKIMMYSEILDFHNVDANAEQAAHNNDTVAG", "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. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily."}
{"protein": "MGLGFLRLALPLLMVAASAPAVAIPRLDLSGYPAPKQGLKRWVIQPSGLLPKSDDALISPHPLDWRVQLIVGKEVEMDCNVKRLSGPSLSMQRLPQASGKALFEVSGPVLVLSTRMACNSEQAKGKSFLSLGKQPYLIPYNASWPVVVDLPDGVELRWRVWKAETRQQEAVRL", "text": "SIMILARITY: Belongs to the protease inhibitor I11 (ecotin) family."}
{"protein": "MARHPRWTLSQVTELFEKPLLELLFEAQQIHRQHFDPQQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLDSARKAKNAGSTRFCMGAAWKNPHERDMPYLEQIVQGVKAMGLETCMTLGMLNESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVREAGIKVCSGGIVGLGETVTDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPAEDKDLQLFRKLGLNPQQTRVLAGDNEQQQRLEQTLMTPDTDDYYNAAAL", "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": "MSHLVKMENGQSQTIQEMLGCIERYNPDHLKILESYVQDQAKNNSYDLEANLAVLKLYQFNPHMLNFDITYTILLKSLTNLPHTDFVMAKCLLLPQQMKDENVQTIIDLADILERADFTLFWQRAEVNRTMFRHIAGFHDSIRKFVSHVVGTTFQTIKKDLLKELLGGIEDSTLESWIKRNGWKHQGHDLVVVATQDDKIKTKNITEKIEFENVGALMAQCL", "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": "MQFDVITLFPEMFRALTDWGITSRAAKQQRYALRSWNPRDFTVDNYRTIDDRPYGGGPGMVMLAKPLDDAIDAAVAAQAQAGVAKPHVVLMSPQGKTLTHAKVMELARRPGLVLLCGRYEAIDQRLIDRRVDEEISLGDFVLSGGELPAMALIDAVVRHLPGVLGDAQSAVQDSFVNGLLDCPHYTRPEEYEGVRVPDILLGGHHAEIEKWRRQQALANTASKRPDLIEAAREQGLLTRADEKFLSEWAAKAGRGETPAR", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
{"protein": "MRWIEEELKRIKEANLYRERILLEGVKDFCSNDYLGLRKHPEVVEESIRVLKEAGLGSGASQLVSGYTKHHRELEEKLAEFKGTESCVLFGSGFLANVGTIPALVEEGDLVLSDELNHASIIDGVRLSKAQKRVFKHKDYEELEEFLKKNRKKFRRVLIITDTVFSMDGDVADLKRLTQICEEYDCMLYIDEAHTTGTIGKGGLDYFGIEHKEYIIVMGTLSKALGSYGAFVCGTKLLIDYLVNKARSLIFSTSLPPSVCAGAKKAIEIIEENPKLIEFLRKKEKEILEILEQFSLDYKYYSTPIIPIMVYDEKETVRIKEELLKEGVFIQAIRYPTVPKGKARLRLTASLNYTRKDLEFLKNALEKVLKGRA", "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": "VEQNWATLQGGEMTIQTTQASEATQAVASLAEAAVAASQEMQQGATVTMALN", "text": "FUNCTION: Transcription factor that activates the expression of the EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key metabolic genes to cellular growth and development. Implicated in the control of nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NRF1/Ewg family."}
{"protein": "MKIMITISENSEAKELMPIAQAVHILVNKLPVAMRSKNKPGVRLEKGEVVDTNYEGYVLKVAIEKGEVVRATPIIGPYAGLPVIVAPIKDGDNVLGAIGVVDITAGIFEDIVAISRRPELYKFLPEDAFPK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MPHSDELDSRDVLSVSGLNIAFHHEGQQVDAVRNVSLRLKRGETLAIVGESGSGKSVTALALMRLIEQSGANVRCGEMLLRRRNRQVIELSEQSDAQMRRVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQRASHEEALAEAKRMLDQVRIPESQAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQEMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPTHPYTQTLLAAVPQLGAMRGHSLPRRFPLISADEPALYESQIEQDTVVEGEPILQVRGLVTRFPLRSGLFNRVTREVHAVENISFDLWPGETLSLVGESGSGKSTTGRALLRLVESRQGEIIFNGQRIDTLSAGKLQPLRRDIQCIFQDPYASLDPRQTVGYSIMEPLRIHGLGQGDAAAKRVAWLLERVGLRPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSVRGQIINLLLDLQREMGIAYLFISHDMAVVERISHRVAVMYLGQIVEMGPRRAVFENPQHPYTRKLMAAVPVADPSRHRPRRVLLSDDIPSNIHKRGEETPAVSLQLVGPGHYVARPLQDNALSRL", "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": "MSPQTETKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAQEGNEIIREACKWSPELAAACEVWKEIVFNFAAVDVLDK", "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": "MAKGYYVKFETPKDLVNPILEALRAATQSGKVKKGTNEATKAIERGTSKLVVIAEDVEPPEVVAHLPILCDEQGAAYAFVPSKQDLGKALGIDITSAAAILDSGDAQHIVDQVISSIAKIKGETGK", "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": "MGILGKIKNKLKSIGKRVIIDFYRFLDNSGVLKIYEKILEEAIDKDNLPKHVAIIMDGNRRAAEIYGKDRYYGHYLGAEKVREVLRWARDLGINVVTLYAFSTENFRRPKEEVDKLMELFEKKFYEIADDEEIHRYEVRVRAIGRINLLPKNVQKAIKYAEERTKNYNKFFVNIAIAYGGQQEIIDAVKKIAEKVKRGEIEPEDIDKELIDKHLYTANLPFPNPDLIIRTSGEERISNFLIWQSSYSELYFCDIYWPLFRRVDFLRAVRDYQRRQRRFGK", "text": "FUNCTION: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids. SIMILARITY: Belongs to the UPP synthase family."}
{"protein": "MSKSENLYAQAQQLIPGGVNSPVRAFNGVGGVPLFIERANGAYLYDADGKAYIDYVGSWGPMVLGHNHPAIRNAVIDAAERGLSFGAPTEMEVKMAALVTELVPTMDMVRMVNSGTEATMSAIRLARGFTHRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKHTLTCTYNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPDFLPGLRALCDEFDALLIIDEVMTGFRVALAGAQAHYGVEPDLTCLGKIIGGGMPVGAFGGRREVMEALAPGGPVYQAGTLSGNPIAMAAGFACLTEVAQPGTHATLTELTNQLADGLLAAAKAENIPLVVNHVGGMFGLFFTDAASVTRYADVIRCDVERFKRFFHLMLAEGVYLAPSAFEAGFMSLAHGQAEIQHTIDAARRSFAKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
{"protein": "MGRDTIADIITSIRNVDMDRKVTVRIASTNITENIVKILLREGFIENVRKHQESNKYFLVLTLRHRRNRKGTYRTILNLKRISRPGLRIYSNYQRIPRILGGMGIVILSTSRGIMTDREARLERIGGEILCYIW", "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": "MIAGSMVALVTPMDAQGGLDWDSLSKLVDFHLQEGTNAIVAVGTTGESATLSVAEHIEVIRRVVDQVNGRIPVIAGTGANSTSEAVELTENAKTAGADACLLVTPYYNKPTQEGLYLHFKHIAEAVAIPQILYNVPGRTVCDMLPDTVERLSKVPNIIGIKEATGDLKRGREVLDRVSTDFLVYSGDDPTAVELMLMGGKGNISVTANVAPRAMSELCAAAMAGDAETARAINERLMPLHRALFLEANPIPVKWALHEMGLMGNGIRLPLTWLSQSYQEPLRQAMRQTGVLA", "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": "MASDAFMQTACPADAAEQLEAEHAEWAQLGCGAVPPPPAAASRPSRAAVAAYVGEVVDRMRAQSRADERVYVKCGQLVHLRVRARSVPLDDWLTSAELALVSEVAEPVRANRAFVEVSLRYFELTEYATLRALGLQSALKYEEMYLAKLEGGAIESMGQFFVRIAATAATWTMREPAFGRALVGEGATWCAVFNAYLTALYRQLVVPATPIMLFAGRARGSLASCYLLNPQVSSSTEAVEAITTEVARILLNRGGIGISFQSFDRAVSRDCKRGIMGALKLLDSMAMAINSDSERPTGICVYLEPWHCDVRAVLNMRGLLARDESTRCDNLFSCLWVPDLLFDRYLAHLEGREGVVWTLFDDRASHLSRLHGPAFTAEYERLEREGLGVETVPVQDLAFLIVRSIVMTGSPFVMFKDACNRHYHMDTAGDALTGSNLCTEIVQRASPDAHGVCNLASVNLPRCVREGEGGALAFDFAALSTAAATAAIFVNAMMLGGQYPTEKAARGVARHRSLGIGFQGLHTLLLELGMDMLSPAARRLNVEIAERLLLAVMATSATLCEYGCAPFEDFARSKFARGLMPFDGYEGVVLSLPRAWARLREKVARHGLYNAQFVALMPTVSSSQVTEGSEGFSPVFTNMFSKVTMSGELLRPNLPLMRALRKHFTREASRLGAVRALDREQWSVAAALGDLAPGHPLAKFKTAFEYDQERLIDLCADRAPFVDQSQSMSLFVTEPMDGKVPASQIMNLLVYAYKKGLKTGLYYCKIRKATNNGVFTGGDLVCSGCHL", "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. SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large chain family."}
{"protein": "MEYWKHTNHGKDACNELGTSMATHGNKITNKITYILWTIILVLLSIIFIIVLINSIKSEKAHESLLQDVNNEFMEVTEKIQMASDNINDLIQSGVNTRLLTIQSHVQNYIPISLTQQMSDLRKFISEITIRNDNQEVPPQRITHDVGIKPLNPDDFWRCTSGLPSLMKTPKIRLMPGPGLLAMPTTVDGCVRTPSLVINDLIYAYTSNLITRGCQDIGKSYQVLQIGIITVNSDLVPDLNPRISHTFNINDNRKSCSLALLNTDVYQLCSTPKVDERSDYASSGIEDIVLDIVNHDGSISTTRFKNNNISFDQPYAALYPSVGPGIYYKGKIIFLGYGGLEHPINENAICNTTGCPGKTQRDCNQASHSPWFSDRRMVNSIIVVDKGLNSIPKLKVWTISMRQNYWGSEGRLLLLGNKIYIYTRSTSWHSKLQLGIIDITDYSDIRIKWTWHNVLSRPGNNECPWGHSCPDGCITGVYTDAYPLNPTGSIVSSVILDSQKTRVNPVITYSTATERVNELAIRNKTLSAGYTTTSCITHYNKGYCFHIVEINHKSLDTFQPMLFKTEIPKSCS", "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": "MATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELEA", "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 (PubMed:31015432). Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (PubMed:31015432). SUBCELLULAR LOCATION: Mitochondrion outer membrane Membrane Note=May localize to non-mitochondrial membranes. SIMILARITY: Belongs to the eukaryotic mitochondrial porin family."}
{"protein": "MDLKTSYKGISLNPIYAGSSAVATVSENGKILATPVLDEINIIDLTPGSRKILHKISNEDEQEITALKLTPDGQYLTYVSQAQLLKIFHLKTGKVVRSMKISSPSYILDADSTSTLLAVGGTDGSIIVVDIENGYITHSFKGHGGTISSLKFYGQLNSKIWLLASGDTNGMVKVWDLVKRKCLHTLQEHTSAVRGLDIIEVPDNDEPSLNLLSGGRDDIINLWDFNMKKKCKLLKTLPVNQQVESCGFLKDGDGKRIIYTAGGDAIFQLIDSESGSVLKRTNKPIEELFIIGVLPILSNSQMFLVLSDQTLQLINVEEDLKNDEDTIQVTSSIAGNHGIIADMRYVGPELNKLALATNSPSLRIIPVPDLSGPEASLPLDVEIYEGHEDLLNSLDATEDGLWIATASKDNTAIVWRYNENSCKFDIYAKYIGHSAAVTAVGLPNIVSKGYPEFLLTASNDLTIKKWIIPKPTASMDVQIIKVSEYTRHAHEKDINALSVSPNDSIFATASYDKTCKIWNLENGELEATLANHKRGLWDVSFCQYDKLLATSSGDKTVKIWSLDTFSVMKTLEGHTNAVQRCSFINKQKQLISCGADGLIKIWDCSSGECLKTLDGHNNRLWALSTMNDGDMIVSADADGVFQFWKDCTEQEIEEEQEKAKLQVEQEQSLQNYMSKGDWTNAFLLAMTLDHPMRLFNVLKRALGESRSRQDTEEGKIEVIFNEELDQAISILNDEQLILLMKRCRDWNTNAKTHTIAQRTIRCILMHHNIAKLSEIPGMVKIVDAIIPYTQRHFTRVDNLVEQSYILDYALVEMDKLF", "text": "FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
{"protein": "MQPIYQYAWIIPFVPLPVTMSIGLGLLLVPTATKNLRRMWAFPSVSLLSIVMVFSADLSVQQIDGSSIYQYLWSWTINNDFSLEFGHLIDPLTSIMSILITTVGIMVLIYSDKYMSHDQGYLRFFAYMSFSNTSMLGLVTSSNLIQIYIFWELVGMCSYLLIGFWFTRPIAANACQKALVTNRVGDFGLLLGILGLYWITGSFEFRDLFEIFNNLIHNNGVNSLFATLCASLLFAGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFTVIPYIMNLISLIGVITVLLGATLALAQRDIKRSLAYSTMSQLGYIMLAPGIGSYRAALFHLITHAYSKALLFLGSGSIIHSMEPIVGYSPDKSQNMVLMGGLRKYVPITKMTFLLGTLSLCGIPPLACFWSKDEILNDSWLYSPIFAIIACATAGLTAFYMFRTYLLTFEGYLYAHFQNYSGTQNSSFYSISIWGKEEPKLVNRNLLLSTINKNEKVSFFSKKTCKINGNVRNLMRSFSTHFDNKDTSMYPHESDNTMLLPLLVLVLFTLFVGFIGIPFDQGVMGLDILSKWLTPSINLLHQNSNYSVNWYEFATNAFFSVSIAYFGIFIASLLYGSVYLFFQNLELINSFVKIGPKRIFLDQIINVIYNWSYNRGYIDVFYATSLTKGIRGLAKLTHFFDRRVIDGIMNGVGVSSFFVGEGIKYLGGGRISSYLFVYLSYVSIFLLIYIFFFRKVESIKLFQTKNGIPLYL", "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": "MNVYYEKDADLAYLQGKKIAVLGYGSQGHAHSLNLHESGLNVRVGLRPESASCAKAREAGLEVTSVAEATKWADIVMVLLPDQNQKAVYEAEIAPNLEPGNTLAFGHGFNIHYKQIVPASSVNVIMIAPKSPGHLVRRTYTEGNGVPCLIAVHQDPTGEAKQQALAWAKALGGTKAGVIETNFKNETETDLFGEQAVLCGGSAELIKAGFETLVEAGYPEELAYFECMHELKLIVDLYYEGGLSRMNYSVSDTAEYGGMTRGPRLITPAVKAEMKKILEEVQDGRFAKEFIDECNGGYQNLSKLRESNSNHAIEKVGAKLRNMMSWLIKK", "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": "MIPVVIEQTSRGERSYDIYSRLLKDRIIMLTGPVEDNMANSVIAQLLFLDAQDSTKDIYLYVNTPGGSVSAGLAIVDTMNFIKSDVQTIVMGMAASMGTIIASSGAKGKRFMLPNAEYMIHQPMGGTGGGTQQTDMAIAAEHLLKTRKTLEQILADNSGKTVEQIHADAERDYWMSAEETLAYGFIDEIMANNNLS", "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": "MIDSVKLRRDCAADFFSHYEYLCALQDSVPLPAVRACLRDGVLDFNADRLRAVDWAPLLSTLRVNRDLPLVAIKSSFQPWLGETVLRSGGADTHRICRNRVPAVRSKDISFQLCKALRGCLSVSGVLRNLELNGLILRERDLTSLTKGLSKSTSLVHLSLANCPIGDGGLEIICQGIKNSVTLKTVNFTGCNLTWQGACHMAKILKYQTMRRHEETWAESLRYRRPDLDCMAGLRRITLNCNTLIGDQGASAFADSLSEDLWLRALDLQQCGLTSEGAKALLEALETNRTLVVLDIRKNPLIDHSMMKAVIKKVLQNGRSADSEYQWVTSPSSKEPSKTAKQRKKTIVLGSSRKGKATIRIGLATKKPSSNGRKQGLGKDCYAPNPLPPGASGFLPWRTAERAKRSRSSSLIKTRDLSNHLKKSDFPVTVTVESPSSSETDETEDSSESVQEAPQKTSIKEETLQEKLEECLRQLKEERVIRLKADKRVSELEHENAQLRNINFSLSEALHAQSLTNMILDDEGVLGSIENSFQKFHAFLDLLKDAGLGQLATMAGIDQSDFHLLGRPQMNSTVNTPIQEQKALEDETLHPKQTATGQMQDIRFQKITSDALIPLPLNTVQDPASAQEAVGASRDHLGVVGLEQQEGSAAGFIAKTGSPLAGGIPGGRSQREEEVLSKHSRSSSEKGSTASEPSRRPSAERHPRKDLLSDADPPGNSESKGPGDRRSLLNEPIKSESLKKCISIKKENRIVTVSSKTIKSKPNLLEHSESDTLGSDFELQERVHSSAHLT", "text": "FUNCTION: May be required for efficient PLK4 centrosomal localization and PLK4-induced overduplication of centrioles. May play a role in cilium biogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Note=Mainly localizes at the centriolar wall, but also found in the pericentriolar material. Expressed in photoreceptor inner segment. SIMILARITY: Belongs to the CEP78 family."}
{"protein": "MSILKIQAREIFDSRGNPTIEVDLYTKKGLFRAAVPSGASTGIYEALELRDNDKTRFLGKGVSKAVEHVNKTIAPALVNKNVSVVEQEKIDKLMIEMDGSENKSKFGANAILGVSLAVCKAGAAEKDIPLYRHIADLAGNKEVILPVPAFNVINGGSHAGNKLAMQEFMILPIGAECFKEAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKTAISKAGYADKIVIGMDVAASEFYRDGKYDLDFKSPDDRSRYITPDQLADLYKGFVKNYPVVSIEDPFDQDDWPAWKKFTAESGIQVVGDDLTVTNPKRIAKAVQEKSCNCLLLKVNQIGSVTESLQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKARFAGRNFRNPRVN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the enolase family."}
{"protein": "MAQIKYYATGRRKTSVAKVWLSPGNGKIIVNDKNMEEYFPLETLRIIVKQPLTLTETLGKYDVIAKVKGGGLSGQAGAVRHGIARALVLADPTLRPVLKKAGFLTRDPRMVERKKYGLKKARRAPQFSKR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MKKWFIALAGLLLTVTLAGCGSQTVATTNGGKITESAYYSSLKGTSSGKQVLQQMILNKVLEKQYGDKVSKSAVTKQFDKYKSQYGSSFSSVLSQSGMTQSSLKTEIRSNLLLKEAVKDNVTVTDAQLKKQFKSYEPEVSVAHILVSKKSTAQTIIKDLKSTKSSDMTSEFTKLAKKYSTDTATKNKGGKLSSFDSTDTSLDSTFKKAAFKLKTGEYTATPVKTQYGYHVILMLKNPGKGTIKEHKAELTKQIIDNDMNDSTVLHNVVAKVLKKGNVSIKDNDLKNILSDYLSSSSSSSASSSSK", "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": "MLFRFGVVVPPAVAGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAAALALQEPGLWLAEVELEAYEEAGGAEPGRVDTFWYKFLQREPGGELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQLEHVTIKLKHELGVTAVMNFQTEWDIIQNSSGCNRYPEPMTPDTMMKLYKEEGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAQQDFSQKFGKVHSSICAL", "text": "FUNCTION: Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin (PubMed:18040046, PubMed:18852261, PubMed:19036738, PubMed:23663739, PubMed:24430976, PubMed:24068615). Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro) (PubMed:16971387, PubMed:24430976). Has also been shown to dephosphorylate MAPT (PubMed:19542233). Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates (PubMed:18040046, PubMed:18852261, PubMed:23663739). Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS) (PubMed:19036738, PubMed:24068615). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway (PubMed:20453062). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane Note=Colocalizes with glycogen synthase in punctate structures in the cytoplasm. Primarily associated with polyribosomes at the rough endoplasmic reticulum, and also detected at the plasma membrane. Under glycogenolytic conditions localizes to the nucleus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family."}
{"protein": "MIDPGTVGAALETAVFGLLALVTVFFAIFVVIAKDVVRAGLALIMCMFGVAGLYILLNAQFLGVIQVLVYIGAIGVLILFAVMLTKREIGGGPVQINRPLAFLVCLLFVAVVVTGAFGTSWNTVSELPENPADPSNIEGIGMLIFTHFVAPFEVLSIVLLASLIGAIYMAKGEGNR", "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. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 6 family."}
{"protein": "MEDFVRQCFNPMIVELAEKAMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELDDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRRLADQSLPPNFSCLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKTTPRPIRLPDGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPYVVKPHEKGINPNYLLSWKQVLAELQDIENEEKIPRTKNMKKTSQLKWALGENMAPEKVDFDDCKDISDLKQYDSDEPELRSLSSWIQNEFNKACELTDSIWIELDEIGEDVAPIEHIASMRRNYFTAEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMLLRSAIGQVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEEGSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLVVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALR", "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": "MNKLANQHLIWIDLEMTGLDPNQDRIIEIATIVTDKDLNILAKGPVLAVHQPNTLLSKMNEWCIKTHTANGLIERVKQSKLTERAAELQTLDFLKQWVMKGSSPICGNSVAQDKRFLYQYMPDLADYFHYRHLDVSTLKELARRWKPEILQQFSKKNSHLALDDIRESIEELKFYREHFIKLA", "text": "FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the oligoribonuclease family."}
{"protein": "MLKMDREKLIVPNQIGYLILKEDGAVLESGGDLKNDERSANVIMGLLNLTETIDESFMPSSSCERITIDYEHHYYSICMSNRRIYIIKISKSQNGVTTTTSSSSSNSVYNDASDSGAVLA", "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. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the LAMTOR4 family."}
{"protein": "MADNQIPSSVADAVLVKSIEMPEGSQKVEELDFNKFKGRPITVDDLLQGMKHMGFQASSMCEAVRIINEMRAYRDPTTSEKTTIFLGYTSNLISSGLRGTLRYLVQHKHVSAIVTTAGGIEEDFIKCLGDTYMSSFSAVGADLRSKGLNRIGNLVVPNSNYCAFEDWVVPILDKMLEEQEASRGTENEINWTPSKVIHRLGKEINDERSVYYWAWKNDIPVFCPALTDGSLGDMLYFHTFKASPKQLRIDIVEDIRKINTIAVRAKRAGMIILGGGIVKHHIANACLMRNGAESAVYINTAQEFDGSDAGARPDEAVSWGKIKVGADAVKVYMEATAAFPFIVANTFAKEDGL", "text": "FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. SIMILARITY: Belongs to the deoxyhypusine synthase family."}
{"protein": "MNKKILETLEFDKVKALFEPHLLTEQGLEQLRQLAPTAKADKIKQAFAEMKEMQALFVEQPHFTILSTKEIAGVCKRLEMGADLNIEEFLLLKRVLLASRELQNFYTNLENVSLEELALWFEKLHDFPQLQGNLQAFNDAGFIENFASEELARIRRKIHDSESQVRDVLQDLLKQKAQLLTEGIVASRNGRQVLPVKNTYRNKIAGVVHDISASGNTVYIEPREVVKLSEEIASLRADERYEMLRILQEISERVRPHAAEIANDAWIIGHLDLIRAKVRFIQERQAVVPQLSENQEIQLLHVCHPLVKNAVANDVYFGQDLTAIVITGPNTGGKTIMLKTLGLTQVMAQSGLPILADKGSRVGIFEEIFADIGDEQSIEQSLSTFSSHMTNIVDILGKVNQHSLLLLDELGAGTDPQEGAALAMAILEDLRLRQIKTMATTHYPELKAYGIETAFVQNASMEFDTATLRPTYRFMQGVPGRSNAFEIAKRLGLSEVIVGDASQQIDQDNDVNRIIEQLEEQTLESRKRLDNIREVEQENLKMNRALKKLYNELNREKETELNKAREQAAEIVDMALSESDQILKNLHSKSQLKPHEIIEAKAKLKKLAPEKVDLSKNKVLQKAKKKRAPKVGDDIVVLSYGQRGTLTSQLKDGRWEAQVGLIKMTLEEKEFDLVQAQQEKPVKKKQVNVVKRTSGRGPQARLDLRGKRYEEAMNELDTFIDQALLNNMAQVDIIHGIGTGVIREGVTKYLQRNKHVKSFGYAPQNAGGSGATIVTFKG", "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": "MLSDPIADMLTRIRNATRTHKETVDVPASNFKEQLANLLVAEGYVAGVERTRLDGQPADVLRLTLKYGAKREQVIKHIERISRPGRRAYVSAENLPRIQRGMGVAVVSTSKGLLPDREARKLGVGGEVICVLW", "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": "MFDLNQSLFLRALRRQPVERTPIWIMRQAGRYLPEYRKVREHAGDFLNLCKNPELACEVTLQPLRRYALDAAILFSDILTIPDAMGLGLYFAEGEGPRFTNPLQDTKAIHTLKIPSIPESLSYVFDAARLIRQEMPKELPLIGFSGSPWTLACYMVEGGSSRDFKRILNLIYTEKEAAHLLLNKLAVSVTAYLIEQIKAGVNAVMIFDTWGGVLTPQNYKDFSLAYMHQIVQQLKKEYPDIPVILFTKNGGQWLEWMAETGCDALGVDWTCDLASARKRVGGKVALQGNLDPAVLLTTKNCIRSEVGSVLASYGYGTGHIFNLGHGITPDVPPENVAIMIEAVHEISPQYHL", "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": "MLRPWLRQCPRATRSLACPQCHLPRPQTARRALRPLPALSLSHPIRSLQTTTTESPDRIPLRKQLKQDAKAVKARKRQTRENEEASREKWELTVGIEIHAQLNTESKLFSRASTSSTDLPNSNVALFDLAFPGSQPEFQIATLLPALRAALALNCEIQPVSKFDRKHYFYQDQPAGYQITQYYEPFAKNGYVDLFRHDGIAPEDGDTVRIGIKQVQMEQDTAKSQEYPPSTQLLDFNRVSHPLVEIITMPQIHTPATAAACVRKIQSILQSCNAVTTGMELGGLRADVNVSIRQRGDTAGTHQYGGIGGLGQRTEIKNLSSFKAVEDAIIAEKNRQIAVLESGGVVEGETRGWTIGSTETRKLRGKEGEVDYRYMPDPDLPPLYIGADLVAALRTNLPTSSDALIELLAGPEYGLPIEDAKPLVELEDGARLEYYQEVVDLLRALQSDQDPKAQKGLARVAGNWVLXELGGLWAKAEEAWDAARVPAPTLAALIDQLQRKHITGPTAKQVLAMVFAGDERPIPQLLEEENLLLRPLSREEYVTLAEAAISLNPAMVEQIRQKNQLGKLGWFVGQMMRMGEKGRVEAPRADAILRELILDQR", "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": "MSKVFKLHSDFQPGGDQPEAIRQLQEGLEDGLAHQTLLGVTGSGKTFTVANVIANLNRPTMVLAPNKTLAAQLYSEMKDFFPENSVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVIVVASVSAIYGLGDPDSYLKMMLHLTNGMMIDQRSILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDEHALRVELFDDEVERLSLFDPLTGQVQYHVPRYTVYPKTHYVTPRERIIQAMEAIKIELEQRRKVLLANGKLLEEQRITQRTQFDLEMMNELGYCSGIENYSRYLSGRTEGEPPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRSRKETLVEYGFRMPSALDNRPLRFEEFEALAPQTIYISATPGKYELEKSSGDVVEQVVRPTGLLDPEVEVRPVATQVDDLLSEIRIRAVKNERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERVEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNLHGKAILYGDKITDSMAKAIGETERRRAKQQIFNEKHGIVPKGLNKKINDILQIGQPAGGKRKGRGKAVATAETFSNLSAKELESKIRELEAKMYQHAQDLEFEQAASVRDQVQALREQFIANF", "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": "MNGIINVYKEKGFTSFDVCAKLRGILKQKKIGHTGTLDPDAEGVLPVCVGNATKLCDLLTDKDKVYEAVLTLGIITDTEDMTGEVLERRLVTATYDRVLEVVEQFTRTYDQIPPMYSAIKVNGQKLYELARQGKVIERKPRTVTIHAIDILGVTPLEEQPEIVHEVRMRVSCSKGTYIRSLCRDIGEALQCGGCMKSLIRTQVSIFTLENTLRLAEIEECVKNQTLEQVLMPVDKLFLSMPKVVVKKESCKFLYNGNQLVEDNFTWEKVSDQINIDKIRVYDSEDVFTGIYEYDEKKNCYQPVKMFL", "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": "MKQVKELIGKRVLVLGMAKSGVASALLLARIGAEVVINDSKSRADQPQAGELEAAGIQVVCGGHPLTVLDGCSLLVKNPGIPYTNIVVKEAEARGIPIWTEIELAYLISEAEMVAITGSNGKTTTTTLVKEMLEHSGRKPLIAGNIGTVASEVAQKAKAEHVIVLEVSSFQLMGTNAFQPKVAVWLNIFDAHLDYHGTREDYIAAKARIAANMGPADYLVYNADDPTVVQAIARIGATLVPFSRINVVEDGAYVKDGTIFFKDEPILALADAVLPGAHNVENMLAATAAARLAGATVEQIRHVLSHFPGVKHRLQYVGSWEGRQFYNDSKATNILATKAALSGFAKPVVLIAGGLDRGNDFDELLASLKYVKAVVAYGETKSKLLALAAKANVQAVTAERVQDATEKAVALSQPGDVVLLSPACASWDQYRSFEERGDEFLDYVNTIIKPS", "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": "MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTVKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVIPPTENEHDEQDENSAEASAELSSEGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM", "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": "MARYIGPKCKLARREGTDLFLKSGVRAIESKCNIEAAPGIHGQRRGRQSDYGTQLREKQKVRRIYGVLERQFSGYYKEAAGKKGATGENLLQLLECRLDNVVYRMGFGSTRAESRQLVSHKSISVNGQTVNVPSYQVRAGDVVAVREKAKNQLRIVQALDLCAQRGRVEWVEVDTEKKSGVFKNVPARSDLSADINESLIVELYSK", "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": "MDWEKLGLKMGLEIHQQLNTKHKLFCPCKTELVDEDYNEIVERNLRPTQSELGEIDRAALQESLRGLNFKYESYDHHTCLVESDDEPPHSLNKEALEICITIAALMNMHIVDEFHTMRKQVIDGSNTGGFQRTGLAATDGYLDTPYGRVAIESLGLEEDAARRIETTEDYTEFRLDRLGIPLAEITTDPSMHHPDQVREVAYMIGQVLRSTNVKRGLGTIRQDLNISIEKGARVEIKGVQNLDLMSEIVENEVQRQLALIEIKEELNKRNAEVLEEIHDLDSLFENTKSKILSSAESIKAVVLKGFNGLIGKEVQPGRRFGTEIASYAKKRGVSGIFHSDELPAYGITQDEVNSVKDYLNVGSQDAFIIVAHDENVAISALEEVKRRANLGFEGVVEETRKSLDDGNTEYMRPLPTANRMYLETDIPLFKITDELVEPIKNNLPELPDVKKERIIKEYNLSEDLASQLVKRLEADVFEEILTDVEVDPTPVASLLAYDLREIKREGLDIDILTTRHLKDIFQLLADSKIAKDSVTKLTTCVIQSPDEEIEITAKNNNLTLLSHEEVTQIIEDIVNKNEAMVKERQMGAMGPLMGMSMKELKGKADGSIVNRIVKESIQKML", "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": "MRIAGVNLPLNKHAVIALTHVYGIGKTSARNILERAGIDPAKKIAEMSDEEAHAIREIIAEEYKVEGQARGLQQLAVKRLMDIGCYRGLRHRRSLPVRGQRTQTNARTRKGKRKTVAGKKKAVKK", "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": "MNDMTLYLIIALVPLAGSLIAGLFGNKIGRAGAHTVTILGVAVSAVLSAYVLWGFLNGSRAKFDENVYTWLTMGGLDFSVGFLVDTMTAMMMVVVTGVSLMVHIYTIGYMHDEKVGYQRFFSYISLFTFSMLMLIMSNNFIQLFFGWEAVGLVSYLLIGFYFKRPSATFANLKAFLINRVGDFGFLLGIGLVLAYFGGSLRYQDVFAYLPNVQNATIQLFPGVEWSLITVTCLLLFVGAMGKSAQFPLHVWLPDSMEGPTPISALIHAATMVTAGLFMVSRMSPIYEMSSTALSVIMVIGAITALFMGFLGVIQNDIKRVVAYSTLSQLGYMTVALGASAYSVAMFHVMTHAFFKALLFLAAGSAIIGMHHDQDMRHMGNLKKYMPITWLTMLIGNLSLIGTPFFSGFYSKDSIIEAAKYSTLPGSGFAYFAVLASVFVTAFYAFRQYFMVFHGEEKWRSLPEHHSDGHGEEHHGLGKNDNPHESPLVVTLPLILLAVPSVIIGYIAIEPMLYGDFFKDVIFVNADAHPTMHIMKEEFHGALAMVSHSLHSPVLYLAIAGVLSAWLLYVKLPHLPAKIAQAFRPVYVLFENKYYLDALYFNVFAKGTRALGTFFWKVGDTAIIDNGIVNGSARLVGAVAAQVRKVQTGFIYTYAAAMVFGVLVLLGMTFWGLFR", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 5 family."}
{"protein": "MPNRVIIFDTTLRDGEQALAASLSVKEKLQIALALERLGVDVMEVGFPVSSPGDFNSVQTIAKTIKNSRVCALARALPADIDAAAQALAVAEQFRIHTFISTSTIHVESKLKRSFDDVLAMAVNAVKYARRFTDDVEFSCEDAGRTPIDNLCRMVEAAITAGARTINIPDTVGYTIPSEFSTIIETLFNRVPNIDQAIISVHCHDDLGLSVANSIGAIEKGARQVECTVNGIGERAGNCSLEEIAMILATRKDKLGLETGIVAKEIHRTSNLVSQLCNMPVQANKAIVGSNAFSHSSGIHQDGMLKAKNTYEIMTPESIGLHRNNLNMTSRSGRHVIKHRMEEMGYHTDDFDIDSLYEQFLKLADKKGQVFDYDLEAIVFMATQVAEDDHYRLQHLSVHSDSSEGVATATVRIKVEGEDLTEAAIGNGPVDAAYKAIARASGREVEISSYKLSAKGQGQDALGQVDITAKYQGRTFHGVGLATDVVEASAQALVHVMNLICRADKVADIKSQIQFNREHAGV", "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": "MELVLKDAQSALEVSEATFGRDFNEALVHQVVVAYAANARQGTRAQKTRAEVTGSGKKPWRQKGTGRARAGTVKGPIWRGGGVTFAAKTQDHSQKVNKKMYRGALKSIFSELVRQDRLIVVESFGVDAPKTKELKAKLDAMQLQDVLIVTPEVDENLFLAARNLYKVDVRDVAGVDPVSLIAFDKVLVTAEAIKQIEEMLG", "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": "MTNEFAIPRSVEWKETYIRILNQQKLPDVTEYVELETKEDVFDAIVTLKVRGAPAIGITAAFGLALSAKSFEARDLSDFRRQFADVKTYLNSSRPTAVNLAWALDRLTDSIRDAISINEAKTTLVHEAIQIQIEDEETCRMIGQNALHLFKKGDQIMTICNAGSIATSRYGTALAPFYLAKQKDLGLHIYACETRPVLQGSRLTAWELMQGGIDVTLITDSMAAHTMKEKHISAVIVGADRIAKNGDTANKIGTYGLAILANAFQIPFFVAAPLSTFDLQIENGDQIPIEERDPDEVRQISGIRTAPEDVPVFNPAFDITPGSLISGIITEKGIVTGSYTEEIEQLFADCQLS", "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": "MNLQRFPRYPLTFGPTPIQPLKRLSAHLGGKVKLYAKREDCNSGLAFGGNKTRKLEYLIPDALAQGADTLVSIGGVQSNQTRQVAAVAAHLGMKCVLVQEHWVNYDDPVYDRVGNIQLSRMMGADVRLVADGFDIGIRRSWEEAMESVRQAGGKPYPIPAGCSEHPLGGLGFVGFAEEVRAQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASATPEKTHAQITRIARHTAEIVELGRRIDEQDVVLDTRYAGPEYGLPNDGTLEAIRLCARLEGVLTDPVYEGKSMHGMIDKVRLGEFEPGSKVLYAHLGGVPALSAYAEIFRNG", "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": "MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS", "text": "FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis (PubMed:11447297, PubMed:12121969, PubMed:9230442, PubMed:11257230, PubMed:11257231, PubMed:12620238, PubMed:17967870, PubMed:19473982, PubMed:20154138, PubMed:22103349, PubMed:17560374). Acts as a direct caspase inhibitor (PubMed:11257230, PubMed:11257231, PubMed:12620238). Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry (PubMed:11257230, PubMed:11257231, PubMed:16352606, PubMed:16916640). Inactivates CASP9 by keeping it in a monomeric, inactive state (PubMed:12620238). Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin- protein ligase activity include: RIPK1, RIPK2, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS, PTEN and BIRC5/survivin (PubMed:17967870, PubMed:19473982, PubMed:20154138, PubMed:22103349, PubMed:22607974, PubMed:30026309, PubMed:29452636, PubMed:17560374). Acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (PubMed:19667203, PubMed:22607974, PubMed:30026309, PubMed:29452636). 'Lys-63'-linked polyubiquitination of RIPK2 also promotes recruitment of the LUBAC complex to RIPK2 (PubMed:22607974, PubMed:29452636). Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation (PubMed:17560374). Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation (PubMed:20154138). Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation (PubMed:17967870, PubMed:22103349). Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation (PubMed:14685266). Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation (PubMed:21145488). Ubiquitinates and therefore mediates the proteasomal degradation of BCL2 in response to apoptosis (PubMed:29020630). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase- independent manner (PubMed:22095281). Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8 (PubMed:22095281). Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES (PubMed:22304967). Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program (PubMed:22304967). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=TLE3 promotes its nuclear localization. SIMILARITY: Belongs to the IAP family."}
{"protein": "MIVILDNGGQYVHRIHRSLKYIGVSSKIVPNTTPLEEIESNKEVKGIILSGGPDIEKAKNCIDIALNAKLPILGICLGHQLIALAYGGEVGRAEAEEYALTKVYVDKENDLFKNVPREFNAWASHKDEVKKVPEGFEILAHSDICQVEAMKHKTKPIYGVQFHPEVAHTEYGNEILKNFCKVCGYKFE", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP."}
{"protein": "MLQKISSDSYRRLLAPVLSSSSSLSSTSINRTEIERITIIINGHPFPNHPIQPILAKHIPLSSLSPEFVSEVLGRLFAAHSNGLKALEFFKYSLKSSKSSPTSDSFEKTLHILARMRYFDQAWALMAEVRKDYPNLLSFKSMSILLCKIAKFGSYEETLEAFVKMEKEIFRKKFGVDEFNILLRAFCTEREMKEARSIFEKLHSRFNPDVKTMNILLLGFKEAGDVTATELFYHEMVKRGFKPNSVTYGIRIDGFCKKRNFGEALRLFEDMDRLDFDITVQILTTLIHGSGVARNKIKARQLFDEISKRGLTPDCGAYNALMSSLMKCGDVSGAIKVMKEMEEKGIEPDSVTFHSMFIGMMKSKEFGFNGVCEYYQKMKERSLVPKTPTIVMLMKLFCHNGEVNLGLDLWKYMLEKGYCPHGHALELLTTALCARRRANDAFECSWQTVERGRCVSEPVYRMLETSLSSNNELKKLEELKEEIQKLHSFLPPPEIQLM", "text": "SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MPSKKTDAPKQSEAAGTQTPDRANTNAKLQSLETFRSDATGQALRTNQGVKIADNQNSLKAGARGPSLLEDFIMREKITHFDHERIPERIVHARGTGAHGYFQSYGNHADLTKAGFLQDPDKITPVFVRFSTVQGPRGSGDTVRDVRGFAVKFYTDEGNFDLVGNNMPVFFIQDAIKFPDFVHAVKPEPHNEIPTGGSAHDTFWDFVSLVPESAHMVMWAMSDRAIPRSLRMMEGFGVHTFRLINAEGVASFVKFHWKPRQGVHSLLWDEAQKLAGKDTDFQRRDLWEAIENGDYPEWELGVQIVPEADEHKFDFDLLDPTKIIPEELVPVTPLGKMVLNRNPDNFFAEVEQVAFCPGHIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHQIPINRPVAPNHNNQRDALHQHVVHKGRASYEPNSIDGGWPKETPAAAQDGGFESYQERIDAHKIRQRSESFGDHFSQARLFFQSMSPTEQQHIIKAYSFELGKVEREHIRAREVNEILANIDLKLAAAVAANLGLPAPKAGTVQVKGSQLAQSPALSQMNHPGSVGIKGRKIAVLVANGVDAASVDKLIKALEAHSARPMLLGPTSAPVKATDGKQLPVEASMEGMPSIMFDGIVVPSGKASTDALAASGLAKHFLLEGYKHLKAMVLTKELATGLGLKEDKGLLLADDQKAVDAFVKAVEGHRVWEREAAAEAVPA", "text": "FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the catalase family. HPII subfamily."}
{"protein": "MATTATRFPQFSQDLASDPTTRRLWYGIATAHDFETHDGMTEERLYQKLFATHFGHLAIIFLWASGNVFHIAWQGNYEQWVANPTGVTPIAHAIWDPQFGKAAVEAFTQPGGGGPVNAAYSGLYYWFNTIGLRTNGDLYAGAIGLLLLAAVFLFAGWLHLQPRFRPSLSWFKNAEARLNHHLAGLFGVSSLAWAGHLVHVAIPESRGQHVGWDNFLTTLPHPAGLKPFFTLNWGVYAQNPDTANHVWGTAEGAGTAILTFLGGFNPNTQSLWLTDMAHHHLAIAVIFIVAGHMYRTNWGIGHSIREILGAHNPPKGTPFGGLLGEGHRGLYDTVNNSLHFQLALALACLGVVTSLVAQHMYALNPYVFMSMDHTTEAALYTHHQYIAGFLMVGAFAHGAIFLVRDYDPEANKNNVLARVLDHKEAIISHLSWVSLFLGFHTLGLYVHNDVMQAFGTPEKQILIEPVFAQFIQASHGKMIYGMDVLLSNPDSIASTAWPNYGNVWLPGWLQAINDPNGFLFLPIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAMFWMLNTIGWVTFYWHWKHLGIWSGNTAQFNENSTYLMGWLRDYLWANSAQLINGYNPYGMNNLAVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLVWAHERTPLANLIRWKDKPVALSIVQGRLVGLAHFTVGYVLTYAAFVIASTASLSG", "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": "MPLPPSTLNQKSNRVYSVARVYKNACEERPQEYWDYEQGVTIDWGKISNYEIINKIGRGKYSEVFSGRCIVNNQKCVIKVLKPVKMKKIYRELKILTNLTGGPNVVGLYDIVQDADSKIPALIFEEIKNVDFRTLYPTFKLPDIQYYFTQLLIALDYCHSMGIMHRDVKPQNVMIDPTERKLRLIDWGLAEFYHPGVDYNVRVASRYHKGPELLVNLNQYDYSLDLWSVGCMLAAIVFKKEPFFKGSSNPDQLVKIATVLGTKELLGYLGKYGLHLPSEYDNIMRDFTKKSWTHFITSETKLAVPEVVDLIDNLLRYDHQERLTAKEAMDHKFFKTKFE", "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). Phosphorylates YTA7 during S-phase to promote transcription of histones (PubMed:22156209). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily."}
{"protein": "MELPLSQAQFSGTFLMLAVSNMLLWEKVSSIPACLAEEGGCWNPIVETFNSAMQRGETLRNLADQLYTELYHNQFSSEQFLALNSKLIRRDKTAVRAGTYCHSTLSNSPDGETKHADVETEKYLKMLINFVGAWISPLYHLVIELSAMQDVPETILSKAKDIEENKRELLDDLKWILTKVYPTAEMKEEFPSWEHLSFLKSSNKDSKFLAMFNLSKCIYNETYYILFYLRTLKCHITGKDC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MAQHTFLVEIGTAELPPKALRSLAEAFADNLKSELTKADLAFGDVEWFASPRRLALKVSELAGEQPSKSVEKRGPAVAQAFDAEGKPTKAAEGWARGNGITVEQAERLVTDKGEWLVHTAKVEGRPAKDLLGELVSQALAKLPIPKMMRWGDKTIQFVRPVFTVTLLLDGELVPAHILGIDSARTLRGHRFMGESEFTIDNASQYPQILQERGMVIADFMARKVKIKADAEAAAAAFGGVADLDDALLEEVTALVEWPVVLTANFEEKFLAVPAEALVHTMKGDQKYFPVYDKNGKLLPKFIFVTNIESKDPSQIISGNEKVVRPRLSDAEFFFKTDLKQTLASRLPRLETVLFQQQLGTVKAKVERIETVAGFIAERIGADVAQAKRAGLLSKCDLMTNMVGEFTDTQGVMGMHYARHDGEDEAVAVALNEQYMPRFAGDALPSGLVACAVALADKFDTLAGIFGIGMLPKGDKDPFALRRAAIGALRIMTEKQLDLDLVELVEEAVRVYGDKLTNKTVVTDVVDFMLGRFRAAYQDEGIGADVVLAVLARRPTRPLDFDRRVKAVSHFRSLDAALALAAANKRVSNILAKVEGELPTAVKPELLVDAAEKALATQVAELQAELAPLFAAGDYQAALTRLAALREPVDTFFNEVMVMADDEALKANRLALLNNLRNLFLQVADISLLQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MSERESWHKEIDLFLVAMGYFTRIPMPKWVEVDSDKLNKASRYFGLVGLLIGLLSAIVFWLTQNWLPAGVSVLLAMLVGVLLTGGFHEDGLADTFDGFGGGWTAEDKLRIMKDSRLGSYGAIALILALLLKWQLLVELALYDPVVAGSALIVAHTVSRVVAASIIFTEKYVRDDETSKSKPLSQHQGINELFILVASGVLVLLFLKGLAALSLLLVMIGLRRLIVVIFRRQIGGYTGDTLGAAQQICEIVCYLVLLIVGSIL", "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": "MALNIKDPSVHQAVKQIAKITGESQARAVATAVNERLARLRSDDLAARLLAIGHKTASRMSPEAKRLDHDALLYDERGLPA", "text": "FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC28. FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system."}
{"protein": "MQQPWKAVALSDLPLREDLKLQHAYGAPQLDVPVCLNVNENPYPPSPALVERIATAVADAARAANRYPDRDFAALRSHLAAYLTHDTGVTVDASSVWAANGSNEVIQQILQAFGGPGRSALAFTPAYPMYDEYCRTTFTRLHTLPRTEDFALDLNQALDSIRAHQPGVVLLTSPNNPTGTALPIDDIRAILDAAPGVVVVDEAYAEFRRHGVPSAVTLLPAYPRLIVTRTLSKAFKFAGGRVGYCACAPAIVEALKLVRLPYHLSAFTQAAACAALVARDEMLSQVEAIKAERDSTVDWLRGLGLTVADSDANFVMFGEFADRHRIWSGLLRRGVLIRESGPPPYLRVSIGTGAEMAAFRAALLDVMALE", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
{"protein": "MAQASDSTAMEVEEATNQTVKKRFEVKKWSAVALWAWDIQVDNCAICRNHIMDLCIECQANQAAGLKDECTVAWGNCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH", "text": "FUNCTION: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate (By similarity). Essential for meiosis, mitotic chromosomal condensation and cytokinesis. Involved in histone H3 phosphorylation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RING-box family."}
{"protein": "MADFVGSWKLEHSENMDGVWKALGVPSDMVDKARNEKPEFTFELEGNKMTIKMVSSLKTKTTTFTFGEEFKDETFDNRTVMSTVTKDSENKITQVQKGPEHTTHIVREVTGDKMVITITVGDVKAVNTLRKM", "text": "SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MLIAQRPTLSEETVDEFRSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGASVTSIKIDNVLHEFSTIEGVKEDVTEVILNLKGLVVSSEHDEPVTMYLRKSGAGDVTAADIAPPAGVEVHNPDLKIATLSDKGKLEMELVVERGRGYVSAVQNKGADNEIGRMPVDSIYSPVLKVTYKVEATRVEQRTDFDKLVIDVETKPSIRPRDAIASAGKTLVELFGLARELNVEAEGIDIGPSPVDEQLAADLALPVEDLQLTVRSYNCLKREGIHTVGELISRSEQDLLDIRNFGAKSIDEVKAKLVEMGLSLKDSAPGFDPHAALAAYGDDDDDAFVEDEQY", "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": "MTLPSGHPKSRLIKKFTALGPYIREGKCEDNRFFFDCLAVCVNVKPAPEVREFWGWWMELEAQESRFTYSYQFGLFDKAGDWTSVPVKDTEVVERLEHTLREFHEKLRELLATLNLKLEPADDFRDEPVKLTA", "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": "MGGKHVAVLLGGFSSERPVSLSSGNACALALEGEGYKVTRVDVGRDVAAVLDELRPDVAFNALHGPFGEDGTIQGILEYLAIPYTHSGVLASALAMDKAQAKKVAAAAGIPVAGERVMNRFDFTSEHPLQPPYVVKPVREGSSFGVVIVKEDQSHPPQILTSSEWPFGNQVMVERYIHGRELTCGVLDGEALGVTEVVPLGHNFYDYDAKYAAGGSKHVIPAGISPKIYQKIQTLAVMAHQAIGCRGVSRSDFRYDDRFSEDGEVIWLEVNTQPGMTPTSLVPEMAAHAGRSFGDLVSWMVEDASCLR", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MRTFSGKRSTLALAIAGVTAMSGFMAMPEARAEGFIDDSTLTGGIYYWQRERDRKDVTDGDKYKTNLSHSTWNANLDFQSGYAADMFGLDIAAFTAIEMAENGDSSHPNEIAFSKSNKAYDEDWSGDKSGISLYKAAAKFKYGPVWARAGYIQPTGQTLLAPHWSFMPGTYQGAEAGANFDYGDAGALSFSYMWTNEYKAPWHLEMDEFYQNDKTTKVDYLHSFGAKYDFKNNFVLEAAFGQAEGYIDQYFAKASYKFDIAGSPLTTSYQFYGTRDKVDDRSVNDLYDGTAWLQALTFGYRAADVVDLRLEGTWVKADGQQGYFLQRMTPTYASSNGRLDIWWDNRSDFNANGEKAVFFGAMYDLKNWNLPGFAIGASYVYAWDAKPATWQSNPDAYYDKNRTIEESAYSLDAVYTIQDGRAKGTMFKLHFTEYDNHSDIPSWGGGYGNIFQDERDVKFMVIAPFTIF", "text": "FUNCTION: Involved in the uptake of chitosugars. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane porin (Opr) (TC 1.B.25) family."}
{"protein": "MDRFPRSDSIVQPRAGLQTYMAQVYGWMTVGLLLTAFVAWYAANSAAVMELLFTNRVFLIGLIIAQLALVIVLSAMIQKLSAGVTTMLFMLYSALTGLTLSSIFIVYTAASIASTFVVTAGMFGAMSLYGYTTKRDLSGFGNMLFMALIGIVLASLVNFWLKSEALMWAVTYIGVIVFVGLTAYDTQKLKNMGEQIDTRDTSNLRKYSILGALTLYLDFINLFLMLLRIFGNRR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family."}
{"protein": "MPLTPPPDFTKVYLSAALGVSLALVVWLLIRSTLPVVGDRDHNLPHGGWYRDGTKSVFYNSPGRLNSIEARKAPLLGQPWAIVVLLVLLIWASHKLGRPNCRACAGSHT", "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": "MPVTLEVSNHVAYVTLNRPEAMNSLDPESTADLTEIWARVRTDPDIRVAVLTGAGEKSFCTGTDMKKSPPPTECMAATYLRDGQPILPHMKMWKPIIAAINGYAVGGGLEIALACDLRIASTNAKFGLTEVKVASLAGLNGTQALPRAIPQAVAMKMLLTGEMISAEEALRYGLVSDVVEPSALADLARSYAEKIASAAPLSVQATKQAAVLGKDMPLEHGILYSHLLWGVLRDTEDRKEGFKAFGERRAPAFRGA", "text": "FUNCTION: Involved in an anaerobic toluene degradation pathway (PubMed:34601806). Catalyzes the hydration of (E)-2- benzylidenesuccinyl-CoA to the corresponding alcohol intermediate, 2- (alpha-hydroxybenzyl)succinyl-CoA (PubMed:34601806). Also accepts the N-acetylcysteamine (NAC) thioester of (E)-benzylidenesuccinate (PubMed:34601806). SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MAAPRLPQLPPHDGPMLSVVDMHTGGEPLRIVLSGAPAPEGRTILEKRRWVRENADWLRKVLMFEPRGHRDMYGALLVPGDEEEANIGVLFMHNEGYSTMCGHAIVALGRFAVDYGLVNAAQGPETAVNIQCPCGLIRAYVSYTGGRSGSVRFRSVPAFAFATDVTVDVPGYGKVVVDIAYGGAFYAFVSAETFGLDVCSSRTRDLVDVSAAVTESVKAQVKLNHPDSDDLAFLYGTILTDGKDSYSEEPTANICIFAESQVDRSPTGSGVTARIALQYHKGLIQLEQIRTFKSGATGSLFTGKAVKETLCGNFKAVVVEVSGQAYYTGASSFVIENKDSLKDGFLLK", "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": "MADDKGTDPKEGCSDFIYLEAECSDISDLDNDLETLLEEGAGSDISDLINDEVVEQGNSRELLCQQEREESELQVQYLKRKCFSPKAVQELSPRLQSMNISSEHKSKRRLFVEQDSGLELSLNEAEDSTQELEVPASAPAPAAEGDIGLGTVRDLLRSSNSRATLLSKFKDSFGVSFTELTRQYKSNKTCCHHWVLAVYAAKDDLIDASKQLLQQHCFYIWLQSFCPMSLYLCCFNVGKSRDTVVRLIATLLQVHENHILSEPPKNRSIPAALFWYKGSLNSNVFCFGEAPDWILSQTMIQHQTADTLQFDLSRMIQWAYDNDHIDESIIAYQYAKLADIDSNAKAFLAHNSQVKYVKECALMVRYYKRGEMKEMSISAWIHHCISKVEGEGNWQHIVRFIRYQNLNFIMFLDKFRTFLKNLPKKNCLLIYGPPDTGKSMFAMSLIKLLKGSVVSFANSKSQFWLQPLADGKIGLLDDATDVCWQYIDSFLRNGLDGNLVSLDIKHKAPCQMKFPPLIITSNINLLKEERYRFLHSRVTQIDFPNKFPFDSDNKPLFELTDQSWASFFKRLWTQLELSDQEDEGDNGNSQRTFHCTAREVNGHI", "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": "MEKYEKLEKVGEGTYGKVYKAMEKTTGKLVALKKTRLEMDEEGIPPTALREISLLQMLSQSIYIVRLLCVEHVIQSKDSTVSHSPKSNLYLVFEYLDTDLKKFIDSHRKGSNPRPLEASLVQRFMFQLFKGVAHCHSHGVLHRDLKPQNLLLDKDKGILKIADLGLSRAFTVPLKAYTHEIVTLWYRAPEVLLGSTHYSTAVDIWSVGCIFAEMIRRQALFPGDSEFQQLLHIFRLLGTPTEQQWPGVMALRDWHVYPKWEPQDLSRAVPSLSPEGIDLLTQMLKYNPAERISAKAALDHPYFDSLDKSQF", "text": "FUNCTION: Together with CDKB1-1, promotes both the last division in the stomatal cell lineage as well as the number of stomata (PubMed:20675570). In collaboration with MYB124 and MYB88, restrict the G1/S transition and chloroplast and nuclear number during stomatal formation, and normally maintain fate and developmental progression throughout the stomatal cell lineage (PubMed:24123248). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MKSLFVAGTGTDLGKTHVACALLEAARAGGLSVDAFKPVVSGFDPDAPDDSDPARLARALGRPEAWTDVSPRRYRAPLAPNIAARLEGDTLQMDDLITDCREWLIGRDVGLALIEGAGGVMSPMTDEATNLDLMVALGLPVLLVAGSYLGTASHLLTALEVLRARGLSIAAIVVSESLDAPDLDQTLGLLRAFEHQATILSAPRAGNWDAGSLVDLLMA", "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": "MNNYFSMEAFDYDDIQLVPNKAIVNSRKECVTSVKFGNRTFKIPVVPANMESVIDEKLAVWLAQNGYYYVMHRFQPEKRADFIKMMHEKGLFASISVGIKDDEYDFIDELVEKDLIPEYTTIDVAHGHSVYVIDMIKYIKEKMPDTFLTAGNVATPEAVRELENAGADATKVGVGPGKACITKLKTGFGTGGWQLAALRMCSKVARKPLIADGGIRHNGDIAKSVRFGASMVMIGSMLAGHEESPGNVIKIDGKTYKQYWGSASEVQKGAYRNVEGKQMLVPYRGSIANTLEEMKEDLQSSISYAGGRDLESIKRVDYVIVKNTIMNGDY", "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": "MAAAEPDADPKAAIPVDLRRERRLVCVEYPGVVRNEAKMLQTLGGEESVSRIYTDPTKRLELYFRPKDPYCHPVCANRFSTSSLLLRIRKRTRRRRGVLGDEAHPQVTFNLEIIGIISTIYKFQGMSDFQYLAVHTEAGGKHVSMYDRVLMRKPEKEEFFHQELPLYIPPPIFSRLDTPVDYFYRPETQHREGYHNPTISGENLIGLSRARRPHNAIFVNFEDTEVPEQPLEAAVQTWKKACTNPIDQKVEEELRKLFDIRPVWSRNAVKSNVSVHPDKLKILLPYMAYYMITGPWRSLWIRFGYDPRKHPDAKIYQVLDFRIRCGMKYGYGSRDMPVKAKRSTYNYSLPITVKKTSNQPGTMHDLKQGLGPSGTDGPRKLTYNKYKLKDSVYIFREGALPPYRQMFYQLCDLNVEELQKIVHRNDGTETVCTERDGWCLPKTTDHLRDTMSLMILQTIRSERPALFSNTGKADRGKEQLMFESGEEEEEEEEEEEEEEEDFKPSDGSENEMETEILDYV", "text": "FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIIC subunit 5 family."}
{"protein": "MFVTAYFAVISLLALCVGLELTARRLTPPESSAAVNPAFRRFQATFLRAYLLALWADWLQGPYLYKLYRHYSFLESQIAILYVCGLASCVLFAPFSGWLSQALGRRHMCIFFCLSYATCCLTKLSRDYFVLIVGRILGGLSTSLLTTTFESWYVHHHVEIHDFPKEWIPTTFTKAATWNHGLAVGAGLVANLLAEWLHLGPVAPFLLAVPFLACCAWFVLTDWAKEEAEKSPEGIKQTLPLGTLNGGVTHLSARARFSRSCSDGLRCMLSDKRVMLLGGVQALFESVLYIFIFLWTPVLDPHGSPLGIVFSCFMAASMVGSLLFRVATSTRYHLQPGHVLCVAVLMAFFSFFMLTFSTVPGQPRPHESFLAFLLLELACGLYFPALNFLQGRIIPEEKRASVLAWFRLPLHLLACLGLLALHGEVSGTGAGETGSGTRHMFGGCAVMMLAALMAVVSLFTLGRNDTDLKLEGSRGEGEMY", "text": "FUNCTION: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "DRICTGITSSNSPHVVKTATQGEVNVTGVIPLTTTPTKSHFANLKGTKTRGKLCPKCLNCTDLDVALGRPKCTGTIPSAKASILHEVKPVTSGCFPIMHDRTKXRQLPNLLRGYEHIRLSTHNVINAEKAPGGPYKIGTSGSCPNVTNGNGFFATMAWAVPKNDNNKTATNSLTVEVPYICTEGEDQITVWGFHSDNETQMVKLYGDSKPQKFTSSANGVTTHYVSQIGGFPNQAEDGGLPQSGRIVVDYMVQKSGKTGTITYQRGILLPQKVWCASGRSKVIKGSLPLIGEADCLHEKYGGLNKSKPYYTGEHAKAIGNCPIWVKTPLKLANGTKYRPPAKLLKER", "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": "MLSLKEFNTFGLSAYAKRLDIAESAESLLALWQKAKSEKQPVLLLGGGSNVLFTTNFEGTVILNRIMGIQQRETDESWHLHVGAGENWHELVCHSLKNQIYGLENLALIPGCSGAAPIQNIGAYGIEFRDVCEYVDVLNLETGEQTRLSVGECQFRYRDSIFKHKYKANHSIISVGLLLKKNWQPILNYGNLTRLSKDNVTPQQIFDSVCAMRTSKLPDPAITGNAGSFFKNPIVSAEVAAKIKENYPDSPQYSYTNGMFKLAAAWLIERCNLKGYRIGGASVHLRQALVLINQENATGKDVVLLAAYIRRQVISKFGVLLEPEVRFIGSKGEIDAVECIS", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
{"protein": "MTNIRKSHPLLKIINNSFIDLPAPSNISSWWNFGSLLGICLALQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWVLRYLHANGASMFFICLYLHVGRGLYYGSYMYTETWNIGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFAFHFLLPFIIAAMVMVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGLLLMIMALLTLVLFSPDMLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILAIIPLLHTSKQRSMIFRPLSQCLFWLLVADLLTLTWIGGQPVEHPYVIIGQLASILYFSIIIILMPLTSLVENYLLKW", "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": "MQIKWFGHAAFMVEVGGARLLIDPWISNPLSPATPQDVINARPTHIMITHDHFDHMGEAVDIAKATKAPIVGTFELTLEVAEKGIPEAQTMPMNIGGTIKLGDGIELYMTPALHTANRGAPSGFVIATPEGTVYHAGDTALFRDMELIGELYDIDVALLPIGSVFTMGPREAAIATQLLRARRVVPMHYNTFPLIKQDPEDFKARVEAVSRAKVFVMKPGDVLKV", "text": "SIMILARITY: Belongs to the UPF0173 family."}
{"protein": "MPEHEERHSHGVNRSLSLGSSMRSLFKSQRSRGPSDRGANGTPGPAQKVDIRVDTASASREHTPVVHKTPQSANPELQQPRHHLGLPNILKLNLTPTNSNPQSKSGSPVSQNTSQESLITDTDIEVEDYRPSKDSRRTVRNASPMSSNGNLPINANTVIGPDTSSNNIDSMLDGTGLRPFYEEADSSDYIENLRSFPLPTGHYAPGFIQPPKSPTSSRVPSRSNSRKGREHAGTVSAAQLPRYNETPGKCILDLEYFKLYEDGHHVHTLKVMTSVNSDANGNSHNHASKNDGHLDLPKGDDGSVVRQKSKFSLSGFFKPHSKEDIANADEKLKYAVSLLPRNKICSKVETDRDTFAPVFTKTRSHVQSGSDDSSDDDEELDDPSIPKIVNKNAAVGSQELKLINNLSEKIRMGLSTAAKNKHNQSSKHRTPSGAGVQDENQPAFADLYGKCVAVVGHGAYGVVKVCARTRDEKDDLPATKTYMDSKKIYFAVKELKPRPSDPIEKFSTRITSEFIIGHSLSHYYDKNGEQSAPNILSIIDLLEYNDTFIEVMEFCPAGDLYSLLTARKNKIGKPLHPLEADCFMKQLLKGIQFMHDHGVAHCDLKPENILLHPNGLLKICDFGTSCVFQTAWERHVHFQTGLQGSEPYVAPEEYNPKKEYDPRLVDCWSIGIVYCTMIMGHYLWRNAARGKDSLYDSFYEEMASKKEFYVFEELRHINQEINRLRRIALYQIFQPNPEKRISIDKLLQTGWMRHTKCCVPYKNIPR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NPR/HAL subfamily. HAL5 sub-subfamily."}
{"protein": "MSSAIKILALLMVLVALAQAKPRKDYRAYPDFDDKSVILEDDKRCDPDKRDSVCKDVCGMLDIGTENGECPGKEVCCVDLFGR", "text": "FUNCTION: In vivo, induces immediate paralysis on shrimps (C.multidentata), followed by death when high doses are injected. No activity is observed when injected into fly larvae (M. domestica). SUBCELLULAR LOCATION: Secreted Nematocyst."}
{"protein": "MAEKKEPAEGWPILKGEYEVGDPNNCVAVITCGSHLEGQPMLDAGASIVGPCKTENLGLEKVVSHIISNPNIRYLIVTGAEVKGHITGEAMMMLHKNGVKDNRIVGATGAIPYVENLTEESVERLQQQLEECVDLLGTEDLNTITSKIKELAEKDPGAFDAEPMIIQLEEEEEEEEEGGIKPMSAEIATIQARIRNIEKDMINAGEMNKLHSGVLAGKIEGIMVGLVLSLFVLGLLLFGGM", "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": "MAGEQTTTEYISHHLTNWTYGYLPGEGWKVAYNAEEASAMGFKAIHLDSMLWSIGLGIVFCAIFWMVARKVTSGVPGKTQAAVEMIVEFVDNNVRDSYSGTSKLIAPLALTIFVWIFLMNLMDLLPVDFIPMIAGQIGALMGHDPHHVYFKIVPTTDPNITLGMSFSVFILILFYSIKEKGLGGFVGELTLHPFSAKNPIVQIILIPINFILEFVTLIAKPISLGLRLFGNMYAGELIFILIALMPFWIQWALSVPWAIFHILIITLQAFVFMMLTIVYMSLASSTEH", "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": "MALAVADTQNETFARSESPTSGPSDQLSTHDLDRHIEKLMRCELIAEQDVKTLCAKAREILAEEGNVQVIDSPVTICGDIHGQFYDLMELFRVGGPVPNTNYLFLGDFVDRGFYSVETFLLLLALKARYPDRMMLIRGNHESRQITQVYGFYDECMRKYGNASVWKHCTEVFDYLALAAVIDGKVFCVHGGLSPSISTMDQIRVIDRKQEVPHDGPMCDLLWSDPEEGNVGWGLSPRGAGYLFGADASKTFCEANSVDLICRAHQLVMEGYKWHFNEKVLTVWSAPNYCYRCGNVAAILELDENLNREFTIFEAAPQENRGAPAKKPHADYFL", "text": "FUNCTION: Protein phosphatase which plays an essential role in meiosis and in early embryonic mitosis. During spermatocyte meiosis and the first embryonic mitosis, regulates centrosome maturation, and thus spindle formation, by recruiting some of the components of the pericentriolar material (PCM). During oocyte meiosis I, regulates meiotic chromosome dynamics including synapsis-independent chromosome pairing, restriction of synapsis to homologous chromosomes, programmed DNA double-strand break initiation and crossover formation resulting in chiasma formation. During oocyte meiosis II and probably together with regulatory subunit ppfr-1, may regulate microtubule severing by dephosphorylating and activating mei-1, a component of the katanin microtubule severing complex. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes at centrosomes from prophase to telophase but not during interphase. Also localizes to the cytoplasm throughout the cell cycle. SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily."}
{"protein": "MNDVRKILLRISYDGTRFCGWQKQVSGSRERAPSVQGELEKVAEKIHHQKIAVIGSGRTDSGVHAVGQAAHFCTPMRNILAYRFIPAFNSLLPHSIRITDAREVSSQLHARFSAVMRTYRYHLHCAPVAYAHELPYCWHIARMPDIHLLNQYAATLKGELDCTSFAAAGDKSASKSRYFYDTHFSFNHRVLTFEISANAFLWKMVRSLTGTLLHCEKKRCSVREFVRILHAKDRRLQGPPHRRMGYSYGTSVTPNTYSVQNRNTLARELASTGNARWKTY", "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": "MPALPLDQLQITHKDPKTGQPKTSAALNPEQKADRYFVLYKPPPKDNIPALVEEYLERANFVANDLDWLLALPHDKFWCQVIFDETLQKCLDSYLHYVPRKFDEWVAPTPEVADMQNHLHRSVFLTFLRMSTHKESKDHFISPSAFGEILYNNFLFDIPKILDLCVLFGKGNSPLLQKMIGNIFTQQPSYYTDLDETIPTILQVFSNILQHCGLQGDGTSTTPQKLGERSPLTPSDMPLLELKDIVLYLCDTSTTLWAFLDIFPLACQTFQKHDFCYRLASFYEMAIPELESAIKKRRLEDSKLLGDMWQRLSHSKKKLMEVFHIILNQICLLPILESSCDNIQGFIEEFLQIFSSLLQEKRFLRDYDTFSPVAEDISLLQQASSALDETRTAYILQAVESAWEGVDRQKIKDIKDPPRAKGSNNEVTVTAEPVSEMPSQLENLEEDEECMGAAAALGPAVSGVELDSLISQVKDLLPDLGEGFILACLEHYSYDSEQVINNILEDRLAPELSQLDRGLERQVKPDPTPLLSSRHNIFQNDEFDVFSRDSVDLSRVHKGRRKEENVRSLVNDKQAVVAQWQRYQKYSVVVEEVPLQPGEYQADDYEDEYDDTYDGNQVGANDADSDDELISRRPFTIPQVLRTKMPGEVQEEEWDEEDEVEEEAPKPDHFIQDPAVLREKAEARRMAFLARKGYRPENSTAVTGGPRGHGQSRETTQERRKKEANKAARANHNRRTMADRKRSKGMIPS", "text": "FUNCTION: Ubiquitin-binding protein involved in DNA repair and rescue of stalled ribosomes. Plays a role in DNA damage repair as component of the ASCC complex. Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains. Part of the ASC-1 complex that enhances NF-kappa- B, SRF and AP1 transactivation. Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation. Specifically recognizes and binds RPS20/uS10 ubiquitinated by ZNF598, promoting recruitment of the RQT (ribosome quality control trigger) complex on stalled ribosomes, followed by disassembly of stalled ribosomes. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Note=Colocalizes with the spliceosomal components PRPF8 and SNRNP200/BRR2 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. Colocalizes with RNF113A and 'Lys-63'-linked polyubiquitinated proteins, ALKBH3 and ASCC3 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. SIMILARITY: Belongs to the ASCC2 family."}
{"protein": "MRGCLQLARWLSAAPKGTAASLTRAPFVLANAPRFFTSSASHAGSRSTATKPVSDLENRIAAIPIERYRNFCIVAHVDHGKSTLSDRLLELTGTIEPGSNKQVLDKLDVERERGITVKAQTCSMIYNHNGEDYLLHLVDTPGHVDFRAEVSRSYASCGGALLLVDASQGIQAQTVANFYLAFAQGLELIPVINKVDLPSAEPERALEQMKNSFELDTENAVMVSAKTGLNVEKLLPTVIEKIPAYGYFPVYLHKLFPLLTLTSPIGDCKKPLRMLLVDSWYDSYKGVICLVRIFDGEIRAGQQVVSFATGLKYYVGEVGIMYPNETPQSVLRAGQVGYIYFNPGMKRSKEAKIGDTFTRVGFEKAVEPLPGFEEPKSMVFVAAYPVDADHFEHLEDSINQLVLNDRSITVQKESSEALGAGFRLGFLGTLHCSVFEDRLRQEHGASIIITPPSVPVKIIWKDGKEEIITSPAKFPEDEELRSKVAEIQEPYVLATLTFPEEYLGKVIELCEANRGEQKSLEYFTATQVILKYELPLAQLVDDFFGKLKGSTKGYASLDYEESAWQTGNIVKLQLLVNKAPVDAVARIVHLSQVERLGRQWVTKFKEHVDRQLFEVVIQAAVGKKIIARETVKPYRKDVLAKLHASDVSRRRKLLEKQKEGRKRLRAVGNVVIEHKAFQAFLAK", "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": "MLKFREWSKEFFGRKLTIQYGKVAKQSSGAAWVQFGDSVVLATANISDRVIEGVDFVPLTVEYQEKFYAAGKIPGGFIKREGKPTESAILSARLIDRPIRPLFPKYLRNDVQLIVTVLSVDGDTPPDVTGIFAASLALNFSKIPFQGIVAGVRIGYVDGEFVIFPTEEQLKNSKLDIVVAGSKDAITMVEGEAKEVTEEEMVQALMVAHEAIKKLIEFEEEILREFNVEKMEIEEPKPKDELIGRFEELLVENELRKRLLIKEKLERSLKLKEYKEELISKIFEEFEIDDEEKLTQEMLLKELFDEKAKKLMRKIIINEGIRADGRTPEEIRPITCEVGVLPRTHGSALFTRGETQSLGIVTLGAPMEEQIVDTIMEEGTKRFILHYNFPPFSVGEVKPLRGPGRREIGHGHLAERALKAVAPDEEDFPYVVRVVSEILESNGSSSMATVCSGSLALMDAGVPIKTHVAGVAMGLIVDEENEVVLTDIQGLEDHWGDMDFKVAGTRNGITAFQMDCKIAGVGEELLKKALKQARVARMRILDIMFETIKEPRKSLSPYAPLIANIEIDPMKVGELIGPGGKVIKSIVKEFDVEISIDDVTGKVSVYGKDQNKVNQAIEYIKTLTREIEVGDMFEGKITRIEPYGLFVELMPGKIGLAHSSKLGNDSKEFRKKYKVGDVIKVVVVNIDDSGRIQLGKAEE", "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": "MYSGNKVVISWIVSIGFVGMPEFMSSKTFALCRQRSFLHGPAGIRSDEEKENNFFGRVSFMDAALLLEYGWVLLVLIGLEGILAADNALVMAVMVKHLPEEKRKKALFYGLAGAFVLRFGSLFAISFLVNVWQVQAIGAIYLLYISASHLLKRYVFKKEDTHKETKQSGFWPTVLKVELADIAFAVDSILAAVALAVTLPGTSLPKIGGLDGGQFLVILAGGIIGLVIMRFAASMFVKLLKERPSLETAAFVIVGWVGVKLALYTLAHRDIAVVSEHFIHSGTWKLIFWGVLAAIAVCGWFMSGGKKQPEGAQNEQKNSTRERA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TerC family."}
{"protein": "MGYVVSTFYRFVHLSNYYDIQPVLKEFCVQHSIKGTIILAEQGINATIAADKQSSLDEFFSFLNLDDRLKDIRYHKSFAMHNPFSKMKVKLRKELVCLGIEDFDNSVCGEYVSPQDWDDLISRSDVYTIDTRNTYEINFGKFKNAINPQTKCFRDFPEWAISWASNKVDQDPIIAMYCTGGIRCEKSTAFMKDLGFSKVYHLKGGILEYFKSTQNKNSLWEGDCFTFDDRIAVDNKLVPAHVKCVSCDVCVTPEEMKSITRGHVLCFNCKENVKI", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family."}
{"protein": "DILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYRXXRVIGEKDQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRXLRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEDMNKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKSHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDLVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREACKWSPELAAACEVWKEIRFEFKPVDTLDPDEKK", "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": "MSPECARAAGDAPLRSLEQANRTRFSFFSDVKGDHRLLLAAVETTVLALIFAVSLLGNVCALVLVARRRRRGTTACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYLMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLTLIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIAGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSVISG", "text": "FUNCTION: G-protein-coupled receptor for long-chain fatty acids (LCFAs) with a major role in adipogenesis, energy metabolism and inflammation. Signals via G-protein and beta-arrestin pathways. LCFAs sensing initiates activation of phosphoinositidase C-linked G proteins GNAQ and GNA11 (G(q)/G(11)), inducing a variety of cellular responses via second messenger pathways such as intracellular calcium mobilization, modulation of cyclic adenosine monophosphate (cAMP) production, and mitogen-activated protein kinases (MAPKs). After LCFAs binding, associates with beta-arrestin ARRB2 that acts as an adapter protein coupling the receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis (By similarity). In response to dietary fats, plays an important role in the regulation of adipocyte proliferation and differentiation. Acts as a receptor for omega-3 polyunsaturated fatty acids (PUFAs) at primary cilium of perivascular preadipocytes, initiating an adipogenic program via cAMP and CTCF- dependent chromatin remodeling that ultimately results in transcriptional activation of adipogenic genes and cell cycle entry. Induces differentiation of brown and beige adipocytes probably via autocrine and endocrine functions of FGF21 hormone. Contributes to the thermogenic activation of brown adipose tissue and the browning of white adipose tissue. Activates brown adipocytes by initiating intracellular calcium signaling leading to mitochondrial depolarization and fission, and overall increased mitochondrial respiration. Consequently stimulates fatty acid uptake and oxidation in mitochondria together with UCP1-mediated thermogenic respiration, eventually reducing fat mass. Regulates bi-potential differentiation of bone marrow mesenchymal stem cells toward osteoblasts or adipocytes likely by up-regulating distinct integrins. In response to dietary fats regulates hormone secretion and appetite. Stimulates GIP and GLP1 secretion from enteroendocrine cells as well as GCG secretion in pancreatic alpha cells, thereby playing a role in the regulation of blood glucose levels. Negatively regulates glucose-induced SST secretion in pancreatic delta cells. Mediates LCFAs inhibition of GHRL secretion, an appetite-controlling hormone. In taste buds, contributes to sensing of dietary fatty acids by the gustatory system. During the inflammatory response, promotes anti-inflammatory M2 macrophage differentiation in adipose tissue (By similarity). Mediates the anti- inflammatory effects of omega-3 PUFAs via inhibition of NLRP3 inflammasome activation (By similarity). In this pathway, interacts with adapter protein ARRB2 and inhibits the priming step triggered by Toll-like receptors (TLRs) at the level of TAK1 and TAB1 (By similarity). Further inhibits the activation step when ARRB2 directly associates with NLRP3, leading to inhibition of pro-inflammatory cytokine release (By similarity). Mediates LCFAs anti-apoptotic effects (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Cell projection, cilium membrane; Multi-pass membrane protein Note=Sorted to late endosome/lysosome compartments upon internalization (By similarity). Specifically localizes to the primary cilium of undifferentiated adipocytes. Ciliary trafficking is TULP3- dependent. As the cilium is lost during adipogenesis, moves to the plasma membrane (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MWSRMNRAAEEFYARLRQEFNEEKKGASKDPFIYEADVQVQLISKGQPSLLKTILNENDSVFLVEKVVLEKEETSQVEELQSEETAISDLSAGENIRPLALPVGRARQLIGLYTMAHNPNMTHLKIKQPVTALPPLWVRCDGSDPEGTCWLGAELITTNDIIAGVILYVLTCKADKNYSEDLENLKTSHKKRHHVSAVTARGFAQYELFKSDDLDDTVAPSQTTVTLDLSWSPVDEMLQTPPLSSTAALNIRVQSGESRGCLSHLHRELKFLLVLADGIRTGVTEWLEPLETKSALEFVQEFLNDLNKLDEFDDSTKKDKQKEAVNHDAAAVVRSMLLTVRGDLDFAEQLWCRMSSSVVSYQDLVKCFTLILQSLQRGDIQPWLHSGSNSLLSKLIHQSYHGAMDSVPLSGTTPLQMLLEIGLDKLKKDYISFFVSQELASLNHLEYFISPSVSTQEQVCRVQKLHHILEILVICMLFIKPQHELLFSLTQSCIKYYKQNPLDEQHIFQLPVRPAAVKNLYQSEKPQKWRVELSNSQKRVKTVWQLSDSSPVDHSSFHRPEFPELTLNGSLEERTAFVNMLTCSQVHFK", "text": "FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (By similarity). SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the ZWILCH family."}
{"protein": "MPPKPADKKPASKAPATASKAPEKKDAGKKTAASGDKKKRTKARKETYSSYIYKVLKQVHPDTGISNRAMSILNSFVNDIFERVATEASKLAAYNKKSTISSREIQTSVRLILPGELAKHAVSEGTKAVTKYSSSTK", "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": "MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF", "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": "MDVLLGRDETMDESDYLHVNNTCAPSLGLSIARDAETAINTVIILIGGPMNFVVLTTQLLSNRIYRSSAPTLYMTNLYFANLLTVTMLPFLILSNRGQISSSPEGCKLVAVTYYASCTAGFSTLALISVNRYRVIHQSTNKNAAGSKKKTYGVLALVWLTSLMCASPAPTYVTVLAHDGDTPDSVHETCIIFFNYDQVKTVLATFKILICIVWGVMPVVMMTWFYLFFYKRLKLTSYRRRSHTLAFVSTLILSFLVLQTPFVGIMIFDSYAVIEWDVTCESINSRDAVAMLARVVPNFHCMLNPVLYAFLGRDFNKRFMQCITGKLFSRRRMLQERAGVRSPSTPHRAARQLAKIGTLTRSCSRSELQRSASAPPPQ", "text": "FUNCTION: Plays an important role in vivo, in particular in the dissemination to or replication in the salivary gland. SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MADNEKNSCSCSFCGKIHSEVRKLIAGPSVFICNECIDLCSGILQEESRSYKKTDTLKLKPKEIKKVLDEYVIGQEHSKKVLSVAVYNHYKRLSNLSVISEVEISKSNVLLIGPTGSGKTLLARTLARVLQVPFAMADATTLTEAGYVGEDVENILLKLLQAANFNVDAAQRGIIYIDEVDKISRKSENTSITRDVSGEGVQQALLKVIEGTVSSVPPQGGRKHPHQEFIQINTDNILFIFGGAFDGLDKIIESRHRGSSMGFEANVQKVSKNKDIFCYTEPEDLVKFGLIPEFVGRIPVITSLGELDESTLCRILVEPKNSLVKQYKKLFEMDNINLQFDDSALSVIAKKAAVRKTGARGLRAILEALLLDLMFESPGSSDVNQVVISKEMVEELMVSSHLFLKH", "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": "MVVEDALKTSASEDQAKTETNPKPREEDDEPEEGEIVGDEESASKPSKGIAPESHALEHSWTFWFDSPAAKSAKTKQEDWGSSIRPIYTFSTVEEFWSIYNNIRHPSKLAIGTDFHCFKYKIEPKWEDPVCANGGKWTVTLPKGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKISIWTKNAINEAAQLSIGKQWKGLLDYNETIGFIFHEDAMRHERSAKNKYVV", "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). FUNCTION: (Microbial infection) Not involved in the plum pox virus (PPV) strain D infection process. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family."}
{"protein": "MSLISRLRAVVAGDDYLDGDFDELDYETGDDFDTGNDGGGNYSSGLAALSNANPFNNRGGSSKVIGMPGISTAAAEVSLMEPRSFDEMPKAIQALRERKTVILNLTMMEPDQAQRAVDFVAGGTFAIDGHQERVGESIFLFAPSCVTVTNSFQEEPSPSSVMNKDNEGPVSESVMAPEPAWGASVPSAI", "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": "MGRVGVLLLNLGGPDKLEDVGPFLFNLFSDPEIIRLPFRWLQKPLAWFIASRRTKTSQENYKQIGGGSPLRRITEAQGEALKEQLHDLGQEANIYVGMRYWHPYTEEAIALLTQDNLDNLVILPLYPQFSISTSGSSFRLLERLWQEDPKLQRLDYTVIPSWYKEPCYLQAMAELISQEVDQFPDPDQVHVFFSAHGVPKSYVEEAGDPYQQEIEECTALIMQTLNRPNPHTLAYQSRVGPVEWLQPYTEDALKELGAQGVKDLVVVPISFVSEHIETLQEIDIEYREIAEEAGIHNFRRVAAPNTHPVFIRALANLVIDALNKPSFKLSQAAQIKKMVKMYPPESWEWGMTSSAEVWNGRIAMLGFIALIIELVTGQGLLHMIGLLQ", "text": "FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferrochelatase family."}
{"protein": "MFTVFLLVVLATAVVSFTSDRASDDGKAAASDLITLTIKGCCSRPPCIANNPDLCG", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits rat alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=3.5 nM), rat alpha-7/CHRNA7 (IC(50)=392 nM) nAChR, and the L.stagnalis soluble acetylcholine receptor (all tested without hydroxyproline). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
{"protein": "MYTDLKDKVVVITGGSTGLGRAMAVRFGQEEAKVVINYYNNEEEALDAKKEVEEAGGQAIIVQGDVTKEEDVVNLVQTAIKEFGTLDVMINNAGVENPVPSHELSLDNWNKVIDTNLTGAFLGSREAIKYFVENDIKGNVINMSSVHEMIPWPLFVHYAASKGGMKLMTETLALEYAPKGIRVNNIGPGAMNTPINAEKFADPVQRADVESMIPMGYIGKPEEVAAVAAFLASSQASYVTGITLFADGGMTKYPSFQAGRG", "text": "SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MANQPSIAERRTKVWEPYIRAKLGFRNHWYPVRLASEIAEGTPVPVKLLGEKILLNRVGGKVYAIQDRCLHRGVTLSDRVECYSKNTISCWYHGWTYRWDDGRLVDILTNPGSVQIGRRALKTFPVEEAKGLIFVYVGDGEPTPLIEDVPPGFLDENRAIHGQHRLVASNWRLGAENGFDAGHVLIHKNSILVKGNDIILPLGFAPGDPDQLTRSEVAAGKPKGVYDLLGEHSVPVFEGMIEGKPAIHGNIGSKRVAISISIWLPGVLKVEPWPDPELTQFEWYVPVDETSHLYFQTLGKVVTSKEAADSFEREFHEKWVGLALNGFNDDDIMARESMEPFYTDDRGWSEEILFEPDRAIIEWRGLASQHNRGIQEAR", "text": "FUNCTION: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Catalyzes the dioxygenation at the angular (C-9a) and adjacent (C-1) positions of carbazole to yield a highly unstable cis-hydrodiol intermediate which is spontaneously converted to 2-aminobiphenyl-2,3- diol."}
{"protein": "MKFFAVFALCVASVSAANLDAIAKPGFPAGRIINGHEAEKGEAPFIVSLKAGKGHFCGGSIIAENWVLTAGHCLIFDEFEIVAGLHSRNDESDVQIRKVTGKHQQIVHEKYGGGVGPNDIGLIYVDKPFNLNALTRDGTAAVAKVNLPTGKYESTGEGKLYGWGLDNSGFSPNILNTLDVNIIGYEECKNALNSDAPLDPVNICSYTAGAIDGACNGDSGGPMVRITPDGTELVGIVSWGYQPCASTTMPSVYTWTSAFDKWIEDSIENYAQLL", "text": "FUNCTION: Protein with lectin and protease activity involved in the establishment of trypanosome infections in tsetse flies. Binds D- glucosamine and agglutinates bloodstream-form trypanosomes and rabbit red blood cells. Capable of inducing transformation of bloodstream-form trypanosomes into procyclic (midgut) forms in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MGLKHFLEKIEPHFLPGGKHEKWYALYEAAATIFYTSGAVTRKAAHVRDALDSKRMMILVWLALFPAMFYGMYNVGAQAFGALTPDLLQQNIANDWHYAFANALGINMSSEAGVSDKMLFGAIYFLPIYATVFVVGGFWEVLFATVRKHEINEGFFVTSILFALIVPPTLPLWQAALGISFGVVVAKEVFGGTGKNFMNPALAGRAFLFFAYPANLSGDAVWTAVDGYSGATALAQWAAHGADGLKNAVTGQTITWMDAFIGKLPGSIGEVSTLALLIGGAFIVFARIASWRIIAGVMIGMIAMSSLFNFIGSDTNAMFAMPWYWHLVVGGFAIGMLFMATDPVSASFTNVGKWWYGALIGVMCVLIRVVNPAYPEGMMLAILFANLFAPIFDYFVAQANIKRRKARSNG", "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": "MKKALQVAMFSLFTVIGFNAQANEHHHETMSEAQPQVISATGVVKGFDLESKKITIHHDPIAAVNWPEMTMRFTITPQTKMSGIKTGDKVAFNFVQQGNLSLLQDIKVSQ", "text": "FUNCTION: Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide (By similarity). SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MKLIVGLGNPGFEYEHTRHNIGFKIIDKLLDVLNLELNKSQFNGLYVKHDDFIIAKPLTYMNLSGNFIRQLVNFYKIQIDDILVIHDELAFNLGVVRLKQNGSANGQKGVANIISQLGTQNFKRLRVGIKNEDLKNIASFVLSKFAPNELILLESAIASASVIAYDFLKSNKSFSKLMNEYNQ", "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": "MTDYLNVGKIVNTQGIKGEVRVISKTDFPEERYQKGAMLLLFQEKKAPIELVVKSHRKHKNFDILSFEGHPNINDVEKYRDGILKVAKDNLAELAEDEFYYHQIIGATVYDETGSELGKIKEILSPGANDVWVVQRPKKKDLLLPYIEGVVTKVDVENQRIDVDIPEGLIDDEN", "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": "MARTKQTARKSTGGKAPRKQLATKAARKTPATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSQAVVALQEAAEAYLVGLFEDTNLCAITAKRVTIMPKDIQLARRIRGERA", "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": "MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR", "text": "FUNCTION: Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus (PubMed:10655584, PubMed:18559669, PubMed:18829466, PubMed:26742426, PubMed:28074573). Positively regulates MAPK signal transduction pathway (PubMed:28074573). Dephosphorylates GAB1, ARHGAP35 and EGFR (PubMed:28074573). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity (PubMed:18559669). Dephosphorylates CDC73 (PubMed:26742426). Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification (By similarity). Dephosphorylates tyrosine-phosphorylated NEDD9/CAS-L (PubMed:19275884). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class 2 subfamily."}
{"protein": "MSQQLSPINIETKKAISNARLKPLNIHYNESKPTTIQNTGKLVRINFKGGYLSGGFLPNEYVLSSLHIYWGKEDDYGSNHLIDVYKYSGEINLVHWNKKKYSSYEEAKKHDDGLIIISIFLQVSDHKNVYFQKIVNQLDSIRTANTSAPFDSVFYLDNLLPSKLDYFKYLGTTINHSADAVWIIFPTPINIHSDQLSKFRTLLSLSNHEGKPHYITENYRNPYKLNDDTEVYYSGEIIRAATTSPARENYFMRWLSDLRETCFSYYQKYIEGNKTFAIIAIVFVYILTAILFLMSRRYSREKQN", "text": "FUNCTION: Binds to chondroitin sulfate on the cell surface to provide virion attachment to target cell. SUBCELLULAR LOCATION: Virion membrane Note=Component of the mature virion (MV) membrane. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
{"protein": "MFSLQNLCRKTLPDCKLPEFFDEYILQLLGLYWENHGTIQRAGNNCVLIQQHTLIPVNEALRIAASEENYEIVSLLLAWEGNLYYAIIGALEGNRHDLIRKYDDQIKDHHEILPFIDDPVIFHKCHIMRRCFFDCILYQAVKYSKFRVLLYFKYRLENDLPLAHLLIKKACEDHNYEVIKWIYENLHIYNIMDTFGCAIAHKDLRLYRLGYTFIYNRIVPYKYHYLDVLILSGLHLLYKVAAKGYLDFILETLKYDHNNDNLDIILTQAATYNHRKILTYYIPQLTYAQIEQCLFMAIKKKSSKKTLNLLLSHLKLSIKLIKKISQYVATYNSTNIIGILNMRRKKKIYLDIILTKFVKKAIFNKFVVRCMDTFSINPERIIKMAARINKMLLVKKISEHAWKNHAARLKHLKHAVYTMKHKDGKNRLMNLIYDHYYYHMQGEEIFSLARFYAIHHAPKLFDVFYDCCLLDTIRFKNLLLDCSHIIGKNAHDATNITIVNKYIGNLFAMGVLSKKEILQDYPSIYSKHYMP", "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": "MPDRTGPLLRTPAWRALEAHLAELQPLHLRELFARDPGRGERLVADGAGLHLDYSKQRVTEETVRLLVALAEARGLPERRAAMFRGEKVNVTEGRAVLHVALRAPRGERILVDGNDVVPEVHAVLDRMAAFADQVRSGAWTGFTGKRIRTVVNVGIGGSDLGPAMAYRALRAYAIRDLAFRFVSNVDGTDLAEAVRDLDPAETLFLVASKTFTTLETMTNAASARSWLLAALGDPRAVARHFVAISTNEAEVRRFGIDPANMFGFWDWVGGRYSMDSAIGLSTMIAVGPEGFRELLAGFREMDEHFRDAPLERNLPALIGLIGVWNANLLGAGTVAVLPYDQYLDRFPAYLQQLTMESNGKRVTASGTPVEGHGTGAIYWGEPGTNGQHSFYQLLHQGTHLVACDFIGFCQPLHALGRHHDLLMANLFAQGEALAFGKTAEEARAEGTPEPLVPHRTFPGNRPSSTILSDRLTPRTLGALVALYEHAVFTQGVIWDVDSFDQWGVELGKVLANRIVKELESPAEPALAHDGSTNALIRRYRARRGG", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MPLLFLERFPWPSLRTYTGLSGLALLGTIISAYRALSQPEAGPGEPDQLTASLQPEPPAPARPSAGGPRARDVAQYLLSDSLFVWVLVNTACCVLMLVAKLIQCIVFGPLRVSERQHLKDKFWNFIFYKFIFIFGVLNVQTVEEVVMWCLWFAGLVFLHLMVQLCKDRFEYLSFSPTTPMSSHGRVLSLLVAMLLSCCGLAAVCSITGYTHGMHTLAFMAAESLLVTVRTAHVILRYVIHLWDLNHEGTWEGKGTYVYYTDFVMELTLLSLDLMHHIHMLLFGNIWLSMASLVIFMQLRYLFHEVQRRIRRHKNYLRVVGNMEARFAVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSLNIADNNRVREEHQGENLDENLVPVAAAEGRPRLNQHNHFFHFDGSRIASWLPSFSVEVMHTTNILGITQASNSQLNAMAHQIQEMFPQVPYHLVLQDLQLTRSVEITTDNILEGRIQVPFPTQRSDSIRPALNSPVERPSSDQEEGETSAQTERVPLDLSPRLEETLDFGEVEVEPSEVEDFEARGSRFSKSADERQRMLVQRKDELLQQARKRFLNKSSEDDAASESFLPSEGASSDPVTLRRRMLAAAAERRLQKQQTS", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins, such as CD3D, CYP3A4, CFTR, INSIG1, SOAT2/ACAT2 and APOB for proteasomal degradation (PubMed:10456327, PubMed:11724934, PubMed:12670940, PubMed:19103148, PubMed:24424410, PubMed:28604676). Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD) (PubMed:10456327, PubMed:11724934, PubMed:19103148, PubMed:24424410). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG1 complex at the ER membrane (PubMed:16168377, PubMed:22143767). In addition, interaction of AMFR with AUP1 facilitates interaction of AMFR with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase RNF139, leading to sterol-induced HMGCR ubiquitination (PubMed:23223569). The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction (PubMed:16168377, PubMed:22143767, PubMed:23223569). In addition to ubiquitination on lysine residues, catalyzes ubiquitination on cysteine residues: together with INSIG1, mediates polyubiquitination of SOAT2/ACAT2 at 'Cys-277', leading to its degradation when the lipid levels are low (PubMed:28604676). Catalyzes ubiquitination and subsequent degradation of INSIG1 when cells are depleted of sterols (PubMed:17043353). Mediates polyubiquitination of INSIG2 at 'Cys-215' in some tissues, leading to its degradation (PubMed:31953408). Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex (PubMed:21636303). Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation (PubMed:21636303). Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor (PubMed:10456327). In association with LMBR1L and UBAC2, negatively regulates the canonical Wnt signaling pathway in the lymphocytes by promoting the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (PubMed:31073040). Regulates NF-kappa-B and MAPK signaling pathways by mediating 'Lys-27'-linked polyubiquitination of TAB3 and promoting subsequent TAK1/MAP3K7 activation (PubMed:36593296). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Palmitoylation promotes localization to the peripheral endoplasmic reticulum."}
{"protein": "MPKMKTKSSAKKRFKITASGKVKVAAAGKRHGMIKRSNKFIRDARGTMVLSEQDAKKVIQHYLPNGL", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "MTQLAIGEATPHGATYDGHGVNFTLFSAHAERVELCVFDSRGNERRYDLPGRRGDVWHGYLAGARPGLRYGYRVHGPWQPVQGHRFNPAKLLLDPYARRVEGELKDHPLLHGGHDEPDYRDNAAVAPKSVVISDHYDWEDDAAPRTPWGKTVIYEAHVKGLTYLHPELPQEIRGTYKALGHPVMVAYFKQLGITALELLPVAQFASEPRLQRMGLTNYWGYNPMAMFALHPAWASSPEMALDEFRDAVKALHRAGIEVILDIVLNHSAELDLDGPTFSLRGIDNRSYYWIRDDGDYHNWTGCGNTLNLSHPGVVEYACECLRYWVETCHVDGFRFDLASVMGRTPTFRQDAPLFAAIKACPVLSTVKLIAEPWDIGEGGYQVGNFPPPFAEWNDHFRDAARRFWLPRNLTTGEFACRFAASSDVFKRNGRAPGASVNLLTAHDGFTLRDCVCFNQKHNEANGEENRDGTNSNYSDNNGKEGLGGPLDLMERRRDSIHALLATLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNALTWLDWQQANRGLTTFTAALIRLRQQIPALTGNSWWEEGDGNVRWLNKNAQPLSADEWQNGPKLMQILLSDRFLIAINATLEVTDIVLPEGEWRAVPPFAGEDNPVITAVWQGPAHGLCVFQRG", "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": "MSNKKADSKPQAKYPVNLLDTPFPMRGDLPKREPQWVKEWEERGVYEKIRAASKGRPKFILHDGPPYANGDIHLGHAVNKILKDIVVKSRNMAGFDAPYVPGWDCHGMPIEIQIEKQFGKSLPAAEVMSKARAYATEQIEKQKAGFKRLGVLGDWADPYKTMNFVNEAEEIRALGKIIEKGYVYRGLKPVNWCFDCGSALAEAEVEYKDRTDPTIDVMFPFAEPEKTAQAFGLPALPRAEGGIVIWTTTPWTIPANQALNLHPEIVYALVDTERGLLIVAEERVAACMEEFKLSGRVVATAPGVKLVNLRFHHPLASAHPGYKRTAPVYLGDYVTTDTGTGVVHSSPAYGVEDFISCKTHGMTDSDIINPVMGDGRYIESLPLFGGLSIWDANPKVVDALRDAGTLLRSEKYTHSYMHCWRHKTPIIYRATSQWFAGMDVTPREGGKTLRETALEGVEATAFYPSWGKQRLFSMIANRPDWTLSRQRQWGVPMAFFVHKETGELHPRTLELLEEVAKRVEKSGIEAWQTLDPRELIGDDANLYEKNRDTLDVWFDSGTTHWHVLRGSHKDQLQFPADLYLEGSDQHRGWFHSSLLTASMLDGRAPYKGLLTHGFTVDGEGRKMSKSLGNGVDPHEVANRLGAEIIRLWIASTDYSGELAISEEILKRVTEGYRRIRNTLRFLLANLSDFDYAQHAVPVDEWLEIDRYAVAFSAQLQTELLAYYEKYEFHPVVAKLQTYCSEDLGGFYLDVLKDRLYTSAPDSRARRSAQTALYHLTQGLLRVLAPFLSFTAEEAWKVFQPASDTIFTETYYAYPDVADADALIDKWSLLRDVRGTVTKALEEARTANRIGSSLQAEVTVHASGARYDALASLGDDLKFVLITSAATVVKVDDEAQEGVDVAASKYQKCERCWHYREDVGAHADHPTLCGRCFSNLFENGEIRSAA", "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": "MKSVTLKELSLLLDGVVQGDETLVINSVATLEHATAGQISFLANSKYRAQLELTQASAVLLSAKDAQDYSGTALVVKDPYVGFARVAQLLDTTPKAAIGIHPSAQIDPSALLGEGVAIGANAVIGANVILGENVQIGAGTVIGQDCIIGSNTRLWANVTLYHNVHLGQDCIIHSGAIIGSDGFGYANERGQWIKIPQTGGVRIGDRVEIGASSTIDRGALGHTEIHNGVIIDNQVQVAHNDIIGENTAIAGSTTLAGSVTIGKHCIIGGNCAIAGHLTIADGVHLSGATNVTGNMREPGLYSSATVAMENKVWRKNTVRFRQLDELFQRVKTLEKNSNTPE", "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": "MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPASKKAVQGGAAAPVVGAVQGPVPGMPPMTQTPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK", "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 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRM U1 A/B'' family."}
{"protein": "MRLPKEGDFITIQSYKHDGSLHRTWRDTMVLKTTENALIGVNDHTLVTENDGRRWVTREPAIVYFHKKYWFNIIAMIRETGVSYYCNLASPYILDPEALKYIDYDLDVKVFADGEKRLLDVDEYEQHKAQMNYPTDIDYILKENVKILVEWINENKGPFSSSYINIWYKRYLELKKR", "text": "SIMILARITY: Belongs to the UPF0374 family."}
{"protein": "MEFSPPLQRATLIQRYKRFLADVITPDGRELTLHCPNTGAMTGCATPGDTVWYSTSDNTKRKYPHTWELTQSQSGAFICVNTLWANRLTKEAILNESISELSGYSSLKSEVKYGSERSRIDFMLQADSRPDCYIEVKSVTLAENEQGYFPDAVTERGQKHLRELMSVAAEGQRAVIFFAVLHSAITRFSPARHIDEKYAQLLSEAQQRGVEILAYKAEISAEGMALKKSLPVTL", "text": "FUNCTION: Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism. SIMILARITY: Belongs to the SfsA family."}
{"protein": "MELSTVLLLLGLCSAGLVLGSEHETRLVAKLFEDYSSVVRPVEDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKEARGWKHWVFYSCCPTTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTSLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHIMPEWVRKVFIDTIPNIMFFSTMKRPSRDKQEKRIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGVKYIAETMKSDQESNNAAEEWKYVAMVMDHILLGVFMLVCLIGTLAVFAGRLIELHQQG", "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": "MSLLFDPGFVILREDQSVKLFNIILVMSQVFGGLAVLLVTIWMSKFESGFAWNEDPDKEFNYHPTFMIMGMVFLFGEALLVYRVFRNERKKFSKTLHVILHSCVLVFMLMALKAVFDYHNLHKDPSGNPAPIVNLVSLHSWIGLSVVILYFAQYIVGFITYFFPGMPIPIRQLVMPFHQMFGVLIFIFVSITVAMGISERAAWKHTCWTKEGQMCAQQATSSFVGVFTFLYTVCVLLLVLNPRWKRQSLPEEEGLHHLTSSHSMSD", "text": "FUNCTION: Putative transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein."}
{"protein": "MERAPPDGLMNASGTLAGEAAAAGGARGFSAAWTAVLAALMALLIVATVLGNALVMLAFVADSSLRTQNNFFLLNLAISDFLVGAFCIPLYVPYVLTGRWTFGRGLCKLWLVVDYLLCASSVFNIVLISYDRFLSVTRAVSYRAQQGDTRRAVRKMALVWVLAFLLYGPAILSWEYLSGGSSIPEGHCYAEFFYNWYFLITASTLEFFTPFLSVTFFNLSIYLNIQRRTRLRLDGGREAGPEPPPDAQPSPPPAPPSCWGCWPKGHGEAMPLHRYGVGEAGPGVEAGEAALGGGSGGGAAASPTSSSGSSSRGTERPRSLKRGSKPSASSASLEKRMKMVSQSITQRFRLSRDKKVAKSLAIIVSIFGLCWAPYTLLMIIRAACHGRCIPDYWYETSFWLLWANSAVNPVLYPLCHYSFRRAFTKLLCPQKLKVQPHGSLEQCWK", "text": "FUNCTION: The H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system. Signals through the inhibition of adenylate cyclase and displays high constitutive activity (spontaneous activity in the absence of agonist). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MHIESPIKRRQSTRIYVGNVPIGDGAPIAVQSMTNTRTTDVDATVAQIKSLEKVGADIVRVSVPTMDAAEAFKVIKQQVSVPLVADIHFDYRIALQVAEYGVDCLRINPGNIGNEQRIRSVVDCARDKNIPIRIGVNGGSLEKDIQAKYKEPTAEALLESAMRHVDILDRLNFDQFKVSVKASDVFLAVDSYRLLAKQIAQPLHLGITEAGGARAGSVKSAVGLGMLLSEGIGDTLRISLAADPVEEIKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIATVNELEQRLEDLITPMDVSLIGCVVNGPGEAEVSHMGIAGSNRKSAFYEDGVRQKERFDNDNIVDQLEAKIRAKAAMLSKENQIDINQID", "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": "MKKVSRNLLQARQMVDKNRFYSLEEAMELVKKTSYTKFSGSVDLAIRLNLDTRKADQQLRGAVVLPHGTGKSVRVLVATDSSEVAAKSLEAGADLIYSTAELEQNLKIDNFNFDVIVVEPKLMPILGRYGKKLGPKGLMPNPKTGTVSPNPEKAVAEIKKGKANYRADRYGIIHSLIGKTNMEVPQLVENANTLLRLIKRLKPNTVKGNYFKNLTVSASMGPSIKIRFDNL", "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": "MVRVAINGFGRIGRIVLRIAMKRDGIDVVAINDPFITNDYAAYMFKYDSTHGRYDGEVTHDDKDLIIDGKAIKCYQERDPADLPWGDNDIDIVIEATGVFTAKDLAEKHITAGAKKVVITGPSATAPMFVKGVNDDKYTSDVTVISNASCTTNCLAPLAKVLQDNFGIEEALMSTVHSQTATQKTVDGPSKKDWRGGRTASANIIPSSTGAAKAVTKVLPELEGKLTGMAFRVPTVDVSVVDLTVRFAKDVTYDEIKAAIKKASEGEMKGILAYTEDAVVSTDFLGDTHSSIFDASAGIQLSPRFVKLVSWYDNEYGFSARVVDMVELVSKA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MQKYDIKTFQGMILALQDYWAQNGCTIVQPLDMEVGAGTSHPMTCLRALGPEPMSTAYVQPSRRPTDGRYGENPNRLQHYYQFQVALKPSPDNIQELYLGSLEVLGIDPLVHDIRFVEDNWENPTLGAWGLGWEVWLNGMEVTQFTYFQQVGGLECKPVTGEITYGIERLAMYIQEVDSVYDLTWNIAPDGSKVTYGDIFHQNEVEQSTYNFEHADVDFLFSFFEQCEKECQQLLELEKPLPLPAYERILKAAHAFNLLDARKAISVTERQRYILRIRNLTKSVAEAYYASREALGFPMCKKEQA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MEQPQPAPGSLSWRLSSHPITLLTFLGFRVSSLLVYLFGLLFTDNLVMIFIITILLLAADFYYLKNIAGRRLVGLRWWNEVDPSTGDSHWVFESSEPGSKVINATDSRFFWIAIYAQPLFWIALAVVAVFSFKFIWLPLVAIALVLTITNSLAFSRCDKFSQASNIAGSAFNGGNLAGSIASNMVGRFFTR", "text": "FUNCTION: Golgi membrane protein involved in vesicular trafficking. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the TVP23 family."}
{"protein": "MTDKTSLSYKDAGVDIDAGNALVDRIKGVVKKTRRPEVMGGLGGFGALCALPQKYREPILVSGTDGVGTKLRLAMDLKRHDAIGIDLVAMCVNDLVVSGAEPLFFLDYYATGKLDVDTAASVITGIAEGCSQSGCALVGGETAEMPGMYHGEDYDVAGFCVGVVEKSEIIDGSKVAEGDVLIALGSSGPHSNGYSLVRKILAFSNTDPETTQLEGKPLADHLLAPTRIYVKNILSLIEQVDVHAIAHLTGGGFWENIPRVLPDNTQAVLDESSWEWPAVFGWMQQAGNVSRFEMYRTFNCGVGMVIALSAADADKALRLMNDAGEKAWKIGVIKASDSEERVVINA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
{"protein": "MSEQAVEVSPKCLGPQHHINPLRFVMPPGSWDTHFHVFGPTTKYPYSETRKYTPPDSPFEEYVKLMLALGIERGVCVHPNIHGPDNSVTLDAVERSEGRFLAIVKIAPDVTLPQLKEMKKKGACGVRFAFNPEHGSGELDTALFDRVVQWCGELDWCVNLHFASNAIHSLAERLSQLTIPTLIDHFGRVHPTKGVDQPDFKTLVDLMRLPHMWVKLTGADRISRNSPSYQDVVPLARTLVDVAPDRVIWGTDWPHSGYFDVKRMPNDGDLTNLLLDFAPSEEQRRRILVDNPSRLFGQVAKGA", "text": "FUNCTION: Involved in the degradation of 4-sulfocatechol which is a central intermediate in the degradation of substituted sulfonated benzenes. Catalyzes the hydrolytical desulfonation of 4- sulfomuconolactone to yield maleylacetate. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Sulfomuconolactone hydrolase family."}
{"protein": "MEPERNESGTPSVAVTPAAPINAGRAPVRRVANQIPDEIAHNPLLLEAMKVLPENYNFEIPKTIWRIQQASAKRVALQMPEGLLMFACAIADIIERFTSAETVVMGDVTYGACCVDDYTAQALGADFMVHYGHSCLIPIDATHGVRMLYVFVDIKIDTSHFVDTIRFNFQAGASLALVSTVQFVSALQAARQALQTDYNVTVPQCKPLSPGEILGCTSPRLNKSVDAVVYLGDGRFHLESVMISNPDTKAYRYDPYSKVFSREYYDHSTMLRHRGEAISVATNAKTWGLILGTLGRQGSPKIMEHLESRLQALGCRYVRLLLSEIFPNKLKLFAEVEVWVQVACPRLSIDWGTAFSKPLLTPYEASVALKEAEWQLTYPMDFYANESLGPWTVNHESHRPTRATVRRTQKPEQRKLQCTDVGATVEECPCQEKVETKTE", "text": "FUNCTION: Catalyzes 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). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily."}
{"protein": "MSQIVVCAMYKFVTLEDFEAMRQPLLDTMIKNNVKGTLLLANEGINGTVAGTRESIDNLLAYLKADPRLVDIDYKESYHQEMPFYRSKVKLKKEIVTLGIDEIDPNKICGKYVEPKDWNDLISDPETVLIDTRNEYEIEIGTFKNAINPHTENFREFPQYVDENLDPKKHKKVAMFCTGGIRCEKSTALLKAKGFDEVYHLKGGILKYLEEVPKEKSMWQGECFVFDSRVAVNHDLEKGNYDQCFACRMPITEDDKKRPEYVKGISCHHCYDKVTEKQKARFAEREKQSQLAAEKGFSHVGDEAKKLAQLNKQKKQQAKEAARKKAQQ", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family."}
{"protein": "MSGGSTGERPFSDIITSVRYWIIHTITIPSLFVSGWLFISTGLAYDVFGTPRPNEYFTQDRQQVPLVNDRFSAKQELEDLTKGL", "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": "MARISGVEIPNNKRVVVSLTYIYGIGLPTAQSVLKTLNISEDIRVKDLTEEQIKNISMEISKYKTEGKLRREVSLNIKRLMEIGSYRGLRHRKGLPVRGQSSKTNARTVKGPRKTVANKKK", "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": "MNPEHSPLGKATVYAAQYDASLLFPIPRAGAREQLGITSALPFFGTDIWNAYELSWLNARGKPQIAVATFYVPAESPNIVESKSFKLYLGSFAQTTFDSIDAVRDTLKRDVSAACGATVSVQLVSPHDFGKLEMEELDGLSLDRLDLDTDVYEPDPSLLKAAEDEAPVEETLVSDLLRSNCPVTGQPDWGSVQIHYVGPQIDHAGLLRYIISFRNHTGFHEQCVERIFLDILHACKPVKLAVYARYTRRGGLDINPFRTNYNQPMPDNARNARQ", "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": "RKRGSQTYTRYQTLELEKEFHFNRYLTRRRRVEIAHVLCLTERQIKIWFQNRRMKWKKDHKDESSSSNLSANSEN", "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": "MVSESCSRNYNHPYTPYDIQIQLMDAIYNTIENGYKIGLFESPTGTGKTLSIICSSMTWLRTFKRNNTFLETNNEVEDVYESESEEDEPEWVKKAYQSSIVNRSKNKLIEYEHYLDKIEKEHAQNKRKEEELEIKVHKRRKAMTAAGTDLSEESYLPMDYYSDSEVGKIEDQNLAITKEINRLLKKVENKEEVSYINECPIKIFFSSRTHSQLNQFSSQLRLTNFQASFEDLEERTKYIPLGSRKQLCINEKVRSKGNDQSVNDACLDLQRETNGCQYLPKNYMMSSVTKEFADLSLAKIRDIEDLNELGIELNICPYYSVRKGIEMTEIISLPYQMIFQDTTRKILNLDIKDSIIIIDEAHNIIDVITSMYSIKITSDQLNKVIKSLKIYLNKFLKRLNSGNRINLMKLIKICQILLKFLNTNSEKVKSGDEVQIQDIFKDSTGDLVNIHKLDQFLTKSKIAYKIESYIEKTEMETDNGEKKGRITNSGGSSSSSSSSNPLLFTIIKFLRTLTNLSKEGKFFWDNENGTISLNYMLLDPSAVFKEIVDQAKCVLLCGGTMEPMSDYMDYLFPSVPTNKINTFACGHVIPKENLQVFPISQWNDTNFEFSYQKRNDSKQLMALGEFLIEITKRVPYGVVIFFPSYKYLDQVLQFWRDTKILTSIESEKTIFREPKDPSNVEKVLNEYGYLIQTERKGAILFSVVGGKMSEGINFSDDLARAVIMVGLPYPNAYSGEMVTKRKYIETSELSNGGTTTDAKEKSRNYYENLCMRAVNQSIGRSIRHINDYSIIYLVDRRFSTPRIQNKLSQWVKERISITTTNNNNNNSIYIMESTTDFFNIIR", "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": "MSHSDHTAPLEARLSAALSGTARVPGDKSISHRALILGALAVGETRISGLLEGEDVLNTARAMRALGAQVERTGDCAWSVHGVGVAGFAPPAAPLDFGNSGTGCRLAMGAVAGSPIIATFDGDASLRSRPMRRIVDPLEQMGARVTQSADGGRLPLTLQGARDPLPITYRTPVPSAQIKSAVLLAGLSAPGVTTVIEAEASRDHTELMLQHFGATVVTEPEGPHGRKISLTGQPELRGAPVVVPADPSSAAFPMVAALIVPGSDVVLTEVMTNPLRTGLITTLREMGGLIEESETRGDAGEPMARFRIRGSQLRGVEVPPERAPSMIDEYLVLAVAAAFAEGTTIMRGLHELRVKESDRLEATAAMLRVNGVTVEISGDDLIVEGKGHVPGGGLVATHMDHRIAMSALVMGLAADKPVRVDDTAFIATSFPDFVPMMQRLGAEFG", "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": "MFFGILKAIILGIVEGITEFLPISSTGHLIIVDQFVKISSNKAFTTTFEYVIQLGAIIAVVLLYWKRLWPFGGGKTEKQRFNIWATWVKVVVGVIPSVIIGFLLNDWMDKHLMNWLVVSIALIVYGIAFIFIENYQKNRRPRVRTINHLTLADVLKIGFFQVLSIVPGTSRSGATILGGISIGVSREAAAEFSFFLSIPTMLGVSVLKIGSYLHSHGMFSGEQIVILLVGMFVSFVVAYVVIKWLLRFIQTHDFKAFGWYRIILGVLVIALGAIGIID", "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": "MDKAQQDALKKAAGIEAAKLIQNGMIAGLGTGSTVRFLVDELGRRVKEEGLEFTGVTTSRRTQEQAEGYGIKIVNIDDVDHIDVTIDGADEVDKNFNGIKGGGAALLWEKIVATNSNKIVWIVDESKVVDTIGKFPLPVEVIPFGAGQVVKKFEAKGYKPVLRLDANGEPVRTDENNYVVDLHLERIDHPQELAQDLITTVGVVEHGLFLNMVDQVIVGDPNGPRVMDNPNK", "text": "FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. SIMILARITY: Belongs to the ribose 5-phosphate isomerase family."}
{"protein": "MSAPRTLYDKIWDDHLVNQQDDGTCLLYIDRHLVHEVTSPQAFEGLRMAGRKVRAPEKTLAVVDHNVPTSPDRHLGIKNEESRIQVEALARNAADFGVEYYSENDKRQGIVHIVGPEQGFTLPGMTIVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQTLIQKKAKNMLVRVDGQLPPGVTAKDIILAIIGEIGTAGGTGHVIEFAGEAIRSLSMEGRMTICNMTIEGGARAGLIAPDETTFDYIKDKPRAPKGKAWDMALDYWKTLHTDEGAHYDRIVVLDAADLPPIVSWGSSPEDVISVQGAVPNPDDIQEETKRASKWRALDYMGLKPGTKITDIAVDRVFIGSCTNGRIEDLRAVAKVVEGRKVASTVSAMIVPGSGLVKEQAEAEGLDKIFKEAGFDWREPGCSMCLAMNDDRLKPGERCASTSNRNFEGRQGFKGRTHLVSPAMAAAAAVAGHFVDIREWK", "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": "MMGIGKNTASKSVEAGGSTEGKYEEEAKHSNFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGDDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTEITVANGTAELLEHIWHPRIQEIQGAIIMSSLIEVVIGLLGLPGALLRYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKFQLFKMFPIILAILVSWLLCFIFTVTDVFPSNSTDYGYYARTDARKGVLLVAPWFKVPYPFQWGMPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFVEGLSCVLDGIFGTGNGSTSSSPNIGVLGITKVGSRRVIQYGAALMLGLGMVGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLVTGITGIDQILNVLLTTAMFVGGCVAFILDNTIPGTPEERGIKKWKKGVSKGSKSLDGMESYNLPFGMNIIKKYRCFSYLPISPTFAGYTWKGFGKSENSRSSDKDSQATV", "text": "FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family."}
{"protein": "MNRIRNFSIIAHIDHGKSTLSDRLIQVSGIVAARDFRDQILDSMDLERERGITIKSQTICLPYKAKDGAVYSLNLIDTPGHVDFSYEVSRAIASCEGALILIDASQGVEAQTVANLYLAVDHDLEIIPVINKIDLISADVERVMEQIEEDLGLDSSAAVKVSAKEGVGIEDLMETIVAKLPPPKGNLEAPLQALIFDSTYDDFRGTVIHVRVFEGKVKPGDMIMFMSNDSVYKVEEVGIFQIVRKPRKVLAAGEVGYIIAGIKSLSDTRCGDTITLKTNRCAAAMPGFREAKPVVFSSIFPIGSDEYEDLATAIDKLKLNDASLVYEKTSSLALGFGFRCGFLGLLHLEIVQERLEREYDQSLIITAPTVRYEVVYHDGTSMFIDNPELFPDPTLIQTTREPFIKASIIIPDKYMGAVMTLCMERRGISTTYHYLTGSRMEMVFELPLAEVMYDFYDKLKTVTQGYGSFDYEMLDYRDSRLVKLDILVNGERVDALSQLAHEDKAVERARHACKMLSEEIPRQMFKIPIQGAIGGKIISRETISALRKDVTAKCYGGDISRKRKLLEKQKKGKKRMKTIGKVAIPQSAFLAVLKSDQT", "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": "MAKTLYEKLFDSHIVYEAEGETPILYINRHLIHEVTSPQAFDGLRVANRQVRQVNKTFGTMDHSISTQVRDVNKLEGQAKIQVLELDKNTKATGIKLFDITTKEQGIVHVMGPEQGLTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQARAKSMKIEVRGKVASGITAKDIILAIIGKTTMAGGTGHVVEFCGEAIRDLSMEGRMTVCNMAIEMGAKAGLIAPDETTFAYLKDRPHAPKGKDWDDAVAYWKTLKSDDDAQFDTVVTLEAKDIAPQVTWGTNPGQVISVNETIPNPQEMADPVQRASAEKALHYIGLEAGTNLKDIKVDQVFIGSCTNSRIEDLRAAAAVMKGRKKADNVKRILVVPGSGLVKEQAEKEGLDKIFIAAGAEWRNPGCSMCLGMNDDRLGEWERCASTSNRNFEGRQGRNGRTHLVSPAMAAAAGMFGKFVDIREVALN", "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": "MTSTANYNNSGKDSYFSEIKKSELGLIKNNLSTAINERNADKIKDILQRIIYYMTIGMDVSVLFPDVIMVASSNDIIIKKLVYLYIVHYSKSNPDLLLLVVNTLRRDCIDRNPIIRGLALRSLCSLDSKNTLEYATIEINRSLTDFSGYVRKTALLGLAKLYHLSKEAFDLDIIIPKIFDMIMDQDPQVIVNAVSTLNEIKPGWSFTFDLVQHLMIKFKEFNEWSQCIILECLSRYTPSSEDESLDILNLLDDRLSHSNSALTLSTIKIFLKYTDEFEEIQEQVYERIKEPLITLMESSESNETSFTILHHIHLLMSRSPRLFNRYYKHFYCKFDDPLYIKTLKVQVLKEIASNQTFIESIDEILQELSEYVYEGDHSLCKQSINAITVIAQKHKNTQEKYPIDESVLEKIFLPYLSVSSNLGGAGDDNISINEGILSFILISLKDFLRVFPKHLKTVLPYINENLIGIGSVSNYTLPPSANESVLWMLGESPNSQVNSPYIIEEFFNEKFDQQPTFVKTQLLTTSLKVFFDRPGEMLPILKRILKKCCSDLSQDPGLHEISLFYSRIILLLDIDKAASIINSSKQTTSINTFLEDEINEYRDKIFDEFNTLSVLFGKHSTKFIKNKKQIENEKLQFLENQKNYLLSITDGNQNNNQNNNQNNNQNNNQNNNQNNQNNNNQNNNSKQLLKEIESSPNNLIDTFILDQQPELSPELFQSLWLSLEDGHKIDIQLDSPIDNSEIESVMSKQGIICLAFGSVDQQTKLYYYARQNLSFDIDFNSEQNQQQPQPIFIIEILIDENTLLMSILFKSPILKTLHNKFIPKFLSILSIPIPKIFN", "text": "FUNCTION: Probable component of an adaptor protein complex. Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. SIMILARITY: Belongs to the adaptor complexes large subunit family."}
{"protein": "MSLMPFAPSRPLSIGVELELQLLGCNDYNLAPSAPEILRRVAKRTHPGEIKPEMTRSMIEINTSVQQEYAGLVTELRALRDVVSEAGCFLNVAVAGGGTHPFQHWSEQKIFDAPRFHYLSELYGYLAKQFTIFGQHVHIGCPGPDEALHLTHMLSRYIPHFIALSASSPFVQGHDTGFASARLNSVFSFPLSGRAPFVLRWNDFEKFFAKMTGTGVVESMKDFYWDIRPKPEFGTIEVRVCDTPLTVEIAASIACYIQAMSRYIMVEQRMAPEEDDYLVYTFNRFQACRFGLEGVFIDPRTHQQRSIREDIMEMLEHISDHARELHAVEAMERIREILIVGNGTSWQRRAYASEHNLADVMQLQAELWMGN", "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": "MFSGASAINLDAKGRIAIPKRYRESLHACHNNQLVITVDIQSSCLLLYPIHEWEQVAAKLASLSDTQPTERAIKRMLLGYAHECELDGNGRMLLPPPLRQYANLDKRAMLVGQLNKFELWDEAAWQQQIEQSRIAILNEDLAANERLADFSL", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family."}
{"protein": "MSVLSDKSIRKLAVEQSMISPFIDKQVRDGKISYGLSSFGYDARVGDEFKIFHNVNSSIVDPKEFSSDNFVTKKSSDYIIIPPNSFALGTTIEVFKIPRDIMCIVVGKSTYARTGIIVNVTPIESEFFGTVTLEFSNTTPLPAKIYANEGVAQFLFLKGDQSPETSYADRKGKYMGQTGVTLPKV", "text": "FUNCTION: Catalyzes the deamination of dCTP to dUTP. SIMILARITY: Belongs to the dCTP deaminase family."}
{"protein": "MSSTKDELQLYAKAIYNCAISNHQSLDHWKTMLQLMANILNNEIIKNLISKAYFSQHVISLFIDLCCNKVNQYGINLIKILAENKRLMLLEKLYKEFINLCELYQGVVNITVISAHKLNEEYISKINIMLKKRFFKKINVTYVIDESIIGGLIIKFCDTVINASIHSRLEKLLNILQY", "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": "GFLDIVLHVGLAAGKAALNAVNEAVNQ", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Cruzioseptin subfamily."}
{"protein": "MPKASHQDLRFAFRELLASGSCYHTASVFDPMSARIAADLGFEVGILGGSVASLQVLAAPDFALITLSEFVEQATRIGRVAQLPVLADADHGYGNALNVMRTVIELERAGVAALTIEDTLLPAQFGRKSTDLIPVEEGVGKIRAALEARVDSSLSIIARTNAGVLSTEEIIVRTQSYQKAGADAICMVGVKDFEQLEQIAGHLSVPLMLVTYANPNLHDDERLARLGVRIVVDGHAAYFAAIKATYDCLRLQRGQQNKSENLTATELSHTYTQPEDYIRWAKEYMSVDE", "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": "MFVTAAYAQSSTTEGAEAHDAAAAGEVHTETGVAHEADHGAGVFPPFDTTHFASQLLWLAITFGLFYLLMSKVIIPRIGGILETRHDRIAQDLDEASRLKGEADAAIAAYEQELAGARAKGHSIADTAREAAKAKAKADRDGVEAGLAKKIAAAEARIADIKSKALADVGAIAEETATAVVKQLIGGTVTKAEIAAAFKASAGN", "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": "MDMVSLKFIGIGLMAIGMYGAALGVSNIFSSLLSSIARNPSAAENLQRMALIGAGLAEAMGLFSFVIAMLLIFS", "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": "MKAGIIYNEGKPLAVELAAHVRRILELQGWEVHMATGIGGILGYSRPDSPVCHTPIDQLVPPGFDASMAFAVVLGGDGTVLSAFRQLAPCEIPLLTINTGHLGFLTEGYVADLEPALDQVLRGDYTIEDRTMLTVQVLRDQTVIWEALSLNEMVIHKEPLTGMCHFEVDVGAHARVDIAADGLILSTPTGSTAYALSAGGPVITPGVAALQLVPICPHSLASRALVFSNSEPVWIYPANPFKHLILVVDGNAGCYIQPEDQVFVQRAPYRARFIRLRAPEFFHVLQQKLGWGLPHVAKPRAKKSTDS", "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": "MKSRYLVFFLPLIVAKYTSAETVQPFHSPEESVNSQFYLPPPPGNDDPAYRYDKEAYFKGYAIKGSPRWKQAAEDADVSVENIARIFSPVVGAKINPKDTPETWNMLKNLLTMGGYYATASAKKYYMRTRPFVLFNHSTCRPEDENTLRKNGSYPSGHTAYGTLLALVLSEARPERAQELARRGWEFGQSRVICGAHWQSDVDAGRYVGAVEFARLQTIPAFQKSLAKVREELNDKNNLLSKEDHPKLNY", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class A bacterial acid phosphatase family."}
{"protein": "MIAKVFKSITPESYILLVNAGLISAYGVRIIFQSVKNDEGKVDEKAHIGIGHFFKKRGAQLVDGKNLTDILKEKKKKKKKKKKINISNKLIIFKISRQLYSKLKLK", "text": "FUNCTION: Involved in starvation response and aggregation stage of the life cycle. May be involved in fruiting body morphogenesis and spore formation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MNVGTAHSEVNPNTRVMNSRGIWLSYVLAIGLLHVVLLSIPFVSVPVVWTLTNLIHNLGMYIFLHTVKGTPFETPDQGKARLLTHWEQMDYGVQFTASRKFLTITPIVLYFLTSFYTKYDQVHFILNTVSLMTVLIPKLPQLHGVRIFGINKY", "text": "FUNCTION: Negative regulator of sphingolipid synthesis. May indirectly regulate endoplasmic reticulum-mediated Ca(+2) signaling (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ORM family."}
{"protein": "MTKKIEEKIEGVIESLGYLLYDVSLVKENEQHVLRVSLKNPNGAVSLDICQQVSEIISPLLDVCDFIQDAYILEVSSMGLERTLKTPKHFKLSLGEKVEVKLINKESFQAVLKDANDLSADFELDNHAIKSVEYKDLKKVKTLFEW", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MSINATARSLLLTEFISAFFLTMRYFFKPKPTINYPFEKNPISPRFRGEHALRRYPNGEERCIACKLCEAVCPAQAITIEAGPRRNDGTRRTVRYDIDMVKCIYCGLCQEACPVDAIVEGPNFEFATETREELYYDKAKLLANGDRWEREIAKAIELDAPYR", "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": "MGPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLYSKAGREELERVNV", "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": "MAFRGIRPSNKVAASRPDVWTLVNQATAECKVPPVSLSQGFFNYNPPKFVLDAAKKSIDEVACNQYSHTRGRPSLRKALSEAYSPYFKRTLNPDTEIVVTAGANEGFFSVFAAFLNPGDEVIVMEPFFDQYISNITMNGGVPVYVPIIPPEEGSVKPVSAGAWKLDMNKLRNAITEKTKMIVINTPHNPLGKIFSEEELNEIADLVLKHNLLVVSDEVYDRLSFVPFVRLATLRPELFKHVVTVGSGGKTFGCTGWRVGWLIGDESLIKYSAAAHTRICFAVNSPCQEALAIAFGEAEKHNYYEEYKSSYKKRFEILAKAFDQLEIPYTIPDGSYYTMANFSKLKLPKDYPFPEEIANRPRDFKLCYWILKEIGVATIPPTEFYTDEDAPVAENYLRFAFCKTFETLEEAARRLQKLKDYF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MKFLGVKVYRFPLVKYYWPFFVGFGLTFYGVAKIQNAMMDTAEFINDPRHPRFKKGDLEKK", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Part of the complex F(0) domain (PubMed:27791192). Minor subunit located with subunit a/ATP6 in the membrane (PubMed:27791192). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein 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 j subunit family."}
{"protein": "MLGAWAVEGTAVALLRLLLLLLPPAIRGPGLGVAGVAGAAGAGLPESVIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRASDYGMKLPILRSNPEDQILYQTERYNEETFGYEVPIKEEGDYVLVLKFAEVYFAQSQQKVFDVRLNGHVVVKDLDIFDRVGHSTAHDEIIPMSIRKGKLSVQGEVSTFTGKLYIEFVKGYYDNPKVCALYIMAGTVDDVPKLQPHPGLEKKEEEEEEEEYDEGSNLKKQTNKNRVQSGPRTPNPYASDNSSLMFPILVAFGVFIPTLFCLCRL", "text": "FUNCTION: Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N- glycosylation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the malectin family."}
{"protein": "MSSPHVLVVDDTLVDRHVVSMALMRHNVRVTAVESVMQALMFLDSEHDVNMIVSDYCMPDMTGYDLLMEVKKSPKLAHLPVVIASSDNIPERIRKCLDGGAKDYILKPVKIVDLPRILNYI", "text": "FUNCTION: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling. SIMILARITY: Belongs to the ARR family. Type-A subfamily."}
{"protein": "MAKVIGIDLGTTNSCVAVMEGGEPIVIANPEGNRTTPSVVAFSKTGERMTGQVAKRQAITNPERTIISIKRDMGTDHKVDIDGKKFSPQEISSMILQKLKSDAEAYLGETVTQAVITVPAYFSDAQRQATKDSGKIAGLEVLRIINEPTAAALAYGLDKEHDQKIMVYDLGGGTFDVSILEIGDGVFEVLATNGNNKLGGDDFDQRIIDFLVDTFKKESGIDLKNDKMAMQRLKEAAEKAKVELSGVTSSNINLPFITADASGPKHLDVTLTRAKFDEITADLVENTMVPTRQAMQDAGLTPDKIDKILLVGGSTRIPAVQEAVKKYLGKDPFKGINPDECVAVGAAIQAGVLTGDVTGLLLLDVTPLSLGLETLGGVFTKLIERNTTIPTKKSQVFSTAADGQTSVEIHVLQGEREMAQYNKSLGRFQLTGIPSAPRGVPQIEVTFDIDANGIVHVSAKDLGTGNEQKITITASTNLSDSDIDKAVKEAEKFAAEDKQRKEEIDVRNNADSLIYQSEKSLKDLGDKVSADDKSKIESGVNKVKDALKGTDIEVIKKATEELQQSFYDISSKIYQQTQGAQSDPGAAGFGGQQEAPGAGQDENVVDADYKVVDDDK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MSEKKINLLDLDRKALRALFTEMGEKPFRADQLMKWIYHFGVSDFEEMTNINKVLRAKLAAKCEIVAPEISSYQKSVDGTIKFAINVGDGQEVETVYIPEDDRATLCVSSQVGCALECTFCSTAQQGFNRNLTVAEIVGQIWRVADFIGFVKDTGERPITNVVMMGMGEPLLNLKNVIPAMDIMLDDFGFSLSKRRVTLSTSGVVPALDKLGDVLDVALAVSIHAPNDELRDVLVPVNKKYPLEEFLGGIRRYIAKSNANRGRVTVEYVMLDHINDSTDQAHELAKLMKDTPCKVNLIPFNPYPGSPYGRSSNSRIDRFSKVLMEYGLTVIVRKTRGDDIDAACGQLAGDIRDRTKRLAKKQMQQNQISVTIN", "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": "MSASPLKVAVTGAAGQIGYSLLFRLASGSLLGPDRPIELRLLEIEPALKALEGVVMELDDCAFPLLSGVEIGSDANKIFDGANLALLVGARPRGPGMERSDLLEANGAIFTAQGKALNEVAADDIRVGVTGNPANTNALIAMTNAPDIPRERFSALTRLDHNRAISQLAAKTGVAVTDIKKMTIWGNHSATQYPDLFHAEVKGKNAAEVVNDQAWIEEYFIPTVAKRGAAIIDARGASSAASAASATVDAARSWLLGTPADDWVSMAVLSDGSYGVPEGLISSFPVTTKDGNWSIVKGLEIDEFSRGRIDKTTAELADERKAVTELGLI", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MTKLRLKSKDEIKKIKASASLLALTLLEVERNIVPGISTKELDLIAYDFIIKNRAKPAFKGYRGFKGTICASVNEEVIHGIPGKRKLADGDIVSIDCGVILDGFYSDMAKTFKVGNVDSSIDKLLEVTNASLYKGIAEMKVGNRILNISKAIEDYIKPFGFGIVREYTGHGVGFELHEEPSVPNYYAPFFKNIRIQEGMVLAIEPMVNLRGHKVSIKSDGWTVFASDLSYSAHFEHTVAVVDGLPLILSEV", "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": "MSSMNLRRLLPQRAKQERPQPESSKKKGFLERKKDYVERAKDYNNKRDTLKKLKLQAAFKNPDEFNYKMISSKLVDGVHSEISKTSLKKEQIIDIKTQDILYLQSKRRADDKKIERLQATLQYMDSGLEPTEQIIYVDDEKEVKNFSATKYFDTVPDAFNGSLSTIPKISKLKEGSLVVNPKTAPTLGQLEAMTATSYKELKERKLRRDQLFKAEMDLSKSKIQLKRGTKSGVTKKVGKKEVVFKQVRSK", "text": "FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP11 family."}
{"protein": "MARIAGVNIPTAKRVPIALTYVTGIGHTSAAAICEAVGIDVTRRVNELSDAEVLAIREHIDANYAVEGDLRRETQMNIKRLMDLGCYRGLRHRRNLPVRGQRTHTNARTRKGPAKAIAGKKK", "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": "MAIANKNIIFVAGLGGIGFDTSREIVKSGPKNLVILDRIENPAAIAELKALNPKVTVTFYPYDVTVSVAETTKLLKTIFDKLKTVDLLINGAGILDDYQIERTIAVNFTGTVNTTTAIMSFWDKRKGGPGGVIANICSVTGFNAIYQVPVYSASKAAALSFTNSLARLAPITGVTAYSINPGITKTTLVHKFNSWLDVEPRVAELLLEHPTQTTLQCAQNFVKAIEANQNGAIWKLDLGTLEAIEWTKHWDSHI", "text": "SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MIYNNTYDVIVVGGGHAGVEAAAASARIGAKTLLLTHNIDTIGQMSCNPAIGGIGKGHLVKEIDAMGGIMAKAIDMAGIQFRILNSRKGPAVRATRAQADRVLYKKAINSLLNDQENLDIFQDSVDDLVVENDTVCGVITKTGIIFKSKKVVLTVGTFLGGKIHIGQVSKEGGRAGDQPSNALAARLRALPFRVDRLKTGTPPRIDSRSVDFSVMDVQHGDTPTPYFSFFSKGKIEHPRQIPCYITYTNSKTHEIITNNLDKSAMYSGLIEGIGPRYCPSIEDKVVRFAEKDRHQIFVEPEGLNSIELYPNGLSTSLPFEVQCEYIRSIKGFENAFIMRPGYAIEYDFFDPRDLKPTLETKHIKNLFFAGQINGTTGYEEAGAQGLVAGINAAISIDSDKSWYPTRSNSYMGVLIDDLITKGTKEPYRMFTSRAEYRLILREDNADLRLSDKACELGLLNKQDQEIFINKKTAIDENIAIMKNTWIGPQTQKARDLEKFLDKKMTRESTLFDLLKRPELDYKKLQQIPDTNLKLEDESVIEQIEISAKYSGYIERQSKDIAKISTLESKTIPESFDYSQVKGLSNEVLQKLSEQKPTTLGEASRIPGVTPAAVSLLTIYMKKTGFIK", "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": "MKLNGVFTALATPFRDDLSLDERALASFVDWQISSGISGIVPCGTTGESATLNFEEYCTVVRLCIETARGRILVIAGAGSHCTTETISRALFVQSAGADAALIVVPYYNRPSDEGVYQHFRAVHDATNIPIVLYNVPQRTAIDISNDTIRRIAELPRVVGIKDCTGAERVAALKAILPEKVAILSGEDETALASYMNGGSGCISVVSNVAPKMAVELYRLHALGKINMAKQVSGNLAALSRVLFIEPSPSPTKYALSLMGKMRPKVRLPLVELTSSGQTAVKNVLETLDLLRQQKAMHSQL", "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": "MQKRVVILLLDSFGIGASEDARDFGDLGANTLGNIAKACFNNLADSNDRNGALKLPYLESLGLGLSALKATNELPLGFESKPNLIGAYAYAQELSSAKDTISGHWEMMGAPVLFEWGYFKDKNNSFPKEILDEIMRKTKIKGYLGNCHASGTEIIKDLGEKHLETLYPIFYTSADSVFQIVAHEEKFGLDNLYALCEEAFQILEPLKIARVIARPFIGANREDFKRTAHRKDYAIKPHKKLLFEKFIEEKQGEVISIGKIADIYAHVGITQKFKAGSLMELCDVTLEQIKNAKNNSLIFTNFVHFDSDYGHRRDISGYANALEYFDARLKEVLENLRENDLLILCADHGCDPSFKGTDHTREYIPVLFYHKDLQPAFLGKSESFADIGQSIAYFLGLSPLDYGKNLLNFKGQS", "text": "FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of pentose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphopentomutase family."}
{"protein": "MGKGILSLQQEMSLEYSEKSYQEVLKIRQESYWKRMKSFSLFEVIMHWTASLNKHTCRSYRGSFLSLEKIGLLSLDMNLQEFSLLNHNLILDAIKKVSSAKTSWTEGTKQVRAASYISLTRFLNRMTQGIVAIAQPSKQENSRTFFKTREIVKTDAMNSLQTASFLKELKKINARDWLIAQTMLQGGKRSSEVLSLEISQICFQQATISFSQLKNRQTEKRIIITYPQKFMHFLQEYIGQRRGFVFVTRSGKMVGLRQIARTFSQAGLQAAIPFKITPHVLRATAVTEYKRLGCSDSDIMKVTGHATAKMIFAYDKSSREDNASKKMALI", "text": "SIMILARITY: Belongs to the 'phage' integrase family."}
{"protein": "MGAYRYMQKLWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRVRVRRGGRKRPVPKGATYGKPVHHGVNQIKFARSLQSVAEERAGRHCGGLRVLSSYWVGEDSTYKFFEVILVDIFHKAIRRNPDTQWITKAVHKHREMRGLTSAGKKSRGLGKGHKFHLTIGGSRRAAWRRRNTLQLHRYR", "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": "MKIMVINGPNLNLLGIREKEIYGAKDFNQVIDYIKEEGKELGLEINCFQSNIEGEIINFIHNAYFKKYDGIIINPGAYTHYSIAIYDALKGVEIPTVEVHLSNIHKREEFRHKSVTAPACIGQISGFGEYGYIMAMNALKKHIKSK", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
{"protein": "MTKTFIFGHKNPDTDAISSALIMADFEQQTGNTEAKAYRLGEISAETQFALDYFNVEAPELLNEDLKGQDVILVDHNEFQQSADTISNATIKHVIDHHRISNFETAGPLYYRAEPVGCSATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTKEDVDAAQALKDIANVDLEAYGLEMLKAGASTTDKSAETLVNMDAKSFNMGDYVTRIAQVNTVDIDEVLDRKEEFEKVMLEMSANEKYDLFVLVVTDIINSDSKILVVGAEKDKVGEAFKVQLDDGMAFLSGVVSRKKQVVPQITEVLTQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase class C family."}
{"protein": "MREVISVHVGQAGVQIGNACWELYCLEHGIGPDGFPTENSEVHKNNSYLNDGFGTFFSETGQGKFVPRSIYVDLEPNVIDQVRTGPYKDLFHPEQMVTGKEDASNNYARGHYTVGKEMIDSVLERIRRMADNCSGLQGFLVFHSFGGGTGSGLGALLLERLNMEYGKKSNLQFSVYPAPQVSTSVVEPYNSVLTTHATLDNSDCTFMVDNEACYDICRRNLDIERPTYENLNRLIAQVVSSITASLRFAGSLNVDLNEFQTNLVPYPRIHFPLVTYSPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRTGRYMATCLLYRGDVIPRDVQAAVTSIKSRRTIQFVDWCPTGFKIGICYEPPQHVPGSGIAKVNRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVGQDSMDNEMYEADEEY", "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": "MKIRNSLKSLLGRHRDNRLVRRKGRVYIINKTQKRYKARQG", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MSKFEAFLRPTQTYHSRTYDRISKHHNFNGTGKTILVTGGSSGVGYSICQAFAEADVARIAIVSRSPGPQAAAKAALEAAHPAVQIVTYAASITDHARMAAILAELGPVDVLVLCAAVVHRQVPATAITAAEMQAAFDVNVLAPFHLVQAYLATTTAGTKTVIHVSSAAAQSRSPFRAGYGPSKAAATQVMQHFAAERASPALRVFSFHPGAFYTPSVAEHYAPDSTGWEDINLPAHFARWLAGPESGFLNGRYLWAHWDVDELIALRDRVERDSSFLTIGLVV", "text": "FUNCTION: Short chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer secalonic acid D (PubMed:30996871, PubMed:33891392). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase AacuL (Probable). The atrochrysone carboxyl ACP thioesterase AacuM then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase AacuI, and oxidized by the anthrone oxygenase AacuG to yield emodin (Probable). Emodin is then reduced to emodin hydroquinone by a yet unidentified oxidoreductase (Probable). A-ring reduction by the short chain dehydrogenase AacuN, dehydration by the scytalone dehydratase-like protein AacuK and probable spontaneous re- oxidation, results in overall deoxygenation to chrysophanol (PubMed:33891392). Baeyer-Villiger oxidation by the Baeyer-Villiger monooxygenase (BVMO) AacuH then yields monodictyphenone (PubMed:33891392). Monodictyphenone is transformed into compounds with the tetrahydroxanthone skeleton via methylesterification by the methyltransferase AacuQ, followed by the action of the flavin-dependent monooxygenase AacuC, the isomerase AacuP, and the short chain dehydrogenase/reductase AacuF or AacuD (PubMed:33891392). AacuF and AacuD should accept the same compound as a substrate but perform the ketoreduction with a different stereoselectivity, thus yielding blennolides B and A, respectively (PubMed:33891392). In the final step of the biosynthesis, the cytochrome P450 monooxygenase AacuE accepts blennolide B and/or blennolide A to conduct the dimerization reaction to furnish the tetrahydroxanthone dimers, secalonic acids D, B, and F (PubMed:33891392). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MALKKRSKHSKKFKLNLGPQHPATHGVLRLILEMDGEIVERADPHIGLLHRGTEKLIEYKTYLQAIPYFDRLDYVSPMCQEHAFALAIEHLLKCEVPLRAQYIRVMFSELTRILNHTLNIATQALDVGATTPLLWMFEEREKIMEFYERVSGSRLHANYFRPGGVSQDLPEGLIENIADFCEQFPCKIADLETLLTDNRIWKQRTVDIGIVSKQQAMDWGFSGVMLRGSGIAWDLRKSQPYDQYANLDFDVAIGKNGDCYDRYLIRIEEMYQSIKIIKQCIQKMPAGEIRTQDPSISPPKRSEIKKSMEALINHFKLYSEGYNVPAGEVYAAVEAPKGEFGVYLYSDGTNRPYRCRIKAPGFAHLQGLDFMARGHSLSDIITIIATLDIVFGEIDR", "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": "MFVKTGDKVKVIAGKDKGKEGTVLSVNVKKNRVVVKGVNKIKKHQKPSQTNANGGVVESEGSIHASNVKVISKKEDK", "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": "MSELKQAAAPEQALVVGRITSVYGVKGWVKLYSHTEPMQGIFDYKHWWLKTPSGWKTVELSQGRLQGRGLVASVKGYTDRDQVKDICGMDVYIDAAELPELEEGDYYWSQLEGLRVITKEGVLLGKVSQLMETGANDVIVVRACEGSFDREERLIPYAPGTYVLNIDLEQQEMVVDWDPEF", "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": "MPKMKSNRAAAKRFKRTANGGFKSGNSFTSHRFHGKTKKQRRQLRGLSMMDKTNVKRYKKLLPFK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "MTMQFLIASNVLLWLALIGCAVLMLGLLRQVGLLHERSSPMGAMITDHGPDVGDAAPTFDLPDHSGAMVRIGGPSALKRPTLLMFTAPTCPVCDKLFPLIKSIARAEKFSVVMISDGQPDEHQRFLAKHELGDIRYVVSAEVGMAFQVGKIPYGVLLDPEGVIRAKGLTNTREHLESLLEADKSGFASIQQFMTSRKHSHDAKAA", "text": "FUNCTION: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MGDHNLPDFQTCLKFSVTAKKSFLCMYRDSVSKEKLASSMPSTCDIQLKRAINDAYPGGGIKVTVLNSTTASLDSLATTHVKEFEIVIIPDINSLLQPDQAKLVKIMRDCTVAIEKAQSTRIFIGVVHWNNPVQPSGAAKDGDEAGKPAPKTRIFLPTSFRMGAWLKHKFWFACAPPYLDFESSTESSINTRANNSIGMAEEEKQEPESKRSIILNEEANLNDVFVGSTVRRYILDIMVHLRTHRLTYNAKAGGVYTNSLDDVVLLSRLIGLHSGKMFVSPSHVKEASRWYFPMHLELVQRSSMDSSLLYGSDPNLVDEMLEKLAKIKCEEVNEFENPLFLESLVVKNVLSKVVPPV", "text": "FUNCTION: May be involved in telomere capping. FUNCTION: May be involved in telomere capping. SIMILARITY: Belongs to the MTC2 family."}
{"protein": "MTATLLDGKATAAEIKDELRVRVKALAERGVTPGLGTVLVGADPGSQAYVNGKHRDCAEVGVASLRRELPADASQEQVDAVLADLNADPACHGYIVQLPLPDHLDTQRVLELIDPEKDADGLHPVNLGRLVLGYPGPLPCTPRGIVELLRRHDVALRGARVAVVGRGNTVGRPLGLLLTRRSENATVTLCHTGTLDLSAHTRAADIVIVAAGVPGLLTPDMITPGAVVVDVGITRVIGPDGKGRYTGDVDPGVTEVAGALVPMPGGVGPMTRAMLLTNVVERAERG", "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": "MRISLNWLRELVQVDLEPEVLAEKLTLAGFEVEEIEDRRTWAAGVVVGRVLEREQHPNADRLSVCQVEIGQAEPVTIVCGASNVRADIWVAVATLGSYLPCIDLKLKPTKLRGVRSEGMICSLSELGLTKESEGIHIFPEDAGLQAGQPVGPLLGLDDVVLDLTSTANRADALSLIGIAREVRALTAATLTLPEVELQTYPELPCLAISLQSEACSHYSGTIIEGVTIAPSPEWLQKRLQLAGIRTINNVVDITNYILLEYGQPLHAFDRQKLQAIAGSSDLAIGVRSAQAGETLKTLDDQERTLAEAALVITAGDCPVALAGVMGGADSEVSQETTQLLLEAAWFEPIAVRRSARSQGLRTEASARYERGVNVTELPIATQRAIDLLLQIAGGTVISQTVATTTQTEPEHSITLRLQRINELLGPVQAEDEELKDLGADDIERLLTAIGCHLTLVDDAVWQVRVPPYRYRDLEREIDLIEEVARLYGYDNFGETLPPLGSDEGALSIDESLRRQIRAVCRGVGLTELQHYSLVKPGSDRQVHLANPLLAEYSALRLDLLSGLIDAFQYNWEQGNGPLWGFEIGRIFWREEDGFFEADRMGGILGGDPSRGRWQRGGKEQAIDWYAAKGVLEEIFERFGLTIEFQPDRQDDRFHPGRTASLWLQGDRLGRFGQLHPSLCEGRGLPAEVYAFELDLDVWLDHLDQPERQVPRFQPYSSFPASDRDLAFFVDQSVTVAELERIIRRQGGALLSEVELFDQYCGEHVPENQRSLAFRLTYRASDRTLTEAEVEPVHDQVRQSLVERFRVTLRS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily."}
{"protein": "MKPAIVLLSGGLDSATVLAIAKAEGFAPAALTFRYGQRHAVEIRAAERVAAALGIRDHRIADIDLRVFGGSALTSDIAVPKGELDEAIPAGIPVTYVPARNTIMLSFALAFAEVLGAADIFVGVNAVDYSGYPDCRPDYIKAFEAMANLATKAAVEGTRLTIHTPLIDLTKGQIIRRGLDLGVDYSITSTCYDPTPDGKACGHCDSCRLRLKGFAEAGLADPAEYAS", "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": "MDIRAAEISKVIRDQIASFGSEAQISEVGQVLSVGDGIARIHGLDNVQAGEMIEFSNGIKGMALNLEADNVGAVIFGSDSQIKEGDVVKRTGTIVDVPVGKGLLGRVVDGLGNPIDGKGPIVAEQRSRVEVKAPGIIPRKSVHEPVQTGLKALDALVPVGRGQRELIIGDRQTGKSAVAIDTFINQKTANAGTDESKKLYCVYVAIGQKRSTVAQLVKTLEENGAMEYSIVVAATASDPAPLQYLAPYTGVAMGEYFRDNGMHGLIVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDANGNGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETDLFYQGVRPAINVGLSVSRVGSAAQTKAMKKVAGSIKLELAQYREMAAFAQFGSDLDASTQRLLNRGARLTELLKQPQFQPLPFEEQVASIFAGVNGYLDSIPTNAVTRFEAGFLAEMRSKHADVLAAIRDSKDLSADSTAALKSALEAFVKTFA", "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": "MALWGGRFTQAADTRFKDFNDSLRFDYRLAEQDIVGSIAWSKALLSVNVLSKEEQQKLEFALNELKLEVMEDPHQILHSDAEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGHQLLLGLDKLQTQMVNVAKQHQATVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLSDALTRLDTCPLGSGALAGTAYPIDREQLAQDLGFRRATRNSLDSVSDRDHVMELMSVASISMLHLSRLAEDMIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGSLAGMMMTVKALPLAYNKDMQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANSTELADYLVAKGIPFREAHHIVGVAVVGAIAQGCALEELSLEQLQSFSPVIEADVYQILTIESCLEKRSALGGVSPKQVAYAVEQADKRLAARDTTLVKVRPARITDIETLESMVAYWANLGENLPRTRSEIIRDIGLFAVSEHQGLVTGCASLYIYDSGLAEIRSLGIEAGWQRQGQGTAVVQYLIDKAKDMAIKKLFVLTRAPEFFLKQNFVQTSKSLLPEKVLKDCDQCPRQHACDEVALEFNLSEQIISQVKVA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MALRIEDKKAIVAEVAEQMSSALSAAVADYRGLTVNEMTSLRKQARESGVYLRVVRNNLARLAIKGTEFECLADALKGPLVLALSKDAPGAAAKLFKNFQKDHNAFEVKNLAMSGELFGPEKLDDFAKLPTREEALATLLNVMQAPVTKFVRTLNEIPSQAVRVFAAVGDSK", "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": "MEYDEKLVRFRQAHLNPFNKHLGPRHHEQEPNEKAQEVTSEDTLPELPAGEPEFCYSERMMDLGLSEDHFSRPVGLFLASDVQQLRQAIEECKQVILELPEQSEKQKDAVVRLIHLRLKLQELKDPNEEEPNIRVLLEHRFYKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISRPCVSSKVSHQAEYELNICPETGLDSQDYRCAECRAPISLRGVPSEARQCDYTGQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFNYVEELVEIRKLRQDILLMKPYFITCKEAMEARLLLQLQDRQHFVENDEMYSIQDLLEVHMGRLSCSLTEIHTIFAKHIKLDCERCQAKGFVCELCKEGDVLFPFDSHTSVCNDCSAVFHRDCYYDNSTTCPKCARLTLRKQSLFQEPGLDVDA", "text": "FUNCTION: Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. Involved in bone resorption. SIMILARITY: Belongs to the DEF8 family."}
{"protein": "MRKASLSRKTNETSVHLTLELDGEGTSTIETGIGFFDHMLTLLAKHGGINLDLSCDGDLEVDQHHTVEDIGIVLGQTLREALGNKEGITRYANVMSPMDEALSSIAFDISGRSYLVYNVEGLKEKVGTFDTELVQEFFQAFASNAQVTLHINLLYGVNSHHIIESIFKGFGRVIRQGCSIDLNQKGIPSTKGSL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MMKFIKKEQIKNLGPNSKLLKQYKSQLTNLTSEQLEIGVGLLLGDAYIRSRDNGKTNCIQFEWKNKAYIDHICLKFDEWVLSPPHKKMRINHLGNEVITWGAQTFKHEAFNELSKLFIINNKKHIINNLIEDYVTPKSLAYWFMDDGGKWDYNKGSMNKSIVLNTQCFTIDEVNSLINGLNTKFKLNCSMKFNKNKPIIYIPHNSYNIYYELISPYIITEMRYKLPSYEGTSKDYNKIH", "text": "FUNCTION: Endonuclease involved in mitochondrial 21S rRNA gene intron homing. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the LAGLIDADG endonuclease family."}
{"protein": "MISTVALFWALCVVCIVNMARYFSSLRALLVVLRGCDPLLYQYVDGGGFFTSHGQPSKQMRLVWYIYAQRYRDHHDDEFIRRCERLRCQFILTSALCGLVVVSMVALLIWH", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the universal stress protein B family."}
{"protein": "MARDATKLEATVAKLKKHWADSAPHDMRAAFKSDPGRFERYSLSLDDLLFDWSKCRVNDETIGLLKELAIAADVEGRRAAMFAGEHINNTEDRAVLHVALRDTSSKEVLVDGHNVLPDVKEVLDRMAAFADGIRSGAIKGATGKKITDIVNIGIGGSDLGPVMATLALSPYHDGPRAHFVSNIDGAHIADTLGILDPATTLVIIASKTFTTIETMTNAQTARKWVADALGEAAVGAHFAAVSTALDRVAAFGIAEDRVFGFWDWVGGRYSVWSAIGLPVMIAIGPEDFRKFLAGAHSMDVHFRDAPLEKNLAVWLGLIGYWHRAICGYGSRAIIPYDQRLARLPAYLQQLDMESNGKSVTVDGKPVSGPTGPVVWGEPGTNGQHAFFQLLHQGTDTIPLEFIVAAKGHEKHLDHQHEMLLANCLAQSEALMKGRTLDEARAQLKAKNLPESEVERIAPHRVFSGNRPSLTLVHDKLDPFALGRLVALYEHRVFVEAQIFGINAFDQWGVELGKELATELLPVVSGEESSDGRDASTQGLVAHLHARRKA", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MRKYFKERDVPFIIFLMGPTASGKTSVVIELKKQKLGIKIISVDSALVYKNMNIGTAKPSVDELEIAPHQLIDIRDPADCYSVSDFYHDAILEINKIIRSGYVPVLVGGTMLYFKTLLTGLYQLPGKSQNIRNDLIYEAQKIGWVNMYNKLKCIDPIVSKTIHCNDHKRIIRALEVFLSSGKTLTELKQKFLNQQSQRYKVLQFALMPSKREFLYNRIEQRFYKMLKSGFEDEVRLLFSRPDLHDGYQSSISCVGYRQMWEYLSGNVEYDQMIYKGIYATRRLVKNQLTWLKKWPNVHWLNGDNVLIAVNDMLSVLSKYSCVI", "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": "MTTLFISDLHLTPSRTDITECFVQFMRNEAVNAEALYVLGDLFEFWIGDEDCTPFAERIRNEFKALTTSGVPVYFIQGNRDFLLGQRFCRETGITLLDDVCTIDLYGEKVVILHGDTLCIDDLKYQEFRKTVHQRWLQWIFKRIPWFIKKRIVAKVQSGVRDDKQHKSLEIMDVNQQEVAQVMSQFCVKLMIHGHTHRPNIHHFEHDNLPLTRIVLGDWYSQGSVLKVTADGYSLEQRPFFTE", "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": "MIKLIVGLGNPGAEYTATRHNAGFWLIDQLAREAGTTLRDERRFHGFYAKARLHGEEVHLLEPQTYMNRSGQSVVALAQFFKILPDQILVAHDELDLPPGTVKLKLGGGSGGHNGLKDITAHLSSQQYWRLRIGIGHPRDLIPESARAGAKPDVANFVLKPPRREEQDVIDASIERALAVMPMVVKGELDRATMQLHRN", "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": "MVVFTGSTVEEAIQKGLKELDIPRMKAHIKVISREKKGFLGLFGKKPAQVDIEAISETTVVKANQQVVKGVPKKINDLNEPVKTVSEETVDLGHVVDAIKKIEEEGQGISDEVKAEILKHERHASTILEETGHIEILNELQIEEAMREEAGADDLETEQDQAESQELEDLGLKVETNFDIEQVATEVMAYVQTIIDDMDVEATLSNDYNRRSINLQIDTNEPGRIIGYHGKVLKALQLLAQNYLYNRYSRTFYVTINVNDYVEHRAEVLQTYAQKLATRVLEEGRSHKTDPMSNSERKIIHRIISRMDGVTSYSEGDEPNRYVVVDTE", "text": "FUNCTION: Forms a complex with KhpA which presumably binds to about 170 cellular RNAs (mRNA, tRNA intergenic RNA and sRNAs); the proteins alone each bind the same set of RNAs. Suppresses the requirement for PBP2b (penA, a transpeptidase) in peripheral peptidogylcan (PG) synthesis (PubMed:28941257). May function as a pleiotropic RNA chaperone controlling pneumococcal cell division, including PG homeostasis and regulating peripheral PG synthesis by the elongasome (Probable). FUNCTION: Forms a complex with KhpA which stimulates or controls elongasome-mediated lateral cell wall biosynthesis (PubMed:30842445). RNA-bonding protein; overexpression leads to cell elongation, suggesting it plays a role in cell division and maintenance of cell shape (PubMed:27776484). In cell elongation the phosphorylated form activates cell elongation while the non-phosphorylated form is less active or inactive (Probable). Probably plays a role in regulation of other RNAs (By similarity). FUNCTION: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to midcell in the septal area; some protein remains in the cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Some protein localizes to midcell in the septal area, the rest remains in the cytoplasm. SIMILARITY: Belongs to the KhpB RNA-binding protein family."}
{"protein": "MPLIFKIGYNVIPLQDVILPTPSSKVLKYLIQSGKLIPSLKDLITSRDKYKPIFISHLGFNQRRIFQTNGNLKTITKGSRLSSIIAFSTQANVLSEVADEGIFETVYGKFHIMIESIEIVEVEKLKEEVEKHMNDNIRVRFVSPTLLSSKVLLPPSLSERYKKIHAGYSTLPSVGLIVAYAYNVYCNLIGKKEVEVRAFKFGILSNALSRIIGYDLHPVTVAIGEDSKGNLRKARGVMGWIEFDIPDERLKRRALNYLLTSSYLGIGRSRGIGFGEIRLEFRKIEEKEG", "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, generating an 8 base- long tag known as the 5' handle. SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas6 family."}
{"protein": "MASEDPSVSGVSGRYATALFELARDEKVIDAVKADLDKFSAMLVESPELLRLVRSPVFGAEAQTKALGAVLDKAGIAGISANFLKLLAANRRLFVVADVIGAYRALVARFKGEATADVTVAETLSDKNLEALKLALKSVTGKDVTLNINVDPAIIGGLVVKLGSRMVDSSIRTKLNSIKHAMKEAG", "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": "MIYKVLFQADKTQSPLREATKSLYLEANSAVEARQLVEDNTPYNIEFVQELTGEHLAYEQESEDFKLTEF", "text": "FUNCTION: A non-essential component of RNA polymerase (RNAP). SIMILARITY: Belongs to the RNA polymerase subunit epsilon family."}
{"protein": "MKVTLIVILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLFECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKV", "text": "FUNCTION: Neurotoxin active on both insects and mammals. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2) subfamily."}
{"protein": "MTLLAVNGGSPIRSQQWPLWPAPAPGALDALNEVLHSGRWAISGPYQGKQSFERRFAAAFAEFHEIGHCVPTSSGTASLMVALEACGVGAGDEVIIPGLTWVANASTVAGVNAVPVPVDVDPQTLCLDPAAVERAITPRTAAIVVVHLYSAVADLDALTAIAERHEIPLIEDCAQAHGARYRDRRVGTFGAFGTFSMQHSKVLTSGEGGAVITGDAALSRRAEHLRADGRTYTPDEPAVGEMELAQTAELMGSNRCLSEFQAALLLGQLELLDEQNERRRANAALLDEGLGALGIQPQVSSPGTTERTYYEWAGRIEDDGIGQIGVERIAPAVAAELSGAAIYASYPPMNHNRLYQPATRARFKGIAGLDLTGYSLPVAEDAGQRVVTIHHSALLGDESDMKDIVRAFEKVFANHRELRG", "text": "FUNCTION: Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo- inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L- glutamine as the amino donor. Also catalyzes the transamination of 3- amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine (2-DOS). SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-deoxy- scyllo-inosose/scyllo-inosose aminotransferase subfamily."}
{"protein": "MAEKVLVTGGAGYIGSHTVLELLEAGYSPMVIDNFHNAIRGGGSMPESLRRVQDLTGRSVEFEEMDILDQAALQRLFKKHSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKAWNAVLLRYFNPIGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREVLNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLALKELGWSAALGLDRMCEDLWRWQKQNPSGFGTQA", "text": "FUNCTION: Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MSLYEHAALPLASSPSILGPISGGRNRGNIQLQSIPIEFQAVVFAGFGNSLYPLTGSDALPKALLPIGNKPMLHYPLYWLEAAGFTSAILICMEEAEAHINAWLRSGYEGHMRIHVEAPTILDDSKSSADALRAVSHLIKNDFVCLSCDSIVGLPPIYGLDKFRLDNPSALAVYSPVLKYEHITSQSKEIDAKQLIGIEEKTSRLLYAKSSADVGSDFTFRMSLLWKHPRVTLNTNLSDAHIFVFKHWVIDLIREKESISSIRGDLIPYLVKCQYQKSFTVRENIQRFLSSPNNIDNYDGGLSSQEIKINALIAKDGIICSRANNLPNYFELNKCIAKLTPEQRLVDVTVSERALVGADCMVNEGTTIKDNSNIKKSIIGKNCVIGKGVVVSNSILMDNIVVEDGVRLESCIVASGAQIGAKSKLRECEIGVDHRVEAGRIARGERLVDMEKIETDMD", "text": "FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2- bound GDP for GTP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family."}
{"protein": "MARPDGRLPDHLRPVTLTRGWSTHPEGSVLVEFGATRVLCTASVTEGVPRWRKGSGLGWVTAEYAMLPRATNTRSDRESVKGRVGGRTHEISRLIGRSLRASIDLKALGENSVVLDCDVLQADGGTRTAAITGAYVALYDAVTWLAARRSLAGRPENVMHRSVAAVSVGVVAGEPRLDLNYDEDATAEVDLNVVCTGTGDFVEVQGTGEAGVFSRGQLDALLDLAVAGCLDLAEAQRKALS", "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": "MSEIRLIRAINDELYLVEVQATLERKADSLHIGDLKIIKEKNSEKKKATLTVGNQYMEGVVESLKKPLAVLQKTNADPVDVYSSPSHELKCCSIIRERIRFSSRPLPTK", "text": "FUNCTION: Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Replication factor C (RFC) complex has an essential but redundant activity in sister chromatid cohesion establishment. An RFC-like complex (ctf18-RFC) is formed where ctf18 replaces rfc1 in the RFC complex along with the association of dcc1 and ctf8. This complex is required for efficient establishment of chromosome cohesion during S-phase. Acts as a PCNA loader, loading PCNA onto primed templates. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CTF8 family."}
{"protein": "MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSADQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTTSFDEYWKKDSDAELYHFIGKDIVYFHSLFWPAMLEGSHFRKPTNLFVHGYVTVNGAKMSKSRGTFIKASTWLKHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLAAELADPQLYKTFTDAAAVIGEAWESREFGKAIREIMALADIANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPTLSERVEAFLNSELNWDAIEQPLLGHKVNTFKALYNRIDMKQVEALVESSKEEVKAAAAPVTGPLADFPIQETITFDDFAKIDLRVALIENAEFVDGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRQTVMVANLAPRKMRFGVSEGMVMAAGPGGKDIFLLSPDDGAKPGQQVK", "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": "MMRYGSAATVTTSETASSQKPGGVCRLRLTLPAEASLRPKQEEINRDTSVNADIRSTNERRKKRNGYVLSEKNTAEPPTLHLYTIPKNNTPSAVASSGVVYGVVQRAENNHQNEVVVYEWSTNQLKEEMNYIKDVRGTLEKIREKMFGEYDEMKQKVKQLTQEIKVSSVQKEFLESHSQAQSTALDTFGTINSSLNAASIEMQKTLVDMTLENTNIKDEMKNIKHSYEESLVRLKEKQQLLDSAQNENQLLKVKIESSQEANAEVMREMTRKLYSQYEEKLRQEELKYTAEKDMLVDQTRQYLKAIEDASEKVRLAENKIEERDAKIAELDKLVHRMEQEREHLQDQLIRHEERIQDLDNRMQMQSPDRNQRLEEVATSLRERIKHLDDMVHCQQKKVKHMIEEIELLKKKVHYKDLLIQQLLERIAFLEGENTELQDKVDYLMANKPKTDKETKDIGTSCNLSESQRILTVCVTENEARSIFSI", "text": "SIMILARITY: Belongs to the MYZAP family."}
{"protein": "MSIQASPVTILGAGSYGTALAIALSRNGYPTYLWGHNPTACAQMAQERQNARFLPDISFPEALRVESDLKSAVEKSKDLLIVVPSHVFGEVIQQIKPFLHNRHRIIWATKGLERGTGRLLQNLVEQELGSQYPLAVLSGPTFAKELAAGLPTAITLAAENEQFAKEFQARIHCSKHFRVYINNDMVGVQLGGAIKNVIAISAGMSDGMGFGANARTALITRGIAEISRLGVSLGANVNTFMGMSGLGDLVLTCTDNQSRNRRFGMMLGQGVDARTAMDEIGQVVEGYYNTKEAYMLAQKQGIEMPITEQIYQVLFCGKDAKEAATALLGRKSKVE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MKFYLVGGAVRDNLLKLPIKDRDYMVVGAAPEQMFELGYKQVGKDFPVFLHPKTQQEYALARTERKTGSGYGGFSCDASPDVTLEEDLLRRDLTINAIAQDDKGELFDPYGGIKDIESKMLRHVSDAFVEDPLRVLRVARFAARFHHLGFTVADETLALMTKISQSGELEALTSERVFLELDKALSTQNPQIFIEVLNQCQALEILFPEIHALFGVPQPEKWHPEIDTGIHTLMVLAQAAKLSDENSVRFAALVHDLGKALSPKATLPKHHGHGQSGLALIKVLCARAKVPNEYRDLALLVSDQHQNVHNIRELRPETLIKIFDKADLWRKPDRLEQLATACEADSKGRLGLENSPYPQADYLRESFQVANSVAVKPIIEAGFKGAEIKEQLKLKRIEIVTEFKRNFNESAIE", "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": "MEPFVSRIYFGDLLAGTDEAGRGPLAGEVVAAAVILDPAQPITGLADSKKLSEKKREALFVEIQEKALAYGIARATIEEIDELNILHASMLAMSRAVALLSIEPEYVLVDGNRIPPNLPCSAEAVVKGDARHAAISAASILAKVTRDRDIVQVAQIYPEYGFEKHKGYPTALHLEAIRLHGITPIHRRSFGPVKKILEG", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MTDKKVTRLRRARKARLKMHELEAVRLCVFRSSQHIYAQVISADGSKVLASASTLDKELRDGATGNIDAATKVGKLVAERAKAAGVSQVAFDRSGFKYHGRVKALADAAREGGLEF", "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": "MTRLEKIYREKVVPVMQKEFSYSSSMQLPGIEKISLNIGLGAASQNNKLMEEAVAELSAIAGQKAVVTRAKKSIAAFKLREGMPIGARVTLRRDRMWDFLDKLMNFALPRVRDFRGIPDRGFDGRGNFTLGIKEHTIFPELEVDRVENPKGMNITIVTTAATDKEGKFLLDQLGMPFRK", "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": "IVTVDCSDYPKPVCTLDYMPLCGSDNKTYSNKCNFCNAVVDSNGTITLSHFGRC", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MEIKKAAFVISNTDVRKCPDTRLPEYAFIGRSNVGKSSLINMLTGQKGLAMTSQKPGKTQLINHFIIDDSWYLVDLPGYGYARLGASNRESLRRIIETYILCREQLSSLFVLIDCRHEPQKIDLEFLQWLGENGIPFSIVFTKADKLSFSRLKENTEAYKQKLLETWEELPPVFITSSEKKTGKEELLDYIDSINQELATK", "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": "MPNIEIAQADEVIITTLEELGPAEPTTDQIMRFDAAMSEDTQGLGHSLLKEVSDIQKSFKTVKSDLHTKLAVSVDNPNDLMLMQWSLIRITIQEELIAKTAGRMSQNVETLSKGG", "text": "FUNCTION: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function. FUNCTION: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function. SIMILARITY: Belongs to the YscI/HrpB family."}
{"protein": "MGKKYTESVKLVDKNTLYTVQEAIELVTKTSKAKFDETVELAVRLGVDPRHADQQVRGAVVLPHGTGKTVRVLVFAKGDKVNEAQEAGADFVGAEELVEKIQKENWFDFDVVVATPDMMGVVGRLGRVLGPKGLMPNPKSGTVTFDVAKAIADIKAGKVEYRVDKTAIIHVPIGKSSFGEEKLSDNFHVLMEAVVKAKPAAAKGQYIKSVAISSTMGPGIKINPGKVLE", "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": "MSIRNDNASGGYMQPDQSSNASMHKRDLRVEEEIKPLDDMDSKGAVAADGEVHLRKSFSLWSILGVGFGLTNSWFGISTSMVAGISSGGPMMIVYGIIIVALISICIGTSLGELSSAYPHAGGQFWWSLKLAPPKYKRFAAYMCGSFAYAGSVFTSASTTLSVATEVVGMYALTHPEFIPKRWHIFVCFELLHLFLMFFNCYGKSLPIISSSSLYISLLSFFTITITVLACSHGKFNDAKFVFATFNNETGWKNGGIAFIVGLINPAWSFSCLDCATHMAFEVEKPERVIPIAIMGTVAIGFVTSFCYVIAMFFSIQDLDAVLSSTTGAPILDIYNQALGNKSGAIFLGCLILFTSFGCVIACHTWQARLCWSFARDNGLPLSRLWSQVNPHTGVPLNAHLMSCAWITLIGLLYLASSTAFQSLITGCIAFLLLSYIIPVICLLAKKRNIAHGPFWLGKFGFFSNIVLLGWTVFSVVFFSFPPVLPVTKDNMNYVCVVIVGYTAYSILYWKYKGKKEFHALEESENEQAEYSNNFDTIEDSREFSVAASDVELENEHVPWGKK", "text": "FUNCTION: Sole choline transporter in yeast. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid/choline transporter (ACT) (TC 2.A.3.4) family."}
{"protein": "MQNVMKFHLVIFMLFGSVRLQNPTIERKQCTMSNCFDFSKCSTSKKVYIHPMEKRFEESPQSVIYSKILKHFLESNHYTNDPNEACIFLLGIDTTDRDVRSQNYVKNVNDYIESLDPSVWNNGRNHLIFNFYHGTFPDYDDHNLNFDTGEAMIARASSSENNFIKVFDVSLPLFHENHPYEIKESKSERNDDRIENQRKYLVSFKGKRYVYGIGSGTRNLVHHLHNGDDIVMVTTCKHNNDWQVYQDDRCQRDNDEYDRWEYDELLANSTFCLVPRGRRLGSFRFLETLRSGCVPVVISDSWILPFSETIDWNSAAIVVAERDALSIPELLMSTSRRRVKELRESARNVYDAYLRSIQVISDHVLRIIFKRIDNKIELEDHQ", "text": "FUNCTION: Required for the biosynthesis of heparan sulfate by positively regulating N-acetylglucosamine transferase II (GlcNAcT-II) and glucuronyl transferase II (GlcAT-II) activities of glycosyltransferase rib-2 (PubMed:17237233). Probably not directly involved in chondroitin sulfate biosynthesis but negatively regulates chondroitin sulfate levels (PubMed:16828468, PubMed:17237233). Maternally required for normal ventral epidermal enclosure and for embryo elongation during the early stages of embryonic development (PubMed:17237233). In addition, involved in the elongation of the pharyngeal isthmus and in the organization of the actin cytoskeleton in the pharyngeal muscles during the later stages embryonic development (PubMed:16828468). In adults, regulates egg-laying and the normal morphogenesis of the vulva (PubMed:17237233). Also involved in the directed migration of hermaphrodite-specific neurons (PubMed:17237233, PubMed:24052309). SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus. SIMILARITY: Belongs to the glycosyltransferase 47 family."}
{"protein": "MTTTIPTSKSACSVTTRPGNAAVDYGGAQIRAYLHHLATVVTIRGEIDAANVEQISEHVRRFSLGTNPMVLDLSELSHFSGAGISLLCILDEDCRAAGVQWALVASPAVVEQLGGRCDQGEHESMFPMARSVHKALHDLADAIDRRRQLVLPLISRSA", "text": "FUNCTION: Part of a signaling pathway that enables adaptation to osmotic stress through cell wall remodeling and virulence factor production (PubMed:24309377). Unphosphorylated OprA forms a complex with the anti-anti-sigma-factor paralog Rv2638 that dissociates on OprA phosphorylation by PknD (PubMed:17411339). Phosphorylation of OprA may stimulate the release of SigF from an inhibitory complex and enable the transcription of osmotically regulated genes, such as oprA and the ESX- 1-associated virulence factor espA (PubMed:24309377). SIMILARITY: Belongs to the anti-sigma-factor antagonist family."}
{"protein": "MSERKLFTSESVSEGHPDKIADQISDAILDAILAKDPEAHVAAETAVYTGSVHVFGEISTNAYVDINRVVRDTIAEIGYTNTEYGFSAETVGVHPSLVEQSPDIAQGVNEALEVRGNADQDPLDLIGAGDQGLMFGFAVDETEELMPLPIALSHKLVRRLAELRKSGEISYLRPDAKSQVTVEYDENDRPVRVDTVVISTQHDPEVTNEQIHQDVIDKVIKEVIPSSYLDDKTKFFINPTGRFVIGGPQGDSGLTGRKIIVDTYGGYSRHGGGAFSGKDATKVDRSASYAARYIAKNIVAADLAKKAEVQLAYAIGVAQPVSVRIDTFGTGTVAESQLEKAARQIFDLRPAGIIQMLDLKRPIYRQTSAYGHMGRTDIDLPWERLDKVDALKEAVK", "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": "MKMELKVKPIENGTVIDHISGSKALKVYKILNIEEKLPITLALNVPSKKGVMKDILKIEGLELTKDDVNKIALISPDATINIIKEGKVIKKFKVDLPKRIDGIIKCTNPNCITNKENIEGKFSIEQKNTLKIRCEYCEKFINSIIISK", "text": "FUNCTION: Involved in allosteric regulation of aspartate carbamoyltransferase. SIMILARITY: Belongs to the PyrI family."}
{"protein": "MFESKINPLWQSFILAVQEEVKPALGCTEPISLALAAAAAAAELDGTVERIDAWVSPNLMKNGMGVTVPGTGMVGLPIAAALGALGGDAKAGLEVLKDASAKAVADAKAMLASGHVAVMLQEPCNDILFSRAKVYSGDSWACVTIVGDHTNIVRIETNKGVVFTQADNAQEEEKNSPLGVLSHTSLEEILAFVNAVPFDAIRFILDAARLNGALSQEGLRGSWGLHIGSTLAKQCDRGLLAKDLSTAILIRTSAASDARMGGATLPAMSNSGSGNQGITATVPVMVVAEHVGADDERLARALMLSHLSAIYIHHQLPRLSALCAATTAAMGAAAGMAWLIDGRYDTIAMAISSMIGDVSGMICDGASNSCAMKVSTSASAAWKAVLMALDDTAVTGNEGIVAHNVEQSIANLCSLACRSMQQTDKQIIEIMASKAH", "text": "SIMILARITY: Belongs to the UPF0597 family."}
{"protein": "MFEYPQGYKLIAGVDEVGRGPLVGAVVTAAVILDPHNPIEGLADSKKLSEKKRLALAEEIKEKARAWALGRAEADEIDEINILQASLLAMTRAVKSLKIQPHFVLIDGNKIPKDLAIPAQAVVKGDSLVAEISAASILAKVARDQEMEELDKQYPEYAFAQHKGYPTKLHLEKLAELGALPQHRRSFAPVKKALEQF", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MSAAADRLNLTSGHLNAGRKRSSSSVSLKAAEKPFKVTVIGSGNWGTTIAKVVAENCKGYPEVFAPIVQMWVFEEEINGEKLTEIINTRHQNVKYLPGITLPDNLVANPDLIDSVKDVDIIVFNIPHQFLPRICSQLKGHVDSHVRAISCLKGFEVGAKGVQLLSSYITEELGIQCGALSGANIATEVAQEHWSETTVAYHIPKDFRGEGKDVDHKVLKALFHRPYFHVSVIEDVAGISICGALKNVVALGCGFVEGLGWGNNASAAIQRVGLGEIIRFGQMFFPESREETYYQESAGVADLITTCAGGRNVKVARLMATSGKDAWECEKELLNGQSAQGLITCKEVHEWLETCGSVEDFPLFEAVYQIVYNNYPMKNLPDMIEELDLHED", "text": "FUNCTION: Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MIIANVIRSFSLTLLIFAALLFRPAAAEEFSASFKGTDIQEFINTVSKNLNKTVIIDPSVRGTITVRSYDMLNEEQYYQFFLSVLDVYGFAVINMNNGVLKVVRSKDAKTAAVPVASDAAPGIGDEVVTRVVPLTNVAARDLAPLLRQLNDNAGVGSVVHYEPSNVLLMTGRAAVIKRLLTIVERVDNAGDRSVVTVPLSWASAADVVKLVTELNKDTSKSALPGSMVANVVADERTNAVLVSGEPNSRQRIIAMIKQLDRQQATQGNTKVIYLKYAKASDLVEVLTGISSTMQSEKQAAKPVAALDKNIIIKAHGQTNALIVTAAPDVMNDLERVIAQLDIRRPQVLVEAIIAEVQDADGLNLGIQWANKNAGMTQFTNSGLPISTAIAGANQYNKDGTVSSSLASALSSFNGIAAGFYQGNWAMLLTALSSSTKNDILATPSIVTLDNMEATFNVGQEVPVLTGSQTTSGDNIFNTVERKTVGIKLKVKPQINEGDSVLLEIEQEVSSVADAASSTSSDLGATFNTRTVNNAVLVGSGETVVVGGLLDKSVSDTADKVPLLGDIPVIGALFRSTSKKVSKRNLMLFIRPTVIRDRDEYRQASSGQYTAFNDAQSKQRGKENNDAMLNQDLLEIYPRQDTAAFRQVSAAIDAFNLGGNL", "text": "FUNCTION: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of pullulanase (PubMed:2677007). 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": "MSTLARTAHVTRQTSESTIDLQLDLDGTGASEISTSVPFYDHMLTAFAKHSLTDLRVTATGDTHIDVHHTVEDVGIVLGQAIREALGDKSGIARFGDALVPLDEALVQSVVDISGRPFLVHSGEPAGFEMHLIGGHFTGSMVRHVFEAITFHAGLTVHVTVLGGRDPHHIAEAEFKSFARAFRQAKELDPRVSGIPSTKGAL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MAFKLPNLPYAYDALEPYIDQRTMEFHHDKHHNTYVTKLNATVEGTELEHQSLADMIANLDKVPEAMRMSVRNNGGGHFNHSLFWEILSPNSEEKGGVIDDIKAQWGTLDEFKNEFANKATTLFGSGWTWLVVNDGKLEIVTTPNQDNPLTEGKTPILLFDVWEHAYYLKYQNKRPDYMTAFWNIVNWKKVDELYQAAK", "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. 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. May play a role in maintaining cell viability during the late-exponential and stationary phases of growth since it becomes a major source of activity under oxidative stress. Has a role in resisting external superoxide stress. Involved in acid tolerance and the acid-adaptive response. Mediates the derepression of perR regulon in the response to HOCl stress at low level of SOD activity (By similarity). SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MSLTTYPHIYKKEQILKLKRLNKLSNDRKFFFSSVKGTLPGIISHCNNINEILGRCYLGICKLNSFFGLSKDPSDKLSVSKSPSVYTLPSKIFKEGGGNGDNTTTQTDILKNAQDQVILSKKIDELQTQVKELSSKIEPEPLTKEDIKKTYETLSRIESGLKGIIGIE", "text": "FUNCTION: This protein is involved in virus transmission. SIMILARITY: Belongs to the caulimoviridae ORF II family."}
{"protein": "MARKTPLNRIRNIGIAAHIDAGKTTTSERILFYTGVSHKIGEVHDGAATMDWMEQEKERGITITSAATTCFWKDHQINLIDTPGHVDFTIEVERSMRVLDGAVSVFCSVGGVQPQSETVWRQANKYGVPRIVFVNKMDRIGANFYNVENQIKQRLKANPVPINIPIGAEDTFIGVIDLVQMKAIVWNNETMGAKYDVEEIPSDLLEKAKQYREKLVEAVAEQDEALMEKYLGGEELNIEEIKKGIKTGCLNMSLIPMLCGSSFKNKGVQTLLDAVIDYLPAPTEVVDIKGIDPKTEEEVFVKSSDDGEFAGLAFKIMTDPFVGQLTFVRVYRGNLESGSYVYNSTKDKKERVGRLLKMHSNKREDIKEVYAGEICAFVGLKDTLTGDTLCDEKNAVVLERMEFPEPVIHIAVEPKTKADQEKMGVALGKLAEEDPSFRVMTQEETGQTLIGGMGELHLEIIVDRLKREFKVEAEIGQPQVAFRETIRSSVSKEHKYAKQSGGRGQYGHVFIKLEPKEPGSGYEFVNEISGGVIPKEYIPAVDKGIQEAMQNGVLAGYPVVDFKVTLYDGSYHDVDSSEMAFKIAGSMAFKEASRAANPVLLEPMMKVEVEVPEEYMGDVIGDLNRRRGQINSMDDRLGLKIVNAFVPLVEMFGYSTDLRSATQGRGTYSMEFDHYGEVPSNIAKEIVEKRKG", "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": "MKFFAVLALCIVGAIASPLTADEASLVQSSWKAVSHNEVEILAAVFAAYPDIQNKFSQFAGKDLASIKDTGAFATHATRIVSFLSEVIALSGNDSNAAAVNSLVSKLGDDHKARGVSAAQFGEFRTALVAYLQANVSWGDNVAAAWNKALDNTFAIVVPRL", "text": "SIMILARITY: Belongs to the globin family."}
{"protein": "MAKDIKFSEEARRSMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGLRKGIEKAVTAAIEELKTISKPIEGKSSIAQVAAISAADEEVGQLIAEAMERVGNDGVITLEESKGFTTELDVVEGMQFDRGYASPYMITDSDKMEAVLDNPYILITDKKISNIQEILPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGEVITEELGRDLKSATVESLGRAGKVVVTKENTTVVEGIGNTEQIAARIGQIRAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVAGGGTSLMNVYTKVASIVAEGDEATGINIVLRALEEPVRQIAINAGLEGSVVVERLKGEKVGVGFNAATGEWVNMLESGIVDPAKVTRSALQNAASVAAMFLTTEAVVADKPEPNAPAMPDMGGMGMGGMGGMM", "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": "MWKFIKSATDQNNWLEHDQNEIVFWGRSNVGKSSLINALASQKIAKTSSTPGRTRLINYFETQRKKIIVDLPGYGFASMSKKAQSKISGIIDFYFRNSKNSKNICILIDAKIGFSYIDLEMIDYLKSLGLLFDIIITKIDKANQSQKHRVKQQALTFSDDINIFMVSSEKKQGLSDLVEHFEL", "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": "MDFKQYSPEELKECSMIEVVHSVLGDKRQATTFNELVQEIAQVLGLSQEQVNAKIAQFYTDLNIDGRFINLGENRWGLRSWYPYEQIDEEILPQPKPKKKRKVEDDGFDDYIEEDEDFDDADVTEDEDDDVEDLDKVLEDEDGDDDDLDDLDEDDDDFAEEELEYDETEEEEEEEL", "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": "MKRNFDSVKRLVIKIGTSSLVLPSGKINLEKIDQLAFVISSLHNKGIEVVLVSSGAMGFGLNVLDLETRPAEVGKQQAVSSVGQVAMMSLYSQVFSHYQTKVSQLLLTRDVVEYPESLANAINAFESLFELGVVPIVNENDAVSVDEMDHATKFGDNDRLSAIVAKVVGADLLIMLSDIDGLFDKNPNVYEDATLRSYVPEITEEILASAGAAGSKFGTGGMMSKIKSAQMVFENQSQMILMNGENPRDILRVLEGAKIGTLFKQED", "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": "MPTYNFAAGPATLPRPVLEQVQRELLDYQGSQVSILEISHRSPVFREIYQQAKERLLQLMGLSADEYTPLFLQGGGTLQFTMVPLNLARDHHRVAYADTGHWSARAIEEAKKLPDLTVDVVTEAGPDFAHIPAVPDLPADTYDYLHITTNNTIMGLAYQDLPQTAVLLVGDLSSNFLGQAYDFSSFDLIYAGAQKNLAPAGVTIVVVKNDYLTEDHGLPSMLNYPALAKKESALNTPPVFQIYFANLVLKWLKEQGGVQAMDELNRQKAGLVYDYLDQSKLFSNRVAPDSRSLTNIPFTTGKADLDQRFIKEAAAAGLVNLKGHRLVGGMRASLYNAMPLAGAVALRDFMHQFEQEI", "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": "MAIKKYKPTTNGCRNMSVSAFSEITTQTPERSLLVSHKDQAGRNNQGKITVRHRGGGVKRKYRLIDFKRNKDNIVGKVATIEYDPNRSANIALIHYVDGEKRYILAPKGLTVGMQIVSGKETDIKVANCLPLMNIPVGTTVHNIELKPGKGGQIARSAGSSCQIISREDKYVLLRLQSGEVRKVLATCRATIGEIGNESYKLINYGKAGKKRFLGIRPTVRGSAMNPNDHPHGGGEGRAPIGRKSPMTPWGKKARGVKTRDRKKASNALIIRRRKK", "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": "MEINKFRALSRRAQQLHYTSLNGLKRRCNNAHGAANFHSLKRATQTQIQKSQTKPLLKCGDSDIKEWNVAISSYMRTGRCNEALRVFKRMPRWSSVSYNGMISGYLRNGEFELARKLFDEMPERDLVSWNVMIKGYVRNRNLGKARELFEIMPERDVCSWNTMLSGYAQNGCVDDARSVFDRMPEKNDVSWNALLSAYVQNSKMEEACMLFKSRENWALVSWNCLLGGFVKKKKIVEARQFFDSMNVRDVVSWNTIITGYAQSGKIDEARQLFDESPVQDVFTWTAMVSGYIQNRMVEEARELFDKMPERNEVSWNAMLAGYVQGERMEMAKELFDVMPCRNVSTWNTMITGYAQCGKISEAKNLFDKMPKRDPVSWAAMIAGYSQSGHSFEALRLFVQMEREGGRLNRSSFSSALSTCADVVALELGKQLHGRLVKGGYETGCFVGNALLLMYCKCGSIEEANDLFKEMAGKDIVSWNTMIAGYSRHGFGEVALRFFESMKREGLKPDDATMVAVLSACSHTGLVDKGRQYFYTMTQDYGVMPNSQHYACMVDLLGRAGLLEDAHNLMKNMPFEPDAAIWGTLLGASRVHGNTELAETAADKIFAMEPENSGMYVLLSNLYASSGRWGDVGKLRVRMRDKGVKKVPGYSWIEIQNKTHTFSVGDEFHPEKDEIFAFLEELDLRMKKAGYVSKTSVVLHDVEEEEKERMVRYHSERLAVAYGIMRVSSGRPIRVIKNLRVCEDCHNAIKYMARITGRLIILRDNNRFHHFKDGSCSCGDYW", "text": "SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
{"protein": "MNHLLRRCRSISYVGLIITALIAILIGFLAGFLARKVIAESKIKSAENLARTILESAKKDAENKKREALLEAKEEIHRLRSDFEKEVRDRRGELQRLEKRLLQKEEILEKRAESLEQKEILLEQKQKEIQQLEEQITLLHKKQLEELERISGLTQEEAKSILLESVQKEIQHDMAVMIKEMENKAKEEADRRAREIVGLAIQRCAADHAAETTVSVVTLPNDEMKGRIIGREGRNIRTIETLTGIDLIIDDTPEAVVISGFDPIRREIARIALEKLIEDGRIHPARIEEMVEKAKKEVDNMIIKAGEEAAFEVGVHGLHPELIKLLGRLKFRTSYGQNVLKHSIEVAHLAGLMAYELGADASIAKRAGLLHDIGKAVDHEVEGPHVMIGAELAKRYHESDAVVHAIMAHHNDVEPQTIEAVLVQAADAISAARPGARREALEAYIKRLDKLEQIANSFEGVEKAYAIQAGREIRIMVKPEAISDDELVILARNISKKIEEEVEYPGQIKVTVIRETVAIDYAK", "text": "FUNCTION: Endoribonuclease that initiates mRNA decay. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RNase Y family."}
{"protein": "MSAITPYDWAIIAFVIGVTFLCVFMLTVPLLLGGKSWGRAKQEQFESGVVSAGGARIRLSAKFYLVAIFFVVFDLEALYLYAWSTSVREVGWLGYTTVVIFVVDLLIALVYAFSVGALSWAPADRRKLAGEKIKVGSPTMNIAEITRFNSIEELVTDPTGQIPAQSSGRVKSKTTPALSSEKE", "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": "MFLTLIAAIISFMVSAFTMPYFIKFYQLKKIGGQQMHEDVKQHLAKAGTPTMGGTVFLLVATAVSLLVSLFSIKNTQSLALISGILSIVVIYGIIGFLDDFLKIFKQINEGLTAKQKLALQLAGGLMFYFLHVSPSGISSINVFGYQLSLGIFYLFFVLFWVVGFSNAVNLTDGIDGLASISVVISLVTYGVIAYVQSQFDVLLLIGAMIGALLGFFCFNHKPAKVFMGDVGSLALGAMLAAISIALRQEWTLLIIGIVYVLETSSVMLQVSYFKYTKKKYGEGRRIFRMTPFHHHLELGGLSGKGKKWSEWQVDAFLWGVGSLASLLVLAILYVF", "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": "MRKRISAIIMTLFMVFMSCNNGGPELKSDEVAKSDGTVLDLAKISKKIKDAVEFAASVKEIETLVKSIDELAKTIGQKLTKDTGVLAADANNNNGGLIAGVYGIVTDVGTKLDGLLKVNGISEDIKTKINDSKSKGTAFLSKVKGDDDLCKKDATDAHAKNAIDKNDNTGGKGKTELIALNTAIDELLKAANEAVEAAIKELTAPVKAEKPSQNN", "text": "FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable small protein (Vsp) family."}
{"protein": "MKTKWLISVIILFVFIFPQNLVFAGEDKNEGVKVVRDNFGVPHLYAKNKKDLYEAYGYVMAKDRLFQLEMFRRGNEGTVSEIFGEDYLSKDEQSRRDGYSNKEIKKMIDGLDRQPKELIAKFAEGISRYVNEALKDPDDKLSKEFHEYQFLPQKWTSTDVVRVYMVSMTYFMDNHQELKNAEILAKLEHEYGTEVSRKMFDDLVWKNDPSAPTSIVSEGKPKRDSSSQSLQILSSAVIKASEKVGKERENFVQTSEELGLPLKIGSNAAIVGSEKSATGNALLFSGPQVGFVAPGFLYEVGLHAPGFDMEGSGFIGYPFIMFGANNHFALSATAGYGNVTDIFEEKLNAKNSSQYLYKGKWRDMEKRKESFTVKGDNGEKKTVEKIYYRTVHGPVISRDETNKVAYSKSWSFRGTEAQSMSAYMKANWAKNLKEFENAASEYTMSLNWYYADKKGDIAYYHVGRYPVRNSKIDERIPTPGTGEYEWKGFIPFKENPHVINPKNGYVVNWNNKPSKEWVNGEYSFYWGEDNRVQQYINGMEARGKVTLEDINEINYTASFAQLRANLFKQLLIDVLDKNKSTNGNYIYLIEKLEEWNNLKEDENKDGYYDAGIAAFFDEWWNNLHDKLFMDELGDFYGITKEITDHRYGASLAYKILNKESTNYKWVNVDQEKIIMESTNEVLAKLQSEKGLKAEKWRMPIKTMTFGEKSLIGIPHGYGSMTPIIEMNRGSENHYIEMTPTGPSGFNITPPGQIGFVKKDGTISDHYDDQLVMFAEWKFKPYLFNKKDINKAAKNVSALNMSK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S45 family."}
{"protein": "MSDLLDTVRGLAKKTDSKILMVVLDGVGGLPLTVNGDTELATARTPNLDALAQESQLGQLELVGAGITPGSGPGHLSLFGYDPLKYVVGRGALSAVGIGVKLNRGDVAVRGNFATLGAGRLILDRRAGRPSDEKNAEIVAKLRAAIPEIDGVAVEVYTESEHRFVVVFRAPEGQPLGANISDVDPQVTGVEPKTAIANDPSSEVTAGLINTFVARAEVALADEPQVNGVLFRGYSDVPHFPSFEDAYQLKAACIASYPMYKGLASLVGMDVLPVEGHEDALEGKVKALRENWAKYDFFYFHIKKTDSTGEDGDFAEKVHKIELFDELLPQLLELQPDVIAVVGDHSTPSKLKSHSWHPVPLLIRSNYGRRDPAQRYTEEEAARGTLGLRHGPDLMPLLMANALKLNKYGA", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily."}
{"protein": "MARRTRSSRAWHFVLSAARRDTDARAVALAGSSNWGYDSDGQHSDSDSDPEYSSLPPSIPSAVPVTGESFCDCEGQNEATFCNSLHTAHRGKDCRCGEEDEDFDWVWDDLNKSSATLLSCDNRKVSFHMEYSCGTAAIRGTKELGDGQHFWEIKMTSPVYGTDMMVGIGTSDVDLDKYHHTFCSLLGRDEDSWGLSYTGLLHHKGDKTSFSSRFGQGSIIGVHLDTWHGTLTFFKNRKCIGVAATRLQNRRFYPMVCSTAAKSSMKVIRSCASSTSLQYLCCYRLRQLRPNSGDTLEGLPLPPGLKQVLHNKLGWVLSMNCNHWKSPVPPPGTATPGAESLETRPCQRKRCRRS", "text": "FUNCTION: May be a 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. SIMILARITY: Belongs to the SPSB family."}
{"protein": "MGRGGGMGNPVNVGIAVQADWENREFISNISLNVRRLFDFLLRFEATTKSKLASLNEKLDILERKLEVLEVQVGSATTNPSVFN", "text": "FUNCTION: Promotes multiple, actin-dependent cell polarization events in the developing leaf epidermis. Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the BRK1 family."}
{"protein": "MIIRSPESEVKILVDRDPVKTSFEEWARPGHFSRTLAKGPETTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIRPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYADFLTFRGGLDPVTGGLWLTDIAHHHLAIAVLFLIAGHMYRTNWAIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWACIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWVQNTHALAPGATAPGATTSTSLTWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSIVQGRAVGVTHYLLGGIATTWAFFLARIIAVG", "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": "MAKQSMIARDVKRAKLADKFYAKREELKKIISDANSSDEDRWAAVLKLQTLPRDSSPSRQRNRCRQTGRPHGVLRKFGLSRIKVREAAMRGEIPGLKKASW", "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": "WIMGHMVNDLSLVDEFLNDGANSLELDVEFSSSGTAQRTHHGFPCDCFRYCTNSEKFSTYLDYIRQLTTPGNSKFRSRLILLVMDLKLNPLSSSAAYNAGADVALNLLNHYWQRGESEARAYIVLSLSTIDGAEFISGFKSTMEKEGFADKYYDKIGWDFSGNEDLQQIRDVLENYGIREHIWQGDGITNCLPRGDSRLKEALNLRYSPSYIYADKVYTWSIDEENSIKHALWLGVDGVMTNHPERVIEVLGKSKYSDKFRLATYDDSPWEK", "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": "MKKPFYKVLYVQVIFAIVVGVILGHYYPSLAVDMKPLGDGFIKLIKMVIGPIIFCTVVTGIAGMQDMKKVGRVGGKALLYFEIVSTCALVLGLAATHILRPGVGFNIDPATLNGKEVASYAAKAHGQSSVDFLMHIIPNTMIDAFAQGEILQILLIALLFGSVLAHLGERGRVVTDFIDGITRVLFGIVHIVTKLAPIGAFGAMAFTIGKYGVGSLVPLLKLIGTFYLTSVVFVLVVLGAIARFTGFSIIRFVGYIKEELLIVLGTSSSEAALPQLMEKLEKAGCSRSVVGLVVPTGYSFNLDGTNIYMTMAVLFIAQATNIELTWMQQLTLLAVAMLTSKGASGVTGAGFITLAATLAVVPTIPLSGMVLILGIDRFMSECRALTNIVGNGVATVVVSAWEKELDRAKLRAALSGNGEAAAGEAARV", "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": "MSEGVDLKELKRRMDGAIAAFKHDIASLRTGRASANVLDPVTVEAYGSRMPLNQVANITVPESRMLSVSVWDKSMVGAVERAIRESNLGLNPIVDGQNLRIPLPELNEERRKSLVKVAHDYAEKSKVAVRHVRRDGMDDLKKAEKDGEIGQDESRAQSERVQKMTDDVISEIDRLLAEKEKEIMQV", "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": "MLLNILAIILVFVISSQSEAVIPGCDYFDTVDISHIPKLNDSYAYEELIIPAHLTGLYTFRQLADGSQEPVKSHLRACICKLKPCIRFCCPRNKMMPNSRCSDGLTENLKRINPYLKITLEDGTIGKYYLLTDMIVLRYEFRYCEKVVSVQEDQYKLYENGSFMIKPDVNWTLSKQWYCLHPRLEDPNSIWILEHVYIPKSMPAVPQVGTISMVGCILTIAVYLYIKKLRNLLGKCFICYVFCKFVQYLIWAGGDLNLWNNICSLAGYTNYFFALASHFWLSVMSHQIWKNLRLINRDERSYHFLIYNIYGWGTPAIMTAITYLVDWAWEDRPDKLNWIPGVGLYRCWINTYDWSAMIYLYGPMLILSLFNVVTFILTVNHIMKIKSSVKSSTQQQRKCIQNNDFLLYLRLSVMMGVTGISEVITYFVKRHKFWRQVLRVPNFFHLGSGIVVFVLFILKRSTFQMIMERISGPRRQQPAS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth subfamily."}
{"protein": "MTSHAPDPIHQFEISRLINVSIGNVDFSFTNVSFFIIATVVLSSVFLFISSSSRRLVPTRMQSISEMAYEFVASTLRESAGVQGMKFFPLVFSLFVFILVANFIGLFPYFYTITSQIMITFSLAMLVILTVIGCGFYKHGIGFLKLFVPSGVPVMILPLVTVIEVISFFSRPISLSLRLFANMLAGHITLKVFSGFIVSMVGLGFIGVGGSILPLIMTVAITALEFLVAFLQAYVFTVLTCMYLNDAVHPGH", "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": "MTDTIGAGQPGQDAFPPVEELSYEQARDELIETVKILELGQMGLDESLKYWERGEALAKACEAHLDGASKRVEEALRKNAEGTDSAAHNEEAGED", "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": "MDDDQQFCLRWNNHQSTLISVFDTLLENETLVDCTLAAEGKFLKAHKVVLSACSPYFATLLQEQYDKHPIFILKDVKYQELRAMMDYMYRGEVNISQDQLAALLKAAESLQIKGLSDNRTGGGVAPKPESSGHHRGGKLSGAYTLEQTKRARLATGGAMDTSGDVSGSREGSSSPSRRRRKVRRRSMENDAHDNSNSSVLQAAASNQSILQQTGAGLAVSALVTTQLSSGPAAGTSSQASSTQQQQPLTSTNVTKKTESAKLTSSTAAPASGASASAAVQQAHLHQQQAQTTSDAINTENVQAQSQGGAQGVQGDDEDIDEGSAVGGPNSATGPNPASASASAVHAGVVVKQLASVVDKSSSNHKHKIKDNSVSSVGSEMVIEPKAEYDDDAHDENVEDLTLDEEDMTMEELDQTAGTSQGGEGSSQTYATWQHDRSQDELGLMAQDAQQRDPQDVSTNQTVVLPHYSIYHYYSNIYYLLSHTTIYEADRTVSVSCPGKLNCLPQRNDLQETKSVTVLYTIHFFLYILMIYIFVLCKILPRIVFVWVST", "text": "FUNCTION: Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRTPIIAGNWKMNKTVQEAKDFVNTLPTLPDSKEVESVICAPAIQLDALTTAVKEGKAQGLEIGAQNTYFEDNGAFTGETSPVALADLGVKYVVIGHSERRELFHETDEEINKKAHAIFKHGMTPIICVGETDEERESGKANDVVGEQVKKAVAGLSEDQLKSVVIAYEPIWAIGTGKSSTSEDANEMCAFVRQTIADLSSKEVSEATRIQYGGSVKPNNIKEYMAQTDIDGALVGGASLKVEDFVQLLEGAK", "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": "MNRQSVLRLARQTGAFPLAELPPPYLAPSLHFSMNRSTVQCSNFSSTAAVAAGRGDLNKVRGVSAIHRTGPKYKLGVSKYPLPKPVSPDALPKRNATPDHGLWGFFPTDRTALSTPTYDIECGRSWSIQELREKSWDDLHSLWWVCVKERNRIATSDMERKRLKAGYGEWESSERDRVIRVTQNGIKHVLRERWYAWEEAQRLYRKGYRPQEDSQEAIWEMRADSVSNSQGAGQLLVVSKAEDMIDPLRHDRWEKGQEENSGGETEDGNAPSN", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MSAVPNAVIPNPDNLSVSAPEKLSGFEWWRRSLQYRTGMGLDPQEKAQFEFDYQHKYLPQQCNSCIEFRDWMLTYSPSVTFMMDHIKKLSPNKEQILNKSNIICDVCDDLKGGGFHPQEGILLCANRIQSKWQLEDILTHELVHVYDHLKFQVNLNDLKHHACTEIRASMLSGECRIFNEIKKTGLGDFGKKFQSCIKRRAILSVSANPICKDSEEAEKVVNSVWQSCFNDTRPFERVYR", "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": "MPRKGPAPKHPVVVDPVYGSPLVTALVNKVLLSGKKSVAERIVYGALEGAKNKTGNDPVVTLKRALDNVKPTLEVRSRRVGGATYQVPVEVRAGRSTTLALRWIVGYSRGRREKTMTERLMNELIDASNGLGASVKRREDTHKMAESNKAFAHYRW", "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": "MEKYDLAIIGAGPIGLFAASFANLHGLKTISFDALDEIGGQINMLYPQKNIKDIPAFPSIKGKKLVSQLLEQNINTKFILSHKVKEISFLENENILVDKKYEVKSLLIATGLGAFKPKTLPLSTTLDVNQHIHYSMQHPEIFANKKVAILGGGDSALDWALELANTSDVFLIHRRNEFRGLESSVNKLKSLKNVELLTPYLPKDLQLNNNRMELVLHKVGASQDFVTKNVDEILVAYGFKSDNRQLRKWGIKLDHNLIAVSQKMHTNLPHVYAIGDAITYPGRVPMIALGFGEAQIAISNIMQDLFPEKTMTFHSTSI", "text": "SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family."}
{"protein": "MAAPGSEKSSKKKTEKKLAAREEAKLLAGFMGVMNSMRKQRTLCDVILMVQERRIPAHRVVLASASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPYMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELVEGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIRCPFEKRRDAACVFWDNVVYILGGSQLFPIKRMDCYNVVKDSWYSKLGPPTPRDSLAACAAEGKIYTSGGSEVGNSALYLFECYDTRTESWHTKPSMLTQRCSHGMVEANGLIYVCGGSLGNNVSRRVLNSCEVYDPATETWTELCPMIEARKNHGLVFVKDKIFAVGGQNGLGGLDNVEYYDIKMNEWKMVSPMPWKGVTVKCAAVGSIVYVLAGFQGVGRLGHILEYNTETDKWIANSKVRAFPVTSCLICVVDTCGANEETLET", "text": "FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MDTSGGNLDSLDDTEPLPELSFEDFLEPTSEKSSQHMEIEALDSEEDNIGGEDLADPANDSLNTPQFKKNVVHILEDKRLNSSGLTVLKSHAIKMVTAGGTPPAKAQVTDVKILNKLKPIPSSTLKIGSTTIATKSTPGSITKTLGNLTQIRTKDGQVIFVQKSVPGTQSSTAVTGSPSGGIRRLVAPSGIQKAVLSKGVTMASTGLVKAAVPAKASTSVPGSAITLKGIQPLAGGTAKASTSSTTATTSPSLAQPNKIQVVRTADGKIIKINQAGPSLLVNAKQGTGTTVTPGGSAATSVKLSPSTGNVVLNKPVGQVVVRTETPVKTATGSVASASATPGKMLVQSGGKQILVSNKNIIKLSPNASATSSTTHTTGGQTPSTSSGLHAIQLPGKGGIQYVRVLNNNKSAAGTSATASIPKTVQTQKITVVRPPAATGVPATSTTTSAAAASPAAASKANLAMGNTNKIVMRSMGGSIVPLPSVQTLVSKRALGAISNASKPASAASSSATPSASQELPRKHRLTDLNVQLKQSASVSSEASDSSDAGPEAKKPRYVITMQQGSQKAASQPVQKLINRTANVQRVVSSSTSPSSNSTKKIYNYVQPTGSNGAKYMICNSGVPQSSTSAMRRGYTGYVENKTRRPPPISPQQHRFKQMGPQQQSKHQQLQAQAKQRIRQQQLPTEQSTPIKVEPKLPTLPPGVKANVPAKPLFEVLKPPATAAAAGAVDPLGGMTSRRKHCNCSKSQCLKLYCDCFANGEFCQDCTCKDCFNNLDYEVERERAIRSCLDRNPSAFKPKITAPNSGDMRLHNKGCNCKRSGCLKNYCECYEAKIPCSSICKCVGCRNMEDRPDVDMDSLDGLMGVEGQKKDKAKNKQLNENRANIYFTDDVIEATIMCMISRIVMHEKQNVAVEDMEREVMEEMGESLTQIIAFAKEKQETSQIDESKPSS", "text": "FUNCTION: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the lin-54 family."}
{"protein": "MVSFTSIITAAVAATGALAAPATDVSLVARQNTPNGEGTHNGCFWSWWSDGGARATYTNGAGGSYSVSWGSGGNLVGGKGWNPGTARTITYSGTYNYNGNSYLAVYGWTRNPLVEYYVVENFGTYDPSSQSQNKGTVTSDGSSYKIAQSTRTNQPSIDGTRTFQQYWSVRQNKRSSGSVNMKTHFDAWASKGMNLGQHYYQIVATEGYFSTGNAQITVNCP", "text": "FUNCTION: Major xylan-degrading enzyme. Contributes to the hydrolysis of arabinoxylan, the major component of maize cell-walls. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MVLYFIGLGLYDEKDITLKGLETARRCDKVFAEFYTSLLAGTTLEKIEELIGKPIVRLSREDVELNFERIVLPEAKDKDVAFLTAGDPMVATTHSDLRIRAKKAGVKSYVIHAPSIYSAVAITGLQIYKFGKSATVAYPEKNWFPTSHYDVIRDNKERGLHTLLFLDIKADQNRYMTANEAMEILLKVEEMKGEGVFTPETLVVVLARAGSLEPTLRAGYVRELINEDFGRQPHVLIVPGRLHIVEAEYLVEFAGAPEKILEEV", "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": "MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHEAGHTVIMVTHDPGIAANANRVIEIRDGEIISDTSKNPEIPASNVGRIQEKASWSFYYDQFVEAFRMSVQAVLAHKMRSLLTMLGIIIGIASVVSVVALGNGSQKKILEDISSMGTNTISIFPGRGFGDRRSGKIKTLTIDDAKIIAKQSYVASATPMTSSGGTLTYRNTDLTASLYGVGEQYFDVRGLKLETGRLFDENDVKEDAQVVVIDQNVKDKLFADSDPLGKTILFRKRPLTVIGVMKKDENAFGNSDVLMLWSPYTTVMHQITGESHTNSITVKIKDNANTRVAEKGLAELLKARHGTEDFFMNNSDSIRQMVESTTGTMKLLISSIALISLVVGGIGVMNIMLVSVTERTKEIGIRMAIGARRGNILQQFLIEAVLICIIGGLVGVGLSAAVSLVFNHFVTDFPMDISAASVIGAVACSTGIGIAFGFMPANKAAKLNPIDALAQD", "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. Overexpression 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": "MTATPLYRQDTIAAIATPPGRGGVGIIRLSGPASRDLAERILGHCPAPRHAHYGPFYDADAQVLDEGIALFFPGPHSFTGEDVLELQGHGGPVIMDLLLARCVALGARLARPGEFSERAFLNDKLDLAQAEAIADLIDASSRAAAENALRSLQGEFSTRVSALVDKLIELRMFVEAAIDFPEEEIDFLADGKVAAMLQGAQETLGEVRAAAGQGALMREGMNVVIAGRPNAGKSSLLNALTERDSAIVTDIEGTTRDVLREYIHIDGMPLHVIDTAGLRDTPDAIEKIGVARAWEEIEKADRVLLLVDATTTTQTDPMQLWPEFVARLPHPERLTLVRNKIDESGETEQSDLSTSPPIVRLSAKTGLGVDNLKEHLKAVMGFDATTEGRFSARRRHLDALDRAGDALDNGIAQLRGHGAGELLAEDLRDAQQALSEITGEFTADDLLGEIFGSFCIGK", "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": "MAPVRAAAAKRWCFTLNNYTAEEEAKVRALLPGEFHFAICGKERGEQGTPHLQGFLHFKKKQRLSALKKLLARAHWEKARGSDHDNEEYCSKENDVILTIGEPVQGNRSDLAGAVAAVKAGRRMVDIAREFSEIYVKYGRGLRDLALMIGQKPRDFKTEVVVITGPSGVGKSRLASEMEGSKFYKMKGDWWDGYSNEDIVIMDDFYGWLPFCEMLRLMDRYPHKVPVKGSYVEFTSKKIVITSNTHPESWYCPDKCYLPALFRRINKWMYWDGLRFEDVPDAMKKHPINY", "text": "FUNCTION: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-3' in the intergenic region of the genome, 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. ATPase activity is probably carried by the isoform Rep (By similarity). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the nanoviruses/circoviruses replication- associated protein family."}
{"protein": "SIQHVYGAQHPPFDPLLHGTLLKSTAKMPTTPVKAKRVSTFQEFESNTSDAWDAGEDDDELLAMAAESLNSEVVMETANRVLRNHSQRQGRPTLQEGPGLQQKPRPEAEPPSPPSGDLRLVKSVSESHTSCPAESASDAAPLQRSQSLPHAAAVTLGGTSDPGTLSSSALSEREASRLDKFEQLLAGPNTDLEELRKLSWSGIPKPVRPMTWKLLSGYLPANVDRRPATLQRKQKEYFAFIEHYYDSRNDEVHQDTYRQIHIDIPRMSPEALILQPKVTEIFERILFIWAIRHPASGYVQGINDLVTPFFVVFICEYIEAEEVDTVDVSGVPAEVLRNIEADTYWCMSKLLDGIQDNYTFAQPGIQMKVKMLEELVSRIDEQVHRHLDQHEVRYLQFAFRWMNNLLMREVPLRCTIRLWDTYQSEPEGFSHFHLYVCAAFLVRWRKEILEEKDFQELLLFLQNLPTAHWDDEDISLLLAEAYRLKFAFADAPNHYKK", "text": "FUNCTION: May act as a GTPase-activating protein for Rab family protein(s)."}
{"protein": "MTISPPERGEKAKGAAPTPYDQPVDRDHAPIDYEKLNKPGFWSSKLSKGPKTTTWIWNLHADAHDFDTHLGDLEETSRKIFSAHFGHLAVVFIWMSAAFFHGARFSNYTGWLADPTNVKPGAQVVWPVVGQEILNADLGGNYQGLQITSGIFQMWRAWGITSEVQLMALAIGGVIMAALMLHGGIYHYHKAAPKLEWFRKIEPMLQHHQIALIGLGSIAWAGHLIHIGAPVAALLDAIDAGNPLVVDGVSIASAADVTNLAPRLCDPAVASQIFPSLAGRTVENFFTLNWWAFTDILTNKGGLNPVTGSLWMTDISHHHLAFGVFAIFGGHMWRNNVHGVGHSMKEIMDVHKGDPILFPAPKGHQGIFEFLSNSWHGQLSINLAMVGSASIVVAHHMYALPPYPYIAIDYPTVLGLFTHHMWIGGLFICGAAAHAGIAMIRDYDPAVHIDNVLDRILKARDAIISHLNWVCMWLGFHSFGLYIHNDVMRALGRPKDMFSDTGIQLQPFLAQWVQNLQQSAVGTGDLVGAGNLPGSVLSEVFNGNVVEVGGKVAIAPIPLGTADLMIHHVHAFTIHVTLLILLKGVLYARSSRLIPDKAQLGFRFPCDGPGRGGTCQVSSWDHVFLGLFWMYNSLSVVIFHFSWKMQSDVWGLTGGNFAQSSITINGWLRDFLWAQSSQVLTSYGQPISMYGLMFLGAHFVWAFSLMFLFSGRGYWQELFESIIWAHNKLKVAPTIQPRALSITQGRAVGVAHFLLGGIATTWAFFHARLIGLG", "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": "MPKQKAAKKDHYQYSDLSSIKKEGEEDQYHFYGVVIDASFPYKGEKRYVVTCKVADPSSVAKGGKLNTVNVVFFSQNFEDLPIIQRVGDIVRVHRARLQHYNDAKQLNVNMYYRSSWCLFIGNDKEAPLEPKVENEDGTNNYFSYTPYNFSGKSFTQEGHETKILKDLKKWSKDYFSNNDVVEQVKKADIETAMKNKTDFDLLAKVTEISDNDQYTNTVSLNDSTGQTWTGHLFKRKFPHLVKGDVLRIKSVSAKEDNSLIFSSHSNILKFFSFSSIHKKLKSSISSDTHIKTCVTKIDKAAHNKMDITPLKKLFFNPKKSEKLFRSQFSVLKVDTKNLEDYVGAFDGKKWHSYKGKKTPKDAELRWNIKLIVTDYKNQQDDKAYMIHLDDNSFFKGINPANWSNAATKKKAEKAFSVLTNNKVNYVDAILERDKKNYHIRHTQFK", "text": "FUNCTION: May function as protective capping of the single-stranded telomeric overhang. May also participate in telomere length regulation during DNA replication. Binds specifically to the T4G4-containing extension on the 3'strand and protects this region of the telomere from nuclease digestion and chemical modification. SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. SIMILARITY: Belongs to the telombin family."}
{"protein": "MAATIQSVKARQIFDSRGNPTVEVDVFCSDGTFARAAVPSGASTGVYEALELRDGGSYYLGKGVSKAVNNVNSVIGPALIGKDPTAQTEIDNFMVQQLDGTKNEWGWCKQKLGANAILAVSLAVCKAGASIKRIPLYQHIANLAGNKQLVLPVPAFNVINGGSHAGNKLAMQEFMILPTGAASFKEAMKMGVEVYHHLKSVIKKKYGQDATNVGDEGGFAPNIQENKEGLELLKTAIEKAGYTGKVVIGMDVAASEFYSDKDQTYDLNFKEENNDGSQKISGDSLKNVYKSFVSEYPIVSIEDPFDQDDWVHYAKMTEEIGEQVQIVGDDLLVTNPTRVAKAIKEKSCNALLLKVNQIGSVTESIEAVKMSKRAGWGVMTSHRSGETEDTFIADLAVGLSTGQIKTGAPCRSERLAKYNQLLRIEEELGAIAVYAGAKFRAPVEPY", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the enolase family."}
{"protein": "MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVKGPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSSSTENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFF", "text": "FUNCTION: Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate- early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. FUNCTION: [Isoform IFI16-beta]: Isoform that specifically inhibits the AIM2 inflammasome (PubMed:30104205). Binds double-stranded DNA (dsDNA) in the cytoplasm, impeding its detection by AIM2 (PubMed:30104205). Also prevents the interaction between AIM2 and PYCARD/ASC via its interaction with AIM2, thereby inhibiting assembly of the AIM2 inflammasome (PubMed:30104205). This isoform also weakly induce production of type I interferon-beta (IFNB1) via its interaction with STING1 (PubMed:30104205). SUBCELLULAR LOCATION: [Isoform IFI16-beta]: Cytoplasm. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Cellular distribution is dependent on the acetylation status of the multipartite nuclear localization signal (NLS); NLS acetylation promotes cytoplasmic localization. Localizes in the nucleus during human herpes simplex virus 1 (HHV-1) infection. SIMILARITY: Belongs to the HIN-200 family."}
{"protein": "MLYSLITQLIDQYSFLNVFKYLTFRTGLSMFTSMFVVLLIGTPFIKFFSARKILNPIRDDGPTEHIVKKIGTPTMGGVLILLGLFSGILLWGDLSNYHIWFLLFIVSGFGLLGAYDDYKKIKFKNSSGVSFKFKIISQILIAIVGIYGLTQLSQNTELTNLYFPFFKNLIINLGWFFIPFSIFIIVGSSNAVNLTDGLDGLATVPVILVAACFAFISYVTGNIVFSEYLNIPYLEGMGEVSVFCGSIIGACLGFLWFNAPPAKIFMGDTGSLALGGSLGAIGIITKHEIVLAITGGLFVLEAVSVIIQVFSFKLTGKRIFRMAPIHHHFEKKGWAESTVVIRFWIISIILAMIGLATLKLR", "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": "MTTRLFIQDVTLRDGMHAVRHRITPDDVGKIVAALDAAGVDGIEVAHGDGLAGGSLNYGPGSNTDWEWIEAAADNLTHARLTTLLLPGIGTIAELEHAYVLGVRSIRIATHCTEADVSAQHIGKARELGMDVSGFLMMSHMASPAELAAQAKLMESYGAHCVYVTDSGGRLTMDGVRERVRAYRDVLDEATEIGIHAHENLSLSVANSVVAVEEGVTRVDASLAGHGAGAGNCPIEPFIAVADLQGWKHNSDLFALQDAADDLVRPLQDRPVRVDRETLTLGYAGVYSSFLRHAEAASQRYGIDVRTILLEVGRRGLVGGQEDLIVDIALDLLAANSDSVAS", "text": "SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family."}
{"protein": "MKVRASVKKICDKCKIVRRKGIVRIICASNPRHKQRQG", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MKELARFSVTLPNELFDEINKRVKNTEYPSRSEFIRDLVREKIIADKWKDDSQSDAIAVLSIVYSHHQNNLVSQMLELEHHADVKIACSTHIHIDKENCLEMISLQGSGKNIEKFSQKIGSLKGVKFSNLARIGITKA", "text": "FUNCTION: Transcriptional regulator. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family."}
{"protein": "MAQTFSDEHFTLGIEEEYLLVDAETYDLAEAPDALMAACADKLSSKVSPEFLQCQIEVGTGVCASIADARADLRNLRATVAECAGRFGLAPIAVSCHPFADWKDQSHTDKDRYNQLARDLGGVVERMLICGAHCHVGLPSENDRVDIMRQMTYFLPHLLALSTSSPFWQGRDTGLASYRLTVFDNLPRTGLPPSFASFDEFQRTVDLLVDMEMIEDSSKIWWDLRPSAAFPTLETRICDVSPRLEDQLSLSALIQCLTRMLMRLRGSNQRWRVYDRFLINENRWRAQRYGVSDGLIDFGRGAVVPLPELVDELIELTEQDAEALGCVDEVQRLRDLAVETSSDRQRKIYKGTRAAGGSHQAAMRSVVEHLLEDFHVDL", "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": "MATILKQKLKTFFVPTAITLLLSACNSTSLFENSVTYLIKQEAYASSEFYINKAEQTLNSQDKITYQLLAVRKLIDENKVVEAQNTLNDLTTRLNIMEQNPLQQLEYQLVTAQLAALKGNNHQAEVTLQHISAANLSHSQLLRFYQTQAKIAENSKNTIEAVRIRSLIATQLVDNKLRQENNDKIWSLLRNANRGMLSSAQAGAGEMELAGWLALIEIYNQSVSTPAQMPQNINYWKRLYPNHSALAVMPTELQRVFNFQQTLLNNVALLLPLSGDAKILGEIIKKGFDDAKEQDPTIVQVFDTDSNSIENILMQAKQQGAQMIIGPLLKSRVNQMLASDQIRDINVLALNATQDVKPIVGVCYYGLSPEAEARSGADRLSRDGYTKAIVVAARDEFGQRSAEAFAQRWRQLTNTDADIRYYNQPLDVITTIQNSANNLQETALYALGNAEQLLEIKQGLENSTIAGQLAIYTASRSNSPNNGIEFRTAMEGVKFSEIPLLADHNSNEYQKAYSLADSDFSMMRLYAMGSDTWALANKFNEFRQIPGYSISGLTGNLNAGPNCNIERNMTWLQYHNGAVETTN", "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": "MAVFTTVSQDEIARWLLDFNLGEVRELRGIASGIENSNFFLTTEHDGQTRQYVLTIFERLTFAQLPYYLHLMAHLAERGIRVPAPIPARDGEILRPLKGKPATIVTRLPGASQLAPDAQHCAEVGDMLARMHLAGQDYPRQQPNLRSLPWWRQTEPEILPFLDAGQRALLQQEIAHQAAFFASTDYAGLGSGPCHCDLFRDNALFEEDGSGRHRLGGFFDFYFAGNDKWLFDVAVTVNDWCIDLASGELDPARTQALLRAYHAVRPLTATEAAHWQDMLRAGALRFWVSRLWDFYLPREADMLQPHDPTHFERILRRRIGADPASAPLPWI", "text": "SIMILARITY: Belongs to the pseudomonas-type ThrB family."}
{"protein": "MKFVLAIASLLVLSVVYAYPSEIRTFEEFKKAFNKHYVTPEAEQEARQNFLASLEHIEKAGKGRINQFSDMSLEEFKNQYLMSDQAYEALKKEFDLDAGAQACQIGAVNIPNEIDLRALGYVTKIKNQVACGSCWAFSGVATVESNYLSYDNVSLDLSEQELVDCASQHGCGGDTVLNGLRYIQKNGVVEEQSYPYKAREGRCQRPNAKRYGIKDLCQIYPPNGDKIRTYLATKQAALSVIIGIRDLDSFRHYDGRTILQSDNGGKRNFHAINIVGYGSKQGVRYWIIRNSWDTTWGDKGYGYFVADKNLMGIEKFPLAAML", "text": "FUNCTION: Probable thiol protease. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MPLEPEKHEEILNMLLDPELPQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTDKQEEDHKKADVSETITIEDLEGK", "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": "MIKFLSTFMLLLVTTVVQAERIRDLTSVQGVRQNSLIGYGLVVGLDGTGDQTTQTPFTTQTLNNMLSQLGITVPAGTNMQLKNVAAVMVTASLPPFARQGQTIDVVVSSMGNAKSLRGGTLLMTPLKGVDSQVYALAQGNILVGGAGASAGGSSVQVNQLNGGRITNGAIIERELPSQFGAGNTLNLQLNDEDFAMAQQIADTINRARGYGSATALDSRTIQVNVPSGNSSQVRFLADIQNMQVNVTPQDAKVVINSRTGSVVMNREVTLDSCAVAQGNLSVTVNRQANVSQPDTPFGGGQTVVTPQTQIDLRQSGGSLQSVRSSANLNNVVRALNALGATPMDLMSILQSMQSAGCLRAKLEII", "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": "MSILVTRPSPAGEELVSRLRTLGQVAWHFPLIEFSPGQQLPQLADQLAALGESDLLFALSQHAVAFAQSQLHQQDRKWPRLPDYFAIGRTTALALHTVSGQKILYPQDREISEVLLQLPELQNIAGKRALILRGNGGRELIGDTLTARGAEVTFCECYQRCAIHYDGAEEAMRWQAREVTMVVVTSGEMLQQLWSLIPQWYREHWLLHCRLLVVSERLAKLARELGWQDIKVADNADNDALLRALQ", "text": "FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. SIMILARITY: Belongs to the uroporphyrinogen-III synthase family."}
{"protein": "MWRNILGRASLRKVKFLSDSSSSGTHYPVNRVRGILSSVNLSGVRNGLSINPVNEMGGLSSFRHGQCYVFEGYATAAQAIDSTDPEDESSGSDEVNELITEMEKETERIRKKARLAAIPPKRVIAGMGAQKFYMLKQRQVKMETEEWERAARECREILADMCEQKLAPNLPYMKSLFLGWFEPVRNAIQDDLDTFKIKKGKIPYAPFMEQLPADKMAVITMHKMMGLLMTNAEGVGIVKLVNAATQIGEAVEQEVRINSFLQKKNKKNATDKTINTEAENVSEEIVAKETEKARKQVTVLMEKNKLRQVKALVRKHDSFKPWGQEAQVKVGARLIQLLMENAYIQPPAEQFDDGPPDIRPAFKQNFRTVTLENTKTSRRYGCIECDPLVLKGLDKSARHMVIPYLPMLIPPQNWTGYDQGAHFFLPSYVMRTHGAKQQRTVMKRTPKEQLEPVYEALDTLGNTKWKINKKVLSLVDRIWANGGRIGGLVDREDVPIPEEPEREDQEKFKNWRWESKKAIKQNNERHSQRCDIELKLEVARKMKDEEGFYYPHNVDFRGRAYPIHPYLNHLGSDLCRGILEFCEGKPLGKSGLRWLKIHIANLYAGGVDKLAYEDRIAFTESHLEDIFDSSDRPLEGKRWWLNAEDPFQCLAACINLSEALRSPFPEAAISHIPIHQDGSCNGLQHYAALGRDKLGADAVNLVTGEKPADVYTEIAARVLKIMQQDAEEDPETFPNATYAKLMLDQVDRKLVKQTVMTSVYGVTYSGARDQIKKRLKERGTFEDDSLTFHASCYAAKITLKALEEMFEAARAIKSWFGDCAKIIASENNAVCWTTPLGLPVVQPYRKPGRHLVKTTLQVLTLSRETDKVMARRQMTAFAPNFIHSLDGSHMMMTAVACNRAGLSFAGVHDSFWTHACDVDVMNTILREKFVELYEKPILENLLESFQKSFPDISFPPLPERGDFDLRKVLESTYFFN", "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": "MRLVILGGSGSGKSTQAQRLCSHLEITQISTGEILREAISHLSELGRHAQPYMIKGELVPDEMIIELIRLRLKKSDVIDGWVLEGYPRTAFQAEELDFLLDELGQKLDWAIYLQVPEAVMVSRSLGRSLPDDQPEIVQRRVEIFYDRTVPILEYYDRRRRLLTINGDQSPELVLQSILKLLLVT", "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": "MARATPIERYRNIGISAHIDAGKTTTTERILFYTGVNHKIGEVHDGAATMDWMEQEQERGITITSAATTCFWSGMGKQFQPHRVNIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFINKMDRTGANFLRAVEQIKTRLKGHAVPLQLPIGAEENFKGVIDLVKMKAINWNEADQGVTFEYEDIPAELLPEAQKWHQHLVESAAEASEDLMEKYLGGEEFTELELKAALRDLALRNEIVLVTCGSAFKNKGVQAMLDAVIEYLPSPTDVPAIAGQLEDGTPAERHPTDDEPFSALAFKIATDPFVGNLTFFRCYSGVVNSGDFVLNSVKDKRERVGRIVQMHANKREEIKEVRAGDIAAAIGLKDVTTGDTLCVESAPIILERMEFPEPVISVAVEPKTKADQEKMGLALGRLAQEDPSFRVWTDEESSQTIIAGMGELHLEIIVDRMRREFKVEANVGKPQVAYRETVRNEVKDIQGKHAKQSGGRGQYGHVVIDLFPLEEGAGYTFTNDIKGGVIPGEFIPGVDKGIREQLKSGPLAGYPVVDVGVRLHFGSYHDVDSSELAFKIAASMAFKSGFMQAKPVLLEPVMKVEVETPEDYMGDVIGDLNRRRGIIEGMEDGPSGKLVRALVPLAEMFGYATDLRSATQGRASYSMEFGKYAETPNNIAQAVIEARQSK", "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": "MSLLHQARFFITVNHLRDLPATAVPEVAFAGRSNAGKSTAINILCNQKRLAFSSKTPGRTQHINYFSVMPAKAEDPLGFLVDLPGYGYAEAPGETKSHWVHLLGDYVKARQQLAGLVIMMDARRPFTDLDCQMVEWFLPTGKPIHVLLTKADKLTNNDASRALMAARKVLADYRAQIDGDVSLTVQLFSSLKRRGIEEAQRIVAGWLCLPEALEAEPQAEPAKKTPSPNAQRG", "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": "MAQLLVIVKILPKGTEVDLDEMMEGLKGGLKGGIVLRRYAKEPLAFGLHFVKAEFILEDKEGQNDALEATVRSAKGVSEYEVLNMSRMSVDMK", "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": "AIANAPLLDTTITDRVFFD", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen."}
{"protein": "MSWRSESIWIEFITGSRKTSNFCWAFILFLGSLGFLLVGTSSYLGRNVISLFPSQQIIFFPQGIVMSFYGIAGLFISCYLWCTILWNVGSGYDLFDRKEGIVRIFRWGFPGKTRRIFLRFFMKDIQSIRIEVKEGVSARRVLYMEIRGQGAIPLIRTDENFTTREIEQKAAELAYFLRVPIEVF", "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": "MDSNTVSSFQVDCFLWHVRKRFADRELGDAPFLDRLRRDQKSLRGRGNTLGLDIETATRAGKQIVERILEEESDEALKMPAPRYLTDMTLEEMSRDWFMLMPKQKVAGSLCIKMDQAIMDKNIILKANFSVFFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTDEDVKNAIGVLIGGLEWNDNTVRVSETLQRFAWRSSDEDGRPPLPPNQKRKMARTIESEV", "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": "MSNKMWGGRFSERPDEIMEEINVSIDVDRHLYAQDIAASKAHAAMLATQGIITASDAKNIGKGLDTILSEIGKGGFTFKRALEDIHMNVESRLSELIGPAAGRLHTARSRNDQVATDFRLYVRDVIDETDAALAAFQQALVARALEHAGTVMPGFTHLQTAQPVTFGHHLLAYVEMAARDRGRFQDARKRLNESPLGAAALAGTSFPIDRHATAKALLFDRPMANSLDAVSDRDFVLETLSAASICAVHMSRFAEEIVIWTSPLVGLIRLSDKFTTGSSIMPQKRNPDAAELVRAKTGRVIGALNGLLIVMKGLPLAYQKDMQEDKQGAMEGFAALSLAIRAMTGMVRDLAPDEAKMKAAAGEGYATATDLADWLVRTLKMPFREAHHVTGRIVAKAAEGGVALHELPLKEMQAIEPRITKDVLGVLSVESSVKSRTSFGGTAPKNVASQAKSWAKRLEKERKLG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MFTIRPDEISSVIRDQIQKYNTELQVTNVGTVLQVGDGIARVYGLEKCMASELLEFEDGTIGIALNLEEDNVGAVLMGAGRTIEEGSTVRATGRIASIPVGPAFLGRVVNALAIPIDGKGDIVGSETRLLESPAPGIIKRKSVYEPLATGITAIDAMIPIGRGQRELIIGDRQTGKTTIAIDTILNQKGKGVVCVYVAIGQKASTVAQIVEVLRSRGALEYTIIVAANANEPAALQYLAPYTGCTLGEYVMYNGLTLPGSDKKINAALLVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSPDLGEGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLDSGLFNSGLRPAIDAGISVSRVGGAAQTKAMKKVAGKLRLDLAQFSELEAFSQFASDLDKATQAQLARGLRLREILKQPQYSPLSVAQQVAIIYAATNGYLDDIDVKGIQPFKQQFLNYLDSSVSEYGQEIETTKALTDKAVDLLKKALNDFKTTVKK", "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": "MVMTDPIADFLTRIRNANQVKHEVLEVPASNIKKGIAEILKREGFVKNVEVIEDDKQGIIRVFLKYGKNGERVITNLKRISKPGLRVYAKRDDMPKVLNGLGIAIISTSEGLLTDKEARQKNVGGEVVAYVW", "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": "MERRADAATGKRPIRSFVRREGRLTAGQQRALELLWPAFGLERPPAGQPLDLDRAFGRRAPRILEIGFGNGESLAEQAATHPERDYLGIEVHRPGVGHLLMEVEKRHLGNVRVMMADAAEVLAHHIPDGSLHGVQLFFPDPWPKKRHHKRRLVQPQWVRAVAAKLAPGGFLHLATDWADYAEHMLDVLEAEPDLENTCGPRQFSPRGERPETKFERRGLRKGHQVFDLYYRKREHPG", "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": "MAPKIFIDGEHGTTGLQIRTRMAGRRDVELLSIPEAERRNAAMREDMLNSADIAILCLPDDASKEAVQMVSANNNVRVIDTSTAFRVNPGWAYGFAEMDGAQADKIKAARFVANPGCYPTGAIGLIRPLRAAGILPDGYPVTVNAVSGYTGGGKQMIAQMENPDHPDAITAPHFLYGLPLTHKHVPEMTVHGLLDRAPIFSPSVGKFAQGMIVQVPLHLDDLAEGTTMESIHAALTAHYAGQDIVTVVPLADSKALARVNAVELEGKDTMKLFVFGTPGGSQVNLVALLDNLGKGASGAAVQNMDLMLAS", "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": "MFSKQDQIQGYDDALLSAMNAEEQRQEDHIELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEQLAIERAKQLFGADYANVQPHSGSQANAAVYLALLQAGDTVLGMSLAHGGHLTHGAKVSFSGKLYNAVQYGIDTTTGLIDYDEVERIAVECQPKMIIAGFSAYSKTLDFPRFREIADKVGAYLFVDMAHVAGLVAAGLYPNPLPYADVVTTTTHKTLRGPRGGLILAKANEELEKKFNSAVFPGGQGGPLMHVIAAKAVCFKEAMEPGFKAYQQQVIDNAQAMAQVFIDRGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAHITVNKNSVPNDPQSPFVTSGLRIGTPAVTTRGFKVTQCVELAGWICDILDNLGDADVEANVASQVAALCADFPVYR", "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": "MGRYSVKRYKTKRRTRDLDLIYNDLSTKESVQKLLNQPLDETKPGLGQHYCIHCAKYMETAIALKTHLKGKVHKRRVKELRGVPYTQEVSDAAAGYNLNKFLNRVQEITQSVGPEKESNEALLKEHLDSTLANVKTTEPTLPWAAADAEANTAAVTEAESTASAST", "text": "FUNCTION: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome (PubMed:23045392). Involved in positioning the proximal bud pole signal (PubMed:11452010). 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": "MSFVRVNRYGPRGGGRKTLKVKKKTSVKQEWDNTVTDLTVHRATPEDLIRRHEIHKSKNRALVHWELQEKALKRRWKKQKPEISNLEKRRLSIMKEILSDQYQLQDVLEKSDHLMATAKGLFVDFPRRRTGFPNVTMAPESSQSPTVVSKDPVTQAIRSESVIEPQALNEVDDDEQEGTVNSQSEESENELDNSLSSQSNANAGTFLHQIKEENSELINKLWTDIQQKVATQSQMTASSGTPSSASPSGEQKAALNATNAVKRIHTRLQPEESTETLDSSYVVGQVLNSRKQKQLLNKVKRKPDSRAPSKQKSSMLSASTASTDLPSSSNPSLDVLKHMIHEVEHEIEEYERWTGREVQGLQNSQGLTGFTLSLVSSLCRLVRYLKESELQLRKEVETRQRLEEALGDHRELIDALTAEVLFLREENTATQARLQQYMITTDEQLISLTHAIKNCPVISNKESQALERGATSQRHIDNPEDPAVNASVSMPLMFRGEDVVEFPQEDLPVKLSQVPNPPESGDLASSLPGHIFEPAVLLTPPRQKSNSEFSPLQDVLRRTVQTRPAPRIPPTVEIIEKEQNWEKKTLPVGADIQNSSDESHLFTQRWRASHMGEDSQSKTQAPFVSLSQPLCSSQSSMQQSRNPTLSEEPLVLGDGQQLRTNETLIQRKDIMARIAELTLQNSDIRAHLNNIIGPGGEQGDGLREFNRQETSHASDTMATFPAVQPLTPSSMEERIAELNRQSMEARGKLLQLIEQQKLLGLNPSSPPVSPVQSPLRAWAEGGKRTIEVSIPGAEAPESSKCSTDSPTSGLNSRRSSGAASNSCSPLNATSGSGRLTPLNPRAKIEKQNEEGWFALSTHVS", "text": "FUNCTION: Regulator required for centriole duplication. for proper bipolar spindle formation and chromosome congression in mitosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, spindle."}
{"protein": "MSASAQHSQAQQQQQQKSCNCDLLLWRNPVQTGKYFGGSLLALLILKKVNLITFFLKVAYTILFTTGSIEFVSKLFLGQGLITKYGPKECPNIAGFIKPHIDEALKQLPVFQAHIRKTVFAQVPKHTFKTAVALFLLHKFFSWFSIWTIVFVADIFTFTLPVIYHSYKHEIDATVAQGVEISKQKTQEFSQMACEKTKPYLDKVESKLGPISNLVKSKTAPVSSTAGPQTASTSKLAADVPLEPESKAYTSSAQVMPEVPQHEPSTTQEFNVDELSNELKKSTKNLQNELEKNNA", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
{"protein": "MSSGIILLLVAIVLLVIIAYVVGVVIRKRNDTLIANLETRKQELVDLPVQEEIEQVKLLHLIGQSQSTFREWNQKWTDLSTNSFKDIDFHLVEAENLNDSFNFVRAKHEIDNVDSQLTIIEEDIVSIREALEVLKEQEEKNSARVTHALDLYETLQKSISEKEDNYGTTMPEIEKQLKNIEAEFSHFVTLNSTGDPIEASEVLNKAEEHTIALGQITEQIPAIVAKLEDDFPDQLDDLETGYRRLLEENYHFPEKDIEQRFQEVREAIRSNSDGLVSLDLDRARDENEHIQEKIDKLYDIFEREIAAYKVAHKDSKIIPQFLAHAKSNNEQLGHEIKRLSAKYILNENESLSLRSFTNDLEEIETKVLPSVENFGQEASPYTHLQILFERTLKTLTTVEENQMEVFEAVKTIESVETRARQNMDKYVNKLHMIKRFMEKRNLPGIPQDFLSTFFTTSSQIEALINELSRGRIDIEAVSRLNDVTTNAIANLEQATYLVVQDATLTEQLLQYSNRYRSFEQNVQKSFEQALYLFEVEHNYKASFDEISYALETVEPGVTDRFVTSYEKTQERIRF", "text": "FUNCTION: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Note=Colocalized with FtsZ to the nascent septal site. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Colocalized with FtsZ to the nascent septal site. SIMILARITY: Belongs to the EzrA family."}
{"protein": "MSYRRLGLRSDHRRSVLRNSVTSLLKEEKISTTETRAKEIKRLTEKMITLGKRGDLHARRQAAAYIMSDEVVQKLFSDIAARYEERNGGYTRLVKTGYRKGDGAPMVMIELVE", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MIALIQRVTRADVRVGGRTTGEIGAGLLALVCAERGDTEAAADKLLAKLLGYRVFSDAAGKMNLPVSNIDGEGRAGGLLLVSQFTLAADTNSGLRPSFTPAAPPDEGARLFDYFVAAARARHPVVETGEFGADMQVSLVNDGPVTFWLQVRP", "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": "MIEFVYPHTQLVAGVDEVGRGPLVGAVVTAAVILDPARPIAGLNDSKKLSEKRRLALCEEIKEKALSWSLGRAEPHEIDELNILHATMLAMQRAVAGLHIAPEYVLIDGNRCPKLPMPSMAVVKGDSRVPEISAASILAKVTRDAEMAALDIVFPQYGFAQHKGYPTAFHLEKLAEHGATEHHRRSFGPVKRALGLAS", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MTEFESAPAYQEAKYLTSAAEFDQLPPDQGAEIAFIGRSNAGKSSALNIITGIKGLARTSKTPGRTQMINFFALNEHERLVDLPGYGYAKVPRMVQKRWEELVDSYLKKRRCLKGLVVVMDIRHPLKEMDEDVIEWAVNYDIPIHILLTKSDKLSQNAAKKTLGEVQTAISAYGEKLTLQLFSSHDRTGLDEVKAVLSQWFRSEP", "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": "MKPLRLIAVGQVRTPYFREACAHYLTAVRRYLPAEEILARDGKSADPARRKAEEAKAVLAALAPRDFVVVLDEHGPSLPSTELAALLKKRIEDPGRAPAFVIGGPFGLDKAVLDRADRLLALGPGTLPHELARVVLYEQLYRAASINAGAPYHH", "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": "SGSCTVKTCWMRLPTFRTVGNLLKERFDGASRVIYGNKGSNRASRADMRHLEPEDPAHKPHSPQDLVYFERSPNFCAANSKVGTAGTTGRACNNTSLGLDGCDLLCCGRGFRTLTERVTERCHCTF", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MEDDKLIVRIISKEGEIIRLTEEGERFLSSCLSSLKDAILSLHSIEIKGNIVSGLGEGKIFLSMEYYKSQINKIMGFDPFPGTLNIVIYDKASLENRLLLDSSPSLMVPEYKQKDRVLGAVKLYPAAINKLTPAAVVIPLRTTHPKSVIEIISPFHLREKLNLKDGDEVTIEVYV", "text": "FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). SIMILARITY: Belongs to the archaeal riboflavin kinase family."}
{"protein": "MAAAGRFGLLLLIVLWTMVTVVLPASGEGGWKQSRLGTEAAVMEEERCTVERRAHLTYSEFMQHYAFLKPVILQGLTDNSKFRALCSRENLLASFGDNVVRLSTANTYSYQKVDLPFQEYVEQLLHPQDPESLGNDTLYFFGDNNFTEWAPLFQHYRPPPFRLLGTTPAYSFGIAGAGSGVPFHWHGPGFSEVIYGRKRWFLYPPEKTPEFHPNKTTLAWLLEIYPSLAPSARPLECTIQAGEALYFPDRWWHATLNLDTSVFISTFLG", "text": "FUNCTION: Functions as a positive regulator of TNF-induced NF-kappaB signaling. Regulates angiogenesis and cellular metabolism through interaction with PKM. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Cytoplasm."}
{"protein": "MIDIGLSKMALIGAVALIVIGPEKLPRVARTVGTLLGKAQRYVADVKAEVNRSMELDELRKMKDTVENAARDVEQTIHTSASDFQKDMEHSLGDASATGSTYGVDQGLSTVVPAYKHPAKNWRLKRGAMPQWYKARAGVRTRVQSGAARVARFRPQKFH", "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": "MAKNRNEIPEKLTWDLTTIYKTDKEWEAELTRIKSELSLVEETDPGHLLDSAESLLTITEKMLSISQQVEKLYVYASMKNDQDTREAKYQEYQSKATALYVKFGEVYAFYEPEFLKISKEVYNKWLGELQKLKNYDHMFERLFAKKAHILSQKEEKLLAAAGEIFESPSETFEIFDNADIKLPMVKNESDEMIQLTHGNYSSLMESKNRGVRKAAYKALYSNYEQYQHTYAKTLQTNVKVHNLNAQIRSYDSARQAALANNFVPEKVYDVLMEAIHQHLPLLHRYIELRKKILGITDLKMYGIYTPLSNLGYKFNYEDGVKKAEEVLAIFGKEYKGKVKAAFEQRWIDVEENIGKRSGAYSGGSYDTNAFMLLNWQETLDDLFTLVHETGHSMHSAFTRENQPYVYGNYPIFLAEIASTTNENILTETLLKESKDDKERFALLNHWLDSFRGTVFRQSQFAEFEQKIHEADAAGEVLTSEYLNSLYGEINEKYYNLAVKGNPEIQYEWARIPHFYYNFYVFQYATGFAAATFLAEKVVHGSTEDRQKYLEYLKAGSSAYPLEVIAKAGVDMESTDYLDAAFELFENRLSELEKLVEKGVHL", "text": "FUNCTION: Hydrolyzes peptides containing between 7 and 17 amino acids with a rather wide specificity. SIMILARITY: Belongs to the peptidase M3B family."}
{"protein": "MQKLTRNHWIGLGDCFGGITTVYCGEKLKLLTIFLVCVLGCQLLRNIEVEMPRPLKQSLDQSRWLREAEKQLRVLENLVDSNLEEEKLKPQLSMGEDVQSPGKGEPLHPNVRAPLSHVVRAATIDLPRLGNKLPARHHLGKLSGLYQMKGCTFNPEWKVPDISDTHFNLDVVNECPSRNWKYLTPAKFWPKSISYFPVQVGVKPKYPDNVMQHESIVGKYLTRLYEAGILYKRISKHLVTFKGQPYNWEQQHLVNQHHIYDGATSSKINGRQTDRRRRNTVKPTCRKDDPKRDFDMVRQVSNTRSRVRPCANNGGDKHPPESGSLACWGGKESRIIKSDSSRDSSAPVDSRGRPKSTRSFSPLSRRKTTGNHHHSSVFPSSVEATTRGRSTPGKSVSPRDSSAIPVRTSGASDKNSPLEEENVWYLRGNTSWPNRITGKLFLVDKNSRNTEEARLVVDFSQFSKGKNAMRFPRYWSPNLSTLRRILPVGMPRISLDLSQAFYHLPLNPASSSRLAVSDGQRVYYFRKAPMGVGLSPFLLHLFTTALGSEISRRFNVWTFTYMDDFLLCHPNARHLNAISHAVCSFLQELGIRINFDKTTPSPVNEIRFLGYQIDENFMKIEESRWKELRTVIKKIKVGEWYDWKCIQRFVGHLNFVLPFTKGNIEMLKPMYAAITNQVNFSFSSSYRTLLYKLTMGVCKLRIKPKSSVPLPRVATDATPTHGAISHITGGSAVFAFSKVRDIHVQELLMSCLAKIMIKPRCLLSDSTFVCHKRYQTLPWHFAMLAKQLLKPIQLYFVPSKYNPADGPSRHKPPDWTAFPYTPLSKAIYIPHRLCGT", "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 (By similarity). SIMILARITY: Belongs to the hepadnaviridae P protein family."}
{"protein": "MTVPVLRTLSALRSATREWHLAGETIGVVPTMGALHDGHLSLVAAAKSACDRVIVTIFVNPKQFNKASDLASYPRTEEDDARKLARFDVDAVYAPDVSQIYPEGFCTNVSVAGMTDVLCGAHRPGHFDGVATVVTKLFTQTSADKAFFGEKDFQQLMVVQRMARDLDIPIEVVGCPTIREEDGLAMSSRNLLLSDRARTMAPRMHEIMQEAATALGQGAPFDALQATALRQLTAAGFTDVDYFELRSCASLSLLDHASVPARLFAAAWLAGVRLIDNIDVPVAR", "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": "MSNKKIIFFTGGGTGGHIFPGISIIQKLKELDNEIEFFWIGKKNSIEEKLIKEQNNIKFISIPCGKLRRYFSFQNFTDFFKVIFGIIKSFYILKKYKPQIVYATGGFVSTPTIIASSLLKIKRITHEMDLDPGLATKINSKFANKIYISFKESEKYFKNHKNIIHTGSPIRKEFLTPNPKIIKQLTQNTNKPIVSILGGSLGANALNNLALCIKKDAEIYFIHQSGKNLNDLREDNYIRRQFFNAEEMASIVKFSNIIISRAGAGAIKEFANACTCTILIPFKKGSRGDQIKNAKLLKTQNACIYIDEDEILNANILKIIKETLKDKEKINTLKANIKKFNNKNSSALIAQLLIKDIKETKSK", "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": "MWELRSASFWRAIFAEFFATLFYVFFGLGASLRWAPGPLHVLQVALAFGLALAXLVQTVGHISGAHVNPAVTFXFLVGSQMSLLRAFCYMAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVXQATTVEIFLTLQFVLCIFATYDERRNGRLGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFTNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGTRPSDNNGQPEGTGEPVELKTQAL", "text": "FUNCTION: Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, gap junction. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MSSNAPVGQLAYVLHSRAYRESSALVDFLTPQGRLRAVLRNARGKAGTLARPFVPLEVEFRGRGELKNVGRMESAGIAAWLNGEALFSGLYLNELLIRLLPAEDPHPAVFDHYAATLLALAEGRPLEPLLRAFEWRLLDDLGYGFALDSDIHGAPIAADGLYRLQVDAGLEQVFLLQPGLFNGTELLAMADADWSAPGALSAAKRLMRQALAVHLGGRPLVSRELFRKP", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family."}
{"protein": "DCVGESQQCADWAGPHCCDGYYCTCRYFPKCICVNNN", "text": "FUNCTION: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insects. Modifies presynaptic voltage- gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neurons. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 03 (aga-4) subfamily. Aga sub-subfamily."}
{"protein": "MNWITKFTVDFFCKLTKKQQIKNKTTTYEAKQENLATEVPVALVYNGISHTVMMCSPENLADFAMGFSLAEGIIDKPSDIYGIDVVPACQGIEVQIELATRCFVRLKAQRRTLAGRTGCGICGTEQLQQVHKNLPPLERTIQFDLNRLDACLIQLQQAQVLGQQTGSTHAAGFFDLAGNLLCLREDVGRHVALDKLLGWHAKQPAAKGFVLVTSRASYEMVQKTAACGIEMLIAISAATELAVNMAEQYQLTLVGFAREGRATIYTGKERLFF", "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": "MAAREEVLALQAEVAQREEELSSLKQRLAAALSTGQESARSVPVSPLPPRAALSREEIRRYSRQLVLPELGMQGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEASNLARQVLHGEALAGQAKVFSAAAALRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNAPTRYLVSDACVLAGRPLVSASALRFEGQLTVYHYGGGPCYRCVFPRPPPAETVTSCADGGVLGAVTGVLGCLQALEVLKTAAGLGPSYSGRLLLFDALRGDFRCIRLRRRRPDCAACGERPTVTDLQDYESFCGSSATDKCRSLRLLSPEERISIMDYKRLLDSRSPHLLLDVRPQVEVDICRLPHALHIPLKSLERRDAESLKVLGEAIREGKQGAQEGASVPIYVICKLGNDSQKAVKILQSWADLDSLTVKDVVGGLMAWAAKIDGTFPQY", "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": "MAEKIKVKLVKSTNGRLEKHRACVRGLGLRRIGHTVEVEDTPSVRGMINKVSYLVQVEGE", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MQAPSLTVTAPASPSPDERKQEYRDAMARLGAAVNIVTTDGPGGLAGFAATAVCSVTDSPPTLLVCLNRTSSAYPAVNANRVLCVNTLERGHEDLSRLFGGKTPVHERFEGASWSSLETGAPVLDDALISLDCRVKAISDGGTHDILICDVVAIRENDGGQALIYFDRRYHAI", "text": "FUNCTION: Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family. RutF subfamily."}
{"protein": "MPNYINYPSWLHPEVIQGIPITWYSLSYILIILISYKFIWYQIQSDNVDIKKEDYEIFMFSLVLGAILGGRLASTLVYDKSGIYYSNPWLILLPFDQHWNFTGFRGMAIHGGFLGAIIAPLITINTKLKNTNVQKYFLKLTDYGSIAFSSGYILGRLANFANAELYGRVMKGGIIFPNAEPFDTNIPGVKEFASSVGLEISPHDLLINLPRIPSQLIEGFFEGPVTFLLLWFLFKKIKKYDGFIFGVYVMLYAFFRFFIEYLREPDKELGFIITYKPITSLSEFSFLNISMGQILSLTLMLSGLIWIIVTKKIADKKIKNNTNLAYKN", "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": "MKALVKEKAEPGLWLMDVPEPEIGPGDVLIKVLRTGICGTDLHIRSWDGWAQQAVRTPLVLGHEFVGEVVETGRDVVDIKAGDRVSGEGHLVCGKCRNCQAGRRHLCRATVGLGVGRDGAFAEYVALPAANVWVHRVPVDLDVAAIFDPFGNAVHTALSFPLVGEDVLITGAGPIGLMAAAVARHAGARNVMITDVSEERLELARKIGVSLALNVADTTIADGQRALGLREGFDIGLEMSGRPEAMRDMIANMTHGGRIAMLGLPSQEFPVDWARIVTSMITIKGIYGREMFETWYAMSVLLEGGLDLAPVITGRYGYRDYEAAFADAASGRGGKVILDWTL", "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": "MTGLNTAGADRDLATAELNRELQDKGFLLTTTEDIINWARNGSLHWMTFGLACCAVEMMQTSMPRYDLERFGTAPRASPRQSDLMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRRASGAPARW", "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": "MESIAKAKSLPNKGRTYDSQRPWNRDSPFSFAAWWSTPSTRYLKVDQPSGRDEHDSLDLEDEDVSKYLASHRERQKRRASCAAKAKVLIIGCAVISLFAIIGALGFALGRRATLPGSCASPAHQNPHTPPHPRPTKGEAHDAGHSGSHSSSSSTNNHHHSHDDSPPPPHVGIDKPKQCGESPDEAQSRGCIFEPQLTAWVAPECAFPAVVAEYQDAVGDMMTEWPWFWDTGLQKAVSPEEFPSLQAGNYSVVYTPYQASHALHCLYCWRKVSYALEHGVDWMDARCHQFYHQRHCAFFIADKLLEMEDWRAAAEVDVQGRLTTWTYPLLYHNCVPLSSTMES", "text": "FUNCTION: 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). The role of phomB within the phomopsins biosynthesis pathway has still to be determined (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). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MLEDVIKETNDKLRSSYEVFLSDLKGIRSGSLSVSILDGVIVSTHMGKLRLNQVASLSVVNNKMLSVQVWDKSTVGAVKDAILTSNLGMNPIVEGSVLRLPVPDLTEERRKELVKVLKKYGDRAKVAVRNIRRDAISRIKVLEKAKEISENDMHALLKKIDKIISEEDARIDDAVSKKETDILKV", "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": "MGTPPVIAVVGPTGSGKSDLAVNLALELDGEVINADAMQFYRGMDIGTAKITPAERRGIPHHLLDILDVTQEASVSDFQDQARRLIGDIHSRGKRAILVGGSGLYVRAALDILEFPGTDPALRRRLEDDLAAHGTATLRARLQDVDPVSAERLSDDRRIIRALEVHELTGRPFSSFMPRREYFQPAVQVGLSVDRAALHERLAARVHAMVDSGLQAEVRRLDGLGLRTGKTACRALGYSQFLQVLDGSATVAEAAESTIVATRQFARRQLTWFRADPRITWIDWQDPDLVARAAGLCSQ", "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": "MAVSSEQHELSHFKRTQTKKEKFNCSEYGNRSCPENERSLGVRVAMYSFMAGSIFITIFGNLAMIISISYFKQLHTPTNFLILSMAITDFLLGFTIMPYSMIRSVENCWYFGLTFCKIYYSFDLMLSITSIFHLCSVAIDRFYAICYPLLYSTKITIPVIKRLLLLCWSVPGAFAFGVVFSEAYADGIEGYDILVACSSSCPVMFNKLWGTTLFMAGFFTPGSMMVGIYGKIFAVSRKHAHAINNLRENQNNQVKKDKKAAKTLGIVIGVFLLCWFPCFFTILLDPFLNFSTPVVLFDALTWFGYFNSTCNPLIYGFFYPWFRRALKYILLGKIFSSCFHNTILCMQKESE", "text": "FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MDALLQVSVDGFRFENGSGSCCKPRNNLESGNNLFPDFHESQNQSSPNDSPPTVCLDNSPVLKYINDMLMDEEDFVGISRDDLALQAAERSFYEIIQQQSPESDQNTSSSSDQNSGDQDFCFPSTTTDSSALVSSGESQRKYRHRNDEEDDLENNRRNKQPAIFVSEMEELAVKLEHVLLVCKTNQEEEEERTVITKQSTPNRAGRAKGSSNKSKTHKTNTVDLRSLLTQCAQAVASFDQRRATDKLKEIRAHSSSNGDGTQRLAFYFAEALEARITGNISPPVSNPFPSSTTSMVDILKAYKLFVHTCPIYVTDYFAANKSIYELAMKATKLHIVDFGVLYGFQWPCLLRALSKRPGGPPMLRVTGIELPQAGFRPSDRVEETGRRLKRFCDQFNVPFEFNFIAKKWETITLDELMINPGETTVVNCIHRLQYTPDETVSLDSPRDTVLKLFRDINPDLFVFAEINGMYNSPFFMTRFREALFHYSSLFDMFDTTIHAEDEYKNRSLLERELLVRDAMSVISCEGAERFARPETYKQWRVRILRAGFKPATISKQIMKEAKEIVRKRYHRDFVIDSDNNWMLQGWKGRVIYAFSCWKPAEKFTNNNLNI", "text": "FUNCTION: Probable transcription factor involved in plant development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MEARDIILRPVVTEASMAGMDNKRYTFDVDLRATKTQVKNAVEEIFGVKVVKVNIMNVKGKLKRQGRYEGYTKRRRKAIVTLSADSNEIKLFNDNNEN", "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": "METGRQTGVSAEMLAMPRGLKGSKKDGIPEDLDGNLEAPRDQEGELRSEDVMDLTEGDSEASASAPPAAKRRKTHTKGKKESKPTVDAEEAQRMTTLLSAMSEEQLSRYEVCRRSAFPRARVAGLMRAITGSSVSENAAIAMAGIAKLFVGEVVEEALDVCEMWGETPPLQPKHLREAVRRLKPKGLFPNSNCRRIMF", "text": "SIMILARITY: Belongs to the TAF11 family."}
{"protein": "MARIAGVNIPNHQHTEIGLTAIYGIGRTRSRDICVAAGVAFSKKVKDLTDADLEKLREEVGKFIVEGDLRRETTMNIKRLMDLGCYRGVRHRKGLPLRGQRTRTNARTRKGPRRAAQSLKK", "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": "MRLKVLWVGKTQEEWVRRGIDEYAGRIGRYMSIDLAEARDEKGAAVEAMREREGERLLKLLPKNARLVLLDERGEQMSSPELARFLATNRDGGTQELVFVIGGAYGFSDSLRAKAFKTISLSRMTFTHQMVRIFLLEQLYRGFTIINGEPYHH", "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": "MSACQTPVIVALDFPTREAALRLADQLDPKLCRVKVGKELFTSCAADIVETLRHRGFEVFLDLKFHDIPNTTAMAVKAAAEMGVWMVNVHCSGGLRMMAACREVLEQRTGPQPLLIGVTVLTSMEREDLAGIGLDIDPQVQVLRLAALAGKAGMDGLVCSALEAQALKAAHPSLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQAADPAKALAAVVAELA", "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": "MRVKIVSKPTSQLNNIIEKIKNISTKLGFEVVDKDFDYVIAVGGDGTLLRAVKQNKPVIAVKAGRRGLLMDVPVDKFEEALLRLKKGDYEEEEYMLLEMIYNDKVELGFNEVGILYDRPEAIKVGISFDTERVSVEGDGVLVSTPQGSSGWGMSATNSLLYKDLSAIEIIFVNPIFYYLRSVVIPPKPLTLRLEDKGYPQTARAVVDGEVVTLIKTNQEITVRVSQRKAKILRFFKLDLIGEVLHAYHI", "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": "MALVLHTFDGNKNAFKALIAAEYSGVKVELAKNFQMGVSNKTPEYLKMNPIGKVPILETPDGPVFESNAIARYVTRSKSDNPLYGSSLIEYAHIEQWIDFSATEVDANTGKWLFPRLGFAPYVAVSEEAAIAALKRSLGALNTHLASNTYLVGHSVTLADIVMTCNLYMGFARIMTKNFTSEFPHVERYFWTMVNQPNFKKVMGDVKQADSVPQVQKKAAAPKEQKPKEAKKEAPKEAPKPKAAEKPEEEEEAPKPKPKNPLDLLPPSKMILDEWKRLYSNTKTNFREVAIKGFWDMYDPEGYSLWFCDYKYNDENTVSFVTMNKVGGFLQRMDLCRKYAFGKMLVIGSEPPFKVKGLWLFRGPEIPKFVMDEVYDMELYEWTKVDISDEAQKERVSAMIEDLEPFEGEALLDAKCFK", "text": "FUNCTION: Probably plays a role in anchoring the complex to other cellular components."}
{"protein": "MVSMRDLLECGVHFGHQTRRWNPKMKKFIFGERKGIYVIDLQKTLRYFRYTYNIVRDAAAEGKTILFVGTKKQAGGAIKEYAEKCGMPYVNHRWLGGMMTNFGTIRQSIRKLEVIEKMEEDGSIKLLTKKEALMLTRKKEKLLAYLGGIRYMKTQPDMIFVIDTVKEKIAVQEANRLKIPVVAPLDTNCDPDLVDFPIPGNDDAIRSVQLFCQEMAEAINEGKALREQDGEANEEQPISEEEKKEVLEEAMSEEDFEGDKE", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MEQVSATARYLRIGPQKVRMLVDGIKGKSVEKGLNTLRFMPNKGAGLVEKALRSAVANAEEKNMDVDGLVILNVLVDQGPTLKRFRPRARGRATRILKRTSHITVVLAEKAAKN", "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": "MEPTQVAENLVPNQQPPVPDLEDPEDTRDESPENSDTVVLSLFPCTPDAVNPEADASASSLQGSFLKHSTTLTNRQRGNEVSALPATLDSLSIHQLAAQGELSQLKDHLRKGACPACTCLSGNNLINKPDERGFTPLIWASAFGEIETVRFLLDWGADPHILAKERESALSLASMGGYTDIVRLLLDRDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKVQQVMESHILRLFQSTLGPVDPE", "text": "FUNCTION: Activates transcription from class II MHC promoters. Activation requires the activity of the MHC class II transactivator/CIITA. May regulate other genes in the cell. RFX binds the X1 box of MHC-II promoters (By similarity). May also potentiate the activation of RAF1 (PubMed:10329666). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MLRKKFENTKIILASGSPRRQEFFKNLDLDFEVRLKEIEEIFPKTLQSLEITDYLAKLKASAFDGDLLQNELLVTSDTLVWLQNEALGKPKDYDDAFAMLQKLSNQTHEVITSVCFKTKNKTEIINDITQVTFGKLSDEAIKYYLDNYKPFDKAGSYGIQEWIGLIGITNIHGSYTNVVGLPTEKVYLYLLNHTF", "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": "MTKKDKGPKFANVTTKSGEVVKVFEDLNDFETFIKNETEDEEFDHVHCHLKYYPPFVLHESHEDPEKIKDSANSHSKKFVRHLHQHIEKHLLKDIKERIKLPDLKFKDKAKEESFEHIVWKYNDVTQYHGKDFEIHITVECHNDSAIVDVDYLTKPLTAAVEA", "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": "MAKADKATAVADIAEQFKASTATVVTEYRGLTVANLAELRRALGDSATYTVAKNTLVKRAASEAGIEGLDELFAGPTAIAFVKGEAVDAAKAIKKFAKDNKALVIKGGYMDGKALSVADVEKIADLESREVLLAKLAGAMKGNLSKAAGLFNAPASQVARLAAALQEKKAGEEAA", "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": "MYRSGERLLGSHALPAEQRDFLPLETTNNNNNHHQPGAWARRAGSSASSPPSASSSPHPSAAVPAADPADSASGSSNKRKRDNKASGGRAAGGGRADGGGVVYSGTPWKRRNYNQGVVGLHEEISDFYEYMSPRPEEEKMRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVFGKWENLPLWTLEEALRKHKVADEDSVKVLDKATVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDFTKKYPVLPYLVLVLKQFLLQRDLNEVFTGGIGSYSLFLMAVSFLQLHPREDACIPNTNYGVLLIEFFELYGRHFNYLKTGIRIKDGGSYVAKDEVQKNMLDGYRPSMLYIEDPLQPGNDVGRSSYGAMQVKQAFDYAYVVLSHAVSPIAKYYPNNETESILGRIIRVTDEVATYRDWISKQWGLKNRPEPSCNGPVSSSSATQSSSSDVDSDATPCKTPKQLLCRPSTGNRVGSQDVSLESSQAVGKMQSTQTTNTSNSTNKSQHGSARLFRSSSKGFQGTTQTSHGSLMTNKQHQGKSNNQYYHGKKRKHKRDAPLSDLCR", "text": "FUNCTION: Terminal nucleotidyltransferase that catalyzes preferentially the transfert of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (PubMed:21788334, PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro) (PubMed:21788334, PubMed:21855801). Required for cytoplasmic polyadenylation of mRNAs involved in carbohydrate metabolism, including the glucose transporter SLC2A1/GLUT1 (PubMed:28383716). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion (PubMed:18172165). Mediates 3' adenylation of the microRNA MIR21 followed by its 3'-to-5' trimming by the exoribonuclease PARN leading to degradation (PubMed:25049417). Mediates 3' adenylation of H/ACA box snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation (PubMed:22442037). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Cytoplasm Note=Predominantly expressed in the cytoplasm (PubMed:18172165). SIMILARITY: Belongs to the DNA polymerase type-B-like family."}
{"protein": "MNQTTKLCAATTLALGTLIGATVVGTASPIHQEAQAATTPYYTYHGYIGHNANFIMDKHFINAIKYDNVTFNGIKLAKTNATKKVEKYDQTFKGVTAKGNEANQLQFIVKNNISLKDIQKAYGKDLKKENNKTKESDSGIFYYQHSKKSLGIWFVVDHNRVVEVTVGHTPYKTSK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IsaB family."}
{"protein": "MYAIVEIAGKQFKVTKDLYIYTPKMDQEAGSSVSFDKILLLQNDQDIQVGDPTVAGAKIEGKVIEHVKGDKIIVFKRKRRKGYKTKQGHRQGYTKVLIQNILR", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MLNKSLLIRFVLTILIIVQVIIFDTQPVQAAVDSYVKRYLDAEIPVGIKLNKQGELKNFSAEDLSEGKQTFAKNCLNCHVGGANLVNPSVSLSLEKLKGATPPRDDLNNLVAFLRDPMIYDGSSYTLFCRQITENWMSQQEVENIAAFILRAAQKAPYWGVENVR", "text": "FUNCTION: Possible low-potential cytochrome c. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily."}
{"protein": "MAHSFLDEQREETRLIIDELLEDGSDPEALYTIEHHLSADDFDTLEKVAVEAFKLGYEVTDAEELEVEGGEKLMCCDAVSEIALQAELIDAQVEQLFTLTQRLEVNYDGWGTYFEDPDGEEEEGDEFDQDDEDGPADRDEVPATRH", "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": "MVSWKDIYLVLEATVPLYVAMILAYLSIKWWKLFTPEQCSGINKFVAKFSIPLLSFQVISTTDPYDMNIKLIYSDILQKSLALLGFAAISKACCAEKFDWLITGFSLSTLPNTLIVGIPLLKGMYGEQAGKLLSQIVVLQSLIWYTLLLFLFELRAANGMATTTSSETTGLIWALVGFRWHIRLPLIVSNSIRMLSDGGLGMAMFSLGLFTALQTKIIACGAKRMLLALAIRFFLGPALMGMSSYAIGMRGVLLKIAIVQAALPQGIVPFVFAKEYNVQADILSTAIIVGMMVAVPVALAYYFAMIIPAIK", "text": "FUNCTION: May act as a component of the auxin efflux carrier. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family."}
{"protein": "MKSGKFQTKGFKFKQFCIEGGESGMPVSTDGVMLGAWMESPSPAHILDIGTGTGLLALMCAQRFPDAKITAVDIETTAVEAASHNFSHSPWHDRLSVQHTDVLIFSPPQRFQRIVCNPPYFNTGEQAKQSQRATARHTDSLRHDALLKCCYQLLDAEGKASFVLPITEGELFIELALTQGWSLSRLCRVQPSEKKPVHRLLFELAKQPCDTQESHLIIHSSDGYSDDFVRLTHEFYLKM", "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": "MKKIGVESGLSAIADYLKNEGYSVELLGGNLENNAAKCDSFDAVVTADYNTNMMGFCNTSTKTPIVNASGLTREEVKNMIEQKTSR", "text": "SIMILARITY: Belongs to the UPF0180 family."}
{"protein": "MAAFQTAAQLARAVQSGETTPQQLLHGALARAEAVRGLNALVSLNSHAEEQAAAVQGRMQAGETLPLAGVPIVVKDNINVTGTRTTCGSRMLANYVSPYTATAAQKLQGAGAVIVGKANMDEFAMGSSTESSASGPTLNPWDHERVPGGSSGGSAVAVAAGISPVSLGSDTGGSVRQPAALCGVYGFKPTYGRVSRYGLVAYASSLDQIGPFARSAEDLALLMNVIAGHDPRDATSLDAPARFAVGGADSLRGLRVGVIRESLGGNTPGVEAALGATLDALRGAGAVVGEVSIPELEYAIAAYYLIAMPEASSNLARYDGMVYGERVPGGDVTRSMTLTREQGFGQEVQRRILLGTYALSSGYYDAYYAKAMKVRRLIADEFTTAFGQYDVLVTPTSPFPAFRRGEKASDPLAMYAADVDTVAVNLAGLPALSVPAGFEEVDGKRLPVGVQFIAPALQDERLLALAGALEAVGAVQLEMPQD", "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": "MIKPTFLRRVAIAALLSGSCFSAAAAPPAPPVSYGVEEDVFHPVRAKQGMVASVDATATQVGVDILKEGGNAVDAAVAVGYALAVTHPQAGNLGGGGFMLIRSKNGNTTAIDFREMAPAKATRDMFLDDQGNPDSKKSLTSHLASGTPGTVAGFSLALDKYGTMPLNKVVQPAFKLARDGFIVNDALADDLKTYGSEVLPNHENSKAIFWKEGEPLKKGDTLVQANLAKSLEMIAENGPDEFYKGTIAEQIAQEMQKNGGLITKEDLAAYKAVERTPISGDYRGYQVYSMPPPSSGGIHIVQILNILENFDMKKYGFGSADAMQIMAEAEKYAYADRSEYLGDPDFVKVPWQALTNKAYAKSIADQIDINKAKPSSEIRPGKLAPYESNQTTHYSVVDKDGNAVAVTYTLNTTFGTGIVAGESGILLNNQMDDFSAKPGVPNVYGLVGGDANAVGPNKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIITTVLQMVVNSIDYGLNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAKGQKVALKEAMGSTQSIMVGPDGELYGASDPRSVDDLTAGY", "text": "FUNCTION: Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acceptors (PubMed:2877974). The KM values for gamma- glutamyl acceptors are so high that it has been proposed transpeptidation is not the physiological role in E.coli (PubMed:2877974, PubMed:8104180). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the gamma-glutamyltransferase family."}
{"protein": "MHPRFQTAFAQLADNLQSALAPILADHHFPAMLAAEQVSTLKNATGLDEDALAFALLPLAAACARTDLSHFNVGAIARGVSGNWYFGANMEFLGATMQQTVHAEQSAISHAWLCGEKGLAAVTVNYTPCGHCRQFMNELNSGLDLRIHLPGRAPHTLRDYLPDAFGPKDLEIKTLLMDEQDHGFALTGDTLTQAAITAANKSHMPYSQSPSGVALECKDGRIFTGSYAENAAFNPTLPPLQGALNLLSLNGYDYPDIQRAILAEKGDAALIQWDATAATLKALGCHNIDRVLLG", "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": "MRSQDLHQRLADLGAKPLHCGRIVRAWLQGRALDACTARQRAEDFLPLGVRHGLPQVAAELEGIARLHSEHPASDGSSRLLVELADRQMVESVLLPRGGLCVSTQVGCAVGCVFCMTGRSGLLRQVGSLEMVAQVVLARRRRAVKKVVFMGMGEPAHNLDNVLEAIDLLGTDGGIGHKNLVFSTVGDPRVFERLPRQRVKPALALSLHSTRAELRRQLLPKAPPLSPEELVEAGEAYARRVDYPIQYQWTLLEGINDSLEEMDGILRLLKGRFAVMNLIPYNSMDGDAYRRPSGERIVELVRYLHSRGVLTKVRNSAGQDIDGGCGQLRARATQGTAERRIPARQA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
{"protein": "MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQDPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEIVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDITTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGAARMEGNLPAKLRKMNSDRFT", "text": "FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ3 subfamily."}
{"protein": "MGEVAATVEPLAAVKSKSMRSRKRRQRRRRQIAYLAICGLSVAIFGFALATLIRPTTAQADADPGSWRKGYVGHGTTHEQLGQPHWPPVQYTVYRPTTNYTKAPPPPTSAMNPIFNFTHFLYDKVLYRDEPIPEGYIVVKNSDTLSLGPKVEENDWRDLLAHYWMVLIWVVILVVLIIVIPFIAVCYCCFCCCRRCRQGCPPCTSKQDAQRRFCCGICLLILIIGLIFGIIIAFVTNKMIDSGFAETSETMKRGSEDTCTYLKDVADHVHHLMMYNYEEMETHVLDQLTHAHRHIFLDLSDTSESNSLAEMERVLENMPEALELMRQVEKMEKDLRFYGSQLRDGVRGIKRDVNFAVANLCQLQMCQKFLISSNIEHIDSSQCLHFDNLPNTKEFVEGMENIVASEYYAIPQRGLSRLKKVSDKVKTQLSFVVPPMMRDLTKGRTIFREHATNVRNIVEGVLSDIHIKTLHSTKSFEDVYERFGHDRNVVSLIVCLLILLVLFILIFALLCGCFGRRRTGYGDECCSKSTGATCLLLAILLIFCVFSFIALVGLFYFMLGMVTYQGACAPLRDQENNTLFRQLDASIDLNHYLPPSESNKEVVQPLKMSSAIKACHANQTIFDMMRQHNIYDINDLTRIKVMSHSQENTDSIKVFDEDLSTVVLLTKEERDELKTAGESKLAKYHSSLYMPSLCTQFTPMNLNALSEQLYKLSNDLEYPAYGWAKVSFWNEGLNTKAFYRNFVPKLTSLVEKMKANLKKIDELISYENHDFTNTIKILTATAINSEQFIQTRGKDYINALGGNLTNSIDQMIDDYIDMIIKEANESVGHCAPLSYIYYRGVDLICHRIVDPINGFWVGILLCALLFLPILFVAHRLMCLYKKIYPYLATVGAAGVVEGGSDYLYDAYSERDREHVPLANVPKKRRKAYERRREQQDYFEDASPSVSRGNRSGGDRGGGGGDGAPGSSSMRYNDMAPTHWDHEPPRYHNPPAAPPSSEYERPPPYYYPGASEQD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the prominin family."}
{"protein": "MLCRAACSTGRRLGPVAGAAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNATEEKYHEALAKGDVTTQVALQPALKFNGGGHINHTIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYTACKK", "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": "MSAKKSYLKVWRGLAGAAGSCARVFSKKSLARRDRRDQLPFALFLFGLVGAVFQWFLYGNWLSGIVSEYTVAAFFGGFSIVLPILLIGFSIWLFRNPQKTHDNIRVSIGLFMFSSFSAAFLHFSAGFPYPSSGIRILSTAGGIIGWLVGLPLTTLPSYLAKTVCIIFIVLSVSVISKTPISKIVRVIFRYAKWLFNSDSVKTSPNSSVSSSSEHQELTGRDMPDTAGDNRHDETVTVLSGTSLTGSPVSEYRGESSDYALPSLDILNSYPPVKHDDAENEKVITALSGVLRQFSVNARFSGFSRGPTVTQYELELGEGVKVERIIALTKNISYAVASDKVSILSPIPGKSAIGIEIPNKKRELVALGSVLQSIHPDAHPMTVGLGKDSSGGFVLTNLTTMPHLLVAGATGSGKSSFVNSMITSILLRAHPSQVRLVLIDPKRVELAIYSGVPHLITPIVTDPKKASEVLQWVVKEMERRYDDLASFGFRHIDDFNLAVRAKKIASDSRELTPYPYLLVIVDELADLMLVAAKDVEESIVRITQLARASGIHIVLATQRPSVNVVTGLIKANVPSRLAFAVSSLVDSRVILDRPGAEKLVGQGDGLFLPISAGKPIRIQSSWVTENEILRVVEYVKSQAHPDYYVLEVQNQGNIDSHIGDDMPLLLKATELVINSQLGSTSMLQRKLRVGFAKAGRLMDLMESMGIVGPGQGSKAREVLVTPQDLDSTLARISASVSDSKLD", "text": "FUNCTION: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located at the septum. SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family."}
{"protein": "MPSEGRCWETLQALRSSDKGRLCYYRDWLLRGEDVLEECMCLPKLSSYSGWVVEHVLPHMQENQPLSETSPSSTSASALDQPSFVPKSPDTSSAFSPASPATPNGTKGKDESQHTESMVLQSSRGIKVEGCIRMYELVHRMKGTEGLRQWQEEQERKVRALSEMASEQLKRFDEWKELKQHKEFQDLREVMEKSSREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQERLRKEEGQVRLRALYALREEMLQLSQQLDASEQHKGLLKVDLAAFQTRGNQLCSLISGIIRASSESGYPTTESQAEAERALQEMRDLLMNLGQEITRACEDKRRQDEEEAQVKLQEAQMQQRPEAHKEPPAPSQGPGGKQNEDLQVKVQDITMQWYQQLQDASMQCVLTFEGLTNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKLAEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGDLILAHLHKKCPYSVPFYPTFKEGMALEDYQRMLGYQVKDSKVEQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQEIHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMLILIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHKDIPVPKGFLTSSFWRS", "text": "FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, nuclear pore complex Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. SIMILARITY: Belongs to the GLE1 family."}
{"protein": "MIDLLGLDLDGTLLSRTRQINDPTKQALANLIQKKPSLKVMILTGRSLFSTLKYVQELNELCKKPLVEYFCCYGGAKLYQLNNNQPQEQYKFLIDSRQVKTVFEIVEQHKGLFLAYLDKPKAPYIILGANQFYAWLIKQFWYKQRCEYFKNDHLTDGILKINVYFACPLRLKKVYQIIKRQFQDTLNVVNFSKHLIEITHKDGNKGYAIEAIAKKQGLSLKRMAVIGDSLNDRSMFEKVQYSFAMSKSPDELKLLATEIGTKTNRFRFSSLVDLITEKIIN", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family."}
{"protein": "MPPHARSGRGPKPQKNGRTEQRQQKRKRDQEDLQQLQQRVDELDLKSDATKKFSELPLSVPTAEGLEIAHFQTLTDVQARAVPLALKGKDILGAAKTGSGKTLAFLIPVLEKLYRAQWTEFDGLGALIISPTRELAAQIFEVLRKVGTKHSFSAGLVIGGKSLKEEAERLDRMNILVCTPGRMLQHFDQTAGFDANNLQILVLDEADRIMDMGFQSAVDALIEHLPRERQTLMFSATQSKKVSDLARLSLKDPEYVSVHEAAVSATPTNLQQHYIVTPLTEKLDTLYGFIKANLKSKIIVFLSSGKQVRFVYESFRHLQPGIPLLHLHGRQKQGARMEITSRFTAAKQTCLFATDVVARGIDFPAVDWVIQADCPEDVDTYIHRVGRTARYESNGRAVLFLDPSEEPGMLKKLELKKIPIQKVNVKEKKKKSIKDQLQSMCFQNPDLKYLGQKAFISYSRSIHLQRDKDVFKFNKLDLDGFAASLGLPGTPQVKFRKGEDIKKIKNAPRQGMSSGSESDEDGEKKTKKKEVRTKYDKMFERTNQDVLSSHYNKLVLDGDDNDDDEEDFLSVKRVLRDDDLDDEAGAYKSTAKIIDGLGGEEPFVVDSKRREKALKSKKKMLKFKGNSTKMVFDDDGNAHAVYELRDEDDFMGEGPAEEQRRKFVEDETSRVREADVDDKALAKQKRREKREKRKAAERAELMGIVSDGEDAPVLHNADDGEDPLALLRSLPMGDGSDSEGDREPPKKRAKKWFEDDSDEENKSKSKSKGKVIRVQEEPETLEDLEALATGLLD", "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": "MQRFVCSGVFRQTSVLLQISPVSHCHTRRMQDSPSHRSLKQLISSQRWLNSTTALCSPTSQKTSASGQEEPDPLHDKSSGLIQRFKKTFKQYGKVMIPVHLLTSTMWFGTFYYAAMKGVNLVPFLEYVGFPDKVVKLLENSQSGYALTAYAMYKIATPARYTVTLGGTSLSVKYLRKHGYMSTPPPVKEYLQEKMEETKERISGKMEETKDRFSERMEETKDKFNEKLQETKDKVSFRKKKE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MYDWLNALPKAELHLHLEGSLEPELLFALAERNRIALPWDDVETLRKAYAFNNLQEFLDLYYRGADVLRTEQDFYDLTWAYLLRCKAQNVVHTEPFFDPQTHTDRGIPFEVVLAGITGALKDGKSKLGVDSGLILSFLRHLSQEEAEKTLDQALPFRDAFVAVGLDSSEMGHPPSKFQRVFDRARNEGFLTVAHAGEEGPPEYIWEALDLLKIQRIDHGVRAIEDERLMQRIIDEQIPLTVCPLSNTKLCVFDDMAQHNILDMLERGVKVTVNSDDPAYFGGYVTENFHALYTHLGMTEDQAKRLAQNSLDARLVKP", "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": "MKKQNLIHAEGLVTESLPNGMFRVLTDNGCQILTHISGRIRRNSVRILPGDRVKVELSAYDLTKGRIIYRLSNKSSND", "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": "MGIDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSSFNRVVLKRLFMSRTNRPPLSMSRLIRKMKLPRRENKTAVVVGCITADVRIHDIPKLTVCALKLTSGARSRILKAGGQIMTFDQLALAAPKGQNTVLLSGPRKAREVYRHFGKAPSTPHSRTKPYVLSKGRKFERARGRRASRGYKN", "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 eL18 family."}
{"protein": "MATTILKNEGLDFHIKISTPLSEIDNDIQKELVDLTKKVKIAGFRAGKVPIAIVEKKYGASVRNDIIEKRINDSVNHVIKEHNLNIIGRPKIDDLQNEPNKPLEFTIKMELLPKIDIPDLKKISINRPKLEVSPDDVEEQLKKLAEMMKSYTKESKAKAKDGDQITMDAVGYVKDEAFEGGKLTDFKVVIGSNALIPGFEKQLIGSKAGSEVEVNVTFPENYHAKDLAGKDARFVVQVKAVHTAEPTVIDDEFAKKFQSNSLEELRTHFTKKIENESEEAISTIMKMNLFDQLEKLLDFDVPESLLDQEKNILKSETDKSEQDDSVFKDKSPEQVKEYYDKLALRRVRIGLMLAEYAKDKNLQVEPDDLRRIIMQQARSFPGQENMLFDFYKNNPRAVEQLKGPALEEKAVQHIFDNAVNLKEKKYNRKELEKLLESEEQRITAM", "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": "MIDYSQFPRKNILCVDMKSFYASVSAVTMGLNPLTCYLAVVGNTDRQGSVVLAASPALKKDFGIKTGSRLFEIPEDPRIHIVNPQMKLFIRVSTEITKLFYRFVPEKCVHTYSIDESFLDAGKEDPEEMAKAIQSSMWREFGLMCTVGIGDNMLLSKLALDLESKKTKSGIARWRYEDVPNKLWKVRPLSKMWGIGGRMERNLNRMGISTIGQLAKFPLELLEKKFGIMGNQLYYHAHGIDLSEIGAPLMQGQISFGKSQILLRDYTRSEEIKAVLLEICEEVARRARTHNKVGRTISLGIGYSKDELGGGFHRSKTIDLPTSITMDIYRCCLMLFNKFYSGKTVRSVSVTLSNIEDDVNQQLSLFEVDNEKRRKLGFVMDGIRSKYGSKAILRAVSYTPAGTALQRAGLTGGHKS", "text": "SIMILARITY: Belongs to the DNA polymerase type-Y family."}
{"protein": "MKVKICGITDMETAKRACEYGADALGFVFAESKRKITPGLAKEIIQELPANVLKIGVFVNESVEVIQKITENCGLTHVQLHGGEDNHQIRRLNIPSIKSLGVTSESDMKNAQGYETDYILFDSPKEKFHGGNGKTFSWELLAHMPKELREKAILAGGLNTLNIEEAIRTVRPYMVDVSSGVETEGKKDVEKIKQFIIKAKECSK", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MAIERTFSMIKPDATKRNLTGAITKMLEDAGLKVVASKRVWMSRRQAEGFYAVHKDRPFFDELCEFMSSGPTVIQVLEGENAIAKNREVMGATNPANAAEGTIRKVFALSIGENSVHGSDAPETAEQEIRYWFSETEIVG", "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": "MMPPVRGTLTQGRILADLTWLRVGGPADWLFQPADEADLVQFLGALDPAVPVFPMGVGSNLIVRDGGLRAVVIRLGRGFNAIRIEGDRVIAGAAALDAHVARRAAEAGRDLTFLRTIPGSIGGAVRMNAGCYGSYVADHLIEVRAVTREGRAVTLPAAELGLAYRQSALPEGCVLTEATFRAEAGDPAELARRMDEQIARRDSSQPTKERSAGSTFRNPAGFSSTGRADDTHELKAWKLIDEAGLRGARRGGAQMSEMHSNFLINAGGATAADLEGLGEEVIKRVFQSSGIRLEWEIMRVGELPVNKE", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
{"protein": "MKKVPGPIVLVEPLSGNTSLLIKVNEVLAVRRSRYQEIMVVETEDYGRALILDDYIQSSYYDEAFYHESLVHPAMVTHPAPRDVLILGGGEGATLREVLKHPTVEKAVMVDIDGDVVELSKRFLPQMHQGAFDSPRAEVVIEDGFVYVKRALEEGRKFDVVIMDLTDPYSSEIAKQLYTAEFINQIMKLLRGDGIMVTQAGNSFYFPEAYDMVLSAVKANFPVVAEYNVWIPSFGYAVNYILGSLKYDPRALPAEEVDKRLADRGVKTRFYTGRAHVALMNMPVYRRLR", "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": "MTDLSNLVSQCGVDLYDAEVVNENGRVIYRVYITKNGGVSLEECEAVSKLLSPIYDVMPPVSGEWILEVSSPGLERKLSKIEHFTLSIGEFAKIILNDKTEIKGKIVSVKDDNICINIKNNESIEVKFENIKKAKTYMEW", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MKIPILPIVALLSLLALHAAQGAALGTPMEDTTSSNYPSGTEGLSEFLNFNKLQSAFKSDDFLNWHVLTDMFKKALPFINWEFFPKVKGLRSAVPDSQ", "text": "FUNCTION: May act as a soluble regulator of keratinocyte differentiation (By similarity). May play an important role in embryonic skin morphogenesis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTMDQKTDNAGKCPVAHTAPRGRSNRDWWPDQLDVQVLHRHSDLSDPMGKSFNYAEEFRKLDLDALKRDLHALMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRITDGRGGAGQGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGNRISWADLLILTGNVALESMGFKTFGFAGGRTDVWEPEELFWGPEGTWLGDERYSGERQLSEPLAAVQMGLIYVNPEGPNGNPDPVAAAHDIRETFARMAMNDEETVALIAGGHTFGKTHGAGDPSFIGADPEGGAIEDQGLGWKSTFGTGVGKDAITGGPEVTWSQTPTRWSNYFFENLFNFEWELSKSPAGAHQWKAKNAEASVPDAYDATRKHVPTMLTTDLSLRFDPVYEKISRRFLENPDQFADAFARAWFKLTHRDMGPKVRYLGPEVPAEDLIWQDVIPPVDHELVDDADVAGLKAKILASSLSVQELVSTAWDSASTFRGSDKRGGANGARIRLAPQKDWEVNQPAQLARVLSVLEGIQRDFNASQAGGKKISLADLIVLAGNAGVEKAARAAGQEIIVPFTPGRMDASEAQTDAASFAALEPRADGFRNYVNSSRLQFMKPEEALVDRAQLLTLTAPEMTVLVGGLRVLKAGQPEHGVFTSRPEALTNDFFVNLLDMGTQWSPVEGKEGVYEGRDRKTGAARWTGTRVDLIFGSHSQLRAFAEVYAQTDAREKFVKDFVAAWTKVMNADRFDLV", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MITLGEYIIKKQHESPEATGELSSILGAIRLATKVVNRDINKAGLVDIIGATGVENVQGEVQQKMDLYANDVFKAALEARGEVCGVASEEEDEFVSFNDQRCINSKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRISEPGKPAILEDFLQPGTEQVAAGYVIYGSSTMLVYTTGYGTHGFTCDPSLGTFYLSHENMKIPDNGSIYSINEGNYLKFPQGVKKYLKYCQEIDGPTNRPYTSRYIGSLVSDFHRNLLKGGIYIYPSTASAPKGKLRLLYECNPMAFIMEQAGGRATDGFNRRIMELTPTELHQRVPFFCGSSKMVDKVEAMMEEYSSEEK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
{"protein": "MEALRQRIEAAFEARANITPSSVEPGVRADVETVINMLDKGEMRVAEKIDGQWHVNQWLKKAVLLSFRIFDNGVIEGGETKYFDKVPMKFADYDEARFRAEAIRVVPPAAVRKGSFIGKNTVLMPSYVNLGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQAGPTIIEDNCFIGARSEIVEGVVVEEGSVISMGVYIGQSTRIYDRETGEIHYGRVPAGSVVVSGTLPSSCGKYNLYAAIIVKKVDEKTRGKVGINELLRIVD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
{"protein": "MKQSVLDLQATIQETLGDAIVVSDIKLDELTVELAPEQSLSALTKLKEKLGFDQLIDVCGVDYLAFGDVTWETRKATNSGFSRGVFDFAEEDGEADTNIPRRFAVVYHLLSVENNRRVRVKVYPEDTQMPMVDSVVSVWNCADWFEREAFDLFGILFNGHPDLRRILTDYGFVGHPLRKDFPLTGHVEMRYDAEKGRVVYEPVTIENRVNVPRVIRNDVEPKG", "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": "MLRRTVSNFAMSPYMLFISDLAKTGKLKGIRTPGKFVGKKYRQLSAKEKAALQQRAKQASTPAMTAYRRMAHREMSNKSVPIEQRRANLTKKWNETKQAQRAKAQKAQKKPKSAKSKVKKAAKKAKKSKK", "text": "FUNCTION: Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation. SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast. SIMILARITY: Belongs to the KAP family."}
{"protein": "MSKKFIITWDAMQTYCRELAEKQMPAEQWKGIWAVSRGGLVPGAILARELGIRYVDTICISSYDHDHQRDMTVLKAPEGDGEGYLIVEDLVDSGDTARKLREMYPKAKMIAVCAKPSGKELLDDYVVDIAQDTWIEQPWDMSIQYAEPVNRKQK", "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": "MGQELSQHELYVEQLKKALKTRGVKVKGNDLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKIPVTAFSYWNLIKDLIDKKEADPQVMAAVTQTEKILKVSSQTDLRDNSHNKDMDLISLESDDEEAKAPSEKMTMSNKSPKKYPAMLASQNNNTDKDPDLSEVDWDGLEDEAAKYHNPDWPPFLSRPPPYNRTAATAPAVMAVVNPKEELKEKISQLEEQIKLEELHQSLIIRLQKLKTGNERVTSSGNIESHSRTPKWPGQCLPKGKYLINKNTEEYPPKDIFPVTETMDGQGQAWRHHNGFDFTVIKELKTAVSQYGATAPYTLAIVESIADNWLTPTDWNTLVRAVLSGGDHLIWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYANTDAQMQYDPGLFAQIQAAATNAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGNAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDLLNNKNKDRGGCFKCGKKGHFAKDCRDHSNKNPESKVPGLCPRCKRGKHWANECKSKTDSQGNPLPPHQGNGMRGQPQAPKQAYGAVSFVPANSNNPFQNLIEPPQEVQDWTSVPPPTQY", "text": "FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein. FUNCTION: [Capsid protein p27]: Capsid protein. FUNCTION: [Matrix protein p10]: Matrix protein. SUBCELLULAR LOCATION: [Matrix protein p10]: Virion. SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion. SUBCELLULAR LOCATION: [Capsid protein p27]: Virion."}
{"protein": "MNILKSLISVGIMTLISRIFGFFRDVLIAHIFGASMFTDAFFIAFKIPNLLRRIFAEGAFYQSFIPILIDYKSRKDKEYIQEFIRSTCGFTILVLTTFVILGIIFSDYIIFISAPGFSESSKKLQLASNLLKIMFPYILFISLSSLCSSILNSYNYFFIPSLSSSLLNISIIVFSFFFSDYFEPSIISLAWSVMIGGFFQLFYQFPHLYKIKMLVFPKINFKNIGLIKVLKKMGPSTLGSCANQISLIFNTIFSSLLHSGSISWIYYADRLIEFPIGIIGVSLSTILFTSFSCSYSNNTQSEYKILLNWGIRFGLILSLPISVILFMFSKPLVIILFQYGKFTDFDVLMTQKALELYSFGLVSFILVKILVSAFYSCQEVNIPMRISILTLFLTQLMNPFLIFYFQHSGLALSCSIASWINFFLLYWKLYQKGIINFKLNDFIFIFRLLIAVLVMTFFLIFMLYFIPSWKIGSFFDKIIRLFTILSISGIVYLIALHFLGIRLLNYSDKLFQKK", "text": "FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MurJ/MviN family."}
{"protein": "MQVRIIAVGKIKERFLSEGIAEYTKRLSPYLKLSIVEIPEEHRGTRAPAGQEELAKEKEGGRILAAIPERAYVVALDLRGTEISSIELAARMHDWQLAGTNTIAFVIGGDLGLSDAVINRAAFRLSLSPLTFTHPMARLILVEQLYRACRINSGEPYHK", "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": "MNNWKRIVVKVGTSSITDGRGSPSGEKILSLVKECVKLIRADKELVLVSSGAIASGREIIQKLSKRKDLPAKQALSAVGQVRLMQYYSQLFSIFKQPIAQILLTAEDLRDRKRYINISQTFETLLEEKIIPIVNENDTVAVEEIKIGDNDTLSAKVACAINADLLVILSDVEGLYSEDPNISSNALLITDVYEIDESIEKIAGPGKGTGGMFTKVQAAKIVTEAGIPMILARADVENILERIVLKKEKVGTFFYPSEKHLNKRKHWMLFMAKPEGRIYIDDGAKDALLKRGKSLLPVGIKKVEGEFTRGDTVSIFDLRGEEIARGITNYDSLELDKIKGKNTEEIRNILGEDFYEEVIHRNNLVLTNRGDL", "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": "MLDPIAIQLGPLAIRWYALCIVTGLILAVYLTMKEAPRKKIIPDDILDFILVAFPLAILGARLYYVIFRFDYYSQNLGEIFAIWNGGLAIYGGLITGALVLYIFADRKLINTWDFLDIAAPSVMIAQSLGRWGNFFNQEAYGATVDNLDYLPGFIRDQMYIEGSYRQPTFLYESLWNLLGFALILIFRRKWKSLRRGHITAFYLIWYGFGRMVIEGMRTDSLMFFSLRVSQWLSVVLIGLGIMIVIYQNRKKAPYYITEEEK", "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": "MKISANSIRTGNILVYNNDLWVVSKQPEHTQPGKGGAYVQVEMKNLKTGTKRNERFSSSDHLEKAELEQKDYQFLYFEDNNIVLMDNQTFEQISVNKEILDEKLPFLTENMIVKVEFYNEKPLSIELPATVILEIIETDPVIKGATATASYKPATLANGVKVKVPQYLEIGEKIVVKTEDLTYVERSK", "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": "MTVKTRFAPSPTGYLHVGGARTALYSWLYAKNQGGEFVLRIEDTDLERNSQEAVDAILEGMEWLGLEWNEGPYFQTQRFDRYNEMVDKLLEEDKAYKCYASKELLDEVRAEQEANKEMPRYDANHPKIKAANEAAKDGEPCVIRFRNPKEGSVVFDDQIRGRIEISNTQMDDLIIRRTDGSPTYNFCVVVDDWDMGITHVVRGEDHINNTPRQINIYEALGAPVPTFAHCAMILGDDGAKLSKRHGAVSVMQYRDMGYLPAALNNYLVRLGWSHGDQEIFTQEEMINLFSLNAVSKSASAFNTDKLQWLNNHYIKNSDPAYVAEHLQWHLDQQKLDVTNGPAITEVIKLVGERCNTLVELAEQIGYFYEDFAEFEAGAAKKHLRGVAKEPLELALAKAEALTEWTTANIKDGVIAAVCEELEIGMGKIGMPLRVAVTGGGQSPSVDAVMELIGKERCVARIKMALEFIAEREANA", "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": "MGTVTTADPHASFLADKGGKVFVAGHRGLVGSAILRHLVSLGFTNVVVRTHAELDLTRQSDVEAFFAAELPRYVVLAAAKVGGIHANSTFPADFIAANLQIQTNVVDAALKCGSVRKLLFLGSSCIYPKFAPQPIPENSLLSGPLEPTNEWYAVAKIAGIKMCQAYRIQHGFDAISAMPTNLYGPQDNFHPENSHVLPALIRRFHEAKASNAAEVVVWGTGSPLREFLHVDDLADAVIFLMDHYSGLEHVNVGSGSEVTIKELAELVKEVVGFQGKLVWDSSKPDGTPRKLMDSSKIQEMGWKPKVPLKEGLVETYKWYVENVISAKK", "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. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily."}
{"protein": "MTQAQDHAKDHAMNIGVFIPIGNNGWLLSENAPQYMPSFELNKQITLKAEQHGLDFVLSMIKLRGFGGKTEFWDHNLESFTLMAGLAAVTSRIKLYATAPTLCLPPAIVARMASTIDSISNGRFGLNLVTGWQRPEYAQMGLWPGDEYFGRRYEYLSEYAQVLRELWETGRSDLKGEFFQMEDCRLSPRPQAEMKIICAGQSAAGMAFTATYADYNFCFGKGVNTPTAFAPTVERLEEAKAKTGRDVSSYVLFMVISDETDEAARAKWEHYKAGADAEAIAWLGLQGAADTKSGADTNIRQMADPTSAVNINMGTLVGSHATVAALLDEVVTVPGTGGVLLVFDDFLKGLDDFGTKIQPLMRSRRHVTGEALAEVA", "text": "FUNCTION: Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen atoms in the process to yield ureidoacrylate peracid, that immediately reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN- N(5)-oxide reacts spontaneously with NADH to produce FMN. Requires the flavin reductase RutF to regenerate FMN in vivo. SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA subfamily."}
{"protein": "MAKKGKKIVAAQQKVDADRKYDISEGIDTALQARFAGFDESVDIAVRLGVDPRHADQMVRGSVVLPHGTGKEIKILVFAKGEKEKEALDAGADFVGNDELIEDIKNGWFGFDKAVATPDMMGAVGKIGKLLGPRGLMPNAKTGTVTFDVARAVNDLKAGKIDFRVDKAGIVHAPLGKASFGTEKLQDNMLALLRMLVAMKPATSKGAYMRSLAVSTSMGAGVRLDPLLVKDAVK", "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": "MFENTLQGALIGVTVIPTLILSLPTTSFVRYAIYPLPALLVLRALLWPPTEGLAKETYLLGLLMTDTSFKMFDYLYLQGYNAPAKFLQVDRVGRTITKVHEYPKDTLGQVKWALSLVTSHRGIGWNIQVPLQKIKYPSSRVAYIFESMVSILSIYLGLYTCGSLCDYMVQVLRKEADSPYPWVYGLFKNSIFQMVVAFMGIFAMVSNSVLVYNLARMICVTSGIKGDWGKIESWPNMFGGFEDAWSIRNVWGRAWHQNLRRCLTAPGEKVSSLIFGSSPKLGRVPRLIRRYFLVFSAFGVSGLLHSLAVYYGSKTDTMPYEDSTPLHMRPGWYVTGYFFYIQPFAITLEDFICWATGTSTESKGVKATKVRWFVGMVYTLTWFTWGTAVLWIHPQLASLGYQRTSDAELGYVHILVSTSEAASILPLNPWPAVVKTVSPTFWDVYGYFKSSGLGGYLYLYAYTTLEILGGSGFNVLKSASSVV", "text": "FUNCTION: Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sesquiterpenyl epoxy-cyclohexenoids (SECs) such as anthrobotrisins and arthrosporols, metabolites that possess a novel hybrid carbon skeleton consisting of a polyketide-derived epoxycyclohexenol combined with a terpenoid-derived monocyclic sesquiterpenol substructure (PKS-PTS hybrid) (PubMed:33823587). The SEC pathway plays an important role for fungal soil colonization via decreasing fungal nematode-capturing ability (PubMed:33823587). The role of the acetyltransferase in SEC biosynthesis has still to be determined (Probable). The pathway begins with the biosynthesis of 6- methylsalicylic acid (6-MSA), the first precursor of the polyketide- derived epoxycyclohexenol in arthrosporols, by the polyketide synthase (PKS) AOL_s00215g283 via condensation of 1 acetate and 3 malonate units. The 6-methylsalicylic acid decarboxylase AOL_s00215g281 then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m- cresol. The cytochrome P450 monooxygenase AOL_s00215g282 further oxidizes m-cresol to yield toluquinol. With the assistance of the oxidoreductase AOL_s00215g277, the polyprenyl transferase AOL_s00215g276 catalyzes the farnesylation of toluquinol to produce farnesyl hydroquinone, the hybrid precursor for biosynthesis of SECs. Farnesyl hydroquinone undergoes epoxidation and then subsequent dehydrogenation to form farnesyl epoxy-quinone, the first and simplest SEC. The cytochrome P450 monooxygenase AOL_s00215g278 and the FAD- dependent monooxygenase AOL_s00215g279 might be involved in the oxygenation of the phenol moiety, most likely in the epoxy formation. The cytochrome P450 monooxygenases AOL_s00215g274 and AOL_s00215g280 are involved in specific regional ketone reductions at respectively C-4 and C-1 of farnesyl epoxy-quinone PubMed:33823587 (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the wax synthase family."}
{"protein": "MTNSCDRPLITPLEPPNASFIHISVLSQETIAGLNIIPGGHYLDATVGSGGHSRLILATFPDVRITAIDRDSQAIAAAASNLAELGSERLKFWQGNFADYPGKIAEFSGIIADLGVSSPQFDFPERGFSFRHEGALDMRMDQTQSLTAGEIINQWSETALADLFYQYGEERRSRSMAKHIVQQRPFKTTTQLAEAIAQTVPPKYRYGRIHPATRVFQALRIAVNEELSSLERFLDQAPQWLQPGGRIGIISFHSLEDRIVKYRFRDSSWLTVMTKKPIIPQREEQLKNPRSRSAKLRLAERHLV", "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": "MARYRCCRSQSQSRCRRRRRRRCRRRRRRCVRRRRVCCRRYTVLRCRRRR", "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": "MRVGIKVLGCPKNEADCEVLAGVLREGGHEIVFDVKDADVVVLDTCAFIEDAKRESIDEIFSFVDAKDQYGYKLVVKGCLVQRYYEELKKEVPEVDQWIGVADPEEIANAIENGTDLVPDQPETVYRYRKRIDLEERPYAYVKISDGCDRGCTFCSIPSFKGSLRSRSIEDITREVEDLLKEGKKEIILVAQDTTSYGIDLYRKQALPDLLRRLNSLNGEFWIRVMYLHPDHLTEEIISAMLELDKVVKYFDVPVQHGSDKILKLMGRTKSSEELKKMLSSIRERFPDAVLRTSIIVGFPGETEEDFEELKQFVEEIQFDKLGAFVYSDEEGTVAFNLKEKVDPEMAKRRQEELLLLQAEISNSRLDRFVGKKLKFLVEGKEGKFLVGRTWTEAPEVDGVVFVRGKGKIGDFLEVVIKEHDEYDMWGSVI", "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": "MWSRQRMRHKPLWALISLTVLLLVLDKSNANTEPVETSTTSEPDASPGCRAPDVRFTIVKPEATTEQPLAKFETTQIYLPEDFTTADVEFVDSVPRHPNENHAAVINPYSLDLGDDHLHVGDAAASLVGDDDLGDEDEDHHGDPEDKRLNANRKQGKRRRAGSGRRRRIENENGQTGRGRGSRYKRHAILHDTEASPETDRWAGSKLAAEGDVYYVHIADILKSREPNRELKSKLHKLKMKARLNKCLAEGGKEKCTRLLKKKPKKKVVEKEQTLKKEKKFPKEEQSKEKVPENGQTPKEDELELDHPETAAAHHRRRGDSHAAELDQRDRSPRWRRRRSTEFKGDLGQLPPESGIGPEPEPLADQDLKDLQQYGNQSSSARVALLWQRVKRKSGKTTGALSRPKGGGDSSSKTTSRKDKGIYDEEAGYTPIHPDDPEFDEEEEEDEEVDILQQFTEVSEIRFPGEIGPMGDRRLCKIRCVKGKWVGPLCATNEEDDNGNVKFQPLYKSCHVNRIPSHLLLSYRNISVTPIPPNRGWRKTRLSKSTLLSNTEINVGWDLPHGHSLQARCQELGIYKLLGESRVLCSNGLWAPRMPSCVPTTVLTNYSEDSAPSIRIKIFNGSHSFEPSGVMAVPPHSTVLMDCMYPRVRGTPEWSWTSWYMQYSTGWSPAQEEKAVRYRLSIKNIENNDSGTFTCTSPRGLTNSIAVVVATSTCPQLTEPLAPLKLRLEGNKLGQRAHYECPEGFRLDGAWNATCLASGNWSSPTPTCHAIQCPRLELDDPHLSLIELNTSAWGRAVFKCQWGFKLTGPAQLDCEPSGVWSGPVPRCKVIQCVMPVAPLNGRIGGTSLSQRRLTVGALVTFSCNDGHSLVGESSIICTENGQWSHSPPFCKSQCPYPGDPPNGLIAPLKFNYDAGDYLSVQCRPGFVQSYEGPPERPKCQPDGRWSGPMPKCKSYEEV", "text": "FUNCTION: Plays a role in the formation of functional neural circuits from the early stages of synapse formation. Has a role in the development of CNS functions involved in locomotor activity. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MPTYAPKAGDTTRSWYVIDATDVVLGRLAVAAANLLRGKHKPTFAPNVDGGDFVIVINADKVAISNEKLRNKRAYSHSGYPGGLRKRSIGELMEKHPDRVVEKAIVGMLPKNKLSRQIQSKLRVYAGPGHPHTAQQPVPFEIKQVAQ", "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": "MAFENKIVEAFIEIPTGSQNKYEFDKERGIFKLDRVLYSPMFYPAEYGYLQNTLALDGDPLDILVITTNPTFPGCVIDTRVIGYLNMVDSGEEDAKLIGVPVEDPRFDEVRSIEDLPQHKLKEIAHFFERYKDLQGKRTEIGTWEGPEAAAKLIDECIARYNEQK", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase family."}
{"protein": "MALIFGTVNANILKEVFGGARMACVTSAHMAGANGSILKKAEETSRAIMHKPVIFGEDYITEADLPYTPLHLEVDAEMERMYYLGRRALTHGKRRKVSVNNKRNRRRKVAKTYVGRDSIVEKIVVPHTERKVDTTAAVEDICNEATTQLVHNSMPKRKKQKNFLPATSLSNVYAQTWSIVRKRHMQVEIISKKSVRARVKRFEGSVQLFASVRHMYGERKRVDLRIDNWQQETLLDLAKRFKNERVDQSKLTFGSSGLVLRQGSYGPAHWYRHGMFIVRGRSDGMLVDARAKVTFAVCHSMTHYSDKSISEAFFIPYSKKFLELRPDGISHECTRGVSVERCGEVAAILTQALSPCGKITCKRCMVETPDIVEGESGESVTNQGKLLAMLKEQYPDFPMAEKLLTRFLQQKSLVNTNLTACVSVKQLIGDRKQAPFTHVLAVSEILFKGNKLTGADLEEASTHMLEIARFLNNRTENMRIGHLGSFRNKISSKAHVNNALMCDNQLDQNGNFIWGLRGAHAKRFLKGFFTEIDPNEGYDKYVIRKHIRGSRKLAIGNLIMSTDFQTLRQQIQGETIERKEIGNHCISMRNGNYVYPCCCVTLEDGKAQYSDLKHPTKRHLVIGNSGDSKYLDLPVLNEEKMYIANEGYCYMNIFFALLVNVKEEDAKDFTKFIRDTIVPKLGAWPTMQDVATACYLLSILYPDVLRAELPRILVDHDNKTMHVLDSYGSRTTGYHMLKMNTTSQLIEFVHSGLESEMKTYNVGGMNRDVVTQGAIEMLIKSIYKPHLMKQLLEEEPYIIVLAIVSPSILIAMYNSGTFEQALQMWLPNTMRLANLAAILSALAQKLTLADLFVQQRNLINEYAQVILDNLIDGVRVNHSLSLAMEIVTIKLATQEMDMALREGGYAVTSEKVHEMLEKKLCKGFEGCMGRINLVGKILRNQAFKKALEIWAKAFNHEKHRRLRRTYRLVCEIAFQVPLGTPEGNHLKSRKWWRKKGKSSEECHDKRGFSQNLQHAS", "text": "FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma. SIMILARITY: Belongs to the potyviridae P3N-PIPO polyprotein family."}
{"protein": "MHNQYGSLFSITTWGESHGPSIGVVIDGCPAGLPLAPEDFLPAMKRRRPGQLHTSPRQETDSVTILSGVYQQKTTGTPISLLIQNEDASSTSYEQLNDCYRPGHAQFAYEGKYGFADNRGGGRSSARETAARVAAGVVAKKILSSQGIKTLAFLSGFGPLENKTYPKLTDPLIRKVYSSPFYTILSQEEIQNLLLHDPEDSFGGIVSFITSPLPIGLGEPVFGKLPALLAAGMMSIPATKGFEIGEGFASAHMTGSTYLDSFIAKEGEISFQTNRCGGTLGGISIGQPLEGRVAFKPTSSIRKPCPSVSKDGEPITYKTPKQGRHDPCVAIRAVTVVEAMLDLTLVDLLLQHRCAKL", "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": "MSERDSGSSGRAKAAAAVAAATPRAKTSGPAPFGAFVRKPVEKAEGKAKAQVANAGSGAAEMRMETVESWPADAVEVGAIVDAYGLKGWVKVAAHADAGHGGDALLSAKRWWLIKGQERKSAPSLQAKMHSDSVVAHLGGVTDRDVALALRGSRVYISRSEFPALGADEFYWVDLLGLDVVNVAGVNLGKVADMIDNGAHSVLRIEYPDTDKSGKPVIGERLIPFVGVFVKTVDQAAKQITVDWEADY", "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": "MILFPAIDLKDGQCVRLKLGDMEQATVYNPDPGAQAKAFEDQGFEWLHVVDLNGAFAGESVNGAAVDAILKATKNPVQLGGGIRSLAHIETWLQHGLSRVILGTVAVRDPALVIEACKLFPGKIAVGIDAKGGKVAVEGWAEASELGVVELAKKFEGAGVAAIIYTDIDRDGILTGINWESTLELADAVSIPVIASGGLASIEDIRRMLEPDARKLEGAISGRALYDGRIDPAEALALIQAAKG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MTEITNLQDKVDVDETLLNIITQAVSLTLNEEGRAGVVSIALVDNNYIQSLNREYRQKDVPTDVLSFPLADDKDDEVLGDVVISLEKAAEQAKEYGHSFFREVAFLTVHGVLHLLGHDHYEEEETRIMREKEEKILSALGLER", "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": "MERTCLAVILAAGDSTRMKSSKSKVLHPVAGRPMIAHVVEAVASAGISSVALVVGRDAEDVAKAASIAGVDIESFLQKERLGTGHAVLAAREAIAKGYDDILVTYGDVPLQTDGPLKAARQGLADGSDVVVIGFHTDRPTGYGRLLVKDGELIAIREEKDATDAERTVTWCNSGLMAINGRKALDLLSRIGNANAKGEFYLTDLVEIARSLGGRVTAVDAPEIEMTGCNTRAELAVIERFWQERRRHQMMLSGVTMIAPETVFLAYDTVIGQDALIEPNVVFGPGAVIDSGAVIHAFSHIEGAHVSQGATVGPFARLRPGADLGTGSKVGNFCEVKNGRLGEGAKVNHLTYIGDAVIGAGSNIGAGTITCNYDGVNKSETVIGENAFIGSNSSLVAPVTIGDGAYIASGSVITVNVPADALALGRARQEIKTGRATLLRERALAIKAAKKAKA", "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": "MTQGKQPDGVARTSYKDTLNLLQTSFGMRANASQREPELQEFWKQQGIDLELGLNNQGQNFTLHDGPPYANGALHMGHALNKVLKDIINKHQILRGRQVRFVPGWDCHGLPIELKVLQNLNQEQREALTPLKLRKKAAAFARKQVDSQMAGFRRWGIWADWEHPYLTLQKEYEAAQIQVFGKMFQKGYIYRGLKPVHWSPSSRTALAEAELEYPDGHTSPSVYVAFPAAKLPEKLRTSLGNQGLELPNNGLELGQALQIAIWTTTPWTLPANLAVSVNEKLDYSFAVDNQGRLLLVAAELLPSLRDTLALELTARATVKGALLAGLIYKHPLLDRDSPIVIGGEYITTESGTGLVHTAPGHGVDDFNTGQKHDLGMLCPVDESGTMTSEAGPFAGLNVLKDANPTIIAALEERGALLKHEPYAHRYPYDWRTKKPTIFRATEQWFASVEGFRNEALTAINSVEWLPASGRNRMEAMVRERGDWCISRQRTWGVPIPVFYEREGNEVLLNDETLAHVKALITEHGADVWWERNEVELLPPAYAAEAERWRKGTDTMDVWFDSGSSWAAVASQQEGLAYPTELYLEGSDQHRGWFQSSLLTSVAINSQAPYRQVLTHGFALDEKGRKMSKSLGNVVDPAVIIDGGKNQKQEPPYGADVLRLWVSSVDYSADVPIGASILRQIADVYRKVRNTSRYLLGNLHDFDPERDAIPVPELPLLDRWMLQRTAEVMDEISTAFDRYEFYRFFQLLQSYCVVDLSNFYLDIAKDRLYVSSPSERRRRSCQTAMALIIERLAGAISPVLCHMAEDIWQNLPYSVAEDSVFRRGWPTVPETWRDPSMMAPMHQLRELRSAVNRVLEDCRSQGELGAALEAAVRLEAHSEALQEALDWLRQQGDPDVDGLRDWLLVSHLQVGGEPWAELLASQDNALATIEVARARGSKCERCWHYETDVGQHTTHPTLCGRCVGVLEHQ", "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": "MTERRIIHIDMDYFFAQVEMRDNPKLKGKPVIVGGKASSRGVVSTASYEARKYGVHSAMPMSQAHKLCPNGYFVTSNFGAYRETSAQIMSIFRSYTDKVEPMSLDEAYLDITELVRPDLPASKIAQYIRKDILEQTHLTASAGVSYNKFLAKLASGMNKPDGMTVIDYRNVHDILMTLDIGDFPGVGKASKKVMHDNGIFNGRDLYEKTEFELIRLFGKRGRGLYNKARGIDHSEVKSTRVRKSVGTERTFATDVNDDEEILRKVWELSGKTAERLNKLQKSAKTVTVKIKTYQFETLSKQMSLRDSVSSEEDIYNIAYLLYNDLKDPDVPIRLIGVTVGNLEQSTYKNMTIYDFI", "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": "MAKVRTKDVMEQFNLELISGEEGINRPITMSDLSRPGIEIAGYFTYYPRERVQLLGKTELSFFEQLPEEEKKQRMDSLCTDVTPAIILSRDMPIPQELIDASEKNGVPVLRSPLKTTRLSSRLTNFLESRLAPTTAIHGVLVDIYGVGVLITGKSGVGKSETALELVKRGHRLVADDCVEIRQEDQDTLVGNAPELIEHLLEIRGLGIINVMTLFGAGAVRSNKRITIVMNLELWEQGKQYDRLGLEEETMKIIDTEITKLTIPVRPGRNLAVIIEVAAMNFRLKRMGLNAAEQFTNKLADVIEDGEQEE", "text": "FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-45' 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 'Ser-46'. 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. SIMILARITY: Belongs to the HPrK/P family."}
{"protein": "MRILLSNDDGVFAQGLAELYKELKEDHEITVIAPDRNCSGASNALSLQQPLRMEQMQSGFYAVNGTPSDCVHVGVNSFLQQDPELVISGINHGANLGDDVIYSGTVAAATEGRYMGLPAIAVSLCAHTSDNFVSAAKFVRRIVTHLQAHPLPADQILNVNIPDLPYGEIKGIKVTRQGRRHRAKTMIKDTDPRGKTIFWYGPVGEEQDAGPGTDFHAISEGFCSVTPLSVDMTAHQSLEDVRQWITKI", "text": "FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family."}
{"protein": "MKMEELVREIERLKEERNAIIMAHNYQLPEIQDIADFLGDSLELARKAVNVDADVIVFVGVDFMAETAKILNPEKTVLLPTRRATCAMANMLKVEHILKAKEQYPDAPVVLYVNTTAETKAYADVTVTSANAVRIVEKLDSDVIIFGPDKNLASYVAKMTGKKVIPVPEYGHCYVHRQFTLEDVERARKLYPNAKLMVHPECEPEVQERADIIVSTGGMIRRAPEHDEWVVFTEREMVYRLQRLYPDIKFHPAKEDAICIGMKAITLNHIYESLRDMKYEVEVPEDIAEKARRAIERMLEMS", "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": "VLIIAVLFLTACQLTTAETSSRGKQKHRALRSTDKYSRMTKHCTPPEVGCLFAYECCSKICWRPRCYPS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
{"protein": "MQYRSKNLPIILASQSPARVELLKRIKITPAQIIPADIDETPNLRESPNHLATRLAYEKATKIASQIEDSAIIIAADTVTALGRRILPKASSAEEVRYCLNILSGRRHRVYTGLCIIKKDKDQLVTRQKIVQTVLKFKRLSEEELNFYCSLDEGIDKAGGCKISGYAEAFISFISGSYSNVMGLPLFETVNSLNSLGFISYK", "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": "MKAEIHPDYHTIKVVMTDGTEYLTRSTWGKEGDTLNLDIDPKSHPAWTGGNAQIMDRGGRVSRFQKKFSGFLKKD", "text": "FUNCTION: Binds the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily."}
{"protein": "MNDSVKTSLKRTLVGRVVSNKMDKTVTVLIEHRVKHPIYGKYVVRSKKYHAHDEANTCNEGDLVEIQETRPVSKTKAWTVSRLVEAARVI", "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": "NNYCKIKCRSGIHTLCKYGTSTKPNCGRSVVKASGLTKAEKLEILKQHNEFRQKVARGLETRGNPGPQPPAKSMNTLVWNDELAQIAQVWASQCKYGHDNCRNTAKYLVGQNIAEQSTTAASFEPVSNMVKMWSDEVKDYQYGSSKNKLNDVGHYTQMVWAKTKEIGCGNIKYIENGWHHHYLVCNYGPAGNIGNEPIYEKK", "text": "FUNCTION: Does not show toxicity when intravenously injected into mice tail. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MIIPALDLIEGQVVRLYQGDYGQVTEYKVDPAEQFNLYHQAGANWLHLVDLTGAKDTTARQLDLIAKLLASTPANIQIGGGVRTEQDVIDLLEAGAQRVVVGSTAVKQPELVKGWMEKYGAEKIVLALDINIYQDGTRKVAISGWQEDSGVTIEALINDYLTVGLQHVLCTDISRDGTLEGSNVELYVDLCKQYPQVQFQSSGGIGSLADIEALKGSGVAGVIVGRALLDGKFTAEEAFACWQSE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MQHLAIFGGTFDPIHWGHLLIAEAALQQISIEKVIWVPSLNPPHKKASAFRHRLAMLQLATQDNPAFTVSSVEKNRSGVSYAINTLTDLSVCFPNTHWYWIVGLDTFQTLPRWYRGQELAPMCDWLIAPRLVGGENIAQSELICKQVKQQLRKQSNTIHWHLLHIPLVGVSSSLIRKLYRVGKSIRYLVPEDVRSYIADHKLYSEDSE", "text": "FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). SIMILARITY: Belongs to the NadD family."}
{"protein": "MKIISDIQELRDHLRGQNRASFVPTMGNLHEGHLSLMRLARQHGDPVVASIFVNRLQFGPNEDFDSYPRTMQADIEKLEKEGVYILFAPTERDLYPQPQEYRIDPPQQLGDILEGEFRPGFFKGVCTVVLKLFSCVQPKVAVFGKKDYQQLMIIRQMAKQFALPVEIIPGETIRAEDGLALSSRNGYLSVEERAEAPELQRVLQQVREQVLGLKHRDVSSLLEIEKKAIATLAGRRWEPDYIAIRQQGDLAPASNEQLQAGEPLVILTAAKLGKTRLIDNLEI", "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": "MESLFPAPFWEVLYGSPLQGNLSLLSPNHSLLPPHLLLNASHGAFLPLGLKVTIVGLYLAVCVGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTAVLLTLPFQGTDVLLGFWPFGNALCKAVIAIDYYNMFTSAFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASIVGVPVAIMGSAQVEDEEIECLVEIPAPQDYWGPVFAVCIFLFSFVIPVLIISVCYSLMVRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLVQGLGVQPGSETAVAVLRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCAPTRRREMQVSDRVRSIAKDVALACKTSETVPRPA", "text": "FUNCTION: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. 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 via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasmic vesicle Note=Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface. Internalization requires phosphorylation at Ser-363. Can recycle to the cell membrane (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MKKVIITPSKLRGSVKIPPSKSMAHRAIICASLSKGESVISNIDFSEDIIATMEGMKSLGANIKVEKDKLIINGENILKDSNYKFIDCNESGSTLRFLVPISLIKDNRVNFIGRGNLGKRPLKTYYEIFEEQEIKYSYEEENLDLNIEGSLKGGEFKVKGNISSQFISGLLFTLPLLKDDSKIIITTELESKGYIDLTLDMIEKFGVTIKNNNYREFLIKGNQSYKPMNYKVEGDYSQAAFYFSAGALGSEINCLDLDLSSYQGDKECIEILEGMGARLIESQERSLSIIHGDLNGTIIDASQCPDIIPVLTVVAALSKGETRIINGERLRIKECDRLNAICTELNKLGADIKELKDGLIINGVKDLIGGEVYSHKDHRIAMSLAIASTRCKKEVIIKEPDCVKKSYPGFWEDFKSLGGILREE", "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": "MKIFVPLLSFLLAGLTTGLDWWEHGNFYQVYPRSFKDSDGDGIGDLDGVTEKLKYLKDIGMDGVWLSPIFSSPMADFGYDISNFREIQTEYGDLDAFQRLSDKCKQLGLHLILDFVPNHTSDQHEYFKKSVQKDETYKDFYVWHPGVHGPNNTKVPPSNWISVFRGSSWEWNEERQEFYLHQFLKEQPDLNYRNPAVVEEMKNVLRYWLDRGVSGFRIDAVPYLFESDIIDGRYRNEPESRTTDDPENPAYLVHTQTMDQPETYDMIYQWRAVLDEYSKTDNRTRIMMTEGYTSLPKIIEFFGNATANGAQIPFNFEVISNVKKNSTGADFATYVKRWLDAKPANRRSNWVLGNHDNNRLGSRLGENKIDLYNIALQTLPDIAVTYYGEEIGMLDQWIPWNETVDPAACRSDEASYSAYSRDPARTPMQWDSGKNAGFSKAAKTWLPVADNYKTLNVKIQDRARKSHLKIFKKLTKYRKRQILTEGDIDIKVSGENLLVYKRKVDKVGYVVVALNFGTEPVALGLSSLFDRADQRMQVVVSSNRVSTPDNVWVDVDNYVLIGESGIVLQYLWGKNPIVS", "text": "FUNCTION: Assists the mosquito in its sugar-feeding capabilities (Potential). Glucosidase (By similarity). SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
{"protein": "MSATGPFSIGERVQLTDAKGRRYTMSLTPGAEFHTHRGSIAHDAVIGLEQGSVVKSSNGALFLVLRPLLVDYVMSMPRGPQVIYPKDAAQIVHEGDIFPGARVLEAGAGSGALTLSLLRAVGPAGQVISYEQRADHAEHARRNVSGCYGQPPDNWRLVVSDLADSELPDGSVDRAVLDMLAPWEVLDAVSRLLVAGGVLMVYVATVTQLSRIVEALRAKQCWTEPRAWETLQRGWNVVGLAVRPQHSMRGHTAFLVATRRLAPGAVAPAPLGRKREGRDG", "text": "FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA. FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family."}
{"protein": "MSFSVDVLANIAIELQRGIGHQDRFQRLITTLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRRFALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPGQESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDVFSDEELRLIAALAAGALSNALLIEQLESQNMMPGDATPFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLISGETGTGKELVAKAIHEASPRAVNPLVYLNCAALPESVAESELFGHVKGAFTGAISNRSGKFEMADNGTLFLDEIGELSLALQAKLLRVLQYGDIQRVGDDRSLRVDVRVLAATNRDLREEVLAGRFRADLFHRLSVFPLSVPPLRERGDDVILLAGYFCEQCRLRLGLSRVVLSAGARNLLQHYRFPGNVRELEHAIHRAVVLARATRNGDEVILEAQHFAFPEVTLPPPEAAAVPVVKQNLREATEAFQRETIRQALAQNHHNWAACARMLETDVANLHRLAKRLGMKD", "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": "MTSTEGILAGKYPAKAHARRVVEYLRQNGFEGDGVLYLEAQKTKMIEDNDSEQPFRQRRFFFYLSGCLLPDAHLTYHISSDKLALFIPPLDPESVIWSGLPLSPTQAKELYDVDEVLYTTDINPTLAHLASEVGTSGFVFAIDGQISDDISFKNFPETDLVALKTAIEECRVVKDAYEVAMIRKANDVTAQAHVAVLKATKSATNERELEAAFIGTCIAHGCREMAYHPIVASGTSSATLHYVNNDEPLIDLTTNKKKLNLLLDAAGEYKTYCADVTRTFPLSGKFSPESRQIYDIVLEMQTKSLAMLKEGVLWEDVHVTAHRVAIKGLLKLGILRGSEEELLEKRISVAFFPHGLGHYLGMDTHDTGGHANYADKDKMFRYLRVRGKLPAGSVITVEPGVYFCRFIIEPYLKDSELSKYIDADVLEKYWEVGGVRIEDNIHITKEGYDNLTTAPKTADQLELMINGS", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MGSVLGLCSMASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPGMEEQLNKIPGFCENEKGMVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAAIHNGFWFFKFAAAIAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNESWVEKMEEGNSRCWYAALLSATALNYLLSLVAVVLFFVYYTHPASCAENKAFISVNMLLCLGASIMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETECNPSLLNIIGYNTTSTVSKEGQSVQWWHTQGIIGLILFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGGARNDGSLEDGDDVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQWTAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD", "text": "FUNCTION: Enhances the incorporation of serine into phosphatidylserine and sphingolipids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TDE1 family."}
{"protein": "MATSKPASIAMISLGCPKALVDSERILTQLRTEGYQVTPSYDDADVVVVNTCGFIDSAKAESLEAIGEAIAENGKVIVTGCMGVEESVIREIHPSVLAVTGPQQYEQVVLEVHRAAPPKADHNPYVDLVPPQGVKLTPRHYAYLKISEGCNHRCSFCIIPSMRGDLVSRPVGDVLSEAERLVKAGVKELLVISQDTSAYGVDLKYRSGFWNGRPIKTRMTELCAALSELGVWTRLHYVYPYPHVDEVIPLMAQGKVLPYLDIPFQHASPRILKAMKRPAFEDKTLARIKRWREECPDLTLRSTFIVGFPGETEADFQYLLDWMSEAQLDRVGCFQYSPVNGAPANELDGAVPDEVKQERWDRFMAHQQAISAARLQTRVGREIDVLIDEVNADGAVGRSSADAPEIDGCVYVGNAATLRPGDMARVRITAADEYDLHGDAV", "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": "MKSSAQLCMEARNYNFNAAAPLRLYLATCVRLVEEAQAAAQADDVARAYMLYVRYLDLCMHQLSGHREVQQPVTDAERLSRDEYEQLLRLEVPAVLRLTEELKSAVDLRHERGRASLARSVVPEAGRGEHSRQEVQLPPSFDEERFNRTVQWFLAAGRSMSLPVSAEEPAVREVFSYPELPKLSMAAESWAPS", "text": "FUNCTION: Inhibitor of the DOA4 deubiquitinase involved in the regulation of protein degradation by the proteasome and maintenance of a normal level of free ubiquitin. SUBCELLULAR LOCATION: Endosome. SIMILARITY: Belongs to the RFU1 family."}
{"protein": "MKKLTTIFIVFTLALLFVGNSTSANNGSVVEQNGQLSIQNGQLVNEHGDPVQLKGMSSHGLQWYGQFVNYDSIKWLRDDWGITVFRAAMYTSSGGYIEDPSVKEKVKEAVEAAIDLGIYVIIDWHILSDNDPNIYKEEAKEFFDEMSALYGDYPNVIYEIANEPNGHNVRWDSHIKPYAEEVIPVIRANDPNNIVIVGTATWSQDVHEAADNQLDDPNVMYAFHFYAGTHGQQLRNQVDYALSRGAAIFVSEWGTSAATGDGGVFLDEAQVWIDFMDERNLSWANWSLTHKDESSAALMPGANPTGGWTAAELSPSGAFVREKIRESASIPPSDPTPPSDPDPGEPDPTPPSDPGEYPAWDPNQIYTNEIVYHNGQLWQAKWWTQNQEPGANQYGPWEPLGDAPPSEPSDPPPPSEPEPDPGEPDPGEPDPGEPDPTPPSDPGEYPAWDPTQIYTNEIVYHNGQLWQAKWWTQNQEPGYPYGPWEPLN", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSGSGKNGQGEPTRVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE", "text": "FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis- promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization."}
{"protein": "MSTVNELVNRVDETYDVLQIEKEIGLDNIALSDLELLATGGYSPLTGFLGKKDYDSVVETLRLANGSVWSIPITLPVTEEVAETLKVGEEVKLVNGGNVYGVIQIEDIFVPDKEKEALLVYKTTDEAHPGVKKLYERPNVYVGGAIVLTKRFENNPFPSYHLDPIETREEFKKRGWKTVVGFQTRNPVHRAHEYIQKSALEIVDGLFLNPLVGETKSDDIPADVRMESYEVLLQNYYPKDRVFLSVFPAAMRYAGPREAIFHALVRKNFGCTHFIVGRDHAGVGDYYGTYEAQEIFTNFTVEELGITPLFFEHSFYCTKCEAMASTKTCPHGKEDHVILSGTKVRELLRNGEIPPSTFSRKEVVEVLIKGLKKEVVTE", "text": "SIMILARITY: Belongs to the sulfate adenylyltransferase family."}
{"protein": "MSGRELRHGYTTGACAAAAAAGAARMLRRQELADEAEIVLPRGERVAFRLHGQEFTETWATCHVVKDAGDDPDVTNGAEIHATVRREALNRPGARTMVFVTGGRGVGTITKPGLAVPVGEPAINPVPMRMITEAVKAEFSVVCLPQILTVTVSIPNGEELAKKTLNARLGIVGGLSILGTTGIVRPISAKAWTDTLDAAIDVALACGCRTLVLSTGRTSELVVQGALAGEHLREEACVMMGDHVGYALRACARKGAEQAVLAGQFAKLLKIACGHEQTHVSSSELDLRLLAEWIAATPAASHLASLVEGANTARQVLEASGNDPALMELVCSRAREAARLLAPSLRIKVLLAGYDSTVLYFG", "text": "FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. SIMILARITY: Belongs to the CbiD family."}
{"protein": "MSEPTTTPVVGNSASGDSAEQHDLGQKRGKGGNWNRPRGDHQAKKQKMDRRGDRQREQEKQGEGRDTRRKTDGPLVADEVRQPKRKVACMIGYCGTGYHGMQLNPPQKTIEGDIFQAFVKAGAISQNNADDPKKSAFMRAARTDKGVHAAGNVISLKMIIEDENIVEKINSHLPEQLRVWGVSRTNKAFECRKLCSSRVYEYLMPTYSFLNPRPGTVMSEKLLKDGTSPDEEGKKYWESVAADLESQGVSYDEWMKRACIDEIKGEETKEVAESEVKTDSKTDAATLEKIKAVERRHREEFRISGERLAKIREILKIYEGTHNFHNFTLGKAFKDPSAMRTMKSLTCSDPFLIDGTEWVSIKIHGQSFMLHQIRKMISMVALSVRCNADPQKLIPQTFEKARINIPKAPALGLLLERPVYDSYNKKLQGEFGREGVHFDNWNDQIEAFKHKFIYDKIYAEEKGQHVFHAFFSFVDVFTGDASFDFLLKQGITKECTTDYMNKKAKEEGKEIKKLEEDDDEVANEQNEG", "text": "FUNCTION: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron- containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family."}
{"protein": "MAQRFITLILLLCSVLLAPHSAQSSLFGENASFGTKNSQSRFIPVDQAFAFDFHQQGDQLNLSWQIHPGYYLYRQQIKIVPQQAALGAFTLPEGITHHDEFYGEVEIFKQQLTLKIPITQAAEQASVSVTYQGCAEAGFCYPPETRVIPLDVVVAASTASGTAAVNSSATVNPPATTQPEGDATPVPSTLPFSPLWALLIGIGIAFTPCVLPMYPLISAVILGREKPHSQRRILILAVVYVQGMALTYTLLGLVVAAAGLQFQAALQHPYVLIGLSVLFVLLALSMFGLYSLQLPSSLQTRLTQWSNSQRGGSLAGVFAMGALAGLICSPCTTAPLSAILLYIAQSGNMLAGGGTLYLYALGMGIPLVVVTLFGNKLIPRSGPWMQYVKEAFGFVILALPVFLLERVLGDVWGLRLWSLLAVAFFGWAFVLSLKAHAGWVRVCQLLLLAALLIVARPLQDWAFNGNTQQNAVKHINFQPVANLPQLQAVLAQAQGKPVMLDLYADWCVACKEFEKYTFSDDKVQRQLANTLLLQADVTANNAEHATLLKKFNVLGLPTILFFDSQGNEITAARVTGFMDAAQFLQHLQNTPAVTK", "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": "MTDYVTDIAVIGAGPVGIFTVFQAGMLKMRCCVIDALSEIGGQCLALYPEKPIYDIPGYPVINGKELIDSLKKQSEPFNPQYLLGQVAEKIEDYSDYFLIRTTTGIVVQSKVIIIAAGAGAFGPNRLPIDNILDYENKSVFYQVRKVSDFCDKNIMIAGGGDSAADWAVELSKVAKQLYVVHRRKNFRCAPNTALQMDNLSQSGKIKIIVPYQVKKLCGENGKLHSVIVKNITNHEEMALQVDYLFPFFGTSANLGPILNWGMEVKNYQILVNAETCLTNRNRIYAVGDIATYPGKLKLILTGFSEAAMACHHIYHVIYPNSPLNFQYSTSKGIPENC", "text": "SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family."}
{"protein": "MNRVVVGLQWGDEGKGKVVTYLSRYHDIVARFSGGANAGHTVNYGDFKVIHHLLPSADFTKNRGIAIGSGVLLDPQVLTEELRELKEKFPDYSGEIFISESAHVVLPVHKEMDRIIDEVLKIGTTKRGIGPACADRVMRVNVRVAELGNEEKLRYFLEKNLSLKKIYGVDFDAEKMMGDLSTFYETIKDFVVSPVQLKRILEEKSVLFEGTQGVLLDLDVGTYPYVTSMNCSSSGVSAGMGFPVEVDEVLGVFKAYTTRVGEGPFPTELTGEEGEKLRKAGHEYGSTTGRPRRCGWLDLPLLRYAIEISGVDSLVMTKADVLNGFEKIKVCVRYSDGRDLVSLRDLEKKEPVYEVFDGWKSLEDKNFERFVDFIERETGRPVRYISTGEKLEDIVEV", "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": "MYIPSARTAIVQDDKGGLKIDRNAPMPQPRPNELLVQVKAVAINPCDHKMYERFPTPGAVDGCDFAGIVVQLGSDVKTFQIGDRVCGAVHGSNPSRPESGTFAEYTVSDGEFTLKLPPNLSFREAMGLGTTGLSTIGMAIYKGLMLPGSPLEPAEKPRTVLVHGASSSVGTMALQLIRLMGHIPIATCSPRNFELVKKYGAEEVFDYNDPECGQQIKQYTGNTLAYIIDPFTDVKSVALCYEAMGRAGGRYACLEMYPEFALERRSIKVFFALGMALLGHSLDLAYGYERDEDPEMRSFGIGWYKVLQELLYQGKLRPHPLRELEGGFEGILKGVQMVKNKEVSGQKLVVSLE", "text": "FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars (PubMed:18433432). The first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone (PubMed:29142718). The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor (PubMed:29142718). Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 (PubMed:29142718). Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds (PubMed:31644300). Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars (PubMed:18433432). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MGQKIHPVGFRLGITKDHKSCWYADPKRYPELLQEDHKIRQYIEKTLNNAGISDIRIERKAEQIELGIHTARPGVVVGRGGSGIEQLREGLQKLLGSARQIRVNVIEVPNADADAALMAEYIGQQLERRVSFRRVVRQALQRAERAEVKGIKIQVSGRLNGAEIARTEWVREGRVPLHTLRADIDYAYRTALTTYGILGIKVWIFKGEVIPGQEAAIVAPPSQPRRKSRRQQFDDRSQDG", "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": "MSVANSRTAVYPGTFDPITNGHIDLVNRAAPLFERVVVGVAYSPSKGPALPLERRVELAQEALAAHANVEVRGFDTLLAHFVRDMGAGVLLRGLRAVSDFEYEFQMASMNRHLIPEVETLFLTPAEQYSFISSSLVREIARLGGDVSGFVPASVVDALRQVRESRAQV", "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": "MSEQSQLDDSTIDKLIPQIFNEMRSNLNNTTNKFPKSTGGGASDNISANSNSIRSFNSITTQSLLKESESLDKITAMIKNVTAALKNNLPVYVNQVHEVCKSTNSILDSWINIHSQAGYIHKLMSDQTYLKLINDRLHNENVNTNDEDGSTLHNVIALKKKEILDLRQKLENRKGEKDAAPAKPPNQGLNPRYGVQSGRRPVPSAGISNNGRVRKTHVPASKRPSGIPRVTNRWTKPTASSSRKMFR", "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. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle pole Chromosome, centromere, kinetochore Note=Associates with the mitotic spindle and the kinetochore. SIMILARITY: Belongs to the DASH complex DUO1 family."}
{"protein": "MEEGKRWIVVPIWRVPGRMERWHSLVKYLKYRTKDLEKVCYVPHHKVGWAWWTCSRVIFPLKENSHLEIQAYWNLTPEKGWLSSHSVRITWYTEKFWTDVTPDCADTLIHSTYFSCFTAGEVRRAIRGEKLLSCCKYPRAHRSQVPSLQFLALVVVQQNDRSQGNSATRKQRRGDYRRGLRMARQDSRGYKQRGSESPPTRAHFPGLAEVLEILA", "text": "FUNCTION: Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity). SUBCELLULAR LOCATION: Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Virion Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor (By similarity). SIMILARITY: Belongs to the primate lentivirus group Vif protein family."}
{"protein": "MQRHMLKSKIHRAAVTHCELHYEGSCAIDEDLLEAAGLIENERIDIWNINNGERFSTYAIKGERGSGMISLNGSAARRAQLGDLVIIAAFAMVDEAELQAGWKPKLVFIDEGNKIKGHRDHVPTQSWT", "text": "FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family."}
{"protein": "MFLAQEIIRKKRNAEALSKEEIQFFVKGITDNTVSEGQIAALGMAVYFNDMNMDERIALTTSMRDSGTVLDWQSLDLNGPIIDKHSTGGVGDVISLMLGPMAAACGGYVPMISGRGLGHTGGTLDKFDAIPGYQTEPDSALFRKVVKEAGVAIIGQTGDLVPADKRFYSIRDNTATVESISLITASILSKKLAAGLDALAMDVKVGSGAFMPTYEASEELARSITAVANGAGTKTTALLTDMNQVLASCAGNAVEVKEAIDFLTGRYRNPRLYEVTMGLCAEMLMLGGIASTETQAREKLNAVLDNGKAAEIFGRMISGLGGPTDFVENPGLYLPESKIIRPVYAEQTGFATSMDTRELGLAVVTLGGGRRKPGDALDYSVGLTQVCALGDEISKDKPIAMIHAQTETAFAEAERAVRKAIHIGDSRPEKTPEIYRYIRASDL", "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": "MPVINTHQNIAAFLDMLAVSEGTANHPLTKNRGYDVIVTGLDGKPEIFTDYSDHPFAHGRPAKVFNRRGEKSTASGRYQQLYLFWPHYRKQLALPDFSPLSQDRLAIQLIRERGALDDIRAGRIERAISRCRNIWASLPGAGYGQREHSLEKLVTVWRTAGGVPA", "text": "FUNCTION: Endolysin with transglycosylase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer. SUBCELLULAR LOCATION: Host cytoplasm Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. SIMILARITY: Belongs to the glycosyl hydrolase 24 family."}
{"protein": "MEKIKVREIFNNAYSVDFGDGLKRIATKSLVPGKRVYGEKLVYSDNIEYRVWNPNKSKLGAAIINGLKKMPIKKGTKVLYLGASAGTTPSHVADIAETSLVYALEFAPRIMREFIDSCNERKNLIPVLGDANRPQDYSNIVEKVDVIFEDVAQPNQAEILVKNAKWFLKENGYAMISIKARSVDVTKNPREIFAEQKKILIEGGFEIVDEVNIEPFEKDHMMMVGIWKGN", "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": "MLSGLVIVDKPQGWTSHDVVGRMRRLAGTRKVGHAGTLDPMATGVLVLGINKATRLLTYIVGTSKTYTATIRLGETTITDDAEGEVTEARTAAHITDDAVAVGVAALTGPIQQVPSSVSAIKVNGERSYARVRSGEEVKLAARPVTIHRFDVHSITRIDGGRVVDVDVTVECSSGTYIRALARDLGNALGIGGHLTALRRTQVGPYSLDQARTLEELAEELEVLEMSLAARSLMPNRELSEQETTEISFGRRIAAGPGAGTPDAATAEKPAAAFAPSGELVALLADTGSFAKPVLVFAPGTGTGTGTGQAK", "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": "MSAKSRILVLNGPNINLLGLREPGHYGHQTLPQIVDTLTQQAQTAGIELEHLQSNREYELIEAIHAAHGNVDFIIINPAAFTHTSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKALGVICGLGAQGYEFALSAAIARLQAK", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
{"protein": "MALYEVYSHPALLRYRSSICSKATLFILIVLLLTYIPPLLVAFRSYGFWLKTSTYEEQPNVRFQYDVLLIALSSTTGNYLAWSTYPGFNNLVGDKLRLPHISAREEDRNQDGKMDLLNFQLELPLQPTDNIYGVQLILTFSYQLSKMSTFIMQSMALIQYSSPIPGSQLYMNGDLKLQQRQPLNHRGLDTTYNVSVINRSSPFASTYALTNIISSYQERNVTTVLNAPNPLWIVGRAASDPFVIKAVIRYPVESISYVPGFWEMLKYAWIQYVSILLIFLWVFERIKIFVFQNQVLTTVSGPIPSLYKSHQS", "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; SEPT2 is required for localization to the transition zone. SIMILARITY: Belongs to the TMEM231 family."}
{"protein": "MSRLAKRHPDLLSCNFNQDYSCIAVGHKKGYTILNCDPFGKVHSNNDQGATGIVEMLFCTSLVALVGAAENQPSNSPRKLQIVNTKRQSTICELIFPTSVLAVKMNRKRLIVVLENEIYIYDISTMKLLHTIETGPNPNAVCALSSSSERSYLAYPSPVPSASSTPLSSSAIPAPPPAPTTGDVLLFDTISLTALNVIQAHKTPIAALALNSTGTMLATASDKGTVVRVFSVPDAKKLWQFRRGSSSARIFSINFNLMSTLLAVSSDTSTIHIYRLASSRKGGKDADDASTEEARSPTPSETPLASSPPLAGGKLDSHSAASSLRRRSYHLGKSFVGGVGGYLPKSVSEMWEPQRDFAFIKLRGNHGRTVVAMSATVPQVMVISSEGLFQAYNIDLENGGECSLMKEFALLGSEDFGNGSNGI", "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": "MSGNEDFIYDDNSSSSISNQTDGGGGGGSSNNNSGGNANNNNNEGDREQDRYLPIANIIRIMKKALPNNAKVAKDAKETVQDCVSEFISFITSEASDKCQQEKRKTINGEDIIAAMVSLGFENYVEPLKVYLLKYRETEKNSNNKRSPKKSESSSPPESPPLAHLDNSINSGYQPPPPPQQQQQQPPQVQQQQQQQQQQQQQQLQQQQQLQQHQQQQLQPQQQQQHLQQHLQQQQPQQQQQPPQQQQQQLTTTTTTTSTNNQQYQQQPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQVQPPYILQQHNIQQPNVFLNQQAQQQQQQQQQQQQPMMNIQSHQQQFPQQHQIQQHLQQQHQHLQQIHNMQPPHQQMQFNQQFQMSQQIQMPQQFSNNNNNNNNNNNNNNNNNNNNNSNNNNNNNNNNNNNNNNPNNNINNNLNNSSNSLHNSGNSLHNSGNSGQIPPLYQQPYISTNPEYPSTS", "text": "FUNCTION: Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NFYB/HAP3 subunit family."}
{"protein": "MKRAVVVFSGGQDSTTCLAQARHQYDEVHCVTFDYGQRHRAEIDVARDLALKLGARAHKVLDVTLLNELAVSSLTRDSIPVPDYEPNADGIPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVNLGMAKDIRFETPLMWIDKAETWALADYWGQLDLVREETLTCYNGIKGDGCGHCAACNLRANGLNHYLSNKAAVMAAMKQKTGLR", "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": "MSSMVTPQHAQELSTGARELGIDLSPAQHEQLLAYLALLIKWNKAYNLTAVRNPDEMVSRHLLDSLSVVPFIEGTRWIDVGSGGGMPGIPMAILFPERKVALLDSNGKKTRFQTQVKLELKLDNLEVIHSRAESYQPEVPFDGIISRAFSSLEDFTGWTRHMGDVNTRWLAMKGLHPDDELVALPSDFHLDSAHALTVPGCQGQRHLLILRRTA", "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": "MISSNDFRPGVSIELDGAVWRVVEFLHVKPGKGSAFVRTKLKNVQTGNVIERTFRAGETVPQATLEKRTMQHTYKDGEDYVFMDMESYEEARLTPAQVGDRAKYLKEGMEVNIVKWGEQVLEVELPNSVVLEVVQTDPGVKGDTATGGSKPAIVETGAQVMVPLFISVGERIRIDTRSDTYLGRE", "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": "MYHLYSHNDLDGVGCGIVAKLAFGKDVEIRYNSVNGLNAQVQYFLEKAKESNRQDALFITDLAVNEENEERLNEYVHAGGKVKLIDHHKTALHLNEHEWGFVQVEYDDGRLTSATSLLYGYLIENGFMKPTNALDQFTELVRQYDTWEWERYDQKQAKRLNDLFFLLSIDEFEAKMIQRLSTHDEFFFDDFEEKLLDLEDEKIERYLRRKKREMVQTFVHEHCVGIVHAESYHSELGNRLGKDNPHLDYIAILSMGSKRVSLRTIHDYIDVSEIAGRYGGGGHAKASGCSITDEVYELFVAEAFRIDPVRPDAFRNIYNLKGSANGSLYENRAQMRFFLFPLDNEWNIQINGETQDETFAAFEEAEWFIKRNYAASLVRDEVFVAFLAENLKLANQHRK", "text": "FUNCTION: Degrades RNA oligonucleotides with a length of 5 nucleotides in a 3'- to 5'-direction. Less active on shorter RNA oligonucleotides and on those with a length of 24 nucleotides. Prefers RNA oligonucleotides containing adenines rather than cytosines. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MASTLSPSITPQTEEPPVVPVRIQNAADISVIVIYFIVVLAVGLWSMVRSNRGTVGGFFLAGHDMAWWPMGASLFASNIGSNHFVGLAGTGAASGIAIAAVEWNALLMVLVLGWVFLPIYIKAGVLTMPEYLRKRFGGKRLQIYLSVLSLFIMVALQTSSIIFSGAIFIQLALGLNLYLAVFILLAITAFYTVAGGLASVIYTDSVQTFIMLLGSLILMGFAFAEVGGYESFTEKYMNAIPSVVEGDNLTISPKCYTPQPDSFHVFRDPVTGDIPWPGLIFGMTILAIWYWCADQVIVQRCLCGKNMSHVKAACILCGYLKLLPMFLMVMPGMISRILYTDKVACVVPSECEKQCGTAVGCTNYAYPTLVLELMPDGLRGLMLSVMLASLMSSLTSIFNSASTLFTIDLYTKIRKKASERELMIAGRIFGMVLIAVSILWVPLVQVSQNGQLFHYIGSVSSYLGPPLGAVFMLAIFFKRVNEQGAFWGLMVGLVVGLIRLIAEFVYGTGSCVAPSNCPKIICGVHYMYFAIILFFVSIIVILGVSFLTEPIPDVHLYRLCWSLWNNTEERIDLDAEELETQEEAGGALEEDSEQSRGCLKRACCLLCGLQNTGPKLTKEEEAALRQKFSDTSEKPLWRTVMNINAVLLLGVAVFVHAYFA", "text": "FUNCTION: Low-affinity sodium/D-glucose symporter (Probable) (PubMed:22301059). Generates D-glucose-induced depolarization in a pH- independent manner (PubMed:22301059). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
{"protein": "MLSNARIIAAGCIAAGSLVAAGPCDIYSSGGTPCVAAHSTTRALFSAYTGPLYQVKRGSDGATTAISPLSSGVANAAAQDAFCAGTTCLITIIYDQSGRGNHLTQAPPGGFSGPESNGYDNLASAIGAPVTLNGQKAYGVFVSPGTGYRNNAASGTAKGDAAEGMYAVLDGTHYNGACCFDYGNAETNSRDTGNGHMEAIYFGDSTVWGTGSGKGPWIMADLENGLFSGSSPGNNAGDPSISYRFVTAAIKGQPNQWAIRGGNAASGSLSTFYSGARPQVSGYNPMSKEGAIILGIGGDNSNGAQGTFYEGVMTSGYPSDATENSVQANIVAARYAVAPLTSGPALTVGSSISLRATTACCTTRYIAHSGSTVNTQVVSSSSATALKQQASWTVRAGLANNACFSFESRDTSGSYIRHSNFGLVLNANDGSKLFAEDATFCTQAGINGQGSSIRSWSYPTRYFRHYNNTLYIASNGGVHVFDATAAFNDDVSFVVSGGFA", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 54 family."}
{"protein": "MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI", "text": "FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tropomyosin family."}
{"protein": "MLTFVGLGLYDLGDISVKGLEYVRNADTVFLEAYTSRLMGTDTAAMEAFFEKDIRVLGREDVEQTPREILECAAAGRVAFLTGGDPMVSTTHADLRMRAAAAGIETSIIHASSISSAVSGLSGLQNYRFGRSCSVPFPAKGWFPTAPIETIAANLALNLHTLVFLDIQNDRYMRVPEAIAVLEEMAEKRGIEPPALYVGIARAGSERPVVAAGAGANLKEMDFGPPLHILAVPADLHPMEREYLETFAGL", "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": "MESDLTTEHHLPFIRIHKNGRVERLSGNDIKPTSLNPQNDVVSKDVMYSSDHNLSVRMFLPNKSRKLDTAGNKIPLLIYFHGGAYIIQSPFSPVYHNYLTEVVITANCLAVSVQYRLAPEHPVPAAYDDSWSAIQWIFSHSDDWINEYADFDRVFIAGDSAGANISHHMGIRAGKEKLSPTIKGIVMVHPGFWGKEPIDEHDVQDGEVRNKIAYIWENIVSPNSVDGVNDPWFNVVGSGSDVSEMGCEKVLVAVAGKDVFWRQGLAYAAKLEKSQWKGSVEVIEEEEEGHCFHLHNHNSQNASKLMQKFLEFIIS", "text": "FUNCTION: Carboxylesterase acting on esters with varying acyl chain length. SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family."}
{"protein": "MEEEKYLPELMAEKDSLDPSFVHAMRLLDEEIVKFQDSEGNKEDGEKKYLDIISNKNIKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKIKEEELRKSDEAKHAHLSDELHVLLEVFAPPGEAYSRMSHALEEIKKFLVPDYNDEIRQEQLRELSYLNGSDDSERGKGTRGRGIRVPSTPSRNRGGVISPAFPGRGASATRGAPITRGTISTVARGIPTPRAKAAPTTPGYRLPPPLTIETYDDYGYDDGFGEDYDEQSYDIYENNYNSQTQSVSEYYDYEHGTNEESYNHYEQEEWSKSRSTLKAPLQRPARAGYREHPYGRY", "text": "FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the KHDRBS family."}
{"protein": "VIGGAEENINEHRSL", "text": "FUNCTION: Snake venom serine protease that potently induces platelet aggregation. Its aggregatory activity is partially inhibited by monoclonal antibodies against GPIb and the thrombin receptor. Its ability to induce intracellular Ca(2+) release is blocked by pretreating platelets with thrombin. Hydrolyzes thrombin chromogenic substrate CBS 34.47, but shows very weak coagulant activity. Can hydrolyze fibrinogen alpha-chains. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MSSISQKVVIGLNKAAANNNLQNLDRRGFKTRCVSSSKAASCLRASCSLQLDVKPVQEGRRSGNYQPSIWDFNYVQSLNTPYKEERYLTRHAELIVQVKPLLEKKMEPAQQLELIDDLNNLGLSYFFQDRIKQILSFIYDENQCFHSNINDQAEKRDLYFTALGFRLLRQHGFDVSQEVFDCFKNDNGSDFKASLSDNTKGLLQLYEASFLVREGEDTLEQARQFATKFLRRKLDEIDDNHLLSCIHHSLEIPLHWRIQRLEARWFLDAYATRHDMNPVILELAKLDFNIIQATHQEELKDVSRWWQNTRLAEKLPFVRDRLVESYFWAIALFEPHQYGYQRRVAAKIITLATSIDDVYDIYGTLDELQLFTDNFRRWDTESLGRLPYSMQLFYMVIHNFVSELAYEILKEKGFIVIPYLQRSWVDLAESFLKEANWYYSGYTPSLEEYIDNGSISIGAVAVLSQVYFTLANSIEKPKIESMYKYHHILRLSGLLVRLHDDLGTSLFEKKRGDVPKAVEICMKERNVTEEEAEEHVKYLIREAWKEMNTATTAAGCPFMDELNVAAANLGRAAQFVYLDGDGHGVQHSKIHQQMGGLMFEPYV", "text": "FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products (PubMed:17187833). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into geraniol (PubMed:17187833). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
{"protein": "MNGMWALLRLASPQLPIGGYSYSQGLELAIERGLVCDPPTARRWLEDQLLLNLARFEAPLLLAQCRAAADGDWTALEALAERHRASRETRELHLESRQMGFSLRQLLEDLPELDEPSRAVFARLVEPGLAPAWALAARAWGIAPEDALAAWLWSWLENQLAVLMKSLPLGQQAAQRLTSALLPALGQAQRTACAHAPDDWGTVAFGLTLASMAHERQYSRLFRS", "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": "MATCPSIFDALVIGAGPAGLSAALALGRVMRTAAIFDTGVFRNAPANHMHTVPTWDHQSPVAYRQQCITELRQRYNGTIHFANTGVASVKAGKDSDYVVTDEAGKTWMGRKVILATGVKDVMPDVKGYAQAWGRYIFHCLFCHGFEQRGSESAGLLVLDKTILSTEIEIAVHFGHLALQFAKKITVFLDGHVEFLEDPRIKGLEAQGFLINPKPISKITYAADPEPGFATVHLEDGSEENMSFLVHRPRTLLAGDFANQLGLELTEAGDVKTTPPFYETSVKGVFAAGDCAVPLKQVVWAVSTGVSAGSGVNFQCLGADMAARSKLS", "text": "FUNCTION: Thioredoxin reductase; 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 class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MVHFTAEEKAAITGLWGKVNVEEAGGEALGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSFGEAIKNLDNLKGAFAKLSELHCDKLHVDPENFRLLGNVIVIILATHFGREFTPDVQAAWQKLVSGVATALAHKYH", "text": "FUNCTION: Beta-type chain found in early embryos. SIMILARITY: Belongs to the globin family."}
{"protein": "MAKYTNDELLEAFGEMTLVELSEFVKAFEEKFDVEAAAPVAAVAAVAGAAAPAEEEKDEFDVILSAVGDKKIQVIKAVRAITNLGLAEAKALVDGAPKAVLEKAKKEDAEKAKAQLEEAGASVELK", "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": "MAAVMSAQAMADAVRVVRASISELGKSAKKSDAFSARDLKSRSGFTESVDRLGLVNLQVQARKKRVRGLRLVPTRVVSAIEGSNSTTADAPVDEDVLAWTKAYRAENSTAITRDETLKSNAQSALQWKCVETQVEGERLHYGRFAVSPFRSGQANTVGVSMQKALLGEVEGAAVSCATFKNVKSEYAAMKGVEETPMDILVNLKELVIRSDSDEPQKAIISAIGPGPVTAGDIVLPPSLEVTDPTQHIAYLTKEVSLDIELDVEKGCGYRMGDHTKSGDGRFYIDSVFMPVRNANYSVHSYESEPDVTQEILFLEIWTNGSITPEEALHEAARCLIDLFLPFLHPKKKEVTNSATKMHKSFTMSQFNSSAEMSAKEVDLRHVYVDQLRIPSKAYNSLKRANINTVSDLLDYTQDDLLSIPNFGRKSVDDILEALQAQFSIDLPENNPLCN", "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": "MPASRRVLIAGNWKMNGLKSSLAEIEALAAGYDGDLKAKLDLLVCPPATLLISAAERLAGSGVQLGGQNCHPAPAGAHTGGISAEMLKDAGVTSVIVGHSERRTNLSESDAVVMAKVKAAWCFGLLPIVCVGETAEERDAGEAVGVVTRQVHQSLPEGCTASNLVIAYEPVWAIGTGRTPTPEDVANIHGTIRSVLRSQFGAEADGIRILYGGSVKPDNAATLMAVADVDGALVGGASLKAADFLAIARATPAR", "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": "MTDLEKPNLAGHMFDVGLIGGGISGLAAAKLLSEYKINVLVLEARDRVGGRTYTVRNEHVKWVDVGGAYVGPTQNRILRLSKELGIETYKVNVNERLVQYVKGKTYPFRGAFPPVWNPLAYLDYNNLWRTMDEMGKEIPVDAPWQARHAQEWDKMTMKDLIDKICWTKTAREFAYLFVNINVTSEPHEVSALWFLWYVRQCGGTARIFSVTNGGQERKFVGGSGQVSEQIMGLLGDKVKLSSPVTYIDQTDDNIIVETLNHEHYECKYVISAIPPILTAKIHFKPELPPERNQLIQRLPMGAVIKCMVYYKEAFWKKKDYCGCMIIEDEEAPIAITLDDTKPDGSLPAIMGFILARKADRQAKLHKDIRKRKICELYAKVLGSQEALYPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIYFAGTETATQWSGYMEGAVEAGERAAREVLNALGKVAKKDIWVEEPESKDVPAIEITHTFLERNLPSVPGLLKITGVSTSVALLCFVLYKIKKLPC", "text": "FUNCTION: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:18391214, PubMed:9162023). Preferentially oxidizes serotonin (PubMed:20493079). Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (PubMed:18391214). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the flavin monoamine oxidase family."}
{"protein": "MPAGRRGPAAQSARRPPPLLPLLLLLCVLGAPRAGSGAHTAVISPQDPTLLIGSSLLATCSVHGDPPGATAEGLYWTLNGRRLPPELSRVLNASTLALALANLNGSRQRSGDNLVCHARDGSILAGSCLYVGLPPEKPVNISCWSKNMKDLTCRWTPGAHGETFLHTNYSLKYKLRWYGQDNTCEEYHTVGPHSCHIPKDLALFTPYEIWVEATNRLGSARSDVLTLDILDVVTTDPPPDVHVSRVGGLEDQLSVRWVSPPALKDFLFQAKYQIRYRVEDSVDWKVVDDVSNQTSCRLAGLKPGTVYFVQVRCNPFGIYGSKKAGIWSEWSHPTAASTPRSERPGPGGGACEPRGGEPSSGPVRRELKQFLGWLKKHAYCSNLSFRLYDQWRAWMQKSHKTRNQDEGILPSGRRGTARGPAR", "text": "FUNCTION: In complex with CLCF1, forms a heterodimeric neurotropic cytokine that plays a crucial role during neuronal development (Probable). May also play a regulatory role in the immune system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type I cytokine receptor family. Type 3 subfamily."}
{"protein": "MVWCCRVLLRKYGNFVDNLRIYVKGGTGGMGLPRLGGQGGNGGDVCLLAKKGVTLKNIKDKYPHKRFIGGVGVNSSVRALKGLAGEVCQVEVPPGIVITNEHGVKIGELDKEGDEIRVARGGHGGIFKTDFLPSKGQTRVIHLDLKLISDVGLVGFPNAGKSSLLGKISHAKPQVADYAFTTVKPELGKIMYPDYKQVSVADLPGLIEGAHYNRGMGHKFLKHIERTKQLLFVVDIAGFQLSAITPCRSAFETVQLLILELQLYKEELLDKPAVLAVNKMDLPNADEKLGELLKQLENPTGNLHSLPDELVPERQIEFKHIVPVSAATGQGLEDLIGCIRKTIDEQADVQIQELAQERLQSLHKETPRTVKRNFQTSPRHKHH", "text": "FUNCTION: May be involved in the ribosome maturation process. SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Found in the dense fibrillar compartment region of the nucleolus. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family."}
{"protein": "MDISGMQINEVQSKLKEYYNVLKMARKPDWEEFSMTAKVALAVMFIVGFVGFVIYILMEILPGALK", "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": "MKVLIQRVTQAAVDVDSITIGQIDAGILALVGVEKQDNRETLGRMAQKLLKYRIFPDSEGKMNLSLTDTGGGLLVVSQFTLAADTRKGLRPSFSSSAPPDLARSLFDEFVAALRAQHPNVETGRFGADMKVRLINDGPVTFMLES", "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": "MAATGVLAEIIDGDVYKYYADGEWKKSTSGKSVAIINPTTRKPQYKVQACSQEEVNKVMDSAKSAQKSWAKTPLWKRAELLHKAAAILKEHKAAIAECLVKEIAKPAKDAVTEVVRSGDLVSYCAEEGVRILGEGKFLVSDSFPGNERTKYCLTSKIPLGVILAIPPFNYPVNLAVSKIAPALIAGNSIVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKSGMIPLQMELGGKDACIVLEDADLDLVAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVKVKVAKLSVGPPEDDSDITPVVSESSANFIEGLVNDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTKDINKAIMISDAMESGTVQINSAPARGPDHFPFQGIKDSGIGSQGITNSINMMTKVKTTVINLPSPSYTMG", "text": "FUNCTION: Important as a means of generating NADPH for biosynthetic reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MDDTKTASPAPARAYETPPAERPITDAEAARAAALSANEHIKIASGYLRGTLADGLLKHATGAISEDDGQLVKFHGMYLQDDRDLRPERTRKKLEKAYSFMIRLRIAGGVVSPRQWLALDDIARTYANGTLRATTRQTFQYHGVIKSNLKRTLQAIDAVLLDTIAACGDVNRNVMAATNPAQTGAHAAAYRLAKDISDSLLPKTNAWREIWLDGERVAGGEDEAAEPVYGRTYLPRKFKTVVAVPPSNEVDVFAHDLGFIAILDKKNALKGWNVTVGGGMGMTHGEPDTFPRTADLLGFCEPADALKVAEAVMTVQRDWGNRKSRKNARLKYTIERYGLAAFRAEVERRVGKPLREPKPFQFTGNGDRYGWVEGEDGRHHLTLYVPSGRIRDVEGGPRYLSGLRRIAEIHEGDFRLTGNQNVIVANVPAGARAEIDRLVAEYGLTIGAGALRRNSLACVALPTCGLALAESERFMPDLLTRLEERLAAHGLRDEDITVRMTGCPNGCARPFIAEIGFVGRGPERYNVYLGAAFDGSRLSKLYADDVAAADIPALLDPLFAAYARERIPGERFGDFVIRAGYVARTVNGPDFHDRTGPLRAVA", "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": "MLRRKPTRLELKLDDTEEFESVKKELESRKKQRDEVDVVGVATSSEMSGAAGGTADGKTREQMIHERIGYKPHPKPNTLPSLFGNLQF", "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). May recruit the E2 ubiquitin-conjugating enzymes to the complex. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CDC26 family."}
{"protein": "MKPSERICAALDFPTFAAAEPFARAVAPEVGLLKVGLELFAAEGPAAVRAAARLGRPVFLDLKLHDIPNTVEGAARSAAASGAALLTVHAAGGAEMVKAAVRGAGPGVRVLAVTVLTSLDAAALDAVGLAGPPEAAVVRLARLAVGAGAGGIVCSPHEVAAVRAAVGPGPLLVVPGVRPAGAAKGDQARVATPAEAVRAGADVIVVGRPLRDAPDPAAAARAIAAGL", "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": "MYAVIKTGGKQHRVSEGDLLTVEKLAGSKGDSVVFDDVLMVAKEGEIRVGKPVLEGAKVVGEIVAQVKGPKIYVFHMKKRKGFHKKTGHRQQLTRMRIKEISI", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MWKVSALLFVLGSASLWVLAEGASTGQPEDDTETTGLEGGVAMPGAEDDVVTPGTSEDRYKSGLTTLVATSVNSVTGIRIEDLPTSESTVHAQEQSPSATASNVATSHSTEKVDGDTQTTVEKDGLSTVTLVGIIVGVLLAIGFIGAIIVVVMRKMSGRYSP", "text": "FUNCTION: Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation (PubMed:14522983, PubMed:15231832, PubMed:17616532, PubMed:18215137, PubMed:17222411). Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN (PubMed:18541721). Through MSN or EZR interaction promotes epithelial- mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness (PubMed:17046996, PubMed:21376833). Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (PubMed:20962267). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (By similarity). Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix (PubMed:19268462). In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion (PubMed:15515019). Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (PubMed:25486435). Required for normal lung cell proliferation and alveolus formation at birth (By similarity). Does not function as a water channel or as a regulator of aquaporin-type water channels (PubMed:9651190). Does not have any effect on folic acid or amino acid transport (By similarity). SUBCELLULAR LOCATION: [29kDa cytosolic podoplanin intracellular domain]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Podoplanin]: Membrane; Single-pass type I membrane protein Cell projection, lamellipodium membrane; Single-pass type I membrane protein Cell projection, filopodium membrane; Single- pass type I membrane protein Cell projection, microvillus membrane; Single- pass type I membrane protein Cell projection, ruffle membrane; Single-pass type I membrane protein Membrane raft Apical cell membrane Basolateral cell membrane Cell projection, invadopodium Note=Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles (By similarity). Association to the lipid rafts is required for PDPN-induced epithelial to mesenchymal transition (EMT) (PubMed:21376833). Colocalizes with CD9 in tetraspanin microdomains (PubMed:18541721). Localized at invadopodium adhesion rings in tumor cell. Association to the lipid rafts is essential for PDPN recruitment to invadopodia and ECM degradation (PubMed:25486435). SIMILARITY: Belongs to the podoplanin family."}
{"protein": "MGSKTKGCCGWLIVALVASLVATAAVVAIMKKKVGGGSGRKLKPLPVPGPPGAIDSKYGDALGVALQFFQVQKAGKLENNQIPWRGDSALDDGKPAGLDLSKGMYDAGDHIKFSFPMAFTATVLSWSILEYGDQMSATKQLDPALDALRWITDFLVNAHPSDNVFYIQVGDPDLDHNCWERPETMSEKRPLTQINTKSPGSDVAAEAAAAMASASIVFKSRDTTYSDSLLQHAQKLFTFADTYKGLASDTYPKLQNYYNSTGYQDELLWAASWLYHATGDQTYLSYVTVENGKAFADWGRPTWFSWDDKLAGTQVLLSRLNFFGSKQTSNAENMGLKMYRDTAEAVICGLLPDSPSATASRTGGGLVWISGWNSLQHATNAAFLAVVYSDYMLTSQTAAVQCSGKYYSPTDIRNFAISQANYILGDNPMKLSYLVGYGSSYPQQVHHRGASIPADAKTGCKGFQYLHSTSPNPNVAMGALVGGPFQNDTFVDSRDNAVQTESSTYNSGTLVGLLSGLVTTSSVAQSFT", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family."}
{"protein": "MGRLLDTIDSPADLKKVPVEQLPALCQEIRELIIQTCARNGGHLGSSLGAVEINVALHHVFASPQDKLVWDVGHQAYAHKLLTGRRDAFRTIRTEGGLAGFPERHESAHDAFGVGHASTAISAALGMIEAKRVTGEPGKVVAVVGDGAMTGGVAFEGLNQAGYLGRNLLVVLNDNEMSISPNVGALSEWFSKKFASRTYNRWRRQVKEFLESVPKGPEAIGIIRHGINATKALVTPGILFEGLGFHYVGPVDGHDVKGLVETFQKLAVFDGPVLLHAITTKGKGYHPAESDKATRGHGLSFFDVATGKPVKKSPGAKAYTDLFAEALCEEMEHDPRVVAITAAMLEGTGLIKAKQRFPDRTYDVGIAEQHAVTFAAGLACEGIRPVVAIYSTFLQRAYDQIIHDVALQKLPVTFALDRGGLVGADGKTHQGAFDLAYLRCVPGLVLMAPSDENELRHMLHTSLQHDGPAALRYPRGAGEGVPLEPARVLEIGKGRLVRNVPGKPDVCVVAAGTTLKAALAAAEALAAEGVAVTVVDPRFVKPLDEALICAEAARAKRVVTVEEGCLAGGFGTACLEAFERHGLLEAGLGVRRLGIPDEFITHAEQAKQRAWVGIDAEAIAAACRALVGDRKARGVA", "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": "MAFLKKSLLLVLFLGLVSLSICEEEKRENEDEEEQEDDEQSEMKRGMWSKIKEAGKAAAKAAAKAAGKAALDVVSGAIGEQ", "text": "FUNCTION: Has antibacterial activity against Gram-positive bacterium M.luteus NCT C2665 and against Gram-negative bacterium E.coli K12D31. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MFVEKVLERTTNLELCSILILLVISLSIYTFYATLNTYLRSVLLSLRLTGPPSLPFLGNCMLVTDKDLMRRCAGKAFDLYGSLVRIWVLLFPFFAVLEPEDLQVILSSKKHTNKVFFYRLMHNFLGDGLITSSGSKWSNHRRLIQPAFHHNLLEKFIDTFVDASQSLYENLDAEAVGTEINIAKYVNNCVLDILNEAVLGVPIKKRGQDVAMMEDSPFRQGKIMMPARFTQPWLLLDGIYHWTKMANDELNQKKRLNDFTRKMIQRRRQIQNNNNGNSERKCLLDHMIEISESNRDFTEEDIVNEACTFMLAGQDSVGAAVAFTLFLLTQNPECQDRCVLELATIFEDSNRAPTMTDLHEMRYMEMCIKEALRLYPSVPLIARKLGEEVRLAKHTLPAGSNVFICPYATHRLAHIYPDPEKFQPERFSPENSENRHPYAFLPFSAGPRYCIGNRFAIMEIKTIVSRLLRSYQLLPVTGKTTIAATFRITLRASGGLWVRLKERDHPLIAH", "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": "MSNQKALVIFSGGQDSTTCLIQAIQTYGRENVQAITFRYGQRHAVELERAEWIAQDLGVSQTVLDLSLMRQITHNALMDETAAIETAAIETADNGVPNTFVDGRNALFLLYAAIFAKGQGIRHIIAGVCETDFSGYPDCRGVFVKSMNVTLNLAMDYDFQIHTPLMYLTKAQTWALADEMGVLDYIREQTHTCYKGIVGGCRECPSCILRERGLAECLESKKAV", "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": "MTQDWDAGRLDSDLEGAAFDTLAVRAGQRRTPEGEHGEALFTTSSYVFRTAADAAARFAGEVPGNVYSRYTNPTVRTFEERIAALEGAEQAVATASGMSAILALVMSLCSSGDHVLVSRSVFGSTISLFDKYFKRFGIQVDYPPLSDLAAWEAACKPNTKLFFVESPSNPLAELVDIAALAEIAHAKGALLAVDNCFCTPALQQPLKLGADVVIHSATKYIDGQGRGMGGVVAGRGEQMKEVVGFLRTAGPTLSPFNAWLFLKGLETLRIRMQAHSASALALAEWLERQPGIERVYYAGLPSHPQHELARRQQSGFGAVVSFDVKGGRDAAWRFIDATRMVSITTNLGDTKTTIAHPATTSHGRLSPEDRARAGIGDSLIRVAVGLEDLDDLKADMARGLAAL", "text": "FUNCTION: Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. Cannot use the other activated form of L-homoserine, O-acetyl-L-homoserine, as a substrate. SIMILARITY: Belongs to the trans-sulfuration enzymes family. MetZ subfamily."}
{"protein": "MALSQATPFSATELLLASATFCLVFWVVKAWQPRVPKGLKSPPGPWSWPLIGHVLTLGKSPHLALSRLSQRYGDVLQIRIGCTPVLVLSGLDTIRQALVRQGDDFKGRPDLYSFTLVADGQSMTFNPDSGPVWAAQRRLAQNALNSFSVASDPASSSSCYLEMHVSKEAEALIGKFQELMAGSGRFDPYDHVVVSVAKVIGAMCFGQHFPQSSGEMVSLVRNTHDFVETASSGSPVDFFPILKYLPNPALQKYKSFNRRFLQFLWKMVQEHHQDFDKNRVQDIVGALFKHYEDNSRASGGLMPQKKTVNLVNDIFAAGFDPITTAISWSLLYLVTNPEIQRKIQQELDTVIGRARRPRLSDRSQLPYLEAFILETFRHSSFVPFTIPHSTIRDTTLNGFYIPKELCVFINQWQVNHDPKLWGDPSEFRPERFLTSHDTTISKTLSEKVMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPTYGLTMKPAPCEHVQARLRFPIK", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25- hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase- like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "WYSSMFAANIKEEPMSHHHHHSHHSHGHHHSNSNSNASSPRQSPLPSPNPPSSSNLHLEQYLKQQQQHQQQQQQPMDTPLPLTPPGLPNPMQIIMPANMRPATQPTPTIATPTTTSSAIVALQSNDKLQALTPPMDVTPPKSAAKSQQSWAEPEKDHDLMSNSSEDMKYMA", "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": "MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGIFFPQKISVIGNGVVVNPKSLVKELAYLHDEGVTTDNLRISDRAHVILPYHIQLDQLQEDAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDKDIFAERLRINLAEKNRLFEKMYDSTPLDFDAIFEEYYAYGQEIKQYVTDTSVILNDALDAGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPNKINKVVGVCKAYTSRVGDGPFPTELFDEVGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNSIDVLSGLDTVKICVAYDLDGKRIDYYPANLEQLKRCKPIYEELPGWQEDITGVRSLDELPENARNYVRRVGELVGVRISTFSVGPGREQTNILESVWASI", "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": "MTILRKSHPLLKMVNHAFIDLPAPSNISGWWNFGSLLGLCLIIQIASGLFLAMHYTSDTISAFSSVAHICRDVNYGWLIRYIHANGASLFFMCLYLHIGRGIYYGSYMYKETWNIGIMLLFLTMATAFMGYVLPWGQMSFWGATVITNLLSAIPYVGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIAATAMVHLLFLHETGSNNPLGIPSDSDKIPFHPYYTFKDFLGVIIILASFLTFVLFFPDLLGDPDNYSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVIALVLSILVLALFPLLHTANQRSMMFRPISQFLFWTLVSDLFILTWIGGQPVEPPFIIIGQIASILYFSIILVLLPIAGLIENKILKW", "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": "MTAPNRNTLWARAIADELAAAGVHAVCVCPGSRSTPLTVAVDAHDDLTVYSHLDERSAAFFALGRGKRTGAPTAVLTTSGTATANLHPAVMEAAQARIPLVVLTADRPPELRGSGANQTVDQEQLYGSAVRYYEDLPEPEVTARKLRSLRTSVCRAVGHTTGPKPGPVHLNVPFRKPLEPVSVPGDVPPSFDDDHPLAAAGRGGDTPFVSVHDGTTEPAGETAAALAAAATTAARPLVVAGPADGGAGITPDAAAALADATGAPIFADPLSGLRFGPHVGDAPVVGGYDGFLAADVPHPEFVLRFGASPTSKPLRKWLAASDARQVVVDPAGGWREAEFTATDVVAADPAATARAIAARADGTRSAWTDAVLDLEARYWAAVDDFQPAATLEGEIAATVAAGAPDPATVFVSNSMPIRDFDRFAAPRGADLAVLGNRGASGIDGVVSSALGAGSATADPVVGLVGDLAYFHDSNGLLALERCGVDATIVLVNNDGGSIFHMLPIEQFDPPFTGQFKTPHGLDFAPTADTYALSFARTDTVGEFRAAYRAALGDAGTHVIEVSTDAEASHRERERLADRVTGLSV", "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": "MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGEWPSNNTSAGVASSTDIKGKYVQSVEVKNGVVTATMASSNVNNEIKGKKLSLWAKRQDGSVKWFCGQPVKRNDTATTNDDVKADTAANGKQIDTKHLPSTCRDAASAG", "text": "FUNCTION: Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation as well as twitching motility. SUBCELLULAR LOCATION: Fimbrium. Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the N-Me-Phe pilin family."}
{"protein": "MTDIVVVRVKPGSRKGPLVETGSDAELTIYVRERAVDGKANEAAARLLAAHLQLPRSRVELVAGATSRLKRFRVER", "text": "SIMILARITY: Belongs to the UPF0235 family."}
{"protein": "MFFKIDLKNHPYLIRLKKQEE", "text": "FUNCTION: Binds directly to F-actin and induces actin filament bundling. May function as a regulator of actin filament organization. SIMILARITY: To yeast fimbrin."}
{"protein": "MAEKLKVDLVTPYKKILSEEVDEITATGALGEFSVLPGHAPFLTSLKIGELTYKKGGQFFHLAVNWGYFEVEDDKVTVLVETAERADEIDLERAKAALGRAEAALKGLSPEDKSYKTQEAALERALIRMQVAGKSTRK", "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": "MREEQPHLATTWAARGWVEEEGIGSATLGRLVRAWPRRAAVVNKADILDEWADYDTLVPDYPLEIVPFAEHPLFLAAEPHQRQRVLTGMWIGYNERVIATEQLIAEPAFDLVMHGVFPGSDDPLIRKSVQQAIVDESFHTYMHMLAIDRTRELRKISERPPQPELVTYRRLRRVLADMPEQWERDIAVLVWGAVAETCINALLALLARDATIQPMHSLITTLHLRDETAHGSIVVEVVRELYARMNEQQRRALVRCLPIALEAFAEQDLSALLLELNAAGIRGAEEIVGDLRSTAGGTRLVRDFSGARKMVEQLGLDDAVDFDFPERPDWSPHTPR", "text": "FUNCTION: Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:20798054, PubMed:18458342). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar- NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four- electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054). SIMILARITY: Belongs to the AurF N-oxygenase family."}
{"protein": "MNNAPHLYFAWQQLVEKSQLMLRLATEEQWDELITSEMAYVNAVQEIAHLTEEVAPSTTMQEQLRPMLRLILDNESKVKQLLQIRMDELAKLVGQSSVQKSVLSAYGDQGGFVLAPQDNLF", "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": "ETLMDTRTATAELGWTANPPSGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWTEAPYLKVDTIAADESFSQVDFGGRLMKGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFFKKCPSVVQNFAIFPETMTGAESTSLVTARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKAGYEPENNVACRACPAGTFKASQGAGLCARCPPNSRSSAEASPLCACRNGYFRADLDPPTAACTSVPSGPRNVISIVNETSIILEWNPPRETGGRDDVTYNIVCKKCRADRRACSRCDDNVEFVPRQLGLTETRVFISSLWAHTPYTFEIQAVNGVSNKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYELRYYEKLSRICTPDVSGTVGSRPAADHNEYNSSVARSQTNTARLEGLRPGMVYVVQVRARTVAGYGKYSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFIVSLVAISIVCSRKRAYSKEVVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNTRPRLAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTSVEDWLSAVKMSQYRDNFLSAGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMRVQMSQSPTSMA", "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 Cell projection, dendrite. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily."}
{"protein": "MSFIFDWIYSGFSSVLQFLGLYKKTGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHLQARRVWKNYLPAINGIVFLVDCADHERLLESKEELDSLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQTTGKGSVSLKELNARPLEVFMCSVLKRQGYGEGFRWMAQYID", "text": "FUNCTION: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex (By similarity). Synergizes with the cargo receptor SURF4 to mediate the export of lipoproteins from the endoplasmic reticulum, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Golgi apparatus, Golgi stack membrane; Peripheral membrane protein Note=Associated with the endoplasmic reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi region. SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family."}
{"protein": "QDTYLNAKKYIEFYLVVDNGMFXKYSXXFTV", "text": "FUNCTION: Snake venom zinc metalloprotease that has potent hemorrhagic activity, fibrinogenolytic activity on the alpha-subunit of human fibrinogen (FGA) in vitro and provokes necrosis in skin, muscle and lung tissues. May contribute to local edema and ecchymosis induced by venom. Hydrolyzes model substrate (beta-chain of insulin) at Ala(14)- Leu(15). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily."}
{"protein": "MSIKHWMSAPIAVATLFASQLLLAGSVLAAENNDRLDPRNDAFEQKHPDQYHSWKATSESKHIEDALSEDPNMVILWAGYGFAKDYNKARGHFYALDDVRQTLRTGAPADENSGPMPMACWSCKSPDVARVIEERGEDGYFSGKWARLGSEIVNPIGCSDCHDTRSEKFNQGEPELALTRPYVERAFDVIGKNFDDQSRLDKQASVCAQCHVEYYFTGPTKAVKFPWDMGTTVGDMEKYYDALDFKDWTHAVSKAPMLKAQHPGFETWREGIHGKNKVVCVDCHMPKVTKADGTVYTDHKVGNPFDRFEDTCAQCHTQTKEQLRNIVSSRKALVLNMKLTAEKQIVAAHFEAGEAWKAGATEEEMKPILQDIRHAQWRWDYAIASHGVHMHAPEVALEVLGTAVDRAADARTKLVRLLATKGITEPVQIPDISTKAKAQEALGMDMEKMNADKKHFLDTVVPDWDKAAAEREATY", "text": "FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the cytochrome c-552 family."}
{"protein": "MKRTKNINHSSFRKSWSARHLTPVALAVTAVFMLAGCEKSDETVSLYQNADDCSAANPGKAAECTTAYTNAVKEAERTAPKYATREDCVAEFGEGQCQQTPAQAGVAPENQAQAQSSGSFWMPLMAGYMMGRLMGGGMAQQQPLFSSKNPASPAYGQYTDASGKSYGAAQPGRTMNVPKTAMAPKPATTTTVTRGGFGESVAKQSTMQRSAAGSTSSSRSMGG", "text": "SIMILARITY: Belongs to the UPF0441 family."}
{"protein": "MQFKVYTYKRESRYRLFVDVQSDIIDTPGRRMVIPLASARLLSDKVSRELYPVVHIGDESWRMMTTDMASVPVSVIGEEVADLSHRENDIKNAINLMFWGI", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system, functioning in plasmid maintainence. Responsible for the post- segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system. Half-life of over 2 hours. Cell killing by CcdB is accompanied by filamentation, defects in chromosome and plasmid segregation, defects in cell division, formation of anucleate cells, decreased DNA synthesis and plasmid loss. Interferes with the activity of DNA gyrase, inducing it to form a covalent GyrA-DNA complex that cannot be resolved, thus promoting breakage of plasmid and chromosomal DNA. DNA breakage requires hydrolyzable ATP. Toxicity is inhibited by labile antitoxin CcdA, which blocks the activity of CcdB; CcdA also removes bound CcdB protein from the CcdB-GyrA complex by forming a CcdA-CcdB complex, a process termed rejuvenation. Also acts to inhibit partitioning of the chromosomal DNA. Functions as a transcriptional corepressor for the ccdAB operon, repression also requires CcdA. FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system, functioning in plasmid maintainence. Responsible for the post- segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system. Half-life of over 2 hours. Interferes with the activity of DNA gyrase, inducing it to form a covalent GyrA-DNA complex that cannot be resolved, thus promoting breakage of plasmid and chromosomal DNA. Toxicity is inhibited by labile antitoxin CcdA, which blocks the activity of CcdB; CcdA also removes bound CcdB protein from the CcdB-GyrA complex by forming a CcdA-CcdB complex, a process termed rejuvenation. Functions as a transcriptional corepressor for the ccdAB operon, repression also requires CcdA (By similarity). SIMILARITY: Belongs to the CcdB toxin family."}
{"protein": "MAFKHFNPTTPGQRQLVIVDRSCLYKGKSVKALTAGLSSKGGRNNHGRVTARFQGGGHKRSYRFVDFKRLKRGVFAKVERLEYDPNRTAFIALIRYEDGQLSYILAPQRLDVGDSIIAGSNVDVKPGNAMPLGNMPVGTIIHNVEMKPGKGGQIARSAGTYAQLVGRGQGMVILRLNSGEQRLVSGSCFATVGAVSNPDHANINDGKAGRSRWRGKRPHVRGVAMNPVDHPHGGGEGRTSGGRHPVSPWGKSTKGKRTRSNKATDKFIMHTRHQRKK", "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": "MVSLEVRLRTPKGKREAKRLRRRGEVPAVVYGPATDPIPVKIKRSLLEKVFHTITETTPIRLVIKDDEERTVSEKTVFLKMIQRDKVSEAIVHVDFYEPVKGHRMRINVPLKVVGKPVGVEKGGFLEVYHEEIPVETDPDRVPQEIEVDVSSLDLGDVIHARDLKLPEGVKCLLEDEEAVVSILVPKEVSIEEEEVEEEVAEPEVIKRKEEEEEE", "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": "MNPENYLYLSALLFTIGAAGVLIRRNAIIVFMCIELMLNASNLAFVTFARMHGNLDGQVFAFFTMVVAAAEVVVGLAIIMTIFRSRRSASVDDANLLKN", "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": "MKLILKENVDNLGHIGDIVKVAPGYARNFLLPKGFAIEATEKNAKALEHAKRHLEYKKNKVLEAAKQLAAKIEGLSLSIAHQAGADDRLFGAVTNMELAEQLKANGIEVDRKRIVLAEPIKQLGDFTATVKIHPEVSATLKVAVTKA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MKVLTPAALILLFFFYTVDARTREYTSVITVPNGGHWGKWGIRQFCHSGYANGFALKVEPSQFGRDDTALNGIRLRCLDGSVIESLVGKWGTWTSFLVCPTGYLVSFSLRSEKSQGGGDDTAANNIQFRCSDEAVLVGDGLSWGRFGPWSKRCKICGLQTKVESPQGLRDDTALNNVRFFCCK", "text": "FUNCTION: Exact function not known, component of the outer membrane of the vitelline layer of the egg. Seems to be able to synthesize N- acetylchito-oligosaccharides (n=14-15) from hexasaccharides of N- acetylglucosamine in a manner similar to the transferase activity of lysozyme. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the VMO1 family."}
{"protein": "MKTLKVLKIFIIVYISSVSLESFAGFGESCSNLPITSDGYLETYTAYGYIIRSIDMKDPRGNCNPSTSSITFCFKNVEGSASPCTIYTLNEGDTRKISDLSTDNNPDLGANTVLKNIVLTVKKFGNDLCLAMPTSRGPMPVACKSLSVTPTATKPKDENCNIGKSCYTGANYSQSLINFSGLAVQCLSETLNKIFFTGSSCSAQDQNSRITHLASFATFQGYLKRIIGAALILYTMFFAFNMALNKEYATTEKITLFIIKFLFVVYFSIGLGPLDFSGGQPVKENGMLKYGLPLLTGAAPDFAGMIFNAAGSRGLCQFDNTKYKDGYKFYGLWDAIDCRIGYYLGLDLLYNIDKNGILGRPVSNGTSGNNKPIPNFDPDGKKDRPHDLSKAGALRFFTVMFGFFMSGHVIILVAGMVFSVIFLSILLYFITHYLVCMVTIYVMTYISPIFIPMVLFTRTKAYFDGWLKVCISCALQPAVVAGFIALLITMYDSAIFKNCEFLRYDYEKGDIRFSTFELRLPSIDADKCQESFGYKMLKYYAGEGWEEHLLILFPIKSIVRDVVSILAELLCVLIFSVIFYYFSKSIGRFAADLTNGPNMDAVTASPTKIVDLVKKGAAFLKDASVHEHGKSSLGDKPDIGNKRKDGAQQGEDAVNSSGGEVADLASGSGGGK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TrbL/VirB6 family."}
{"protein": "ANERPPGSCSSSGCRRCCRPGPYHSHLAVLKAEQAAVFKFPLAPLGCSGLGSALLAAGPGMPGPAGASHLPLELQLRGKLEAAGSGEPGSKAKKGRRSRTVFTELQLMGLEKRFEKQKYLSTPDRIDLAESLGLSQLQVKTWYQNRRMKWKKIVLQGGGLESPTKPKGRPKKNSIPSSEQLSEQERAKETEKPPESPGEPSERQQEE", "text": "FUNCTION: Transcription factor, which is involved in craniofacial development, in odontogenic region definition, and in stomach organogenesis. Binds to a regulatory module of the NCAM promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BAR homeobox family."}
{"protein": "MSSSEEVSWVTWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPNYRQALDMILDLEPEDELEDNPLQSDMTEQAAEMLYGLIHARYILTNRGIAQMIEKYQTGDFGHCPRVYCESQPMLPLGLSDIPGEAMVKTYCPKCIDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPTNQFVPRLYGFKIHSLAYQIQLQAAANFKMPLRAQRGQPPKDEEPENNADTVPKRL", "text": "FUNCTION: Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit. SIMILARITY: Belongs to the casein kinase 2 subunit beta family."}
{"protein": "MAMGSASCISLVVLVALATAASGQLSSTFYDTSCPRALVAIKSGVAAAVSSDPRMGASLLRLHFHDCFGCDASVLLTGMEQNAGPNVGSLRGFGVIDNIKTQLESVCKQTVSCADILTVAARDSVVALGGPSWTVPLGRRDSTTASASLANSDLPGPSSSRSQLEAAFLKKNLNTVDMVALSGAHTIGKAQCSNFRTRIYGGDTNINTAFATSLKANCPQSGGNTNLANLDTMTPNAFDNAYYTNLLSQKGLLHSDQVLFNNETTDNTVRNFASNAAAFSSAFTTAMIKMGNIAPLTGTQGQIRLSCSKVNS", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. FUNCTION: Involved in defense response to powdery meldew fungus. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MYVVFEGIDCVGKSTQISLLKEIYKDAIFTLEPGGTELGKHLREILLNKTHPISKRAELLLFLADRAQHFEEILKTNQNKLIISDRSFISGMAYAKDFENDLLFTLNSFALEDFFPQKIIFLKGDENLIQERLSQKELDSIEKRGIEYFLSVQDKLKKVLHFLKEKISIEILTLDAKESKEKLHQQIKEFLQ", "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": "MPKQKTHRASAKRFKRTGSGGLKRFRAFTSHRFHGKTKKQRRHLRKASMVHSGDFKRIKSMVSQMR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "MRTIVVCSGGLDSVSLAHKIAAEQQLIGLVSFDYGQRHRKELDFAARCAARLAVPHHIIDISAIGGHLSGSALTDDIEVPDGHYAEETMKATVVPNRNAIMLAIAFGLAAAQKADAVAVAVHGGDHFIYPDCRPGFIDAFQRMQNEALDGYASVRLLAPYVEVSKAAIVTDGEKHATPFAETWSCYKGGRLHCGRCGTCVERREAFHLAGIPDPTEYEDQDFWKAAVSQYSAAEVR", "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": "MRKKRYVWLKSILVAILVFGSGVWINTSNGTNAQAATITQDTPINQIFTDAALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGLEYLNNLTQINFSNNQLTDITPLKDLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTNLQQLSFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISPISNLKNLTYLTLYFNNISDISPVSSLTKLQRLFFYNNKVSDVSSLANLTNINWLSAGHNQISDLTPLANLTRITQLGLNDQAWTNAPVNYKANVSIPNTVKNVTGALIAPATISDGGSYAEPDITWNLPSYTNEVSYTFSQPVTIGKGTTTFSGTVTQPLKAIFNAKFHVDGKETTKEVEAGNLLTEPAKPVKEGHTFVGWFDAQTGGTKWNFSTDKMPTNDINLYAQFSINSYTATFENDGVTTSQTVDYQGLLQEPTPPTKEGYTFKGWYDAKTGGDKWDFATSKMPAKNITLYAQYSANSYTATFDVDGKSTTQAVDYQGLLKEPKAPTKAGYTFKGWYDEKTDGKKWDFATDKMPANDITLYAQFTKNPVAPPTTGGNTPPTTNNGGNTTPPSANIPGSDTSNTSTGNSASTTSTMNAYDPYNSKEASLPTTGDSDNALYLLLGLLAVGTAMALTKKARASK", "text": "FUNCTION: Mediates the entry of Listeria monocytogenes into cells. Binds to host receptor cadherin-1 (E-cadherin, CDH1). SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. SIMILARITY: Belongs to the internalin family."}
{"protein": "MKNYIITGRPGIGKSTLFNNIINTLRKSGIIVGGIKSPEVRDSKGFRIGFKIIDLMSNEEGWLAKRNYYSTIKVGKYGIVLDESSRIIREALRKALEKADVIGIDEIGPMELKIHVFRTMLEQVLNSDKPKILVIHYRLRDPSILDKIYRVENEKYVLTEHNRDLLNKVLPQKIVMEIKQIIKK", "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": "MVKIVTVKTQAYPDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFEPFTVEIVDSVEAYATMLRNIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGSRIIFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQERTGRSAPTVIT", "text": "FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MTALAAVPDLQDAAGPSTTTVHSPNYSGSPADISSSPTTRAVSRNTARQTASAPPNHAESSPPGNASPTGPPSPSGNNVSPHGRHQGMSKLRACLVIATLSGVSFLNTMGSGILTVSLPTMARDVRLDDSLLLWPASVYSLAAGCTLLVFGAVGHIIGPKRVWITGACLYAAFTLGVGRSATGSQLIAFRSVLGVSIAMCLPTAVSLTTNGFGAGRWRNMAFAFQGMGQPLGYSTGLILGGIFTDTVGWRFGFYISGGINAVLAICALVVLPSPPRHDEGDGEQREVEEEATDATVAAAAVNRSSRSRPLISRLAHDVDWTGTLAISASMGFLSYVFSVVSKDYDRMAAPQNIALLVAAALLLPTFTLWVGRQERLDRPALIPNSLWRKAAFSSTCAAVFFTWAVFNAFQYFSALYFERIEHITALQTSLRFLPMVLVGAATNIVTGYLVETVEVRWLVVVSAIFSLFSPLIMALVRPGWGYWKGAFFAMLLSPLHPDVLFTVSNLIISRVYDGRSQSLAGAVFNAVSQVGNSVGLGLTAVVSSAVARSYHGSGGVGNAMDPPTGRPQHLPSSPTVEATLAGYHAAFWLMFGAAALVTVITFLGLRRGGKVGAVE", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyriculol and pyriculariol, two heptaketides that induce lesion formation upon application on rice leaves but are dispensable for pathogenicity (PubMed:27902426). With the ABC transporter ABC7, is most likely responsible for pyriculol and pyriculariol secretion and thereby may contribute to intrinsic resistance (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. EmrB family."}
{"protein": "MRQNQLIEKVTAGQLRSDIPAFRAGDTVRVHALIVEGTRERVQIFEGVVIKRHGAGISATYTVRKISNGIGVERTFPLHSPRVEKIEVVRYGRVRRAKLYYLRERTGKSARIAERRRDK", "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": "MNPLGLFLIYLYTCALTPVSGYPNGKVTSACRSMRPDHGHAPQSEPIHSINVEKTIFKPGDRIKVTLSGSRFDGFLVQARDAENLEGSAVGSFSLTDERISQLLTCDGIQNSAVSHTSKERKLQVELFWIAPANSPKHIQFLATVVEKYKIYWVKIPGPIISQPKAPSIAPKIPSSTIPVVPPPSLSLHKRFNSAGCGSSKFCIRNPVSCDPEHNPECFFLSFRKDGQSVLVEMSGPGQGYISFALSHDQWMGDDDAYLCVKEDDGVQINPAYIRGRSHPEVSSMDVLRDVAWRLEDGVIQCSFRRNIQIPIPKERFDLGRSYFIFLADGDAKDGLLYRHHRQPLMTNRKYCITDFPEDVGGSRSPLIIKLHGAMMFIAWMTTVSIGVIIARFFKPVWPTSSLFGEKIWFQIHRCLMITTVFLTVVAFVLPFIYRGYFSKRAGYHPHLGVTVMILTVLQPVLAVFRPPPQTHRRGIFNWTHWATGTAARIIAVAAMFLGMDLQALDLPDPWDTYTMIGFVLWHVFVDLLLEAHGFCLLKKAKTMEEDQIGILNSSPDEAEGHTFKKIVMTVYICGNLAFLITFLAAINQL", "text": "FUNCTION: Putative ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FRRS1 family."}
{"protein": "FLSLIPHAINAVSALAKHF", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Phylloseptin subfamily."}
{"protein": "MPKILWKSLHLCFPSNLTKCYSSPCIPPSSADPDGIIQPNRPSIVLLNNFNLLYHNDNHHHPHRVIDLPSSSTTTTPAATSSSSTSSYESDISPDVSAAFASRRFFFSSPGRSNAITDSPEPRSREFSDNYDDATITSTKKKKKKVYDNSVTTTTTRLISGGTAVTQHVDSPDPLTDFRRSMQEMIDAAIDAGELSRDPNDGYDFLDELLLTYLSLNPADTHKFVIRAFSDILVSLLSEERRIC", "text": "FUNCTION: Transcriptional repressor that regulates multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGDIMIDWFFHTLKSYPEIAIFLSLALGYYFGSFTYKGLGLGAVTATLIAAVIIGQIGITITGPLKPFFFLMFLFAIGYGVGPQFVRGIAQDGVPQAIFAAVVCVFCLLAPYVAAKIAGYDVGSAAGLYAGSQTISASMGLATDAINRLGLSPEETKKILDGMPVAYAVTYIFGTVGSAIVLALLGPALLGIDLEAACKRYEEEYGGKKQLGGPGTAWHQFDVRAFRVRERGPAVGKTVQEAEALIPDQRVFILRLRQEGKIVDATSDAVIHAGDVVAVAGRRDVLVQLIGEQAEEVDDRELLAMPIEGVDVYVTSKDVDSKTLEQLAKAPAARGVFLRKITRGAIAVEIPILPNTKLNRGDIVTIVGRTPDVAAATKMLGRPDRATDMADVAFIGAAIAIGALVGAIVYKIGSVPLTLSTSGGALISGLFFGWLRSVRPTFGRIPSPTVWFMNSVGLNVFIAIVGISSGPGFVAGLKALGFGLFLWGVVATTAPLILAMYVGKYVFRFHDAIVLGCCSGARTTTASLGMVNDRAKSQIPGLGYTVTYAVGNTLLTIWGMVLVMLMT", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family."}
{"protein": "MDTDSGDLSEGELSPGPEQFSSKSFAVQAQKKILSKMATKTMANMLIDDTSSEIFDELFKVTKEYVKNKKEAHKVLKDLVKVAVKVGILYRNKQFSLEELEIVENFRKKLNQTCMTAVSFFEVEYTFDKNVLSGLLHECKTLLHELVQRHLTPKSHSRIDRVFNHFADVEFLTALYSLEGNYRPYLKRICEGVNKLLDERVL", "text": "FUNCTION: May act as a lipid transfer protein. SUBCELLULAR LOCATION: Cytoplasm Cell membrane. SIMILARITY: Belongs to the TNFAIP8 family."}
{"protein": "MTTAHRPQFDPARGHSEMAPTRITSSRALPAHLKLKYRQESQGTEEEVRKQDLREALLRAEAAHFATQEHGASSEEVSQNSKLIEGFTSPSTDDKPNNDVEVDYQELLRQTLEADEDASDSDDSVDSSNKNSEVSIKRRKTESNSQESVDSSNSESSDEESDSEDETQQLLRELENIKQERKREQMLQEEKNRALEQEKREREIAFGNELLNKASSGSFQVKRRWDEDVVFRNTHKGVDDTPRPGFVNDMLRSEFHKKFLARFVD", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC15 family."}
{"protein": "MPSMDIVSEVDEVELRNAVDNSVRELKSRFDFRGKDASIEYKDHVVTLSAEDDFQCQQLVDILRMQLSKRNVDPASMDVDDKSVHSGKTFSLKVRFKEGIEVLTAKKLVKIIKDSKLKVQSSIQGDSVRVTGKKRDDLQAVMTLARESGLDQPFQFNNFRD", "text": "SIMILARITY: Belongs to the UPF0234 family."}
{"protein": "MSLANRIEEIRCLCQYKLWNDLPSYGEDENVPQNIRRCYQLLDMTSRSFAVVIKELPNGIREAVMIFYLVLRGLDTVEDDMTLPLDKKLPILRDFYKTIEVEGWTFNESGPNEKDRQLLVEFDVVIKEYLNLSEGYRNVISNITKEMGDGMAYYASLAEKNDGFSVETIEDFNKYCHYVAGLVGIGLSRLFAQSKLEDPDLAHSQAISNSLGLFLQKVNIIRDYREDFDDNRHFWPREIWSKYTSSFGDLCLPDNSEKALECLSDMTANALTHATDALVYLSQLKTQEIFNFCAIPQVMAIATLAAVFRNPDVFQTNVKIRKGQAVQIILHSVNLKNVCDLFLRYTRDIHYKNTPKDPNFLKISIECGKIEQVSESLFPRRFREMYEKAYVSKLSEQKKGNGTQKAILNDEQKELYRKDLQKLGISILFVFFIILVCLAVIFYVFNIRIHWSDFKELNLF", "text": "FUNCTION: Squalene synthase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:8474436). Erg9 produces squalene from 2 farnesyl pyrophosphate moieties (PubMed:8474436). 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; Single-pass membrane protein. SIMILARITY: Belongs to the phytoene/squalene synthase family."}
{"protein": "MQFMTISNDNKIVLSIPMLSTLSLNCLVKITGSISQSKQLLVENNLLLSNFEIIYNNLVSIKRQIIYKDIFDKMFSYKLRKHPISLNSFYKDNIFYLKGMYLANLFSDKVSKNINSKCIFGMNSISDIIINMRTQKITHRNPKVLCKKINKLNKYTVDEVVEKGEIFEQSVNYIIIKDKYHPEFFVKIKFETNYIYDFFDIECLEYSCNIGDKDLKVIPKITNPNLSVGKVIDNCRNKKFRILSIGKPIIKHDCTNIIVDENGYVSGSMKNCIDRYSCYGNYILRKYRKLINDGWQCLNEVCDNPVCILAQEDFAEKMYKLRKSYDESVPQLEEVNE", "text": "SIMILARITY: Belongs to the mimivirus R69 family."}
{"protein": "MSAFQPTIKRRESTKIYVGNVPIGGDAPIAVQSMTNTRTTDVEATVAQIKSLERVGADIVRVSVPTMDAAEAFKQIKQQVNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGREDRIRAVVDCARDKNIPIRIGVNAGSLEKDLQEKYGEPTPEALLESALRHVEILDRLNFNQFKVSVKASDVFLAVEAYRLLAKAIKQPLHLGITEAGGARAGAVKSAVGLGMLLAEGIGDTLRVSLAADPIEEIKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIGTVNALEQRLEDIITPMDVSIIGCVVNGPGEALVSDLGVTGGNKKAVIILTANVKKSVLITKI", "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": "MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIIQPLTIYGPHGIREFVETALRISGSWTDYPLEIVEIGAGEIFDDGLRKVTAYPMEHPLECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQELKAGKTIMLDDGRQINGADYLAAPVPGKALAIFGDTGPCDAALELAKGVDVMVHEATLDMAMEAKANSRGHSSTRQAAALAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFAVFSI", "text": "FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities. SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily."}
{"protein": "MPLSKEQKQEVMEKYKLHEHDTGSPEVQIAILTEKIKQLNEHLKTHQQDHASRRGLLKMVGKRRGLLNYLKSNSADRYLELIKKLGLRK", "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": "MDLSAIYESLMSMSHDLSPDHGGTESSGGLWNINSSDSIPSGVTSRLTGRSTSLVEGRSCSWVPPPPGFAPLAPRPGPELSPSPTSPTATPTTSSRYKTELCRTYSESGRCRYGAKCQFAHGPGELRQANRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPTEDLALPGQPHVLRQSISFSGLPSGRRTSPPPPGFSGPSLSSCSFSPSSSPPPPGDLPLSPSAFSAAPGTPVSRRDPTPACCPSCRRSTTPSTIWGPLGGLARSPSAHSLGSDPDDYASSGSSLGGSDSPVFEAGVFGPPQPPAPPRRLPIFNRISVSE", "text": "FUNCTION: Zinc-finger RNA-binding protein that destabilizes numerous cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:27193233). Acts as an 3'-untranslated region (UTR) ARE mRNA- binding adapter protein to communicate signaling events to the mRNA decay machinery. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation. Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs. Self regulates by destabilizing its own mRNA (By similarity). Binds to 3'- UTR ARE of numerous mRNAs (PubMed:27193233). Binds also to ARE of its own mRNA. Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF- alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages. Also plays a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response. Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia. Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA. Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE- mediated mRNA decay of the myogenic determination factor MYOD1 mRNA. Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs. Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs. May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE- containing RNAs, in vitro. Involved in the delivery of target ARE-mRNAs to processing bodies (PBs). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing. Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages. Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion. Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis. Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasmic granule Cytoplasm, P-body Note=Shuttles between nucleus and cytoplasm in a CRM1-dependent manner (PubMed:12054509). Localized predominantly in the cytoplasm in a p38 MAPK- and YWHAB-dependent manner. Colocalizes with SH3KBP1 and MAP3K4 in the cytoplasm. Component of cytoplasmic stress granules (SGs). Localizes to cytoplasmic stress granules upon energy starvation. Localizes in processing bodies (PBs). Excluded from stress granules in a phosphorylation MAPKAPK2-dependent manner. Shuttles in and out of both cytoplasmic P-body and SGs (By similarity)."}
{"protein": "MFVVIFGRPGCPYCVRAKNLAEKLKGEVADFDYRYVDIHAEGITKEDLSKSVGKPVETVPQIFIDEKPIGGCTDFEALMKEQFGIVA", "text": "FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family."}
{"protein": "MPEHPRHCDFQRGNVEIGLGPGGDLLGKRLSCPCITSHCSSEKKARSKDPQATSLLPELESTMAPEDHYHQLMSALSEASSFEETQRLYHLGIPSHDLLRVRQEVATATLRGPSGLEVHLPSSTADHRRKQGLVQRREGAVPAAATSFSEREMSQPPPLLSPQNAAHITMSSHLRPPFLGMPTAVCQTPGFSFLPSAQAEMLARQQELLRKQSLARLEMSELLRQKELGSVHRPLLPAPEVALHIPEGPDELQRRGSMLVLKHSSAPLLALPPQGPPGPGPPIPPKESARSRSEKGSLGVQPSQPKETTGAGLWAQEVSEEPSKDSDGEDPETAAAREGTSTPSQVPAGGTRAEGRGLLSGSTLPPPLPLGFPCGAVSPYFHTGTMGGLFTDEETTTLEDVNKWTVDDVCNFVGGLSGCGEYARVFGEQGIDGETLPLLTEEHLLNTMGLKLGPALKIRAQVAKRLGRVFYMASFPVALPLQPPSLQAPELSPGHQPLSPATTTSPYEGTHLPTGQASPKQENGSGTIALLSGAPDPSQLLQ", "text": "FUNCTION: May play a role in photoreceptor development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDYEFLRDITGVVKVRMSMGHEVVGHWFNEEVKENLALLDEVEQAARALKGSERSWQRAGHEYTLWMDGEEVMVRANQLEFTGDEMEEGMNYYDEESLSLCGVEDFLQVVAAYRHFIQQR", "text": "SIMILARITY: Belongs to the UPF0231 family."}
{"protein": "MTLDQVRIPFLVEQTYPIIVPSYAGWFDMSKIHDIERRSNPEFFNGKSPLKTPSIYKDYRDFMINSYRLEPNEYLTVTACRRNLVGDVCAIIRVHAFLEQWGLINYQIDPETRPAFRLPPISGHVQAISNTPIVTQEMLAQHPPPSTVGGSSSQEFVKLEEKHYSPSLNAMEQTSPKEEDEKSDKVPRVDKVCFTCGVNCSQTWYHNLKNKKYDICPNCYKQGRFSSSFNSSDFLCMDAIDFNHDEEKPWSNQETLLLLEAIETYGDDWNQIALHVGSRTKEQCLIHFLQIPIEDPYRQKLQGDFSPFKKGFLPFDENENPVLSTLTYLASIVQQGMKERKQNESVKQGETSFGNSEFKNPLERVAYYALKSAAQKAKLIAAFENRQLRRLVFSLIQAQLEKLQLKMKVLEQLEKMCSLELSELDLRGKNLLLSRLSTKKMLLAFNKKLEEAVNLGGEDGLKIIDDLMSTEHAEALLTFEMPTATTVSPLSKQYPDKFRTIAL", "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. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SMARCC family."}
{"protein": "MEQAPGDQGPQREPYNEWALEILEELKNEAVRHFPRPWLHGLGQHIYNTYGDTWEGVEAIIRILQQLLFIHFRIGCRHSRIGIVPQRRVRNGASRS", "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": "MASKERQTILLACTECKNKNYYYARGKKKEFKLELNKFCKACGKSTKHKEGKAN", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MARIGRILTLVVFAAVGLFLFMGQTVEAKGPKITSKVYFDIEHDGQPLGRIVMGLYGKTVPKTAENFRALATGEKGFGYEGSTFHRVIKDFMIQGGDFTNGDGTGGKSIYGNKFEDENFKLRHTKKGVLSMANAGKDTNGSQFFITTAITAWLDGKHVVFGEVLEGYDIVDKIQVVPKGFQDRPTKDVKIVKCGELDMKEEAEGEGTESPSKPDSEKEQAPVRDEI", "text": "FUNCTION: PPIases accelerate the folding of proteins (By similarity). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). 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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B subfamily."}
{"protein": "MAAALQRIEQLSSRVVRVLGCNPGPMTLQGTNTYLVGTGSRRILIDTGEPSVPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNISNDATYCIKKLRRNPQKEEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTIFEDLSDYMNSLKDLLKVKANIIYPGHGPVIHNAEAKILEYISHRNNREEQIITVFRDNLEESFSVSELRKMIYKNVPENLHKMAEHNLLLHLRKLEKDGKIFSIASPAKKWRASL", "text": "FUNCTION: Endoribonuclease; cleaves preferentially 3' to purine- pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double- stranded RNA or DNA. Required for normal mitochondrial function and cell viability. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family."}
{"protein": "MKFQMIAAVLLIAFCLSVVVTARMELQDDEDMKNGSFQKRRTCIDTIPKSRCTAFQCKHSMKYRLSFCRKTCGTC", "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": "MGQKIHPTGFRLAVTRNWSSRWYADDKDFGGMLAEDIRVREYLKKKLKSASVGRVVIERPAKNARITVYSARPGVVIGKRGEDIESLKADLQRLMGVPVHVNIEEIRKPETDAQLIADSISQQLEKRIMFRRAMKRAMQNAMRLGAQGIKIMSSGRLNGIEIARTEWYREGRVPLHTLKANIDYGTSEAHTTYGVIGIKVWVYKGDMLANGELPVETAAPREEERRPRRAPRGDRPDGARNGRPGGGRGRAPRKADAAPAPEGE", "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": "MAGTKEIRTKIKSVQNTRKITKAMEMVAASKMRKAQERMRNARPYAEKVRNIAAHLATANPEFKHPFMQEREVKRVGMIVVTTDKGLCGGLNTNVLRSVTNELKSLQGRGVDVQATAIGTKGMQFLGRIGAKVVSHVVHLGDTPHLEKLIGAIKVQLDAFTNGEVDAVYLAYTKFINTMKQEPMVEQLLPLAADKLSQTEEEKRAYSWDYIYEPDAQTVVEELLVRYVEALVYQAVAENMASEQSARMVAMKAASDNAKNVIGELQLVYNKTRQAAITKELSEIVSGAAAV", "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": "MTTQLDRVVLIGVAGDSGCGKSTFLRRLTDLFGEEFMTVICLDDYHSLDRQGRKAAGVTALDPRANNFDLMYEQIKTLKSGQSIMKPIYNHETGLLDPPEKVEPNKVVVIEGLHPLYDERVRELVDFGVYLDISEEVKINWKIQRDMAERGHTYEDILASINARKPDFTAYIEPQKQYADVVIQVLPTRLIEDKESKLLRVRLVQKEGVKFFEPAYLFDEGSTIDWRPCGRKLTCTYPGIKMYYGPDNFMGNEVSLLEVDGRFENLEEMVYVENHLSKTGTKYYGEMTELLLKHKDYPGTDNGTGLFQVLVGLKMRKVYEQLTAEAKVPASV", "text": "SIMILARITY: Belongs to the phosphoribulokinase family."}
{"protein": "MGDSHVDTGATSTEAVAEEVSLFSMTDMILLSVLVGFLTYFFLFRKKKEEIPEFTKISTTTSSVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMAADPEEYDLADLSSLPEIDNSLAVFCMATYGEGDPTDNAQDFYDWLQETDLDLSGVKYAVFGLGNKTYEHFNSMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVLHADTDPAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSNLVNQLGKILGADLDVVMSLKNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEQLHKMASSSGEGKELYLTWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKSGRINKGVATSWLQAKDPAGENGRRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGVAPFIGFIQERAWLQQQGKEVGETLLYYGCRRSDEDYLYREELAQFHKDGTLTQLNVAFSREQAQKVYVQHLLKRDQEHLWKLIHEDGAHIYVCGDARNMARDVQNTFCNIAAELGGMEHTQAVDYVKKLMTKGRYSLDVWS", "text": "FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. 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--cytochrome P450 reductase family."}
{"protein": "MKKKRVILAYSGGLDTSIIVRWLTEKGYEVITYTADVGQGEELSEIPEKARRAGAIEAIVEDLKETFAENYCLPTLRALALYEGKYPLTAALSRPLIAERLVYYAEKFNADYVAHGSTGKGNDQVRFELSVWALNPDIEVLAPVREWEFKSREEQVEYAQRFNIPVKATKEKPYSIDRNLWGVSIECGPLEDPWQEPPQDAYQITQSPEEAPDEPEYVTVGFEKGKPVYLNGERYEEQWKLIANLNEIAGRHGVGRIDMVENRLVGIKSREIYEAPGAMVLYEAYRDLLSLVLDRFTFHYFLTHIPHEYAKLVYEGLWFTPLREALDAFTNKIAEFATGEVRLKLYKGSVSVVGRRSPNSLYVEELATYSEKDQFDQIAGKHFTKVWGLPLKVLGRVRKGK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
{"protein": "ITEFSWNKYLYELIQRFEYWTVFCTSVNTSSSEGFLIGVNYLGPYCDKAIVDGNIMHANYIFWRNSTIMALSHNSVLDTPKFKCRCNNALIVNLKEKELNEMVIGLLRKGKLLIRNNGKLLNFGNHFINTP", "text": "FUNCTION: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products."}
{"protein": "MSSLRPEEARKLATAASVSPLSNCQFCGVVISSIADEQKLEFTNKYKGSCTLLCSYDSQGVVLRVVSDDDRSHVLKEYMITADTDAAQMGRRSYAVSLDADNLVLRFGSEQDQQLFRKVVENVKHLRPKSVFSQRTEESSASQYFQFYGYLSQQQNMMQDYVRTSTYQRAILGNAVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQYAQQLVESNNVQHKISVIPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKWLKPQGKMYPTHGDLHIAPFSDESLYSEQYNKANFWYQSAFHGVDLTTLHKEGMKEYFRQPIVDTFDIRICMAKSVRHVCDFLNDKEDDLHLISIPLEFHILQTGICHGLAFWFDVEFSGSSQNVWLSTSPTAPLTHWYQVRCLLPMPIFIKQGQTLTGRVLLEANRRQSYDVTIDLHIEGTLISSSNTLDLKNPYFRYTGAPVQAPPGTSTQSPSEQYWTQVDTQGSRNSSSMLNGGLSVNGIGDGMDITHGLMHPH", "text": "FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
{"protein": "MELILGSQSSARANLLKEHGIKFEQKALYFDEESLKTTDPREFVYLACKGKLEKAKELLANNCAIVVADSVVSVGNRMQRKAKNKREALEFLKRQNGNEIEVLTCSALISPVLEWLDLSVFRARLKAFDCSEIEKYLESGLWQGSAGCVRLEDFHKPYIKSSSKNLSVGLGLNVEGLLGALKLGVKLSLL", "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": "MASERLPSRPACLLVASGASEGVSAQSFVHCFTLASAAFNLQVATPGGKAIDFVDVTESNARWVQDFRLKAYASPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFRSESKPICAIGHGVAALCCATNEDRSWVFQGYSLTGPSVYELIRAPGFARLPLIVEDFVKDSGAGFSASEPDAVHVVLDRHLVTGQNANSTVPAVQNLLFLCGSRK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C56 family."}
{"protein": "MDRFTIKGPVKLQGEVEISGSKNAALPILMATLLTDEKCVLNRVPNLRDIRTTFKLLEVLGKKVEYNNGTAVITKNKELNSILPYELVKQMRASFWVAGPLLARLKHTQIPLPGGCAIGVRPVDIHLQGFKKFGAAESTKKGDVVISADELKPAKIVLRFPSVGATINIMMCASLIPGKTIIENAAKEPEVEDLICALKTMGAQISIDSKGRIIVEGKKTLGSMTHTVVADRIETGTFILAAAATKGDVVIKNCVPEHNDILLENLKDAGFGVSVGQGRIHITAPSNGKIKPVGIRTMPYPGFATDLQAPYMVLLCVADGGSDITEDIFENRYMHAPELVRMGADITIEKTMAKVKGVKELSGANVMASDLRGGAALVIAALCAAGDTVIDRVYHIDRGYENIEAKFAALGAKIVRDNPLKD", "text": "FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily."}
{"protein": "MSIAHIVDWRLYVVTDAGLSRGRSHRAVIEAAIVGGATVVQYREKHASTRQMIEEALELRDLTRRAGVPLIVNDRVDVALAVDADGVHVGQDDMPVALARRLIGNKLLGVSAHNLSEALQAVRDGADYLGVGPIFATTTKPDAAAPIGLDGLRAIRQHVSIPIVAIGGINQANAADVMRAGADGIAVVSAVVAADDVTAAARQLRALVSVTQEKAL", "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": "MSRKMTGIVKTFDRKSGKGFIIPSDGRKEVQVHISAFTPRDAEVLIPGLRVEFCRVNGLRGPTAANVYLS", "text": "SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAVPKKRTSASKKRIRKNSWKGKGYGTALKAFSLGKSLSTGNSKSFFVPKNSLKVFKRIIKNWNNLNRLGSKN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "MKFTGSPLLWPSWLPLPAPPPPLPSVTRRRDPRTVGKRAAITDACDVGYGAGTTGGSGGTTTTVSTPAQFTAAATSDEKAVIVVKGAITGATKVKVGSNKSIIGRAGSSLTGVGLYINKQENVIVRNMKISKVLADNGDRIGIQASSKVWVDHCDLSSDKKNNGKDYYDGLLDITHASMAVTVSNTYIHDHYKGSLVGHSDSNSAEDTGKLYVTYANNHWYNVASRNPSVRFGNVHIFNNYAEKLETSGVNTRMGAQLLIESSVFSDTKKAVTFLDSKSTGYAVVNDVDLGGSTNDRPQGTFTKPDYSYTLLGSSKVKAAVVGTAGQTLTF", "text": "FUNCTION: Acts as a virulence factor active in plant tissue maceration. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 1 family."}
{"protein": "MAVGKNKRTSKGKKGGKKKVTDVFTKKEWYDLKAPKMFLVRNFGKTLVTKTIGKKLATDGLKGRIYEVNLADLNNDEDQAHKKIKLCCDHIINKDCYTDFCGLSITRDKLCSLIRKGYTLIEGYTDVKTIDNYQLRMFCIAFTKKRPNQTKTTCYAQTSQIKKIRKKMVDIMNAEASKVMLKDLVKKFIPESIGKEVEKQCKKIYPLQNVLIRKVKILKRPKLDISKLMELHTDSKEDAGKNVKSLPESKEATNILSAELKH", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family."}
{"protein": "MAGARRLELGEALALGSGWRHACHALLYAPDPGMLFGRIPLRYAILMQMRFDGRLGFPGGFVDTQDRSLEDGLNRELREELGEAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEELLAVEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDLGLLQSGSISGLKIPAHH", "text": "FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms (PubMed:20385596, PubMed:26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed:20385596). Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (PubMed:20385596). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (PubMed:32432673). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Nucleus, nucleolus Cytoplasm Note=Localized predominantly in the cytoplasm (PubMed:21070968). Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity). SIMILARITY: Belongs to the Nudix hydrolase family. NUDT16 subfamily."}
{"protein": "MAQSEYLFTSESVSEGHPDKVCDRISDAIVDAFLAEDPHSRVALETMATTNFVVLAGEVRGPDSLTHDRLKEIAREAIKDIGYEQRGFHWKDAEIVSHVHSQSADIAVGVDAAGNKDEGAGDQGIMFGYACTETEELMPAPIALSHAILKSLAEFRHGGDTSFGPDSKSQVTLRYVDGKPVGAASVVVSTQHAGNLSQDEVRELVRPHVLKVLPEGWMCPEEEFYVNPTGRFVIGGPDGDCGLTGRKIIVDTYGGAAPHGGGAFSGKDPTKVDRSAAYAARYLAKNVVAAGLAEKCVIQVSYAIGVSKPLSVYVNTQGTGQVDEQRLAVVLQQLMDLSPRGIRQHLQLSRPIYARTAAYGHFGRKPEKDGGFSWERTDLVAGLKTAFGA", "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": "MPADIMEKNSSSPVAATPASVNTTPDKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMTAALSTDPSVLGKYRAGFSECMNEVTRFLSTCEGVNTEVRTRLLGHLANCMTQINAMTYPGQAHPALQAPPPPPPSGPGGPQHAPFAPPPPLVPIPGGAAPPPGSAPCKLGSQAGEAAKVFGGFQVVPAPDGQFAFLIPNGAFAHSGPVIPVYTSNSGTSVGPNAVSPSSGSSLTADSMWRPWRN", "text": "FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'- CANNTG-3' with low affinity. May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSYGSITFGDVAIDFSHQEWEYLSLVQKTLYQEVMMENYDNLVSLAGHSVSKPDLITLLEQGKEPWMIVREETRGECTDLDSRCEIISDGKMQLYRKHSCVTLHQRIHNGQKPYECKQCQKSFSHLTELMVHQTIHTSEEPDQCEKFRKAFSHLTDLRKHQKINAREKPYECEECGKVFSYPANLAQHGKVHVEKPYECKECGEAFRTSRQLTVHHRFHYGEKPYECKECGKAFSVYGRLSRHQSIHTGEKPFECNKCGKSFRLKAGLKVHQSIHTGEKPHECKECGKAFRQFSHLVGHKRIHTGEKPYECKECGKGFTCRYQLTMHQRIYSGEKHYECKENGEAFSSGHQLTAPHTFESVEKPYKCEECGKAFSVHGRLTRHQGIHSGKKPYECNKCGKSFRLNSSLKIHQNIHTGEKPYKCKECGKAFSQRAHLAHHNRIHTGYKPFECKECGKSFRCASYLVIHERIHTGEKPYVCQECGKGFSYSHKLTIHRRVHTGEKPYECKECGKAFSVSGQLTQHLSIHSGKKPFECNKCGKSFRFISVLKAHQNIHSAEKPYECKECGKAFRHATSLIYHDRTHAGEKSYECKECGETFSHASHLIIHERIHTSDKPYECKRCGKAFHCASYLVRHESVHADGNPYMCEECGKAFNSSHELSIHHRVHTGEKPFKCNKCRRSFRLRSILEVHQRIHI", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MASLTDLVNLDLSDCTDRIIAEYIWIGGTGIDLRSKARTVKGPITDPIQLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRKGNHILVMCDCYTPQGEPIPTNKRYSAAKVFSHPDVAAEVPWYGIEQEYTLLQKDVSWPLGWPVGGYPGPQGPYYCAAGADKAFGRDVVDAHYKACLYAGINISGINGEVMPGQWEFQVGPSVGISAGDEIWVARYILERITEMAGIVLSLDPKPIKGDWNGAGAHTNYSTKSMREAGGYEVIKAAIDKLGKRHKEHIAAYGEGNERRLTGRHETADINTFKWGVANRGASIRVGRDTEREGKGYFEDRRPASNMDPYVVTGMIAETTILWNGN", "text": "FUNCTION: Plays a role in the flow of nitrogen into nitrogenous organic compounds. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MLVLGLETSCDETGVALYDSERGLLADALFSQIDLHRAYGGVVPELASRDHVKRMLPLIRQTLAEADCVATDIDAIAYTAGPGLVGALLVGASCAQALAFAWDIPALGVHHMEGHLLAPMLEENPPQFPFVALLVSGGHTQLVRVDGIGQYELLGETLDDAAGEAFDKTAKMMGMQYPGGPEISKAAMQGVAGRFVFPRPMTDRPGLEFSFSGLKTSALNTWQQCRNAGDDSEQTRCDIALAFQQAVVETLTIKCKRALKQTGLKSLVIAGGVSANKALRASLESMLGDLRGHVYYARPEFCTDNGAMIAFAGCQRLQVGQKEDLSISVQARWPMEQLSGL", "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": "MEVKMNKNEQEDSKKLKYFRLLAKQYPNIALASTEIINLEAILNLPKGTEHFLSDIHGEYEPFVHVLRNGSGVVKRKIEDLFCKSLLESDIKSLATLIYYPEQKLDIVLKEERNIDDWYKITLNRLIEICRFCSSKYTRSKVRKALPADFAYIIEELLHEQFNGIDKEEYYDRIITTIIDIGRAKEFIIALSKLIQRMIIDRLHIIGDIYDRGPRPDIIIDTLMEYHSVDIQWGNHDMLWMGAAAGVRTCVANVLRISTRYANLDLVEEIYGINLLPLATFALKYYRDDPCESFIPKVKEDDPAASQEVDLVSKMHKAITILQFKLEKEIIDRRPEFELEGRLLLDKIDYEKGTIILNGIEYKLNDNNFPTIDPKDPYKLTDEESVLIDKLVYSFVNSDKLQKHVRFLFSKGNMYLKFNSNLLFHGCIPLDDEGNLKSMCIQGEEYESKRLLEKFDSLSREGYFEKVGSEEKTYGMDIMWYLWTGPVSPLFGKKQMATFERYFIDDEIAHIEQKTGYYKLRDREEMCDMILREFGLDPSESRIINGHVPVKKKNGESPIKANGKMIVIDGGFSKAYQKQTGIAGYTLIYNSYGLQLVSHEHFSSTEESIMKEKDILSTTLVVEQKLKRKTVEDTDIGKDLQVQIKDLKELLLIYRKGIIKEIR", "text": "SIMILARITY: Belongs to the FBPase class 3 family."}
{"protein": "MSEQQQQGAEQALDLNNEMQARREKLAALRKEGIAFPNDFRRDTTSDKLHSLYDGKSKEELEALNVEVSVAGRMMTRRIMGKASFVTLQDMGGRIQLYVARDDLKDDVYSEQFKKWDLGDIIGARGTLFRTQTGELSIHCHSIHLLTKALRPLPDKFHGLSDQETRYRQRYLDLIANESSRETFRTRSKILAAIRNFMVNKGFMEVETPMMQVIPGGASARPFITHHNALDIDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGVSPRHNPEFTMMELYMAYADYKDLIVLTEELFRTISQDVLGSSVVQYGDQTFDFGKPFIKMSMKEAICHYRPDIASADLDDMDKACKIAESLGIKIEKSWGLGRVQCEIFDETAESQLIQPTFITEYPAEVSPLARRNDDNPFITDRFEFFIGGREIGNGFSELNDAEDQAERFQDQVKAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGVGIDRMMMLFTNSHTIRDVILFPAMRPQK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MGGSALNQGVLEGDDAPGQSLYERLSQRMLDISGDRGVLKDVIREGAGDLVAPDASVLVKYSGYLEHMDRPFDSNYFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPNYAYGTLGCPPLIPPNTTVLFEIELLDFLDCAESDKFCALSAEQQDQFPLQKVLKVAATEREFGNYLFRQNRFYDAKVRYKRALLLLRRRSAPPEEQHLVEAAKLPVLLNLSFTYLKLDRPTIALCYGEQALIIDQKNAKALFRCGQACLLLTEYQKARDFLVRAQKEQPFNHDINNELKKLASCYRDYVDKEKEMWHRMFAPCGDGSTAGES", "text": "FUNCTION: Has an essential role in spermatogenesis (PubMed:36150389). It is required to repress transposable elements and prevent their mobilization, which is essential for the germline integrity (By similarity). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (By similarity). Acts as a co- chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis (By similarity). May be required together with HSP90 in removal of 16 nucleotide ping- pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=In spermatocytes, it colocalizes with PIWIL1 in large cytoplasmic granules (PubMed:36150389). Does not localize to the synaptonemal complex (PubMed:36150389). SIMILARITY: Belongs to the FKBP6 family."}
{"protein": "MSGKSPAQTRVVVGMSGGVDSSVTALLLKEQGYDVIGVFMKNWDDTDENGVCTATEDYKDVAAVADQIGVPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAMELGADYVATGHYAQVRTDENGIVHMLRGADNNKDQTYFLSQLTQEQLKKTMFPLGHLEKPEVRKIAEKAGLATAKKKDSTGICFIGEKNFKKFLGEYLPAQPGKMMTLDGIEMGNHAGLMYYTIGQRGGLGIGGQHGQLTSDPWFVVGKDLTTNTLYVGQGFHHEHLYSTSLDASDLSFTREMPETFDLHCTAKFRYRQEDTGVTIHVNGDKVTVDFDEPVRAITPGQAVVFYDGEECLGGAMIDVAYKAQKVMQYQ", "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": "MNLPIVNERNRPDVPRKGVQKIRTVIEGFDEITHGGLPIGRTTLVSGTSGTGKTLLAVQFLYQGIHHFDYPGLFITFEESPSDIIENAYSFGWDLQQLIDDGKLFILDASPDPEGQEVVGTFDLSALIERIQYAVRKYKAKLVSIDSVTAVFQQYDAASVVRREIFRLVARLKQLQVTSIMTTERVEEYGPIARFGVEEFVSDNVVVLRNVLEGERRRRTVEILKLRGTTHMKGEYPFTITHDGINIFPLGAMRLTQRSSNARISSGVQTLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLQEGCRQRERAILFAYEESRAQLSRNASSWGIDFEEMEHKGLLKLLCTYPESAGLEDHLQMIKSEISEFKPSRIAIDSLSALARGVTNNAFRQFVIGVTGYAKQEEITGFFTNTTDQFMGAHSITESHISTITDTILMLQYVEIRGEMSRALNVFKMRGSWHDKGIREYSISHDGPDIRDSFRNYERIISGSPTRISVDEKSELSRIVRGVKDKTAE", "text": "FUNCTION: Has a weak, temperature-independent ATPase activity; ATPase activity defines the circadian period. The phosphorylation state of KaiC modulates its ATPase activity and effects KaiB binding. FUNCTION: Component of the oscillator and circadian clock in this organism, enhances fitness in a rhythmic environment (PubMed:25139948). Autophosphorylates in the presence of KaiA, no activity is seen in its absence (PubMed:23449916). FUNCTION: Central 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. Clock output pathways impact the RpaA transcriptional regulator. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. KaiB and KaiC together enhance the phospho-RpaA dephosphatase activity of CikA. SIMILARITY: Belongs to the KaiC family."}
{"protein": "QQCGRQASGRLCGNRLCCSQWGYCGSTASYCGAGCQSQCRS", "text": "FUNCTION: Chitin-binding protein with a defensive function against numerous chitin containing fungal pathogens. It is also an inhibitor of Gram-positive bacteria such as B.subtilis."}
{"protein": "MATPVNAQCSSKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQDRVLAKLNRLHNQQALSSSIEEGLKMQAMHRAQRVRKHQHESDNTTFSGGEDNCDSRSHVSNPSVHSNQEAGPSRKRSRASEDSGAEPDLSHEGGVRSPDPPGGGETGSEIELVFRAHPLLVEKDGYSQTRYVKTTANATVDHLSKYLALRIALEEEVLRGEAEGVTLGEVSEKQYTIYICTGVAGGQYTTLNGSLTLELVNEKYWKVSKPLELYYAPTKEQK", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression. Essential 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, rendering chromatin heritably changed in its expressibility. SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome."}
{"protein": "MVTIVPYSHQYLKDICQLIQKDLSEPYSKYVYRYFVHQWPEFSFVALDNDRFIGAVICKQDVHRGTTLRGYIAMLAIVKEYRGQGIATKLTQASLDVMKNRGAQEIVLETEVDNEAAMSFYERLGFCRYKRLYRYYLNGTDAFRYILYPN", "text": "FUNCTION: Catalytic component of the NatC N-terminal acetyltransferase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily."}
{"protein": "MAIQHPDIQPAVNHSVQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVENVLPHTTPWHAMRFLTPKGRCFADIQPMTDEFGWPRRNAFIQPQVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLHLKTAEGQRETIKAQWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVDIANDPLSTPHIYLCCDPVRPYVSAALPHAVRRFEFMVMPGETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQGTLRDGVSWLLNYLPPVKRYFLEMRFKPMPQYYGGALVREGEAKHSPVGKMFIQPKVTLENGDVTLLDNAIGANFAVIGWGCNPLWGMSDEQIQQWRALGTRFIQVVPEVQIHTAQDNHDGVLHVGDTQGRLRSWFAQHNASLVVMRPDRFVAATAIPQTLGNTLNKLASVMTLTRPDADVSVEKVA", "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": "MIIPVRCFTCGKVIGDKYYEFKRRVEAGEDPEKVLDDLGLERYCCRRMLLSHVELIDDIMHYKVY", "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": "MNSPVLQDCVREWGEIQENYQDIQETHRLYKQKLEELSKLQTRCSGTISRQKKKLRELSVELKKCKSKAKNVEEEEEQIRDLNNQIRAREKTFFEMESFLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILMVLSFICRFLLNSRVTDAVFNFLLVWYYCTLTIRESILINNGSRIKGWWVLNHYISTFLSGVMLTWPDGLMYQMFRNQFLSFSMYQSFVQFLQYYYQSGCLYRLRALGERHNMDLTVEGFQSWMWRGLTFLLPFLFFGQFWQLYNAITLFKLARHPECKEWQVIMCGLPFLVHFLGNFFTTLRVVHQKFQKQN", "text": "FUNCTION: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Nucleus inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM120 family."}
{"protein": "MNLQNNKGKFNKEQFCQLEDEQVIEKVHVGDSDALDYLITKYRNFVRAKARSYFLIGADREDIVQEGMIGLYKSIRDFKEDKLTSFKAFAELCITRQIITAIKTATRQKHIPLNSYASLDKPIFDEESDRTLLDVISGAKTLNPEEMIINQEEFDDIEMKMGELLSDLERKVLVLYLDGRSYQEISDELNRHVKSIDNALQRVKRKLEKYLEIREISL", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This sigma factor is involved in the transition to post-exponential phase in the beginning of sporulation. It is also required for transcription of several stationary phase genes. Association with the RNAP core increases rapidly in early exponential phase, and reamins constant expression level after (PubMed:21710567). SIMILARITY: Belongs to the sigma-70 factor family."}
{"protein": "MKISLHNKRQRGDQNQNMSVFNVLKPLLKGSNSFKVKLNGFLFNNVSTITIRTLMKTHKGTAKRWRRTGNTFKRGIAGRKHGNIGWSHRSLKALTGRKIAHPAYSKHLKRLLPYH", "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. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "NECIRKWLSCVDRKNDCCEGLECYKRRHSFEVCVPIPGFCLVKWKQCDGRERDCCAGLECWKRSGNKSSVCAPIA", "text": "FUNCTION: This toxin potently and selectively inhibits ASIC1a, an isoform of the gene ASIC1. It incompletely inhibits ASIC1a activation in a pH-independent and slowly reversible manner. This toxin acts by binding to and stabilizing the closed state of the channel, thereby impeding the transition into a conducting state. This toxin may bind to the acidic pocket of ASIC1a, since mutation of a key residue of this pocket (Arg-350) abolishes the ability of the toxin to inhibit ASIC1a. In vivo, this toxin protects the brain from neuronal injury when administered up to 8 hours after stroke onset. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the psalmotoxin-1 family. Double-knot toxin subfamily."}
{"protein": "MFITFEGIEGTGKTTQIKKLTAFLEESGHNVDVTLEPGGSRIGKELRKILLNMDSTDITGECELFLYLADRAQHVGQVIKPAVEAGKIIISDRFADSTIVYQGYGRGLDPKLLRELNDVAVSGNWPDLTILLDIDPEIGLKRAMTRNLQENKMQEEGRFEAESLEFHNRVREGYLTWAALNNDRIVVVNADQTPDEIFKEIKAKVVERIKGDFVTNG", "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": "MNDFWQHCSALLERELTPQQYVTWIKPLAPVAFDASANTLSIAAPNRFKLDWVKSQFSGRISDLAREFWNTPIEVQFVLDPKAGMRSAAAGAAPAAPRAPLTPNGPAATVAAIAANLTANAAAAPSAPADVPMTPSAAAAHHLNADDADIDLPSLPAHEAAAGRRTWRPGPGAAPANGGEADSMYERSKLNPVLTFDNFVTGKANQLARAAAIQVADNPGISYNPLFLYGGVGLGKTHLIHAIGNQLLLDKAGARIRYIHAEQYVSDVVKAYQRKAFDDFKRYYHSLDLLLIDDIQFFSGKSRTQEEFFYAFEALVANKAQVIITSDTYPKEISGIDDRLISRFDSGLTVAIEPPELEMRVAILMRKAQSEGVNLSEDVAFFVAKHLRSNVRELEGALRKILAYSKFHGREISIELTKEALKDLLTVQNRQISVENIQKTVADFYNIKVADMYSKKRPANIARPRQIAMYLAKELTQKSLPEIGELFGGRDHTTVLHAVRKIADERSKDAQLNHELHVLEQTLKG", "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": "MVRERTKKLRGGHYGRGFKAGRGKGKKGGSGNAGMGKHKWIWMVKYDPLHFGGKGFTSHHISQVEVPINLGDVEYMYESLKRDGFVREENGEIIVDLRAAGYDKLLGNGNFTVKSTIIIDKATEKAISKLSAIGSKIENDGSSA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MTGTTLAATYGPISGADLEAELAQPRIADGDAQDAAVYERDGGAHAPPFASGGAPPDGDRADVRRAAGAGDASVRLTRVSKRYGERAVLADVDLSIGRGSFVSIVGRSGCGKSTLLRLVAELETPSAGTLVKRGDGGGALDTRIMYQEARLLPWKTVLQNVMLGLGRRAKDDARAVLDEVGLLARANDWPAQLSGGQRQRVALARALVHRPQLLLLDEPLGALDALTRIEMHALIERLWREHRFTALLVTHDVQEAVALADRVLLIEAGRIAFDQRVPLDRPRARASAAFAALEDRVLQRVLTGSDAAPAAPNAAGPEGASRGRAAPASGLRWAV", "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": "MHTPVVFIDGDQGTTGLQIHARLQGRSDLRLLTLPEAERKDPQRRCEAINSADIALLCLPDDAAREAVAAIHNPQVRVIDASSAHRTTPGWVYGLPELDEQQAERIAQSTRVSNPGCYPTGAIALLHPLVKAGLLPADYPLNIHAVSGYSGGGRAAVERHEQPGAAKAPALQLYGLELAHKHVPEIQQHAGLSARPMFMPGYGAYRQGIALSIPLQLRLLPGQVSAEHLQACLEQHYQGARHVQVMPLHQCGAAANLDPEALNGSNDLRLALYANPEHGQVLLTAVFDNLGKGASGAAVQNLDLMLGALQAHG", "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": "MAEKVNVCIVGSGNWGSAIAKIVGANAAALPEFEERVTMFVYEEMIDGKKLTEIINETHENVKYLKGHKLPTNVVAVPDLVEAAKNADILIFVVPHQFIPNFCKQLLGKIKPNAIAISLIKGFDKAEGGGIDLISHIITRHLKIPCAVLMGANLANEVAEGNFCETTIGCTDKKYGKVLRDLFQANHFRVVVVEDAEAVEVCGALKNIVACGAGFVDGLKLGDNTKAAVIRLGLMEMIRFVDVFYPGSKLSTFFESCGVADLITTCYGGRNRRVSEAFVTSGKTIEDLEKEMLNGQKLQGPPTAEEVNYMLKNKGLEDKFPLFTAIHKICTNQLKPKDLIDCIRNHPEHM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MAGNPANTESHDDDALHRRGLMFILSSPSGAGKTTIARKLLSEDSEIAMSVSVTTRPMRPGEVDGKDYFFVEPAEFERMVEANEFYEWATVFGNCYGTPKAHIRERLKTGGDVLFDIDWQGTQQLYQKAQADVVRVFILPPSLDELRRRLTGRGTDSAEVIAARMDRAQAEISHWDGYDYVVVNDDVDGCFGKVREILAAERMRRTRQTGLIDFVRGLMRG", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family."}
{"protein": "MYSAQSSISKLTNLCEISSVEVGQHFYWQIGGFQVHAQVLITSWIVIAILLGLAILATQNLQTIPTSGQNFVEYILEFIRDLTRTQIGEEEYRPWVPFIGTMFLFIFVSNWSGALLPWRIFELPHGELAAPTNDINTTVALALPTSVAYFYAGLRKKGLSYSGKYIQPTPILLPINILEDFTKPLPLSFRLFGNILADELVVAVPISLVPLVVPIPMMFLGLFTSAIQALIFATLAAAYIGESMEGHH", "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": "SMLSVLKNLGKVGLGLVACKINKQC", "text": "FUNCTION: Antibacterial activity against Gram-positive bacterium S.aureus (MIC=55 uM) and Gram-negative bacterium E.coli (MIC=1.5 uM). Has activity against C.albicans (MIC=58 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ranatuerin subfamily."}
{"protein": "MSHKIMAINAGSSSLKFQLLAMPEGEILCQGIIERIGLADARLVVKTATEKWQEITPVADHREAVTLLLEQLINRKIINSLHDIDATGHRVAHGGETFKDSALVTDDVMAEIERLAELAPLHNPVNLLGINIFRQLLPSAPTIAVFDTAFHQTLEMPAYIYPLPWRYYHELGIRRYGFHGTSHKYVSGKLAEKLGVPLSALRVVCCHLGNGSSVCAIKGGKSVNTSMGFTPQSGVMMGTRSGDIDPSILPWIALREGKTPQELNQLLNNESGLLGVSGVSPDFRDIEQAAENGNQQAQLALALFAERIRATIGSYVLQMGGLDALIFTGGIGENSARARAAICNNLHFLGLSIDADKNQHNATFIQSEQAMVKVAVINTNEELMIARDVMRIALPEPALQEVLA", "text": "FUNCTION: Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of 1,2-propanediol (1,2-PD). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase family. PduW subfamily."}
{"protein": "MKNSTAASSRWTKSRLSHFFPSYTNSSGMGAASTDQSSTQGEELHHRKHCEEDNDGQKPKKSPVSTSTMQIKSRQDEDEDDGRIVIKPVNDEDDTSVIITFNQSISPFIITLTFVASISGFMFGYDTGYISSALISINRDLDNKVLTYGEKELITAATSLGALITSVGAGTAADVFGRRPCLMFSNLMFLIGAILQITAHKFWQMAAGRLIMGFGVGIGSLISPLFISEIAPKMIRGRLTVINSLWLTGGQLIAYGCGAGLNHVKNGWRILVGLSLIPTVLQFSFFCFLPDTPRYYVMKGDLKRAKMVLKRSYVNTEDEIIDQKVEELSSLNQSIPGKNPITKFWNMVKELHTVPSNFRALIIGCGLQAIQQFTGWNSLMYFSGTIFETVGFKNSSAVSIIVSGTNFVFTLIAFFCIDKIGRRYILLIGLPGMTVALVICAIAFHFLGIKFNGADAVVASDGFSSWGIVIIVFIIVYAAFYALGIGTVPWQQSELFPQNVRGVGTSYATATNWAGSLVIASTFLTMLQNITPTGTFSFFAGVACLSTIFCYFCYPELSGLELEEVQTILKDGFNIKASKALAKKRKQQVAEGAAHHKLKFEPTQEIVES", "text": "FUNCTION: Minor transporter for myo-inositol. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MKCTLRWTITALVLLGICHLARPAYHKKCGRYSYCWIPYDIERDRRDNGGKKCCFCRNAWSPWQCKEDERYEWLRCGHKFYYMCCYTDDDNGNGDGNGNGFNYLKSLYGGYGNGNGEFWEEYIDERYDK", "text": "FUNCTION: May be specifically involved in the formation of the nacreous layer. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the N16 matrix protein family."}
{"protein": "MAKEATRVRRRERKNIVSGVAHVNASFNNTMITITDAQGNTISWSSAGAMGFKGSRKSTPYAAQVAAEDAGRKAAEHGMRTLEVEVSGPGSGRESALRALQAAGFTVTSIRDVTPIPHNGCRPRKRRRV", "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": "MKPEFWQDRWNKDQIGWHQKSANPHLVKYWPTLNISQGSTVIVPLCGKSLDMRWLEGLGYNVLGVELSEKACKQYFDQMELEPKVSKNASGKFTIYEAGNTQIWCGDLFDLDADDVKYVSALYDRASVIALPPDMRERYAAHLGALIPDPQGLIITLDYDQSKMNGPPHAVSDAEVQRLFGTNWKLTLLEEVDKKDMFKEEGIEPVERVYKLN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family."}
{"protein": "MEIIFYHPTFDTQYWICELEKQLPGARVREWKAGDNRPADYALVWHPPVEMLQGRALKAVFALGAGVDSILSKLRDHPDMLPLSIPLFRLEDTGMGRQMQEYAVSQVLHWFRRFDDYQALKLASRWQPLPEYRADEFTVGIMGAGVLGAKVAESLQPWGFPLRVWSRSRKSWPQVQSFAGQAELGEFMQGTRVLINLLPNTAETAGIINQTLLAQLPDESYVLNLARGVHVVEEDLLAALNSGKLKGAMLDVFSREPLPQESPLWAHPRVAMTPHVAAVTRPMEAITYIAETISRLERGEPVSGQVDRQRGY", "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": "MAKVLVLYYSSWGHVEQMAKAVAEGARETGAEVALKRVPELVPDEVAKQFHYKLDQEAPIATVEELADYDAIIFGTPTRYGNMASQMKQFIDQTGGLWAKGALVGKVGSAFTSTASQHGGQETTLTSFHTVLFHHGMVVVGLPYSFAGQNGVEQVKGNSPYGATTIADGDGSRQPSEVELDGARFQGRHVAGIAAKLAG", "text": "SIMILARITY: Belongs to the WrbA family."}
{"protein": "MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTETGAPQLNPIDGPLPENHEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNDLTANESGRLIDFLKDVMESMDKEEMEITTHFQRKRRIRDNMTKKMVTQRTIGKKKQRLNKKSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYITRNQPDWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLANIDLKYFNESTRKKIEKIRPLLIDGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAM", "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": "MALLQISEPGMAPAPHQRRLAVGIDLGTTNSLVAAVRNSVPEVLPDEAGRALLPSVVRYLEKGGRRIGHEAKEQAATDPRNTIVSVKRFMGRGKAEVEGAANAPYEFIDAPGMVQIRTIDGVKSPVEVSAEILATLRYRAEDTLGDELVGAVITVPAYFDEAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDNAAEGLYAVYDLGGGTFDLSILKLTKGVFEVLAAGGDSALGGDDFDHLLFGHVLAQAGIDAKALAPEDVRLLLDRVRVLKEALSSAPQASLDVTLSNGTRLVQTISHDTFASLVEPLVQRTLTPTRKALRDAQVTPADIKGVVLVGGATRMPVIRDAVAKYFGQPPLVNLDPDQVVALGAAIQADLLAGNRGGGDDWLLLDVIPLSLGVETMGGLVEKIIPRNSTIPIARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMTAGAARIRVTYQVDADGLLSVFAREQHSGVEASVVVKPSYGLADDDIAKMLEDSFKTAEIDMRARALREAQVEAQRMIEATQAALAADGELLDDAERTQVDALVAALRTIAQGDDADAIETATKALADGTDEFAARRMDKSIKRALSGRRLDEI", "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": "MASAEIIAVGTELLLGQIVNSNAAFISQELAADGIYVYHHTVVGDNPTRLKEVIEIAEKRSDILIFTGGLGPTEDDITKQILADHLQKQLVEDEYHMNKINEYFASRNRTMTENNKLQAVIIKDSVVLNNDYGFAAGMYLKENNHTYVLLPGPPSEMKPMFTKYANPLLLSENGNQNILESKIMRFFGIGESQLAADLNDLIVNQVNPTIATYAGDNEVVVRITATAKTKEEASSLVKDTEEEILRRDGTFLYGYGEVSLPELVTAMLLEKELTISAAESFTAGLFQAEIARFPGISKIFKGGMVTYSEETKQSILQVSPQVIKEKGVVSAECAKEMAENVSRLCKTDIGISFTGVAGPDSLEGHPAGTIWIGLSVKGHETEAFQFVYGRDRNHNRRRAVKQGFQLIKQFLDAN", "text": "SIMILARITY: Belongs to the CinA family."}
{"protein": "MVNSLLFGEMALAFGCPPGGGGCAGGGGGGGAGPGPSPVTAALRDDLGSNIHLLKGLNVRFRCFLAKVHELERRNRLLEKQLEQQQSERDRRLRYKTFSREQAVQTGPELLRPSAAGSGQALGAATGVNANAVALGGLPPGGGSHPQHYGRLPGTIWSYTQVRRTGGGGVETVQGPGVSWVHPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEELAKRMNLQTMVDTLQEAAQEAEAIQEEMNEKIERLKAELVVFKGLMSDPMTDLDTKIQEKAMKVDMDICRRIDITAKLCDVAQQRNSEDVSKIFQVVPKKKDRKVASDEDISEQDGEVNRFSDEEVGSMNITDEMKRMFNQLRETFDFDDDCDSLTWEENEDTLLLWEDFTNCNPTIDLQGEQEENLGNLIHETESFFKTRDKEYQETIGQIELELATAKSDMNRHLHEYMEMCSMKRGLDVQMETCRRLIKGSADRNSPSPSSVASSDSGSTDEIQEDLEREADVEPMVS", "text": "SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MQKTSMNPVTDPVAAATGRVAIRQLPIKTQPNSQSLTPFLQLPPKPPPNLLFSSPLASVELRHRARARRRRRPSHPRRAPAMRMGKYEMGRALGEGHFGKVKLARHADTGAAFAIKILDRQRILAMKIDEQIKREIATLKLLKHPNVVRLHEVSASKTKIYMVLEYVNGGELFDKIALKGKLSEKEGRKLFQQLMDAVSYCHEKGVYHRDLKPENVLVDAKGNIKVSDFGLSALPQNQRKDGLLHTTCGSPNYIAPEVLLNRGYDGSLSDIWSCGVILYVMLTGNLPFDDQNTVVLYQKILKGDARIPKWLSPGAQDILRKILDPNPITRLDITGIRAHEWFRQDYTPAMPFDDDDDNNISDGNLHMTENQDIETSPAISQINAFQLIGMSSCLDLSGFFEKEDVSERKIRFVSNYSPTSLFEKIESTVTEKGFQVQKNSGKLKVIQVCKEPANPRGHGNLLISAEVFEINESLYVVELKRSSGDCSLYRQLCASLSEDLGICKRQQLLKKDSMRQDLCRYNSSF", "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": "MNYLEFEKPLSEIEGKAEELRALARGNREMDVEKEASALDKKAETLLKDLYKDLTPWRKCQVARHPDRPHCKDYIEGLFTEYTPLAGDRNFADDHAIMGGLARFNDNPVVVIGQEKGHDTKTRIERNFGMARPEGYRKAIRLMEMAHRFRLPVITLVDTPGAYPGKGAEERGQAEAIARATQKCLEIGVPLVAVVIGEGGSGGAVALATANRIAMLEHSVYSVISPEGCASILWKDAEKMREAAEALRLTAQDLHKLGVIDRIIKEPLGGAQRGRRETVDAVGKAIEMMLKELVGRKPEWLVKDRRNKFLDMGSKGLAA", "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": "MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR", "text": "FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis (PubMed:18436533, PubMed:31019025, PubMed:24362451). Induces cartilage and bone formation (PubMed:3201241). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2 (PubMed:15064755, PubMed:17295905, PubMed:18436533). Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A (PubMed:7791754). In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation (PubMed:20851880, PubMed:16771708). Stimulates also the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation (PubMed:24362451). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MDQAIYTLHEFMLHTKNWTYILMGVTLLVYVGYWLFLTGRDEKIRKY", "text": "FUNCTION: HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MLSNCRQNTLGHNTQTSIAQDFSSEQGRTAPQDQKASIQIYPWMQRMNSHSGVGYGADRRRGRQIYSRYQTLELEKEFHFNRYLTRRRRIEIANALCLTERQIKIWFQNRRMKWKKESNLTSTLSGGGGGAAADSLGGKEEKREETEEEKQKE", "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": "MATTKSSYRRIFGGNPRSSSSGNRYATSSTRYTLGSAMRPSTSSRMVYSTSSSPAVFKSSSVRLRSSLPPARMADSVDFALADAVNLEFKANRTNEKAEMIELNDRFANFIDKVRFLEQQNKILVAELEQLKGKGTSRIGDLYEEEMRELRRQLDQATNDKARVEVDRDNLADDLQRLREKLQDEMIQKEEAEGNLQSFRQDVDNASLARIDLERKVESLQEEIAFLKKLHDEEIRELQLQIQESHIQVDMDVSKPDLTAALRDVRQQYENVAAKNLSDAEEWYKSKFADLSEAANRNNDALRQAKQETSDFRRQIQTLTCEIDAMKGSNESYERQMREMEENFAIEAANYQDTIQRLQEEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPVHSFSTMSLRETNLDSHPAETHSKRTVLIKTVETRDGQVVNESSQHHDDFE", "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. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MHLMEFPREVILGKNLIQEINNVIKRLKLGSPGLVVYGPITKKIAGSNVEKIVKEEFEVYSITVKEAHINEVERVISKIRDKGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRYLAAGVGDIVSNITAVRDWKLAHKLKGEYFSEYAASLSLMSAKMVIRDAEIIRLGQDEGIRKVVKALISSGVAMSIAGSSRPASGAEHLFSHALDMLLDKPALHGEQTGIGTIIMAYLHGINWKKIRDTLKIVGAPTTAYELGIDPEIIIEALTIAHTIRPERYTILGKEGITREAAEKAAKITGVI", "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": "MAGKGKGAKAAAKKRLEAQKLLADNRQARHQYEILDTLETGIELLGTEVKAIRAGKANLRDGFCLIRQGQLQLHNVHIAGHEQASRYFNHEPLRVRRLLAHRREIDKLRGQLDTKGLTLIPLNIHLKGSWIKLTIGLGKGRKLHDKRQEERRKQDQKDLRSALKRL", "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": "MADWQEITGGITAPKGYRAAGITAGLKPSGLPDLALIVSDVEAIASGVFTTSQVKAACVDYCRQRLQAKQSARAILCNAGQANAATGSQGIKDAEESAELLAKELNISPELILLASTGVIGQRIKMDALRNGIPKLIASLTDTGSDAAAGAIITTDLVTKSIALETTIGDRPVRIGGIAKGSGMIHPNMATMLAFVTCDAAVSSHLWQQMLTRAADRSFNSITVDGDTSTNDSLIALANGQSRTPAITEVGAESEKLEAMLTAVCQHLAKAIARDGEGATCLIEVQVTGAHDEQAARQIAKTIAGSSLVKSAIFGRDPNWGRIAAAAGRAGVPFEQENLQIQLGDFLLLDNGQPLPFDRAAASAYLKQAATGAYLQQDTVLISVKVGNGHGTGKAWGCDLSYDYVKINAEYTT", "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": "MPFVMAIDQGTTSSRAILFRGDISIAASAQQEFPQHFPASGWVEHEPEDIWASTLATCRAAMEKAGATAADIAAIGITNQRETVVVWDAASGKAIHRAIVWQDRRTAEVCTRMKADGYEPMITDKTGLIIDPYFSGTKVAWLLDNVPGARARAERGELKFGTIDCWLLWRLTGGRVHATDATNASRTLLFNIHTGDWDDELLQLLRVPRSMLPEVKDSSAHFGDSAYELFGAPIAIRGIAGDQQAATIGQACFSPGMIKSTYGTGCFALLITGATPVKSHNKLLTTIAYQLGGKRTYALEGSIFVAGSAVQWLRDGLGIIKHASETGPLADKSDSMQSVYLVPAFVGLGAPYWNPRVRGALFGMTRNTGPAELAHAALESVCYQTYDLWAAMRADWSGADAAPPVLRVDGGMAASDWTMQRLADLLDAPVDRPVIQETTALGAAYLAGLSAGVFPEPQKFADNWRLDHRFRPAMSQATRERKLAGWGRAVKGLLASDEGEG", "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": "MKVLFATGEAFPFVKTGGLGDVSYSLPKTLKQKENVDIRVILPKYSKISNELLKDARHLGHKEIWVAHHNEYVGIEEVELEGVIYYFVDNERYFKRPNVYGEFDDCERFLFFCKAVVETMDITKFKPDIIHCNDWQSALIPIYLKERGIYDVKTIFTIHNLRFQGFFFNNVIEDLLEIDRAKYFQEDGLKYYDMISFLKGGVVYSDYITTVSDSYAEEIKTQELGEGIHGLFQKYDYKLSGIVNGIDKISYPLSKKPHKILKADLQKKLGLDVEEDTPLIVIITRLDRQKGLDYIVEKFDEMMSLGIQFILLGTGEKRYEHFFAYQEYLHKGQVCSYIGFNQELSTEIYAGADIFLMPSVFEPCGLSQMIAMRYGCIPVVRETGGLKDTVKPYNEYTGEGDGFGFKQANADDMIKTLKYAIKMYHRPNVWQEIIKNAKKRDNSWDKPAKRYKELYQRLIEG", "text": "FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. SIMILARITY: Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily."}
{"protein": "MAVKIRLTRMGSKKKPFYRINVADSRAPRDGRFIETVGTYNPLVTENQVTLKEDRILEWLGNGAQPSDTVRNILSKAGIMQKFHEAKYSKK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MEIKQIKAREVIDSRGNPTVEADVILNDDTIGSAMVPSGASTGQKEALELRDRDKSRYLGKGVLKAVKFVNTEICDTLIGFDINNLSKIDQTMIDLDGTKTKSRLGANTILSVSLAAAHANANRQHKPLYASLNQGGNYKLPVPMMNIINGGEHANNNIDIQEFMIIPVGAPSFKEALRYGIEVFHHLKSILEIKGMSTTVGDEGGFAPNLASNEDAIKIILEAINNAGYKPGKDIFIGIDAASSEFYDNDNKTYNLISENKSFSSEEFVNYLAKWVENYPIISIEDGMDENDWNGWNLLTKKLGDKVQLVGDDLYVTNSKILKQGIERNIANSILIKVNQIGTLTETFATIKVAMNARYTSIMSHRSGETEDTTIADLAVACTCSQIKTGSLSRSDRLAKYNRLLRIEEELGTQAVYPGLNAFNHLN", "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": "MFSKTLTIADFDPVLWDAMRKEARRQEDHVELIASENYASPMVMAAQGSVLTNKYAEGYPGKRYYGGCEYVDIAEQLAMDRALELFGAEHANVQAHSGSQANQAVYLSVLQPGDKIMGMSLAHGGHLTHGAKVNVSGKLFQVAAYGVRAEDGRIDYDAMAEQAERERPKMIVAGASAYSRVIDFARIGEIARSIGAYLLVDMAHIAGLVATGLHPSPVPHADFVTTTTHKTLRGPRGGLILCREQYAKKVNSLIFPGLQGGPLMHVIAAKAVAFREALQPEFKSYQQQVIHNAQTLSKVLAGRGYGAVSGGTDNHLFLLNLGEKVTGKEAEEALGQANITVNKNAVPFDIRPPAVTSGIRIGTPAATTRGFGEAEMHRLGNGIADVLDASSDAAVIERVRADMKALCHQFPVYG", "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": "MLDLHYITENTEDLKKVLELRGFKEVGIIDELKSIIQRKRELQREVDLLREERNKVSKEVGRIKQSGGDITEISASVKLVGEKIKEIETKLEQEENVLININLGLPNILDPKVPNGKSEYDNVVQYEVGKIPSFSFPPKPHFEIGEALNWINFEKGVKLSGARAYTYWKDGAKLERALMNFMLDVHTKEHGYTEVWVPSMVNDESMTATGQYPKFKDEFYRIEKDELNLIPTAEVPLTNLYRDEIIPEDQLPISVTAHTSCFRREAGSYGKDTRGLVRVHQFQKVELVKFCKPEDSEEEHKKMLSHAENILKKLKLPYRVIILCSGDISANSSITYDIEVWMPGLNRFMEISSVSNFRDFQARRGKIRYKSKDGKNQLVHTINGSGLAIGRTYAAILENFQDANGTVHIPEVLKSYF", "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": "MTAAAPTLAQALDEATGQLTGAGITADAARADTRLLAAHACQVAPGDLDTCLAGPVPPRFWHYVRRRLTREPAERIVGHAYFMGHRFDLAPGVFVPKPETEEITRDAIARLEALVRRGTTAPLVVDLCAGPGTMAVTLARHVPAARVLGIELSQAAARAARRNARGTGARIVQGDARDAFPELSGTVDLVVTNPPYIPIGLRTSAPEVLEHDPPLALWAGEEGLGMIRAMERTAARLLAPGGVLLLEHGSYQLASVPALFRATGRWSHASSRPTCNDGCLTAVRNHTCAPPA", "text": "FUNCTION: Involved in pristinamycin I biosynthesis (PubMed:9044253). Catalyzes the SAM-dependent methylation of 4-amino-L-phenylalanine (PAPA) to 4-methylamino-L-phenylalanine (MMPAPA), and of MMPAPA to 4- dimethylamino-L-phenylalanine (DMPAPA) (PubMed:9044253). SIMILARITY: Belongs to the protein N5-glutamine methyltransferase family."}
{"protein": "MNIKPLADRVLILPAPAEEKTIGGIIIPDTAKEKPLQGEVVAIGNGTKDEEMVLHVGDQVLYGKYSGTELEHDGKKYLIMRQSDVLAVLG", "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": "MKLLAVRRLLRIQRVVIRYRLDDLILELPMLPWWLRLLGATLPWRWLPRRKLELTRGARLRLALQDLGPIFIKFGQILSTRRDLLPDDIANELAWLQDKVPPFPPELAVKRIEEQLGAKIEQVFARFEREPLASASVAQVHAARLKSGEEVVVKVIRPNLEPVIRSDIAWLFILARLAERVSSEARRLHPVEVVSDYEKTIVDELDLLREAANASQLRRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIPVTDLETLRDQRTDFKALAERGVEIFFTQVFRDSFFHADMHPGNIFVSTRAPWSPQYIAVDCGIVGSLTDEDQDYLARNLIAFFKRDYRKVAQLHIDSGWVPAETKVNDFEAAIRTVCEPIFEKPLKDISFGQVLLRLFQTARRFNMEIQPQLVLLQKTLLNIEGLGRQLYPELDLWATAQPFLERWMRERVSPKQLLRNFQQQVEQVPHLSQMARDTLERLSQPHAHNTPPPEWKGSRHDWLGRLVGAVLLVGAAEVGLGQQLEAWPAWVMLAGGVFLILRR", "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": "MSQLYDITIVGGGPVGLFAAFYAHXRQAKVQIIDSLPQLGGQPAILYPEKEILDVPGFPNLTGEELTNRLIEQLNGFDTPIHLNETVLEIDKQEEEFAITTSKGSHLTKTVIIAMGGGAFKPRPLELESVEGYENIHYHVSNIQQYAGKKVTILGGGDSAVDWALAFEKIAPTTLVHRRDNFRALEHSVQALQESSVTIKTPFAPSQLLGNGKTLDKLEITKVKSDETETIDLDHLFVNYGFKSSVGNLKNWGLDLNRHKIIVNSKQESSQAGIYAIGDCCYYDGKIDLIATGLGEAPTAVNNAINYIDPEQKVQPKHSTSL", "text": "SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family."}
{"protein": "MRAARLMGALLALAGLLQLALSLRIAAFNIRTFGETKMSNATLSNYIVRILSRYDIALIQEVRDSHLTAVGKLLNELNQDDPNNYHHVVSEPLGRSTYKERYLFVFRPDQVSVLDSYLYDDGCEPCGNDTFNREPSVVKFSSPSTQVKEFAIVPLHAAPSDAAAEIDSLYDVYLNVRQKWDLEDIMLMGDFNAGCSYVTTSHWSSIRLRESPPFQWLIPDTADTTVSSTHCAYDRIVVAGPLLQRAVVPDSAAPFDFQAAFGLSEQTALAISDHYPVEVTLKRA", "text": "FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:3782104). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:3782104). Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). SUBCELLULAR LOCATION: Secreted Zymogen granule Nucleus envelope Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. SIMILARITY: Belongs to the DNase I family."}
{"protein": "MSEEKERLISGKLAADDAKLDTSLRPRCLSDFIGQKRLKDNLGVAIQAAKQRGEALDHVLLYGPPGLGKTTLSHIIALEMGVNIRITSGPAIERQGDLAAILTNLKPFDILFIDEIHRLSRNVEEVLYPAMEDYALDIMVGKGPGARSLRLKLPHFTLIGATTRYAMLSAPLRDRFGSIFRLDFYDEDAIHDIVSRSAHILGVEAEENGIRQIACRSRGTPRVANRLLRRVRDYAQVKGNGLITGDMAAESLACLEVDRLGLDEIDHKVLKTIIHKFGGGPVGLETIAAAISEEADTIMDVYEPYLLQLGFLERTPRGRQATRLAYQHLNIPYPADKNNQQGLWAENGT", "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": "MVDELGSNSEVGTLKVVILHRPGTELRRLTPRNTDQLLFDGLPWVSRAQEEHDQFAELLRSRGVEVLLLSELLTEALHSGAARMQGVAAAVDSRRLGIPLAQELSAYLRGLDPVRLSHVLTAGMTFNELPADARTDVSLVVRMHHDADFVIEPLPNLLFTRDSSIWIGPRFVIPSLAMRARVREASLTDIIYAHHPRFTGIRRAYESRTAPVEGGDVLLLAPGVVAVGVGERTTPAGAEALARSLFDDDLAHTVLAVPIAQRRAQMHLDTVCTMVDVDKVVMYANVVDELTAFTIERQPDGVTISDAAPFVEAAARAMGIEKLQVIGTGIDPVVAEREQWDDGNNTLALAPGVVVAYERNAQTNARLEAAGIEVLTIGGSELGTGRGGPRCMSCPVARDPLP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arginine deiminase family."}
{"protein": "MAFTEIKHPLIIDKLTRMRKTETSSKDFRENLSEIAQLMVYEIFRDLKLESVDIETPVSKTTGYTINQPVVLVPILRAGIGMLDGIQKLIPTARIAHIGLYRDEETLETHQYFAKTTKDIDKSYVIVVDPMLATGGSACKAIDIVKQWGAKEIKFVCLVAVEPGIKRLQEQHPDVEIYAASKDEKLNEKGYIVPGLGDAGDRIFGTK", "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": "MAREFSLEKTRNIGIMAHVDAGKTTTTERILYYTGKIHKIGETHEGASQMDWMEQEQERGITITSAATTAQWNNHRVNIIDTPGHVDFTIEVQRSLRVLDGAVTVLDSQSGVEPQTETVWRQATEYGVPRIVFANKMDKIGADFLYSVSTLHDRLQANAHPIQLPIGSEDDFRGIIDLIKMKAEIYTNDLGTDILEEDIPAEYLDQAQEYREKLVEAVAETDEELMMKYLEGEEITNEELKAGIRKATINVEFFPVLCGSAFKNKGVQLMLDAVIDYLPSPLDIPAIKGINPDTDEEETRPASDEEPFAALAFKIMTDPFVGRLTFFRVYSGVLQSGSYVLNTSKGKRERIGRILQMHANSRQEIDTVYSGDIAAAVGLKDTTTGDSLTDEKAKIILESINVPEPVIQLMVEPKSKADQDKMGIALQKLAEEDPTFRVETNVETGETVISGMGELHLDVLVDRMRREFKVEANVGAPQVSYRETFRASTQARGFFKRQSGGKGQFGDVWIEFTPNEEGKGFEFENAIVGGVVPREFIPAVEKGLVESMANGVLAGYPMVDVKAKLYDGSYHDVDSSETAFKIAASLALKEAAKSAQPAILEPMMLVTITVPEENLGDVMGHVTARRGRVDGMEAHGNSQIVRAYVPLAEMFGYATVLRSASQGRGTFMMVFDHYEDVPKSVQEEIIKKNKGED", "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": "MDSNTVSSFQVDCFLWHVRKRFADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILEEESDEALKMPASRYLTDMTLEEMSRDWFMLMPKQKVAGSLCIKMDQAIMDKTIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTGEDVKNAIGVLIGGLEWNDNTVRVSETIQRFAWRSSDEDGRLPLPPNQKRKMARTIESEV", "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": "MAREKFDRSKPHVNVGTIGHIDHGKTTLTAAICTVLAKEGKSAATRYDQIDKAPEEKARGITINSAHVEYSSDKRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDSVMPQTREHILLARQVGVPRMVVFLNKCDIATDEEVQELVAEEVRDLLTSYGFDGKNTPIIYGSALKALEGDPKWEAKIHDLMNAVDEWIPTPEREVDKPFLLAIEDTMTITGRGTVVTGRVERGELKVGQEIEIVGLRPIRKAVVTGIEMFKKELDSAMAGDNAGVLLRGVDRKEVERGQVLAKPGSIKPHKKFKAEIYALKKEEGGRHTGFLNGYRPQFYFRTTDVTGSISLPENTEMVLPGDNTSITVELIAPIACEKGSKFSIREGGRTVGAGSVTEVLE", "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": "MKAKIHPKYHQAKARCACGNEFEVGSTSENIRVEICSKCHPFYTGAKGRLVDTTGRVDRFKKKYGLS", "text": "FUNCTION: Binds the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily."}
{"protein": "MQRLCAHVLILVLALAAFCEASWKPHSHLQDAPVAPGANRGQEPLRMNRLGPASNPRRQLGLQDPPHMVADLSKKQGPWVEEEEAAYGWMDFGRRSAEEGDQHP", "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": "MIKEFNTQTTLNVGLEALWAAQSKDITLVVPKVLPNIVKDVQVIEGDGGVGTKLIFNFLPGIAPVNYQREVITEYDELSHTIGLQVVEGGYLNQGLSYYKTTFQFSAISENKTLVNVKISYDHESELIEEKVKPTKTSESTLFYLGQLEKFLLNGA", "text": "FUNCTION: Binds gibberellin A3 (GA3) in vitro. SIMILARITY: Belongs to the BetVI family."}
{"protein": "MFKPRVILLITIIAVFSEFKKAFKGLFEKAANKYLH", "text": "FUNCTION: Peptide with insecticidal and antiparasitic activities. Induces irreversible paralysis in D.melanogaster when tested at high doses. It shows a moderate antiparasitic activity against the major pathogenic nematode of ruminants (H.contortus, EC(50)=41.3 uM). Does not show antimicrobial activities. Does not induce increase in intracellular calcium in mouse DRG neurons, suggesting that it does not induce pain. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the limacoditoxin-7 family."}
{"protein": "MPIRVQDELPAVNFLREENVFVMKASRATGQEIRPLKVLILNLMPKKIETENQFLRLLSNSPLQVDVQLLRIDARESRNTPSEHLNNFYCDFEDIRNDNFDGLIVTGAPLGLVEFNDVAYWPQIKQVLEWAKDHVTSTLFVCWAVQAALNILYGIPKQTRSDKLSGVYEHHILHPHALLTRGFDDFFLAPHSRYADFPAALIRDYTDLEILAETEDGDAYLFASKDKRIAFVTGHPEYDAHTLASEFFRDVEAGLSPEVPYNYFPKNDPQIPPRASWRSHGNLLFINWLNYYVYQITPYDLRHMNPTLE", "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": "MAKNEKIRIRLKSYDHKLLDFSAGKIVETAKKAGSQVSGPVPLPTEKQVVTILRAVHKYKYSREQFEIRTHKRLIDIANPTPKTVDSLMRLDLPAGVDIEIKL", "text": "FUNCTION: Involved in the binding of tRNA to the ribosomes. SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
{"protein": "MKRNNMKRARMEQSRRPKKNPLKAEGIEQVDYKNYALLRKFISDRGKIRSRRVTGLTPQQQREVATAIKNAREMALLPFNSR", "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": "MGCISSKNVSCLTDQGDSPLPEPGLLSTSQQHRVLIDHSLEASHNSKRSRKSRRLGGSDLRIGVSLGSSHRNIEAEQAAAGWPAWLCSAAAEAVHGWVPLKAEAFQKLEKIGQGTYSSVFRAREVETGKMVALKKVKFDNLQPESIRFMAREILILRKLNHPNIMKLEGIVTSRASSSIYLVFEYMEHDLAGLSSNPDIRFTEPQIKCYMKQLLWGLEHCHMRGVIHRDIKASNILVNNKGVLKLGDFGLANVVTPSNKNQLTSRVVTLWYRAPELLMGSTSYGVSVDLWSVGCVFAEILMGKPILKGRTEIEQLHKIYKLCGSPQDSFWKRTKLPHATSFKPQHTYEATLRERCKDLSATGVYLLETLLSMEPDKRGTASSALNSEYFLTRPYACDPSSLPKYPPNKEMDAKYRDDMRRKRANLKLRDSGVGRKHKRPHRAEYDPKNYAKLPIRKDTLEVKNIPNEASRATTTTHGNYYKVSDLPMTTGPASGFAWAVKRRKDPDNISTLTYYQPSSKSQLSGTSVAFAKNTFGLNLKPDNDSVWEVQGNNYDDVIEEVPSHESKLSRIGERHGSLDGSGLDFSQREEDSPKKTLEHLQFGKQSISGPLIFKSGKIDEILQRNESNIRQAVRKSHLQREQDDR", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MKNKVFLIGMPGCGKSTIGELISKELLLKFIDMDIYIEEKTSKTISELFEQGEDYFRDIESEACKEIIKYDNVVIATGGGVVKKGINVETLKNNGLVIFIDRPVEKIISDIDVSRRPLLKNGKERIIGLYKERYDIYNKACHKIVVNDGTIDEVIEEIKKIIINN", "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": "MLRVRILLIYLCTFVVITSTKTIEYTACNDTIIIPCTIDNPTKYIRWKLDNHNILTYNKTSKTIILSKWHTSAKLHSLSDNDVSLIIKYKDILPGTYTCEDNTGIKSTVKLVQRHTNWFNDHHTMLMFIFTGITLFLLFLEIAYTSISVVFSTNLGILQVFGCIIAMIELCGAFLFYPSMFTLRHIIGLLMMTLPSIFLIITKVFSFWLLCKLSCAVHLIIYYQLAGYILTVLGLGLSLKECVDGTLLLSGLGTIMVSEHFSLLFLVCFPSTQRDYY", "text": "FUNCTION: Promotes, when overexpressed, the influx of extracellular Ca(2+), leading to membrane permeability and host cell necrosis. SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the orthopoxvirus OPG166 protein family."}
{"protein": "MRVATQLRVGIVGGGWNGCHLALELKKQGHRVSLFEQKPDIFQGVSGNFGIRLHKGPHYPRSKATRDSCREALVKFCETYPELVVHHESAIYAHGEADALGNPSKVSDEAFRDVCYESPECTAVDPKANGFQGLISAYNLDEPSVAIGDRLRNTFKEKLGRAGIYVHLNATVDRIIHTEDTNRIQTGDGQYVFDVVINATGYTSLLPQNIADALPVDIGITYQTCIALVYEDQQPQEKPLSFIVMDGWFPCVMPAIDTNEPLQKKYILTHGSYTILGSFDRHEEGQELLDSLDEEAIAARIKPHCEREITRFWPGFLDRFQYRGWKGSVLAKLKTTSEFRSSLTFEKDGVIHIFPGKVSNVVTAAEEVVPLINDIARRRHGVVREWNGVRFTVSSAFHTHSKEIGDKPGLGEHHTSNLQTYVSLVTAN", "text": "FUNCTION: Probable FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of 5-hydroxy-2-hydroxymethyl- 1,4-pyrone, also know as kojic acid, a by-product in the fermentation process of malting rice that acts as a chelation agent (PubMed:20849972, PubMed:35034313). Glucose might be converted to kojic acid by a combination of dehydrogenase and dehydratase reactions involving kojA and probably additional enzymes (PubMed:20849972). SIMILARITY: Belongs to the aromatic-ring hydroxylase family."}
{"protein": "MTEITHRTKTRPVKVGNLTIGGNNEVVVQSMTTTKTHDVEATVAEIKRLEEAGCQVVRVACPDMRAAEAIPAIKKQISIPLVVDIHFDYKLALKAIEGGADKIRINPGNIGKRHKVEAVVKAAKEKGIPIRIGVNAGSLEKRILDKYGYPTADGMVESALHHIKILEDLDFHDIIVSMKASDVNLAIEAYEKAAKAFDYPLHLGITESGTLFAGTVKSAAGLGAILNMGIGNTVRVSLSADPVEEVKVARELLKSFGLASNAATLISCPTCGRIEIDLISIANEMEEYISKIRAPIKVAVLGCAVNGPGEAREADIGIAGARGEGLLFRKGEIVRKVPEETMVEELKKEIDKIAEEYFAKQKELEKA", "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": "MTHCFIRALLRQPVERTPVWMMRQAGRYLPEYREVRERAGSFMNLCTSPELACEVTLQPLERYRLDAAILFSDILTVPDAMGLGLEFVEGEGPRFRNPIRGAADIHRLGVPDPEAELAYVPAAVRLIKQRLGDRAPLIGFSGSPWTLATYMVEGGSSREFRKVKCLMYEEPALMHELLEKLADAVALYLNAQIAAGVDAVMVFDTWGGNLDTEHYLAFSLRYAERVRQQLRLTGRGRIPAIFFTKGGGQWLEAMADAGYDALGLDWTTDIGSARQRVGDRVALQGNLDPVALYARPEIIRGEVRKILERYGRGSGHVFNLGHGVTPDIKPEHVGAMIEAVHEFSPAFHRT", "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": "MALLQISEPGMAPAPHQRRLAVGIDLGTTNSLVAAVRNSVPEVLPDDAGRVLLPSVVRYLENGGRRIGHDAKAQAATDPRNTIVSVKRFMGRGKAEVEGAANAPYEFVDAPGMVQIRTVDGVKSPVEVSAEILATLRQRAEDTLGDELVGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDNAAEGLYAVYDLGGGTFDLSILKLTKGVFEVLAAGGDSALGGDDFDHALFDHVLAQAGLDAKTLAPEDVRLLLDRVRVLKEALSSAPEAALDVTLSNGAHLAQTISHDTFATLVEPLVQRTLTPTRKALRDAQVTPADIKGVVLVGGATRMPVIREAVAKYFGQPPLVNLDPDQVVALGAAIQADLLAGNRGSGDDWLLLDVIPLSLGVETMGGLVEKIIPRNSTIPIARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMTAGAARIRVTYQVDADGLLSVFAREQHSGVEASVVVKPSYGLADDDIAKMLEDSFKTAEVDMRARALREAQVEAERMIEATQAALAADGELLDAVERAEIDARVAALRTIAQGDDADAIEAATKALADGTDEFAARRMDKSIKRALSGRRLDEI", "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": "MSMQDPIADMFTRIRNGLSAEKEFVSVPFSKIKMEIANFLVNEGYIKSCSKGTTSMGHPSIEIELKYHAGVPVIEMIKRVSRPSLRIYKSHADLPKVYGGYGVAIVSTSKGLVSDRKARDLGVGGEIIGYVA", "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": "MKVAVIGAAGGIGQALALLLKNRLPAGSDLALYDIAPVTPGVAADLSHIPTPVSIKGYAGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAEVLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEGVEFTDEEIAALTTRIQNAGTEVVEAKAGGGSATLSMGQAACRFGLALVKALQGEENVIECAYVEGEGEHAPFFAQPVKLGKEGAEAILSYGELSDFERNALDSMLETLNGDIEIGVEFAK", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family."}
{"protein": "MASKLKTFINLRDYPITLFNQIRSLSSRILTPINQSHYRKRILLANLLQRYGFPPSSLQHFLSRNNHLLNSDLVETEISLGILLSLKIPQKSLVSLISDCPNVLRSEFLRKWRVPLSNCGKHGVVSSSAIKSVLEHSSRIGIGPDKFNECVRVLKSLGFCDSTVSRILSSFPGVLLVNEIEIRRKIEFLVGIGIARDNIERFFHVFPEVLGIGTETRLKPLLDEFMKMGFSKDDVKKEIAREPRVLGLELGELPRCLELINTLKCREVIRVSIISEGAFRAGFEVKLRVDCLCKYGLIRRDAFKVVWKEPRVILYEIEDIEKKIEFLTNRMGFHINCLADVPEYLGVNLQKQIVPRYNVIDYLKLKGGLGCDIGLKGLIKPSMKRFYNLYVMPYPECERIFGKRKENVRVNKRHPAGLWKLMKPPSNLTTKEDVQNMKSFIESLA", "text": "FUNCTION: Transcription termination factor required for mitochondrial NAD2 intron 3 splicing and normal membrane respiratory chain Complex I activity. Essential for normal plant growth and development. Binds to RNA but not to double-stranded DNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mTERF family."}
{"protein": "MSVVGIIAEFNPFHSGHEFLLNQARLIAGNDPIVVVMSGNYVQRGEMAIMSKYQRAKVALQSGADLVFETPFSTAVEPADLFSLGNIEQLAKLGVTDLVFGVENANLNFAYLGSKIAEIPQNHMDFKDYSQTYSTQYNQMVAREVGHEVNQPNAILGLAYAVANHNLGSPLKLHPVNRIGAGHDDLLQRNGVVQSASAIRNLLLHGEDTSNLKYWVPKAEAIELSKQEIYPNWNLLYPFLKYRIESSSIDDLRQIYQMSEGLEYKMKQEIHLSRDFTEFLRRIKSKRYTYSRLRRLSLYTLLNVTQDDMIASFNEESLMLLGFSKTGRQYLKKNRKDFQTEIISKVDKRSAKSGSLALQVRTDRLFEQIMGVDQNFGQRPIEV", "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": "MTKKRVLSGVQPTGAIHIGNWLGAIRNWVSLQNEYDTYVCVVDLHAITVPHDPQQLKENTLRTAALYVACGMDPKKCSIFVQSHISAHSELCWLLNCVTPLNWMERMIQFKEKAIKQGDNVSIGLLDYPVLMAADILLYDADLVPVGEDQKQHLELARDIAQQRVNSRFNKESKSILKIPKPLIMKEGGKIMSLIDGNMKMSKSDPNENSRIALLDSPEIIKKKIKRAKTDSFLGLEFDNNQRPEANNLLGIYSMVSNQNREAVQKEFSNIGWGKFKPILTDAIIESLNPIQQKYYSLIKDKTELNNILNKGYIKANTISNQTLKRVRNALGFLDKPIS", "text": "FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MAAKVEPFWIRKTLEHLDQEEWESLCDGCGLCCLQKLEDEDDNSVYYTRIACKLLDLKTCQCTDYPNRRASVPDCIQLTPGQADQFKWLPPTCGYRLVSERNDLPLWHHLVCGDRDAVHHERISQSGRMLSEGSVPEDDWEDYLIFRAG", "text": "SIMILARITY: Belongs to the UPF0260 family."}
{"protein": "MLFSCRAPSLLQRTALSSPLRLFAPCRPSFSRTFVTTTVRFSVEMETVNTSERLAQLRELMKQNNLDVYIVPSEDSHQSEYIAHCDARREFISGFTGSAGTAVISTTAAALSTDGRYFNQAAKQLDSNWKLLKRGLEGVLTWQEWTAEQAEGGKIVGVDPSVITAASARKLSETLEKGGSKLVGIEQNLVDQIWGTHRPQRPSEKVKIHPIEYAGKPFQEKIADLRKELKTKKRAGFIVSVLDEIAWLFNLRGNDIPYNPVFFSYAVITPDTVDLYIDDEKLSPEVKVHLGSDVVIKPYESIFADAKALSAKAPLTESGAPMKYLTSNKASWALSLSFGGEKKLDEARSPISDAKAIKNEVELKGMRDCHIRDGAALTEYFAWLENELINKKSTLDEVDGADKLEQIRSKHDKFVGLSFDTISSTGPNAAVIHYKPEKGVCSVIDPNAIYLCDSGAQYLDGTTDTTRTFHFSTPTEMEKKAFTLVLKGLIALDTAVFPKGTSGFALDALARQHLWRQGLDYLHGTGHGVGAYLNVHEGPIGVGTRIQYSEVSLSPGNVISDEPGYYEDGKFGIRIENIIMAREVETPYKFGDKPWLGFEHVTMTPIGQNLIETSLLSKEERQWVDNYHAEVWEKTSGFFKQDELTLNWLKKETQPLK", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MALRHFLTLRDLSTLELNRILERASELKKMQQSNKVYQPFVGKVLGMIFEKSSTRTRISFEAGINQFGGSAIFLSPRDTQLGRGEPIEDSARVISSMLDIVMIRTFGHDIVERFASYSKVPVINGLTDDHHPCQLLADLQTYIEHRGSIEGKTVAWIGDGNNMCNSYIEAAHMMGFKLKIASPKGYEPKPEFLAEFGHCVELFDNAEDAAVNADLIVTDVWASMGQEEEQKLREKAFANFQVNEKLMGLAHPDCLFMHCLPAHRGEEISETMLDHKNAVVWDEAENRLHAQKALMEFLLNENLKKA", "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": "MEYTPSPKPQLSSRANAFSIAALMSSGTPKDKETQESTIKPLEQFVEKSSCSQPLGDISIVDSHGEFTNSPSSLCTEPLIPTTPVIPSEEMAKISCSLETKELWDKFHDLGTEMIITKSGRRMFPTIRVSFSGVDADAKYIVLMDIVPVDNKRYRYAYHRSSWLVAGKADPPLPARLYVHPDSPFTGEQLLKQMVSFEKVKLTNNELDQHGHIILNSMHKYQPRVHIIKKKDHTASLLNLKSEEFRTFIFQETVFTAVTAYQNQLITKLKIDSNPFAKGFRDSSRLTDIERESVESLIQKHSYARSPIRTYGDEDVLGEDGQTMQSRGSAFTTSENLSLSSWVSSTSGFSGFQHPQSLTALGTSTASLATPIPHPIQGTLPPYSRLGMPITPSALASSMQGSGPTFPSFHMPRYHHYFQQGPYAAIQGLRHSSAVMTPFV", "text": "FUNCTION: Transcriptional regulator that may be involved in heart developmental processes. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MFAKLQRIHFVGIGGIGMSGIAEVLLNLGYKVSGSDLKPSAVTERLESLGAKVFEGHRASNVEGAEVVVTSSAIDSRNPEVAEAHANHIPVIQRAEMLAELMRLKYGIAIAGMHGKTTTTSMVAAVLAGGELDPTVIVGGRVDAMGSNARLGKSHYLVAEADESDRSFLKLWFIHAVVTNIDREHMDTYHDMEDVERTFVEFMDRVPFYGMVVACNDNEPLRAILPRVRRRIVTYGTTEGSDFLIRCVPCDSEQLLLGFLNRFSVEYRGKSLGEFLLRVPGLHNVRNATAAIAIGVGLDIPADKIRAALAEFRGVDRRFQLKGKANDISVIDDYGHHPTEIRATLAAAKQCGFRHIHVVFQPHRYTRTRDLMDEFASSFGDADSLYLLDIYPASEQPIEGVNTEALARRITEVSGRATFYAKSFQVAAIMAATAAEPGDMILTLGAGNVSQLGPQILERLSAKKVAAE", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family."}
{"protein": "MTDVPEPVRKCASLLKGTKSDTEKFAALFMVTKLVKGKDCNAAGKKLLFEAIGFPFLKKLLVSKDLPNDCPPLVYKSVALSILTCFCQEEELATHKDIIDAIPTLLEIVEQADDEDYEDNLIVVSEAYSCLKSIASHEPGQQALLATGAIPKMSQIYSAQSFQTDEALHLIVLLVKQFGVVSWPEDPTAFHALIQRIALDMETDDTERKYELCRILADILITCRREIVINSLEGQIWPESLFKGCGDILKAKIGPKQRDPALHLIATTLHVLGIQWAFMDEQKTFFLQLLQLGAIEVRMQMDEKKLETTFKQAELLTCCFSILEHCIEYMATDQLDLEPKEKQTTYTALKGAFNQVLAVLTRVSQDKIRESSNPKDKKFVFAIVKVLSAWLAQETTAMRPAIYKLLPFMLKVANESFQELKTWRAGTREGEPPIDVLRIMLPALCHFAVEEEARRVLFTHKQDEVLLESLEFYFSIAHWKRPPIPRAERLKRMNEPDPVPTPEQQAEMKVARSAIVALCNILMNFTVLEPKKAEDGPTFANLLKFVVENLPELKDTPDNLVIHGNLAVLGLLLLKQQSKKVKQNDFSICRYIQATIRFLWDAYNIDESNDPTALVVSIAYKGYWSDLSELWFLGMQTMCGVLPLVPWLSEFALESGWAEGIVKTLKKVKIGTLPANVKSAYEDFLSQLVDVNGDVQAVLKKADALRVCRNHRMMDLGKKLFGD", "text": "FUNCTION: Strongly up-regulated in Mhc mutants suggesting a role in muscle function. SIMILARITY: Belongs to the neurochondrin family."}
{"protein": "MRVKDTLNLGKTKFPMRGNLPKREAEWEKNWEDQKFYERRLKLNEGHERFDLHDGPPFANGNIHMGHALNKITKDIIVRSKNMEGYYAPYVPGWDTHGLPIEQQLTKQGVDRKTMDRAAYRELCRKFAMEQVEKQRTDFKRLGVMGDWDHPYITLLPEFEAAEIRVFGKMYENGYIYQGKKPVYWSWSSESTLAEAEVEYHDVESPSIYISFPVKDGKGKLSEENTYFLIWTTTPWTIPSNQGIAVNPKFDYSVVEVGDRRYVVGTDRLSAVAEILGWDSYKTVQHLKGTDMEYMVAKHPYIEGRDSLLMEAVYVTDDDGTGLVHTASGFGEDDYNTAMRYGFDVLSPMDNKGCFTEEIPDPDLVGKFYTDTNEIVKDKLSAAGNLLHYSTFVHSAAHDWRTKKPVVYRATTQWFASISKFRDQILDQIEKTTFYPAWGKTRLYNMIKDRGDWVISRQRAWGVPLPIFYAEDGTAIVTHETIEHVADLFAKEGSNAWFTHPVEELLPEGFTSEHSPNGKFTKETDILDVWFDSGSSWSGVQALGRAVHYPTSMYLEGSDQYRGWFNSSLITSVATNGVAPYKSVLSQGFTLDGQGRKMSKSLGNTIAPNDVIKQMGAEIIRLWVASVDASGDVGVSMDILRQVSEGYRKIRNTFRYMLANTADFDPEKDRVAYKDLCKIDQYLEVKLNDLVAESIVNYDKYDFADVYKLVFKFITNDLSAFYLDFAKDVLYIEGKDSHARRSMQTVIYDAAVKLAKILAPILPHTMGEVWGYLKEKEEDVYLSNFPEIEDYADADDLKESWGEFMKLRDDVLKALEEARDQKLIGKSFEASVTVYPGEAAKAALDKLAGEDFREILIVSNLVMGQGEVPAEAKQFDQASVLVRRAEGEVCPRCRMYRTDLGADSRLPQLCGRCASIVAGDHPEILEEGLED", "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": "MGDKIWLPFPVLLLAALPPVLLPGAAGFTPSLDSDFTFTLPAGQKECFYQPMPLKASLEIEYQVLDGAGLDIDFHLASPEGKTLVFEQRKSDGVHTVETEVGDYMFCFDNTFSTISEKVIFFELILDNMGEQAQEQEDWKKYITGTDILDMKLEDILESINSIKSRLSKSGHIQTLLRAFEARDRNIQESNFDRVNFWSMVNLVVMVVVSAIQVYMLKSLFEDKRKSRT", "text": "FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle-mediated retrograde transport. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein Note=Probably cycles between compartments of the early secretatory pathway. SIMILARITY: Belongs to the EMP24/GP25L family."}
{"protein": "MSGHGAPEIDLTTLNPAETSQLKLAIVAASWHTQIMDGLLDGALRAAKDAGISEPTVLRVPGSFELPVAAARLAKHFDAVVALGVVIRGGTPHFEYVCEAATMGLTDVSVNTGVPVGFGVLTCDTEQQGLDRAGLPGSKEDKGHEAVTAALATAVTLKQYS", "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": "MPRVKTGTNRRRRHKKVLKLAKGYRGTKGNLFRIANQQVMKSLTYAYRDRKQRKREFRRLWISRINAACRQNGISYNKFINGLKKAGVEINRKMLADMAVNDEQAFGELVDLAKKSV", "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": "MNQTLMEIKERALSQINASDTLDALNEIRVNFLGKKGELTSVLKSMKDVAPEDRPKVGQLVNEARESLEEALESKKEAFGKVLREAKMKAETIDVTLPAKKPMLGHRHPNTIALEEAERIFVGMGYEVVEGPEIEYDYYNFEALNIPANHPAKDEQDTFYVTSNILLRTQTSPVQVHVMEQGKLPIRMIAPGRVFRSDEVDATHSPSFHQIEGLVIDKNITFADLKGTLAEFAKQLFGEETKVKFRPHHFPFTEPSAEVDVSCFKCGGKGCRFCKGSGWIEILGCGMVHPRVLEMSGIDPEEYTGFAFGVGLERIALLKYEIDDMRLLYENDMRFLKQF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MRTTVAILLVLFALSAILAFYPDTTAEAKGCVKKVDCVCKGKGKKNHRSMCINGKCYCLKG", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKTDDFDYKLPEELIASYPLENRDASRLLKLNKQTGEIADHKFTDFIDFISPGDLLVFNNSKVMLARLYGSKTTGAKLEYLIERIKNPKLFETHIKANRSPAIGSEIYVEDTLAKVLDKDGGMYLLEIQGDKDIYQLMEEFGHIPLPPYMKRDDEEFDAERYQTVYAQDLGSVAAPTAGLHFSKELMQQIKNKGVDIAYITLHVGSGTFKPVQVDDVESHKMHAEVISVPVEVCQKIRQTKENGGRVIAIGTTSVRSLETAGQNGQIEPYQGETDIFLYPGKKFNVVDAMITNFHLPKSTLIMLVSAFADKEKIIKAYEHAIAERYRFFSYGDAMFIY", "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": "MTTLYTVINWLLLFGYWLLIAGVTLRVMMKRRAVPSAMAWLLVIYILPLVGIITYLLFGELNLGKRRAERSKALWPSTAKWIEDLKGCRRIFASENSEVARALFQLCEHRQGMGGLKGNQMQLLTSSDDALRALVRDIGLAQKNIEIVFYIWQSGGLVDQVAEALMAVARRGVRCRLMLDSAGSVDFFRSPYPALMRAAGVHVVEALHVSLLRVFLRRMDLRQHRKMVLIDNYVAYTGSMNMVDPRFFKQDAGVGQWIDIMARMEGPVATAMGIIFSCDWEIETGERILPPLPDVNIMPFEQATGHTIQVIASGPGFPEGVIHQALLTSIYAAREQLVMTTPYLVPSDDLLQAICTAAQLGVEVHIIVPRHNDSMLVGWASRAFFAELLEAGVLIHQFEGGLLHTKSVLVDGQLSLVGTVNLDMRSLWLNFEITLVIDDDDFGSDLARVQEDYIARSRLIEPKVWSKRPYWQRIVERLFYFFSPLL", "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": "MTFLFLILVFIIEILQLSVFPPIFGNAYIVPSLAFLLVLFSSYKIKEKALLLAFLSGLFYDAVVNFLGFISLLNVVFTYLYLVLNNILFVKNPKVEVFLIMPLILLLRKLTIFLVVNTKFPLNIGLKDFGVVLLIDLIFLILLYKVFNKYVYEKA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MKMIVGLGNPGSKYAKTKHNIGFMVIDQLCEKYNVTLNKHDFEAEYGSFKYEGETVLLVKPLTFMNDSGRSVGPLMSYYQVGIDELLVIQDDMDLTMGKLRLRQKGSAGGHNGIKSIIAHTKSQTFKRLKIGIQHPQKSTVVNWVLTPFDKDGAPVINQAIDQACEAIDDWCQNDDFMKTMNKFN", "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": "MVGIFNIVIDEENFKVLDSSLHFEVEAGLMYPSVSVVSWMGLANVFEAGMNASILILPKDAFGNNISFSGKKMEFQEFSLSLISENGSFAGVLNSTHIRWIVSGYISIDFVLVTSGKFLLLVEKESQTLNGGPLPLEVNSGPLDVSNCVSIWKSELSTWQIFSKMEILLHQKDRFGNIVSGFYEFDADVVEVETGLSIPVADFQFEYVEPGIQLMSFTLSEPGNFLLTLSDMKHNKSISSMPYVYTVYIGYCDGSRSIVNGSGINASIAGESLGFSVYLKDAYGYPSPVQVDRLQVRIVLEIDSSIILPTIQPREALNGTGSSHQAATPLYEKHGGRASGNLVTQASIFDVTYTPKRTGIYRIFISSGNIVLNGGQPFIKEVYAGEVNVAACSVTQFNGKVPKEIKNEIVVLLLDGFYNPVPSQPSRLKFEITSANTSSFTTWEFVDNNDGTYTGSYLAMEVGTYRMCISFDNKHIQPCPFDVNVYSNGYFPRAYDDPVNVWEDESISFNPLENDYFAGDNASMLGFSQPGHGSLLRDGNLLRYTPMKNFSGNDSFLYTIADINGNLAAATVYIFVLTAPPQFVSFSGGLQATEDLISPRYGGFSGLEISYSDLLENISVMVQALSGSVILSPMLMQFRPPGSGKLSVSNGGEDRRVLILEGQVGVINPALQSIQYLGNENFAGVDSLRLSTKNKNGINHLDVPVFVEPVNDPPFINVPQYIMLESNGSESLIFHPERDKFNFSVGDPDLVNFPGGESHFLVTFSLEVTDGFLLTNLPSELINSTELKFKNLFQWQPIQTYAAISKHVNVKASGIRFRGTIRQCNDLMQQLLHRGGENGAVLTLKLSDMGNYGCFLDCTERISLPLHAEARVNLIRKRPLSSLGAHGTFMKYLVVVPFSFFSIKLFSLLMVLIG", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MNGILNVYKPIGITSFDVVCQIKKITGIKKIGHTGTLDPLACGVLPVCIGKGTKVVDYLMKDFKVYDATFKLGIITDTYDREGKELSISEVNVSLDEIECAVNSFLGDSFQVPPMYSALKVNGKRLYELAREGKSIEREARPITIYDINILHIDIPYVKFRVKCSKGTYIRSLCYDIGSNLKCGATMWDLERVQSGAFTKENSIELNKLTTDNINDYIISIDESLNQYDKAFVSSKCEKLLVNGVRIGDKRLLPNLDINKMYRIYSEDNKFLGLGMRNSKGLKIEKLLL", "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": "MAEKTANDLKLSEIELVDFRIYGMQEGVPYEGIYGINVAKVQEIIPMPTLFEYPTNLDYIIGVFDLRSIIIPLIDLAKWIGIIPDKSKENEKIVIITEFNNVKMGFLVHSARRIRRISWKDVEPASFSASNSINKENITGTTRIENDKTLLILDLESILDDLKLNEDAKNAKDTHKERFEGEVLFLDDSKTARKTLKNHLSKLGFSITEAVDGEDGLNKLEMLFKKYGDDLRKHLKFIISDVEMPKMDGYHFLFKLQKDPRFAYIPVIFNSSICDNYSAERAKEMGAVAYLVKFDAEKFTEEISKILDKNA", "text": "FUNCTION: Plays a role in chemotaxis signal transduction system in order to colonize the host stomach. May act as a phosphate sink to control the flow of phosphate to CheAY."}
{"protein": "MPWTILLFAAGSLAIPAPSIRLVPPYPSSQEDPIHIACMAPGNFPGANFTLYRGGQVVQLLQAPTDQRGVTFNLSGGSSKAPGGPFHCQYGVLGELNQSQLSDLSEPVNVSFPVPTWILVLSLSLAGALFLLAGLVAVALVVRKVKLRNLQKKRDRESCWAQINFDSTDMSFDNSLFTVSAKTMPEEDPATLDDHSGTTATPSNSRTRKRPTSTSSSPETPEFSTFRACQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MQKDALNNVRITDEQVLMTPEQLKAAFPLSLAQEAQIAQSRGIISDIIAGRDPRLLVVCGPCSIHDPETALEYARRFKALAAEVSDSLYLVMRVYFEKPRTTVGWKGLINDPHMDGSFDVEAGLKIARQLLVELVNMGLPLATEALDPNSPQYLGDLFSWSAIGARTTESQTHREMASGLSMPVGFKNGTDGSLATAINAMRAAAQPHRFVGINQAGQVALLQTQGNPHGHVILRGGKAPNYSPADVAQCEKEMEQAGLRPSLMVDCSHGNSNKDYRRQPAVAESVVAQIKDGNRSIIGLMIESNIHEGNQSSEQPRSEMKYGVSVTDACISWEMTDALLREIHKDLSGQLAVRVA", "text": "FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). SIMILARITY: Belongs to the class-I DAHP synthase family."}
{"protein": "MREILHIQGGQCGNQIGSKFWEVICDEHGIDSTGRYSGDTADLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSIRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDAVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLSTPSFGDLNHLISATMSGVTCSLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYISLTVPELTQQMWDSKNMMCAADPRHGRYLTASAIFRGQMSTKEVDEQILNIQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMAATFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQYQDATADEEGEYDVEEEEEGDYET", "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": "MAPAVAVVAAAAAFPFRLFSAEARRNTKGSRSKRGSARPLKPSPPPRPSASSSAAGGGGATTFTRLPLRNAPASVEVTLDRFPTANPEPRASTFTRRNGERLGDDEEDEEEEEDEVELGLRGATTFARLPLRDSPDGGDLTIGHFDAGVAPQEGLRSRAISRQLVEHLDDVEEEEEEQVVSRLDIFEGAKGREARAFLPDEDDEDDDVVVFDPEYDGYSDDEEFVATAVEQSPRGDAIAVAELEKLKYDNDDDDDDDDEVVVFHPDDDEEVDVFEDYDDDEEEETKEKGVPAVMRCFDTAKIYAKAGDGGNGVVAFRREKYVPLGGPSGGDGGRGGNVFVEVDGDMNSLLPFRKSVHFRAGRGAHGQGRQQAGAKGDDVVVKVPPGTVVRSAAGDVELLELMRPGQRALLLPGGRGGRGNAAFKSGTNKAPRIAEKGEKGPEMWIDLELKLVADVGIVGAPNAGKSTLLTAISAAKPTIANYPFTTLLPNLGVVSLDFDATMVVADLPGLLEGAHRGYGLGHEFLRHSERCSVLVHVVDGSGEQPEYEFEAVRLELELFSPSLVDKPYIVVYNKMDLPEASERWNKFQEKLQAEGIEPYCISAMNRQGTEDVVLAAYKVLQKDRQRMKDDEEWNGPENLNHVADAIKRERRAPMNEFEIFHDKGTNTWNVVGAGIERFVQMTNWQYSESLKRFQHALEACGVNKTLIKRGVKEGDTVVVGEMEMVWTDEPSKTRSSKTMNSKDDSVRWPEFG", "text": "FUNCTION: Probable GTP-binding protein that plays a crucial role in chloroplast development and is required for leaf greening during plant growth. FUNCTION: Probable GTP-binding protein that may play a role in chloroplast development. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family."}
{"protein": "MRELVHIQGGQCGNQIGAKFWEVISDEHGVDPTGSYHGDSDLQLERINVYYNEATGTYVPRAILMDLEPGTMDSVRAGPYGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKIREEYPDRIMCTYSVCPSPKVSDTVVEPYNATLSVHQLVENADEVMCLDNEALYDICFRTLKLTNPTYGDLNHLVCAAMSGITTLLRFPGQLNSVLKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQQFDAKNMMCAADPRHGRYLTAACMFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKASVCDIPPKGLKMSTTFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFDEDEEMDEMM", "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": "MTSLSVNDRKDFVDGQMKYWRQIAESDGFDIDDVPVPRGTRAGLWSVDCKHPRFRLRACLPKIYAMVGLHRYNLLRGTNFEHLELLKYNESMNCVCSYYITSVAVDLSSQLQKTFQIRVDEKSFGDLDLTVSVARPNDEEKVTTEKRFIHHFHCEAAADDFYKGALPDWPSVGDLNNQKRFYMVKKCELQSNDWIRLYLELAVGVRYQQTSESDLSKLQVLKVAIETKEEDVQPPNRRLKSKSLHVYITFKGLAKAPIGDEIGEHVERKAIVRRVIDERSGHLTLLGGFSNAKNDLNQSSDDEQPFGKRRRI", "text": "SIMILARITY: Belongs to the UPF0725 (EMB2204) family."}
{"protein": "MVDEELFDKSSNDHSISSEEEDMLVRSYSNLNVSFGYHCNSYQCFSLDTDEYDISPNKRLETNTMMTSQNGSFTCLSGAAISANFTLANTNICKGLIGEEILPELDSPNSFRKIVSSPSMSRLDLLSTSQGSPVSTESSIFEISKNIWRSSAPTTVSSNFLTSTEIKMAGGAAGEDRVQAVCSEKNGWLICGIYDGFNGRDAADFLAVTLYDNIVYYLYLLECRIKQENGLYGSPEGSLNGVKSELTLAMRFAENEDVKFSETFRAGVLKCLTTAVEQAENDFLCMVEQEMDDRPDLVSVGSCVLVVLLHGTDLCILNLGDSRAVLASVPSSGMDKLKAVQLTEIHSLENPLEYQKLLADHPNEPSVVMGNKIKGKLKVTRAFGVGYLKQKKLNDALMGILRVRNLCSPPYVYTNPHTVSHKVTEDDLFVVLGSDGLFDFFSNDEVVQLVYQFMHDNPIGDPAKYLIEQLLLKAAKEAALTAEELMRIPVGSRRKYHDDVTIIVIILGNAQRTMTASTSL", "text": "SIMILARITY: Belongs to the PP2C family."}
{"protein": "MEFSTQSTASLHQIKTAALAVGVYADGELSPAADVIDRASNNAVRQVVKAEFRGRPGATLVLRALPGVSAQRVVLVGLGKQSEYNARAHAAAEQGFAAACVAARITEAVSTLAANSIADTPIRARARSAAIAAGAATYHYDATFGKPDRDARPKLKKIVQVVERGEAAQTQQGLREGSAIAHGMELTRTLGNLPGNVCTPTYLGDTARKLAREFKSLKVEVLDRKQVEALGMGSFLSVARGSDEPLRFIVLRHAGKPAKKSKAGPVVLVGKGITFDAGGISLKPAATMDEMKYDMCGAASVLGTFRALAELELPLDVVGLIAACENLPSGKANKPGDIVTSMSGQTIEILNTDAEGRLVLCDALTYAERFKPSAVVDIATLTGACVVALGHVNTGLFTQDDALADALLAAGRQSLDTAWRMPMDDAYQDQLKSNFADVANIGGPPAGSVTAACFLSRFAKAYRWAHLDIAGTAWRSGKDKGATGRPVPLLMQFLLDQA", "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": "MLKRILVIIGLAVLATACSNAPRTVSHQVISENDDIQLTGLINNLEKDNRTGIFHKVRTNRSSALMGDKALASVYNEWVGTRYRMGGTTKRGIDCSAFMQTTFSEVFGIELPRSTAEQRHLGRKINKSELKKGDLVFFRKNNHVGVYIGNNQFMHASTGQGVTISSLDEKYWARTYTQSRRIM", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the peptidase C40 family."}
{"protein": "MAKDIKFSEEARRSMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGLRKGIEKAVTAAIEELKTISKPIEGKSSIAQVAAISAADEEVGQLIAEAMERVGNDGVITLEESKGFTTELDVVEGMQFDRGYASPYMITDSDKMEAVLDNPYILITDKKISNIQEILPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFNVVAVKAPGFGDRRKAMLEDIAILTGGEVITEELGRDLKSATVESLGRAGKVVVTKENTTVVEGVGSTEQIEARIGQIRAQLEETTSEFDREKLQERLAKLAGGVPVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVAGGGTSLMNVYTKVASIVAEGDEATGINIVLRALEEPVRQIAINAGLEGSVVVERLKGEKVGVGFNAATGEWVNMLESGIVDPAKVTRSALQNAASVAAMFLTTEAVVADKPEPNAPAMPDMGGMGMGGMGGMM", "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": "MSSVPLSVYLVLALILFCIGLYGALTKRNTVIVLICIELMLNAVNINLVAFAKYGAHPGIAGQIFALFTITVAAAEAAVGLAILMALYRNRKTVHIDEIDSMKH", "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": "MDYEFLRDITGVVKVRMSMGHEVVGHWFNEEVKENLALLDEVEQAAHALKGSERSWQRAGHEYTLWMDAEEVMVRANQLEFAGDEMEEGMNYYDEESLSLCGVEDFLQVVAAYRNFVQQK", "text": "SIMILARITY: Belongs to the UPF0231 family."}
{"protein": "MMNPLIIKLGGVLLDSEEALERLFTALVNYRESHQRPLIIVHGGGCVVDELMKQLNLPVKKKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHHIASVGLYLGDGDSVKVTQLDEELGHVGLAQPGSPKLINTLLEGGFLPVVSSIGVTEEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKAEQLIDQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLPALFNGTPIGTRILA", "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": "MSTIGAVDILNQKTITSEVAASVTSKYLQSTFSKGNTSHIEDKRFIHVSSRSHSRFTSTPITPNEILSLKFHVSGSSMAYSRMDGSLTVWFIKDASFDKSVEVYIPDCCGSDKLATDLSWNPTSLNQIAVVSNSSEISLLLINEKSLTASKLRTLSLGSKTKVNTCLYDPLGNWLLAATKSEKIYLFDVKKDHSSVCSLNISDISQEDNDVVYSLAWSNGGSHIFIGFKSGYLAILKAKHGILEVCTKIKAHTGPITEIKMDPWGRNFITGSIDGNCYVWNMKSLCCELIINDLNSAVTTLDVCHLGKILGICTEDEMVYFYDLNSGNLLHSKSLANYKTDPVLKFYPDKSWYIMSGKNDTLSNHFVKNEKNLITYWKDMFDNTMIEKRRKNNGGGNNHNKRTSKNTDRIGKDRPSRFNSKK", "text": "FUNCTION: Component the TREX complex, which operates in coupling transcription elongation to mRNA export. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRMSCNGCRVLRKGCSEDCSIRPCLAWIKSPEAQANATVFLAKFYGRAGLMNLINAGPNHLRPGIFRSLLHEACGRIVNPIYGSVGLLWSGNWQLCQDAVEAVMKGEPVKEIATDAATIGQGPPLKIYDIRHISKDDNSAAAATGSTDLKLAKTRRAKRVSTVAIQAESEGKSDEASHDSSLSHQSEIVAAHEGESKESESNVSEVLAFSPPAVKGSGEIKLDLTLRLEPVSRAYHVVPVKKRRIGVFGTCQKESTCKTELML", "text": "SIMILARITY: Belongs to the LOB domain-containing protein family."}
{"protein": "MQNHHHQQSSYGGGYPGQAYREQHPPPNPYGYGQPSPQPGYGAPPPHNGYGQPPSGYGQPPPPTGNAVYGGRQPGMNQYQNTYSHGHQGGPPPPPTDPVAFGHGAPQGYSFQYSRCTGKRKALLIGINYFGQKGQLRGCINDVKNMSTYLNQNFGYAREDMVLLTDDQQNPMSQPTKANILRAMHWLVKDAQPNDSLFFHYSGHGGQTPDLDGDEEDGYDEVIYPVDFRQAGHIVDDEMHRIMVRPLRPGVRLTAIFDSCHSGSALDLPYIYSTQGILKEPNLAKEAGQGLLGVVSAYARGDMSGMVSTAVGFLKRATKGDEAYTRSKQTKTSPADVIMWSGSKDSQTSQDAQIGGQATGAMSWAFITALRKNPQQSYVQLLNSIRDELATKYSQKPQLSCSHPLDTNLLYVM", "text": "FUNCTION: Involved in cell death (apoptosis) (By similarity). Required for the apoptotic-like loss of membrane phospholipid asymmetry at stationary phase and facilitates growth under conditions of endoplasmic reticulum stress. SIMILARITY: Belongs to the peptidase C14B family."}
{"protein": "MEELRGYLELDRSWQRDFLYTLILQEYIYSLAHDHGFNRTIFFENAGYEKKYSFLIVKRLITRMYQQNHLILSANDSNQNEFLGQKKNLYSQMISEGFAFIVEIPFSLQLLFSLEGKEIVKSRNLRSIHSIFPFLEDKFSHLNYVLDILIPHPVHLEILVQTIRYWTKDASSLHLLRFCLYEYRNWNSRISRKQYISFFSNRNQRLFLFLYNSHVCEYESIFIFLRNQPSHLRSTFSGAFLERIYFYEKIEHLVKVFTKNFQVILWFFKDTFMHYVRYQGKSFLASKGTSLLMIKWKYYLVNFWQCSFSVWSQPRRIYINXLXNHXLDFMXFLSSVRLNPSVVRIQMLEKSFIIDNAINTFDTRVPNIPMIGSFAKAKFCNIFGHPISKPVWAYLSDSDIIDRFGRICRSLSHYYSGSSRKKSLYRIKYILRLSCARTLARKHKSTVRTFLKRLGSEFLEEFFMEEEKVLSLILPRDSYTSQRLYRGRIWYLDIFCIHDLANHE", "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": "MLPQRPQLLLLAGLLSLQSVLSQECTKYKVSTCRDCIESGPSCAWCQKLNFTGQGEPDSTRCDTRAQLLSKGCPADDIMEPKSLAETRQSQAGRQKQLSPEEVTLYLRPGQAAAFNVTFQRAKGYPIDLYYLMDLSYSMVDDLANVKKLGGDLLRALNDITESGRIGFGSFVDKTVLPFVNTHPEKLRNPCPNKEKECQPPFAFRHVLKLTDNSKQFETEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKSSNEFDYPSVGQLAHKLAESNIQPIFAVTKKMVKTYEKLTEIIPKSAVGELSEDSKNVVELIKSAYNKLSSRVFLDHNTLPDTLKVAYDSFCSNRVSQVDQPRGDCDGVQINVPITFQVKVTATECIQEQSFTIRALGFTDTVTVRVLPQCECQCREASRDRGVCGGRGSMECGVCRCDAGYIGKNCECQTHGRSSQELEGSCRKDNSSIICSGLGDCICGQCVCHTSDVPNKKIYGQFCECDNVNCERYDGQVCGGDKRGLCFCGACRCNDQYEGSACQCLKSTQGCLNLNGVECSGRGRCRCNVCQCDPGYQPPLCIDCPGCPVPCAGFAPCTECLKFDKGPFAKNCSAACGQTKLLSSPVPGGRKCKERDSEGCWMTYTLVQRDGRNRYDVHVDDMLECVKGPNIAAIVGGTVGGVVLVGILLLAIWKALTHLSDLREYHRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES", "text": "FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation. Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages. In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane raft; Single-pass type I membrane protein. SIMILARITY: Belongs to the integrin beta chain family."}
{"protein": "MSMTSPSPVTGGMVDGSVLVRMATKPPVIGLITVLFLLVIGACVYCCIRVFLAARLWRATPLGRATVAYQVLRTLGPQAGSHAPPTVGIATQEPYRTIYMPD", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein."}
{"protein": "MAGNGSAPDTATHQVRQFDQARAEAAVRELLFAIGENPDRHGLAETPARVARAYREMFAGLYTDPDSVLNTMFDEEHDELVLVKEIPLYSTCEHHLVSFHGVAHVGYIPGNDGRVTGLSKIARLVDLYAKRPQVQERLTSQIADALVKKLNPRGVIVVVEAEHLCMAMRGVRKPGAVTTTSAVRGLFKTNAASRAEALDLILRK", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I family."}
{"protein": "MNKKLLSEFGDPVQRVKNALQSLKRGNGILVLDDENRENEGDMIFAAENMTVNQMALAIRFGSGIVCICLTKEKCKILNLPMMVKKNNSKYKTAFTVSIESAYGITTGVSAYDRIITIKTAIKDNAKPDDLNRPGHVFPLQAHPGGILSRAGHTEAAVDLTKLAGLKPAGVICEVMNDDGSMARMPEIINFSKKYNMPVLIIKDIIEYYNFIN", "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": "MTETFQHISVLLNESIDGLAIKPDGIYIDGTFGRGGHSRTILSKLGENGRLYSIDRDPQAIAEAAKIDDPRFTIIHGPFSGMAKYAEEYGLVGKVDGVLLDLGVSSPQLDDAERGFSFMKDGPLDMRMDPTSGIPVSQWLMEADLDDITWVIREFGEDKHARRIAKAIVAYREDEENEPMVRTGQLAKLISDAAPKSFKEKKHPATRAFQAFRIYINSELEEIDTALKGAASILAPEGRLSVISFHSLEDRMVKRFIRKESKGPEVPHGIPMTEEQIRALGSANMKPIGKANKPTKQEIDMNPRSRSSVLRIAEKL", "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": "MARVCAITGRKARSGNSRSHAMNATKRKWGANLQKVRVRINGKVQRVYVSARALKSGKIERV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MYLTKEKKEEIFAQHGDAKNTGKAEGQIALFTYRISHLTEHLKKNRHDYNTERSLVLLVGKRRALLDYLKKKDINRYREIIKVLNIRK", "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": "MQNLPKWKIFLSIICTVFAVICALPNFMQVNSKFLPHDSVNLGLDLRGGAHLLLDVDFDTYLNDSMENLADTLRKNFREDKIGYKNLLVRQNSIQLEVRSPEELKPLKKIINKIDPEIIAEVNENKIKLSYSESRLNDLLNKVVDQSIEIVRMRVDSTGTKEPTLQKQGDKHILLQVPGEENPSYLKNILGKTAKLTFHLVDENANIEEAVKGHVPVGSMLVKGDSESHREYYVVIKKKVVLGGDQLTTASASFDQNSQAVVAFSFNNLGSKIFGEITKNNTGKRLAIVLDNKLLSAPTINGAIMGGSGIITGNFTVESANELALLLRAGSLPAPLKIIEERSIGPSLGADSIESGKKAGLIGFIAVCIFMVWSYGVLGLFANIALSLALLYILALLSLFQATLTLPGIAGIILTMGMAVDANVLIYERIKEELHKGVSNLYAIRTGFESAFATILDSNLTTLIVAFLLYIFGVGAIKGFAVALTIGIISSMFSAIIITKLLIDIWVKYFIPKKLGLV", "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": "MVALSNALSRVFGSLAGYKFPSFIQKGINALYVKIFKIDLSEFEPLENYRSLNALFTRSLKKERPFDKSPNICIAPCDALITECAFLDNDSALQIKGMPYKAHELVGEINPLSPSFFYANFYLSPKDYHHYHAPCDLEILEARYFAGKLLPVNKPSLHKNNNLFVGNERVTLVAKDIQGNRLYFVAVGALNVGKMRFNFDKNIQTNAKARFTQTYSYNPPIKVKKGDNLGNFEMGSTIVLFIQNTAFKDLKEKNVKFGESIGEFHAN", "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": "MAGDVEGFCSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFGVNIEGVREKLDAFLLDNFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQSWLRHDRRRWRHTDTIIQNIRFCLMTPSSVFEKVKTSEFYRYSRQLRYEVDQALNYFQNVHQQPLLDMKSSRIRSAKPQTTVFRGMIGHSMVNSKILLLKKPRVWWELEGPQVPLRPDCLAIVNNFVFLLGGEELGPDGEFHASSKVFRYDPRQNSWLRMADMSVPRSEFAVGVIGKFIYAVAGRTRDETFYSTERYDITNDKWEFVDPYPVNKYGHEGTVLNNKLFITGGITSSSTSKQVCVFDPSKEGTIEQRTRRTQVVTNCWENKSKMNYARCFHKMISYNGKLYVFGGVCVILRASFESQGCPSTEVYNPDTDQWTILASMPIGRSGHGVTVLDKQIMVLGGLCYNGHYSDSILTFDPDENKWKEDEYPRMPCKLDGLQVCNLHFPDYVLDEVRRCN", "text": "FUNCTION: Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex. 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 and regulating PP2A holoenzyme composition. Acts as an adapter for CUL3 to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. 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). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRRLGSVQRKMPCVFVTEVKEEPSTKREHQPFKVLATETLSHKALDADIHNAIPTEKVDGTCCYVTNYKGQPYLWARLDRKPNKLAEKRFKNFLHLKQNSKEFFWNVEEDFKPVPECWIPAKEIEQINGNPIPDENGHIPGWVPVEKNSKQHCWHSSVVDYESEIALVLRHHPDDPGLLEISAVPLSDLLEQTLELIGTNINGNPYGLGSKKHPLHLLIPHGAFQIRNLPTLKHSDLLSWFDGCREGKIEGIVWHCNDGCLIKVHRHHLGLCWPIPDTYMNSKPVIINMNLNKYEYAFDAKCLFNHFSKIDNQKFGRLKDIILTV", "text": "FUNCTION: Functions as an RNA ligase, in vitro. The ligation reaction entails three nucleotidyl transfer steps. In the first step, the RNA ligase reacts with ATP in the absence of nucleic acid to form a covalent ligase-AMP intermediate and release pyrophosphate. In step 2, the ligase-AMP binds to the nucleic acid and transfers the adenylate to the 5'-PO4 terminus to form an adenylylated intermediate. In step 3, the RNA ligase directs the attack of the 3'-OH on the 5'- phosphoanhydride linkage, resulting in a repaired 3'-5' phosphodiester and release of AMP. Exhibits selectivity for single-stranded RNA substrates and may not have nick-sealing activity on double-stranded DNA-RNA hybrids. May play a role in maintaining RNA integrity under stress conditions, for example in response to reactive oxygen species (ROS)."}
{"protein": "MIIAFQFALFALVAISFILVVGVPVILASPEGWSNTKNAVFSGASLWIFLVFVVGILNSFIA", "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": "MTMSSFLINSNYVEPKFPPCEEYSQNNYIPSQSPEYYERPRDPGFHHEALYPQSNYPEPTYSFNNVQGTGNQDMSQRGHVQSQASLQNHIPRQNQLCEVVPVATPALCSQNAKNPTAQKGTLSKEPIVYPWMKKIHVTTVNPNYTGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQVKIWFQNRRMKWKKDHKLPNTKMRSASSSSSTSQQTQVSSQGPQPDGSAPNSSSL", "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": "MNKRPLIEQALKRVNNRYELVHAAAKLAKDLYETGAESYVTEEGIPLKKTVISINEIAKGRAVILRKE", "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": "MKKFGKALLALLVLLLLAAALFLYWPLTQRSVPAASNDKPVDVVLVGAGIMSITLATYLQELQPDWNIQVYERLDGVAGESSDGWNNAGTGHSAFAELNYTPELPDGSIETKRAVGIAESFEVSRQFWSHQVKEGRLSQPSDFINPTPHMSFVWGDDNIAYLHKRQQALVKNPLFYGMQYSEDPAQIKQWAPLLMEGRDPKQKVAATWMPLGTDVNFGVITRQLTAGLQRSPNFSLHLNHEVSALRQNADKSWNVTVKDLKAGTESTTHARFVFIGAGGAALKLLQMSGIPESKDYAGFPVGGQFLAFQGQDVTSRHGVKAYGMAETGSPPMSVPHLDARKLDGKPVVLFGPFALYSTKFLKHGSWWDLYSSVNHNNVGPMLEVGKDNLDLVQYLMGQARLNDADRQAELVKYFPTAKPGDWKLVTAGQRVQIIKRDPLKGPVLQFGTEIVTDKDHTLAALLGASPGASTSPPIMLDLMAKAFPDQMKAGWEARLREIVPSYGRKLNDSAALVNEIRTLTSQTLHLPYLEVPVDANAASPAAAAVPAAAKEKRNANEELQAL", "text": "SIMILARITY: Belongs to the MQO family."}
{"protein": "MSSAFKAMRLHLTCPLPKQVINIPQTLFSYLITNQRAINNSCKPVKTSNAKKPKLPTTKLSWEERLSDTVTPLWRMTYEDQLQWKYEHQKKILLKMMKELSQDPTRAFSDHLNFPLLPIVASPVRDGYRNKSTFSVNKGIDGNPKTLGFYIGTGKAGNIVCVHADHLLSIPSKHKMVARCYEDFIRLSPLRPCILFDDGGHWREITIRTNSTGHTMAIVYFHPQSLTPEETDIHKAALVEYFTQGPGAICQLDSLYFQETTMTRCSHEQSQYQLLYGQTHIYEEVLGFKFRISPDSFFQVNREAAEALYKTVAELSQPCVGGTLLDVCCGTGAIGISLSPQMERVIGIELIEQAVEDAKFNAALNRVCNCEFLAGKAEVVLPDLMGSLSSDGGLTAVVNPSRAGLHYRVVRALRNHSAIRRLVYISCKPDGEAMRNFRELCCSVGLVRRITGEAFKPVVAVPVDLFPHTPHCELVLVFER", "text": "FUNCTION: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine in tRNAs and 12S rRNA. Catalyzes the methylation of uridine at position 54 (m5U54) in all tRNAs. Specifically methylates the uridine in position 429 of 12S rRNA (m5U429). Does not affect RNA stability or mitochondrial translation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
{"protein": "VHLSSEEKGLITSLWGKIDIEQTGGEALGRLLIVYPWTSRFFDHFGDLSSAKAVLGNAKVLAHGAKVLVSFGDAIKNLDNLKGTFAKLSELHCDKLHVDPENFKLLGNVLVICLAEHFGKDFTIDAQVAWQKLVAGVANALAHKYH", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
{"protein": "MASHILLVGIGGFCGAIVRYFFSRKLNSGKLPVGTLTVNLSGAFLLGAMAGANLSTTTTLLLGTGFLGAFTTFSTLKLEMAQLQLKKEHRLFILYTTITYGGGIALAYLGYWLGSFFR", "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": "MKILITGFEPFGGEVVNPSFEAVKHLPDSIEKAQIVKAAIHTVFRKSIEVLEELIVKEKPDIVICVGQAGGRAEITIERVAINIDDAKNPDNEGNTPKDEVIFEDGENAYFSNLPIKKMVEEIKNCKIPASISNSAGTYVCNHLMYGLLYLINKKYKNMKGGFIHVPYLPQQVLNKKNVPSMSLDNIVQALVCSIKAILKEYNDE", "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": "SKSSTETPPSYNQLNYNENLQRFFNSKPATAPVEFDPIKMDQSYNEPAEAECTVSPVQCFEGSGGSGSSGNFTSGSNLNMRSVTNTSNTGTGTSSESVPLVTLTEALIS", "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": "MRVILAQPRGFCAGVVRAIEIVERALQQNGAPVYVRHEIVHNRHVVENLRNKGARFVEELDEVPHGAVAIFSAHGVAQTVEQDAQARGLDVLDATCPLVTKVHVQGRQYVAAGRRLILIGHAGHPEVEGTIGQIPAEVILVQSEAEVDTLTLPADTPVAYVTQTTLSVDDTRGIIEALQRRFTDIVGPDTRDICYATQNRQAAVRELSEQVDVLLVVGATNSSNSNRLREIGTESGVPSYLVADGSEVRAEWFANARTVGLTAGASAPEEMVEDVIAALRALGPLEVATMSGREEKVEFKLPAKLTQAVAREV", "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": "MINISTSPRQTLDWTALKPADGSPAVEWRISDSPVPYPEAVATMEARAAAIAAGEATELVWLLEHPPLYTAGTSGHASDLLEERFPLFTTGRGGQLTYHGPGQRVAYVMLDLKRRRPDVRAYVAALEQWIIATLDAFNIRGERREDRVGVWVRRPDKGVGYEDKIAAIGVRLKRWVSLHGIAINVEPDLSHFKAIVPCGISDPRYGVTSLVDLGLPVVMTDVDIALRAAFENIFGETRAAAPAGI", "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": "MAARSALCFLAIITLFVYACGRPALNFNSIYKDSRSSVKHFPRVTDSRYAYTKIDSKLDSILSELQKEQNDRDDDDDDDDEDDLFDEINDIFDDVMDDDIEEDGDDIHEVEKIEEAVDDVIDMIDDIIDDDADDDSDDVPEDLNDAQEDILELIKDSNDDKNDDETSDIIDDILDIVEDAKDADDHRPIADIRVVESLSKPGAVAEDDKESKKIDETVQELLDEIKDVVEDANDDVNDILDTDDEDEDEDVQEEKDEDIHEDVGNVMVNLMHGVHGVTGGGVNHDIYEEIEEKMDEVDDFIDDAIDEHNDDDVNDDENDDVYDEHDDLVDDVNDDADDDNDDADDDNDDADDDNDDSDDNDDSDDDNDDDDIDDVADDVLEVIVDAVEAMNTPTNV", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MEAVVNSDVFLTSNAGLKSSYTNQTLSLVDEDHIHTSDKSLSCSVCNSLSQIVDDDFISAGARNQRTKPKRAGNNQSQQPIKKDCMVSIDEVASTHDWSTRLRNDGNAIAKYLTTNKYDTSNFTIQDMLNIMNKLNIVRTNRNELFQLLTHVKSTLNNASVSVKCTHPLVLIHSRASPRIGDQLKELDKIYSPSNHHILLSTTRFQSMHFTDMSSSQDLSFIYRKPETNYYIHPILMALFGIKLPALENAYVHGDTYSLIQQLYEFRKVKSYNYMLLVNRLTEDNPIVITGVSDLISTEIQRANMHTMIRKAIMNIRMGIFYCNDDDAVDPHLMKIIHTGCSQVMTDEEQILASILSIVGFRPTLVSVARPINGISYDMKLQAAPYIVVNPMKMITTSDSPISINSKDIYSMAFDGNSGRVVFAPPNIGYGRCSGVTHIDPLGTNVMGSAVHSPVIVNGAMMFYVERRQNKNMFGGECYTGFRSLIDDTPIDVSPEIMLNGIMYRLKSAVCYKLGDQFFDCGSSDIFLKGHYTILFTENGPWMYDPLSVFNPGARNARLMRALKNQYKKLSMDSDDGFYEWLNGDGSVFAASKQQMLMNHVANFDDDLLTMEEAMSMISRHCCILIYAQDYDQYISARHITELF", "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": "MTNAVTVKNITFQEGETLICVPLIGKTLDEILGNAHGLVDAGADIIEWRVDHFAQVREMAQVMAALAEIRGALKALPLLFTFRSKKEGGETELSDEAYFALNREAARSGLVDVIDIELFNDEAQIRALVDDAHAAGVKVIMSNHDFHKTPAQEDIIYRLRRMQDLGADLPKIAVMPQSPQDVLTLLAATLTMKEKYATRPLITMSMGKSGGVSRVTGRLFGSAMTFGTVGQASAPGQIAIAKLREVMDILS", "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": "MFSLLLLTSTALVETALGVSPSYNGLGLTPQMGWNNWNTFACNVTEQLLLGTADRISELGLKDVGYNYVILDDCWSGGRSSNGSLVPDLNKFPHGMKYVADHLHDQDLLFGMYSSAGEYTCAGYPGSLGHEEKDAQFFARNEVDYLKYDNCYNKGQFGTPQASYERYKAMSDALNNTGRPIFYSLCNWGQDLTFYWGSAIANSWRMSGDITADFDRPDSRCPCGDDEYDCKYAGYHCSIMNILNKAAPMGQNANPGGWNDLDMLEVGVGNLTDDEEKAHFSMWAMVRSPLIIGADVNHLKPSSFSIYAQSPVIAINQDPRGVPATRVWRRQVSDTDAYGRGEVQFWSGPLENGDQVIAFLNGGNRMRPMNAGLDDIFFDSHPGAPELNSTWAVYDLWANRMEDSVASDILNGNRSSNGLLYNSTQQSYSQGLARNDSRLFGSQIGTIQAGGRLNVTVPAHGVGLYRLRLQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 27 family."}
{"protein": "MRVAVDVMGGDNAPHVEVEGAVAAAREFGVPVTLVGDVEKVRAELARHDCKGLDIEVWHASEVVGMHDSASDAVRKKKDSSIRVAFELVKGGEAVAVVSAGNSGATMAAGMFVLKRMKGIDRAAIAQLFPTVSGKTLVLDVGGNVDCKPIHLVQFAVMGEVYARFVMGVDNPKVGLLSNGEEASKGNELTRETSALLREKPINYIGYVEGRDIFNGSVDVVVCDGFVGNVALKLSEGLAEAVGKMLKAEIKSSFLSQIGYLLSRKAFNNFKKTVDYAEYGGAPLLGINGVGMICHGGSNPKAIKNAIRFAHEYALKGVNGRMAEKLNESFPGDAREREGAQAPDAGTERVAS", "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": "MTITGSRGFPDGYLAPGSSFLDFAAQHAPTIMPGTQPTFDTIPQDIAPHGTTIVALEYHNGIIIAGDRRATMGTTIAHREIEKVFAADEHSAIAIAGTAGLAIELVRLFQLELEHYEKIEGTPLSLDGKANRLSTMLRSHLHLALQGLPIVPIFAGWDSTRHQGRLFAYDVTGGRYEEPNFTCAGSGSVFARSALKKLWKPQLDATRAITIALEALWDAADDDTATAGPDIIRRIWPIIAVIDHKGFRYVSEADLAHANDTIAHQRSQDHQHVRVLEPGRDGPGNRLPSQGSATIIPESDQS", "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": "MELLKGNAVNLNDTAYYNNRELSWLAFNERVLQEAQDANNPLLERLKFISIFSSNLDEFFMVRVAGLKDQVSAGFNQPENKAGLTPKKQLNKIAIKAHALMTVQYDTFKNYVLPALELEGIERLTFNDLTKEQREFIEEYFDEQIFPVLTPVAIDAYRPFPMLLNKSLNLATLLYDEKQAEEENRTKLGIVQVPSLLERFIILPSEGQKHKFILLEDVISSFTHKLFTGYTVSSVTRFRITRNADLTIHEEGARDLLKVIEKELKKRKWGAAVRLEVGKEHIDERVLALLYEVLEVKDEDVYIMDGPLDLTCLFSLYKKLAPLYEHLVYPALIPQPPQDLGDEEDVFEKAIEHDILLHHPFESFQPVVDFVRDAADDPNVLAIKQTLYRVSGDSPIIQALKIAAEKGKQVTVLVELKARFDEENNVHWAKELEQAGCHVIYGVSHLKTHSKITLVVRRKNGKIERFVHLGTGNYNDATAKLYTDFGYITSRKDFGVDATNFFNYLSGYTTKPHFHHLSVAPFDIREQFMDLIDEEIRYHRQYGNGYIIAKMNSLTDKPLIKKMYEASQAGVKVELIVRGTCCLRPGIPNVSENIRVVSVVGRYLEHSRIYYFHHNGEEKIYLSSADLMTRNMEKRVEISFPILDIEMKARIKAILQLILADNVKTREQNKDGDYYYVINGSTEEIDSQVKLFKMAYQNTDAE", "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": "MVKNSIIPVISQEKKEKNPGSVEFQIFKFTDRIRRLTSHFELHRKDYLSQRGLRKILGKRQRLLSYLSKKDRIRYKKLINQFDIRESQIR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MQLRASVLLSFLGLASVGHAGNVENNHNVCTVRANGGHQDDVPNIMAAFKECGNGGTIIFPEDQSYWIATRLHPTLKDVAIEWRGKWTFSDNLTYWRNNSYPIAFQNHHAGFIISGDNITINGYGTGGIDGNGNTWYTAEKGDTQPGRPMPFVFWNVSEVIVDSFYVKDPPLWSVNIMNGTNMRFNNIYCNATAVDAPWGDNWVQNTDGFDTMDATNIQLTNFVYQGGDDCIAIKPRSYNIDIQNVTCRGGNGIAIGSLGQYLEDSSVANIRVDKVNIIRYNEDMHNSAYLKTWVGALVPQSSYESAGVPRGDGWGSIRNVLFSNFNVQGASAGPSISQDSGDNGSYAGTSKMSISNVAFVNFTGWVDTEKSVVSTVSCSEVHPCYNIDYDNVVLYPGKNATTAGTGSCKYTADGGVHGLSGC", "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": "MSNPTLTFVTGNANKLREVQQIFSLTPNFPYELTNKDLDLPEIQGTTRDVAQAKCAAAAKALGGACITEDTALGFHALGGLPGPYIKDFMKTIGHDGLNKMLDGFEDRTASAICTFAYCAGPDEQVHLFEGRTEGVIVPPRGPTHFGWDPILEIKGTGLTYAEMDPKQKNTLSHRYKALTLLQDYLVGLSKQN", "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": "MSRKQSQKDSSGFIFDLQSNTVLAQGGTFENMKEKINAVRAIVPNKSNNEIILVLQHFDNCVDKTVQAFMEGSASEVLKEWIVTGKKKNKKKKSKPKPASEASGSAPDSSKSAPIQEEQPASSEKGSINGYHVNGAINDAESVDSLSEGLETLSIDARELEDPEFAAAETLDRTGSVLENGVSDFEPKSLTAHSISNVQQSRNAAKSLSRTTPGAQVSNLGMENVPLSSTNKKLGSNIEKSVKDLQRCTVSLARYRVVVKEEMDASIKKMKQAFAELQSCLMDREVALLAEMDKVKAEAMEILLSRQKKAELLKKMTDVAVRMSEEQLVELRADIKHFVSERKYDEDLGRVARFTCDVETLKQSIDSFGQVSHPKNSYSTRSRCSLVAPVSLSGPSDGSAASSSPDASVPSLPGANKRNCAPREASAAMTNSSDRPCQAHREVFPGNRRGGQGYRAQSQKTADPSNPGRHDSVGRYRNSSWYSSGPRYQGVPPQAPGNAGERSRPYSAGTNGTGAISEPSPPKPSFKKGLPQRKPRASQAEAANS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SPATS2 family."}
{"protein": "MAAQRLGKRVLSKLQSPSRARGPGGSPSGLQKRHARVTVKYDRRELQRRLDVEKWIDGCLEELYRGRESDMPDEVNIDELLELDSEEERCRKIQGLLEACANPTEDFVQELLAKLRGLHKQPGFPQPSPSDDPSLSPRQDRAHTAPP", "text": "FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PP1 inhibitor family."}
{"protein": "MTKKAIIPAGTTKPIAPFVPGSMADGVLYVSGTLPFDKDNNVVHVGDATAQTRHVLETIKSVVETAGGTMDDVTFNMIMIRDWADYAKVNEVYAEYFAGEKPARYCIQCGLVKPEALIEIASIAHIG", "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": "MIHPSAKIHPTALIEEGAVIGEDVFIGPFCIIEGTVEIKARTVLKSHVVVRGDTVIGEDNEIYQFTSIGEVNQDLKYKGEATKTIIGNSNKIREHVTIHRGTIQGCGVTAIGNNNLLMINVHVAHDCQIKNNCILANNATLAGHVELDDFVIVGGMSAIHQFVIVGAHVMLGGGSMVSQDVPPYVMAQGNHARPFGVNLEGLKRRGFDKPTMHVIRNIYKMLYRSGKTLEEVLPEIEQIAETDSAISFFVEFFKRSTRGIIR", "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": "MFYQSSSSLTQILHSFCGNTEMETPYPKLIDPSKTRIGWIGIGIMGSAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVDMTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGTVTYMGEAGSGQSCKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAMPGAALSKQLFTGMVANGDGKLGIQGVVSVIRRLNGIS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily."}
{"protein": "MTGPTTNTKNDLMIVNMGPQHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIVQYLPYVTRWDYLATMFTEAITVNAPEQLGNIQVPQRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELIYDLFEAATGMRMMHNYFRIGGVAADLPYGWIDKCLDFCDYFLTGIDEYEKLITRNPIFLERVEGIGIISGEEAINWGLSGPMLRASGISWDLRKVDQYECYNEFDWEVQWQKEGDSLARYLVRMSEMRESIKIIQQALEGIPGGPYENLEVRRFDKTKDSEWNDFEYRFISKKPSPNFELSKQELYVRVEAPKGELGIFLIGDQNVFPWRWKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR", "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": "MGLCASKDSRESTHDGGPRVNRPGANDANRRNDVRKGAGDKKQDKKNKKAKGSIVNAASNINNSSSGKTKISTVSEDGTVSNGVGNTAEYDNANNKNNGNNNNSNNNDNNNNNNNNIGNNINGNNNNDSENIHDSNNSNIENKRYFNNINTGVLNGVNGNSTNSDKALSNQFDQSNNSETHSGTMTGISQALALNDSGVNGFDTDLAKRNGTVNASGGQSPGGSETVNALKVLLLGSGESGKSTVLQQLKILHQNGFSREELLEYKPFIFDNIIETGKDLAKARRTFNVQLEEDAEISESDLDELLSQQYQPTKLPCLPADLAKTLKILWNLQSTQDLLVSEHRSSFYLMDSASYFYENLDRISEPKYIPTITDVIRTRKKTSGIFDTMIDLDKNLKLHFFDVGGQRSERKKWIHCFDNVTLIIFCVSLSEYDQTLLEDNSQNRLEESLILFDSVVNSRWFARSSVVLFLNKIDIFAEKLRHVPLEKYFPDYTGGKDINKAAKYILWRFVQLNRANLNIYPHVTQATDTSNIKLVFAAIKETILENSLKDSGVL", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. This protein may be involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of adenylyl cyclase. SIMILARITY: Belongs to the G-alpha family."}
{"protein": "MFVKICGIKSLEELEIVEKHADATGVVVNSNSKRRIPLEKAREIIENSAIPVFLVSTMVGFSEWAMAIERTGAQYIQVHSNALPQTIDTLKKEFGVFVMKAFRVPTISKNPEEDANRLLSEISRYNADMVLLDTGAGSGKLHDLRVSSLVARKIPVIVAGGLNAENVEEVIKVVKPYGVDVSSGVEKYGIKDPKLVEEFVRRAKNVVW", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MALNLQDKQAIVAEVSEVAKGALSAVVADSRGVTVDKMTELRKAGREAGVYMRVVRNTLLRRVVEGTQFECLKDTFVGPTLIAYSMEHPGAAARLFKEFAKANAKFEVKAAAFEGELIPAAQIDRLATLPTYEEALARLMSTMKEAAAGKLVRTLAAVRDAKEAA", "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": "MSKKIKVGIVGATGYTGVELLRLLAAHPDVEVAAVTSRSEAGTAVADYFPSLRGVYGLAFQTPDEAGLEQCDIVFFATPNGIAMKDAPRLIEQGVRVIDLSADFRIRDIPTWEHWYGMTHAAPDLVSQAVYGLSELNREAVAQARLVANPGCYPTCVSLPLVPLLRQCRLKPGMPLIADCKSGVSGAGRKGNVGSLLCEVGDNFKAYGIAGHRHLPEIRQTIAGLQDGIAEGFVFTPHLAPMIRGMHATVYLHLSDGICPETILRDYYRDSLFVDILPAGSTPETRSVRGANLCRISIQQAAQSDVWVVLSVIDNLVKGAAGQAVQNMNIMFGLKETHGLGAIPLLP", "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": "MTSERIRVAILFGGRSAEHDVSRASAANIFRSLDAGRYALTLIGITHDGRWVLADAVNDATSAALIVPADGPQIVLLPAGRGRALAIDGSAAAPRELAFDVIFPVLHGPNGEDGTVQGALELADVAYVGGRVLGSAAAMDKDVAKRLLRDAGLPIVPFVTMTAASPVSYDDAARAVGSSELFVKPANLGSSVGISKTRDAAEFEAACQLALRFDRKILIERCIAPVREIECAVLEHADGQIKASELGEIVPANSHGFYSYEAKYTDANGAALHVPAQVEPAVAQRIRKMATEVFGALCCESLARVDFFVRGDEIYVNEVNTLPGFTNISMYPKMWEAAGLPQPALMDELVAHALARHARLRELASQR", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MSQPIYKRILLKLSGEALQGEDGLGIDPAILDRMAVEIKELVEMGVEVSVVLGGGNLFRGAKLAKAGMNRVVGDHMGMLATVMNGLAMRDSLFRADVNAKLMSAFQLNGICDTYNWSEAIKMLREKRVVIFSAGTGNPFFTTDSTACLRGIEIEADVVLKATKVDGVYDCDPAKNPDAKLYKNLSYAEVIDKELKVMDLSAFTLARDHGMPIRVFNMGKPGALRQVVTGTEEGTTIC", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MSRQHAYSREELLATARGELFSHSNARLPNDPMLMFDRITGIYADGGSHGKGIVNAELDIRPDLWFFGCHFLGDPVMPGCLGLDAMWQLTGFFLTWSGATPGYGRALGCGEVKFTGQVLPNAKLVRYEVEMTKIINRTLVIGQANARMLVDNREIYFAKDLRVGMFNNTESF", "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": "MKDVVLVKSLYRNTSEYSDKKVKISGWIRTLRASNAFGFIEVNDGSFFKNVQVVFDSAKISNYKEISKLPISSSISVIGTLVETPDSKQPFEIQAEEIIVEGMSDSDYPLQKKRHTFEYLRTIAHLRPRSNAFSATFRVRSVAAYAIHKFFQDQGFVYTHTPILTGSDCEGAGEMFRVTTLDMMAPPISEEGGIDFSQDFFGKETNLTVSGQLNAECFALAFRNIYTFGPTFRAENSNTVKHAAEFWMIEPEMAFADLIDDMEVAENMLKYVIKYVMDECPEEIAFFNQFVDKGLLERLNHVVNSEFGKVTYTEAVKLLQESGKEFEYPVEWGIDLQTEHERYLTEQIFKKPVFVTDYPKDIKAFYMRLNEDGKTVAAMDCLVPGIGEIIGGSQREERLDVLKARMAELNLNEEDYWWYLELRKYGETVHSGFGLGFERLIMYITGMANIRDVIPFPRTTGTAEF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MSRSLSECIDQGRGLVPADLVLKHGRVFDLVTGELVQTDVAICGDRIVGTFGTYTGRREIDCRGRILVPGFIDTHLHVESSLVTPFEFDRCVTPRGITTAICDPHEIANVCGLEGIRYFLEASAHLVMDLRVQLSSCVPSTHMETAGAALEAKDLAPLMDHPRVIGLAEFMNFPGVLMKDPGCMAKLEAFRGRHIDGHAPLLRGKDLNGYIAAGIRTEHEATTAEEALEKLRKGMRVLIREGSVSKDLHALVSILTERHAPYLCLCTDDRNPLDIAEHGHIDHMIRTAIRLGAPPLAVYRAASLSAADAFGLKDRGLIAPGRRADIAVLDSLEGCHAALVLAGGVVADDAAFSARSDIEPVARASVKVAEIAPEAFRCPGNRADTPVIGILPGKIITEHLTAEIEPVDGDKRPDPVRDLARIAVIERHGKTGGRATGFVRGFGMARGAIASTVCHDHHNLAVVGIDYADMALAANRLRALEGGFAVAAGGEILAELALPVGGLMSLRPFEEVRDALVTLREAARSLGVTLEEPFLQLAFLALPVIPHLKITDRGMVDVDRFEILP", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family."}
{"protein": "MPKMKTKSSAKKRFKVTATGKVMAGQAGKRHGMIKRHKKFIRDARGTTTLSAPDAKIVKGFMPYDR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "MTMAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYVTSEILWGYRFTPVLTLEDGFYEVDYNSFHETHETSTPSLSAKELAELANRAELPLSWSVSSKLNQHAELETEEEEKNPEELTERNGDVANLENESKV", "text": "FUNCTION: This potassium channel is controlled by G proteins. It may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters. 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 or cesium. 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": "MVELWQGLGCVFTPEKLLKFITTLTSNSNFCIAYSGGIDSHVLVHAMSHLCQEHPWQLRALHINHGLNPKANDWENHCQQICNRLKIPFQSERVTLSLQPGDSIEAVARKARYAIFQQALSENETLLTAHTENDQAETFLLQLLRGAGVKGLSAMPAKRKLGKGELVRPLLAITRDDLKKYAEKNNLRWVEDDTNLELRFNRNYLRHEVLPILRRRWPEVFAVISRSANHCAEAALLLDQLAESDLQLIQKDSELEILPLLQLTPERQRNVLRRWIYLHGFQLPQTKQLEQIRNDVLLAAHDANPVFSYHTIEIRRHHGKLYLSNALSAHNATPLISWNFSRSLPLPGDLGTLIAEKKKGVGIKTTLDTSKITVRFRQGGEQCQPAGRKETHTLKKLMQEWKIPVWQRDRVPLIYLGDKLIAVVGYCICEGFEAKGEEWGWNVEVQPPK", "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": "MADLIPLAQARCVPRKGSDHKLGEARLAELLPQVPGWELSEGGQALLRTFRFKNYYATMAFVNALAWIAHHEDHHPDLGVHYDRAVVRFSTHDVGGLSENDFICAAKTSALTEQLP", "text": "SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
{"protein": "MEKVSIVCFFFFLLFGSGYGGLPPFWRATVVTMTNLIGGPPLTIHCKSKQDDLGIHVVPFKQEYHFKFQPNLWKSTLFFCSFQWDSQFKSFDIYDAQRDQGICDDCQWEIKPDGPCRLGKKAKCFPWK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant self-incompatibility (S1) protein family."}
{"protein": "MASVQLRNVTKAWGDVVVSKDINLDIHDGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGETRMNDIPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVMNQRVNQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQIWLPVESRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGSACRRLHQEPGV", "text": "FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. 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. 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": "MSCEVLALTEELINRQSVTPEDAGCQQLMAEYLAPLGFDIESMVFDDTTNMWARKGTGGPVFCFAGHTDVVPSGPAEKWTFPPFTATQHEGQLYGRGAADMKGSLAAMLVATKAFVTKHPEHSGSIAFLITSDEEGPFINGTTRVIDTLEARNEKMTWCLVGEPSSTTLIGDVVKNGRRGSLTGDITVKGVQGHVAYPHLAKNPIHLSAPAFAELAQTHWDSGNASFPPTSFQVSNINSGTGAGNVIPGDLSACFNFRFSTEVTDKQLIERVTTILDKYDFDYHIDWTFNGQPFLTDSGKLVEATQSAIKDVTGRETELSTAGGTSDGRFIAPTGAQVIELGPINATIHKIDENVNINDLAQLAKIYEGILQRLLA", "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": "MGSGKPPLILASGSPRRKALLEALGYPIRVAVPGVEEEGLPLPPKALAQALARRKGEAVQGEWVLAADTVVDLDGEVLGKPKDPEENRLFLRRLSGRPHLVHTAFYLRTPKEVVEEVHTAKVFFRPLSEEEIAWYVGSGEGLDKAGGYGAQGLGMALLERVEGDFYTVVGLPVSRVFALLWARGFRP", "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": "MQLGAFRNRGVTVPDCLPGFGHINRYWDPEHQVFAAKILPGEFYVTRGNEMIVTTLGSCVSACVRDRRLGVGGMNHFMLPVRGGDPNHWEGDPLSTATRYGNHAMEQLINRVLALGGQRQELEVKLFGGGRVLAGVTDVGKRNIEFAESYVRTEGLRLIGRDLGGQYPRKVQYFPESGRARSKKLLRTRNDTVVRREEHYLHEIDEQPVSGDVDLF", "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": "MKITAKAWAKTNLHLGVGPARDDGFHELMTVFQTIDLFDTVTLTTLDEELVEEGSVVKQLSVTGARGVPEDASNLAWRAVDALVKRRAEKTPLSAVSLHISKGIPVAGGMAGGSADAAATLRAVDAWIGPFGEDTLLEVAAELGSDVPFCLLGGTMRGTGRGEQLVDMLTRGKLHWVVAAMAHGLSTPEVFKKHDELNPESHMDISDLSAALLTGNTAEVGRWLHNDLTSAALSLRPELRSVLQEGIRSGAHAGIVSGSGPTTVFLCESEHKAQDVKEALIDAGQVYAAYTATGPAASTADQRGAHILTVSQ", "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": "MQPWLWLVFSVKLSALWGSSALLQTPSSLLVQTNQTAKMSCEAKTFPKGTTIYWLRELQDSNKNKHFEFLASRTSTKGIKYGERVKKNMTLSFNSTLPFLKIMDVKPEDSGFYFCAMVGSPMVVFGTGTKLTVVDVLPTTAPTKKTTLKKKQCPTPHPKTQKGLTCGLITLSLLVACILVLLVSLSVAIHFHCMRRRARIHFMKQFHK", "text": "FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A palmitoylation site in the cytoplasmic tail of CD8B chain contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. Once LCK recruited, it initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical role in thymic selection of CD8+ T- cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Requires the partner CD8A for efficient cell surface expression. The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail palmitoylation."}
{"protein": "MDLNNRLTEDEALEQAYDIFLELAADNLDPADILLFNLQFEERGGAELFDPAEDWAEHVDFDLNPDFFAEVVIGLAEQEGEEITDIFARVLICREKDHKLCHILWKE", "text": "SIMILARITY: Belongs to the UPF0263 family."}
{"protein": "MDPLNLSWYDDDLERQNWSRPFNGSEGKADRPHYNYYAMLLTLLIFIIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMIAIVWVLSFTISCPLLFGLNNTDQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRKRRKRVNTKRSSRAFRANLKTPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRMDAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSNPDSPAKPEKNGHAKIVNPRIAKFFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFMKILHC", "text": "FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (PubMed:1321233). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MAETGSVHATRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATQGPCNIPRPGFWDPIGRYKWDAWSALGDMSKEEAMIAYVEEMKKILESMPMTDKVEELLQVIGPFYEIVEDKKNRGSGLTSDLSNVMNSTPNIKAVNGKAESSDSGAESEEEGLREEEEKELQQNVKDCKSPKTESLAAKDLENSVANDCYKDSFIPDMQNGIQTKSALNGLNVEEEIKKTEPSLEIANNCDHRGANEENTEEVSGTQHLTSDSDSEVYCDSMEQLGLEEPLEIITSAKGSLKRSSHFLDVDHRLQLENTDLPRHACTTAGNLQLGTAVDGAVQEKGEVKCGGEDGKASNGAPHKEKKDGEKADFYGVRRGRGHRLHPVGDGSQGGQMGNGGDGERWGSDRGPRGSLNEQIAVVLMRLQEDMQNVLQRLHMLEAVTASQARSATLQSNYQPASSVKKPSWWPFEISPGVLAFAIVWPFIAQWLVHVYLQRKRRKLN", "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 (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATG37 family."}
{"protein": "MDHIRNFSIIAHIDHGKSTLADRIIQRCGGLSDREMEAQVLDSMDIEKERGITIKAQTAALSYKARDGQVYNLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTAIELGVEVVPVLNKIDLPQADPANAIQEIEDVIGIDAQDATPCSAKTGQGVEDVIEALIAKVPPPKGDAAAPLQALIIDSWFDNYVGVVMLVRVVNGTLRPKDKVLLMATGAQHLVEQVGVFSPKSIQRDELTAGQVGFVIAGIKELKAAKVGDTITTMTRRAEAPLPGFKEVKPQVFAGLYPVESNQYEALRESLEKLRLNDASLQFEPEVSQALGFGFRCGFLGLLHMEIVQERLEREFDMDLITTAPTVVYQVQQRDGTVLTVENPAKMPDPSKIEAILEPIVTVNLYMPQDYVGSVMTLCTQKRGAQINMSYHGKQVQLTYEIPMAEIVMDFFDRLKSVSRGYASMDYEFKEYRQSDVVKVDILINSDKVDALSVIVHRSNSQYRGREVAAKMREIIPRQMYDVAIQAAIGSNIIARENVKALRKNVLAKCYGGDISRKKKLLEKQKAGKKRMKQVGTVEIPQEAFLAILQVDDK", "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": "MSSTSQKHRDFVAEPMGEKSVQCLAGIGDTLGRRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDACSANAKQSRDCYGCLKEWCDAFL", "text": "FUNCTION: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response; acts by inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. SUBCELLULAR LOCATION: Nucleus Chromosome Nucleus envelope Cytoplasm Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. SIMILARITY: Belongs to the BAF family."}
{"protein": "MYETYHSGWIECITGSMFSGKSEELIRRLRRGIYAKQKVVVFKPAIDDRYHKEKVVSHDGNELEAINISTSRDILLQDLSHVDVIGIDEIQFFDKEIVNIVEKLAENGHRVVVAGLDMDFRGEPFEPMPQIMAVSEQVTKLQAVCAVCGSSSSRTQRLIDGQPAKVDDPIILVGANESYEPRCRAHHIVAPSTSDEEEM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thymidine kinase family."}
{"protein": "MEICTYFKSQPTWLLILFVLGSISIFKFIFTLLRSFYIYFLRPSKNLRRYGSWAIITGPTDGIGKAFAFQLAQKGLNLILVARNPDKLKDVSDSIRSKYSQTQILTVVMDFSGDIDEGVKRIKESIEGLDVGILINNAGMSYPYAKYFHEVDEELINNLIKINVEGTTKVTQAVLPNMLKRKKGAIINMGSGAAALIPSYPFYSVYAGAKTYVDQFTKCLHVEYKKSGIDVQCQVPLYVATKMTKIRRASFLVASPEGYAKAALRFVGYEAQCTPYWPHALMGAVVSALPESVFESFNIKRCLQIRKKGLQKDSMKKE", "text": "FUNCTION: Beta-ketoacyl-coenzyme A reductase required for the elongation of fatty acids precursors of sphingolipids, triacylglycerols, cuticular waxes and suberin. Responsible for the first reduction step in very long-chain fatty acids (VLCFAs) synthesis. Decreased expression of KCR1 (RNAi) leads to plants with fused vegetative and reproductive organs, and abnormal trichome, epidermal cell and root morphology. Cannot be complemented by KCR2. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MANTTGRIPLWLIGTVAGILVLGLLGIFFYGSYSGLGSSL", "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": "MVCEKCERKLGTVITPDTWKDGARNTTESGGRKLNENKALTSKKARFDPYGKNKFAICRICKSSVHQPGSHYCQGCAYKKGICSMCGKKVLDTKNYKQTSV", "text": "FUNCTION: As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CRIPT family."}
{"protein": "MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL", "text": "FUNCTION: Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:2293021, PubMed:10684867, PubMed:26968463, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:23922390, PubMed:24847884, PubMed:26394692, PubMed:29596046, PubMed:21098034). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (PubMed:23922390, PubMed:26394692, PubMed:29596046). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity). Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (PubMed:9830016, PubMed:26394692) (Probable). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (PubMed:21098034). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (PubMed:21098034). Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I. FUNCTION: (Microbial infection) The membrane-associated isoform acts as an entry receptor for varicella-zoster virus (VZV). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane Secreted Note=Present at the cell surface of neuron cells. The membrane- associated isoform is approximately 5 kDa larger than the known cytosolic isoform. SIMILARITY: Belongs to the peptidase M16 family."}
{"protein": "MGSKTPDGHRQGPNESSTGGTIAVLNPPKSASASGLVQDASGEDDEDGDDDEEKAGTDLNSRAQPNNDGKKRKRKNNKKKKKKRPLSGQQTTPPRVALSSIFSGQRYPEGEIVKYVTNDDNLQRTTAEELRHLSVVNNMDDTFLSDYRQAAEVHRQVRRYVQTIAKPGISMSELAQEIEDGVRALTGHQGIETGDALKAGLAFPTGLCLNNVAAHWTPNPGTKEVILGHDDVLKIDFGVHVHGRIVDSAFTVAFNPVYDNLLTAVRAATNTGLKEAGIDARIDHISGEIQEVMESYEVEINGNLIPVKALRSLSGHNILRYKIHGEKQVPFVKSKTTQRMEEGDVFAIETFGSTGKGYTRDEAGVYGYGLNEHVSATGLRHASAKSLLKTIRENFGTLVFSRRYLEHMGVKNYHLGMRSLISNDIVECYAPLVDVPGSYVAQFEHTVLLRPNCKEVISRGDDY", "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": "MGEVQREKVAVIIGPTAVGKTKLSIDLAKALNGEIVSGDSMQIYRTMDIGTAKVTTDEMDGIPHYMIDIKDPEDSFSVAEFQESVRKCIREITERGKLPIIVGGTGLYIQSVLFDYQFTDEAGDATYREQMEKLALEHGVEYVHKKLQEVDPESAERIHANNVRRVIRALEIFHTTGEKMSNQLEKQENELLYDVSLIGLTMDREMLYDRINLRVNLMIEQGLLEEVKGLHERGVRDCQSIQAIGYKEIYDYFENRVSLEEAVSQLKTNSRRYAKRQLTWFRNKMDVGWFDVTDGEKTSEILRYIEGKLQLKSNNSK", "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": "MSTKVELYMEIGTVITDLEYHTKYMLKKLLGRGAYAQCYLAEIESGEQYAMKVVRLKDIKSRKVHEKLESEIAIHSKLDNPNVVKMYRSFRSSEYVFMVLELCERGALDALLKRNGKLKERHVARFVKQTVEGLIYLHNSVSVVHRDLKLGNLFLDSKFNVKIGDFGLSAVIKDGEKKVTMCGTPNYIAPEVLFGKASGHSFEADIWSLGVIIYTLLVGVPPFQKKNVEDIYKMIKLNNYIFPENCDLSSEAIDLITQILNTNPLERPTLEHILSHKFLSKKEHFLMKIYRNLMTNRTEEGVVDTDYVLFSIPVTKLRGVGYVLKSGVYGIYFSDHRNLMLKPNRKSVIYLNSTIESGKRVFYKEEHLVEKIPAEIAESYKGLQYFIRTFDNGFSFLDVEPCFIVKIRKIECGFLFVMADSTIVFDFVDGWRVVLSRCGERVSCYNGLGLASFNQEIRGRCIEILRGCLGCG", "text": "FUNCTION: Protein kinase required for the cell cycle where it is involved in mitotic exit. Required to form a bipolar spindle, the actin ring and septum. Functions upstream of the whole septum formation pathway, including actin ring formation (regulated by late septation genes) and septal material deposition (regulated by early septation genes). Behaves as a 'septum-promoting factor', and could also be involved in inducing other late events of cell division (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
{"protein": "MNLHEYQAKALLKKYGVSVQEGILARSAEEAVAAFEQLGGKFAVIKAQVHAGGRGKAGGVKVVKSKEEAADYANQLIGTNLVTYQTDANGQPVNSVLVCEDVYPVERELYLGAVVDRSSRRVTFMASTEGGVEIEKVAEETPEKIIKVEVDPLVGLQPFQAREVAFALGLKDKQIGQFVKLMAGAYQAFVENDFALFEINPLSVRENGDILAVDAKIGIDSNALYRLPEIAASRDKSQENERELKASEFELNYVALEGNIGCMVNGAGLAMATMDIIKLYGGQPANFLDVGGGATKERVIEAFKLILADTSVQGVLINIFGGIVRCDMIAEAIIAAVQEVNVTVPVVVRLEGNNAELGAKILDESGLKLTSANGLSDAAEKIVAAVKG", "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": "MRPEDLNDLSLLGQKSVPYIFEYQPEVLEAFPNRHPENDYFVKFNAPEFTSLCPITNQPDFATIYISYIPDEKLVESKSLKLYLFSFRNHGDFHENCINVIGKDLVKLMEPRYLEVWGKFTPRGGISIDPYYNYGKPGTKYEQMAEHRLFNHDLYPETIDNR", "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": "MKMNLPPFIELYRALIATPSISATDSALDQSNHTLINLLAGWFGDLGFHVEVQPVPGTLNKFNMLARIGEGKGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDIDPTKLTKPLYVLATADEETTMAGAKYFSESTQIRPDCAIIGEPTSLQPVRAHKGHMSNAIRIQGQSGHSSDPSRGVNAIELMHEAISHLLVLRNTLQERYHNPIFHIPYPTMNLGHIHGGDAANRICGCCELHMDIRPLPGITLNDLDGLLSEALEPVSQRWPGRLTISELHPPIPGYECPPDHRLVSVVEKLLGTKTEIVNYCTEAPFIQTLCPTLVLGPGSIEQAHQPDEYIDTKFIKPTRELISQVIHHFCHH", "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": "MPYDKKAVHFGGGNIGRGFVAEFLHNSGYEVVFVDVMDSIIEALQKQSSYTVTEIGDDGEREFTIDHYRALNSKHEMDKVVQEIASADVVTCAVGPNILKFVAEPVAKAIDARTLDYPIAVIACENAINATTTWRGFIEGKLSEDSKSNLDKKARFANSAIDRIVPVQDKDAGLNVKIEKFYEWCVEQKPFENGGKKPDVKGIHYVDDLEPYIERKLFTVNTSHATAAYYGHQAKKQYIHEVLQDKKLHDIVRDAVKETAHLIVSKHGVSVQEQNDYVDSIIKRISNPVLKDNVERVGRAPLRKLSRKERFVGPAAQLAERGEKVDALLGAIEQAYLFQNVEGDEESAELAKILKENSAEEVVTKVNGLDKSHPLFEKILPIVKKVQGGS", "text": "FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Required for the process of sporulation on senescing leaf material. SIMILARITY: Belongs to the mannitol dehydrogenase family."}
{"protein": "MPKKVFCGTVTKAKCDKTVKVSVLQVYKDELYKKVIKKYKKYTAHDENNSCKEGDKVLIQEHKPISTTKKWVIVNSSH", "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": "MKFIIEREQLLKPLQQVSGPLGGRPTLPILGNLLLKVTENTLSLTGTDLEMEMMARVSLSQSHEIGATTVPARKFFDIWRGLPEGAEISVELDGDRLLVRSGRSRFSLSTLPASDFPNLDDWQSEVEFTLPQATLKRLIESTQFSMAHQDVRYYLNGMLFETENTELRTVATDGHRLAVCAMDIGQSLPGHSVIVPRKGVIELMRLLDGSGESLLQLQIGSNNLRAHVGDFIFTSKLVDGRFPDYRRVLPKNPTKTVIAGCDILKQAFSRAAILSNEKFRGVRINLTNGQLKITANNPEQEEAEEIVDVQYQGEEMEIGFNVSYLLDVLNTLKCEEVKLLLTDAVSSVQVENVASAAAAYVVMPMRL", "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": "MKTLYSLRRFYPVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVLDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSIVFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRALVWSGEAYLSYSLGALSIFGFVACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN", "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": "MKHFQSKVLTAAILAALSGSAMADNPPPSTDEIAKAALVNSYNNTQDINGFKVGDTIYDINGNGKITRKTATEDDVKADDFGGLGLKEVLAQHDQSLADLTGTVDENSEALVKTAEVVNDISADVKANTAAIGENKAAIAKKADQTALDAVSEKVTANETAIGKKANSADVYTKAEVYTKQESDNRFVKIGDRIGNLNTTANGLETRLADAEKSVADHGTRLASAEKSITEHGTRLNGLDRTVSDLRKETRQGLAEQAALSGLFQPYNVGRFNVTAAVGGYKSESAVAIGTGFRFTENFAAKAGVAVGTSSGSSAAYHVGVNYEW", "text": "FUNCTION: An antigenic bacterial cell surface protein that adheres to and induces bacterial uptake by human epithelial cells. SUBCELLULAR LOCATION: Cell surface Cell outer membrane. SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family."}
{"protein": "MEILPVGEESLGVRSMCLYVETRDVRILFDAGVSLAPRRFGLPPHPRELERARSVRGEIVRLAQQADIITVSHYHRDHFTPWYPSVYMATDGETYKKVYGGKKVLMKSPADLNWSQRRRHYGLAKALQEAGAKAVYADGGEWRIGGTVIRASPPLWHGPAGSKTGRVIAFAVSDGEERLVFVPDVEGPVEPEPVAFLEEVKPTVVVVGGPPTYLGWELERALQRLTEIIDIGPHTLVLAHHLLRDLAWREKIEAVLQRAEKRGVRVATYAGLLGRKDELLEAMRRDLYAAEPAAAQPAEEGIDEGD", "text": "SIMILARITY: Belongs to the UPF0282 family."}
{"protein": "MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYAGNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL", "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 (PubMed:11179971). Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases (PubMed:2110137). Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate (PubMed:20026068). SUBCELLULAR LOCATION: Secreted Note=Secreted in an Xcp-dependent fashion (a type II secretion pathway). SIMILARITY: Belongs to the peptidase M23A family."}
{"protein": "MTDLIKLDAATLAAKIAAREVSATEVTQACLDQIAATDAEYHAFLHVAGDQALAAAATVDKAIHEATAAGERLPSPLAGVPLALKDVFTTTDMPTTCGSKILEGWTSPYDATVTAKLRAAGIPILGKTNMDEFAMGSSTENSAYGPTRNPWNVDCVPGGSGGGSAAALAAFQAPLAIGSDTGGSIRQPAALTATVGVKPTYGTVSRYGLIACASSLDQGGPCARTVLDTALLHQVIAGHDPRDSTSVNAAVPDVVGAARAGARGDLKGVRIGVVKQLRSGEGYQPGVLASFTAAVEQLTALGAEVSEVDCPHFDHSLAAYYLILPSEVSSNLAKFDGMRYGLRVGDDGTTSAEEVMAMTRAAGFGAEVKRRIMIGTYALSAGYYDAYYNQAQKVRTLIARDLDEAYRSVDVLVSPATPSTAFRLGEKVDDPLAMYLFDLCTLPLNLAGHCGMSVPSGLSADDNLPVGLQIMAPALADDRLYRVGAAYEAARGPLPTAL", "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": "MQENQQITKKEQYSLNKLQKRLRRNVGEAIADFNMIEEGDRIMVCLSGGKDSYTMLEILRNLQQSAPINFSLVAVNLDQKQPGFPEHVLPEYLEKLGVEYKIVEENTYGIVKEKIPEGKTTCSLCSRLRRGILYRTATELGTTKIALGHHRDDILQTLFLNMFYGGKMKGMPPKLMSDDGKHIVIRPLAYCREKDIQRFADAKAFPIIPCNLCGSQPNLQRQVIADMLRDWDKRYPGRIETMFSAMQNVVPSHLCDTNLFDFKGITHGSEVVNGGDLAFDREEIPLQPAGWQPEEDENQLDELRLNVVEVK", "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": "MGRLFLCLVVAWCWVALLLVAPVHGRVGLPGEFSGDQRPVPATSFDLVTEPKTKQPRGVKGTRRPSWSSWSSTASRSSPPPGRGAPSAAAAAELRSVPAGPDPMHHHGSPRRPEHARSTGRP", "text": "FUNCTION: Probable extracellular signal that regulates meristem maintenance. May function as a putative ligand for a receptor complex including FON1. Regulates the size of the floral meristem and the number of floral organs. FUNCTION: Probable extracellular signal that regulates meristem maintenance. May function as a putative ligand for a receptor complex including FON1. Regulates the size of the floral meristem and the number of floral organs (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CLV3/ESR signal peptide family."}
{"protein": "MSNVDRAEIAKFEALAHRWWDRESEFKPLHDINPLRVNWIDERANLAGKKVLDVGCGGGILSEAMALRGATVTGIDMGEAPLAVAQLHQLESGVSVEYRQITAEDLAEEMPEQFDVVTCLEMLEHVPDPSSVIRACHRMVKPGGQVFFSTINRNPKAYLFAVVGAEYILNLLPRGTHDFKKFIRPSELGAWSRDAGLQVKDIIGLTYNPLTKHYKLASDVDVNYMIQTLREA", "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": "MTIKREMRNDKRAVPKAPINENISAREVRLIGADGEQVGIVSIDEALRIADEAKLDLVEISADAVPPVCKVMDYGKHLFEKKKQANEAKKNQKQIQIKEIKFRPGTEDGDYQVKLRNLVRFLTDGDKAKISLRFRGREMAHQELGMELLKRVEADLAEYGTVEQHPKMEGRQLMMVIAPKKKK", "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": "MAPKAEKKPAAKKPAEEEPAAEKAPAGKKPKAEKRVPAGKSAGKEGGEGKRGRKKGKKSVETYKIYIFKVLKQVHPDIGISSKAMSIMNSFINDIFEKLAAEAAKLARYNKKPTITSREIQTSVRLVLPGELAKHAVSEGTKAVTKFTSS", "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": "MAKQTVADLKDIKGKKVLVRVDFNVPIKGGVIGDDNRIVAALPTIQYIIDNGGKAILLSHLGRIKSDEDKKELTLKPVAARLGELLNKDVAFVASNEGQELEDAINAMTDGQVLVMENTRFQDIDNDFGKRESKNDPKLGEYWASLGDMFVNDAFGTAHRAHASNVGIATAMKANNKPAVAGYLLEKEIKFLGEAVDAPERPFVAILGGAKVSDKIGVIEHLLAKADKVIVGGGMTYTFYAAKGLSIGNSLVEEDKIELAKELIEKAGDKLVLPVDNVVADAFSNDAKTETVEGNIPDGYMALDIGPKAIADFENVLKDAKTVVWNGPMGVFEMDNFAKGTLAIGEFLGNLSGATTIVGGGDSTAAVKKLGVGDKLTHISTGGGASLEYLEGKTLPGIAAISDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MTENVQLGALLAACHWIGEKGWCPATGGNMSLRLDSAQCLVTESGKDKGSLTADDFLLVETANNHVPSGRTPSAETGLHTLLYRLYPEINAVLHTHSVNATVLSRVERSNELVLHGYEMQKSLSGQRSHLDSVVIPIFDNDQDIPALAQRVAALADNHPLRYGFLVRGHGLYCWGNSVSEARRHLEGLEFLFQCELQRRLLDANFKLGAK", "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": "MINIVLFGKPGAGKGTQAEFLKEKYNLTHLSTGDIFRFNIKNETELGKLAKTFMDKGDLVPDAVTIKMLESEVDKNQHSKGFLFDGFPRTLAQAAALDTFLASKDQEVTATIALEADDEILVQRLLERGKTSGRVDDQDEEKIRNRYQEYNEKTAPLMSYYKNNKKFHAVNGIGTIQEITKRLSEVINNL", "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": "MKKLFALVATLMLSVSAYAAQFKEGEHYQVLKTPASSSPVVNEFFSFYCPHCNTFEPIIAQLKQQLPEGAKFQKNHVSFMGGNMGQAMSKAYATMIALEVEDKMVPVMFNRIHTLRKPPKDEQELRQIFLDEGIDAAKFDAAYNGFAVDSMVRRFDKQFQDSGLTGVPAVVVNNRYLVQGQSVKSLDEYFDLVNYLLTLK", "text": "FUNCTION: Involved in disulfide-bond formation. Required for the functional maturation of secreted virulence factors. Acts by transferring its disulfide bond to other proteins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily."}
{"protein": "MRILKPYLRSTSIQCYLCLLLNSHFLTEACIPVFILSCINAGLPKTEANWQDVISDLKIIDKIIQSLHIDATLYTESDVHPNCKVTAMKCFLLELHVISLESKNETIHQTVENIIILANSGLSSNRNITETGCKECEELEEKNIKEFLQSFVHIVQMFINTS", "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": "MEAVLNELVSVEDLLKFERKFKSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGLALLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS", "text": "FUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. 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. May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event. Also mediates peroxisomal fission. May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FIS1 family."}
{"protein": "MHKSVQDIVNMKKGKKKVSVITGYDYTLASLCDKAGIDVLLVGDSAGMVMLGYENTIPVTMDQMCMFTEAVSRARNNALLVADLPFMSYQASIEDAINNSGKLIKAGADAVKLEGGSIMAETISAIVDVGIPVMGHIGLQPQTTMLSQGYKVQGRTKDSAMQLIQDAKELEEAGVFSIALEMVSHEVAQIISETVSAPTIGIGSGVNCDGQVLVVQDLLGMYDKIKPKFAKRYMNLSEDIVKSLEDYKNDVESNTFPAEENWFSMDPEELKKLREQIGS", "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": "MPKPDIHPTWYPDAKVICNGEVVMTTGSTQPEINVDVWSGNHPFFTGTQKILDTEGRVDRFMRKYGMGSVDNATSEKKSATDETSKES", "text": "FUNCTION: Binds the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily."}
{"protein": "MVAPMYGSPGGRLARAVTRALALALVLALLVGLFLSGLTGAIPTPRGQRGRGMPVPPASRCRSLLLDPETGQLRLVDGRHPDAVAWANLTNAIRETGWAFLELHTNGRFNDSLQAYAAGVVEAAVSEELIYMYWMNTVVNYCGPFEYEVGYCERLKNFLEANLEWMQKEMELNNGSAYWHQVRLTLLQLKGLEDSYEGSVAFPTGKFTVKPLGFLLLQISGDLEDLEVALNKTKTNHAMGSGSCSALIKLLPGQRDLLVAHNTWHSYQYMLRIMKKYWFQFREGPQAESTRAPGNKVIFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVQPTGCVLEWMRNVVANRLALDGDSWADIFKRFNSGTYNNQWMIVDYKAFVPGGPSPGRRVLTVLEQIPGMVVVADRTSELYQKTYWASYNIPSFESVFNASGLPALVARYGPWFSYDGSPRAQIFRRNHSLVHDLDSMMRLMRYNDFLHDPLSLCKACTPKPNGENAISARSDLNPANGSYPFQALHQRSHGGIDVKVTSTALAKALRLLAVSGPTWDQLPPFQWSTSPFSGMLHMGQPDLRKFSPIEVSWD", "text": "FUNCTION: Putative phospholipase. SUBCELLULAR LOCATION: Lysosome lumen. SIMILARITY: Belongs to the phospholipase B-like family."}
{"protein": "MKKPFPFSAIVGQEQMKQAMVLTAIDPGIGGVLVFGDRGTGKSTAVRALAALLPLIKAVEGCPVNSARPEDCPEWAHVSSTTMIERPTPVVDLPLGVTEDRVVGALDIERALTRGEKAFEPGLLARANRGYLYIDEVNLLEDHIVDLLLDVAQSGENVVEREGLSIRHPARFVLVGSGNPEEGELRPQLLDRFGLSVEVRSPRDVETRVEVITRRDAYDADHDAFMEKWGAEDMQLRGRILGARAALPQLKTPNTVLHDCAALCIALGSDGLRGELTLLRAARAQAAFEGAEAVGRSHLRSVATMALSHRLRRDPLDEAGSVSRVERCVAEVLP", "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": "MIYPGRGASLSVAVALVLFSSGAPWTFREEKEDVDREVCSESKIATTKYPCVKSTGEVTTCYRKKCCEGFKFVLGQCIPEDYDVCAGAPCEQQCTDHFGRVVCTCYDGYRYDRERHRNREKPYCLDIDECANNNETVCSQMCVNTPGSYRCDCHSGFYLEDDGKTCTKGERAPLFEKSDNVMKEGTCSATCEDFHQMKMTVLQLKQKMSLLSSNTEINKQMTNEKMMMTTNSFLPGPPGPPGPAGTPGAKGSSGSPGQMGPPGLPGPRGDMGPIGPSPDLSHIKQGRRGPVGPPGAPGRDGMKGERGFPGPSGPPGPPGSFDFLLLMMADIRNDIAELQSKVFSRPLHSSFEDFPSAPDSWRDTPENLDFGSGEDYKSQSPPKSSRKRKLPRNLKNPDWPV", "text": "FUNCTION: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis. Necessary for lymphangiogenesis, but is probably not part of either the vegfc-vegfr3 signaling or sox18-prox1 transcriptional pathways. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CCBE1 family."}
{"protein": "MQCIETNNLQQLLEQVKPYTKKGKLATYIPELGNANPDDLGIAIFHKETEYIHAGNSQTLFTLQSISKVITLALALLDRGQEYVFSKVGMEPTGDPFNSIIKLETTSPSKPLNPMINAGALAITSMLAGKDNEEKMERILHFVREITDNPTINYSSKVANSELETAYLNRSLCYYMKQNGIIDCDIEELMDLYTRQCAVEVNCIDLARIGLIFAMDGYDPYKKKQIIPKHITKICKTFMVTCGMYNESGEFAIRVGIPAKSGVAGGIFGCVKGEMGIGIFGPALDANGNSIAGFKILELLSAQEGWSIF", "text": "SIMILARITY: Belongs to the glutaminase family."}
{"protein": "MLLLVLLFVFISATNASDVGRRELEKHFDVGDSSLDSVGDVLLKLKKLAHQRAFGNREFGHDAEEDSKKPVAISVLQPTVAKDVSPYLFEGDIFLSKKQAINILKEVSGIESKSKPNVRGRRSFDASPESKWPTTAPIKYRFHESIDFYAVSNIIKAIRYWENVTCLEFENSPDVADNEDFIEFFQGQGCYSMIGRNGGRQGVSIGENCVKAGVIEHEIGHAIGMWHEQSRPDAQSYIKVESDFILPSYVSDFLQRDKDIDTLGLPYDLGSVMHYGSTAFSVDQSSKTLITRDPLYQSTIGQRETLSFLDIETINKAYCSDRCSGSNDCKNGGYPHPKQCDTCLCPNGLSGPKCEDFEPPRKAECGGKIVVKEEWQSIESPGFPDPGYDPDQKCNWVFEVAGKRIEFEFIEEFSFLCTSTCVDYVEMKISADLRPTGFRWCCFNIPKGSFVSELNIAVIIFRSQLTNDVGFKLQARATDLPARTTPAPVVITTTPVPTTIEGTDQWAEWGSWSQCSRSCGGCGIMSRVRVCRTKQCKGRRQEFSTCNLKACPIDKHCAKLLANDKICNGRVCTKASQALSGCLEPQCCPPFINVDGTCQSDSPLLNDFELAK", "text": "FUNCTION: Metalloprotease (PubMed:20800010). Involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MQSMNVQPRVLAVGGEQFFSQRQASEQHQQQNMGPQVYSPKVNRARMFPQGMPVNTINGSVNQEMNNAYLLKQKNEPLLTQQQQQQQQQQQPFNIGTPVSVASLPPGLNVLQQQQQQQQQQQQQQQGVGLNRPLASQLPKHLTNQSMPPIFLPPPNYLFVRDVWKSNLYSEFAVIRQLVSQYNHVSISTEFVGTLARPIGTFRSKVDYHYQTMRANVDFLNPIQLGLSLSDANGNKPDNGPSTWQFNFEFDPKKEIMSTESLELLRKSGINFEKHENLGIDVFEFSQLLMDSGLMMDDSVTWITYHAAYDLGFLINILMNDSMPNNKEDFEWWVHQYMPNFYDLNLVYKIIQEFKNPQLQQSSQQQQQQQYSLTTLADELGLPRFSIFTTTGGQSLLMLLSFCQLSKLSMHKFPNGTDFAKYQGVIYGIDGDQ", "text": "FUNCTION: Acts as probably 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. In vitro, POP2 has 3'-exoribonuclease activity with a preference for poly(A) RNAs, but also degrades poly(U) and poly(C) RNAs. Is part of a glucose-sensing system involved in growth control in response to glucose availability. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CAF1 family."}
{"protein": "MCQVCGAAEADLHFGGISCRACAAFFRRFFLSKKQSKKCTCKTRILDSHPCRSCRILKCFEAGMTSKKIQSGRDKTSTKAISCISTESTSNSLSARIIPRSSLNIHGAVHLWQEFENTRACKKGTKRNALIVSTSSAGDMDSTWKMVINLFSSLGELEIKDKTALLRNFMPKFIQIDSVPYFAANIDVFKNIGRDEYESSIIDFYDGVLPETNTISKKDTIRIFEPYWNFYTNKVILPIALMKLEGPEFMALVWLLFFDNGYTNLSDKCREACRNIKKVILRELRSYQIDRNFDRNRFFEILEALQLVERGEKKFMEEMVICELLNIKIDPGFMEIIRESKL", "text": "FUNCTION: Orphan nuclear receptor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family."}
{"protein": "MEQFEAINVEQAYSRWKDGSAALVDIRDPQSFEAGHTPGAFHLTNASLQTFMQQNDFERPVMVMCYHGNSSRSAAQYLLHQGFDAVYSIDGGFEAWARQYPQDVETSA", "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": "MQCPHCQHTDSRVLESRSSENGQSIRRRRECLQCKYRFTTYERIEFVPITVIKKDGKRESFDRCKLLRGIVRACEKTGIPPSRLEAIVNDIESRLQQDSKREVTSQEIGQLVLEYLRQESEVAYVRFASVYGNFQGIRDFIAALALLQSSEIERAHPSWSQVEEASVITSS", "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": "MAEHQVPRPQKPPRRDVHGVLLLDKPIGWSSNDALIRAKRLLWAKKAGHTGTLDPLATGLLPLCFGEATKFSQDLLDADKTYETVVRLGIRTSTADAEGEVLSERPVSVTPEQLQAAIARFVGEIDQVPPMHSALKKDGKPLYEYARAGQTVERAARRVTIYAIDVLATDLQSAEPTVTLRVSCSKGTYIRTLGEDIGEALGCGGHLVALRRTQVGNLTLDGAVTLEALDAAAEDARGALLAPVDALLQTLPRVELDAQESRRFLHGQRLPLQLALPNADQVRVYGVRDAIAADATASLLGVAAWQGGVLRPERLVHL", "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": "MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS", "text": "FUNCTION: Potent pro-inflammatory cytokine (PubMed:3920526, PubMed:10653850, PubMed:12794819, PubMed:28331908). 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 (PubMed:3920526). Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850). Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6 (PubMed:12794819). 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 (PubMed:33377178, PubMed:33883744). Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection (PubMed:28331908). SUBCELLULAR LOCATION: Cytoplasm, cytosol Secreted Lysosome Secreted, extracellular exosome Note=The precursor is cytosolic (PubMed:15192144). In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted (PubMed:24201029, PubMed:33377178, PubMed:33883744). Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744). In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation (PubMed:33883744). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10 (PubMed:32272059). SIMILARITY: Belongs to the IL-1 family."}
{"protein": "MMEEYLGVFVDETKEYLQNLNDTLLELEKNPEDMELINEAFRALHTLKGMAGTMGFSSMAKLCHTLENILDKARNSEIKITSDLLDKIFAGVDMITRMVDKIVSEGSDDIGENIDVFSDTIKSFASSGKEKPSEIKNETETKGEEEHKGESTSNEEVVVLPEEVAHVLQEARNKGFKTFYIKVILKEGTQLKSARIYLVFHKLEELKCEVVRTIPSVEEIEEEKFENEVELFVISPVDLEKLSEALSSIADIERVIIKEVTAVTEESGAEKRTEKEEKTEKTEEKAERKKVISQTVRVDIEKLDNLMDLMGELVIARSRILETLKKYNIKELDESLSHLSRITLDLQNVVMKIRMVPISFVFNRFPRMVRDLAKKMNKEVNFIMRGEDTELDRTFVEEIGEPLLHLLRNAIDHGIEPKEERIAKGKPPIGTLILSARHEGNNVVIEVEDDGRGIDKEKIIRKAIEKGLIDESKAATLSDQEILNFLFVPGFSTKEKVSEVSGRGVGMDVVKNVVESLNGSISIESEKDKGTKVTIRLPLTLAIIQALLVKVNNLVYAIPIANIDTILSISKEDIQRVQDRDVIVIRGEVIPVYRLWEVLQIEHKEELEEMEAVIVRVGNRKYGIVVDDLLGQDDIVIKSLGKVFSEVKEFSGAAILGDGSIALIINVSGIV", "text": "FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MPIQPLKKELVSFLEPYMPENAGVLGEQEKPYVILTYAQSLDARIAKIKGTRTIISHQETNTMTHYLRYKFDGIMLGCGTVLVDDPGLNCKWWPDDEPKPEHFAEHSPRPIILDPNGKWKFEGSKMKTLFDSGDGKAPIVVVKKLPEVVEENVDYLVMQTNFTGKVDWHDLFIQLKSQFGLKSIMVEGGGIVINDLLQRPHLIDALVITVGATFLGSEGVEVSPLIEINLKDISWWKGTRDSVLCSRLVSHS", "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": "MAEFDKEAYAERERSAASRKTLLKKQELVNSYKERLQKSNGFVIFFNFQGIDAYPLTLLRLDIKDLKGEIVVGKNTLFYRAFSDTVLSDHRDIFVGPTAALFAYEDPVAVTKKLVEFLKETFDKEWEGRIKGGLLDYKYITPEQVKELAELPSKEELIAKLLGVLMAPVTQLAMTLKAVPQKLVLVLKAIEEEKSKGGQ", "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": "MANHQIKAQRRKDEGKGASRRLRHAGMIPAIIYGGEQRPVSIQLNHEQIWLAQQNEWFYSSILDLNVDGGGGEKVLLRDLQRHPYRQLVMHVDFQRVSSDAKLSVAVPLHFINQATSPAGKASGVVITHELNEVHVSCLPKDLPEFIEVDLSTLSVGHVIHLSDITFPIGVELSTRLDKEHDMAVVIAKHVVIEDDTPAEEEGEGDTK", "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": "MTNSSLRPSGRRADQLRDVRITRHYTKHAEGAVLVEFGDTKVICTASVAERVPEFLRERGQGWLTAEYGMLPRATHTRSDREAARGKQTGRTQEIQRLIGRALRAVFDLNALGPRTLHLDCDVIQADGGTRTASITGAFVAAHDAVTKLVAAGRIARSPITDYVAAISVGVFGGTPVLDLDYDEDSACDTDMNVVMTGAGGFVEVQGTAEGAPFSRTEMNALLDLAQAGIGELVRLQRAALEA", "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": "MNINPYFLFIDVPIQAAISTTFPYTGVPPYSHGTGTGYTIDTVIRTHEYSNKGKQYISDVTGCAMVDPTNGPLPEDNEPSAYAQLDCVLEALDRMDEEHPGLFQAASQNAMEALMVTTVDKLTQGRQTFDWTVCRNQPAATALNTTITSFRLNDLNGADKGGLVPFCQDIIDSLDKPEMTFFSVKNIKKKLPAKNRKGFLIKRIPMKVKDRITRVEYIKRALSLNTMTKDAERGKLKRRAIATAGIQIRGFVLVVENLAKNICENLEQSGLPVGGNEKKAKLSNAVAKMLSNCPPGGISMTVTGDNTKWNECLNPRIFLAMTERITRDSPIWFRDFCSIAPVLFSNKIARLGKGFMITSKTKRLKAQIPCPDLFNIPLERYNEETRAKLKKLKPFFNEEGTASLSPGMMMGMFNMLSTVLGVAALGIKNIGNKEYLWDGLQSSDDFALFVNAKDEETCMEGINDFYRTCKLLGINMSKKKSYCNETGMFEFTSMFYRDGFVSNFAMELPSFGVAGVNESADMAIGMTIIKNNMINNGMGPATAQTAIQLFIADYRYTYKCHRGDSKVEGKRMKIIKELWENTKGRDGLLVADGGPNIYNLRNLHIPEIVLKYNLMDPEYKGRLLHPQNPFVGHLSIEGIKEADITPAHGPVKKMDYDAVSGTHSWRTKRNRSILNTDQRNMILEEQCYAKCCNLFEACFNSASYRKPVGQHSMLEAMAHRLRMDARLDYESGRMSKDDFEKAMAHLGEIGYI", "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": "MEKRELIYEGKAKKLFSTDDENLLISEFKDDLTAFNGEKKSSEVGKGALNNKISTELFKLLEKSGIQTHFVKMLDDNHLLHKKTKVILIEVIVRNIATGSLSKNLGIKDGTVLPFTLVEFDYKNDALGDPKLNDQHALILGLVEYQDELDKLRRMARQINDILKPYFAQKGLNLVDFKLEFGKDSSGNIILIDEISPDNCRFWDIESGEKMDKDRFRQGLGGLRVAYEQVLSRILAK", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MTKSQQKVSSIEKLSNQEGIISALAFDQRGALKRMMAEHQSETPTVEQIEQLKVLVSEELTQYASSILLDPEYGLPASDARNNDCGLLLAYEKTGYDVNAKGRLPDCLVEWSAKRLKEQGANAVKFLLYYDVDDTEEINIQKKAYIERIGSECVAEDIPFFLEVLTYDDNIPDNKSAEFAKVKPRKVNEAMKLFSEDCFNVDVLKVEVPVNMNFVEGFSEGEVVYTKEEAAQHFRDQDAATHLPYIYLSAGVSAELFQDTLKFAHDSGAQFNGVLCGRATWSGAVKVYIEEGEQAAREWLRTVGFKNIDDLNTVLKTTATSWKNK", "text": "SIMILARITY: Belongs to the aldolase LacD family."}
{"protein": "MNVNQVDLETVCGVTSVLPENTQPEFAFAGKSNVGKSSLINGLMNRKSFARTSSQPGKTQTINFYHLNEKLYFVDLPGYGYAKVSSELKAKWGKMIEKYLRTSTQLKVIFLLIDIRHEPSANDKDMYEWIVHNGFEPVIIATKLDKINRSQRDKHIKMVRTGLCAGANTKILPFSSLSKEGKDDIWRCIEQFLEVPDTENK", "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": "MVTIGNAHNDLIHDAVLDYYGKRLATCSSDKSINIFDIDGTESYKLVSTLTGHDGPVWQVSWAHPKFGSILASCSFDGKALIWKEQPETQQWSIIAEHSVHQASVNSVSWAPHELGAVLLCASSDGKVSVVDFNDDGTTSHVVFDAHAIGANSASWAPLSSTPSPNQKDAASLKQQRRFVTCGSDNLAKIWKYDAANNTYVEEARLEGHTDWVRDVAWSPSMLVRTYIATASQDRTVLIWTQDKAGKWQKQLLTEDKFPDVCWRCSWSLSGNILAVSGGDNKVSLWKENLQGKWESAGEVVQ", "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": "MERRSALPQDFREVLHCLKMRSKYAVLLVFVVGLVIIEKENNFISRVSDKLKQSPQVLPEANETEASPVQAENGSLASLRQLDTAFSQLRTRLRNVTLQLAGELGIAAPEPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVTFEPGGANAVGSALVYRDVLQQLLLCDLYILESFISPAPEEHLTAALFRRGSSHSLCEEPVCTPSLKKVFEKYHCKNRRCGPLNITLAAEACRRKQHMALKTVRIRQLEFLQPLAEDPRLDLRIIQLVRDPRAVLVSRMVAFSGKYESWKKWAAEGEAPLQEDEVQRLRGNCESIRLSAELGLRQPRWLRGRYMLVRYEDVARAPLRKALEMYRFAGIHPTPQVEEWIRANTQAPQDSNGIYSTQKNSSEQFEKWRFSIPFKLAQVVQDACEPAMRLFGYKLASSAQELTNRSLSLLEEGPPTRIT", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin (PubMed:7629189). Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices (PubMed:7629189). Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan (PubMed:7629189). Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (PubMed:9147050). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily."}
{"protein": "MNLHEYQGKQLFAEYGLPVSKGYAVDTPEAAAEACDKIGGTEWVVKAQVHAGGRGKAGGVKLVRSKEDAAAFAQQWLGKRLVTYQTDANGQPVTKILVESCTDIAKELYLGAVVDRSSRRIVFMASTEGGVDIEKIAHDTPEKILKATIDPLVGAQPFQGRDLAFQLGLEGKQVTQFAKIFTGLAKLFQDHDLALLEVNPLVIKADGDLHCLDAKINIDANAMYRQPKLKGFHDPSQDDPREAHAAKFELNYVALEGNIGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVTEAFKIILSDANVAAVLVNIFGGIVRCDMIAEGIIGAVKEVGVKIPVVVRLEGNNAELGAKVLAESGLNIIAATSLTDAAQQVVKAAEGK", "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": "MGFLKFSPFLVVSILLLYQACSLQAVPLRSILESSPGMATLSEEEVRLLAALVQDYMQMKARELEQEEEQEAEGSSVTAQKRSCNTATCVTHRLAGLLSRSGGVVKDNFVPTNVGSEAFGRRRRDLQA", "text": "FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
{"protein": "MSGRFGRFGGQYVPETVMNALIELEREFEKAKEDKDFMEEYRYYLREYSGRPTPLYYAENLTKRLGGAKIYLKREDLNHTGAHKINNVLGQILLAKRMNKKRVIAETGAGQHGVATATAAAMFGMECEIFMGEEDIKRQSLNVFRMKLLGAKVTPVTTGTKTLKDAVNEAIRDWVTNIDNTFYVIGSVVGPHPYPTMVRDFQRVIGDEAKEQILQKEGRLPDYVIACVGGGSNAMGIFYPFIEDKEVKLIGVEAAGEGIETGKHAAAMAKGSVGVLHGMMTYLLQDEEGRIMPVYSISAGLDYPGVGPEHAFLKESNRAQYVYATDEEALAAFMDLSQTEGIIPALESAHALAYAMKLAPNLTKDNIIIVNLSGRGDKDVNTVAKVLGVEL", "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": "MLDREGFRPNVGIILINAQNEVWWGKRVREHSWQFPQGGIKFGETPEQAMFRELEEEVGLRAEHVKIIGRTRDWLRYEVPDHFIKREIRGHYKGQKQIWFLLRMVGRDCDVNLRLTEHPEFDAWRWHDYWVPLDVVIEFKRDVYQRALQELSRFLSRPAHPAPIHNTARYLRQTHSARKTDEPSTEQTKPNNE", "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": "MCGRTACSLGAARLRRACAYRDRQGRRQQPEWLREGRYRPSYNKGPQSSGPVLLSRKHVQQDADSSERVLMDMRWGLVPSWFKEDDPSKMQFKTSNCRSDTMLSKSSYKGPLLKGKRCVVLADGFYEWQQRGGGKQPYFIYFPQNKKHPAEEEEDSDEEWRGWRLLTMAGIFDCWEPPKGGEPLYTYTIITVDASEDVSFIHHRMPAILDGDEAIEKWLDFAEVPTREAMKLIRPAENIAFHPVSTFVNSVRNDTPECLVPIELGVPKEVKATASSKAMLGWLKSSQEGSPQKKEDTLPRWKSQFIHSPSPKKSSAGILRQWLGQEGGPPAKKQKA", "text": "FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. 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. The HMCES DNA-protein cross-link is then degraded by the proteasome. 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. Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). SUBCELLULAR LOCATION: Chromosome Note=Recruited to chromatin following DNA damage. Localizes to replication forks. SIMILARITY: Belongs to the SOS response-associated peptidase family."}
{"protein": "MSTGKIIQVIGAVIDVEFSRDNTPKVYDALNVKEANLVLEVQQQIGDGVVRTIAMGSSDGLRRGMVVENTNAPISVPVGHGTLGRIMNVLGEPIDEAGPIQYTETRSIHQAPPAYDELALSTEILETGIKVVDLICPFAKGGKVGLFGGAGVGKTVTMMELINNIAKEHSGYSVFAGVGERTREGNDFYYEMKDSNVLDKVALVYGQMNEPPGNRLRVALSGLTIAEGFRDEKRDVLMFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAAEMGALQERITSTKTGSITSVQAVYVPADDLTDPSPATTFSHLDATIVLSRQIAELGIYPAVDPLDSTSRQLDPLVVGHDHYETARAVQKVLQRYKELKDIIAILGMDELSDEDKRTVDRARKIQRFLSQPFHVAEVFTGNPGKFVSLKDTVASFKAIVNGEYDHLPEQAFYMVGSIQEAIEKAKTL", "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": "MECPDPQPILELLEAPCPTIGQPRPEVGLRAGAGRVDIARVDGASAIVACVASSPLQLLAPSPRGRCAWIISASHGGGLLAGDEVSLEVDVGAGAVALLSTQAGTKIYRSRGEVASQGLSARVGAGALLAALPHPVSCFSGARFRQEQRFELARGASLLWLDALVAGRIARGERWAFDEYRSRIEVAIDGRTVLADALRLVPGEGPPIVARLPGVELLATVVALGPAVASAARELLERVAASPAERDAGVLAAASPLRDGLLLRVASRSVEAGLAFLRQRLAFVEAVTGADPFARTP", "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": "MNNKGRTPGSAGRTVRSSAQQNGLTMRKRDMTPTRNTNLLPNATFVGDRFLGVRLDQDELDHANHLMTSKLYSNKENLNNSMSEPNSPEKKSVEGEALKQMMRHKSTGALTDADDGDRILCYKKNLAPPPAIGYINQAKVLYSTNSVINPASSVKKSTRHVKETATKVLDGPGLTKDLYSRHLDWGCHNWVAVALGHELYLWNTETCVIKNLFEDNAPTNEGLITSVRWSQEGRYISLGYASGAVKIYDPNRPKTTEYVRELRTLRVGGASRCASIAWRKQGVMTCGYKSGDIVNHDVRISQHVVSSWGGDNGHCRDVTALEWSADENMCVSGSSDRTAKIWDGRHVRGSTVIQDPEPMFTIDEHTGQVRTAQFCSFRDGILATGGGINDGTVKLWDVKRQFQKVRELNVCETGGVGGIVFNRPYSEMLTASDDGFLRIYRFNANYKLSHEIQASNEPIMDLVGSPFDEVLIGDMEETLKVFQLFNVDKSTNILDRTAPKNVGLNVR", "text": "FUNCTION: Plays a role in metaphase-anaphase transition during meiosis I (PubMed:12498686). Required for embryonic anterior-posterior axis formation (PubMed:11832245). SUBCELLULAR LOCATION: Chromosome Cytoplasm Note=At prometaphase, localizes around condensed chromosomes. At metaphase, localizes along chromosomes, dissociates from the sister chromatid after separation and localizes to the cytoplasm at anaphase and interphase. SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family."}
{"protein": "MRSLSLAWLLGGITLLAASASCNRTVNAPGPNSKGRSLIGRLDTPPPITGKGAPVEPGFSVDEFSASVLTGKLTTVFLPVIYIIVFVIGLPSNGMALWVFFFRTKKKHPAVIYMANLALADLLSVIWFPLKISYHLHGNDWTYGDALCKVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKRANIAVGVSLAIWLLIFLVTIPLYVMRQTIYIPALNITTCHDVLPEEVLVGDMFSYFLSLAIGVFLFPALLTASAYVLMIKTLRSSAMDEHSEKKRRRAIRLIITVLSMYFICFAPSNVLLVVHYFLIKSQRQSHVYALYLVALCLSTLNSCIDPFVYYFVSKDFRDQARNALLCRSVRTVKRMQISLTSNKFSRKSSSYSSSSTSVKTSY", "text": "FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to G proteins. Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF- kappaB and Rho. Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates Tlr3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Regulates endothelial cell barrier integrity during neutrophil extravasation, probably following proteolytic cleavage by PRTN3 (By similarity). Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion. Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13, but probably not with G(o)-alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to G GNAQ and GNA11; the function involves dissociation of RIPK1 and Tradd from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves Ikbkb and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by Cops5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as pro-inflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MAVGVSPGELRELSDDELIERLRESKEELFNLRFQMATGQLSNNRRLRVVRQEIARVYTVLRERELGLASGPAGEES", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MTTSTAAKRTKSGCWTCRLRRKKCNEGGPPCDNCEARGIHCHGYGPRPQWKDRGALEREEARKLQYQSGRGRSYSRSSSTAAAAAPKPAEGAMVTGGSSSSSRGSGSSIYVGGNGLGGAQEEQHGDNNAPFSAGTGNFEYQANPAPGMSPLMSDINLALDAHAMDPLDFNIDFSSTPSSAVDKSSSTSADSPSFTSIECSQFPIFSPELPVDTPVALFPQVAPIPPGLPGRESVPVAACTDLVISHGLLLAEMDRPVGQRHGQVMAEGEKGIELMMRCPPAPRAPRLEGQGRSAHILLFVRDWYAASSWRIWSGNIQDCQNHIDAAASLLLEHETALVGEAHRLSNMERKALAFFTVRLIWNDVLLSSTRRTVPKAEMVYRRLLLADSNSRGGDSHTTTSTTGPTTTTPLLAASTFWDLTGCEGAVLLAMLDASILSAWRLGEEASGSLSIRALVGRADKIEAVVEGEIARLSSLLPRSPEKTSSASGKPSHGRKTGPENEVTVATVHSLIFAHAILTDLHQTVSGPRASVPEIGDSISRAISSAWNLWQEQQQQGAGLGLERILAWPYCVAASLAKGDQREVFREIIARTENGDGSSSGGDVQQLKSIVEQCWATSSSNHRDWKDVVQRSNQFGVFLI", "text": "FUNCTION: Transcription factor; 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:26979951). May play a role in the regulation of the production of phomopsins (Probable). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTEQKRPVLTLKRKTEGETPTRSRKTIINVTTPPKWKVKKQKLAEKAAREAELTAKKAQARQALSIYLNLPSLDEAVNTLKPWWPGLFDGDTPRLLACGIRDVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQEEEVYAAERLDKIRRQNRIKAELQAVLDEQ", "text": "FUNCTION: One of the components on the FinOP fertility inhibition complex, which inhibits the expression of traJ gene, which in turn regulates the expression of some 20 transfer genes. The transfer genes are responsible for the process, called conjugal transfer, in which DNA is transmitted from one bacterial host to another. RNA-binding that interacts with the traJ mRNA and its antisense RNA, finP, stabilizing finP against endonucleolytic degradation and facilitating sense- antisense RNA recognition (By similarity). SIMILARITY: Belongs to the FinO family."}
{"protein": "MVLIRVLANLLILQLSYAQKSSKLVVGGDECNINEHPFLVLVYHDGYQCGGTLINEEWVLTAAHCDGKKMKLRFGLHSKNVPNKDKQTRVPKEKFFCLSSKYFIKWGKDIMLIRLNRPVNNSTHIAPLSLPSSPPSQNTVCNIMGWGTISPTKEIYPDVPHCANISILDHAVCRAFYPGLLEKSKTLCAGILEGGKDICQGDSGGPLICNGQIQGIVSVGGNPCAEPRVPAIYTKVFDHLDWIKSIIAGNTAATCPL", "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": "MAKRKVTNKKRVVKKNIARGIIHIAATFNNTSVTITDEMGNVICWSTAGALGFKGSKKSTPYAAQQAVEDAVVKAKEHGIKELGIKVQGPGSGRETAVKSLGSIEGIKVLWFKDVTPLPHNGCRPPKRRRV", "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": "MGINLLPIEMDEIRKRLGREPNETEWRVIDAVWSEHCSYKSSKIFLKSFSIDSPNVIMGIKDWQDAGAVDIGDGWAVVIKVESHNHPSAIDPFNGAATGVGGIIRDIISKGAKPIALMDMIRVGNLKIKKNVWLLKNIIAGIAAYGNSIGVPVVGGELSFDDTYNDNPLVDVAAIGIVRKDKIKPSIVDKAGLKLVLAGLTGVDGLGGASFASRKLSGEDEIGAVQIADPFAGKIILDVTLEIADKVEAIKDLGGGGLAVAVTEITNGLGATVDIEKIPLRVKNMNPSDVIISETQERMLYAVEEKNVKEVCEAFEEYEYPCSVIGEITNEPVIKFRYIGKDLVSLPTNVLLNPPRFLWPIKNTKKNVEEKIVDLPLESAIYTVLTHPDLVSKGWAYSQFDYEVNTSTVVKPGDADSAVVSLPNGKLLAIKADANPDMCAEDGYECGKGIVAEAYRNLATVGARGMVAVDHLQFGDPKKAEVYYTFVEAIRGIGEATRFFNIPIVGGKVSFYNENNQGRPIKPTPLIVMAGLVQDKLLKNRVEDNLYVVSVGYTRKELGGSLLSKIFKIPSQAPKVRLQEDLLSSEVVIDSINEGKITFAKDVSRGGLAASLFSILVHGYGVEISTKSILSDTDNVIENLFSESSGRFIVLTNEPEWIVEKSKSKGIVASIIGRVNKKTNILTIDNIDYNLKNIVDNYFNFLEEVMGNG", "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": "MPLQAIVSFLRLDIAAGVILVGAAVLALIAANSPAAALYEQVFQTPFVIGYGPWLLEKPLLLWINDGLMAVFFLLVGLEIKREVRGGELSTPRLAALPAVAAVGGMVVPALIYASLTWGDAFALRGWAIPAATDIAFALGILTLLGPRVPISLKIFLTALAIIDDLGAILIIAFFYTASLSPLALLLAAACLALLIGLNLSGQRRLWPYLLIGVVLWVCVLKSGVHATLAGVVLALTIPLGATDDESASADKPLERLEHGLHPWVTYAILPLFAFANAGVSLAGLPPSALLAPVPLGIVLGLFLGKQIGVFGFSWLAIRSGLAPMPQGARWRDLYGVALITGVGFTMSLFIGTLAFETSDPLAADFGTEVRLGVLSGSLLSGVIGYLVLRLSRRNPATE", "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": "MKPQFRNTVERMYRGTFFYSFNNRPILSRRNTVWLCYEVKTRGPSMPTWGTKIFRGQVYSKAKYHPEMRFLRWFSKWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPKVTLTIFVARLYYFWKPDYQQALRILCQKRGGPHATMKIMNYNEFQDCWNKFVDGRGKPFKPRNNLPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQHRGFLRNQAPNIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHVSLCIFAARIYDDQGRYQEGLRTLHRDGAKIAMMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSERLRAILQNQGN", "text": "FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, P-body Note=Mainly cytoplasmic, small amount are found in the nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MKKEGILNSELAKIADDLGHTDQVCIGDLGLPVPSGVKKIDLALTRGKPTFQEVLDIYLENILVEKIYLADEIKENNPEQLKILLTKLSADVEVVFVSHETLKLMNHDVKAVVRTGENTPYSNIILQSGVAL", "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": "MTSTEAGALRRLAPPARRFLAHRKGVLVRLALWSLAESGQAFLVGHAVARSVDEGFLAGDPRRGLLWLGVALVAVLSGARVVRGVFAQLAGVTEPLRDGLVRHAVDRSMARAAPGGPGGTDRAAVSRLTNQVEIARDSFAGLVLTLRSFVFTAAGALLGLLSLHPALLVVVLPPLAAGLALFLVTLRPMAAAQRRALAADEALGEHAASARAALRDLTACGTGPGAERHGADLVADAAAAARTLAGWAAVRTAALGVAGHLPVLALLVAVEWLRGHGVSVGALLGAFTYLVQSLLPALHTLMTALGAAGSRLLVVLDRILGPEPEPEPEPEPEPEPELGSGLEPEPEPASEPESGPSTASASAAAFAVHTAAAPAVELRSVTLSYGVRAEPVLDALDLRVAPGEHLAVVGPSGIGKSTLTRLVAGTLAPSRGEVRVAGRVVTGRPAAELAALRVLVPQDAYVFSGTVGDNLAYLRTDPSPAELDAAVEAFGLAPLVERLGGLDATVRPAELSPGERQLVALVRAYLSPAPLLLLDEATCHLDPASEARAEKALAGRSGTLVVVAHRLSSAVRADRTLVLDGIRAQSGTHAELLGRSPLYRDLTGHWNS", "text": "FUNCTION: Probably involved in exporting SapB from the cell (Probable). Expression of the ram locus (ramA, ramB and ramR) induces rapid aerial mycelium formation in S.lividans (PubMed:8206859). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MAVNEFQVESNISPKQLNNQSVSLVIPRLTRDKIHNSMYYKVNLSNESLRGNTMVELLKVMIGAFGTIKGQNGHLHMMVLGGIEFKCILMKLIEIRPNFQQLNFLLNVKNENGFDSKYIIALLLVYARLQYYYLNGNNKNDDDENDLIKLFKVQLYKYSQHYFKLKSFPLQVDCFAHSYNEELCIIHIDELVDWLATQDHIWGIPLGKCQWNKIYNSDEESSSSESESNGDSEDDNDTSSES", "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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PRP38 family."}
{"protein": "MASENMTPQDYIGHHLNNLQLDLRTFSLVDPQNPPATFWTINIDSMFFSVGLGLLFLVLFRSVAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHVLGLPALRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH", "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": "MKAYAKANIFLKLTGFDSRKYHLLESRFILLKDVFDELELVDKESDSKKEFEIISNFKCENNIIQKAYLLLSRRYNNELKELFSKKSLKLTKNIPVCAGLGGGSSDCASFLLLMNETLNLKLNLQELINLSIQLGSDIAFFLSGFNSANVSGCGEIIEEFEDDIPTLKWTFPQISCQTKAVYDEFDREIFDFQKNNNQAQIYKKLSTKELLQNFKNKELNDLFTPCATLYPKMKSYLQEDFFLSGSGSSVFKVDR", "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": "MSAVLLDGKALAAKKRDELKSEVTKLKERGITPGLAVILVGNDPASTVYVRSKQKACEQIGIYSVLKELPASTSEEELLTEIDRLNNDPTIHGILVQLPLPEQISEQAVIERISPAKDVDGFHPISVGRMMIGEDTFLPCTPFGVLVMLQEANVEIAGKHVVVVGRSNIVGKPVGQLMLNEHATVTYCHSRTKNLTEITKQADILIVAVGRARFIDASHVKEGAVVIDVGINRVDGKLCGDVDFESVREVASHLTPVPGGVGPMTITMLLANTIQAAKE", "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": "MINKIYGKVIEKKESSLVLMTAVFEFELLVSAFCLANFKLLDKVELFTYLYTKENELKLFGFLNSDERETFKSLIGVSGIGPRAALRVLSNIRYNEFKDAIDREDIELIAKIKGIGKKMAGKMFLHLQGKLLINNELESSLFRFKELEESIVSMGFDRKIVNSKLKEAFNLVEFSNLKDSEKEQFLFKEVLKRMSN", "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": "MSVLQVLHYPDERLRKIAAPVKEVNGEIQRIVDDMFETMYAEEGIGLAATQVDVHLQIIVIDVSENRDQRLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFELEADDLLAICIQHEMDHLVGKLFVDYLSPLKRQRIRQKLEKMAKLNARAN", "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": "MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFYLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLFELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLYLH", "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": "MKILRGEEIAEKKAENLHGIIERSGLEPSLKLIQIGDNEAASIYARAKIRRGKKIGIAVDLEKYDDISMKDLLKRIDDLAKDPQINGIMIENPLPKGFDYYEIVRNIPYYKDVDALSPYNQGLIALNREFLVPATPRAVIDIMDYYGYHENTVTIVNRSPVVGRPLSMMLLNRNYTVSVCHSKTKDIGSMTRSSKIVVVAVGRPGFLNREMVTPGSVVIDVGINYVNDKVVGDANFEDLSEYVEAITPVPGGVGPITATNILENVVKAAEFQKNNL", "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": "MKLVLMGLPGAGKGTQAEQIVEKYNIPHISTGDMFRAAMKNNTELGRKAKSFMDNGDLVPDEVTNGIVRERLSEDDAKDGFLLDGFPRTVEQAQELENILSDLGTELDAVINIDVEKDVLMKRLTGRWICRTCGKTYHEIYNPPKVPGKCDLDGGELYQRDDDKKETVEKRLNVNMKQTKPLLDFYSEKGKLHNINGEQEIKDVFVDVEKILASF", "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": "MAKLTKESFIQSLKEMNIKEVMELVNAMKEEFGIDPSAVVVAGGAAGGAEVAEKTEVTITLKNAGGNKVPVIKKVREISPELSLMDAKKLVDSAPAKLKDNVKPEEAEEIKAAFAALGAEISID", "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": "MSNAITMGIFWHLIGAASAACFYAPFKKVKKWSWETMWSVGGIVSWIILPWAISALLLPNFWAYYSSFSLSTLLPVFLFGAMWGIGNINYGLTMRYLGMSMGIGIAIGITLIVGTLMTPIINGNFDVLINTEGGRMTLLGVLVALIGVGIVTRAGQLKERKMGIKAEEFNLKKGLVLAVMCGIFSAGMSFAMNAAKPMHEAAAALGVDPLYVALPSYVVIMGGGAIINLGFCFIRLAKVKDLSLKADFSLAKPLIIHNVLLSVLGGLMWYLQFFFYAWGHARIPAQYDYISWMLHMSFYVLCGGIVGLVLKEWNNAGRRPVTVLSLGCVVIIVAANIVGIGMAN", "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": "MIPDPRDIILRPVVSEKSYGLLDENVYTFIVRPDANKTQIKLAVQKIFNVRVTRVNTINRAGKRKRTKHGWGHRSATKRALVSLAPGDSIEIFGGPGA", "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": "MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLIADRVTVTSKNNDDEQYVWESSAGGSFTVKADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKDDEAKKDMDTDEPKIEDVGEDEDADKKDKDGKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLCVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFIKGVVDSEDLPLNISREMLQQNKVLKVIRKNLVKKTMELIEELTEDKENYKKFYEQFSKNLKLGVHEDSNNRAKLADFLRFHTSASGDDFCSLSDYVSRMKENQKHVYFITGESKDQVSNSAFVERVKARGFEVVYMTEPIDEYVIQHLKEYKGKQLVSVTKEGLELPEDEAEKKKREEDKAKFEGLCKLMKSILDSKVEKVVVSNRLVDSPCCIVTSQFGWSANMERIMKAQALRDTATMGYMAGKKQLEINPDHPIVEALRQKADADKNDKAVKDLVILLFETSLLSSGFSLDSPQVHASRIYRMIKLGLGIDEDEPMTTEDAHSGGDAPGLVEDTEDASHMEEVD", "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": "MKFYIDDLPVLFPYPKIYPEQYNYMCDIKKTLDVGGNSILEMPSGTGKTVSLLSLTIAYQMHYPEHRKIIYCSRTMSEIEKALVELENLMDYRTKELGYQEDFRGLGLTSRKNLCLHPEVSKERKGTVVDEKCRRMTNGQAKRKLEEDPEANVELCEYHENLYNIEVEDYLPKGVFSFEKLLKYCEEKTLCPYFIVRRMISLCNIIIYSYHYLLDPKIAERVSNEVSKDSIVIFDEAHNIDNVCIESLSLDLTTDALRRATRGANALDERISEVRKVDSQKLQDEYEKLVQGLHSADILTDQEEPFVETPVLPQDLLTEAIPGNIRRAEHFVSFLKRLIEYLKTRMKVLHVISETPKSFLQHLKQLTFIERKPLRFCSERLSLLVRTLEVTEVEDFTALKDIATFATLISTYEEGFLLIIEPYEIENAAVPNPIMRFTCLDASIAIKPVFERFSSVIITSGTISPLDMYPRMLNFKTVLQKSYAMTLAKKSFLPMIITKGSDQVAISSRFEIRNDPSIVRNYGSMLVEFAKITPDGMVVFFPSYLYMESIVSMWQTMGILDEVWKHKLILVETPDAQETSLALETYRKACSNGRGAILLSVARGKVSEGIDFDHQYGRTVLMIGIPFQYTESRILKARLEFMRENYRIRENDFLSFDAMRHAAQCLGRVLRGKDDYGVMVLADRRFSRKRSQLPKWIAQGLSDADLNLSTDMAISNTKQFLRTMAQPTDPKDQEGVSVWSYEDLIKHQNSRKDQGGFIENENKEGEQDEDEDEDIEMQ", "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/RAD3 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/RAD3 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": "MSHPLRSLPKIDKILQESRFADHSKELLTTLARDYLEEIRAQFLQDATPIPPSESILQEVERRYEASLAPSLVPLVNATGIIVHTNLGRSVFAPELIEEIKPLLTSYNNLEYDLKAGRRGERYSHLHGILKAILGCEEVLVVNNNAAAVFLILHTFAQNQEAIISRGELIEIGGSFRIPEVMKNAGAILKEVGTTNKTHRRDYEEAITPQSALLMKVHKSNYDIVGFTQEVDLQELIELSQKHNLIDYYDLGSGFLESVPFTNEPTLKKIASLSPSLVSFSGDKLLGGAQAGIIFGKKSLIDRLKKNQLLRMLRVDKFTLAALEATLRAHLLHDYEKIPTLKMAHLSLEELEERAKKLKSRVHGYESQILQTQGYAGGGALPNQSFFSIALALCHPQKSPMELEQSLRARGVIARIEQERVLLDMRTIFTSQLESLAQILNEVF", "text": "FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SelA family."}
{"protein": "MTPVEFLASNPLAFVLCALVLGLLVGSFLNVVIHRLPIMMQRDWQSQAREFLELPAEPAGAAFNLFLPHSRCPHCDHQIRAWENIPLISWLALRGKCSACKASISKRYPLVELACGLLSGYVAWHFGFSWQAGAMLLLTWGLLAMSMIDVDHQLLPDSLVLPLLWLGLIINSFGLFASLEDALWGAVVGYLALWSVYWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQVLPLTILLSSVVGAVLGTVMLRMQKAESGTPIPFGPYLAIAGWVALLWGDQITASYLQFARL", "text": "FUNCTION: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha- amino group of the newly exposed N-terminal phenylalanine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A24 family."}
{"protein": "MINYGVVGVGYFGAELARFMNMHDNAKITCVYDPENGENIARELQCINMSSLDALVSSKLVDCVIVATPNYLHKEPVIKAAKNKKHVFCEKPIALSYEDCVDMVKACKEAGVTFMAGHIMNFFNGVQYARKLIKEGVIGEILSCHTKRNGWENKQERLSWKKMKEQSGGHLYHHIHELDCVQHLLGEIPETVTMIGGNLAHSGPGFGNEDDMLFMTLEFPSGKLATLEWGSAFNWPEHYVIINGTKGSIKIDMQETAGSLRIGGQTKHFLVHETQEEDDDRRKGNMTSEMDGAIAYGHPGKKTPLWLASLIRKETLFLHNILCGAKPEEDYIDLLNGEAAMSAIATADAATLSRSQDRKVKISEIIKHTSVM", "text": "SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MKAFSPLAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLELRVSSALSKDEQIKKETRINVTAYQGKVLLVGQSPNSELSARAKQIAMGVEGTTEVYNEIRQGQPIGLGTASNDTWITTKVRSQLLTSDQVKSSNVKVTTENGEVFLLGLVTEREGKAAADIASRVSGVKRVTTAFTYIK", "text": "FUNCTION: Plays an important role in maintaining outer membrane integrity (PubMed:30201701). Contributes to virulence (PubMed:30201701). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the lipoprotein DolP family."}
{"protein": "MTRKLFIETHGCQMNEYDSSRMVDLLGEHQAMEITENPAEADVILLNTCSIREKAQEKVFSQLGRWRELKQDNPQLVIGVGGCVASQEGAAIRDRAPYVDVVFGPQTLHRLPEMIDAARTTRTPQVDISFPEIEKFDRLPEPRVDGPSAYVSVMEGCSKYCTFCVVPYTRGEEVSRPLADVLAEIVHLAENGVKEVTLLGQNVNGYRHDGHDFADLLHAVAAIDGIGRIRYTTSHPLEFSDAIIQAHADIPQLVKYLHLPVQAGSDRILAAMKRNHTALEYKSRIRRLKAAVPDILISSDFIVGFPGETDKDFEQTMKLIEDVGFDFSYSFVYSARPGTPAADLADDTPEEVKKQRLAILQQRINQQGFENSRRMVGTTQRILVSDYSKKDPGMLQGRTEHNRIVNFRCDNPRLIGQFVDVHIDDALPHSLRGSLLS", "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": "MAGRSGDRDEDLLKAVRLIKILYQSNPPPSPEGTRQARRNRRRRWRARQRQIHSIGERILSTYLGRSEEPVPLQLPPLERLNLNCSEDCGASGTQGVGSPQISVESPTVLESGTEEQC", "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": "MDEILKYFPNLTDLQIEQFQKLDFLYHNWNEKINVISRKDIDSLYTKHILHSLGIAKVMKFEPGTTVLDVGTGGGFPGIPLAILFPETRFYLIDVIAKKIKVVQGVVDALELKNVKAEQKRAELVKGDFDFIVSRAVTNMPDFVSWIKDKIKKQHKHKLKNGILYLKGGDLSEELKDFPAATLYDLSEIFEDEFFETKKVVHLPLKFKP", "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": "MMLYIVFILSVIFVIGFVGFSSKPSPIYGGLGLIVSGGVGCGIVLNFGGSFLGLMVFLIYLGGMMVVFGYTTAMATEQYPEIWLLNKAVLGAFITALLMEFFMVYYVLKDKEVEIVFEFNGLGDWVIYDTGDSGFFSEEAMGIAALYSYGTWLVIVTGWSLFIGVVVIMEITRGN", "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 6 family."}
{"protein": "MASLKDMRVRIASTKATQKITKAMQMVAASKLRRAQTAAEAARPYADKMSAVISNIAGAAAGSPGAPALLAGTGRDQVHLLLVCTGERGLSGAFNSSIVRLARERALALMAQGKEVKFFCVGRKGYEQLRRQFDKQIVEHLDLRSVRQLGFVNAEDIAKKVLARFEAGEFDVCTLFYSRFRSVIAQIPTAQQIIPLVVEEGTAASTTSYEYEPEEDEILTRLLPRNLAVQIFRALLENNASFYGAQMSAMDNATRNAGEMIRKQTLVYNRTRQAQITKELIEIISGAEAV", "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": "MTRNSLLNPEAENADPDQALRPRSLDEFIGQQAARENIRVFIEAAKKRQESLDHVLFFGPPGLGKTTLAQIIAREMGVGFRATSGPVIVKSGDLAALLTNLEDGDVLFIDEIHRLQPVVEEVLYPAMEDRALDLMIGEGPSARSVRIDLPHFTLVGATTRQGLLSTPLRDRFGIPVRLQFYSIEELRQVITRAARLLGMEIAPEGAEEIAKRSRGTPRIAGRLLRRVRDFADVAGSKIVDRFIADEALNRLEVDKLGLDLMDRRYLMMIADIYKGGPVGLDTLAAGLSEPRDTVEEVIEPYLIQLGLVARTARGRQLNGLAWRHLGLTDPREAEGKHSEIKNQPGLL", "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": "MKLLLILLGALLAVLTIKRTSAVQGSNHLICYYDGTSYTREGLAKLTLNDLEPALQFCTHLVYGHAAINPSSNKLVSNNEKLDLDVGTGLYRTITGMKKKYPHLKVLLSVGGDKDEVDADNNKYLTLLESSNARIPFINSAHSMVKTYGFDGLELGWQFPKNKPKKVHGSIGKLWKGFKKIFTGDFIVDEKAEEHKEEFTALVRELKNALRPDGYILGLAVLPNVNSSLFYDVPAIVNNLDYVNLMAYDFQTPQRNPEMADFPAPIYELNERNPESNVNYQVQYWLQNHCPASKINVGIPSYGRAWKMTTDSGLTGLPPVSDADGPAAGGLQTQTEGLLSWPEVCAKLPNPANQHLKGADSPLRKVGDPTKRFGNYAYRSTDDKGENGIWVSYEDPDTAANKAAYVKTKGLGGVALVDLSFDDFRGACTGDKYPILRAIKFKFQ", "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. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF subfamily."}
{"protein": "MSRYTGPKWRLSRRLGISLSGSGKELARRPYAPGDHGNTGRRPKLSEYATQLREKQKLRFTYGLSERQFHNLFLKAGKIRKGLHGTNFFILLETRLDSVVFRLGLASTRPQARQLVNHGHILVDGKRVTIPSYEVKPGQIISVRERSKKIVPILNSVEASLNNTPFVEFDADKLEGKLTRYPEREELGADINESLIVEYYNRLG", "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": "MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGAVQAAARVNRGGGPMRNRPAIARGAAGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDTQRRPAQSINRGGMTRNRGSGGFGGGGTRRGTRGGSRGRGRGTGRNSKQQLSAEELDAQLDAYNARMDTS", "text": "FUNCTION: Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway) (PubMed:9119228, PubMed:10786854, PubMed:11158589). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and 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. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability. Involved in mRNA export of C5-methylcytosine (m5C)- containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. SIMILARITY: Belongs to the THOC4 family."}
{"protein": "KNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPHIVVFLNKQDQVDDDELLELVELEVRELLDKYEFPGDEIPVVPGTALLALEALIANPKTQRGENKWVDKIYELMDKVDSYIPTPERETDKPFLLAVEDVLSITGRGTVATGRVERGTLKISDNVEIVGLKPTQTAVVTGLEMFKTLDETIAGDNVGVLLRGVQKKDIERGMVIAKPGTITPHTKFEAQVYVLTK", "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": "MNKNPQRFTITAALPYTNGPIHIGHLAGVYVPADIYSRFLRMQGYDVAFVCGSDEHGVPITIKAKKEGVTPQDVVDKYNGIIKKSFEDFGITFDNYSRTSGKTHHDTASAFFKKMYEDGKFIEESTEQLYDEEAGQFLADRFVTGTCPKCGNEEAYGDQCESCGTSLNATDLINPKSAITGAVPTLKETRHWFLPLDQYEDFLKEWILKGHKSDWKSNVYGQVKSWIDDGLRARAVTRDLDWGIPVPVEGGDGKVLYVWFDAPIGYISSTKEWAEREGKDWEPYWKDENTKLVHFIGKDNIVFHCIIFPVMLKAHGDYILPENVPANEFLNLEGKKLSTSKNWAVWLHEYLEEFPDQQDVLRYVLTANAPETKDNDFTWKDFQARNNNELVAIFGNFINRVVVLTNKYYNGIVPEPGAYSEIDEKTIAELKAYPSVIASSIERYRFREAQGELMNLARLGNKYLADEEPWKLIKTDEERVKTIMYVALQIASALSIISEPFLPFTSAKLKKMLNHVDESSDNTPDWDIIGTKEALILGGHQIGKAELLFSKIEDEQMEKQLEKLEATKTANAMEDQKAEPQKEIATFEDFTKMDLRVGTIIEAQKMPKTKKLMVLKVDTGIDQRTVVSGIAEHFKAEDIIGKKVTVLANLAPRKLRGVDSEGMILMTENAEGKLVFVNPDEDGVKAGTTIN", "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": "MSKRNTPPLRSSGINTIQINAAREMHAQTVRARRMPMPTSGITTPSVQPTAAPATPPRHICNNPNNPQCLHCGSVIIPSPRATLPLEDNPSISINDWTISSRKKPILNSQELDIWENEKLKGLTLPEMIFGNNYIRIENSKQHWSIEFNALDALKEVQLQDSGIRVAYSNDWINSKKRQNSTNGAQRFTNDVNDDSLNIIHKYDWTYTTRYKGTESSPESKFRLDNDQKLPLDKLAVHDKILFYDDMILFEDELADNGISILNVKIRVMNERLLLLSRFFLRVDDVLVRVYDTRIYVEFDENVVIRESKEFEGKYQDVLAKHRLSQSHDPKAALRDSNWVAQNTPMIKRQCEIIQF", "text": "FUNCTION: Involved in negative regulation of the TOR signaling pathway in response to type of available nitrogen source. Indirectly activates the PP2A phosphatase SIT4 via interaction with its suppressor TAP42. This interaction is enhanced under nitrogen limitation conditions. Also has a role in regulation of NPR1 in response to nitrogen limitation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the TIP41 family."}
{"protein": "MYRLAMRTWLAIVIVVVGTSLLFDTASASFIDNTCRGVMGNRDIYKKVVRVCEDCTNIFRLPGLDGMCRNRCFYNEWFLICLKAANREDEIEKFRVWISILNAGQ", "text": "FUNCTION: Inhibits Y-organs where molting hormone (ecdysteroid) is secreted. A molting cycle is initiated when MIH secretion diminishes or stops. Has little or no hyperglycemic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family."}
{"protein": "MAISWRTWLKKTIHCDNSYVRTGLAEFLGTFLLVLLLNGMIITAHMSVRNADGTMAHPLNTAHLAFGGGLAVMVAVLVSGGISGAHLNPAVTTTMLVMGRLSPLKSLVYIFMQYMGAFFAASILYAVYFESILAYDYGERQVLGANGTAGWFATYPQEHISLVTQIFDAILGTGLLVMGIFAIIDPNNMAVPKGQIPLYVGFLISSLIFSFSYNAGAALNPARDLAPRLFLWVIGYGAEAFTARGHLWWLVPVIGPHVGGLLGGVTYQMFIGAHYQSDRKLKPATIMDEDDDTNATYNTITTTTHQKVYNGRRNFDESVPLKTVHA", "text": "FUNCTION: Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis (PubMed:23761966). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MSRPESRSGNASTPQGTSVLKADDGGSGQTPGGSTENSVAYRYVAVQQMTSCRDHIEYQLTVREQPKQSRMCGVGEKADRRPIDPAPIVQLRVVTHDRPIRQSDPVGSASVAPPVERRPGQGAAAPQTPGVRRGLPVTTALGDGWEDKAWYLENPYYFMYAMLCNADTDEELHLLNDGKTRYTSGSCVSCLYHLKDIDGSHQGFFVFPDLSIRVEGRYRLKLCLFETIGHSVHHCKSIYSDPFHVYTAKRFPGMEESTRLSKSFAEQGLKVRVRKHPRSRRRGSKRTKDESDASDETPLARHVSPKRARASDVLPMSGLPMSQPIASSRMPRSMDDRFERADYDRTPSMASAYYDVKGAPPSRHAPWEEEEVLRLRESRAWDPMYDAPSALYSHHAREDRVEDRRLPPRDFADGRYMDGDYPPHTRSAAAPLSSMSARAGPSEYSEHVRSVYLRDDPVRSMHGSPHRLSAALPPLPPPLSKTPSHPALVGRGYPESSASLTPAYSRNYPSVPAPAPAPAPMPMRPAPLLSRSYDHIGQQSSGRIYDDYGPRPNVVAHYSGSYDPRDALARGFSPPSPQPGRRSPYASHHPPTQWRSGPPSPSRPSDYHLGRASAVERGYAAARRSPIPSARGIDTPPEAYAGFESNPFPRRSFGVPDAGRPAATYDAPRAPPADLYAPDEGPPSGRLGGIGFAPSSRERLILPPLPVPSPLSAHRGELTPLGTRDRDREAAYIAMPRDRDQGLAPTERYLSPSGYNPRAGELDQRDREWEWECERERERERERKRGPASPEYRRDFAQATMPSKPSSRGHNQPY", "text": "FUNCTION: Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (By similarity). The complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (By similarity). Required for gall induction and teliospore formation on seedlings (PubMed:24064149). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the velvet family. VosA subfamily."}
{"protein": "MRQRTIVCPLIQNDGCYLLCKMADNRGVFPGQWALSGGGVEPGERIEEALRREVREELGEQLILSDITPWTFRDDIRVKTYADGRQEEIYMIYLIFDCVSANRDICINDEFQDYAWVKPEELALYDLNVATRHTLALKGLL", "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": "MTGIAAASFFSNTCRFGGCGLHFPTLADLIEHIEDNHIDTDPRVLEKQELQQPTYVALSYINRFMTDAARREQESLKKKIQPKLSLTLSSSVSRGNVSTPPRHSSGSLTPPVTPPITPSSSFRSSTPTGSEYDEEEVDYEESDSDESWTTESAISSEAILSSMCMNGGEEKPFACPVPGCKKRYKNVNGIKYHAKNGHRTQIRVRKPFKCRCGKSYKTAQGLRHHTINFHPPVSAEMIRKMQQ", "text": "FUNCTION: Acts as a transcriptional corepressor of orphan nuclear receptor NR2C2 (By similarity). Inhibits expression of the gluconeogenesis enzyme PCK2 through inhibition of NR2C2 activity (PubMed:24380856). Also involved in transcriptional activation of NAMPT by promoting expression of PPARA and PPARD (PubMed:24930994). Plays a role in lipid metabolism by suppressing lipogenesis, increasing lipolysis and decreasing lipid accumulation in adipose tissue (PubMed:24380856, PubMed:25614086). Plays a role in glucose homeostasis by improving glucose metabolism and insulin sensitivity (PubMed:25614086, PubMed:24380856). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSVDTYTETTKIDKLLKKPTSHFQLSTTQLYNKILDNNEGVLTELGAVNASTGKYTGRSPKDKFFVSEPSYRDNIDWGEINQPIDEETFLKLYHKVLDYLDKKDELYVFKGYAGSDKDTMLKLTVINELAWHNLFAKNMFIRPESKEEATKIKPNFTIVSAPHFKADPEVDGTKSETFVIISFKHKVILIGGTEYAGEMKKGIFSVMNYLLPMQDIMSMHCSANVGEKGDVALFFGLSGTGKTTLSADPHRKLIGDDEHGWNKNGVFNIEGGCYAKAINLSKEKEPQIFDAIKYGAILENTVVAEDGSVDFEDNRYTENTRAAYPINHIDNIVVPSKAAHPNTIIFLTADAFGVIPPISKLNKDQAMYHFLSGFTSKLAGTERGVTEPEPSFSTCFGAPFFPLHPTVYADLLGELIDLHDVDVYLVNTGWTGGKYGVGRRISLHYTRQMVNQAISGKLKNAEYTKDSTFGLSIPVEIEDVPKTILNPINAWSDKEKYKTQAEDLIQRFEKNFEKFGEKVEHIAEKGSFNK", "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": "MAAPWVLPAPLSPAQLKRLEQHRYSSAGRSLLEPWLQPYWGWLVERLPPWLAPNAITLGGLLLNCLTALPLIASCPTATEQAPFWAYILGALGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSISTVFVVLGSCIAIRLGTNPDWLFFCCFVGLFMFYSAHWQTYVSGILRFGKVDVTEVQIAITMLLLVSAFCGTAVWDYKVHLVGLELKFFAVVGILCGTAVSCFNYFRIIFGGGVGKNGSTIAVAHMTKSEISLQDTAFIGPGLLFLDQYFNSFIDEYVVLWIALFISLFDMLRYATGVCLQIAAHLHIHVFRISSHQAPEQVQNHND", "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": "MNQLTHFNEQGRAKMVDVSDKSVSTRTAVAKSSIKVNEVIHDQIINHKNKKGDVLGVAQVAGIMAAKNTSQIIPMCHPLNLSGIDISFEWDISDGYEIFITCTVKTTGQTGVEMEALTGASATALTIYDMTKAVDKGMIIGPTYLEHKSGGKNGDFNR", "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": "MKGELIDITMKSGLKCDAYVSRPKDSQKELKPVIFVMDAFGLRDWLYEMADKIAEEGYFVVQPNFYYRIGKNIITNLEKLKSADTKDEVICQIRTQMAKINREETVSDVSEMFDFIDKQEGVRKSKEGVAIVGYCFGGGVAMRSAIAFPDIVKVVASFHAGRLAIPDDENSIHKHLKGVKAECYFGHADNDQSMPLDQIHLFEKSLTEAGIKYTSEIYNNPSCAHGWVMGDTLMYNPIGSDKHYDELFKLLKRAL", "text": "FUNCTION: Cysteine hydrolase. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the dienelactone hydrolase family."}
{"protein": "MPKAKAKTKNTEIISPHHYVYPNTTTLKNKYGIKNLNAFLEKCSHDTAKAMINLREESLPEYFDTAYLCHIHQQLFKNTFEWAGYLRHIPFTFADGTTAAMPEMKRTGWKNAFAIGDEIQEGLQRLDQTLAEKNNLQGLTREEFNSEAIELFNSLNQLHPFREGNGRTQRLFFENLAKAAGHQLNFSLITKERMMVASVAVAENGDLEPMQHLFEDISNPEKIRLLKEFMHTMKNTGRNVNDRPVMVAKEGETYTGTYRGAGLEGFALNVKGAYIIGNIDHLPPEQLKILKPGDKITFTAPKAEELKKTLIPKETLVPLTKLEIAEMVAEDAFVHTCRDQICSLSKIVYGSQGVLNKNIIEIIKNPSKGQQLATQIERTPYSVHSLAGFDLICFKTGARVRAEKHVALLSCAVANFTHAVKHARQEITKEHQAEQNRLRQEVPMPSQSLQDLLSLPKEFQQKALGVSPLLQKELTSLLQKVNSRLSSSEQRALRENNHETLAKNLGVSEQKAKEITKTVMKAREVQQKSQTRTVSHSKTLAMAS", "text": "FUNCTION: Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host target proteins. SUBCELLULAR LOCATION: Secreted. Note=Translocated into the host cell via the type IV secretion system (T4SS)."}
{"protein": "MLKLAGKEDKKLKTTVFQDETRIFNPPKELVEKSIVMQWMKKKGFKTEKEMRAWCSSDEHYLEFWDEMAKTYVDWHKPYTKVMDDSEMPYFHWFTGGEINITYNAVDRHAKGAKKDKVAYIWIPEPTDQPVQKITYGDLYKEVNKFANGLKSLGLKKGDRVSIYMPMIPQLPIAMLACAKLGVSHIVVFSGFSSKGLMDRAAHCGSRAIITVDGFYRRGKPVPLKPNADEAAGGAPSVEKIIVYKRAGVDVSMKEGRDVWWHDLVKGQSEECEPVWVDPEHRLYILYTSGTTGKPKGIEHATGGNAVGPAQTLHWVFDLKDDDVWWCTADIGWVTGHSYIVYAPLILGMTSLMYEGAADYPDFGRWWKNIQDHKVTVLYTAPTAVRMFMKQGAEWPDKYDLSSLRLLGSVGEPINPEAWMWYREHIGRGELQIMDTWWQTETGTFLNSPLPITPLKPGSCTFPLPGYDISILDEEGNEVPLGSGGNIVALKPYPSMLRAFWGDKERFMKEYWQFYWDVPGRRGVYLAGDKAQRDKDGYFFIQGRIDDVLSVAGHRIANAEVESALVAHPKIAEAAVVGKPDEVKGESIVAFVILRVGNEPSPELAKDAIAFVRKTLGPVAAPTEVHFVNDLPKTRSGKIMRRVVKARALGNPVGDISTLMNPEAVDGIPKIV", "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": "MIVTNDQELEGLKKIGRIVALAREEMKRKAEPGMSTKDLDLIGKAVLDEHGAVSAPEKEYDFPGVTCISVNDEVAHGIPSTSKILKAGDLVNIDISAEFGGFYSDTGISFVLGEGEERLHKLCQCAENAFQKGLQQAKAGKRQNQIGRAVYHEARSQGFTVIKTLTGHGIGRSLHEAPNHIMNYYDPFDNALFKNGTVIALEPFISTKAETIVEAGDGWTFKTPDKSMVAQVEHTIVITKDEPIILTKL", "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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily."}
{"protein": "MAGHSKFKNIQHRKGAQDTKRAKVFTKLIREIVIAAKTGSSNNPENNPRLRNALTAARIQNLPKERIDKALNSANDSSNNENYTEIRYEGYAQNGIAIIVEALTDNKNRTAAEVRSSFTKYGGSLGETGSVNYLFNHCGVIQYPINIASNEDVLEAVIEAGGHDIISDDTTHTIYTDIENFSKVLEFLTGKYGIPEDSYIGWIPLNTIIIDDKEKAEKLLKLVEVLEKSDDVQKVFGNYELSDDVYEIIQGEP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family."}
{"protein": "MVDTHKLADDVLHLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLKTLQPNEVAEMIENQGLFKDHVEDVNFQPIKYSALTSNNEECTAVVARGGTANAIRIATVDNPVNVNKLAQDSINIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND", "text": "FUNCTION: ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly. SIMILARITY: Belongs to the YFH7 family."}
{"protein": "MSRRNISKKRFPETDAIYNSYLVSLLISRILKSGKKTIAKKIVYQAFDIIKKKTNEDPLTVFEKAIRNASPIVEVKARRVGGSTYQVPVEVTGFRATNLSLRWIIRYGDQRVGRSMAIKLANEIIDTANDIGNTIKKKEETHKMAEANKAFAHFRY", "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": "MNYPVEWRISDSPVDYPQAIAAMEERVAAIRAGTAPELVWLLEHPPLYSAGTSADPRDLVDPGRFPVYETGRGGQYTYHGPGQRVAYVLLDLKRRGADVRVYVCNLEEWLIRTLARFVVKGERRTGRVGIWVDRGGGREDKIAAIGVRVRHWVTFHGIALNVDPDLSHFEGIVPCGIREHGVTSLWDLGLTPTMDDVDCALMATFPEVFGAD", "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": "MRSVTNAFGNSGELNDQVDETGYRKFDIHEGILFCIELSETMFKESSDLEYKSPLLEILESLDELMSQLVITRPGTAIGCYFYYCNREDAKEGIYELFPLRDINATFMKKLNDLLEDLSSGRISLYDYFMFQQTGSEKQVRLSVLFTFMLDTFLEEIPGQKQLSNKRVFLFTDIDKPQEAQDIDERARLRRLTIDLFDNKVNFATFFIGYADKPFDNEFYSDILQLGSHTNENTGLDSEFDGPSTKPIDAKYIKSRILRKKEVKRIMFQCPLILDEKTNFIVGVKGYTMYTHEKAGVRYKLVYEHEDIRQEAYSKRKFLNPITGEDVTGKTVKVYPYGDLDINLSDSQDQIVMEAYTQKDAFLKIIGFRSSSKSIHYFNNIDKSSFIVPDEAKYEGSIRTLASLLKILRKKDKIAILWGKLKSNSHPSLYTLSPSSVKDYNEGFYLYRVPFLDEIRKFPSLLSYDDGSEHKLDYDNMKKVTQSIMGYFNLRDGYNPSDFKNPLLQKHYKVLHDYLLQIETTFDENETPNTKKDRMMREDDSLRKLYYIRNKILESEKSEDPIIQRLNKYVKIWNMFYKKFNDDNISIKEEKKPFDKKPKFNI", "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. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. 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. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the ku70 family."}
{"protein": "MSTLDTPLVVAGKTYHSRLMVGTGKYQDLEETQNAIQASGAEIVTIAIRRSNIGQNPGEPNLLDVISPHCYTLLPNTAGCYNAKEAVRTCRLARELLDGHSLVKLEVLGDEKTLFPDLVETYQAAEVLIKEDFQVMVYTNDDPIAAKRLEEMGCVAVMPLAAPIGSGLGIRNPYNILEIVQNATVPILVDAGVGTASDAAVAMELGCDGVLMNTAIAGAQNPILMASAMKKAVEAGRDAYLAGRIPRRRYASASSPLEGTFF", "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": "YFFPLFLVTIFLYKWLVKKTPSKNLPPSPPRLPIIGNLHQIGPDPQISLRDLAREYGPVMHLKFGSVPVLVVSSADGAREIFKTHDLVFADRPYSSVANRIFYNGRDMVFARYTEYWRQVKSTCVTQLLSVKRVQSFHNVREEEVALLLDNIENSKSKVINLSEMLIELTGNVVCRAALGSGYNVDSYKSLLLQIMDMLGYSRSIEDFFPSLGWVDWITGLKGKVEKAANGVDAFLEGVLKNHTNPSTSSANKDFVSILLEIQEADAGSSMDKECIKSLIWDMLGAGTETIATALEWTIGALIKSPDAMSKLQKEVREIGKGKSRIEEGDLVKMDYLKAVMKESMRLYFTAPLLVPREARQDVKFMGYDIKSGTQVLINAWAIARDPSSWDNPEEFRPERFLNSPIDYKGFNYEYIPFGAGRRGCPGIQFAISVNELVVANVVNKFNFELPDGKRLEEMDMTASTGITFHKKS", "text": "FUNCTION: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes (PubMed:29971079). Involved in linear furanocumarin (psoralen) biosynthesis (PubMed:19098286). Converts marmesin to psoralen and, with much lower affinity, 5-hydroxymarmesin to bergaptol (PubMed:19098286). SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MTKAVLTSISQLALKALLYEVSLSPKPGLVDRFDNGAHDDMSFMTFIDSMIALSPFFQAYIETGFAYAKEEPLLLFNRLRQLGQKAEETMFCATQGINTHKGLNFSMALLLGATGAYLARTPHLMTDLGRFSKEDTLAICRLVKPMTAHLIQTDLGHLNTKKEFTYGEQLFVTYGIKGPRGEASEGFTTLTDHALPYFRQMISQNDPETSQLRLLVYLMSIVEDGNLIHRGGIEAWKGVKADMRLLLQQDLSTTDLRLALSSYNQCLINQHLSPGGAADLLALTFYFAFLEKLL", "text": "SIMILARITY: Belongs to the CitG/MdcB family."}
{"protein": "MNIHEYQGKDILRKFGVAVPRGIVAYSPEEAKQAAEQLFDELGCPVVVIKAQIHAGGRGKAGGVKLAKSPEESLDIAHQLIGMTLITHQTGPEGKEVRRVLVEEGMNIEKEFYVGITLDRSTSKNVLMVSTEGGMEIEKVAEETPERLLKIQIDPLFGMQGFQAREAAFFLGLKGEQFRNAVNFITALYNAYISIDAALAEINPLVVTKEGKVLALDAKINFDDNALFRHKEFHELRDTNEEDPFEVEASKSNLNYVRLDGNVGCMVNGAGLAMGTMDMIQLAGGKPANFLDVGGSASPQTVEEGFKIILSDKNVKAILVNIFGGIVRCDRVAGGIIEAAKKIDLHLPVIVRLEGTNAPIAQKMLDDSGLNLIAAKGLRDAAQKVQEALAAS", "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": "MVEPLLSGIVLGLITVSALGLFVAAFLQYRRGNQFEI", "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": "MNLAEENTIFKPLYSLKHSSINAYFSKNSDDFVVRERPLYEFSGKGEHLILHINKKDLSTNEALKILSEQSGVKMRDFGYAGLKDKQGSTFQYLSIPKKFESFLSNFSHSKLKILETFTHENKLRIGHLKGNSFFIRLKKVMPSDALKLEQVLMNLDKQGFANYFGYQRFGKFGDNYKEGLEILRGKKMKNIKMKEFLISAFQSDLFNRYLSKRVELSHFANDFSEKELLQIYKISKEEAKELKKQEQFFKLLKGEVLGHYPFGKCFLCEDLSAELERFRARDISAMGLLIGTKAYETGEGLALNLENEIFKDALEFKAKMQGSRRFMWRYLEELKWRYDEEKAHFCIEFFLQKGSYATVVLEEILHKNLPE", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
{"protein": "MPNHSSAKKMVRVIKERTFSNRVRKSRVRNSVKKFLAVLESKGHLEDAVTAFRAAESNIHKCVNKGVMHRNTAARKVKSLAAKLKAFDLSLQGTST", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
{"protein": "MTSMFSLKGKTTLITGGSGGIGFSIAKAFAAAGSNVGLLYGRNKKALEYAAELRDKHGVQAKAYSCPIENRSAVIETTNQAVEELGGRLDVMIANAGIAIPHLSLEDKNEDIWTKVVGINLNGAYYTAQAAGHHFKKQGKGSLIFTASMSGHIANWPQQWASYHATKAAVKHLARALAVEWAPFARVNSVSPGYIDTDLTLYADENLRKKWKEYTPQARIGLPDELPGAYLYLASDASSYCTGSDIIVDGGYCSR", "text": "FUNCTION: Catalyzes the NADP dependent reduction of L-sorbose to D- glucitol. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLVEEFKSGNIERECIEERCSKEEAREVFEDDEKTETFWNVYVDGDQCSSNPCHYRGICKDGIGSYTCTCLSGYEGKNCERVLYKSCRVDNGNCWHFCKSVQNDIQCSCAEGYLLGEDGHSCVAGGNFSCGRNIKTRNKREASLPDFVQSHNATLLKKSDNPSPDIRIVNGMDCKLGECPWQAALVDDKKGVFCGGTILSPIYVLTAAHCINETETISVVVGEIDRSRAETGPLLSVDKVYVHKKFVPPKKSQEFYEKFDLVSYDYDIAIIQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIVSGFGGIFERGPNSKTLKVLKVPYVDRHTCMLSSNFPITPTMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIVSWGEGCARKGRYGIYTKLSKFIPWIKRIMRQKLPSTESSTGRL", "text": "FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V (PubMed:12362232, PubMed:23869089). It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (PubMed:12362232, PubMed:23869089). The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271) (PubMed:23869089). Cleavage at Arg-271 releases active thrombin from its pro-fragment (PubMed:23869089). This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis (PubMed:23869089). The complex converts prothrombin to thrombin in presence but also in the absence of membrane (PubMed:23869089). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MAESIEMGEELVSSPSTLLALKGKLENPSPDDATILGILGKKTPTVKMEKGKGKGDPIEAFLLEFVDERRQVEANKRLRQYIRQLKMSHQEELTAHLERASAENRANLKSMMESQAESNKTTKTILATLITLRDHVIEEGSKKPRGLDKDQIKLERALGFERGYSSAIAIVNQLKVTEPSQVCKPSVRAAALSAMEKGEFESSGEVFKAVVKRAKAELTK", "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 (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm."}
{"protein": "MTQQFYVSPEQLMKDRADFARKGIARGRSVVVISCEEGIALVAENPSPSLHKIGEIYDKIAFAAVGKYNEFESLRQAGVRYADVRGYSYDREDVTARGLASVYAQSLGAVFTAEQKPFEVELAVAEVGGNQSDDHLYRLTFDGSIADEKRFIVMGGQADKVAETVEGGWQQELNFAGAIRLAMKGLVTDKEAGELPASALEVAVLDRASESTRGSRRAFRRLGDDEIAALLSKEN", "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": "MNPLPEQYANTALPTLPGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLIQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG", "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": "MLNKRLTIQLPFYATQTASSSRFWRVLSPKSRTGIALYASLILLCIFFTIFSTMSHPSLQCFSPTSLVGAQPLKNLTHLIIVAGHAVWLGGSTNGEDDSEWILEPYQKGEGKVFAQHVRSGLDLLSQDDSSLLVFSGGQTRNGAGPSSEAQSYYSLSMQINSDEGLAARRTTEEFARDSLENVLFSVARFYEVTSRYPQKITVVSFDFKRDRFLNLHRKAIKFPEHKFHFVGIDPEGGVSDATREAERKNAIIPFTEDPYACSNPLLVKKRMERNPFRRQHSYLITCPELIPLLQYCPSDPSKFFNGKLPW", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: To yeast YOR238w."}
{"protein": "MSKLFSEYKLKDVTLKNRIVMSPMCMYSVENKDGIATDFHFAHYVSRAAGGTGLVILEATAVQEVGRISEFDLGLWNDEQVPALKRLVDGLHYHGAKAGIQLAHAGRKAVLPGEIVAPSAIPFDEKSAKPVELTKEAIKEVVADFKRAAYRAKEAGFDVIEIHAAHGYLIHQFLSPISNRREDNYGGPAGNRYKILSDIIKAVKEVWDGPIIVRVSATDYAHGGLQLEDHIPFAKWMKADGVELIDVSTGGLVNVEPPVFPGYQVPFADEIRRGAGIATGALGLITRGEQAEEILCNERADLIIIGRELLRNPYFAKEAAETLGETIEAPKQYSRAWK", "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": "MEKTVYSVEGVALRSVELDESVFGLSVNRGVIYYAINSELSNKRLGTACTKGRSEVHGSNTKPYKQKGTGRARRGDKKSPLLVGGGTIFGPKPRDFHYALPKKVKRLAMKSLLSLKAQGDALTVIEDFTVESGKTRDLIQVLRHFAQRERTVFILQNDDALLKRAGRNIPTLSFLSYNRLRAHDLFYGRKVLVLETAVHKIADFYRSKDAAQDGTY", "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": "MERYDILRDLGSGNFGVAKLVREKANGEFYAVKYIERGLKIDEHVQREIINHRDLKHPNIIRFKEVFVTPTHLAIVMEYAAGGELFERICNAGRFSEDEGRYYFKQLISGVSYCHAMQICHRDLKLENTLLDGSPSSHLKICDFGYSKSSVLHSQPKSTVGTPAYVAPEVLSRKEYNGKIADVWSCGVTLYVMLVGAYPFEDPEDPRNIRNTIQRILSVHYTIPDYVRISSECKHLLSRIFVADPDKRITVPEIEKHPWFLKGPLVVPPEEEKCDNGVEEEEEEEEKCRQSVEEIVKIIEEARKGVNGTDNNGGLGLIDGSIDLDDIDDADIYDDVDDDEERNGDFVCAL", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MEQRKTQVSSHPFSVESLISSHKTNKDFERRREDVSSQFAQTEIRDSCGSAGIPKHFMLQTSPVKSESPEPDDCTSWVMNSRYSQTRQESPCPLRKHKTNRKPRTPFTTSQLLALERKFRQKQYLSIAERAEFSSSLTLTETQVKIWFQNRRAKAKRLQEAELEKLKLTAKPALHPNFSLPLPLGTQLHSAVSLYGQSYPYQRPLLPVAPVGLYGTPLGYSMYHLA", "text": "FUNCTION: Involved in the development of the inner ear. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Msh homeobox family."}
{"protein": "MGSSSLLLFPSSSSSATHSSYSPSSSSHAITSLLPPLPSDHHLLLYLDHQEQHHLAAAMVRKRPASDMDLPPPRRHVTGDLSDVTAAAAPSSASAQLPALPTQLPAFHHTDMDLAAPAPPPPQQQVAAGEGGPPSTAWVDGIIRDIIASSGAAVSVAQLIHNVREIIRPCNPDLASILELRLRSLLTSDPAPPPPPPPSHPALLPPDATAPPPPPTSVAALPPPPPPQPDKRRREPQCQEQEPNQPQSPKPPTAEETAAAAAAAAAAALAAAKERKEEQRRKQRDEEGLHLLTLLLQCAESVNADNLDEAHRALLEIAELATPFGTSTQRVAAYFAEAMSARLVSSCLGLYAPLPNPSPAAARLHGRVAAAFQVFNGISPFVKFSHFTANQAIQEAFEREERVHIIDLDIMQGLQWPGLFHILASRPGGPPRVRLTGLGASMEALEATGKRLSDFADTLGLPFEFCPVADKAGNLDPEKLGVTRREAVAVHWLRHSLYDVTGSDSNTLWLIQRLAPKVVTMVEQDLSHSGSFLARFVEAIHYYSALFDSLDASYSEDSPERHVVEQQLLSREIRNVLAVGGPARTGDVKFGSWREKLAQSGFRVSSLAGSAAAQAALLLGMFPSDGYTLIEENGALKLGWKDLCLLTASAWRPIQASGR", "text": "FUNCTION: Transcription factor required for quiescent center cells specification and maintenance of surrounding stem cells, and for the asymmetric cell division involved in radial pattern formation in roots. Essential for cell division but not differentiation of the ground tissue. Regulates the radial organization of the shoot axial organs. Restricts SHR movment and sequesters it into the nucleus of the endodermis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIVQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEIFDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQALKAGKTIMLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV", "text": "FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities. SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily."}
{"protein": "MSQTFAVILLLLIFLTHLVSSLIQDFSFIGFKKASPNLTLNGVAEIAPTGAIRLTTETQRVIGHAFYSLPIRFKPIGVNRALSFSTSFAIAMVPEFVTLGGHGLAFAITPTPDLRGSLPSQYLGLLNSSRVNFSSHFFAVEFDTVRDLEFEDINDNHVGIDINSMESSISTPAGYFLANSTKKELFLDGGRVIQAWIDYDSNKKRLDVKLSPFSEKPKLSLLSYDVDLSSVLGDEMYVGFSASTGLLASSHYILGWNFNMSGEAFSLSLPSLPRIPSSIKKRKKKRQSLILGVSLLCSLLIFAVLVAASLFVVRKVKDEDRVEEWELDFGPHRFSYRELKKATNGFGDKELLGSGGFGKVYKGKLPGSDEFVAVKRISHESRQGVREFMSEVSSIGHLRHRNLVQLLGWCRRRDDLLLVYDFMPNGSLDMYLFDENPEVILTWKQRFKIIKGVASGLLYLHEGWEQTVIHRDIKAANVLLDSEMNGRVGDFGLAKLYEHGSDPGATRVVGTFGYLAPELTKSGKLTTSTDVYAFGAVLLEVACGRRPIETSALPEELVMVDWVWSRWQSGDIRDVVDRRLNGEFDEEEVVMVIKLGLLCSNNSPEVRPTMRQVVMYLEKQFPSPEVVPAPDFLDANDSMCLDERSGSAGEFEDFVDSARFYSGPNETTTSSIFSFSGKTRTDPR", "text": "FUNCTION: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae. 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": "MSEKLICNNKKAYHDYFIEEKFEAGMVLKGTEVKSLRIGKANLNDSFALVKNGEAFLHNLHISPYDFGNRENHDPDRMRKLLLHKKEIGKLFSMIREQGYTVVPLRLYFKDGLVKVEVGLAKGKKLYDKREDMKKKDMRRDVAVALKERNR", "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": "MKALYMVFVLWVLIGCFLSSECQRGFRGQHDPTRPLSPSNPSSHFYPQPDPNRVQISQPDNIPIFMFEQPHSLNICVPPPPLYLGEEFEKLPPNTHIPYILIRPDIEPPSKYIQPVPRKKSNATPAANNFITTATAPNSTDSF", "text": "FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MAKRCEVCGKGVVSGVQYSHSHRQSKRRWAPNIKSVRAVVNGVPKKVSVCTRCLRSGKVQRAI", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MAPGGLLTLAGAAAASTAAAAYLDAKLHLTKDLNQLARAERGAQNFARAVEQRKASGFFLFEAAAARLGDAPCIWSRGHPEYSWTQTYQRACQYGHYFRDLGVVAGQHVGVYLYNSPELMFIWMGLLSIGAAPALINYNLGSDALVHCVRLSRSRFLIYDDASDCSSRIHEVGERLRDINVEAIMLSGSGTTGLPKAAPITVARNYPSASLLPKTFGQKPGPNGDRTYYCIPLYHGTGGIAAMNDLMSGISIALAPKFSLSRFWDDCIESGSTIFVYVGELIRYLLSAPASPKDRQHRVRLVWGNGLSPELWTKFQDRFGVSDIGEFYASTEGVLTLLKHYRGGGFGLGAVGHHGWLLRRKFHNDYVPVRIDPETGDIWRSPKTGFAERLPYERGGEILARLPSRSAWAGYWHAEEATQKKLVENVFEKGDLYFRTGDALRRDADGHWYFLDRLGDTYRWKGENVSTTEVGQVLGSHADIAEANVYGVQVPNHDGRAGCAAIALKNAATPDTLDWSRLTSLLRSELPSYAVPVFIRVRETVGGMSTDNHKHNKVPLRDEGVDPRSMGSKVPGSEKDRFFWLPAGASKYVPFTERDWDLLSGQSAARPRL", "text": "FUNCTION: Together with cefD2, catalyzes the reversible isomerization between isopenicillin N and penicillin N. This two-component IPN epimerase system may function by two sequential steps, an activation of isopenicillin N by the acyl-CoA synthase component cefD1, followed by epimerization by the acyl-CoA racemase component cefD2. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MARGRKMSKPRAVEAAAAAAAVAATAPGPEMVERRGPGRPRTNGENVFTGQSKIYTYMSPNKCSGMRSPLQEENSVAQYEVKCQGKPLAGIYRKRDEKRNSGNAIRSSMKAEEQKIKDARRGPLAPFPNQKSEAAEPPKTPTSSCDTPNAAAAKQGLKKPVRGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGEFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIEAGEELLYDYGDRSRASIEAYPWLKH", "text": "FUNCTION: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF- beta response regulation and a positive role in cell migration. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms. Colocalized with SIRT2 at mitotic foci. Associates with chromosomes during mitosis; association is increased in a H(2)O(2)- induced oxidative stress-dependent manner. Not associated with constitutive heterochromatin (By similarity). SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. PR/SET subfamily."}
{"protein": "MPELKIKTEKVEKQLTKEPLVLKTPKEKIDNLGKFYATGKRKNAIARVWLKVGKGKIVVNKKTIAQYFPSETYVKTILQPFVLTKTIDQYDIICTVRGGGISGQKGAILHGISKALDKSAPDFRAILRKGGLLTRDSRVVERKKYGQRKARKKTQFSKR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MSFQVSVAVNDGPFQKKSVTPNTTIGDLNNDAILIWKDTAIVYDISDESKNFGPTVTLEQLGVTQISMVYIYTTAFPCPSGDLRSIVPAQVRLISQFASAASSIFNGQSSSSAQSAQRTRRVEQDDEGEKSMFSRKLLDSPATFKALSENMFFRLKNEPHKLGYGLPELVERFLAKKDMTYKEFEQMFRSYVEEEVHKEEIIKNNPNSAEAKMFLEAKRNKELIDEQYLHSMTHHPEDMIAVTMLYINLTINGVPVKAFIDSGAQKSIMSMACAERCGLNGLIDRRFQSMARGVGGTEKIEGKIHLCDVKVEDAHFSCPFEVMARREMDLLIGLNVLRKHGCCINLKTSRLEFGNGTTTPFLQSNEIDSHLKEIMALPEEEMQFEDGST", "text": "FUNCTION: Aspartic protease. Required for the cleavage and activation of transcription factors such as isoform a of the transcription factor skn-1, which in turn regulates the expression of proteasomal subunits such as rpt-3. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly localizes to the nucleus during proteasomal disruption. SIMILARITY: Belongs to the DDI1 family."}
{"protein": "MAQGQRKFQARKPAKSKTAATASEKNRGPRKGGRVIAPKKARVVQQQKLKKNLEVGIRKKIEHDVVMKASSSLPKRLALLKAPAKKKGAAAATSSKTPS", "text": "FUNCTION: May have a potential role in hypercalcemia of malignancy. SIMILARITY: Belongs to the UPF0390 family."}
{"protein": "MAAAGGITMRQLLEAGVHFGHQTKRWNPKMKPFIFGARNGIYIIDLQKTVVMARSAFRFVADITARGGSVLFVGTKKQAQDVVREEASRAGQFFVTSRWLGGTLTNFKTIKQGIDRLKTLEKMAEDGTFERLPKKEVAQLEREREKLEKNLGGVKEMSKLPRCVFVIDPKKEHIAIHEAGRLGIPVIGLVDTNCDPDGIDFVIPGNDDAIRSIKLFTSKIAEACLEGAARYRASGAAERDEQEEREGRDDRGDRRDDRRGPRRGDRRDDRRDRGGDRGGDRRGPLVEMKGAAPVASAEPAAEAAPEGEAAAE", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MPTINQLIANPRKIQKSRNKVPALEACPQKRGVCTRVYTTTPKKPNSALRKVAKVRLTNGFEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHILRGVLDTQGVKNRKQRRSKYGAKRPK", "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": "MNDTQDFISAQAAVLRQVGGPLAVEPVRISMPKGDEVLIRIAGVGVCHTDLVCRDGFPVPLPIVLGHEGSGTVEAVGEQVRTLKPGDRVVLSFNSCGHCGNCHDGHPSNCLQMLPLNFGGAQRVDGGQVLDGAGHPVQSMFFGQSSFGTHAVAREINAVKVGDDLPLELLGPLGCGIQTGAGAAINSLGIGPGQSLAIFGGGGVGLSALLGARAVGADRVVVIEPNAARRALALELGASHALDPHAEGDLVAAIKAATGGGATHSLDTTGLPPVIGSAIACTLPGGTVGMVGLPAPDAPVPATLLDLLSKSVTLRPITEGDADPQRFIPRMLDFHRAGKFPFDRLITRYRFDQINEALHATEKGEAIKPVLVF", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of geraniol to geranial. Is involved in the anaerobic degradation of the monoterpene beta-myrcene. Can also catalyze the oxidation of (S)-perillyl alcohol to perillyl aldehyde, and to a lesser extent, the oxidation of nerol, citronellol, cumic alcohol, and benzyl alcohol. Cannot use NADP(+) instead of NAD(+) as cosubstrate. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MKNKLKKKKNPKGTKKIKAKAKAHKVGTTKVKVKKKIYTIGTLHDLPSQIESYSDKESYSDKESYSDKESYSDKESYSDKESYSDKNILVKIFYEPEIRYLTPLEIETKPENKYCFFKKNNIKYIDFKNPSFLMKFLNERGEILPRRITGTSKKFQKKLKRAIKKCKHIGLLPYLTDGLR", "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": "MTSAEPRAYPFNDVHGLTLAGRYGELQETEPVSRVRPPYGEEAWLVTRYEDVRAVLGDGRFVRGPSMTRDEPRTRPEMVKGGLLSMDPPEHSRLRRLVVKAFTARRAESLRPRAREIAHELVDQMAATGQPADLVAMFARQLPVRVICELLGVPSADHDRFTRWSGAFLSTAEVTAEEMQEAAEQAYAYMGDLIDRRRKEPTDDLVSALVQARDQQDSLSEQELLDLAIGLLVAGYESTTTQIADFVYLLMTRPELRRQLLDRPELIPSAVEELTRWVPLGVGTAFPRYAVEDVTLRGVTIRAGEPVLASTGAANRDQAQFPDADRIDVDRTPNQHLGFGHGVHHCLGAPLARVELQVALEVLLQRLPGIRLGIPETQLRWSEGMLLRGPLELPVVW", "text": "FUNCTION: Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes consecutive hydroxylation (at C14) and epoxidation (at C12-C13) reactions with mycinamicin IV as initial substrate, leading to mycinamicin II. These reactions require prior dimethylation of 6-deoxyallose to mycinose for effective conversion by the dual function MycG enzyme. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLAGCYPRPGDLLTRVLATGTFDILHPGHVYFLTQARALGDELFVIIARDSNVTHKPKPIVPEEQRLEMVNALGTVDKALLGSEKDMFEPLKEIRPDIIVLGYDQHFDIELLEEELTKRGLPAKVVRVPLSKECPLCSTGAIIKAVLKRYG", "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": "MTATSPYLELGYVARAHGLRGEVAIRALDPASETLDTVDRIWVRTRAGVEREMRLEALRPTPKEDIVVLEGVESRNDAEALVGAKVFVFREDLEPPAEGEFFQGDLVGLDAVDANGNALGRVEEIWTTGEVPNLVIRASGREELVVPFADEFVPTVDLEARRIVIHPPEYVEAGRKGAESGGGPEDAE", "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": "MKKIDVKILDPRVRKEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ", "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": "MRVLCTNDDGVNAPGLKVIEEIADQLSDDVWIVAPELDQSGVSHSLSLNDPLRLREIGPRLFAVRGTPTDCVIMGSRHVLGDKQPNLVLSGVNKGRNVAEDVVYSGTIAGALEGTILGLPSFALSQEFGGPQNRDKPMWDVARAFGADVIRKVMSVGVPTDTVININFPACAPEEVKGVVVTRQGKRNQGFLRIDGHYDGRGNPYYWIGFEKFPVPDIPGEGTDLAALEGNYVSVTPLRLDRTDMRFSEQLANLFNTP", "text": "FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family."}
{"protein": "MGGKWSKSSVIGWPTVRERMRRAEPAADGVGAASQDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC", "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": "MYQPDFPTVPFRLGLYPVVDSVAWIERLLEAGVRTIQLRIKDKRDEEVEADVIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQEDLETTDLKAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIDRLADYPTVAIGGISVERAPAVLATGVGSIAVVSAITQAADWRAATAQLLDIAGVGDE", "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": "MTGKSVKDVDRYQAVLANLLLEEDNKFCADCQSKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQEQIQCMQEMGNGKANRLYEAYLPETFRRPQIDPAVEGFIRDKYEKKKYMDRSLDINAFRKEKDDKWKRGSEPVPEKKLEPVVFEKVKMPQKKEDPQLPRKSSPKSTAPVMDLLGLDAPVACSIANSKTSNTLEKDLDLLASVPSPSSSGSRKVVGSMPTAGSAGSVPENLNLFPEPGSKSEEIGKKQLSKDSILSLYGSQTPQMPTQAMFMAPAQMAYPTAYPSFPGVTPPNSIMGSMMPPPVGMVAQPGASGMVAPMAMPAGYMGGMQASMMGVPNGMMTTQQAGYMAGMAAMPQTVYGVQPAQQLQWNLTQMTQQMAGMNFYGANGMMNYGQSMSGGNGQAANQTLSPQMWK", "text": "FUNCTION: GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci throughout the cytoplasm and in juxtanuclear structures."}
{"protein": "MDLSEPIHDFLLVFLGSGLILGGLGVVLLPNPIYSAFSLGLVLICTSLFYILSNSYFVAAAQLLIYVGAINVLIIFAVMFMNGSEYYKDFHLWTVGDGITSMVCISLFISLITTISDTSWYGIIWTTRSNQIIEQDFLSNSQQIGIHLSTDFFLPFELISIILLVALIGAIAVARQ", "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": "MNTSDFDFNLPEALIAQTPLKKRDSSKLLVVDHQKKTMKDTHFDHIIDELNSGDALVMNDTRVLPARLHGEKTVTHGHVELLLLKNIQGDQWEVLAKPAKRLKVGSHISFGDGRLKAIIKEELDHGGRIVEFSYEGIFLEVLESLGEMPLPPYIHEKLEDRDRYQTVYAKENGSAAAPTAGLHFTEELLSKIEAKGVKLVYLTLHVGLGTFRPVSVDNVEEHQMHSEFYSLSPEAAQTLKDVKANGGRIVAVGTTSIRTLETIGNKFAGQIEADSGWTNIFIKPGYQFKIVDAFSTNFHLPKSTLVMLVSAFAGRDFILDAYKHAVDKHYRFFSFGDAMFVK", "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": "MGCNPPYLLSYRLRLLLLFTLCLTVLGWATSNYFVGAIQVIPRAKNFMATLHKVMYLGNEETLGHGAAMKKAELANCPSVSPNLRGQNKLVFKPDLTLEEVQAKNPKVSRGRYRPEECKALQRVAVLIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYVIHQTGSKKFNRAKLLNVGYLEALKEENWDCFIFHDVDLVPENDFNLYTCGDQPKHLVVGRNSTGYRLRYSKYFGGVTALSREQFFKVNGFSNNYWGWGGEDDDLRLRVELHKMKISRPKPDVGKYTMIFHTRDKGNEVNGSRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVDFWTAA", "text": "FUNCTION: Galactose (Gal) transferase involved in the synthesis of terminal N-acetyllactosamine (LacNac) unit present on glycan chains of glycoproteins and glycosphingolipids. Catalyzes the transfer of Gal residue via a beta1->4 linkage from UDP-Gal to the non-reducing terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in the linearly growing chain of both N- and O-linked keratan sulfate proteoglycans. Cooperates with B3GNT7 N-acetyl glucosamine transferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6- sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6- sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Transfers Gal residue via a beta1->4 linkage to terminal 6-O-sulfoGlcNAc within the LacNac unit of core 2 O-glycans forming 6-sulfo-sialyl-Lewis X (sLex). May contribute to the generation of sLex epitope on mucin-type glycoproteins that serve as ligands for SELL/L-selectin, a major regulator of leukocyte migration. In the biosynthesis pathway of neolacto-series glycosphingolipids, transfers Gal residue via a beta1->4 linkage to terminal GlcNAc of a lactotriaosylceramide (Lc3Cer) acceptor to form a neolactotetraosylceramide. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Secreted. SIMILARITY: Belongs to the glycosyltransferase 7 family."}
{"protein": "MSITKEFDTITAISTPLGEGAIGIVRLSGTDAIAIANKVFKGKNLETVDSHTINYGHIVENNEIIDEVMVSVMRAPKTFTREDVVEVNTHGGVAVTNEILQLLIRSGARMAEPGEFTKRAFLNGRIDLTQAEAVMDLIRAKTDKAMTVAVSQLDGSLKNLINNTRQEILNTLAQVEVNIDYPEYDDVEEVTTNLVREKTQEFQALLENLLATAKRGKILREGLSTAIIGRPNVGKSSLLNNLLREEKAIVTDIEGTTRDVIEEYVNIKGVPLKLIDTAGIRDTDDVVEKIGVERSKKALEEADLVLLVLNSSEPLTDQDRTLLDISQNSNRIILLNKTDLPQAIQTEELPEDLIPISVLKNENIDKIEDRINQLFFDNAGLVEKDATYLSNARHISLIEKALESLEAVNQGLELGMPVDLLQVDMTRTWEILGEITGDAAPDELITQLFSQFCLGK", "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": "MSGAALGLEIVFVFFLALFLLHRYGDFKKQHRLVIIGTLLAWYLCFLIVFILPLDVSTTIYNRCKHAAANSSPPENSNITGLYATANPVPSQHPCFKPWSYIPDGIMPIFWRVVYWTSQFLTWILLPFMQSYARSGGFSITGKIKTALIENAIYYGTYLLIFGAFLIYVAVNPHLHLEWNQLQTIGIAAANTWGLFLLVLLLGYGLVEIPRSYWNGAKRGYLLMKTYFKAAKLMTEKADAEENLEDAMEEVRKVNESIKYNHPLRKCVDTILKKCPTEYQEKMGRNMDDYEDFDEKHSIYPSEKSLVKLHKQVIYSVQRHRRTQVQWQILLEQAFYLEDVAKNETSATHQFVHTFQSPEPENRFIQYFYNPTFEWYWECLLRPWFYKILAVVLSIFSVIVVWSECTFFSTTPVLSLFAVFIQLAEKTYNYIYIEIACFLSIFFLSICVYSTVFRIRVFNYYYLASHHQTDAYSLLFSGMLFCRLTPPLCLNFLGLTHMDSSISHKNTQPTAYTSIMGSMKVLSFIADGFYIYYPMLVVILCIATYFSLGTRCLNLLGFQQFMGDDDMTSDLVNEGKELIRKEKRKRQRQEEGENRRREWKERYGHNREDSTRNRNIHTDPKESNFSDVNTNRSAFKYTRANNRTERDRIELLQDAEPLDFNAETFTDDPLESESGRYQPGGRYLSMSRSDIFNDV", "text": "FUNCTION: Recruited to ligand-activated beta-2 adrenergic receptor/ADRB2, it negatively regulates the adrenergic receptor signaling pathway (PubMed:28388415). May also regulate other G-protein coupled receptors including type-1 angiotensin II receptor/AGTR1 (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LIMR family."}
{"protein": "MGVRAQQKERTRRSLIEAAFSQLSAERSFASLSLREVSREAGIAPTSFYRHFRDVDELGLTMVDESGLMLRQLMRQARQRIAKGGSVIRTSVSTFMEFIGNNPNAFRLLLRERSGTSAAFRAAVAREIQHFIAELADYLELENHMPRSFTEAQAEAMVTIVFSAGAEVLDVDAEQRRQLEERLVLQLRMISKGAYYWYRREQEKLAVSRA", "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": "MKNYLLQIEYFGKNYCGWQRQSHSLSVQEELEKALSKIANQNIEVTCAGRTDTGVHATSQIVNFYSNAYRPLSAWQRGVNALLPQDIKILAVQQVNNNFNSRFTAINRTYNYIIYNSATSSPIFAEHCLWENRELDIDKMNQACEYLLGEQDFSSFRSSQCQSNTPFRNIQKAEFIKQGSFIVFEVVGNAFLHHMIRNLVGSLLKVGLGFESPEWIKVVLEAKDRTQAAETAKAHGLYFVGVEYPEFSFKRQIIKLFC", "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": "MKEVRIEAGWKKVLQEEFDKFYFEKLTDFVREEYRQSPIYPPARFIFRAFDTCPFDRVKVVILGQDPYHEPGQAEGLAFSVPTGIPIPPSLRNICEEIRTDTGQPAHIDGGSLLPWVEQGVLLLNATLTVRASQAGSHQGHGWETFTDAAIEALAKRREHLVFLLWGSYARRKSAMIDPRCHLILEAPHPSPLSAHRGFFGCKHFSRTNAYLRQHGIAPIVW", "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": "MTTNTVSRKVAWLRVVTLAIAAFIFNTTEFAPVGLLSDIADSFGMETAQVGMMLTIYAWVVALMSLPFMLLTSKVERRRLLIGLFILFIASHVLSFFAWNFDVLVISRIGIAFAHAVFWSITSALAIRMAPPGKRAQALSLIATGTALAMVFGIPIGRIIGQYFGWRMTFLAIGLGALATLACLVKLLPTLPSEHSGSLKSLPVLFRRPALVSVYILTVVVVTAHYTAYSYIEPFVQTVAGLSGNFATVLLLILGGAGIIGSILFGKLGNQHASGLISLAIALLLACLLLLLPASHNPQHLMLLSIFWGVAIMIIGLGMQVKVLASAPDATDVAMSLFSGIFNIGIGAGALVGSQVSLHLSMASVGYVGAIPALVALVWSLMIFRRWPVSLEDHQPHHS", "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": "MCATYMFNITVIITHPTPTLRTRGPGFVRNRDLYIYKYKSNLINNLNNMTYIL", "text": "SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MTVRTRVAPSPTGDPHVGTAYIALFNRCFAQQHGGQFILRIEDTDQTRSTDQSEQMILDSLKWLGLTWDEGPDVGGPHGPYRQSERKGIYRQYAEQLIEKGHAFKCYRTSEELDALRAGLKESGENRALKPSDLELPADEQAKREADGAPYVIRMRVPTEGRCEIHDMLRGPVELDWALVDAQILLKSDGMPTYHLANIVDDHLMEITHVIRGEEWLNSAPKHKLLYEYFGWEMPVLCHMPLLRNPDKSKLSKRKNPTSILFYQRMGYLPEALVNYLGRMGWSMPDESEKFSLTQMQEAFDIQRVSLGGPVFDVEKLSWLNGQWLREQSDEQFLDSLLDWAFNRDYAMKIIPHLRQRVETLSEVADKAAFCFNGMPAISEASFEHKQYSADDIKVWLQYLLWTYEARNDWNREGLFADAKAIADALEVKIKDFLFPVFIAIAGTSASFSVVDSMEIIGSDISRARIRHAIEVLGGVSKKQMKKLEKAYRDLPVG", "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": "MLSHVEMAPAAGGFKLFGKVIMQCGVSEGTQDKAQGFVVAREKVEPEEEEEEEQRVPAAATSGQRASIKREAADRDEEQRQGGGDAAGQPTQRRLQDSAEARAAAAAPLPCPRCRSRDTKFCYFNNYNVNQPRHFCKACHRYWTAGGALRNVPVGAGRRKNRPLGPLAVAHHNHHHRAAAGFVLGFPNPSSPTSPSPVYTDRWPVTPDRPF", "text": "FUNCTION: Transcription factor that may transactivate seed storage protein genes in developing seeds. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MASVRASPRSALLLLLAAAGVAEVTGGLAPGSAGAVCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWSCMNSSLPGVFKKSDGWVGLGCCELAIGLECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREFCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRICEYNPVEVSMLTCLADVREPCQLGCTNLTYCTNFNNRPTELFRSCTAQSDQGAMSDMKLWEKGSIKMPFISIPVLDIKTCQPEMWKAVACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEEHTAESICEFLSPADDLESCIPLDTYLRPSALGNIIEEVTHPCNPNPCPANELCEVNRKGCPSADPCLPYSCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFTIDCNVCSCFAGNLVCSTRLCLSEHSSDDDRRTFTGLPCNCADQFVPVCAQNGRTYPSACIARCVGLQDHQFEFGPCISKNPCNPNLCPKSQRCVPKPQVCLTTFDKFGCSQYECVPRQLTCDQARDPVCDTDHMEHSNLCTLYQRGKSLSYRGPCQPFCRAKEPVCGHNGETYSSVCAAYSDRVAVDYYGPCQAVGVLSEYSAVAECAAVKCPSLSAIGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTSKKPITVVEILQKVRMHVSVPQCDVFGYLSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSLPSSAVVGRPLFHSLLLLLSLGLTVHLLWTRP", "text": "FUNCTION: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (PubMed:28803732). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:26658478, PubMed:28803732). Acts as a Wnt7- specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7 (By similarity). ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (By similarity). Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity (PubMed:11747814). Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP) (PubMed:11747814). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the RECK family."}
{"protein": "MPKLKTRKAAAKRFKVTGTGKFMRRRAFRNHLLDHKSSKLKRHLGTKAVVDERDSENVSLMLPYS", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "MLYEKFEHNINNLIGGFGLSKIAIAVSGGSDSVALLYLANIWAKKNNIELFVLSVDHNLRDQSKQEIEYIQNTANDLGLKFYSLFFDHQNNFSNLQERARKGRYDLMTSLCQKLDILVLLTAHHEDDYIENFCLRLERKSGVFGLSSSSVNWHNNTQIIRPLFNIPKSELVNYLATNNIKWFEDQSNLSTKYRRNTIRQKLAKEEVYIKDDIITQQIKVNELIENKFKPELISAIAESVKISEYGFAFLDLIKFSGFSQEVRVQLINFLLIIISGQQRSARFYSVEPILKLIRQSLDFKNTLHGCVIKRMQNKLLIYREFGKKLPESKLLLDKQLVWDNRFRITKNHNIENCVATYLSLEDYKIIKEKLDLEVLKNLSCGNHNAILFTLPIVKILEKVVAIPHISYYDNDIKSFNVSFAPDFTSRFTHFY", "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": "MTYFIDRRANAKNKSAVNRQRFLQRYRSHIKRAVEEAVNRRSITDMERGEKISIPAKDISEPVFQHGPGGARTIVSPGNKEFVEGDRLRRPGGEGRGGSGEGSASNQGEGMDEFAFSLSREEFLDFVFDGLALPHLERKQLRDLDEVRPVRAGVTRDGVPSRINIVRSMREAQARRIGMRAPIKRALREAEEALESEERKDPVLRNPARIGELKAEIERLEKRLEAVPFIDTYDLRYNNLIDQPQPSNKAVMFCVMDVSGSMTQGHKDIAKRFFLLLYLFLERNYEKVELVFIRHHTAAKEVDEEEFFYSRETGGTIVSSALTLVDEIIAKRYSPAQWNLYVAQASDGDNWDDDSLTCRDLLMTSLMAKLQYYTYVEITPHSHQALWEEYERVQAAHPSRFAMQQIVEPGDIYPVFRKLFRKRVAS", "text": "SIMILARITY: Belongs to the UPF0229 family."}
{"protein": "MISVNEMGSYVIEEMLDWSEDLKTEVTKLNSGATIIDCGVKAEGGYEAGMYLARLCLGDLADLKYSTFDLNGIKWPAIQVATDNPLIACMASQYAGWRISVGDYFGMGSGPARALGLKPKELYEEIGYEDDFEVAVLVMESDKLPDEKVVEYIAKHCGVEPENVMIAVAPTASIAGSVQISARVVETGIHKFESIGFDINCIKSGYGIAPIAPVVGNDVQCMGSTNDCVIYCGETNYTVRFEGELAELEDFVKKVPSTTSNDFGKPFYQTFKAANFDFFKVDAGMFAPARVTVNDLKSTKTISSGGLYPEILLESFGIRNV", "text": "FUNCTION: Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MCH family."}
{"protein": "MAKLHDYYKSSVVAELTKQFGYTSVMQVPRIEKITLNMGVGDAINDKKLLENAAADMATISGQKPLITKARKSVAGFKIREGYPIGCKVTLRGERMWDFMERLISIALPRVRDFRGVNAKSFDGRGNYSMGVREQIIFPEIDFDKVDRVRGLDITITTSAGTDEEGRALLAAFNFPFRK", "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": "MNFSKLKFGATIGIIGGGQLGKMMAQSAQKMGYKVIVLDPNEDCPCRYVAHQFIHANYDDEQALNQLGENSDVVTYEFENISSEQLKKLTQLYHIPQGYQAIELLQDRLTEKQTLLEANTQIVPFVQIQTNQDLLKAIEKLGFPFIVKTRFGGYDGKGQILVRNDSELDEAYQLVEKQECVAEQYLDIQKEVSLTVTIGNEQQTTYFPLQENEHQNQILFKTVVPARSDKENEARKEVEKITRAIHFVGTFTVEFFIDKENNLYVNEIAPRPHNSGHYSIEACDYSQFDTHILAITGQKLPQAIELLKPTVMMNLLGRDLDLLENEFSRHPDWHIHIYGKKERKPDRKMGHMTLLTDDVNQTEQYMLMKFEGRDK", "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": "MTDFSLPSILVPLVGLVLPAIAMASLSLHVQKNKIV", "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": "MEGYLVLEDGTSFSGELDGHENCTGEAVFFTGMTGYQEVLTDPSYKGQIIVFTYPLIGNYGINEKDFESKKPQVKAAVVYEACDHFSHYEAVYSLKEYLQKWNIPLLTHVDTRAVVKKIRANGTMGATVTASKEGAEIALQPENVAEQASAQEISTFGDGNKHIALIDFGYKKSIASSLVKRGCKVTVVPYQQMEAVYNIKPDGIVLSNGPGDPKAIQPYLGKIKSIISRFPTLGICLGHQLIALAFGGNTFKLPFGHRGANHPVIDRKTKRVFMTSQNHSYVVDEQSINEEELTIRFHHVNDTSVEGLAHKKLPVMSVQFHPEAHPGPAESEWIFDDYLKNVIPARREIAHA", "text": "SIMILARITY: Belongs to the CarA family."}
{"protein": "MAELATIARPYAEALFGVAEAGDIAAWSTLVQELAQVARLPDVLSIASSPKVSRAQISDLLLAAVKSPLKDNAQAKNLVQMLVDNHRLPLLPEIATQFEELKNAREGAADALIVSAFPLEGAQLDGLVASLERKFKRKLKPTVQVDSSLIGGVRVTVGDEVLDTSVRARLASMQTALTA", "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": "MSIEVDWGAATSGPDGEALAERIRSFIHDKFQQVALPRFIRSVQVHSFDFGTIPPELEIKDLCEPFADFYEEDEDDEASDVSEGLVSRHGSPWHGTHPELNESSFRDDNAINHSLRDPFTEGFQPSALRSPIALSDHLNPHFRSGTPGIPGGTSTLGYHLMSLGGLSGTQTPLAAVAGGSPFAGGWNDSGMMGPGNRGRPPPPIFTAHQSRPEADIDSSNPTSRPSTSSTLPSHPSGSNKNNGDGAGGPDHGSHPEEHGHLDDPTSEEPLRFPRMRERRPEDFQVLCHAKYAGDVRLSLTAEILLDYPMPSFVGLPLKLNVTGITFDGVAVVAYIRKRVHFCFLSSEDADALIGSDQPDVGAQTEYSRSGGDATVSAKRQGGLLQEIRVESEIGRKEDGKQVLKNVGKVERFVLAQVRRIFEEELVYPSFWTFLV", "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": "MSNTTLHATTIYAVRHNGKAAMAGDGQVTLGQQVIMKQTARKVRRLYEGKVLAGFAGSVADAFTLFEKFETKLQQFSGNLERAAVELAQEWRGDKQLRQLEAMLIVMDKDAILVVSGTGEVIAPDDDLIAIGSGGNYALSAGRALKRHASHLSAEEMAYESLKVAADICVFTNDNIVVETL", "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": "MKEIEYVQDLCSRAKKASKVLKQLSSSKKNKILLSLADLLEKRKAEILLANELDLKDGKEKKLSSALMDRLLLNEKRIFSMASAVREIAALPDPIGEVTRGITLPNGLELVTRRVPLGVVMVIYESRPNVTIDVGALSFKSGNACILRGGSEAFYSNEILIKLFHEILIKEEIDIGSVVFVDKTDRSFMIPFFQQTSLIDIVVPRGGEGLIRFVSENSKIPVVKHDKGVCNLYIDQDADPEKVIPIVINSKVQRPGVCNSTENLILHNGYPFRKELLEALAKEGVELLLDPSSLALYPKGKPVKQQDYLEEFLDLRLSVKTVSSLEEALAFIEKTSSGHTEAIVTEDLNTARIFTNSLDSAALFINCSTRFHDGGEFGLGAEVGISTGKLHVRGPMGLVHLTTTTTYVTGNGQIRG", "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": "MNSNSIQSFDALPHNLRECFLDMASFLEDQRIIASTIIDLWSASYGKEGMNNLQDLASRNLLKLLPIGRNEYEDGFYNELLVKQDNVLREFAINQCLKESSSIFERKRLNLEIQDNKFPNWCLNPKQPIVINASLFSISTDDSFASSWFEMDCPNVEALVLNISSSNYALPNFIATMKELKVVIIINHGLEPAKLTNLSCLSSLPNLKRIRFEKVSISLLDIPKLGLKSLEKLSLWFCHVVDALNELEDVSETLQSLQEIEIDYCYNLDELPYWISQVVSLKKLSVTNCNKLCRVIEAIGDLRDLETLRLSSCASLLELPETIDRLDNLRFLDVSGGFQLKNLPLEIGKLKKLEKISMKDCYRCELPDSVKNLENLEVKCDEDTAFLWKILKPEMKNLTITEEKTEHNLNLLQLF", "text": "FUNCTION: Possible disease resistance protein. SIMILARITY: Belongs to the disease resistance NB-LRR family."}
{"protein": "MKYKFSHNFISYNLFLFVFMSLILLPYSHASSMGFNTSQHKFSVRTGETRIIYPLSSVKGVSLSVTNPQDYPILVQTQVKGEDKHSPAPFMATPPLFRLDAGMRGRVRVTRTGGNFPEDRESLQWLCITGVPPKEGDVWDNSQHDKKNNMQDVNLNILLSVGTCMKLLVRPDQLRQKPEEMAGKLIWHRNGQQLQVNNPTPFYMNFKSVSLGNKNIKLSSAGNENYVAPFAERSFSLPVDMAERPAEINWQIINDLGSESQVFKANI", "text": "FUNCTION: Required for the biogenesis of the MyfA fimbria. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the periplasmic pilus chaperone family."}
{"protein": "MFAWWGRTVYRYRFIVIGVMVALCLGGGVFGLSLGKHVTQSGFYDDGSQSVQASVLGDQVYGRDRSGHIVAIFQAPAGKTVDDPAWSKKVVDELNRFQQDHPDQVLGWAGYLRASQATGMATADKKYTFVSIPLKGDDDDTILNNYKAIAPDLQRLDGGTVKLAGLQPVAEALTGTIATDQRRMEVLALPLVAVVLFFVFGGVIAAGLPVMVGGLCIAGALGIMRFLAIFGPVHYFAQPVVSLIGLGIAIDYGLFIVSRFREEIAEGYDTETAVRRTVITAGRTVTFSAVLIVASAIGLLLFPQGFLKSLTYATIASVMLSAILSITVLPACLGILGKHVDALGVRTLFRVPFLANWKISAAYLNWLADRLQRTKTREEVEAGFWGKLVNRVMKRPVLFAAPIVIIMILLIIPVGKLSLGGISEKYLPPTNSVRQAQEEFDKLFPGYRTNPLTLVIQTSNHQPVTDAQIADIRSKAMAIGGFIEPDNDPANMWQERAYAVGASKDPSVRVLQNGLINPADASKKLTELRAITPPKGITVLVGGTPALELDSIHGLFAKMPLMVVILLTTTIVLMFLAFGSVVLPIKATLMSALTLGSTMGILTWIFVDGHFSKWLNFTPTPLTAPVIGLIIALVFGLSTDYEVFLVSRMVEARERGMSTQEAIRIGTAATGRIITAAALIVAVVAGAFVFSDLVMMKYLAFGLMAALLLDATVVRMFLVPSVMKLLGDDCWWAPRWARRLQTRIGLGEIHLPDERKRPVSNGRPARPPVTAGLVAARAAGDPRPPHDPTHPLAESPRPARSSPASSPELTPALEATAAPAAPSGASTTRMQIGSSTEPPTTRLAAAGRSVQSPASTPPPTPTPPSAPSAGQTRAMPLAANRSTDAAGDPAEPTAALPIIRSDGDDSEAATEQLNARGTSDKTRQRRRGGGALSAQDLLRREGRL", "text": "FUNCTION: Is the target of the antitubercular drug SQ109. FUNCTION: Transports trehalose monomycolate (TMM) to the cell wall. Flips TMM across the inner membrane (PubMed:22252828, PubMed:22344175). Membrane potential is not required for this function. Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness (By similarity). Could also be part of a heme-iron acquisition system (PubMed:21383189). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Cell septum Cell tip Note=Colocalizes with TtfA to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for localization to the poles or septa. SIMILARITY: Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily."}
{"protein": "MAKQKKHPTGTIAQNKKARHDYFIEHRFEAGMVLAGWEVKSLRAGKAQLVDSYVLLKDGEAWLLGSHFTPLTTASTHVIADPTRSRKLLLNQRELEKLFAAVQQKGYACVCLSLYWSKHLVKCEIALGKGKKEYDKRHTERERDSDRELQRAVRTKGKED", "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": "MSRETTTKDLDSLRALAERGAAELQDASAEELLRWTDENFGGNYVVASNMQDAVLVDLAAQVRPGVDVLFLDTGYHFAETIGTRDAVESVYDIHVVNVAPEQTVAQQDELVGKDLFASDPGECCRLRKVVPLRKSLAGYAAWVTGLRRVDAPTRANAPLISFDEAFGLVKINAIAAWTDEDMQKYIDEHGTLVNPLVDEGYPSIGCAPCTAKPVLGGDARSGRWQGLAKTECGLHAS", "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": "MSLAVRPPVCLLCRSGAPTLLPSSVSQVARSMATARLRRKVARMALSPDVAKSSINQKRSGKAKFGPWSGMNQTEAHIRGEPRSRSQAALRRSGEKAADTPRKSDSPLYKALKMQTTLAPVPYGRRTAVKSKIADITSFDHFPLLPVVRHSIFSQALPGLVDVTPTPIQRLAIPKLMEDSPDGKRGTKLEDGDPQYDQYLLAAETGSGKTLAYLLPLVDAVKRLEVEDKENERKEEERKAKEKEERLKNRAFDLEPEEPPLSNAGRPRVIILVPTSELVAQVGVKVKALAHTVKYRSGMISSNLTPRRIKSTLFNPDGIDILVSTPHLLASIAKTEPYVLSRVSHLVLDEADSLMDRSFLPTTTEIISKVAPSLRKLILCSATIPRSLDNLLRKRYPDIKRLTTPNLHAIPRRVQLGVVDIQKEPYRGNRNLACADVIWSIGKAGDSEPSEPFASYVGPNIKKILVFVNEREEADEVAQFLRSKGIDAQSLSRDSSARKQEEILAEFTESAPPPSPEEIMLAQKKRRQEDAIPFELPENHNKPENVRRLANTKVLVTTDLASRGIDTLPVKTVILYHVPHTTIDFIHRLGRLGRMNKRGRGIVLVGKKDRKDVVKEVREGMFRGQALI", "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": "MAAKEVKFQADARERMLRGVDVLANAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQMLREVASKTNDLAGDGTTTATVLAQAIVREGAKAIASGMNPMDLKRGIDLAVDAVVKELKSNARKISQNSEIAQVGTISANGDTEIGRYLAEAMEKVGNEGVITVEEAKTSDTELEVVEGMQFDRGYLSPYFVTNQDKMRVELEDPYILIHEKKLSNLQSILPVLEAVVQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVVSEDLGIMLENVTLEMLGRAKKVSIEKENTTIIDGAGSKTEIEGRTAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRVDDALHATRAAVEEGILPGGGIALLRAVNALDGLKTANDDQRVGIEIVRRAIEAPVRQIAENAGAEGSIIVGKLREKVEFSYGWNAQTNEYGDLYTMGVIDPVKVVRTALQDAASVAGLLVTTEAMIAEKPKKESTPALPAGGGMDF", "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": "MDLTPREKDKLLLFTAALVAERRKARGLKLNHPEAIALISAAILEGARDGRTVAELMNYGRTILTRDEVMDGIPEMIPDVQIEATFPDGTKLVTVHQPII", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease gamma subunit family."}
{"protein": "MAALVRAAVVRSQCRQLWRLFPRGHGLRDVAERPRPEEACSCLRSRAFSAGPPPPGAGPEPKGGQAGSHRPKPGPVSWKSLALTFAIGGSLLAGMKYFKKEKIEKLEKQRHRSIGKPLLGGPFSLTTHNGEPKTDKDYLGQWVLIYFGFTHCPDICPEELEKMIEVVEEIDSIPSLPNLTPLFITIDPERDTKEAIATYVKEFSPKLVGLTGTKEEIDGVARAYRVYYSPGPKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKKKAEIAGSIAAHMRSHMKKR", "text": "FUNCTION: Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT- CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (By similarity). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (PubMed:25683716, PubMed:28973536). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Single- pass membrane protein. SIMILARITY: Belongs to the SCO1/2 family."}
{"protein": "MPAVADCTVVFPLRHDPASTHPDVSGLVGKAFERVNWRDAFDTFLAEERSALWAAKTAFDNTDTSAYIAARDALFPQAVSGVHGAVAFRNRAGHKLHETMEAVGLWEYLKGGATRAKGTFTFVDVCGGPGAFSQALFAMGKEHKLRLRGFGLTLRNVKGLDWYTDLPSRSFFPCYGIDGTGDVFKLENIESLCSLTCKENVRLVVADGGFDVPTEVVNFQETISCRIVYGQWLSAVKLLRPGGCFVLKLFDCFSPFTRAILFLTTHLYESVQVVKPRHSRVVNSERYLVCIGFIGAPKQWLEHFERCYQEGFVDNDNIPTVLPTSLFSGDKIFGADVERMSATIASNQVSGLHAILEKLQSKPAMEEVKS", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of spliced leader and U1 small nuclear RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped RNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation. Recognizes a guanosine cap on RNA independent of its N(7) methylation status. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "METQKEIVFIAVESEDGGYIEKTERYSIFTQGDTWEELLEMIKDAVKCHFDEGAPKYVHARFVKDVTIAV", "text": "SIMILARITY: Belongs to the UPF0150 family."}
{"protein": "MTEQKRKIEKLAGVKGMNDILPQDAGLWEFFEATVKSLLRAYGYQNIRTPIVEHTQLFTRGIGEVTDIVEKEMYSFTDALNGENLTMRPENTAAVVRAAIEHNMLYDGPKRLWYIGPMFRHERPQRGRYRQFHQVGVEALGFAGPDADAEIIMMCQRLWDDLGLTGIKLEINSLGLAEERAAHRVELIKYLEQHVDVLDEDAKRRLYTNPLRVLDTKNPALQEIAQNAPKLIDFLGDESRAHFEGLQRLLLANNIPFKINPRLVRGLDYYNLTVFEWVTDKLGAQGTVAAGGRYDPLIEQLGGKPTAACGWAMGIERILELLKEEDLAPEQEGVDVYVVHQGEAAREQAFIAAERLRDTGLDVIFHCSADGAPASFKSQMKRADASGAAFAVIFGEEEVANGTAGVKALRGAGQEGEKNVQQTVPVEGLTEFLINAMVASAEDGDD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MSKNIHDVAYGLQKAIADHTDFKTLKESYAKVQGDADSKQLFDTFRNMQLEIQQKMMQGQEITEEDNKKAQEVIDLIQQNEHIKKLMEAEQRLNVVIGDINKIIMKPLEELYSAYQA", "text": "SIMILARITY: Belongs to the UPF0342 family."}
{"protein": "MTESQRMSRTLAEVDPEIYQAIQHETARQDGQLELIASENFTSEAVLEATGSVFTNKYAEGYPGKRYYGGCEYTDVVENLARERASKLFGAEYVNVQPHSGSQANQAAYGAVVSPGDTVMGLNLAHGGHLTHGHALNFSGKTYKIVPYNVRKEDELIDYDEVEKLAREHQPKMIIAGASAYPRIIDFARFRKIADAVGAVFLVDMAHISGLVAAGVHPNPCEFADIVTSTTHKTLRGPRAGIILAREKYGKEIDKNVFPGTQGGPLVHVMAAKAVCFLEALQPEFAVYQRQVVANAKALAQSLIDAGFRVVSGGTDTHVVLLDVFSKGLRGKESEQALDRARITVNKNAIPFDTNPPMNPSGIRLGSPAVTTRGFKEAEMREVGTLIAEVLTNIANEDVIAGVRQKVQALTTRFPLYSWKRDTVQA", "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": "MGGAISKKQYKRGGNLRERLLQARGETYGRLWEGLEEGYSQSLGASGKGLSSLSCEPQKYSEGQYMNTPWRNPATERAKLGYRQQNMDDVDDEDDDLIGVSVHPRVPLRAMTYKLAIDMSHFIKEKGGLEGIYYNERRHRILDMYLEKEEGIIPDWQNYTSGPGIRYPMHYGWLWKLVPVDVSDEAQEDETHCLVHPAQTYQWDDPWGEVLAWKFDPELAYSYKAFIKYPEEFGSKSGLSEEEVKRRLTARGLLKMADKKETS", "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: Seems to play a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Enhances virus infectivity and pathogenicity. Probably involved in viral immune evasion mechanisms (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": "MILKADVKGTGKKGQTVEVADGYARNYLIPRGLAVAASEGALRSIEAERKAQQEKQQRQVAELSALRDRLDGQTIQLRAKCGEGGRLFGSVTNKDVADAIARHIGKPFDRKMVELDAPIKTLGVHLVTLRFGHNITGKVNVEVLPE", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MGEGDAFWAPSVLPHSTLSTLSHHPQPQFGRRMESKVSEGGLNVTLTIRLLMHGKEVGSIIGKKGETVKKMREESGARINISEGNCPERIVTITGPTDAIFKAFAMIAYKFEEDIINSMSNSPATSKPPVTLRLVVPASQCGSLIGKGGSKIKEIRESTGAQVQVAGDMLPNSTERAVTISGTPDAIIQCVKQICVVMLESPPKGATIPYRPKPASTPVIFAGGQAYTIQGQYAIPHPDQLTKLHQLAMQQTPFPPLGQTNPAFPGEKLPLHSSEEAQNLMGQSSGLDASPPASTHELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGTPANISLAQYLINARLTSEVTGMGTL", "text": "FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSKNNKKKRRWDLKNGGILLEELIASFDGKTNPIRCFSSDQILKATDNFSESRIISSWGYFIWYKGVIEERQVSIKKWSSQNLSSFTEAYRDISVSSQMSGHKNALKLIGCCLEFDLPALVCEYTEHGPLNRDGGLSSGVVLPWKVRLKIAKEIASSVTYLHTAFPETIVHRNINPTNIFIDENWTAKLSDFWFCVAIPEGELYVEDDVKGVIGFVDPDYYWTMKVTEKVDIYSFGVVMLVLLSGRAAVFNGPDEAPMSLNDHVSEVMEKGEFDEIVDKEIWNDLGGDDDLVLRRSQVKAFLRLALRCVRYKKEDPVSGMLEVAKELKLIEKLS", "text": "FUNCTION: Together with RPP13L4/ZAR1, involved in the ambient temperature (above 22 degrees Celsius)-sensitive aerial organ development (PubMed:28499073). Together with RPP13L4/ZAR1, involved in the regulation of the ambient temperature-sensitive intersection of growth and immune response in the absence of pathogens, by repressing the transcription of SNC1 (PubMed:28499073). Probable non-functional kinase required for recognition of the Pseudomonas syringae type III effector HopZ1a by RPP13L4/ZAR1 and, together with SZE1 and SZE2, to trigger subsequent defense responses (PubMed:24170858, PubMed:26355215, PubMed:28652264, PubMed:30947022). May function as a decoy to trap HopZ1a in the ZAR1 complex for recognition by the plant immune system (PubMed:24170858). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Cell membrane Note=Associates with the plasma membrane in the presence of the Xanthomonas campestris effector XopAC/AvrAC. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily."}
{"protein": "MFQTINEISIHPELYNQKKVLIQGWITNIRGNLKIIFVELNDGSSFKNLQCVLKKEFIDFDKIENLALGVAVEISGIFSNTPERQQFGEVLVETLEIKGNNYNTNFPIQNQEISLEVLRQMPHFRHRSRLFRVIMKLRSALFFEIHKFFRRQGFINFSAPILTSNDGEGAGEVFIVDDENKDFFNKKTTLGVTGQLHAEAYALGFKKVYTFAPTFRAERSNTRRHAAEFWMIEPEVAFFTLEQIIELAVKLLQKVIKSVIIRNKDEFIFLEKAGDKNLRKRLLQFCDSQVTQISYEKAIELLLEHQEKFEEKDLFFGCDLKTEHERFLTEEIFHMPVVIINYPKNLKAFYMHQNEDGQTVAAFDLLVPGIGELIGGSQREVRYEKLLARMSELNMNIEEFQWYLDLRKYGNPGSSGFGLGFERLLMYITGIENIRDVIPFPRTSKNILM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MPSHLIKSGISKAPHRSLLKALGITDNELKRPFIGVVHSFSEIVPGHVHLRTVVEAVKAGVRTAGGVPFELPVIGVCDGIAMNHEGMKYSLASRELIADSVEVMVKAHQFDALVFVPNCDKIVPGMLIAAMRLNLPAIFVSGGPMLAGRVRGKSVSLSNVFEGVGAVAAGLMSEEELLEYENYACPGCGSCAGMFTANSMNCLTEAIGMALPGNGTIPAVYAERLRLAKLSGEKVMELLSQNIRPRDIFTRESLLNGLAVDMALGCSTNTVLHLAAVAYEAGVEFDLNLVNEVSERTPNLCRLSPAGPHHMEDLYFAGGIPAVMKELSKKGLIREDLLTVSGKTVGENLKNAVNKNPEVIRPIDNPYSETGGLAILFGTLAPRGAVVKKSAVLPEMLTHTGPARVFDSEEDATTAILTGQIKKGDVVVIRYEGPKGGPGMREMLTPTSALAGMGLDKDVALITDGRFSGATRGAAIGHVSPEGYEGGPIALVREGDLIKIDIPGQRLDLLVSEEELNQRKARLQIPEPKIKEGYLARYQKLVSSANLGAVFLK", "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": "MDWENCSSLTDFFLLGITNNPEMKVTLFAVFLAVYIINFSANLGMIVLIRMDYQLHTPMYFFLSHLSFCDLCYSTATGPKMLVDLLAKNKSIPFYGCALQFLVFCIFADSECLLLSVMAFDRYKAIINPLLYTVNMSSRVCYLLLTGVYLVGIADALIHMTLAFRLCFCGSNEINHFFCDIPPLLLLSRSDTQVNELVLFTVFGFIELSTISGVFISYCYIILSVLEIHSAEGRFKALSTCTSHLSAVAIFQGTLLFMYFRPSSSYSLDQDKMTSLFYTLVVPMLNPLIYSLRNKDVKEALKKLKNKILF", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTDSEYSSAADAVANLVRRVPGFPSEGVVFEDLTPVLADAGAFRLIVDELAEAARSYHADIIGGLDARGFLLGSAVAYQLGLGILAVRKEGKLPPPVFHRGYDLEYGHAALEIPREGLNIQGKNIVLIDDVLATGGTLCASRALLEEAGANVAGLAVILEVEALEGRKRLADLPLTVVGERSE", "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": "MALEKSLVLLPLFVLMLLVLGWVQPSLGKESRAKKFQRQHMDSDSSPSSNSTYCNQMMRRRNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQANCYKSNSSMHITDCRLTNGSRYPNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST", "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": "MGQKVNPIAFRTGVTRGWGSRWYASKQDFADLLVEDRKIREFITKHPKKSQYKSAGIDRIEIERTRDEVRVMLYVARPGLIIGKKGQEIEILQAELQNLVGRRINLKVEEVGRPELQAQLVAEDISQQLAKRSSFRRTMKRMLEQTMDAGAKGIKIQMAGRLGGAEMARREKQSAGSIPLSTLQAKIDYGFTEAMTPQGHIGIQVWINQGTYGDDNDGADAQTGQASKKPKRSYKR", "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": "MEGMLKGEGPGPLPPLLQQYVELRDQYPDYLLLFQVGDFYECFGEDAERLARALGLVLTHKTSKDFTTPMAGIPLRAFEAYAERLLKMGFRLAVADQVEPAEEAEGLVRREVTQLLTPGTLLQESLLPREANYLAAIATGDGWGLAFLDVSTGEFKGTVLKSKSALYDELFRHRPAEVLLAPELLENGAFLDEFRKRFPVMLSEAPFEPEGEGPLALRRARGALLAYAQRTQGGALSLQPFRFYDPGAFMRLPEATLRALEVFEPLRGQDTLFSVLDETRTAPGRRLLQSWLRHPLLDRGPLEARLDRVEGFVREGALREGVRRLLYRLADLERLATRLELGRASPKDLGALRRSLQILPELRALLGEEVGLPDLSPLKEELEAALVEDPPLKVSEGGLIREGYDPDLDALRAAHREGVAYFLELEERERERTGIPTLKVGYNAVFGYYLEVTRPYYERVPKEYRPVQTLKDRQRYTLPEMKEKEREVYRLEALIRRREEEVFLEVRERAKRQAEALREAARILAELDVYAALAEVAVRYGYVRPRFGDRLQIRAGRHPVVERRTEFVPNDLEMAHELVLITGPNMAGKSTFLRQTALIALLAQVGSFVPAEEAHLPLFDGIYTRIGASDDLAGGKSTFMVEMEEVALILKEATENSLVLLDEVGRGTSSLDGVAIATAVAEALHERRAYTLFATHYFELTALGLPRLKNLHVAAREEAGGLVFYHQVLPGPASKSYGVEVAAMAGLPKEVVARARALLQAMAARREGALDAVLERLLALDPDRLTPLEALRLLQELKALALGAPLDTMKG", "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": "MTNLRKTHPLMKIVNSSFIDLPAPSNISSWWNFGSLLGVCLIIQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYMYLETWNIGVLLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGSDLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAGVHLLFLHETGSNNPSGLCSDADKIPFHPYYTIKDILGVLLLILALTSLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILAVVPFLHTSKQRSMMFRPFSQCLFWILVADLLTLTWIGGQPVEHPFIIIGQLASILYFLLILVIMPITSLFENNLLKW", "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": "MDFCLLNEKSQIFVHAEPYAVSDYVNQYVGTHSIRLPKGGRPAGRLHHRIFGCLDLCRISYGGSVRVISPGLETCYHLQIILKGHCLWRGYGQEHYFSPGELLLLNPDDQADLTYSEDCEKFIVKLPSVVLDRACSDNNWHKPREGIRFAARHNLQQLDGFINLLGLVCDEAEHTKSMPRVQEHYAGIIASKLLEMLGSNVSREIFSKGNPSFERVVQFIEENLKRNISLERLAELALMSPRSLYTLFEKHAGTTPKNYIRNRKLECIRARLSDPNANVRSVTEMALDYGFFHTGRFAENYRSTFGELPSDTLRRRKMKWLDPEESLPPLP", "text": "FUNCTION: Regulatory protein of the TOL plasmid xyl operons. XylS activates the xylXYZLTEGFJQKIH operon required for the degradation of toluene, m-xylene and p-xylene. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MELLRSARPHPKEKLKNVIEWFHWLLREAELYDVRYPVKGAYVWRPYGMKLRRNVEELIRRVHDETGHEEVLFPVFIPYEFFGKESQHIRGFEKEVFWVSKGGEGGERLVLRPTSETAIMPMVKLWIQDYKDLPLRLYQIVSVFRAETKMTHPMIRLREISMFKEAHTVHVDREDAERQVREAVEIYKRIFDEMCLAYMINKRPDWDKFAGAEYTIAFDTVLPDGRTLQIGTAHYLGTNFTRVFEVTYLDADGTRKLAHTTSYGISERSIAAMLITHGDDGGTTLPPKLAPIQIAVVPIYYSDEEMPLVMKFVEEVVAALKGAGLRLHVDDRRDKTPGWKFYYWELKGVPLRLEVGKRDVEKRQVVVTRRDTLEKYAVALGELVDAVRELMKAVEDNLRRRAWEELRSKIVKVQSLEEAKKAIKEGKVVEVPWSGDNQCGMKIQELLGADALGIPMDSEASIGGYDARDLACGERRAELWLRLSERY", "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": "MKVIFLVDVKGKGKKGEIKEVPTGYAQNFLIKKNLAREASSQAIGQLRGQQKAEEKAQAEILAEAKAVKKILDDEKTRVQFKEKVGPDGRTFGSITAKKISEELQKQFKVKVDKRHIVLDHPIRAIGLIEVPVKLHKEVIAEIKLNIAEA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MTEQVTDHNLLKHRFRGYLPVIIDVETAGLNAKTDALLELAAITVKMDQQGYLVPDQKCHFHIQPFENANINADSLKFNGIDIHNPLRGAVAEAIAIPEMFKMVRRAIKEQGCQRAVIVAHNATFDQAFLQAAVKRINAKRDPFHPFAMFDTASLAGLMYGQTVLVKACQIANIAFDGKQAHSALYDTEKTTELFCAMVNRLKDLGGFPLLNPK", "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": "MSRACELTGKTVQYGNNVSHANNKTRRRFLPNLCNVTLISEVLQQSYRLRVSASALRSVEHRGGLDSFLVRADDKELSQRARLLKRQIVKKKAEQAA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MFDQIPTQRPNTPLLDVVDTPARLRELSEKQLPQLAKELREYLLYTVGQTGGHFGAGLGVVELTVALHYVLNTPDDRLVWDVGHQTYPHKILTGRREQMSSIRQLDGLSGFPKRSESEFDTFGVGHSSTSISAALGMALAAEMTDNQQQTVAVIGDGSMTAGMAFEALNHAAHADTNMMVILNDNNMSISKNVGGLANYFSKIWASKTYCALREGSKRVLTKIPQAWELARKTEEHMKGMVSPGTLFEELGFYYVGPIDGHDLERLVHDIRNMLAIPGPKLLHIITQKGKGFTPAEKDPVGYHALNKIEPKASITPISASGGAEAPAASTIKKPKYQTVFGDWLCDLAEVDPFVLGITPAMCDGSGMVEFAERFPDRFHDVAIAEQHAVTLAAGLACEKFKPVVAIYSTFLQRAYDQLVHDVALQNLDVTFAIDRAGLVGEDGPTHAGAFDISFLRCIPKIIIATPSDENECRQLLFSAYHHPGAAAVRYPRGTGPGAVIELENQHWPIGKGRELRQGKTVCFINFGVLLPDAIAVAEANNYGVCDMRWAKPLDKDLLLNMAEQYDYLVTLEENAVAGGAGAGVMELLAAEGISTPVLPLGLPDEYLDHGKRSQLLQAAGLDRASINQRINQWLSRHNGAAHDSQIHSL", "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": "MAIRNLRFNDDEILRKKCRVVDDINDRIKVLVEDMIETMYENNGVGLASPQVGILKRIFVVDAMDGAGSRVFINPEILEKSGEQTDEEGCLSLPGRHKPVKRANKIKIKALDVNGNEFVLDAEGFLARAIQHEYDHLEGVLFIDHEL", "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": "MTEKHRTPDGLVIVDKPSGFTSHDVVAKMRGIARTRRVGHAGTLDPMATGVLVLGVEKATKLLGHLALTEKEYLGTIRLGQNTLTDDAEGEIISSTDASRVTRDAIDAGVAKLSGAIMQVPSKVSAIKIDGVRSYKRAREGEDFEIPARPVTVSSFAVYDVRDAVAEDGTPVLDLVVSVVCSSGTYIRALARDLGADLGVGGHLTALRRTRVGPYKLDAARTLDQLQEELTVMPIAEAAAAAFPRWDVDTKRARLLLNGVRLEMPEEYAGRGAVAVVDPAGRFLALVEEQKGKAKSLAVFG", "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": "MRSLTTKTSSALLTVWGLLSVSLMPSVGQADKTAGDYFVHSLPGAPAGPLLKMHAGHIEVTPEHHGNIFFWHFQNRHIANKQRTVIWLNGGPGCSSEDGALMEIGPYRVKDGSNGPKLEYNPGSWDEFANVMFVDNPVGTGFSFVDSDSYIHDLPEMADQFVQFLEKWFALFPEYEHDDLYLAGESYAGQHIPYITKAILERNKKPDAKHKWPVKGMLIGNGWISPVEQYMSYLPFAYEKGLVKKDSEKAKKLESQQAICTKMLNENGGRDKVDNSQCEQILQEILSTTQSKGSDGNMQCYNMYDVRLKDSYPSCGMNWPPDLVNVTPYLRRSDVVAALHISPEKRTGWTECNGAVGSAFRAANSKPSIQILPELLAEVPTILFSGAEDLICNHIGTEELISNMEWNGGKGFELGSGTWAPRRDWEFEGEPAGFWQEARNLTYVLFYNSSHMVPFDYARRTRDMLDRFMKVDIASIGGAPTDSRIDGEKGLETSVGGHPNSTAAAEAEEERLEAAKWNAYYKSGEIVLVIVVIAASAWGYYIWRERRQRAGYAGIFGGDTPMALAGARSGSRGAAGLEDFRNKRNARDVEAADFDESELDELHVRSPTDDMDRDRYSVGSASDDESIGKRNGNGKGKEKSYS", "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": "MSKNKQDAGLSTSAGLVRYMDEDASKIKIAPEKVLGITISIMVLLFILNYGLLA", "text": "FUNCTION: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SEC61-beta family."}
{"protein": "MSTSNRILLGVNIDHVATLRQARGTRYPDPVKAALDAEEAGADGITVHLREDRRHIQERDVLLLKDVLQTRMNFEMGVTEEMMAFAERIRPAHICLVPETRQELTTEGGLDVAGQEARIKAAVERLSKIGSEVSLFIDADERQIEASRRVGAPAIELHTGRYADATTPTEVADELQRIIDGVNCGLNEGLIVNAGHGLHYHNVEAVAAIKGINELNIGHALVAHALFVGFKGAVAEMKALILAAAKA", "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": "MKTVLILLSILGMACALSMKNLNRRAKLEDSEENGVFKYRPQYYVYKHGYFYPALKRFAVQSSSDSSEENGNGDSSEEEEEEEETSNEEGNNGGNEDSDENEDEESEAENTTLSTTTLGYGEITPGTGDIGLAAIWLPRKAGATGKKATKEDESDEEEEEEEEEENEAEVDDNEQGINGTSSNSTEVDNGHGSSGGDNGEEDGEEESVTEANTEGITVAGETTTSPNGGFKPTTPHQEVYGTTPPPFGKITTPGEYEQTGTNEYDNGYEIYESENGDPRGDNYRAYEDEYSYYKGRGYDSYDGQDYYSHQ", "text": "FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "VGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEEDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIQKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAREGNEIIREACKWSPELAAACEVWKEIKFEFKAVDTLD", "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": "MKEFDLESYDYDLPKELIANYPILPKEKAKLLVYERRSQKITHTTFEHVLDFFPKNALVVLNDTKVIKARIFGSKHAFLPSKTTEVFFHRFFKDNTALTQIKGKIKVGDKIFFDAHYHAEVLELLHNGQRLIAFYGNKTPLNQANILKLLEQYGHMPLPPYIKRADESLDAHEYQSVFAKHMGAVAAPTASLHFSQNTLEKLLKDFKHAFLTLHVGAGTFLGVETKDIREHQIHTEVLRIPKKSQEILQKSQEILCIGTTALRSVEYFKRLENPNQEAFECDIFLHLANPILHVNYLLTNFHLPKSSLLMLVSAMVGLEKTKEIYQIAIEKKYRFYSYGDGMLIL", "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": "MDNLWTSLPLPGLSDDQRHWLFAPGSLTLRLKALGRFSLEVTQQRIDFPEPGEAHALGCTTDSPAWIREVALKIDDQVMVCARSLTPMRERRPAWPELAGYGGEPLGSMLYNTPDIHRGAFECQRPQADDPLSRLATSLGQPSGKLLARRSRFLRDGQPLLIAECFVEGFWALLQERSAPLKLAI", "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": "MKRKLFTICLASLQFACAAENLNNKSYEWDIYPVPANAGDGMVWKLHPQSDDFNYIADEKDKGKEFYAKWTDFYHNHWTGPAPTIWQRDHVSVSDGFLKIRASRPEDVPLKKVVSGPNTKELPGTYTGCITSKTRVKYPVYVEAYAKLSNSTMASDVWMLSPDDTQEIDIIEAYGGDRDGGGYGADRLHLSHHIFIRQPFKDYQPKDSGSWYKDDKGTLWRDDFHRVGVFWKDPFTLEYYVDGELVRTISGKDIIDPNNYTGGTGLVKDMDIIINMEDQSWRAVKGLSPTDEELKNVEDHTFLVDWIRVYTLVPEE", "text": "FUNCTION: Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. SIMILARITY: Belongs to the glycosyl hydrolase 16 family."}
{"protein": "MRLTQYLASKLKNFSNLPKEYIERSKKQVYWQTPKEINYLPRTVERKRFRYTTNRSWTGQFRQQNMPGTVRRKVLVEPIEDWSFFRGDRIEVLVGKDKGKQGIVTQVIPERNWVIVEGLNWHYRKVGGEKEFPGIIIKSEAPLHVTKDIRLVDPSDLQGTDFEWRFTEEGEKVRVSLRSGRIIPIPETNNQTHDYKTPNAYIEREKDTPGAVVGEITFQPKLSTFEMDIMEEMGIKEERTPVKSYWY", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "MAAKDIVYREDARTAMERGVNALADAVRVTLGPKGRNVVLEKKFGSPMIVNDGVTIAREIELENPFENMGAQLVKEVATKTNDIAGDGTTTAAVLAQAIVRAGLKNVTAGANPMILKRGIEKAVERTVEEIKSRAKPVESKEAITQVASISANDTTIGNLIADAMEKVGKDGVITVEESKGMGTSLEVVDGMNFDRGYISPYMITDPDKMEATLADPYILITDKKISAVADILPILEKVLQAGKALLIIAEDVEGEALATLVVNKLRGTLNVVAVKAPGFGDRRKAMLEDIAILTGGRVVSEEVGLKLDKAGLDLLGKARQVRVKKDETIVVDGQGDADAITKRLAQIKKQIEDTTSDFDREKLQERLAKLAGGVAVINVGAATETEMKEKKLRIEDALNATRAAVEEGIVPGGGTVYVNVIPVLNGLEPELPDERTGVDIIKRALEAPLRQIANNAGVEGSIVVEKVKESPAGVGFDALSEQYTDMIGAGIVDPAKVTRIALQNAASIAAMILTTETLVAEKVDKDKKGGMGGMGGMGGMGGMDMM", "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": "MVECDYDPTEDATPAEVVEILGRTGMAGEVTQVKVRILEGPDKGRIITRNVKGPVREGDILLLRETEREARPIE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family."}
{"protein": "MERSTTSDTASEKPNPSHSTGAVQMRIKNANSHHDRLSQSKSMILSDNVKVLEPINRHRRNHSQHNLTLADIISTPDHTVVEKEGYLLKAKIADGGKKLRKNWSTSWIVLTSRKMEFYKESKQPALANLKPGYKPECVDLCGAHIEWTPEKSSRKNVFQITTVSGNEFLLQSDIDFLILDWFHAIKNAIDRLPKERSCTSRNLEFKLRRSSSTELLNSLDTESKESKPEHRKSLIFRLNYSASDSNDRSRVKSRLKKFISRRPSLKTLQEKGLIKDQIFGSHLHLVCEHENSTVPQFVRQCIKAVERRGLEVDGIYRVSGNLATIQKLRFVVNQEEKLNLDDSQWEDIHVVTGALKMFFRELPEPLFPYCFFEQFVEAIKIQDNATRIKAVKTLVKKLPRPNYDTMKVLFEHLKKIAAKESVNLMSTQSLGIVFGPTLLRPEKETGNMAVHMLYQNQIVELMLSEYSKIFGSEED", "text": "FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein."}
{"protein": "METWQELKVTVKREGEELVSNLLIELGAQGVAIEDSLDYVGNVDRFGEIFPEVEQQEEIVVTAYYPDTVDVTVVEVDLQARISELTDFMDLGEVKMGTTALAEEDWADNWKKYYEPARITHDLTIVPSWTDYEATAGEKIIKLDPGMAFGTGTHPTTKMSLFALEQVLRGGETVLDVGTGSGVLSIASSLLGAKEIFAYDLDDVAVRVAQENIELNPGMENIHVAAGDLLKGVEIEADVIVANILADILIHLTEDAYRLVKDEGYLIMSGIIKDKWDMVRQSAESAGFFLETHMIQGEWNACVFKKTKDISGVIGG", "text": "FUNCTION: Methylates ribosomal protein L11. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family."}
{"protein": "MWDGPLRSRQNLRTVAKLRSSGCPLTQSAIHPTTTSPSEGETASEILQGQASAGYIEEQQLPATSSQLEMSGDSNAASDNNVVIMTKRQRDDLSQASQAEVLSRLRTEDAQGPAENNGAQSDLALHSCDMEERVDSSKLNLNHVTVNKHSPPASKSAGISQQNDDGGCGASENVDNTTTAASKQRGKLLLDSSSSNCTPKQQAQQAVTQVPEWELSHEQERIFDIVVNHRRSVFLTGGAGTGKSHLLRAIIAALPLSTTFVTATTGLAALNLGGTTLHSFSGCGFVDQHTSTHQMVYRNVLGRKKARANWRKCRVLVVDEVSMLDAWFFDMLEYVARHIRGCRKPFGGIQLVLSGDFLQLPPVNKHSPKQETRLCFEAKSWPRVNPLVCTLSHQFRQKDKEFFSLLNEVRVGALTAPSLGLLSSLSVITTVSFVDEEKLKLKREVGAEAVDIITDSKGRTRRQRQDGFTILRARRSEVDAINTEKFGELDTEIYSYKGAHRGEGHFPSDLPSTVSVRAGCRVMLLANLDLSAGLANGSIGTVESFVSSKLHQTANPSTKDDLQHLADHMMLPVVRFDHKGKQGPGDGGGAAAGRLVVIEPHRWTMRQGDSDVSCSIQIPLQLAYAITIHKSQGMSLSHVNVDFAGIFEEGQAYVALSRCTDVANLVIENFDAQRVNPNIKALAYYRALEFVGTEHREAEKKLIDNGNKMNPWGPYDVEDFEASDDDNGGAVKKEVVENLTYDAENISCMVEQFRQRYMPQYIMFSTLRRRVLSNTEDAARVKGALLVMDTTSLLALTNMTGPTSLYQTIFTERGNMMRVPRVVKEELLFLASTDVKEVSSVTTPTLHSFCSTCSSTPCSTGFSYDFVEVVSCALSIMENAKCDFLLDEQREGEANSLPPVIQEWRSLSPLLMLNSSPDTGEKDAPSVIGFGERSREQHHSTLMFASFLVSRYSGNGAVYVCTETVELAARALAIGLRVCSIAYLCNRARRVN", "text": "FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast Note=Localizes predominantly to the kDNA disk. SIMILARITY: Belongs to the helicase family. PIF1 subfamily."}
{"protein": "MGEICPRREDFDIDYILKNASLLEKVSLLAGYDFWHTAPLPRFNVPSVRVSDGPNGVRGTKFFDGVRAACLPCGTGLAATWDQSLLYDAGVLIGQDVYPTAAYIRGAQSTGVISTIKHFAANDQEHERISVNAVMSERALREVHLLPFQIAIADSAPGAVMTCYNKVNGQHLSESKEMLDGLLRREWGWKGLIMSDWFGTYSTAEALNAGLDLEMPGPTRLRGPLLELAISSRKVSRATLDERARTVLEFVQRARKAEVSAVESTRDFPEDRRLNRKLAADSIVLLKNESGLLPLNPQTLTSVALIGPNMKTAAFCGGGSASLQPYYSTSPYQGITSQLPPGVEVLYETGATSYAFIPELAASEVRTPEGQPGLGMRFYRDPPSVQERRVVEETIIQESSWQLMGFSNPELDRLFHADIEAELIAPATGPFQFGLAVYGSASLFLDDQLIIDNTTVQRGGTFFFGKGTLEETATVDLVQGQSYQIKVQFASGPSSKLVKPGVVNFGGGAGRLGMVQVVDPERAIARAVEAAKRADITILGVGLTRDHESEGFDRSHMDLPPAVASLVTAVLDVAPDAILLTQSGTPFSMLPWADLVKTHLHAWFGGNELGNGIADVLFGVVNPSGKLPLSFPRRIEDTPTYLNFGSERGQVTYGEGIYVGYKLLRKSPTSCALSIRVRSAPVHPCCFRSNSLLTRFVPQARFVVHLLCVLRFDGRHRVRYTECSKLGRRGRSGSSPAVYRGRSNNVVNRTSHQGAQRISKGGFAAR", "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": "MSIDINWDTLTGGADGAARAETIRAFIHDKFQQVTLPKFIRSVHVHSFDFGSASPEIEIKDICDPLPDFYEEDEDYPDNEDDDDDEAGLDSNPRNKCITRKGTNFKSVAISLVARQFETSHQSALTPGIPGGTSNINYFHLPLSAGLSGATTPLAAVAGAQLQGWLDNPYGRPSTPTNMRRLRHAASFNSLTLTPQSHPDPSSRPSSRHQHDDERRRSLAESDDASSQHGYDRTPSVSPHPMREKSPEDIQVVAHVQYSGDIKMSLTAEILLDYPMQSFVGIPLKLNITGLTFDGVALLAYIKRRAHFCFLSPDDAEALVGSDAGFNGLQTDSNGENAQPVQRPKIGGLLENIRVESEIGGQGSGKQVLKNVGKVESFVLEQVRRIFEDEFVYPSFWTFLV", "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": "MDPGREDEVPLAATSPESRRTRSNGRGKATVGDAPPPAETVVSTKAAPLPTGGWKKGIAILDFILRLGAIGAAMGASILMGTNEQILPFFTQFLQFHAQWDDFPVFKLFVVLNALAGGFLILSLPLSIVCIVRPLAVGPRFLLLITDLVNMATVIAAASAAAAIVYVAHNGSQDANWIAICQQFTDFCQGTSEAVVVSFVAAVFLVCLIVVSTLALKRT", "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": "MARRNRRLSSASVYRYYLKRISMNIGTTGHVNGLSIAGNPEIMRAIARLSEQETYNWVTDYAPSHLAKEVVKQISGKYNIPGAYQGLLMAFAEKVLANYILDYKGEPLVEIHHNFLWELMQRQSGAGLGVTSGFIYTFVRKDGKPVTVDMSKVLTEIEDALFKLVKK", "text": "FUNCTION: Self-assembles to form a helical, filamentous nucleocapsid mesuring 1980 nm in length and 24 nm in width. Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form. 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. This certainly protects the viral DNA under conditions such as the extreme desiccation of its host. SUBCELLULAR LOCATION: Virion."}
{"protein": "MRVRPASVYRYLLLGVCALLGIYTVYSIIGYDDGSHVPIHRPQRHLYLTVSQDRIGSRFGKLAPKRILYWTTIFGATVPSTALSDCPGLTDRCVIDTNRHQLDSADAVVFHAADISKFPLPVSRKPDQIFVFNSMETPDNSGRFAVPDGFFNWTSTHLYSSDAIHKYGTFLIPTQIAESRGFKVQSYYVQPKRLVKTMKGIFGLISNCHTKSKRELALQELGKHINVTIGGKCASDDRLKSICPAGVECIDVFEQYPFYIAIENTVCNDYVTEKIWSRITVPSIPIVMRRRVYQNILPPKSFIAMDDYKNPSEMANHLRSLEANSTAYGEYFEWRQKGLWTSAPWNAPGYRNGLCRVCELLWKAKDNETEVYKSYDNIWKWFDNESQCETDEFVRSWLSG", "text": "FUNCTION: Catalyzes the addition of fucose in alpha 1-3 linkage. Unlike fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-Man-beta- 1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-(Man- alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc- beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-beta-1->2- Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc- beta-1-Asn (GnM3F6) acceptors. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 10 family."}
{"protein": "MPRRRRASRRVRRRRRPRVSRRRRRGGRRRR", "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": "MGGVIKNISTFVLIVEFIIGNLGNSFIALVNCIDWVKRRKISLVDQLLTALAISRISLVWLIFGSWCVSAFFPALFATEKMFRMLTNIWAVTNHFSVWLATGLGTFYFLKIANFSNSIFIYLKWRVKKVVLVLLLVTSVFLFLNIALINIHINASINGYGGNKTCSSDSNDFTRFSSLIALTSSVFIFIPFILSLAIFLLLTFSLWKHCKKMQHTVKASGDASTKAHRGVMQTVIAFLLLYPIFSLSFFIAVWTSGWLEENLIILSQVMGMAYPSCHSCILILGNKKLRQASLSVLWWLKYRFKDGEPSGHKGFRESS", "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": "MEQTPITDAEKVRIVSDFILHAPPGEFNEVFNDVRELLKNDTLLKDGASHAFAQYNKDQLTPVRIEGTDHNAIISEHNDLGNGRFYDPRTKQAFKYDHLRKEASDYQDVEADATAEPWRAALDLETLAYTASHYRHGVSSVFGKAQGNQITLTICIEDHQFQPKNYWNGRWRSQWHVTFQAGSGTAELKGVLKVQVHYYEDGNVQLVSSKECRESVVVSNEQQVAKEVIRLIEDAENEYQLAISENYQTMSDTTFKAMRRQLPITRTKIDWSKIVSYSIGKELKTQ", "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": "MQRARPTLWAAALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK", "text": "FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. Inhibits the positive effect of humanin on insulin sensitivity (PubMed:19623253). Promotes testicular germ cell apoptosis (PubMed:19952275). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MPIKKGSLVRAVRDKLDNSLEALANDTRWPSYLFETDGEVLDMRGDYALIKFGAVPTPPVWLRQDQLAESGAAAESTS", "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 NdhO subunit family."}
{"protein": "STITKVHARQIFDSRGNPTVEVEVTTDKGVFRAGVPSGASTGVHEALELRDGVKSDYLGKGVLKAVGNVNTIINEELVKANLSVVDQKAVDDFLIQLDGTENKEKLGANAILGVSLAVAKAGAAEKGVPFYVHIADLAGSKKPFVLPVPAFNVINGGSHAGNKLAMQEFMIMPTGAKSFSEAMKLGSEVYHTLKKVINEKYGQDATNVGDEGGFAPNIQDNQEGLELLVTAIEKAGYTGKIKVAMDCAASDFYKDGKYDLDFKNPNSDPSTYLTGQDLTDLYNSYAGKYPIVSIEDAFDQDDWENWAHMNASADYQLVGDDLTVTNPKRIATAVEKKACNALLLKVNQIGTLTESIQAALDSQKAGWGVMVSHRSGETEDTSIASIVVGLRTGQIKTGAPCRSERLAKYNELLRIEEELGDAAIYAGEHFRKAHDL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the enolase family."}
{"protein": "MEQFNINKGMTIKPGLDVLPPPVTDDEYRALMAGEDRYLMTESNTLEEIEATFFYDTPIHWCATDLLEAISSTRLQLHRTMQAFVRALNQKLNGTGISAGSDKTGDVAQSGARAIGGAEIGRARNVNGLPVLPAIIPLSDGQTISILFHSPTAENRITNSDTLVAFQFLLNKKDVTHTVAPMSGRDMTLAQVTMKLANLAEKNSAKFQRAQKKKKALVDEITQLQADSDQKEDAMSDLADQVAAVEGQKADLEQKINAVASEADSLYEENERLQGEIDRLNRTGGRDTIAPAGMTGGHSRALTDRLASIKNRMHMDGEATLSNGASMKQFIGDGEGYIQLTDPDGSVYMIKAKSIQGVDMADAIGKLFKAYKAGNVSEYLVQPEEHKPENVEPESAEDTGSSSPEPEVSVGAYRYALQMRPAAPGAIPEGNKAILPRPDEGDPYYEYARYGIATYDTPLSDQQMSEYDLKLLPREDSFDFLAKTLTNGPFGKYAQKALELATNSPDEFRVMLKTQFQKTFPNIAFPGGAGTEKMVQSMINALQAEVGEITQPEPAPAQPDETVSEADAEANKAIEYLNNVMDMQSTDMAEIRNARGNVREAIAALQTAGRFEENEELVNGAARHLADLLVAIQKAGVAA", "text": "FUNCTION: Internal capsid protein that is probably ejected along with the viral DNA and prevents degradation of viral DNA by the host type I restriction-modification antiviral defense system (PubMed:3029954). Plays a role in directing proper capsid assembly (PubMed:28509398). SUBCELLULAR LOCATION: Virion Note=Internal capsid protein. A proteolytically cleaved 60 kDa form is incorporated into the virion."}
{"protein": "MKKISLLLASLCALFLVACSNQKQADGKLNIVTTFYPVYEFTKQVAGDTANVELLIGAGTEPHEYEPSAKAVAKIQDADTFVYENENMETWVPKLLDTLDKKKVKTIKATGDMLLLPGGEEEEGDHDHGEEGHHHEFDPHVWLSPVRAIKLVEHIRDSLSADYPDKKETFEKNAAAYIEKLQSLDKAYAEGLSQAKQKSFVTQHAAFNYLALDYGLKQVAISGLSPDAEPSAARLAELTEYVKKNKIAYIYFEENASQALANTLSKEAGVKTDVLNPLESLTEEDTKAGENYISVMEKNLKALKQTTDQEGPAIEPEKAEDTKTVQNGYFEDAAVKDRTLSDYAGNWQSVYPFLEDGTFDQVFDYKAKLTGKMTQAEYKAYYTKGYQTDVTKINITDNTMEFVQGGQSKKYTYKYVGKKILTYKKGNRGVRFLFEATDADAGQFKYVQFSDHNIAPVKAEHFHIFFGGTSQETLFEEMDNWPTYYPDNLSGQEIAQEMLAH", "text": "FUNCTION: Part of the ATP-driven transport system AdcABC for zinc. Required for transformability. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 9 family."}
{"protein": "MQFALALDTNSGPHQIRSCEGDGIDRLEKLSIGGRKQEKALRNRCFGGRVAATTQCILTSDACPETLHSQTQSSRKNYADANRVSAIILGGGTGSQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMSQFNSTSLNRHIHRTYLEGGINFADGSVQVLAATQMPEEPAGWFQGTADSIRKFIWVLEDYYSHKSIDNIVILSGDQLYRMNYMELVQKHVEDDADITISCAPVDESRASKNGLVKIDHTGRVLQFFEKPKGADLNSMRVETNFLSYAIDDAQKYPYLASMGIYVFKKDALLDLLKSKYTQLHDFGSEILPRAVLDHSVQACIFTGYWEDVGTIKSFFDANLALTEQPSKFDFYDPKTPFFTAPRCLPPTQLDKCKMKYAFISDGCLLRECNIEHSVIGVCSRVSSGCELKDSVMMGADTYETEEEASKLLLAGKVPVGIGRNTKIRNCIIDMNARIGKNVVITNSKGIQEADHPEEGYYIRSGIVVILKNATINDGSVI", "text": "FUNCTION: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm. SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family."}
{"protein": "MHLRSKPWASDWLAEHSDIVIDQDRATAQIGQWQSLFDQEQPIHLEIGSGKGQFILGMALAHPEINYIGMEIQETAIAIAARKSFDQVGTLPNLRYIYGNGNGVETYFEKGEVSKVYLNFSDPWPKKRHESRRLTYKSFLKSYEAVLPEHGEVEFKTDNRHLFEYSMVSFMDYGMRWTPEDYTLDLHADEDKVQGNVETEYEQKFMAKGQPIYKIKAHF", "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": "MPFLKDAVTLVKEPQQLPSIPLSWFPSSVFAAFNVTLLLFLSGLFFGFPCRWLVQNGEWAFPAITGPLFILTFFSLVSLNFSDPGILHRGSTKEDPMTVHVVRVNQRAFRLEWCPKCLFHRPPRTYHCPWCNICVEDFDHHCKWVNNCIGHRNFRLFMLLVLSLCLYSGALLVTCLTFLFRTRHLPFSLDKGMAILVAVPAAGFLIPLFLLLLIQALSVSRAESSYESKCRYHPEYNPFDQGFAKNWYLAMFAPLGPNYMSEVVCLQRPVGTAWIQEKTKPSPPRRPKHCRPGPPGPQHQPRRVPGKGPPGSGEAAALQEMRRLPASVEKSPGGPRQPTAEPAAGDP", "text": "FUNCTION: Palmitoyltransferase that mediates palmitoylation of RRAS, leading to increased cell viability. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cytoplasm, perinuclear region. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MRVVFMGTPDFAVGTLKAIIEAGHDVAAVVTQPDKPRGRSKSLVFSPVKDEAVAHGITVLQPERARDEAFVEELRTYNADVIVVVAFGQLLPASIINMPRYGCINVHASLLPKYRGASPIQWAVIDGCEYSGVTTMKMDEGLDTGDILMVEKVKLDAKETGGSLFDRLSDVGAHLLVKTLEGLEAGTITPVKQDDSESTYVKMLHKSFGKMDFNKSAAELERLIRGLNPWPSAFTYIDGKMLKIWDADVADNISEVQTEEVKPGQVVTVGKNTFTIACGQGYLVVNEVQLEGKKRMDSGSFLRGNQLEAGVMLGE", "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": "MFDVAPSELLLVAVVALVVIGPKDLPRAMRVVGRWLGKARKLSRHFRSGIDEMIRQSEMEDMEKRWAEENAKLLAENQGQGNQTASTSSPATPSPVSDDPAEQNIVFTSPADLEVNTADTSHLAANHTETTATTAASTPAKPKEADQQEKQS", "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": "QKDSYVGDEAQSKRGILTLKYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYTFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQIITIGNERFRCPEALFQPSFLGMETCGIHETAYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEITMLAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "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": "MTSARTPRRKTVAGASAQQVGLNFETPDDIVCGVDEAGRGPLAGPVVAAAVIFDPAKPMIRGLDDSKVLTAKKRDELYDKIVDRALAYCIASASVEEIDSLNILHATMLAMKRAVEGLSVVPTLVKIDGNRCPTLSVRSEAVIGGDALVKSISAASILAKVTRDRMLLELHQAHPVYGFNAHAGYGTPQHLAALREHGPCEHHRRSFAPVREAHLRLGTGVPLPAGNVIVVSEVMLDDDAFGERSGAA", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MTEGQAVPGVGDWEIDVESLDLEEDSCGTPLRATPPQEPSPAAADGEEDEDEEEEDEDVEDEGDGEEPGVSSEVPGRPEQPGGLAPRPPPAAQALPAAAAAPERGATAGGGAEPRKLSRTPKCARCRNHGVVSCLKGHKRFCRWRDCQCANCLLVVERQRVMAAQVALRRQQATEDKKGLSGKQNNFDRKAVYQRQVRAPSLLAKSILEGYRPMTAETYLGGTLPLPPPVSDRMRKRRAFADKELENIMLEREYKEREMLETSQAAALFLPNRMVPGPEYSSYKGTYSPTAGELPSKDFCNFLPTCLDLTMQYSGSGNMELISSNVSVATTYRQYPLSSRFLVWPKCGPISDTLLYQQYLLNATTSVQALKPGTGWDLKGTRVQDGLSAEQDMMPPKLEGSLVLPHLPEVPASRTDLQVHQVVPERSAFSPPGRNFSPIVDMDCLAAQGHVLTKLSKENTRPSLPLKTNPFHSVFQQTLSDKSGPELNAPFVKEAFEETPKKHRECLVKESQKYTFTIDRCAKDLFVAKQVGTKLSANEPLSFSVESILKRPSSAVTHVSQ", "text": "FUNCTION: Transcriptional activator that directly regulates early activation of the myogenic determination gene MYF5 by binding in a sequence-specific manner to the early epaxial enhancer element of it. Involved in somitogenesis during embryogenesis and somite development and differentiation into sclerotome and dermomyotome. Required for the initiation and/or maintenance of proper organization of the sclerotome, dermomyotome and myotome. Is not required for sex determination and/or differentiation in embryonic development. Also not involved in symmetric somite formation and hence does not regulate the laterality pathway that controls left-right asymmetric organ positioning. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMRT family."}
{"protein": "MLIYQDVLTGDEMISDAFPIKEIGDIAYEVDCANIIIKEGDVDIGGNPSAEEAAEALEEGAQQVNNVVHSFRLQSTSFDKKSYLTYLKGYMKAIKSKLQESNPDRVAAFEKGAQDFAKKIVANFKDYEFYIGESMNPDGMVCLLNYREDGVTPYFTMWKDGLKEIKI", "text": "FUNCTION: Involved in protein synthesis. Involved in microtubule stabilization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TCTP family."}
{"protein": "MFGKLGMPELVLIFAVALVIFGPSKLPEIGKSLGKSIKEFKKFSKEMKDDLSLEERETKDKDTVKVKEE", "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": "MAVRIARFLGLSTVAYLALANGIDARDTISRDVIILGGGSSGTYAAIRLRDQGKTVAVVERNNYLGGHGETYYTEDNTPLNFGVEGFFNTTVTRNYLERLQVPYGRRDPAPAHEDYVNLNTGQRTEYTPGQLQDREAFAKWVDAISQFGFLDDGVYRIPEPVPEDLISPFADFVKKYHLEDAVYALFSHTSGDVLEMITLYVIQYIGVPHAAALNEGYVRPIEGIAALYKSAGKELGSDVLLETTPEAVQRFEDGVEVIVRSADGTKTLLKGKQLLVTIPPLLENLHGFPLSDQESRLFSKWQYHQYWAALVNDTGLPDDVNIVNVDTERLYGVPEEPFIWRLDNHWAPGYHNIKLVGGSEFGEDEAKAYMYERLDLLHAEGTYATHKPEIVKFASHTPVTMFVSAEEIRGGFYRQLYELQGLNSTFWTGATWASDYSTLLWGYTDEVLDQMASS", "text": "FUNCTION: Beta-cyclopiazonate dehydrogenase involved in the synthesis of the fungal neurotoxin alpha-cyclopiazonic acid (CPA). CpaO carries out the dehydrogenation of beta-CPA to yield an unstable enimine product, which is captured by intramolecular cyclization to create the pentacyclic fused scaffold of alpha-cyclopiazonate. FUNCTION: Beta-cyclopiazonate dehydrogenase; part of the gene cluster that mediates the biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole tetramic acid scaffold (PubMed:21608094). The hybrid two module polyketide synthase-nonribosomal peptide synthetase (PKS- NRPS) cpaS incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L- tryptophan (c-AATrp), as the first intermediate in the pathway. CpaS catalyzes a Dieckmann-type cyclization on the N-acetoacetyl-Trp intermediate bound in thioester linkage to the phosphopantetheinyl arm of the T domain to form and release c-AATrp (PubMed:19663400). CpaD then regiospecifically dimethylallylates c-AATrp to form beta- cyclopiazonic acid. CpaD discriminates against free Trp but accepts tryptophan-containing thiohydantoins, diketopiperazines, and linear peptides as substrates for C4-prenylation and also acts as regiospecific O-dimethylallyltransferase (DMAT) on a tyrosine-derived tetramic acid (PubMed:21608094, PubMed:19877600). The beta- cyclopiazonate dehydrogenase cpaO then carries out the dehydrogenation of beta-CPA to yield an unstable enimine product, which is captured by intramolecular cyclization to create the pentacyclic fused scaffold of alpha-cyclopiazonate (PubMed:21608094). Finally, the cytochrome P450 monooxygenase cpaH mediates the conversion of CPA into the less toxic 2-oxocyclopiazonic acid, the end product of the CPA pathway in A.oryza (PubMed:21608094). SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family."}
{"protein": "MQLTSFTDYGLRALIYMASLPDGRMTSISEVTEVYGVSRNHMVKIINQLSRAGFVTAVRGKNGGIRLGKPANTICIGDVVRELEPLSLVNCSSEFCHITPACRLKQALSKAVQSFLKELDNYTLADLVEENQPLYKLLLVE", "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. May require iron for activity. Represses hmp expression under conditions of elevated intracellular iron concentrations, in the absence of nitric oxide."}
{"protein": "MAEKIVTGDEVIVIRGKDRGARGRVRQNLPREDRVIVEGVNIVKKHQRAIPGVRQAGIIEMEAPIHVSKVMLICPHCGKPTRVGFRFTETGEKVRYCKKCQQVIEKPALHRRTK", "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": "MAFKDLPAHARPREKLIARGAAALADAELLALLLRTGVAGKNVLQLAQELLDHFGGLSGLLQTSAEDLKVIKGMGGDAKRAELIAVLELARRAMAERLKERTVFDSPGTVKQYLQLHIGSRPYEVFAVLFLDAQHRLIVLEELFRGTLTQTSVYPREVVTRALHHQAAAVVLSHNHPSGSIEPSRADESLTQTLRAALSLIDVRVLDHVIVSAGQSYSMAEKGLL", "text": "SIMILARITY: Belongs to the UPF0758 family."}
{"protein": "MHAASRESMTELATTLDNTVAQSNAAVDGAQIGPELFDVVEVLDSNRDLRVALIDPAASSEKRADLADRVFGEKLNQASRSVLRSAVDKDWSNTRDFRNGLVQLGRRALFRAAEADDKLTTVESELFQLARVLEDAPQLEMLLADRQASADRRRQLLASVLYGKVTSITETLALQAISRAKQRPVEACETLSREAAQLRGYEVAHVVTAGELSDTQRSTLADKLGRIYGHKMSIHGEVDPSILGGMVIRVGDERIDGSTSGKLEKLRRAFA", "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": "MLAWRVARGAWGSLRVAVRPPGARLGRGGSRRALLPPAACCLGCLAERWRLRPAAFALRLPGTSPRTHCSGAGKAAPEPAAGGDAAAQAPSARWVRASATSSYENPWTIPNLLSMTRIGLAPVLGYLILEEDFNVALGVFALAGLTDLLDGFIARNWANQKSALGSALDPLADKVLISILYISLTYADLIPVPLTYMIISRDVMLIAAVFYVRYRTLPTPRTLAKYFNPCYATARLKPTFISKVNTAVQLILVAASLAAPVFNYADSIYLQILWCCTAFTTAASAYSYYHYGRKTVQVIKGK", "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": "MNSTVKTIVFWVFILACCILLWQVFQRSSNTGKEQEISFSQFLNDAQQGQIHDVTVVGGEVHGHFRSANAAFHVEVPTNYPQLYDILNKNHVAVTVKDNSGSPWWSILIQFSPVLVLVALWFFMIRQMQSGGNKALSFGKSRARLLSMQQKKVTFKDVAGVDEAKEELKEIIEFLREAQKFQKLGGRIPKGVLLVGPPGTGKTLLARAVAGEANVPFFSISGSDFVEMFVGVGASRVRDLFEQGKKNAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEANDGVILVAATNRPDVLDPALLRPGRFDRRVVVGRPDVRGREEVLRVHAKKVPLAEDVDLRVLARGTPGFSGADLANMVNEGALSAARANRKVVTMQDFESAKDKVLMGAERKSMLLTDEEKRVTAYHESGHAIVAAMRKHADPLHKVTIIPRGMALGVTMQLPEEDKHTVTKDYLETQLAILMGGRIAEEIFLHQMTTGAGNDIERATEMARKMVCEYGMSRLGPLTYGKKEEQIFLGREIAQHRDFSEETARQIDAEVRSLVDEAYRASYQLLNDNQPIMHKMAAALLERETIDANDIRMIIEGKDLPPLKPSGGSGTATTDDVQQVLKPSSDRGAGGLPEGSPSPA", "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": "MNKKPTKDKANGAKATKTIALNKRARHEYHLEERYEAGLALQGWEIKAIRAGRANIVDGYAYVRSGEIYLIGAQITPLIQASTHTVPVERRDRKLLLHRAEIDKVLTRVEREGYTLVPTALYWSSNKVKLEIALAKGKQNHDKRDAAKERDWQRDKQRVMRRHNRDA", "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": "MPQRLKQVYQDTIVPKLTEQFSYKNPHEVPKVVKITVNRGLGEASQNAKALESSINELSTITGQKPVVTRAKKAIAGFKIRQGMPVGVMVTLRSDRMYAFLDRLINLALPRIRDFRGISAKSFDGRGNYSLGIREQLIFPEIDYDTIDQIRGMDVSIITTAQTDEEGRALLKELGMPFRT", "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": "MKLNELSPPKGARTARKRKGRGPGSGLGKTAGKGHKGQKARSGGGVRPGFEGGQMPVHRRLPKRGFCNIFAKKIAAVNVRDLARFEADSVVDAAALREARLISGKVDGVKILGHGEITQALTVKADQWSESAKEKIEKAGGKIEAA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MAKLAKQLIAKRFVSHLTEYDQYAIAQQQINHQLVDLLQANTDKTFQRALEIGCGTGNLTEKLLAKIPIEHLTLNDFNAIYYPTVLQKIKQKKPLVVVDFMQGDAEQLVFTRNFDLVSAASVVQWFDSPQQFLRNSAYALKPGGVVLFNSFSPLNLQEIRQLTGIGLNYPTRLQWQEWLAQDFEQCQLIEQPIKLTFDSPLAVLIHLKKTGVTAVSNKPWNRHQIKQFCMEYQAHFACEQGVYLTYTPILMLGIKKNG", "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": "MQVKETVADGLKREFEVNVPAADIDAQVDARLVDLKDKVKLNGFRPGKVPVSHLKRVYGRSVAAETIDKLVRETNDGIFAERGFRLATEPKITMPQDQKVVEDILAGKSDLNYTVAIEVVPTIELADFKSFSVEKPVVDVGDSDVDEAIKRIAEANRAYADKAEGAKAETGDRVTVSFKGTIDGVAFDGGTGEDIPVVIGSGSFIPGFEDQLAGIGVGETRTIKVSFPANYASDTLAGKPAEFETTATKVEAPQDVTIDDEFAKTLGMESLDKLKEAARARLGAEYAGATRLRVKRQLLDRLDETHKFDAPPSLVEQEFEVMWRSINAEMQQNGKSFADEDTTEEAAREEYRKIADRRVRLGLVLSEIGEKNKIQVTDDEVSRAVIERARQMPGREKEVWDFYRSNNEALAQLRAPIYEDKVVDYILELANVTEKKVTREELYKDDDADKTAA", "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": "MFRFTEIEKTLCMDRTRDCAVRFHVYLQSLDLGSSDPHSPDFDGLAYLRDECLTKHPSLGDSNSDARRKELAYAKLMDSDQRCKIQNSNGYDYSHIESGV", "text": "FUNCTION: This enzyme is part of the viral RNA-dependent RNA polymerase complex."}
{"protein": "MDKLVIEGGVPLTGSIEVSGSKNAALPILFAAILPEEPVTITNVPDLRDIHTTLNLLKVLGCDCQYENGQVRIVPGSLLPEAPYDLVRTMRASVLCLGPLLARIGQARVALPGGCAIGARPVDQHLKGLEQMGASFQLEEGYIIGRCRKLTGAHITFDMPTVGGTENLLMAAVLAEGKTVLENVALEPEVVDLANFLCACGARISGQGTSCIRIEGVTSLHQATYPVMPDRIEAGTFLAAAGITGGELLLHNCPYDELESVILKLRSMGMEITQQGSGVLARCCAAPLRGTDVKTQPYPGFPTDMQAQIMALMCLAQGASVVEESIFENRFMHVLELMRMGAQIKVSGHTAMVRGVQKLTGAPVMASDLRASASLVLAGLAAQGVTEVRRIYHLDRGYEHIEHKLNAVGARIRREKQ", "text": "FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily."}
{"protein": "MISDIEFALSECNFQFAYKDLQKINLYIKRILLLNTRFNLISNSNSNFNSILNLHVIDSLLGLPTIKEANPSEILDVGSGAGFPGIILAIFDSSRKYYLLERSKKKSTFLKMIKLELDLENVKILEYEIEREKKKYEFITIRAFRSMNEYALVLKNLLKNEGLIMAYKGKFDRINLEVNQIKDLFSKIEVKSLSSKLSAERNLVLLYK", "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": "MSGEGKKHGSNVEPLRPTRPCPECGRPSVRERYPFCSERCRNVDLNRWLSGSYAIPVADDESKADDEDR", "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": "MTHAKLVIIGSGPAGYTAAIYASRALLTPVLFEGFFSGIAGGQLMTTTEVENFPGFPEGVLGHQLMDLMKTQAQRFGTQVLSKDITAVDFSVRPFVLKSGKETFTCDACIIATGASAKRLSIPGAGDNEFWQKGVTACAVCDGASPIFRDKDLFVVGGGDSALEEAMFLTRYGKRVFVVHRRDTLRASKVMVNKAQANEKIFFLWNSEIVKISGDTLVRSIDIYNNVDETTTTMEAAGVFFAIGHQPNTAFLGGQVALDENGYIITEKGSSRTSVPGVFAAGDVQDKYYRQAITSAGSGCMAALDAERFLEN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MENRELTYITNSIAEAQRVMAAMLADERLLATVQKVADACIASIAQGGKVLLAGNGGSAADAQHIAGEFVSRFAFDRPGLPAVALTTDTSILTAIGNDYGYEKLFSRQVQALGNKGDVLIGYSTSGKSPNILAAFREAKAKGMTCVGFTGNRGGEMRELCDLLLEVPSADTPKIQEGHLVLGHIVCGLVEHSIFGKQ", "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": "MTTKFEATTICAVRQNGHNAMAGDGQVTMGEKVVMKGTAHKVRRIYNDQVVVGFAGSVADAFNLEDRFEKKLNEFSGNLQRAAVELAQEWRSDQALQKLEALLIVMNKDDMLLVSGSGEVITPDNDVLAIGSGGNFALAAARAMQLHAKDMSAKEVAEAAIHIAGDIDIFTNHNVISETL", "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": "MFKGFQKPKRLVANTETLTERYGMFTAQPFQRGFGTTIGNSLRRVLLSSIEGAAITAVRIEGVEHEFSPIPGVVEDATDIILNLKQIPFKISSDGIKTVRLSVDSHGDVRSGQIETDADVEVLDRDVHVATVSEGGKLNIEMRLKSGRGYVSADKNFDEDLALGYIPIDSVHSPVRKVNFAVEAARLGQMTDYDKLTLEVWTNGAVSPQDSIGYAAKLLKDHMTIFINFEEVPEQTEEISERGMDKMNEVLNRSVEELELSVRSYNCLKNANIQSIGELVQKTEAEMLRTKNFGRKSLNEIKEILANMGLSLGMRIDQHGRLVAPPPSAGGGPDFGPEDDGQDQIGE", "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": "MAKASLDKDPFDVASMFDDVGDKYDLTNTVLSFGQDRVWRRRTRERLDLKPGEKVLDLAAGTAVSTVELAKSGAWCVACDFSQGMLAAGKHRNVPMVVGDGMTLPFADNSFDAVTISYGLRNIHDFRAGLREMARVTKPGGRLTVAEFSTPVIPVFGTLYKEYLMRLLPKVARVVSSNPEAYIYLAESIRAWPDQEDLAREINANGWSDCGWQNLTFGIVAMHSAIKPGN", "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": "MVGDMDAQQQELQQILNPQKLKSLQEWMQRNSITLTQVNGQRKYGGPPPGWQGPAPGSGCEVFISQIPNDVYEDRLIPLFQSIGTIYEFRLMMNFSGQTRGFAYAKYGDPLTASAAVTTLHQYRLPEGGCLTVRRSTEKRQLRLGDLPVSMNESKLLMVLQMLSDGVEDVLLKPPGPKGKEVVALVNYTSHYAASMAKKVLVEAFRNRYGISITVRWTSFSKSKRVEDTPQEDSCVTPLVLKPLSKPSLLHYDVPAHQSLLPLFRAVGGPTTSEQRDEMIPQPTIMSRNELIPQSSIRQRDEMVPQLPIRPRDGMAPQSPISLDAVSHLQWMCEVNRLGSPQYEVHFHHAAPDGFLYFAFKVLIPGLPLPLYGFVQILPGTSARAMKSEVYRAAAEQVIQTLCRVSNLRPF", "text": "FUNCTION: RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression. Relieves miRNA repression in germline cells. Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs (By similarity). Sequence-specific RNA-binding factor that binds to U-rich regions (URRs) in the 3'untranslated region (3'-UTR) of several mRNAs (By similarity). Does not bind to miRNAs (By similarity). Germline-specific protein required for the primordial germ cell (PGC) survival and migration during early embryonic development. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Perinuclear germ granules, also called germ plasm or chromatoid body."}
{"protein": "MWQLLLPTALLLLVSAGMRAEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTRWFHNESLISSQTSSYFIAAARVNNSGEYRCQTSLSTLSDPVQLEVHIGWLLLQAPRWVFKEEESIHLRCHSWKNTLLHKVTYLQNGKGRKYFHQNSDFYIPKATLKDSGSYFCRGLIGSKNVSSETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKKSVPSSTRDWEDHKFKWSKDPQDK", "text": "FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (PubMed:33208458). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory- like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Secreted Note=Exists also as a soluble receptor."}
{"protein": "MAKRSIYFCGSIRGGRNDAQFYAKIIQHLKQYGDILTEHVGHCGPEEEGLDDKTIHDRDLAWLLQSDVIVAEVTQPSLGVGYELGRAIAADKLVLCLFRPDSGRRLSGMIRGAINSVNFFVEDYHQDEYASKIDQFFTVRVTRP", "text": "FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family."}
{"protein": "MTTKGILGKKVGMTQVFTENGELVPVTVVKVDSNVVLQVKTMENDGYEAIQLGFDDLREVLTNKPAKGHAAKANTTPKRFVREIRDVELGEYKVGDEVKADIFEAGDFVDVTGTSKGHGFQGSIKRNGQHRGPMAHGSRYHRRPGSMGVIINRVMKGKLLPGRMGGNRVTIQNLEIVKADTENGVLLIKGNVPGANKSLVTIKSTVK", "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": "MSGYPKSYNPFDDDVEDEDTRPAPWKDARDLPDGPDPPIDRQQYLRQEVLRGPSATAASTSRSLFLMYESEKIGVASSEELVRQRGVLEHTEKMVDKMDQDLKMSQKHINSIKSVFGGFINYFKSKPVEPPPEQNGSIVPQPSSRLKEAINTSKDQESKYQASHPNLRRLHDAELDSVPASTVNTEVYPKNSSLRAYHQKIDSNLDELSVGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTEKKVRQL", "text": "FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein Cell projection, cilium membrane; Peripheral membrane protein Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. SIMILARITY: Belongs to the SNAP-25 family."}
{"protein": "MLPDHFSPLSGDIKLSVLALVVLVVLAQTAPDGWIRRCYYGTGRCRKSCKEIERKKEKCGEKHICCVPKEKDKLSHIHDQKETSELYI", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MAREFSLEKTRNIGIMAHVDAGKTTTTERILYYTGKIHKIGETHEGASQMDWMEQEQERGITITSAATTAQWDGHRVNIIDTPGHVDFTIEVQRSLRVLDGAVTVLDAQSGVEPQTETVWRQATEYGVPRIVFANKMDKIGADFLYSVQSLHDRLQANAHPIQLPIGSEDDFRGIIDLIKMKAEIYTNDLGTDILEEDIPAEYVDQANEYREKLVEAVADTDEDLMMKYLEGEEITNEELMAAIRRATINVEFYPVLCGSAFKNKGVQLMLDAVIDYLPSPLDIPAIKGINPDTDEEETRPASDEEPFAALAFKIMTDPFVGRLTFFRVYSGVLNSGSYVLNTSKGKRERIGRILQMHANSRQEIETVYAGDIAAAVGLKDTTTGDSLTDEKSKVILESIEVPEPVIQLMVEPKSKADQDKMGIALQKLAEEDPTFRVETNVETGETVISGMGELHLDVLVDRMKREFKVEANVGAPQVSYRETFRASTQARGFFKRQSGGKGQFGDVWIEFTPNEEGKGFEFENAIVGGVVPREFIPAVEKGLVESMANGVLAGYPMVDVKAKLYDGSYHDVDSSETAFKIAASLALKEAAKSAQPAILEPMMLVTITAPEDNLGDVMGHVTARRGRVDGMEARGNTQVVRAFVPLAEMFGYATVLRSATQGRGTFMMVFDHYEDVPKSVQEEIIKKNSGE", "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": "MGLLYKGSKLLNTILDSLEDQEGGAMYISCDVSNGGPVEPETGYVPNNPLFGLALDSPQQECAASCVGCLSCQGSTALPISSLTSSDFDCGGCFDPTIGVGVGIGGGHIQISTTPPASSGNGSSNNGAGGGSSGNHGYWSTDEMASTFPGLPPLDIDPLPSLFPFSPCGASYNFAAGNPHQAASLSYTVHPHQMLISPNSHNHGQMHSQHQQHQHQQSQVQASHVGNSLLQSSGGNNIGSNGSAGGVANAASCYYETSAGTAAPPPPPAAAMYPSMSVNVSMNMTMHHGYGAGDAGGVPMQCSQMNWTPPSNSTSAAAAAAAVNVLYPPLLSPGHYPASATYSFTADFRAPAPTGLGALPPLTVGEKESPSPPANSSLAGYYPTGVGNQGYTPPHKSPTSYQAAALGLSLSAFEDEEDSNEDLDGDEGSSGGEMKPNLCRLCGKTYARPSTLKTHLRTHSGERPYRCPDCNKSFSQAANLTAHVRTHTGQKPFRCPICDRRFSQSSSVTTHMRTHSGERPYRCSSCKKSFSDSSTLTKHLRIHSGEKPYQCKLCLLRFSQSGNLNRHMRVHGNNNSSNGSNGATGVGGESSTGSGVGGGNSLLT", "text": "FUNCTION: Transcription factor required for gene expression specific to photoreceptor cells. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MVAGEGFTYAAAGVDIAAGNRAVELMKEHVRRTFRPGVLGDLGGFGGLFALEAGRYRQPVLVAGTDGVGTKLKIAFSLDRHDTIGIDAVAMCVNDILVQGAEPLFFLDYLAVGKMVPERVARIVAGVAEGCRRAGCALIGGETAEMPGFYREDEYDLAGFAVGVVEREELLDGSRIRPGQVVLGLASSGLHSNGFSLARRVLLVEAGYTLERKLPELGRTLGEELLEPTRIYVASILPLLKEGLIKGLAHITGGGLIENPPRILPPGCSLRLDRRSWPVPPAFRLIQATGRVPEEEMYRTFNMGLGMLVVVEESDAGRVKSRLEAAGEKVFVVGEVIPGRREVEFVPGLQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
{"protein": "MHEITLCQRALELIEQQAAKHGAKRVTGVWLKIGAFSCVETSSLAFCFDLVCRGSVAEGCKLHLEEQEAECWCETCQQYVTLLTQRVRRCPQCHGDMLQIVADDGLQIRRIEIDQE", "text": "FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase (PubMed:12081959, PubMed:15995183). Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA (PubMed:23899293, PubMed:27951644). HypA is involved in maturation of hydrogenase 3. It may partially substitute for the function of HybF and vice versa (PubMed:12081959). May act as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center (PubMed:22016389). SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the HypA/HybF family."}
{"protein": "MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAFGKPINF", "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) (By similarity). 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 (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). 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": "MEKVLVVNFGGQYAHLIARRIREVGVYAEIASPEEAVIKASKEEVKAVILSGGPSSVYEPGAPDIDEGIFALSKPVLGICYGHQMIAKKLGGKVERGKGEYGKTIVKILVNDPLFDGWKPEEAVWMSHSDFVEEPPPGFHVLAISENGYIAAMRKGLIYGVQFHPEVHHTSKGRVMFENFLRKIARISDVWRPEDQITRIVEEIRSRVKGGDVIVGVSGGVDSTVTAVLLYKAVGQRVKAVFIDHGLFREGEPEEAASLLKSIGIDVVYIDAKERFLKRLEGVADCEEKRRIIGETFAEVFSDAVKQMPNVKYLAQGTLYPDVVESGAVKGADKIKSHHNVGGLPPWFQLELIEPLREFYKDEVRRIAKALGLPEDVVYRHPFPGPGLAVRIIGPFTREKLAIVRKATKIVEEELRKAGLFRKVWQAFATVGEDKWVGVKGDRRAMGYIVTVRIVESEDAMTADWSRIPFEILEKISSRITSEIPEVTMVTYAVTSKPPSTIEPC", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP."}
{"protein": "GGSCGQCRVKIKSGGGDILPTEMGHITKKEAKEGCRLACQVAVKTDMELELDEEIFGVKKWQCEVISNDNKATFIKELLLKLPEGEDVHFKAGGYIQIEAPAHVVKYADFDIPEKYRGDWDKYGLFDIVSTVNEDVLRAYSMANYPDEKGRIMLNVRIATPPSANVPAGKMSSYIFNLKAGDKVTISGPFGEFFVKETDAEMVFIGGGAGMAPMRSHIFDQLKSKKTKRKMSFWYGARSTREVFYQADFDALAAENDNFVWHVALSEPLPEDNWTGYTGFIHNVIYENYLKNHKAPEDCEY", "text": "FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the NqrF family."}
{"protein": "MIDSILFDLIEREAKRERENIELIASENFVSLGVRQAVGSILTNKYAEGYPSKRYYGGCFVVDDIENLAISRAKELFGASYANVQPHSGSQANMAAIMALIKPGDKILGMELSHGGHLTHGSKVSFSGMLFDAYSYGVSRDSEIIDYDDVRRIARECRPNLIIAGASSYSREIDFKKFREIADEVSAYLLCDIAHTAGLVVTGFHNSPIDVAHLTTSTTHKTLRGPRGGLILAGKESSMIVNFNNKERTLENAVNSCVFPGTQGGPLMHVIAGKAVAFGEALMDEFKDYISSVIENTKAMAEYFVSEGFRIVSGGTDNHLFLVDLGILGITGADAEKVLESVNIILNKNIIPFDSKNPSVASGIRIGGAAITSRGLNRDDSIEVARFIIRALKTKSDYELKKIKCEVVEFISSFNMP", "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": "MAVGKNKGLSKGGKKGVKKKIVDPFTRKDWYDVKAPSMFATRQIGKTLVNRTQGTKIASEGLKYRVFEVSLADLQNDNDAERSFRKFRLIAEDVQGRNVLTNFHGMDLTTDKLRSMVKKWQTLIEANVDVKTTDGYLLRVFCIGFTNKDQMSQRKTCYAQHTQVRAIRKKMVEIITRDVTSSDLKEVVNKLLPDSIAKDIEKACQGIYPLHDVYIRKVKVLKKPRFELSKLLELHGDGKGGSDEPGARVDRPEGYEPPVQETV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family."}
{"protein": "MRNPPALEQLVEALRCLPGVGPKSALRMAYYLLQRDRKGAGILAKSLDQALQVVSHCNLCNNFSEQEICPLCASPARDRTLLCIVEMPSDLMMLEQTQTYQGMYFVLMGRLSPLDGIGPRDIHLDKLLKRAQDGKVEEVILATNYTVEGEATAHYVSELLRARGIQVSRIARGLPMGGEIEHVDSGTLAQALLERRHVR", "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": "MQVILKEKVENLGVLGDIVNVKPGYARNFLIPFGKAVQATKANIETFEAQKAELEKAEKARFDAAVATAEAIKDKVYTIAAQAGEGGKLFGSVGTAEVAEAVSQASGKEIEKSQVRMPEGVIRSIGEFELTIHVYTDVDADIKVNVVASEA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MFKMISSPHTHSNNLTANFMLWVIGAMLPALVVQWYFFGYGIFIQASLAIGLAVVIEIAVAKLRGKATAFYLADLSGILTALILAMAIPPYAPYWVIVIGVIVALLLAKHVYGGLGQNLFNPAMIGYALLLVSFPVQMTAWLPPLALLNEPPTLADSFSLIFANVTTDGFSVHQLIQSVDGVSSATVLDGSKQAMSSIKDNVTLGIQLDKLFADVLVGGWGQVNLAFLLGGLLLIYKRIIHWQIPVAMLGTFALLSFATDFVSETARWTAQAQLFSGAMMFGAFFIATDPVTASITPKGKLIFGALVGLLVYLIRYYGNYPDGVAFAVLLANICVPLIDHYTQPRLYGTKLGRRQ", "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": "MNPILTNRLQKKLGYTFQQHDLLLQALTHRSASSKHNERLEFLGDSILSYVIANALYQRFPRVDEGDMSRMRATLVRGNTLAEMAREFELGECLRLGPGELKSGGFRRESILADTVEALIGGVFLDSDIRTVEKLILDWYRSRLDEISPGDKQKDPKTRLQEYLQGRHLPLPTYQVVQVRGEAHDQEFTIHCQVSGLAQPVVGNGSSRRKAEQAAAEQALKLLELE", "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": "MVPYHIRQYQDSDHKRVVDVFTKGMEEYIPSTFRHMLMLPRTLLLLLGVPLALVLVSGSWILAVICIFFLLLLLRLLARQPWKEYVAKCLQTDMVDITKSYLNVHGACFWVAESGGQVVGIVAAQPVKDPPLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQSYSDVVLETSALQQGAVTLYLGMGFKKAGQYFMSIFWRLAGICTIQLKYSFPSA", "text": "FUNCTION: May play a role in regulation of gastrulation. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the camello family."}
{"protein": "MATSNSSASLPTLFWVNGSGDSVLSTDGAAMPVQFLVLRIMVALAYGLVGIIGLLGNLAVLWVLGNCGQRVPGLSSDTFVFSLALADLGLALTLPFWATESAMDFHWPFGSALCKVVLTTTVLSIYASTFLITALSIARYWVVAMAVGPGSHLSVFWARVVTLAVWVAAALVTVPTAIFGAEVELWGVCLCLLRFPSRYWLGAYQLQRVVLAFIVPLGVITTSYLLLLAFLERQQRCRPRQWQDSRVVARSVRVLVASFALCWVPNHVVTLWEILVRFDLVPWDSTFYTFHTYILPITTCLAHSNSCLNPVIYCLLRREPQQVLVSSFRALWSRLWPQRKACMEQMALKEVGGRTVASTQESGSSRTHTNTMEHLDEGCSLNTLLSETYQGQSPQILGRSSCSLSQAAVSPGEV", "text": "FUNCTION: High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTLFERSAKELQAEIKAGNLSIADLTKEAYERIAKLDGDVQAFLASNEEKATAQAAEMDKVPFEERGPLFGLPIGVKDNIVTEGLETTCASKILEGFMPIYDATVVNKLREAGMITVGKLNMDEFAMGSSNENSYYKTTKNPWNLNHVPGGSSGASAASVAAGEVPFSLGSDTGGSIRQPAAYCGVVGMKPTYGRVSRFGLVAFASSLDQIGPITRNVEDNALLLEAIAGLDPNDSTSADVEVPNYAAALTGDVKGLRIAVPKEFLGEGVGEAARQSVLAALEVLKGLGATVEEVSLPHSKYALAAYYILSSSEASSNLSRFDGIRYGFRAENVTNLMDLYKETRAQGFGDEVKRRIMLGTYSLSAGTYDAYYKKAQQARTLIKADYDKVFEDFDVIIGPTSPTPAFKIGENVDDPMTMYANDILTIPMNLAGVPAISIPCGFDNGLPLGLQIIGKYFDEATIYRVAHAFEQATEFHKQVPQMWEGK", "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": "MGAATKLAFAVFLISCSSGAILGRSETQECIYYNANWEKDKTNRSGIEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRNDCIEKKDSPEVFFCCCEGNMCNERFFYFPEMEVTQPTSNPVTPKPPLFNTLLYSLVPIMGIAVIVLFSFWMYRHHKLAYPPVLVPTQDPGPPPPSPLMGLKPLQLLEIKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEIYSLPGMKHDNILQFIGAEKRGTSIDVDLWLITAFHEKGSLTDFLKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTASDGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRECWQKHSGMAMLCETIEECWDHDAEARLSAGCVEERIIQMQKLTNIITTEDIVTVVTMVTNVDFPPKESSL", "text": "FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. May modulate neuropeptide expression in dorsal root ganglia (DRG) neurons and ovarian follicle development. 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": "MALLTAKRPKKEAAPATDTSNNESDSEDSQNVDGDTGANAGWADCIGKVLKSKSVGPTVLSRAKKNPAVVRSKTSEAAKKPGFDFEVVGGDVKEEDDDDEEDGDADKSALDATLTKTERRNVPLQLRVKPSYQDLERERTLRKVATRGVVQFFNAVRIQQKDLEQQLADAGPLDSRQDAVLNNINKRKFLDVLMSGKRAKSTAIDNAVKKEEQETDDDDEDDTAEASSTGKKKSEWNVLREDFMTNKKIKHWDEEDDEGSDQGANNDEADDSDDDDEED", "text": "SIMILARITY: Belongs to the RRP15 family."}
{"protein": "MTSTSARPARRSRAPLAITAAIIAALVIAFFIFAGFYADVLWYDQLGYLGVLLTQWGAGIALFLVGFLAMAIPVFVSIQVAYRSRPVYAKLNSQLDRYQQVVEPLRRLAMFAIPAVFGLFAGVSASSGWQRTLLWLNRTPSGTVDPQFQLDTSFYMFELPFYHAVVGFASAVVIISMLGVLATSYLYGAVRFTGREVRISKSSRIQIAITAGVYFLLQGVSIWLDQYSSVVNNANGGLFTGAAYSDVNAVIPGRAILAGIAGVVALFFIVTAVIGRWRLPIIGTAGLIVASILVGTAYPAIVQRFQVEPNERALESQYYERNIEATRQAYGLADIEEIPYDATTDTTPGALREDAATTANIRILDPAVVGDAFSQLQQFRQYYQFGDNLDVDRYQIDGRVQDTVVAVRELSPTNTGTSWVNQHLVYTHGYSLVAAYGTQRTSDGQPVFLESGIPASGDLGDFEPRVYFGENSPDYSIVGGPESGDKVELDYPSGVDGADETYTTFQGDGGPKVDNVFKRLIYALKFQSEQIFLANQINDQSQIIYDRDPAERVGKVAPYLTIDKDPYPSVVDGRVVWIVDGYTTSDQYPYSQRQDMSRLIADSQQTQPLVPTDQINYIRNSVKATVDAYDGKVTLYAWDTDDPILKTWQKVFPSTLKPISDISGELMSHLRFPADMFKVQRAVLGKYHVTDPGSIYSNQDLWTTPNDPTATTEAGTPASLQPPYYLTMQMPGQDAPRFSLYSTFIPPATQDTSRSVLTGYLGVDSDAGSTAGEKAADYGKLRLLTLPNDDTIPAPTQIQNNFNSDTNVANQLNLLERGGRTSVVRGNLLTLPVGGGLLYVQPVYVRSTGDTSYPLLRKVLVAFGDKIAFEDTLDAALDSIFEGDSGATAGDEDVVPTTPVDGGTGDGATDGATDGGTGSTPTPAPTTSPSAPAQDVQAALDAANTALQERQAAYASGDLVAAAQADQRFTEAVQRAYELSQQQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0182 family."}
{"protein": "MHVTQSSSAITPGQTAELYPGDIKSVLLTAEQIQARIAELGEQIGNDYRELSATTGQDLLLITVLKGAVLFVTDLARAIPVPTQFEFMAVSSYGSSTSSSGVVRILKDLDRDIHGRDVLIVEDVVDSGLTLSWLSRNLTSRNPRSLRVCTLLRKPDAVHANVEIAYVGFDIPNDFVVGYGLDYDERYRDLSYIGTLDPRVYQ", "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 (PubMed:19362594, PubMed:25915781). Thus, specifically recycles hypoxanthine and guanine imported from the external medium, and converts them to IMP and GMP, respectively. Cannot use xanthine as substrate (PubMed:19362594). 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MNEKSLRVLEFNKIKDELKKYTQTSAAKDLIERLHPYESAYEVREHLMETEEAFKISIKKGDAPFSGLYDIREAISKAQRRFTLFPSELLRVANLLRASRRFKGYVKSDDLSEKYEVLESITEGLVPLNGLEEEISKCIIGEEEISDRASTTLFNIRRSLKDKTSSIKARVNSLIRTYSSHLQENIYTVRGERYVLPVKVEHKGAVPGLVHDQSASGATLFIEPMSLVDLNNEIKELRLKEKAEIDRILAFLSGKVYENVDVIKVDADILWELDFIFAKAKYAQKLGAIMPIISEDGHFNIINAKHPLIDPKKVVENNIYLRDGITSVVITGPNTGGKTVTLKTVGLLHIMAMSGLMITASQGSTISFFKEVFADIGDEQSIEQSLSTFSSHMTNIVNIIDSADENSLVLFDELGAGTDPTEGAALAVSILENLRKRKTKVIATTHYSELKAYALKVDNVENASVEFDVETLRPTYRLLIGVPGKSNAFEISKRLGLPDYIIEDAREGISEETLKFEDLIQSLQHKNIKAQEHARKAESAKEEAVKLKEKYESKLDKFQDIREKAILNAQKEAKEIIKEAKEEADKILKDIRELERMGYSSDVRKLLEENRKKLKDKLEKTESKLNQPKEVGEAVTNVSEGDELYLPKFETKVMVLTNPDNKGDVQVQAGIMKIKVNIKDLRKTKETKIEKRQRKKKQMSLNLKSVATSVDLRGMDSEEATYTADKYLDDACMSGLSEVTIIHGKGTGVLRTAINDMLKRHPHVKSYRLGNYGEGGNGVTVVELK", "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": "MYSSENDYSILEDKTATGKKRDWRGKKRRANLMAEHYEALEKRIGAPYYGKKAERLSECAEHLSFKRDPETGRLKLYQAHFCKVRLCPMCAWRRSLKIAYHNKLIIEEANRQYGCGWIFLTLTVRNVKGERLKPQISEMMEGFRKLFQYKKVKTSVLGFFRALEITKNHEEDTYHPHFHVLLPVKRNYFGKNYIKQAEWTSLWKRAMKLDYTPIVDIRRVKGRVKIDAEQIESDVREAMMEQKAVLEISKYPVKDTDVVRGSKVTDDNLNTVFYLDDALSARRLIGYGGILKEIHKELNLGDAEGGDLVKIEEEDDEVANGAFEVMAYWHPGIKNYILK", "text": "SIMILARITY: Belongs to the Gram-positive plasmids replication protein type 1 family."}
{"protein": "MSRKSLVFVTGNQNKLKEVVAILGDAFPWKVESKDIDLPEFQGEPDEISEEKCKIAAIKIAGPVIVEDTCLCFNAFGGLPGPYIKWFLKKLGPEGLHRMLTGWEDKTAYALCTFAYSSGKPDDPVLLFRGKTMGQIVEPRGPRNFGWDPCFQPDGFHQTYAEMASEVKNGISHRGKALQALKDHFLSLSEPDIKKAKCDEHER", "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": "MDQLFASIHATGQSLLGYYWPLVWNLVKIIAVVAPLMGAVAYLTLWERKVIGWMHVRHGPNRTGPAGLLQPIADGVKLLLKEIVVPAKSSKALFVIAPIMTIMPALAAWAVIPFGPETVLADVNAGLLFVMAITSLEVYGVIVAGWASNSKYAFLGAMRASAQMISYEIAMGFVLVIILMVTGSMNLTTIVNTQNTGRFAEMGLTFLSWNWLPLLPMFFIYIISGTAELNRHPFDVVEGESEIVAGHMVEYSGMSFAMFFLAEYANMWLISIMATLMFLGGWTSPIDMAPFTWVPGWIWLGLKTLMVVTMFIWFRASFPRYRYDQIMRLGWKVFIPLTLVYLLIVAIWMKTPWNIWN", "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": "MTFTKSVDQTTILQGDRSKLKDLLRVRLNACGWNDQVRLLCRETIKDQDTVNCDALVQQVTPKARALIPDTVKKELLQKIKAILIQQEGIDI", "text": "FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the ENY2 family."}
{"protein": "MIENLISHPHHIKLVGDFFNKKLFSSISTDHPLVILTDVQVAKEILPPIVDFIHSLDYTVVPLSFPSGEKNKTWETFISLQNQLIDHDIPLGSTMIGIGGGVVLDMVGFLASTYCRGIPLFLVPTTMTAMIDACIGGKNGINLRGLKNRLGTFYLPQDVWICPEFLSTLPKKEWLYGISEAIKHGCIADASIWEFLHNYGDMLFSSREILSEFIKRNCLVKAAIVAKDPHDQHLRKILNFGHTIAHAIETLSQGCLPHGLAVSVGMMIETKISLESGIMKNPALLEQLHHLSKRFHLPTTLEELRDLIPQHLHHEFYDPENIIHALGYDKKNLSKKAIRMVMMEDAGKATSCNGIYCTVPKMAILYEILKSECYAMCNN", "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": "MRVLGVDPGLTRCGLGVVDGALGSRARLVEAGVVRTPAGAEVADRLRAVADGIDAWLDRTRPDAVAVEKVFSQANVRTVMGTAQAGAVAIMLAARRDLPVGLYTPSEVKAAVTGSGRADKAQVGFMVTRLLGLAEVPRPADAADALALALCHLWRGPALARLRAAAPAAPVSRPAPATPARRSPRPAAPARRPAGAS", "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": "MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPSLRMKWMMAMKYPITADKRITEMVPERNEQGQTLWSKMSDAGSDRVMVSPLAVTWWNRNGPMTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGTRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSIKREEELLTGNLQTLKIRVHDGYEEFTMVGKRATAILRKATRRLVQLIVSGRDEQSVAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEHIDNVMGMIGVLPDMTPSTEMSMRGIRVSKMGVDEYSSTERVVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAIRGQYSGFVRTLFQQMRDVLGTFDTTQIIKLLPFAAAPPKQSRMQFSSLTVNVRGSGMRILVRGNSPAFNYNKTTKRLTILGKDAGTLIEDPDEGTSGVESAVLRGFLILGKEDRRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN", "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": "METLFNGTLTVGGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVSHFVPEKPMYEQGLILLPHIASLGYGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGVYHSLIGPETLEESFPFFGYIWKDKNKMTSILGYHLIMLGCGAWLLVLKAMYFGGIYDTWAPGGGDVRIITNPTTNFATIFGYLLRSPFGGDGWICSVDNLEDIIGGHIWIGTLCIFGGIWHIYTTPWPWARRAFVWSGEAYLSYSLGAIATMGFIACCFSWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVASAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWCEPLRGPNGLDLNKLKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINAVNFVSPRSWLATSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRVDEPVLSMRPLD", "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": "MKSTPKLLLLLLFIINHHVDSGSIVKFLPGFEGPLPFELETGYIGIGEEEDVQLFYYFIKSERNPKEDPLLLWLSGGPGCSSITGLLFENGPLALKSKVYNGSVPSLVSTTYSWTKTANIIFLDQPIGAGFSYSRIPLIDTPSDTGEVKNIHEFLQKWLSKHPQFSSNPFYASGDSYSGMIVPALVQEISKGNYICCKPPINLQGYILGNPITYFEVDQNYRIPFSHGMALISDELYESIRRDCKGNYFNVDPRNTKCLKLVEEYHKCTDELNEFNILSPDCDTTSPDCFLYPYYLLGYWINDESVRDALHVNKSSIGKWERCTYQNRIPYNKDINNSIPYHMNNSISGYRSLIYSGDHDLVVPFLATQAWIKSLNYSIIHEWRPWMIKDQIAGYTRTYSNKMTFATVKGSGHTAEYKPNETFIMFQRWISGHDL", "text": "FUNCTION: Probable carboxypeptidase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MTQLNDLPLQSLQFYATAPYPCSYLPERQARSQVATPSHLIQNDVYSGLVARGFRRSGMFTYRPYCDGCQACTPLRVVVDPFKPDRSQRRAWKRHAGLQARVLRLCYLPEHYQLYLRYQNARHAGGGMDQDSIDQYTQFLLQSRVNSRLVEFRETGADGQPGTLKMVSILDVLEDGLSAVYTFYEPEPGASYGTYNVLWQVQQARTLGLPYVYLGYWIEQSPKMNYKARFMPHELRIDGRWQRSKS", "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": "MKKHAIGIAALNALSIDDDGWCQLLPAGHFSARDGRPFDVTGGQGWFIDGEIAGRLVEGVRALNQDVLIDYEHNQLRKDKGLPPEQLVAAGWFNADEMQWREGEGLFIHPRWTAAAQQRIDDGEFGYLSAVFPYDTATGAVLQIRLAALTNDPGATGMKKLTALAADLPDILQQENKPMNETLRKLLARLGVTVPENADITDEQATAALTALDTLEINAGKVAALSAELEKAQKAAVDLTKYVPVESYNALRDELAQATAQSATASLSAVLDKAEQEGRIFKSERTYLEQLGGQIGVAALSAQLEKKQPIAALSAMQTTTAKIPSQEKTAVAVLSADEQAAVKALGITEAEYLKMKQEQEK", "text": "FUNCTION: Protease I is involved in virion assembly and maturation. Protease I cleaves the portal protein to yield mature procapsids competent for DNA packaging (Probable). Isoform scaffold protein Z probably helps the capsid proteins to assemble into a functional capsid (Probable). SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the peptidase U35 family."}
{"protein": "MAVKTLKDLLDEGVDGRHVIVRSDFNVPLNDDREITDKGRIIASLPTLKALSEGGAKVIVMAHLGRPKGEVNEKYSLAPVAEALSDELGQYVALAADVVGEDAHERANGLTEGDILLLENVRFDPRETSKDEAERTAFAQELAALAADNGAFVSDGFGVVHRAQTSVYDIAKLLPHYAGGLVETEISVLEKIAESPEAPYVVVLGGSKVSDKIGVIEALAAKADKIIVGGGMCYTFLAAQGHNVQQSLLQEEMKATCTDLLARFGDKIVLPVDLVAASEFNKDAEKQIVDLDSIPEGWMSLDIGPESVKNFGEVLSTAKTIFWNGPMGVFEFAAFSEGTRGIAQAIIDATAGNDAFSVVGGGDSAASVRVLGLNEDGFSHISTGGGASLEYLEGKELPGVAILAQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MAVFKTLTDADMAIFSAGLVAGVDEVGRGPLVGDVVTAAVILDPNRPIAGLNDSKKLTEKRREALFDEICEKALSYHVGRATPSEIDELNILHATMLAMQRAVAGLARTPELVLVDGNRSPAFTHQGLSLTSHSIVKGDGLIASISAASIIAKVTRDREMDALDAAYPQYGFAKHKGYPTKAHFDAIAEHGVFDQYRKSFKPVKALLER", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MEVQKLPDQSLISSMMLDSRCGLNDLYPIARLTQKMEDALTVSGKPAACPVDQDCPYTIELIQPEDGEAVIAMLKTFFFKDEPLNTFLDLGECKELEKYSLKPLPDNCSYKAVNKKGEIIGVFLNGLMRRPSPDDVPEKAADSCEHPKFKKILSLMDHVEEQFNIFDVYPDEELILDGKILSVDTNYRGLGIAGRLTERAYEYMRENGINVYHVLCSSHYSARVMEKLGFHEVFRMQFADYKPQGEVVFKPAAPHVGIQVMAKEVGPAKAAQTKL", "text": "FUNCTION: Catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin and octopamine (PubMed:7498465, PubMed:8901578, PubMed:25406072). In astrocytes, regulates sleep homeostasis by limiting the accumulation of serotonin and dopamine in the brain upon sleep deprivation (PubMed:10710313, PubMed:32955431). Is not essential for sclerotization (PubMed:9703021). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=In astrocytes, is primarily cytoplasmic, but in neurons is also nuclear. SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily."}
{"protein": "MALIVQKFGGTSVGSIERIEQVAEKVKKHREAGDDLVVVLSAMSGETNRLIDLAKQITDQPVPRELDVIVSTGEQVTIALLTMALIKRGVPAVSYTGNQVRILTDSSHNKARILQIDDQKIRADLKEGRVVVVAGFQGVDEHGSITTLGRGGSDTTGVALAAALKADECQIYTDVDGVYTTDPRVVPQARRLEKITFEEMLEMASLGSKVLQIRSVEFAGKYNVPLRVLHSFKEGPGTLITIDEEESMEQPIISGIAFNRDEAKLTIRGVPDTPGVAFKILGPISASNIEVDMIVQNVAHDNTTDFTFTVHRNEYEKAQSVLENTAREIGAREVIGDTKIAKVSIVGVGMRSHAGVASCMFEALAKESINIQMISTSEIKVSVVLEEKYLELAVRALHTAFDLDAPARQGE", "text": "FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4- phospho-L-aspartate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartokinase family."}
{"protein": "MNSPDIALIKTYLLTLQDNICAALAQADGHAEFTEECWVREEGGGGRSRVLVNGAVFEQAGVNFSHVSGAMLPASATAHRPELAGRSFQALGVSLVIHPLNPYLPTSHANVRFFIAEKPGEDAVWWFGGGFDLTPYYGFEEDAIHWHQVAHSLCQPFGEQIYPRYKKWCDDYFYIKHRQEARGIGGLFFDDLNSPDFMTCFNFTQAVGDGFLAAYMPIVARRKALGWGDRERQFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSLPPLVRWEYNYQPEADSAEAALYRDFLPVKDWLAIKGETH", "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": "MFCAEIMISKYQEDVKQPRACELCLNKHAVWYCASDDAFLCHVCDESVHSANHVATKHERVCLRTNEISNDVRGGTTLTSVWHSGFRRKARTPRSRYEKKPQQKIDDERRREDPRVPEIGGEVMFFIPEANDDDMTSLVPEFEGFTEMGFFLSNHNGTEETTKQFNFEEEADTMEDLYYNGEEEDKTDGAEACPGQYLMSCKKDYDNVITVSEKTEEIEDCYENNARHRLNYENVIAAWDKQESPRDVKNNTSSFQLVPPGIEEKRVRSEREARVWRYRDKRKNRLFEKKIRYEVRKVNADKRPRMKGRFVRRSLAIDS", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CONSTANS family."}
{"protein": "SPQXETKASVGFKAGVKDYKLTYYTPDYKTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENHFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIIMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIAKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFQAVDTL", "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": "MAKLGKRTRAAREAFAGKSNLTIEEAVALVKANATTKFDETVEIAMNLGVDTRHADQMVRGVVGLPNGTGKTMRVAVFARGPKADEAKEAGADIVGAEDLMETIQGGTIDFDRCIATPDMMPVVGRLGKVLGPRNLMPNPKVGTVTMDVKAAVEAAKGGEVQFKAEKGGVVHAGVGKASFDEAKLVENVRAFVSAVAKAKPSGAKGAYMKKIVLSSTMGPGVTLDVDGAVSE", "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": "MAYTNQISAVVFLAVAIAPLLAEPQSTMFPEMTPECATVMPDLLEKCFATGSVTPTEDCCTDLKSATSTQVTCLCDNYIANPAVSNITGPYSKAITTKCGVFDKYSCDGTSKGGEEKKGGSSSSNGKDNGKSEGNGGRANSVAASMAMFGLLASLVFVMF", "text": "FUNCTION: Probable lipid transfer protein. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the plant LTP family."}
{"protein": "MPLQPPPDHTWAVRIIALGLAVTALIFTSTRDTSRHVGDPSHSLPFGGHYRDGSKVIHYNSPRSSKPSNHTPYLLFAPIGIILLIHALHRLGNSAHICRCTHCMPHSQT", "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": "MYSGAGPVLVPPTTTPPLPMPAYTFKPPPRPDFGTSGRTIKLQANVFEMDIPKIEIYHYDIDIKPEKCPRRVNREIVEHMVQHFKAQIFGDRKPVFDGRKNLYTAMPLPIARDKQVELEVTLPGEGKDRIFKVAIKWMACVSLQALHDALSGRLPNVPFETVQALDVVMRHLPSMRYTPVGRSFFTASEGCANPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFMCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQESGQTVECTVAQYFKDRHKLVLRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQEEISKLMRSASFNTDPFVREFGIMVKDDMTDVTGRVLQPPSILYGGRSKAIATPVQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTEVHLKTFTEQLRKISRDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYTGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLSAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDRNERVGKSGNIPAGTTVDTKITHPSEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDQQALAKAVQVHQDTLRTMYFA", "text": "FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA- induced silencing complex (RISC). The 'minimal RISC' appears to include ago2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by ago2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P- bodies), where mRNA degradation may subsequently occur. SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
{"protein": "METATLVTISISCLLVSFTGYALYTAFGQPSKQLRDPFEDHED", "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": "MNVKGKAILSMLVASTVIVVFWEYINSSEGSFLWIYHSKNPEVGDVRAPMGWWFPSWFNNGTHIYQEEEEDVDKEKGRKKEQREKDDREELQLWDWFTPEKRPEVVTVTSWKAPVVWEGTYNSAILENYYAKQKITVGLTVFAIGKYLEYYLEEFIASADRYFMVGHKVIFYIMVNNVSRMPPLELGPLRSFEVFEIKAEKRWQDVSMMRMKIIGEHILTHIQHEVDFLFCMDVDQVFQDNFGVETLGESVAQLQAWWYKADPNEFTYERREKSAAYIPFGQGDFYYHAAIFGGTPIRVLNITQECFKGILQDKKNDIEANWHDESHLNKYFLVNKPSKILSPEYCWDYQIGLPSDIKIVKISWQTKEYHLVRNNV", "text": "FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. Preferentially glycosylates proteins, can synthesize galactose-alpha(1,3)-galactose on glycoproteins but cannot synthesize the glycolipid called isogloboside 3 (iGb3) (By similarity). 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 6 family."}
{"protein": "MTVSVEELKVLLPELAGRVLVAGAGVSGVGITQLLREMGCAVTVADSNSAQLDKLAQQTGCQTISPADVVSDGFQDYTVVVTSPGWRPDSPLLVAAQSAGLEVIGDVELVYRLDRAEVFGPKRTWMVVTGTNGKTTTTAMLAEIMQHSGARAAAVGNIGVSVADAVRTQPRIDVLVAELSSFQLHWSSTLVPDVGILLNLADDHIDWHGSFAQYAQDKAKVLAAPTAIAGFDNGHVMTETTRIQRAEDADPIIGFTLGEPAKGMVGVRDGQLIDCAFGDNVVLRSAEGIEPAGPAGLNDALAAAAAARSMGVSAVCIEEALSKFEVAGHRGQCVGRHREVVAIDNSKATNPHAADSALAGFSSVVWVAGGQLKGAEIDELIVRHAGRIKAVALLGVDRDVIEDSVRTHIPGIPVLSVSETDPRRAMDEAVAWSVSQAEAGDAIVLAPAAASLDMYTGMGQRGDMFATAIAQHLHD", "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": "MPKAEGRIFDFKGHDAIRTDFLEAIDFDGKDEYIKIETDEFSAVCPFSGLPDIGRVIIEYYPDGGKIVELKSLKYYFVSFRNVGIYQEEATKRIYEDLKNLLKTDRIRVTVIYNIRGGIKTTTQMGSLEGKKSGEVE", "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": "MKLKLRWKGHQRFLTRQNSLVGFIWSPLKNTFSKRNSILNNQVCFEAIKYIQRHYFSSQSHHVTYLHQSPLEKLVSNGVVNENGDLTMDSLSHQIYLLHKNRPTLPLKPTNQPTRFASVLMPLVNTSQGASLLLTQRSPNLRSHAGQMCFPGGRVEPSDGSHYYAALRETYEEIGFLPNFFTYLTTFPPLFTRDEKTEIRAYLAFSVQTSLPSLGTGEVKDLFYVPLTSFLNPKHQKISRFRNTDLLYVEFNIDKIPRIWGITAVILNMYLNSICPDALISIPKF", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily."}
{"protein": "MQLGEQLLVSSVNLPGAHFYSLESARGGGGGGGGGGGGGGGSVSLLPGAAPSPQRLDLDKASKKFPGSLPCQAGSAEPAGAGAGAPAAMLSDADAGDTFGSTSAVAKPGPPDGRKGSPCAEEELPSAATAAATARYSMDSLSSERYYLPSPGPQGSELAAPCSLFQYPAAAGAAHGPVYPASNGARYPYGSMLPPGGFPAAVCPPARAQFGPAAGSGSGAGSSGGGAGGPGAYPYGQGSPLYGPYAGTSAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKMYVHPESPNTGSHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEVTEDGVEDLNEPSKTQTFTFSETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSMYTASENDRLTPSPTDSPRSHQIVPGGRYGVQNFFPEPFVNTLPQARYYNGERTVPQTNGLLSPQQSEEVANPPQRWLVTPVQQPVTNKLDIGSYESEYTSSTLLPYGIKSLPLQTSHALGYYPDPTFPAMAGWGGRGAYQRKMAAGLPWTSRMSPPVFPEDQLAKEKVKEEISSSWIETPPSIKSLDSSDSGVYNSACKRKRLSPSTPSNGNSPPIKCEDINTEEYSKDTSKGMGAYYAFYTSP", "text": "FUNCTION: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MASHQSEKEKPQSCTTEVQVSHVTGLKLGLVVTSVTLVVFLMLLDMSIIVTAIPHITAQFHSLGDVGWYGSAYLLSSCALQPLAGKLYTLLTLKYTFLAFLGVFEVGSALCGAARCSTMLIVGRAVAGMGGSGLTNGAITILASAAPKQQQPLLIGIMMGLSQIAIVCGPLLGGAFTQHASWRWCFYINLPVGALAAILLLAIHIPKSVPTSDCTMPAPRAVGVRVILSQLDLLGFVLFAAFAVMISLALEWGGSDYMWDSSVIIGLFCGAGISLVVFGFWERYVGNSMAMIPFSVASRRQVWCSCLFLGFFSGALLTFSYYLPIYFQAVKDVSPTMSGVYMLPGIGGQIVMAIVSGAIIGKTGYYIPWALASGIIVSISAGLVSTFQPHTSIAAWVMYQFMGGFGRGCGMQTPIIAIQHALPPQMSALGISLAMFGQTFGGSLFLTLAKLVFSAGLDAGLREYAPAVSAEAVTAAGATGFRDVVPANLLSQVLLAYCKGIDHTFYLAVGASGATFLFAWGMGQVGLIWWGEERTGFGRDERV", "text": "FUNCTION: Efflux pump; 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, PubMed:19968298). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MYLSLLLLPMFGSAVTGLLGRKIGVTGAHIITCSCLITSAILAIVAFYEVGLCNSSVSINLISWIDSELMDVSWGFMFDSLTVSMLLPVLVVSSLVHIFSVDYMSADPHNQRFFAYLSMFTFFMLVLVTGDNYLIMFVGWEGIGISSYLLINFWFTRIQANKSAIKALVVNRVGDMFLSIGFFAIFFVFGNLDYSTVFSIAPFINETIITIIGLLLLLAAMGKSAQLGLHTWLPDPSMEGPTPVSALIHAATLVTAGVYLLLRSSPVIEYGPTTLIVITWVGALTAFFAASTGLLQNDLKRVIAYSTCSQMGYLFMACGLSQYNVALFHLVNHAFFKALLFLAAGAVLHATYDQQDQRRLGGLIGFLPFTYTAILIGSLSLIALPWLTGFYSKDLILEVAYGQYEFSGQVAYWLGTLSACLTAFYSLRLISLTFLTYPNASKSVYLHTHDAPTIVMIPLIILSLLAIFFGYVARDLFVGMGSDFLSPSLFTHPSHITLIEAEFGLPQIIKLLPAIGTLLGAGLALYLYHMLPVFTIDLTNSTLGQKLYRFFNGKYYVDVIYNHYIIYGGLQLGYVISKVLDRGIIELVGPYGLATGLTSGSKDIAKLDTGNLTSYALYLAIALVTLIMILLSPVLLNAALINAPLILVLLVAMVCIPYINSSSNDTVTTVQVKL", "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": "MNFLNFSILIFAYLLGSINSAIIVCYIFRLPSPRSVGSGNPGTTNVLRIGGKVLAAITLIFDILKGLVPVVIAKVLTGNDFITACTALYAILGHIFPIFFGFKGGKGVATLIGTLFGFSWILGLIFVITWLCVAIITRYSSLSALVATVIASFSVIFTSDLQVAAPFLIIAIIILVKHKGNIQRLISGQESKIGDKAKAKNDSN", "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": "MSITSDEVNFLVYRYLQESGFSHSAFTFGIESHISQSNINGTLVPPAALISILQKGLQYVEAEISINEDGTVFDGRPIESLSLIDAVMPDVVQTRQQAFREKLAQQQANAAAAAAAAAATATSTAATTPAAAAQQNPPKNGEATVNGEENGAHAINNHSKPMEIDGDVEIPPSKATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENSNGGSTQLVLRHCIREGGHDVPSNKDVTSLDWNSDGTLLATGSYDGFARIWTEDGNLASTLGQHKGPIFALKWNKKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWSPTGPATSNPNSNIMLASASFDSTVRLWDVERGVCIHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGSLVHSYRGTGGIFEVCWNARGDKVGASASDGSVCVLDLRK", "text": "FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Colocalized with MECP2 to the heterochromatin foci. SIMILARITY: Belongs to the WD repeat EBI family."}
{"protein": "MTPIQFTFSSAFLLGLSGLAFHRTHLLSALLCLEGMMLSLFIALSLWSLQLSSISFSSAPMLLLAFSACEASVGLALMVATARTHGSDHLQGLNLLQC", "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": "MQQGSAPKISFVSLGCPKALVDSERIITRLRAEGYELARKHDGADVVIVNTCGFLDSAKQESLSAIGSAMAENGKVIVTGCMGAEPEQIEQAYPGVLSITGPQQYESVLEAVHRASPPIHNPHLDLVPPQGIKLTPRHYAYLKISEGCNNRCTFCIIPKLRGDLVSRPAADVLREAERLVAAGVKELLVISQDTSAYGLDLKYAESSWKDRSVRARFLDLARELGELGAWVRLHYVYPYPHVDEVVGLMAEGRVLPYLDIPFQHASPNVLKAMRRPAAQDKTLDRIKSWRAACPDLALRSTFIVGFPGETDADFAYLLDWLDEAEIDRLGCFKYEPVAGATSNALPDQVPDEVKQERWNALMARQQKISARRLKRKVGTRQQIIIDEVGPTVAKGRSKADAPEIDGSVYVSSRRPLRVGEIVTARIERADEYDLHGTVAGF", "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": "MNIERADFVDRVKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGDGGFVFLRANPSVSTLIEFVNKRKFVAENGKHGMGKKMKGRNGKDLFIDVPVGTVVKDAVTGEIIADLNEPGKIVCVARGGKGGRGNAHFATSTKQAPLIAERGEKGESRWLELELKILADVGLVGYPNVGKSSLISRISNARPKIANYPFTTLIPNLGVVKYDDFSFVVADIPGLIEGASEGVGLGNVFLRHVERCYLIAHVIDVSGYEREDPVRDYFVIREEMKKYSPFLLEKPEIVVANKIDLIGKEELEKILKRLRDATNREVIPVSALTGEGIDLLVSKLASIVREMKVEKSERKEEKFVKPSPVWRRLPEKFHLEVVKEDEGYWVVEGENLRVWIERFDLNQRDARLMLLQVLEKNGLNNKLKEAGVKEGDVVRIGDFEFEYRE", "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": "MKDQLQALIEQAIDALRQDGTLPGDTAVDVQVTRTKDKAHGDFATNVALQLAKPARKKPRDVAEAIVARLPASGLVARTEIAGPGFINLFLGEQAKLSVIATIREQGERYGRSQLGAGKKVQVEFVSANPTGPLHVGHGRGAAYGAAVADLLEAVGFDVHREYYVNDAGRQMDILGTSVWLRYLELTGVELPFPTNAYRGDYVYDIAATLHREHGDHYKREAAEILDGLPPDEPDGGDKEEYIDAMIARAKELLGDNHYRFVFELGLNVILDDIRDDLAEFGVTYDTWYSERSLTDKGAVNLAIERLREAGHLYEKDGALWFRSTDFGDEKDRVVQRDNGQTTYFASDIAYHMDKMERGYDRVIDVWGADHHGYVPRVKAALKALGEDETRLDVLLVQFAILYRGGERVQMSTRSGSFVTLRELREEVGKDAARFFYVMRRCEQHLDFDLDLAKSQSADNPVYYIQYAHARVCSVLRQMEAKGLKHDPSHGEAKLSLLTESHEQEILATLARFPEVIEAAALVEEPHQIANYLRELANDFHTYYNAHQFLVDEPAIRDARLSLILAVRQVIANGLGLLGVSAPQEM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MAFVSRIRRQSDYNTYPSSIPIVIDNGASYFRIGWAGETEPRVVFRNIVQRPRHKATGETVTIVGDLDPSMMKYFDCTRSGPRSPFDSNVVYQFEIMEYILDYAFDRLGANGSGIDHPILITECACNPVQSRSKMAELLFETYGVPAVAFGVDAAFSYKYNQLHGICKKDGIVLCPGFTTTHSIPFVDGEPIYKGSSRTNIGGYHVTDYLKQLLSLKYPFHSSRFTWEKAEDLKLEHCYIAPDYASEIRLFQEGRKEAEEKTSYWQLPWIPPPTEVPPSEEEIARKAAIREKQGQRLREMAEAKRVSKINDMENQLISLRFLLKQVDQVEEDDIPTFLSDTGYASRQELESTITKVTQSLRKARGEPKNEPAEYEENPDSLNNEKYPLMNVPDDILTPEQLKDKKRQMFLKTTAEGRLRARQKRNEEELEKEKRNQLEEERRRENPESYLEELQAQYKEVLERVEQKKRLKTNGSSNGNNKSGGIGRGERLSAAQRERMRLLTTAAFDRGKGEDTFGSRDEDWQLYKLMSKDNDDDDEQPDSDEAELARLSSRLQEIDPTFVQKVEGELSQTSGEVPRVRPLTEEDYKIVIGIERFRCPEILFHPNLIGIDQVGLDEMAGTSIRRLPHDEKELEERLTSSILMTGGCSLLPGMNERLECGIRMIRPCGSPINVVRAMDPVLDAWRGASAFAANLNFLGNAFTKMDYDEKGEDWLRNYQIRYNYL", "text": "FUNCTION: Probable subunit of a chromatin-remodeling complex. Involved in DNA repair. Required for multicellular development of all organs. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Cytoplasm Note=Localized in the nucleoplasm of interphase cells (PubMed:19679120). However, dispersed into the cytoplasm in dividing cells at metaphase (PubMed:19679120). SIMILARITY: Belongs to the actin family. ARP5 subfamily."}
{"protein": "MKICGITDVETAKSACEYGADALGFVFAESKREITPKRAEEIIQELPANVLKIGVFVNESVEVIQKIADECGLTHVQLHGDEDNYQIRRLNIPSIKSLGVTSESDMKNAQGYEADYILFDSPKEKFHGGNGKTFSWELLRDMPKELRKKMILAGGLNALNIEEAIRTVRPYMVDVSSGVETEGKKDVEKIKQFIIKAKECSK", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MSLLDTLQRGLADLDAQGLRRVRRIAYTACDAHMTVNGREIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGGFSDAPRALYFSTGYMANLAAMTALAGKGATIFSDALNHASLIDGMRLSRANVQVYPHADTAALAALLDASAAETKLIVSDTVFSMDGDIAPLTELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPHLVYVGTLGKAAGVAGAFVIAHETVIEWLIQRARSYIFTTAAPPAVAHAVSASLKVIAGDEGDARRAHLAALIERTRALLRNTRWQPVDSHTAVQPLVIGSNDATLAAMRALDAHGLWVPAIRPPTVPAGTSRLRVSLSAAHSFDDLARLEAALIEASEAAAASVGAARQEAAA", "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": "MKTFVAKPHEVTRDWFVIDAKGKVLGRVASEVARRLRGKHKPEFTPHVDTGDYIVIINAADIVVTGKKSQDKKYFRHTTYPGGIRETNFEKMQERFPGRAIQKAVKGMLPKGPLGYAMIKKLKVYAGAEHPHTAQQPKPLDL", "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": "MSDKNRVALAFSGGLDTTVCVPLLEEEYGYDEVIGVTVDVGQPEAEFKEAEETAEALDLEHHVVDAKPEFAELCFDAVRANASYQGYPLGTALARPVIAEAILEVAKEEGCSGVAHGSTGKGNDQLRFEAVWRDSDLEVIAPVRELGLTRTFEQEYAEERGLPIEGGDEGKYSIDTNLWSRSIEGSELEEPGYVPPEDIYEWTTAPTAETLEVEVGFEDGYPVSLDGEKLEPVELIETLNDLAGDYGVGRTDIMEDRMLGLKVRENYEHPAATVLLNAHQALEDLVLTKEERAFKKQVDHEWSEKGYQGLVNAPLVDALEGFIDETQDRVTGTVTIRFEGGQARPVGRESPYAVYSAEAASFNTEDVTGGIEQSDATGVAKYHGFQERLANRVIDAADEE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
{"protein": "MKGFTKHSILMACSIGLAINATAADWDNIPIPAELDAGQSWELQQNYSDSFNYSGKNSTFTGKWKDSYFHSWTGPGLTHWSSDESWVGDGNLIISASRRQGTNKVNAGVITSKTKVKYPIFLEASIKVSNLELSSNFWLLSENDQREIDVLEVYGGARQDWYAKNMSTNFHVFFRNNDNSIKNDYNDQTHFTPTWGNYWRDGFHRFGVYWKSPTDVTFYIDGQKTTKGAWSQVVMKDKDYTGAILDKSRYNMDQEAFIIIDTEDHSWRSEAGHIATDADLADSDKNKMYVDWIRVYKPTGGSTTPPTGDITPPSGYTNLQLAHSNRCVDVINGALWNGSTYQQYSCNTGNNNQRFKFTKIANNQYSINAKVSQLCMELASGSSANGAKVQQWICNHANSNQTWSLEDKGSNTFEIRNKQSGKCLEVANSSNANGGQIRQWACTGATNQRFKFL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 16 family."}
{"protein": "MYPAHLLLLLAVCVSLLGASAIPPLPLNLIQFTYLIECANKGRRTSFNYADYGCYCGIGGSGTPVDKLDRCCKTHDECYAQAEKKGCYPKLTMYNYYCGEGGPYCNSKTECQRFVCDCDVRAADCFARYPYNNKNYNINTSKRCK", "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": "MKPKKIISNKAQISLELALLLGALVVAASIVGFYYLKSVTRGTSTAESISKNITLAAKNKALDNIYKVKRALNGQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0333 family."}
{"protein": "MKTLLLTLVVVTMVCLDLAYTRRCYNQQSSQPKTTKSCPPGENSCYNKQWRDHRGSITERGCGCPKVKPGIKLRCCESEDCNN", "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": "MEHLYIVSYDIRNQRRWRRLFKTMHGFGCWLQLSVFQCRLDRIRIIKMEAAINEIVNHAEDHVLILDLGPAENVKPKVSSIGKTFDPILRQAVIV", "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": "MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF", "text": "FUNCTION: [Isoform 3]: Retained in the ER, unable to perform carnitine uptake. FUNCTION: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine (PubMed:10454528, PubMed:10525100, PubMed:10966938, PubMed:17509700, PubMed:20722056). Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 11.3 (PubMed:10454528, PubMed:10525100, PubMed:10966938). In intestinal epithelia, transports the quorum- sensing pentapeptide CSF (competence and sporulation factor) from Bacillus Subtilis wich induces cytoprotective heat shock proteins contributing to intestinal homeostasis (PubMed:18005709). May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Basal cell membrane; Multi-pass membrane protein Note=In intestinal cells, apical expression is induced by TNF. Localized to the basal membrane of Sertoli cells (PubMed:35307651). SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family."}
{"protein": "MINMDKTLSVIVFLISLIIIFGIYFSSSNFSFKKVEINKSTINDFGDENILTFVPEVCDRFYYEKDGFDWERNINNIETVIIGSDAVVIEKGDFNETEILKELIENGYSVESCRGVYYYKNEKALSDRYIIVGNNLIIKANDISGIRWRYLQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MVCIPCIVIPVLLWVYKRFLEPVLYPIISPIISRFWRKTPLQDTPQQKTSTAECNGAANGSTANGPKTVADKKAD", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet. SIMILARITY: Belongs to the UPF0729 family."}
{"protein": "MKREQLYSGKAKTIYRTDDPDTLIAEFRNSLTAFNGEKKGEMELKGYYNAQISKKIFEMLEASGVKTHFVSMLTDIDMLVREVEIIKIEVIVRNIAAGSITRKYPIKEGTILKPPVLVFDFKSDEYGDPMLNDDIALALGIATREELAELRKLALRVNELLVPYLDEKGILLPDFKLEFGRREGEIVLADEISCDTCRFWDKKTGQSMDKDVFRFDKGDISKAYEEVARRIVPEIFE", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MEKEESTEQRKQARLAIMELANMISVPMALNAVVRLNVADAIWQGGANNPLSAAEILPRLLPAGGGDAENLQRLLRMLASYGVFYEHLSAGERKYSLTDVGKTLVTDEQGLSYAHYVLQHHQDALMRAWPMVHEAVVDPTKEPFERANGEPAYGYYLKHPEMNDLMVRAMSGVSVPFIRAMLEGYDGFQGVEKLVDVGGSGGDCLRMILEKHPTIKEGINFDLPEVVAKAPQIPFVTHVGGDMFKFIPQGDAIFMKWVLTTWTDEECKHIMQNCHKALPEGGKLIACEPVLPEDSDESHRTRALLEGDIFVMTIYRAKGKHRTEEQFRQLAIDAGFPRFRAFHVDHFYTVLEFQK", "text": "FUNCTION: Involved in nicotinate detoxification in planta (PubMed:28533213). Catalyzes the conversion of nicotinate to N- methylnicotinate, which is a detoxified form of endogenous nicotinate in planta (PubMed:28533213). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MAATLGILGRKLGMTRVFGDDGSIIPVTVIQAGPCPVTQVKNLEKDGYNAMQIGFDEIPERKVNKPEKGHLDKAARGYFRVLKEIRLDGPVPFEQGMDVTVDIFAPGEIVKVTGTSIGKGFAGVMKRWNFAGLKKTHGTEKAHRSGGSIGNNTEPGKVMKGKKMAGHMGARTVTVPSITVVDVRPEMNLILVKGQIPGPRNGVVVVRKQG", "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": "MADQLSEEQISEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMRDTDSEEEIKEAFKVFDKDGNGYISAAELRHVMTNLGEKLTDNEVDEMIREADIDGDGQINYEEFVKMMLSK", "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": "MSRSFFATVLGLALAAMTVMAAPADAKSRIKDIVAFEGVRDNQLIGYGIVVGLNGSGDSLRNAPMTKQSLEAMLERQGVNVRDGNLNTKNTAAVMVTANLPPFSAAGARMDVTVSTLGDAKSLLGGTLLVTALQGADGQTYAVAQGSVQTGSVSAGGASGSSVTKGVPTAGRIAAGGIIEKETGFQMVSMDVLRMTLRNPDFTTSRRIADVINGRFPGCAQAQNPTIVAVRPPAGMDMISFVTAIENLEVEPDAPAKVIIDEVAGVIVMGDDVRISQVAIAQGNLTISVQENPAVSQPTPFSRGGQTVVVPQSAVSIEEEKGKKLLTLGGGASLKSLIGGLNALGVTPRDMISILQAIKASGALQAEIEVM", "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": "MELPVKAPIPGGREISYRLETKNLSYRIGGNTPKFSNLCGLLSEKEEKVILKDVSCDARSAEITAIAGPSGAGKTTLLEILAGKVSHGKVSGQVLVNGRPMDGPEYRRVSGFVPQEDALFPFLTVQETLTYSALLRLKTKRKDAAAKVKRLIQELGLEHVADSRIGQGSRSGISGGERRRVSIGVELVHDPNVILIDEPTSGLDSASALQVVTLLKDMTIKQGKTIVLTIHQPGFRILEQIDRIVLLSNGMVVQNGSVYSLHQKIKFSGHQIPRRVNVLEYAIDIAGSLEPIRTQSCREISCYGHSKTWKSCYISAGGELHQSDSHSNSVLEEVQILGQRSCKNIFRTKQLFTTRALQASIAGLILGSIYLNVGNQKKEAKVLRTGFFAFILTFLLSSTTEGLPIFLQDRRILMRETSRRAYRVLSYVLADTLIFIPFLLIISMLFATPVYWLVGLRRELDGFLYFSLVIWIVLLMSNSFVACFSALVPNFIMGTSVISGLMGSFFLFSGYFIAKDRIPVYWEFMHYLSLFKYPFECLMINEYRGDVFLKQQDLKESQKWSNLGIMASFIVGYRVLGFFILWYRCYRTRS", "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": "MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPVEVEAAVA", "text": "FUNCTION: Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Overproduction is toxic. FUNCTION: Inhibits DNA replication at both initiation and elongation steps, most probably by binding to the opened, single-stranded regions at replication forks. Plays a regulatory role in chromosomal replication in nutrient-depleted cells. FUNCTION: Inhibits DNA replication at both initiation and elongation steps, most probably by binding to the opened, single-stranded regions at replication forks. Plays a regulatory role in chromosomal replication in nutrient-depleted cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MTTQSSSDGRMFTSSIIPVIPDSSPTAAEVIELSSQLSLPSPTSLLDFLSTSTSRGPTRSDTVGDKTQGKEVLDTRPILENSFRRENRVVTGTGGKAATGKRLKRRTESPGNACQSKIHIVSGEQIILGQSRPEKKAAKTKRTKKEDGLINYKLHGRVSKANQTVSRQPETKISAPKECNDTTQPAGNDHINDLDDGLQLEQATQRRFDWTPTKDTTIPVIDLVGDSPSSCEKSLSGMRSTRTMLSNYEFSGVVGTLGGSRSEGTPDAPTTKRPIELLKVNNFKEISGLSDDRQSSITEDSESATSKPRRVKAKNRPKSKLTTITSYATAKYTVVEKSVNLDPVETLLSDEPGKEKSAAKRTSGARCAKPGRKKSTTTEKKNEPPIFKVVHPLEAFKAFGGQELLFGTSSQLANGHSEDQHEQNEGTSHISNSSAFLPLSRSESSSKALSQASLGSGFLKLSSSKNLWSAGARDLTGAVLEIDEIDLSEHRMKPSIFAFQPKAPLGCKADTQIPPQLGEIDSDNSCQKPLAAIDPPEFVTRSETPSEKGVLHKYIVKPTHTNSCSQSGSSISVGSPEKPVQDKPIFNGFTTSELAKKVAAYGFKPIKSRDKMISLLEKCWENRNKAPNSVPKLTPGDGLSKVDEPTKGQSLGPHLQPNSISQKATTQVPKVKPAKRATKSQGVPVSSRRSTSTSKVSRKRTVSPSAILVDDDQTSDSTGDSVPPSRPRQPSKSCTPRDRENTPESFNLPTTPLTIRSGKVPSTVTSSESLPSLYTQITAAIKAQPRLRAFNGVKQPTWYEKILMYDPIQLEDLAVWLNTDGFERIGEDREVWPGLLREWCESKGVCCIWRKQRGARAHCPLVRA", "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": "MARYCGPKNRVARRFGANIFGRSRNPLLKKPHPPGQHGMQRKKKSDYGLQLEEKQKLKACYGMIMEKQLVKAFKEVIHKQGNVAQMFLERFECRLDNMVYRMGFAKTIFAAQQLVAHGHILVNGRRVDRRSFFLRPGMQISLKEKSKRLQSVKDALESKDESSLPSYISLDKTGFKGELLVSPEQDQIEAQLPLPINISVVCEFLSHRT", "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": "MAEEIITPVYCTGVSAQVQKQRAKELGLGRHENAIKYLGQDYEQLRARCLQSGTLFRDEAFPPVPQSLGFKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYESLSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQMVNLIRMRNPWGEVEWTGAWSDSSSEWNSVDPYEREQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPALHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTAELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA", "text": "FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1. Cleaves and activates caspase-7 (CASP7). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Translocates to the plasma membrane upon Ca(2+) binding. SIMILARITY: Belongs to the peptidase C2 family."}
{"protein": "MQFLDFLIALLPALFWGSVVLINVFVGGGPYNQIRGTTLGALIVGLGLLITGFAKFNNPTVIIVGLISGALWAFGQANQLKSISLIGVSNTMPVSTGMQLVGTTLFSVIFLGEWSSMTQIIFGLIAMILLVTGVALTSLKAKNERQSDNPEFKKAMGILIVSTVGYVGFVVLGDIFGVGGTDALFFQSVGMAIGGFILSMNHKTSLKSTALNLLPGVIWGIGNLFMFYSQPKVGVATSFSLSQLLVIVSTLGGIFILGERKDRRQMTGIWVGIIIIVIAAIILGNLK", "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": "MSLLDAHIPQLVASQSAFAAKAGLMRHTIGQAEQAAMSAQAFHQGESSAAFQAAHARFVAAAAKVNTLLDVAQANLGEAAGTYVAADAAAASTYTGF", "text": "FUNCTION: EsxG, in complex with EsxH, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. EsxG stabilizes EsxH in the host cytosol. SUBCELLULAR LOCATION: Secreted Note=Secreted via the ESX-3 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily."}
{"protein": "MSEPASISSGIAARYAAAVFELAKDEGALPALEKDMDALGAAWAESADLRDLATSPVYAREDQQKAIAAIAAKMGLSSLTSNTLALMGSKRRLFVLPQMVADVQNRIATEKGEITAEVTAAAPLSPEQAARLAATLKARAGKDVKLKTTVDESLIGGLVVKLGSSMIDTSVKARLAALQNAMKEVG", "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": "MNQEVKSGKILSPSTPWTERQVPGIQVANEQQSLKATSTEPTIECPECHALVTRTAIAFNAYVCPSCDEHLRMKARDRLTWFFDQVDAELGQEFSAKDPLKFVDSKPYPERMREAQSKTGETEALVVMQGTLNNVSMIACAFEFDFMGGSMGTVVGDRFVQAAERAIEQKQALICFAASGGARMQEGMLSLMQMARTSAAIQRMKDAGLPYIVVLTHPVYGGVTASLAMLGDVHIAEPKAMIGFAGKRVIEQTVRETLEEPFQRAEYLLDHGVVDQIVHRHALRDTVSRIVSKLMNLP", "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": "MWFCIDLGADAFEEAGALAGKKNKRALQHILGLNIFKQELIPPCKDPDPFQIQLLLKNYTLKNVSTIFSYYCQ", "text": "SIMILARITY: Belongs to the asfivirus DP63R family."}
{"protein": "MSVQEYLDKHMLSRKIEDAVNAAVRAKTSDPVLFIANHLKKAVSSVITKVKARQILDSRGIPTVEVDLHTNKGVFRASVPSGDSSGTYEAIELRDGDKGMYLGNSVAKAVKNINEKISEALIGMDPKLQGQIDQAMIDLDKTEKKSELGANAILAVSIAACKAGAAEKEVPLCKHLSDLSGRANMVLPVPAFTVLSGGKHASNTFAIQEIMILPIGASRFEEALQWGSETYHHLKAVISEKNGGLGCNVGEDGGLAPDISSLKEGLELVKEAINRTGYNDKIKIAIDIAATNFCLGTKYDLDIKSPNKSGQNFKSAEDMIDMYKEICNDYPIVSIEDPFDKEDWEHTKYFSSLGICQVVGDDLLMSNSKRVERAIQESSCNALLLKVNQIGTVTEAIEVVKMARDAQWGVVTSHRCGETEDSFISDLSVGLATGVIKAGAPCRGERTMKYNQLLRIEEELGDQAVYAGEDWKLSL", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the enolase family."}
{"protein": "MLAVIRIRGRTGIKQDIEDTAHLLRLNRINHLVLLQEDAVTKGMLQKVKDYVTWGEIDVDTLEVLLKNRCLFKGRRKLTEEELKDVTGFGSYRDLAKALVDGKIKFSEINDVVPVIRLNPPYKGYEAIKTSYRNGGSAGYRGKDINNLIRRMIIPGVDLNGQREN", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "GVDSSFVRL", "text": "FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRF amide related peptide) family."}
{"protein": "MTLPSGHPKSRLIKKFTALGPYIREGQCEDNRFFFDCLAVCVNVKPAPEKREFWGWWMELEAQEKSFTYRYQFGLFDKEGNWTAVPIKETEVVERLEYTLREFHGKLRDLLISMGLALEPSDDFNDEPVKLSA", "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": "MLKEKNLKWLSLFTTVLMLFVQIGGALVTKTGSADGCGSSWPLCHGKFVPTHIPKETLIELAHRGVSGLALLSVTWLVILSIKYIGHKKETKFLCYMSIGFIFAQALIGAAAVMWQQNGFVLALHFGISLISFSAVFLLTLLIFEVDQKFDATKLILQPKLRRHTIGLTSFIYFVIYSGALVRHEKASLACSSWPLCRKGAFILPQNFYEWVQMSHRTLAFILFIWLTYVAFHAMRNYAQYRVIKYGYMIAFILICLQVTTGALTIFTAVNLYIALLHALFITLLFGLLCYFILLISRAK", "text": "FUNCTION: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the COX15/CtaA family. Type 1 subfamily."}
{"protein": "MSRRQEICRNFQRGSCKYGAQCRYLHASPHQQQQQQQAKPNPFGFGTGSRQQQQPSFGSQFQQQQQQQQKPNPFGFGVQGANAQSRNAPGPAKPFQNKWVRDPSAPTKQTEAVQPPQAQAAHTSCEDPQSCRQQISEDFKNEAPIWKLTCYAHLRNGPCNIKGDISFEELRAKAYEEGKQGHSLQSIVEGERNLQNAKLMEFTNLLNSARPSQTPSFPTMSSFPEVKNNSSFGASQTNGPPVFSSFSQIGAATNIGPGPGTTAPGMPASSPFGHPSSAPLAAPTFGSSQMKFGVSSVFGNQGSGQPFGSFQAPRFPSSKSPASSVQHRDIDRQSQELLNGMVTPPSVMFEESVGNNKNENQDDSIWLKEKWAIGEIPLDEPPQRHVSHVF", "text": "FUNCTION: Transcriptional activator that binds double-stranded DNA and the single-stranded RNA polymers poly(rA), poly(rU) and poly(rG), but not poly(rC). Mediates optimal plant architecture through brassinosteroid (BR) signaling. May act as a negative regulator in sterol homeostasis (PubMed:18953406). Acts as negative regulator of BR signaling. Binds to the specific DNA sequence 5'-CTCGC-3' of BZR1 promoter and negatively regulates BZR1. Acts as an antagonistic transcription factor of BZR1 to attenuate the BR signaling pathway and regulate leaf bending. Represses the expression of ILI1, and activates that of IBH1 to balance the regulation activity of BZR1 (PubMed:22570626). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Brassinosteroid promotes nuclear localization. Phosphorylation represses nuclear localization."}
{"protein": "GFGSLFKFLGKKLLKTVAKQAAKKQME", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 03 subfamily."}
{"protein": "MFRTISRKNMSQKLSFLLLVFGLIWGLMLLHYTLQQPRRQSSVKLREQILDLSKRYVKALAEESRSTADVDSGASMAGYADLKRTIAVLLDDILQRLVKLESKVDYIVVNGSATNTTNGTNGNLVPVTTNKRTSVSGSVR", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MIKVGILDSTLREGEQTPGVIFTVDQRVEIAKALSDLGVSMIEAGHPAVSPDIYEGIKRIVKLKKEGIITSEIVGHSRAVKRDIEIAAELEVNRIAIFYGVSDLHLKAKHKATREEALRTIAETISYAKNHGVKVRFTAEDGSRTDFDFLVTVSKTARDAGADRVSIADTVGILYPSKTKELFSALTREVPNLEFDIHAHNDLGLAVANALAAIEGGATIIHATVNGLGERVGIVPLQQIAAAIKYHFGIEVVKLDKLQYVSSLVEKYSGIPMPPNYPITGDYAFLHKAGVHVAGVLNDPRTYEFMPPETFGRTRDYTIDKYTGKHALRDKYEKLGVKISDAEMDQILAKIKSNTTIRFYRDVDLLELAEEVTGRVLKPRPPEQIEALISVKCDSNVYTTSVTRRLSVINGVKEVMEISGDYDILVKVQAKDSNELNQIIESIRATKGVRSTLTSLVLKKM", "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": "MVKSHKRTLEKDEEHQEKKKANKISKDDMEIDAELLTQQASDSAHTDTATAAVAAVNNEQGKELEQTESSTNQTSALDKDDKETKDNLNPREETQSSHQEIDIPKDQLTNQQNLADQHQQYQYHQQLAQTNFKTEPTNSAKPPHGSEEWHRQRRENHKEVERKRRESINTGIRELARLIPTTDTNKAQILQRAVEYIKRLKENENNNIEKWTLEKLLTEQAVSELSASNEKLKHELESAYREIEQLKRGKK", "text": "FUNCTION: Transcription factor that binds ribosomal protein gene promoters and rDNA locus with TBF1. Necessary for the expression of genes involved in assimilation of inorganic sulfate. Also required for the expression of respiratory genes and glycolytic genes. Does not bind to centromeres and is not necessary for efficient chromosome segregationas as does S.cerevisiae CBF1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAIEFKRSPKPTIGVEWEIALVDPESRDLAPRAAEVLEIVAERHPEVHLEGEFLQNTVELVTGICDTVPEAVAELDRALAAVQEAATELGLRPWTSGSHPFSDFRENPVSKKGSYDEIIARTQYWGNQMLIWGIHVHVGISHEDRVWPIINALVTNYPHLLALSASSPAWDGLDTGYASNRTMLYQQLPTAGLPYQFQSWDEWVSYMADQDKSGVINHTGSMHFDIRPASKWGTIEVRIADSTSNLRELSAIAALTHCLVVHYDRMIDRGEQLPTLQPWHVAENKWRAARYGLDAEIIISRDTDEAMVQDELRRLVDRLTPLAAELGCLRELDLVLEIIERGGGYERQRRAYQRTGTWIAAVDLACDELNELRPLEAE", "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": "MTLLNPYFGEFGGQFVPQILMPALRQLEEAFVNAQKDPEFQAEFTDLLKNYAGRPTALTLCQNLTAGTKTKLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVATALACALLGLKCRVYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSSTLKDACNEALRDWSGSYETAHYLLGTAAGPHPYPTIVREFQRMIGEETKAQILEKEGRLPDAVLACVGGGSNAIGMFADFIDDTSVRLIGIEPGGLGIESGQHGAPLKHGRLGIYFGMKSPMMQTSDGQIEESYSISAGLDFPSVGPQHAYLNSIGRADYVSITDDEALDAFKTLCRSEGIIPALESSHALAHALKMIKAEPEKEQLLVVNLSGRGDKDIFTVHDILKDRGEI", "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": "MMKKNNSTKRGPQDGNHQCAPPEKVGWVRKFCGKGIFREIWKNRYVVLKGDQLYISEKEVKDEKNIQEVFDLSDYEKCEELRKSKSRSKKNHSKFTLAHSKQPGNTAPNLIFLAVSPEEKESWINALNSAITRAKNRVLDEVTVEEDSYLAHPTRDRAKIQHSRRPPTRGHLMAVASTSTSDGMLTLDLIQEEDPSPEEPTSCAESFRVDLDKSVAQLAGSRRRADSDRIQPSSDRASGLPRLWEKPDKGATYTPQAPKKLTATEKSRCASLEEILSQRDAVPAHTLQRRAEDPPTPIPHAPGQLSRIQDLVARKLEKTQELLAEVQGLGDGKRKAKEPPRSPPDSESEQLLLETERLLGEASSNWSQAKRVLQEVRELRDLYRQMDLQTPDSHLRQTTQHSQYRKSLM", "text": "FUNCTION: Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation (By similarity). SUBCELLULAR LOCATION: Membrane Nucleus Cytoplasm."}
{"protein": "MSVHKTNDAFKVLMNSAKEPIVEDIPKKYRKQSFRDNLKVYIESPESYKNVIYYDDDVVLVRDMFPKSKMHLLLMTRDPHLTHVHPLEIMMKHRSLVEKLVSYVQGDLSGLIFDEARNCLSQQLTNEALCNYIKVGFHAGPSMNNLHLHIMTLDHVSPSLKNSAHYISFTSPFFVKIDTPTSNLPTRGTLTSLFQEDLKCWRCGETFGRHFTKLKAHLQEEYDDWLDKSVSM", "text": "FUNCTION: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species (PubMed:24362567, PubMed:21984208). Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'- phosphate termini that can be efficiently rejoined (PubMed:24362567, PubMed:21984210). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (PubMed:26007660). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MVAKKRTQLRAKAMRQRRNSSEAMETEELPPDPKAFLHQLRESKREKQLNRSQSFLNRLRDQAGNGGISKSALRRRKKRMKEELKPRMEDLLTSLKEEGVLEEDESGELAAVTGVTAITASNGYSGLHDTAEACGTVRIRKNEPSIRTQRGAKLLTTKEQERFTKVISNERFRSSPFETLREIIKSRK", "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": "MALPAGPAEAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPGRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADAGPLCAACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKEEGLPEDELADPTERFRSLLQAVSELEKKHRNLGLSMLLQ", "text": "FUNCTION: E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus."}
{"protein": "MIDREQVRKVALLARLELTPQEEEQFTTQLGSILDYVEQLNELDVSNVPPTARAIDVSNITREDNLQPYADREAILSSAPEQEGEFFKVPKILNAE", "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": "MRSDSARKGLEKAPHRSLFKALGFIDEEMERPLIGIASSYSEIIPGHMNLDKVVQAVKDGVRMAGGVPVTFGTIGVCDGISMNHKGMSYSLPSRQLIADSVEIVASAHAFDGIVLVPNCDKVVPGMMMAAARLDIPAIVISGGPMLAGNTCGKATDLSGVFEAVGAVKAGNMTEEELSELENTACPTCGSCSGMYTANSMNCLSEVLGLALPYNGTIPAVYSERLRLAKTSGMKIVDLVKKGLTPSKILTEEAFMNAITADMALGCSTNSLLHLPAIANEVGITID", "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. Is specific for the (R) isomer of 2,3-dihydroxy-3-methylbutanoate, with no catalytic activity against the (S) isomer. SIMILARITY: Belongs to the IlvD/Edd family."}
{"protein": "MALLKVAPSRLLSRALQLTSTLQNCTATSIAARRNFHFTVYGRKDTSAKVSDSISTQYPVVDHDFDAVVVGAGGAGLRAAFGLSEAGFNTACITKLFPTRSHTVAAQGGINAALGNMEDDDWRWHFYDTVKGSDWLGDQDAIHYMTEQAPASVIELENYGMPFSRTEQGKIYQRAFGGQSLKYGKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCMEDGSIHRFRAKNTVIATGGYGRTYFSCTSAHTCTGDGTAMVTRAGLPCQDLEFVQFHPTGIYGAGCLITEGCRGEGGILINSEGERFMERYAPVAKDLASRDVVSRSMTIEMREGRGCGKDKDHVYLQLHHLPPSQLASRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQVITHVNGEDRVVPGLYACGEAASASVHGANRLGANSLLDLVVFGRACALSIAEECKPGEALPSIKENAGEESVANLDKLRFANGSTRTSELRLNMQKTMQTHAAVFRTGSVLKEGCEKLSVINSAMDDLKTFDRGIVWNTDVVETLELQNLMLCALQTINSAEARKESRGAHAREDYKTRIDEYDYSKPIQGQQKKSFSEHWRKHTLSYVDSKGKVSLEYRPVIDATLNEDCASVPPAIRSY", "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": "MPVLADEGFEGPTKEVFQTPHWFDVGIGSVNLYLNKATALTIFAALFVGVIFWLGFRRAKIIPRGLQNLCESAYDFIDLQIARGVIGEKGTRYTPYLLVLFSFVLICNVLAVVPGAQFPATSRIAVPMVLALVTYVLFNYAGIKANGAGPYFKEMIDPAPTAPLWIRVLLAPIEILSTLIVRPFTLAVRLFANMFAGHILLLVFSLGADYLLPKPPYVFGAASLLVAIILTAFELVIDALQAYIITILTAAYIGGAMVHGEHEVAPSEELASPAPAGVPVSARA", "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": "MLKIFNTKFIRSAPVVAAVWLSLTAGIIIEFNRFFPDLLFHPMS", "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": "MASVNKVILVGNLGRDPEVRYSPDGAAICNVSIATTSQWKDKASGERREETEWHRVVMYNRLAEIAGEYLKKGRSVYIEGRLKTRKWQDKDTGADRYSTEIVADQMQMLGGRDSGGGYGGGYDDAPRQQRAPAQRPAAAPQRPAPQAAPAANLADMDDDIPF", "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": "MARQKFDGNKPHVNIGTIGHVDHGKTTLTAAITTALASQGKGKARKYDEIDAAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPNMVVFLNKEDQIDDADLLELVELEVRELLSKYDFPGDQIPFVSGSALLALESLSSNPKLMRGEDKWVDKILALMDAVDEYIPTPERPIDKSFLMAIEDVFSITGRGTVATGRIERGAIKVGETVELVGLKDTKSTTVTGLEMFQKTLEEGMAGDNIGILLRGVQKTDIERGMVLAKPGSITPHTQFESEVYVLTKDEGGRHTPFFSGYRPQFYVRTTDVTGSIDAFTADDGSNAEMVMPGDRIKMTVSLVHPIAIEQGMRFAIREGGRTIGAGVVSKILK", "text": "FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily."}
{"protein": "MASNDKGLEEIPDNQIESNYDEITDSFDAMNLRAELLRGVYAYGFERPSAIQQRAIMPVIKGSDVIAQAQSGTGKTATFSISALQKVDTNLKACQALILAPTRELAQQIQKVVVAIGDFMSVECHACIGGTNVREDIKALNDGPQVVVGTPGRVHDMIQRRVLKTDQMKMFVLDEADEMLSRGFTEQIYDIFQFLPQSTQVVLLSATMPQDVLDVTTKFMRDPVRILVKKAELTLEGIKQFYIAVEKEEWKLDTLSDLYETVTITQAVIFCNTRRKVDWLTDKLIARDFTVSAMHGEMEQNQRDVIMKEFRSGSSRVLIATDLLARGIDVQQVSLVINYDLPANRENYIHRIGRGGRFGRKGVAINFVTADDVRMMREIEQFYSTQIEEMPMNVADLI", "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": "MYYGFDVGGTKIEFGAFNEKLERVATERVATPRDDYDKLVDTIVGIIQKADNDLGCEGLVGIGLPGMEDARDGSVLTSNIPAAKGRFLRKDLEAKLGRTVTIDNDANCFALSEAWDESLQGEKSVLGLILGTGFGGGLVFDGHVFSGMNHVAGELGHTRMPIDAWFSLGEKAPLFTCGCDNKGCIDNYLSGRGFEQLYAHYYGENLKAIEIIKLHATGEAKAVEHVDRFMEMLAICLANIFTGLDPHVVVLGGGLSNFELLYQELPKRIAKHLLSVAQVPKIVKAKHGDAGGVRGAAFLNIKK", "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": "MEMLKFGKFAALALAMAVAVGCSSKGGDASGEGANGGVDPNAGYGANSGAVDGSLSDEAALRAITTFYFEYDSSDLKPEAMRALDVHAKDLKGSGQRVVLEGHTDERGTREYNMALGERRAKAVQRYLVLQGVSPAQLELVSYGKERPVATGHDEQSWAQNRRVELKK", "text": "FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the Pal lipoprotein family."}
{"protein": "MFGRNFPFFNSIGGFYPRDSLDPRKPSGTGYTSKVRVRDKYHIVGFISSGTYGRVYKAIGKDGRKGEFAIKKFKPDKEGEIIQYTGLSQSAIREMSLCSELDHSNVVQLAEIILEDKCIFMVFEYTEHDLLQIIHHHTQPQRHAIPAPMIKSILFQLLNGLLYLHTNWVLHRDLKPANILVTSSGAVRIGDLGLARLFYKPLNSLYSGDKVVVTIWYRAPELLMGSRHYTPAVDLWAVGCIFAELLSLRPIFKGEEAKMDSKKTVPFQRNQMMKIVEIMGLPRKETWPGLVAMPEFSQLQSLAMARGHLNRQSNLEGWYQSCLKNNGYSPTSSAGTPGPEGFDLLSRLLEYDPLKRISAQEALEHPYFTTGTPITANCFAGYEGKYPHRRVTQDDNDIRSGSLPGTKRSGLPDDSLMGRAAKRLKE", "text": "FUNCTION: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The srb8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MRKRISAIINKLNISIMMMIVVLMIGCGQQAVEAGKDGAAAATGGRSLSEVLMEVGKSAENAFYSFMALVPDTLGLRVTKDTKKNEVGGYFNSLGGKLGKASDELEEVAKKSEVEGAKDGPIAVAIRAAVDTAKTTLSTLKEHLESLKGIGDDDKVGEATSNQNGVAASTDELKGAFKALKGIVDTAGKEGVAKPKAGDTAVKIGNADNKDGAKVLAAAANAGRAVGDKAAAIVSAVSGEEMLASIVASQEGDADAALAADATAQTSALKFARGGGNAGQLAKEAAKAAAVAGGIALRSLVKGGKLAANNNDDDKVVQSAGVTAVNKLLVAVEGIIKKTVKNVLEKAKGEIDKARAPKATGQ", "text": "FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable large protein (Vlp) family. Alpha subfamily."}
{"protein": "MDFIHILALAILQGLTEFLPISSSAHLILLPVLAGWTDQGLAFDVAVHLGTLVAVISYFRLELARMARDWLQSLAAGQQQGESRLAWAVLLGTLPVGLVGIMLTETTQEALRSPLIIAWSTVGFGFLLAYADWAGKQQRNEHTLTWRDILFIGLAQALALIPGTSRSGITITAGLMLGLTREGAARFSFLLAIPVILLAGGLAALDLLNHTETVDWNALALGALISGLCAYACIHYFFKFLQRIGMLPFAVYRLLLGALLFYLFS", "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": "MGLTRRIIPCLDLKAGRVVKGVNFEGLRDAGDPVELASRYNEQGADEVVFLDIAASKDNRDTMIDVIGRAADELFLPLTVGGGIRTVKDIQDILRAGADKVSLNTSAVKTPDVINEGSHLFGNQCIVLAEDVRRNYEMRDGVTPIHLADGRVCWYEVVIYGGSQRTGIDAVSWAQEGVKRGAGEILLTSMETDGVKTGFDLEITAAISENVDVPVIASGGVGTLEHFYDGFVKGKADACLAASVFHYGEMTIRSVKEYLASRGVLVRL", "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": "MNFIDEVKIYIKGGNGGNGCVSFHREKFIDRGGPDGGDGGHGGSVIFRSNHHLNTLVNYRYKQHFTAENGKNGQGSNRSGKSGKPLVLDVPIGTQIFSEDGNILLYDFIEDDQSFEIIKGGSGGLGNSHFKTSVNQAPRKRTEGEVAKEMWIHLSLKLLSDVGFVGLPNAGKSTFLSVVTAAKPKIADYPFTTLVPNLGVVYVDDEEFVIADIPGLIEGAHQGHGLGDKFLKHIERCRVLIHLIDGSSNDVVADYNTVRFELESYSDYLKNKIEIICLNKCDVLTDEEIQDKINKLRKVTNKEVFPISTYTNIGVNKIVKLALEVIKNQE", "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": "MAPAGQTTYQKDERVLCFHHEILYEAKILDLRHTDPDDRKSPYEYLVHYKGWKNTWDDWVPQDRLRKFTEENRELATTLRREAEAALRQKSTKTSLKKKGGSDHSSARGSEERQTSVPGRGTKRARDNDIEKEEHFYTRPSVRIVMPDNLKSLLVDDWENVTKNQQVVALPAKSSVNQILDDYLKEERPKRTGSSEVDVLEEVVMGIRDYFDKSLDKILLYRFEREQYRVLRKRWESETADKGPLDVYGAEHLTRLFATMPELIAQTNMDLQSTNRLREELSKFTIWLSKNSNHYFATRYVTASNEYIEKSRGVPNPAPGTATSRLV", "text": "FUNCTION: Involved in deacetylation of histones, chromatin assembly and chromosome segregation. May act as a transcriptional oscillator, directing histone deacetylases to specific chromosomal domains. 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 MRG family."}
{"protein": "MALSVPGYSPGFRKPPEVVRLRRKRARSRGAAASPPRELTEPAARRAALVAGLPLRPFPAAGGRGGGSGGGPAAARRNPFARLDNRPRVAAEPPDGPAREQPEAPVPFLDSNQENDLLWEEKFPERTTVTELPQTSHVSFSEPDIPSSKSTELPVDWSIKTRLLFTSSQPFTWADHLKAQEEAQGLVQHCRATEVTLPKSIQDPKLSSELRCTFQQSLIYWLHPALSWLPLFPRIGADRKMAGKTSPWSNDATLQHVLMSDWSVSFTSLYNLLKTKLCPYFYVCTYQFTVLFRAAGLAGSDLITALISPTTRGLREAMRNEGIEFSLPLIKESGHKKETASGTSLGYGEEQAISDEDEEESFSWLEEMGVQDKIKKPDILSIKLRKEKHEVQMDHRPESVVLVKGINTFTLLNFLINSKSLVATSGPQAGLPPTLLSPVAFRGATMQMLKARSVNVKTQALSGYRDQFSLEITGPIMPHSLHSLTMLLKSSQSGSFSAVLYPHEPTAVFNICLQMDKVLDMEVVHKELTNCGLHPNTLEQLSQIPLLGKSSLRNVVLRDYIYNWRS", "text": "FUNCTION: Replisome component that maintains genome stability by protecting stalled or damaged replication forks. After the induction of replication stress, required for the stabilization of stalled replication forks, the efficient activation of the intra-S-phase and G/2M cell-cycle checkpoints and the maintenance of genome stability. SUBCELLULAR LOCATION: Nucleus Note=Localizes at DNA replication sites. SIMILARITY: Belongs to the DONSON family."}
{"protein": "MDKRFAVVLAAGQGTRMKSKLYKVLHPVCGKPMVEHVVDEALKLSLSKLVTIVGHGAEEVKKQLGDKSEYRVQAKQLGTAHAVKQAQPFLADEKGVTIVICGDTPLLTAETMEQMLKEHTQREAKRTILTAVAEDPTGYGRIIRSENGAVQKIVEHKDASEEERLVTEINTGTYCFDNEALFRAIDQVSNDNAQGEYYLPDVIEILKNEGETVAAYQTGNFQETLGVNDRVALSQAEQFMKERINKRHMQNGVTLIDPMNTYISPDAVIGSDTVIYPGTVIKGEVQIGEDTIIGPHTEIMNSAIGSRTVIKQSVVNHSKVGNDVNIGPFAHIRPDSVIGNEVKIGNFVEIKKTQFGDRSKASHLSYVGDAEVGTDVNLGCGSITVNYDGKNKYLTKIEDGAFIGCNSNLVAPVTVGEGAYVAAGSTVTEDVPGKALAIARARQVNKDDYVKNIHKK", "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": "MINMRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLLLQILTGLFLAMHYTSDTSTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPTGIPSDADKIPFHPYYTIKDILGVLALFLALMLLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALIASILILLLMPLLHTSKQRSMMFRPISQCLFWLLAADLLTLTWIGGQPVEHPYIVIGQLASISYFSIILVLMPVAGMIENKLLKW", "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": "MCPLTLHVTGLMNVSEPNSSFAFVNEFILQGFSCEWTIQIFLFSLFTTIYALTITGNGAIAFVLWCDRRLHTPMYMFLGNFSFLEIWYVSSTVPKMLVNFLSEKKNISFAGCFLQFYFFFSLGTSECLLLTVMAFDQYLAICRPLLYPNIMTGHLYAKLVILCWVCGFLWFLIPIVLISQKPFCGPNIIDHVVCDPGPLFALDCVSAPRIQLFCYTLSSLVIFGNFLFIIGSYTLVLKAVLGMPSSTGRHKAFSTCGSHLAVVSLCYSPLMVMYVSPGLGHSTGMQKIETLFYAMVTPLFNPLIYSLQNKEIKAALRKVLGSSNII", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSSVATIKRNIIPPHLEVKGGRPLSGILKVSGAKNSSLALMAAALLTKEKLLIQNVPELTDIEVMSEILRNLGAKLTKTNNSIEINSESIHNVELPYELVHSLRASFFCVGPLLTRLGEAKIPLPGGCNIGARPVDEHINGLKALGAEVEVINDVVKAKVSTKDKRLLGANITLKYPSVGATETILMASCLASGKTTISNPAREPEIQDLAKMLNSMGAKVFGAGTKRITILGVESLSGTSHCVIPDRIEAGTFLIAAAITRSPLIIGPVIPNHLSAVISKLKECGCSISQHGNHHLKIIPIEISGVDITTSPFPGFPTDLQAPFMSLMATAKGSSKIKERVFENRMQHVLELNKMGACIYLENNTAYIKGVKELVGSNVEGGDLRSSAAIILACLSAKGNSIFTGLEHLDRGYEKLEEKLTNAGSIISRKFDQITSHSSFSNKIISEDNIDTQKNAA", "text": "FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily."}
{"protein": "MIEYRIEEAVAKYREFYEFKPVRESAGIEDVKSAIEHTNLKPFATPDDIKKLCLEARENRFHGVCVNPCYVKLAREELEGTDVKVVTVVGFPLGANETRTKAHEAIFAVESGADEIDMVINVGMLKAKEWEYVYEDIRSVVESVKGKVVKVIIETCYLDTEEKIAACVISKLAGAHFVKTSTGFGTGGATAEDVHLMKWIVGDEMGVKASGGIRTFEDAVKMIMYGADRIGTSSGVKIVQGGEERYGG", "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": "QTAPVPKAISK", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTLSLNTPPGVHCQPLKHQRIPLLQLQLKSQPKSQLKSQPNKVLALKLLPPTLVPLLRLCQLPVLCWLVLPLYCCNLLNLFFNIFLEKWLSTFPSIQLPQNRFISINKIFW", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MMLEHVLVLSAYLFSIGIYGLITSRNMVRALMCLELILNAVNLNFVTFSDFFDSRQLKGNIFSIFVIAIAAAEAAIGPAIVSAIYRNRKSIHINQSNLLNK", "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": "MIKYSNLVIPKTKSILKSGCNNNIGYGDRYFFNKLFGSNDASDTHNQPTTKIVTKEMTKELKYPVNQVYSVIIKVEDYKEFLPFCLNSTILKREKDKNHFEAELEVGQGTIKESYVSKVVYKENKFIESTATDTPLFHKLINTWSFKQGQTPNTTIAHCKLIYQFKSPFYATLMENFFASSLDVMINSFDKRCDELYGSSNSFKK", "text": "FUNCTION: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ10 family."}
{"protein": "MAKGQSLQDPYLNALRRERIPVSIYLVNGIKLQGQIESFDQFVILLKNTVNQMVYKHAISTVVPARSVSHHNNSNNSNQQNYQQEQQTDSNVEKAE", "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": "SGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQRDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMY", "text": "FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family."}
{"protein": "MRTHYCGDLRASDIDKTVTLFGWVDRYRDHGGVIFADLRDRTGRVQIVSDPQRTPESYQAAANLRNEYVIKVEGRVSKRPKESLNPKIPTGEVEIYADSIEILNGVNKQLPFVISSEDAELVREEVRLKYRYLDLRRDRMRKNLQLRHQVVQAMRRYLEDQQNFMEVETPILTRSTPEGARDYLVPSRTNPGKWYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDNRADRQPEFTQLDMEMSFMSFDEILDLNEGLIAHVFKTVKNIDIPRPFPRLTYAEAMEKYGIDRPDTRFGLELVDVSEIVKDSGFKVFSGAVKSGGIVKVLPIPEATNIISNVQIKPGGELFKEATEAGAKGIAYIRIKDNNELDTIAAIKDNLTDEQKQELIEKTGAKPGHLLLFGAGDTDTVNKSLARLRLVVGEKLGLIDEDKINLLWVTDFPMFEWNAEEKRLEALHHPFTAPKPEDINDLPHARALAYDMIFNGIELGGGSLRIYQRDIQEKVFSTIGLSMEEAYNKFGFLLEAFEYGTPPHGGIAYGLDRFVMLLAKEESIRDVIAFPKTQQASCLLTEAPSTVEPKQLKELHIASTFKPKS", "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": "MKNMDEERKYGLYSLIIGLLCVIGIVMLNGLICYVLYIIAVPSLLYGIGAFIIPKTRRKDAGKLPFRGY", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTQDASPILTSLLDTDAYKLHMQQAVFHHYRHITVAAEFRCRSDELLGVYADEIRHQVTLMGQLALTSDEFIYLSSLPFFQDDYLHWLRDFRFKPEQVSVAVHDGKLDIRIAGLWCEVIMWEVPLLAVISEIVHRRRSTQVTTDQAVQQLRTKLEQFNALSADIDITHFKLMDFGTRRRFSREIQHTVVSTLKDEFPYLVGTSNYDLARTLALAPVGTQAHEWFQAHQQISPTLANSQRVALQVWLDEYPNQLGIALTDCITMDAFLRDFDLAFANRYQGLRHDSGDPIEWGEKAIAHYEKLGIDPMKKVLVFSDNLDLEKALFLYRHFYQRIKLVFGIGTRLTCDIPDVKPLNIVIKLVECNDKPVAKLSDSPGKTICQDPAFVDQLRKAFALPLVKKAS", "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": "MNSTSNLIEQVIEAWQNMQAKTPLVQCITNSVAANYTANVLLASGASPAMIDNPYEAESFTKISSALSINLGTPTSEQMQAMQISAKTAQLNNVPWVLDPVGYGPILAWRSQMTDELLQFKPSVIRGNASEISTLAGNQVQSKGVDSTLSSDQAYQQAFSLLTHASCIAISGESDYILSNEVDAVIQVNGGSPLQPKITATGCALGALIAAYSAVTTPTIAALSAHIHFAIAGKLAANQAQTMGSFSSIFMDYIHMLDANLIEQYADVKLLNKQA", "text": "FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ). SIMILARITY: Belongs to the Thz kinase family."}
{"protein": "MIVVTGGAGFIGSNLVKQLNAQGRTDVVVIDDLTDGTKFVNLVDLTIADYMDKDEFQARIVSGDEFEEWDGGIEVIFHEGACSATTEWNGKFIMEVNYEYSKDLFHYCIEREIPFIYASSAATYGGRNDNFIEDPKFEQPLNVYGYSKQLFDQYVRRWMPEINSQVVGLKYFNVYGPREQHKGSMASVAFHLNTQVKKGENPKLFEGCDGFPNGGQMRDFIYVDDVCKVNLWFWLNPQHSGIFNCGTGRAEPFQNVAEAVIKHHQKGAIEYIPFPDHLKGRYQSFTQADMTKLRGVGYDAEFKTVAEGVADYMAWLNR", "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": "MTIIYFILAALALGILVLIHELGHLVVAKAVGMAVESFSIGFGPALFKKRIGGIEYRIGCIPFGGYVRIRGMERTKEKGEKGKIDSVYDIPQGFFSKSPWKRILVLVAGPLANILLAVLAFSILYMNGGRSKNYSDCSKVVGWVHPVLQAEGLLPGDEILTCNGKPYVGDKDMLTTSLLEGHLNLEIKRPGYLTVPSKEFAIDVEFDPTKFGVPCSGASYLLYGNQVPLTKNSPMENSELRPNDRFVWMDGTLLFSMAQISQILNESYAFVKVARNDKIFFSRQPRVLASVLHYTPYLRNELIDTQYEAGLKGKWSSLYTLPYVINSYGYIEGELTAIDPESPLPQPQERLQLGDRILAIDGTPVSGSVDILRLVQNHRVSIIVQQMSPQELEEVNSRDADKRFIASYHSEDLLQILNHLGESHPVEVAGPYRLLDPVQPRPWIDVYSSESLDKQLEVAKKIKNKDKQRYYLERLDAEKQKPSLGISLKDLKVRYNPSPVVMLSNITKESLITLKALVTGHLSPQWLSGPVGIVQVLHTGWSVGFSEVLFWIGLISMNLAVLNLLPIPVLDGGYILLCLWEIVTRRRLNMKIVERILVPFTFLLIIFFIFLTFQDLFRFFG", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
{"protein": "MKDRYILAFETSCDETSVAVLKNETELLSNVIASQIESHKRFGGVVPEVASRHHVEVITVCIEEALAEAGISEEQVTAVAVTYGPGLVGALLVGLAAAKSFAWAHDIPLIPVNHMAGHLMAAQSVEPLEFPLLALLVSGGHTELVYVSQAGDYKIVGETRDDAVGEAYDKVGRVMGLTYPAGREIDLLAHEGQDIYDFPRAMIKEDNLEFSFSGLKSAFINLHHNAQQKGEVLSNQDLSASFQAAVMDILMAKTKKALEKYPVKTLVVAGGVAANQGLRERLAAEIQDVKVIIPPLRLCGDNAGMIAYASVSEWNKENFASLDLNAKPSLAFETME", "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": "MFNDIPVFDYEDIQLIPNKCIITSRSQADTSVTLGKYQFKLPVIPANMQTIIDETIAEQLAKEGYFYIMHRFDEDSRKPFIKRMHEQGLIASISVGVKACEYEFVTSLKEDAPEFITIDIAHGHANSVIDMIKHIKTELPETFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKVKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMVMIGSLFAGHFESPGKTVEVDGETFKEYYGSASEYQKGEHKNVEGKKILLPTKGHLSDTLTEMQQDLQSSISYAGGKDLDSLRHVDYVIVKNSIWNGDSI", "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": "MAGLSLQHPWAFAFGLLGNLISFTTYLAPIPTFYRIYKSKSTEGFQSVPYVVALFSAMLWIFYALIKSNEALLITINAAGCVIETIYIVMYLAYAPKKAKVFTTKILLLLNVGVFGVILLLTLLLSHGEQRVVSLGWVCVAFSVSVFVAPLSIIKRVIQSRSVEYMPFSLSLTLTLSAVVWFLYGLLIKDKYVALPNILGFTFGVVQMGLYVFYMNATPVAGEGKEGKGKLAAAEELPVVVNVGKLAAATPDRSTGAVHVHPVPRSCAAEAAAAEPEVLVDIPPPPPPRAVEVAAV", "text": "FUNCTION: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. FUNCTION: Confers blight susceptibility (PubMed:25988582). Confers TAL effector-mediated susceptibility to Xanthomonas oryzae pv. oryzae (PubMed:23879865). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SWEET sugar transporter family."}
{"protein": "MILKEEHPHQSIETAANAARQAQVRWRMAHLKALSRTRTPAHGNCCGRVVSKNHFFKHSRAFLWFLLCNLVMNADAFAHSQLLINVQNQGGEVIQESITSNIGEDLITLEFQKTDGTLITQVIDFRNEVQILKALVLGEEERGQSQYQVMCFATKFNKGDFISSAAMAKLRQKNPHTIRTPEEDKGRETFTMSSWVQLNRSLPITRHLQGLCAEAMDATYVRDVDLKAWAELPGSSISSLEAATEKFPDTLSTRCNEVSSLWAPCLCNLETCIGWYPCGLKYCKGKGVAGADSSGAQQQAQPTNYRCGIKTCRKCTQFTYYVRQKQQCLWDEXRRGELQLMQMRCARRRNGSEFGDDASATCPGGETRAATTTATITGGGAGGSGKDTTAATTTTTNKLRQLLLLVQQQMPFALWSFPVHHISQSHHQSQSQHKPSRQQKQHQHHSQVAPTSHHQSSSSTPPTPSTSSSPPSSSSSSSSSAMAAIVA", "text": "FUNCTION: Vital for proper neuronal development and hatching. SIMILARITY: Belongs to the OAF family."}
{"protein": "MTSANKSNIPALLALAVSAFAIGTTEFISVGLLPLIADDLDIPVTTAGLTVSLYALGVTFGAPILTSLTSSMSRKTLLLWIMFIFIAGNTMAATASSIGILLAARVISAFSHGVFMSIGSTIAADIVPEDKRASAISIMFTGLTVATVTGVPFGTFIGQQFGWRFAFMVIIAVGIIAFITNGILVPSKLRKGTKTTMRDQLKLVTNSRLLLLFVITALGYGGTFVVFTYLSPLLQEVTGFKAGTVAVILLGYGIAIAIGNMIGGKLSNRNPIAALFYMFIVQAIVLFVLTFTAPYQAAGLITILCMGLLAFMNVPGLQVYVVMLAERFVPSAVDVASAMNIAAFNAGIALGSYLGGVITDSIGLIHTAWIGGLMVVGAVILTGWSRLMEKRDRQEA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MSHKILLVNGPNLNLLGRREPSVYGHQTLADIVAELNQQAKLAEVELEHIQSNAEFELINAIHATDAQMIIINPAAFTHTSVALRDALLGVAIPFFEVHLSNVHAREAFRHHSYFSDKAIGVICGFGSQGYEFALAAAIKRLNQPL", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
{"protein": "MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKNYDETLAVVRHWDHIEVRAKDENQRPAIRDALTRIPGIHHILEVEDVPFTSLHDIFEQTLPLWREALEGKTFCVRVKRRGKHEFTSIEVERYVGGGLNQHIETARVKLTDPDVTVNLEIENDRLLLVKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIIDLAREIGTEDFARTMPEYCGVISKSPTVKAVKAKIEAEEEHFDFSILDKVVEEASNIDIREIAQQTEETVVEVETVTGFGANDAILDIRSIDEQEDKPLKVEGVEVVSLPFYKLSTKFGDLDQSKTWLLWCERGVMSRLQALYLREQGFSNVKVYRP", "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": "MRTDSGVWLTVVAHMIVGVDEAGRGPLAGPVVAAAVLLCEGGIAGLDDSKKLSARRRGALESAIRAQCRWGIGEASVEEIDRINILQATFLAMTRAVEALGFEPAEVLVDGNRLPRWRYQARAIVGGDALHPCISAASILAKQHRDRLMIAAAQDYPAFGWESNMGYGTAQHLAALRRHGPTPHHRTSFAPVAQLQLV", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVNDGIIRIHGLAEVMQGEMIALPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGEPIDGKGPVEHDGFSAVEMIAPGVIDRQSVDQPVQTGYKSVDAMIPIGRGQRELVIGDRQTGKTALAIDAIINQRDSGIKCVYVAVGQKASTIANVVRKLEEHGALANTIVVVATASESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYVEKFTNGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESSLFNAGIRPAVNPGISVSRVGGAAQTKIVKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLSLFSAERGYLEDIEIAKVIDFESALLAYANREHADLLKEIDQSGGYNEEIEAKLKALLDSFKATQSW", "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": "MSKKDYYDLLEVGRNASIDEIKKAYKKLALRYHPDRNPGNQEAEEKFKEVTAAYEVLSDSEKRAGYDRYGHEGASGGFQGFSSAGDFSDIFNDFFGGGFGGGASRSRAKRSTTGVSGADLRYDLEITLEDAFKGIQAPIHYVTNVKCDTCQGTGGEGAIKPVQCHTCQGSGRIRTQQGFFTIERTCTTCYGEGEIIQNKCKKCGGSGRRRDEVNISVSIPKGIEEGAKVRISGKGEAGTKGGKSGDLYVYVKIIFHKIFARNKADLHCKVPIRMTLAVLGGEIDIQSIDGAKIKVKVPEGTQTGTKLRCREKGMPYMNSHARGDLYVQVIVETLNPKNLTKKQIELLKALEEEENASVQQQSEGFFSKVKKK", "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": "MLFALPALNDNYIWLYQRENLPLIIVDLPETDKLFAWLDKQNATIEAVLLTHEHEDHTQGVSAFKKRYPTVPIYGPQECEKKGATQVVNEGKILTAHYQIDVIPTGGHTKQHVSFLVDNHLFCGDALFSAGCGRVFTGNYAQMFDGLQRLNTLPDETIVCPAHEYTLGNLAFAETVLVEKSAVEKQRIFVETQRAENKPSLPTTLKLEREINPFLQAKTLEEFTALRKAKDIF", "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": "MASIPATVAAVAQANMVAPFTGLKANAAFPVTKKVNDFSTLPSNGGRVQCMKVWPPLGKKKYXTLSYLPNLTEAQLAKEVDYLLRNKWVPCLEFELEHGFVYRENARSPGYYDGRYWTMWKLPMFGCTDSVQVMKELQECKKEYPQAWIRIIGFDNVRQVQCISFIASKPDXF", "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": "MAASDTERDGLAPEKTSPDRDKKKEQSDVSVSPRASKHHYSRSRSRSRERKRKSDNEGRKHRSRSRSKEARRHESKDKSSKKHKSEEHNDKEHSSDKGRERLNSSENGEDRHKRKERKSSRGRSHSRSRSRERRHRSRSRERKKSRSRSRERKKSRSRSRERKKSRSRSRERKRRIRSRSRSRSRHRHRTRSRSRTRSRSRDRKKRIEKPRRFSRSLSRTPSPPPFRGRNTAMDAQEALARRLERAKKLQEQREKEMVEKQKQQEIAAAAATGGSVLNVAALLASGTQVTPQIAMAAQMAALQAKALAETGIAVPSYYNPAAVNPMKFAEQEKKKRKMLWQGKKEGDKSQSAEIWEKLNFGNKDQNVKFRKLMGIKSEDEAGCSSVDEESYKTLKQQEEVFRNLDAQYEMARSQTHTQRGMGLGFTSSMRGMDAV", "text": "SIMILARITY: Belongs to the RSRC2 family."}
{"protein": "MCVCQTMEVGQYGKNASRAGDRGVLLEPFIHQVGGHSSMMRYDDHTVCKPLISREQRFYESLPPEMKEFTPEYKGVVSVCFEGDSDGYINLVAYPYVESETVEQDDTPEREQPRRKHSRRSLHRSGSGSDHKEEKASLSFETSESSQETKSPKVELHSHSDVPFQMLDSNSGLSSEKISYNPWSLRCHKQQLSRMRSESKDRKLYKFLLLENVVHHFKYPCVLDLKMGTRQHGDDASAEKAARQMRKCEQSTSASLGVRVCGMQVYQLDTGHYLCRNKYYGRGLSIEGFRNALYQYLHNGLDLRRDLFEPILSKLRGLKAVLERQASYRFYSSSLLVIYDGKECRSELRLKHVDMGLPEVPPLCGPSTSPSNTSLEAGPSSPPKVDVRMIDFAHSTFKGFRDDPTVHDGPDRGYVFGLENLISIMEQMRDENQ", "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 Nucleus. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
{"protein": "MTLDIFDQFTSPTMFGLPLAWLAMLAPSLMLVSQTPKFIKSRYHTLLTPILTSIAKQLFLPMNQQGHKWALICMASMMFILMINLLGLLPYTYTPTTQLSMNMGLAVPLWLATVLIGLQKKPTEALAHLLPEGTPAALIPMLIIIETISLFIRPIALGVRLTANLTAGHLLMQLVSMTTFVMIPVISISIITSLLLLLLTILELAVAVIQAYVFILLLTLYLQENVYVPPSSCMPHG", "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": "MDVVFALGGSVLMPKEGASTENIQNYAQAFKKLKEMGHRVSVVVGGGNTARQYISVAREFTNESFCDEIGILATRMNSMLLISALGKDAVKQVPENFKDAELILNMDKILVMGGTHPAHTTDAVSATLAEFIDADLLVIATNVDGVYTKDPRCNEDAVKLDKINTKELLEITGSNSMSAGSSGVVDPLASKIIDRAKLKTIVIKGIPEEILASISGNHNGTTITP", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MNNRVHQGHLARKRFGQNFLNDQFVIDSIVSAINPQKGQAMVEIGPGLAALTEPVGERLDKLTVIELDRDLAARLQTHPFLGPKLTIYQQDAMTFNFGELAEKMGQPLRVFGNLPYNISTPLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPNSKAYGRLSVMAQYYCNVIPVLEVPPSAFTPPPKVDSAVVRLVPHATMPHPVKDVRVLSRITTEAFNQRRKTIRNSLGNLFSVEVLTGMGIDPAMRAENISVAQYCQMANYLAENALLQES", "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": "MMTSTFGTTVKVSIFGESHAPKIGCTIEGLPAGFTVDLHELKTFLQRRSPSHPWDTPRKEIDNPKFVSGISAKGILDGFPLTAELPNNNVRQKDYTATKLVPRPGHADFSAWAKWGNSYKQTGGGHFSARLTAPLCIAGGIALQILHAQGITIAAHVLKIKNINDTPFKLIDNSVEANKLLALQMNQLLQAAPQELPFLDAQTGEKTRALLTQLRSEKNTVGGIIECVATGVPAGIGCPHFQGLENTISAAVFGVPAVKAIEFGSGMNVANLLGSENNDAYEVRDGSVVPTTNHAGGILGGISTGAPIWFRCALKPISSIGLSQHSVNLQTMESEQLVVQGRHDVTAVLRAVPCVESAFALALLDTLYSWPSEQNGYHND", "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": "MQEILIPLKEKSYKVFLGELPEIELKQKALIISDSIVAGLHLSYLLKRLKALEVRVCVIESGEKYKNLNSLECILNSAFEMQLNRHSLMIALGGGVISDMVGFASSIYFRGIDFINIPTTLLAQVDASVGGKTGINTPYGKNLIGSFYQPKAVYIDLAFLKTLEKREFQAGVAEIIKMAVCFDKNLVEILETRDLKDCLEEVVFQSVSIKAQVVTQDEKEQNIRAGLNYGHTFGHAIEKETDYERFLHGEAIAIGMHMANDLALSLGMLTLKEYERIEDLLKKFDLIFNYKITDIQKFYERLFLDKKSEDKTIKFILPKGVGAFEIASHIPKETIIKVLEKWH", "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": "MSTLKKPDLSDPKLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACVVGLAVLDPAMLGDKANPFATPLEILPEWYLYPVFQILRVVPNKLLGIALQTLIPLGLMILPFIENVNKFSNPFRRPIAMSVFLFGTFLTIYLGIGACLPIDKSLTLGLF", "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": "MASGSTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKASARADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGNDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV", "text": "FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family."}
{"protein": "MKQIALYGKGGIGKSTTAANLSAALAGEGLDILQIGCDPKHDSTRMLMHGTWIPTVLDLIRERGDEKITVDDVVYRGFRGVRCVEAGGPEPGIGCAGRGIIATFQLLERLNALKGDVIVYDVLGDVVCGGFAMPMREGYAQEIYLVTSGELMSIYAANNIAKAIARLSRRVRSRCTLGGVICNAKNIEGERELVDEFARRIGSRLIAYIPRSRIVQVAELQKQTVVEYAPESDQAAVYQELARTVYGNETTSIPTPLEMDELESFALEFVQV", "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": "MKPEETGGSVYQPLDESRHVQRGVLQALGAIQILNGILILALGIFLVCLQHVSHHFRHFFFFTFYTGYPLWGAVFFISSGSLTVAAGRNPTRMLMQNSFGINIASTTIAFVGTVFLSVHLAFNTQAFKGCQSSPSPDVCISLGSSSDGLVSLMLILTLLELSVTISISAMWCLGNVCGLREAITSPPNSVESGILPEGSDSENLNTQPQASEE", "text": "FUNCTION: Hematopoietic modulator for the G1-S cell cycle transition. Modulates the level of phosphorylation of cyclin-dependent kinase 2 (CDK2) through its direct binding to cyclin-dependent kinase inhibitor 3 (CDKN3/KAP) (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MS4A family."}
{"protein": "MFIYYCKECFVMNKQQSKVRYSIRKVSIGILSISIGMFLALGMSNKAYADEIDKSKDFTRGYEQNVFAKSELNANKNTTKDKIKNEAVVKTSDTSLKLDNKSAISNGNEINQDMKISNTPKNSNQGNNLVVNNNEPTKEIKIANLEAQNSNQKKVNKGTNNYFGYYSFREAPKTQIYTVKKGDTLSAIALKYKTTVSNIQNTNNIANPNLIFIGQKLKVPMTPLVEPKPKTVPSNNKSNSNNSTLNYLKTLENRGWDFDGSYGWQCFDLVNVYWNHLYGHGLKGYGAKDIPYANNFNSEAKIYHNTPTFKAEPGDLVVFSGRFGGGYGHTAIVLNGDYDGKLMKFQSLDQNWNNGGWRKAEVAHKVVHNYENDMIFIRPFKKA", "text": "FUNCTION: Probably involved in peptidoglycan hydrolysis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MLVHTYSAMERPDGLGAAAGGTRLSSLPQAAYGPAPPLCHTPAASATADYHPPYFPPPYPQAPLPYGQGPDATAAFPHLAADPYGGLAPLAQPQPPQAAWAAPRAAARAHDEPPGLLAPPARALGLDPRRDYAAAVPRLLHSLADGAHGLADAPLGLPGLAEPPGLEELQAIDDPGMSLLDQSVIKKVPIPSKAGSLSTLALSKDSLVGGISNPSEVFCSVPGRLSLLSSTSKYKVTVGEVQRRLSPPECLNASLLGGVLRRAKSKNGGRCLRERLEKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAAAEYLCRQHADPGELHSRKSMLLAAKQICKEFADLMAQDRSPLGNSRPALILEPGVQSCLTHFSLITHGFGGPAICAALTAFQNYLLESLKGLEKMFLSGAGGGHGESKASEKDTKHRK", "text": "FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-epsilon may play a role in the development of the CNS and in cartilage differentiation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP-2 family."}
{"protein": "MVKQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPRGHHSFLTLPEIRLVGRAFADLGTEKIRLTGGEPTMRRDFTDIISVIRENKLIKTLAVTTNGYRMERDIAKWKEAGLTAVNVSMDSLDPRQFHAITGQDKFFQVMRGIDAAFAVGFSKVKVNVVLMKNVNDISLSAFLHWIKDRPIQLRFIELMETGDGGEMFRQYHISGEIIRERLLLDGWHLLQRSRSDGPAQVFSHPDYQGEVGLIMPYEKNFCQSCNRLRVSSIGHLHLCLFGEQGIPLRDLLASEKQLDDLKLRIQDGLRHKRETHFLHQGDSGITPNLSVIGG", "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": "MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRSNPCAYTPPSLKAVQRIAESHLQSISNLGENQASEEEDELGELRELGYPREEEEEEEEEDEEEEEDSQAEVLKGSRGSAGQKTTYGQGLEGPWERPPPLDGPQRDGSSEDQVEDPALNEPGEEPQRPAHPEPGT", "text": "FUNCTION: Inhibitor of protein-phosphatase 1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family."}
{"protein": "MALVSSAPKSCLHKSLIRSTHHELKPLRRTIPTLGMCRRGKSFTPSVSMSLTTAVSDDGLQRRIGDYHSNLWDDDFIQSLSTPYGEPSYRERAEKLIGEVKEMFNSMPSEDGESMSPLNDLIERLWMVDSVERLGIDRHFKKEIKSALDYVYSYWNEKGIGCGRDSVFPDVNSTASGFRTLRLHGYSVSSEVLKVFQDQNGQFAFSPSTKERDIRTVLNLYRASFIAFPGEKVMEEAEIFSSRYLKEAVQKIPVSSLSQEIDYTLEYGWHTNMPRLETRNYLDVFGHPTSPWLKKKRTQYLDSEKLLELAKLEFNIFHSLQQKELQYLSRWWIHSGLPELTFGRHRHVEYYTLSSCIATEPKHSAFRLGFAKTCHLITVLDDIYDTFGTMDEIELFNEAVRRWNPSEKERLPEYMKEIYMALYEALTDMAREAEKTQGRDTLNYARKAWEVYLDSYTQEAKWIASGYLPTFEEYLENAKVSSGHRAAALTPLLTLDVPLPDDVLKGIDFPSRFNDLASSFLRLRGDTRCYKADRDRGEEASSISCYMKDNPGLTEEDALNHINAMINDIIKELNWELLKPDSNIPMTARKHAYEITRAFHQLYKYRDGFSVATQETKSLVRRTVLEPVPL", "text": "FUNCTION: Converts geranyl diphosphate to four products with (-)-(4S)- beta-phellandrene (52%) as the major olefin, and lesser amounts of (-)- (1S,5S)-beta-pinene (34%), (-)-1S,5S-alpha-pinene (8.5%), and (-)-(4S)- limonene (6%). Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in monoterpene (C10) olefins biosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
{"protein": "MIKSELIARLANENPHLTQKDVERVVGVILERMIGALEDGGRVELRGFGALSVRSRPARAGRNPRTGETVDVRAKHVPFFKSGKELRGRLNADE", "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": "MNTTHVPEPHRTEQHTENQRHWRKILDIAPIVSIAFPAAMYFIFDEDSFEGSLFLRFVTVLLPFSYSAVQYAVLLHTNRMPHNKPEGILQSMLYYTLNLLLLAFTIISILSIIAFTLDEWENNDDSLLYSITLPSFFIPLTYLLSVSCRLVPGQIGFTDTGINVLIDILILLFPRTALVSKESKHRLLYAVLFLLPILIRLLKEKYCPSGKSSLPTASWRVAVLALILILVFFAYTFMMCRSMVILNNHFGLLNKLKRVSAPSRSDK", "text": "SIMILARITY: Belongs to the UPF0328 family."}
{"protein": "MDGNSTHPAPNLKTTMAWSRISNQLGHWNDRKVIAIPLSDFLNTHPDIQSGIIAEFKKATGEEGMFARDPESLGIMLLGPVKLFKPDSVVVDGNLFWDPKGIHASAPKEQQKKAKIPRPPNAYILYRKDHHREIREQNPGLHNNEISVIVGNMWRDEQPHIREKYFNMSNEIKTRLLLENPDYRYNPRRSQDIRRRVSPYLKIKLLNYDVNGNLLWGTVNAEDAALIRTHFHGVVRVEEMDDGCRIVCRPVAGSRKLRAAVVDTWMPRYTVDTTPVTEDDDAQAFNFNDPLGGAYFPLNEHLWITVNQNPPFNAPPPNPNPHLDFVHPDGMEAVVHNVQNMIAQVQEANEAAALTLPPPPPLRLLSLRLWLMIPLTQLSFPL", "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 a-specific genes like mating factor mfa-1. Required for mating as an a-cell, blocking of heterokaryon formation (vegetative incompatibility) and for perithecium induction. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSKTGGSDSKNTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREESKSSLVKSRDGIPTPKEIRKVLDDYVIGQDHAKKVLSVAVHNHYKRLNHATKHGDVELAKSNILLIGPTGSGKTLLAQTLARILDVPFTMADATTLTEAGYVGEDVENIILKLLQAADYNVERAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLDKIISSRSKGSTSIGFQAKVAPPEDRRPGEVFREVEPEDLLKYGLIPEFIGRLPVLATLGDLDEEALKKILSEPKNALVKQYQRLFEMENVDLTIHEEALGAIARKAIERKTGARGLRSIMESILLDTMFDLPGLEGVEEVVISREVVEQSARPLYIYADRVGDAGASA", "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": "MARIAGVDIPRDKRVEVALTYIYGIGLTRAKTILTKSDVNPDIRVKDLEDGDVQKLRTALEAFTIEGDLRRQEGMALKRLQDIGCLRGRRHRMSLPVRGQRTRTNARTRRGARKTVAGKKK", "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": "MPRRRVVGQRKILPDPKFHSELLAKFINVIMQDGKKSTAEKIIYKALDVVAEKKSENHLSILEAALDNVRPSVEVKSRRVGGSTYQVPCEVRPVRRNALAMRWLVEAARKRGEKSMALRLAGEMLDASENKGTAVKKREDVHRMAEANKAFAHYRW", "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": "MSSAKEIKKSILAPVLDNNPIALQVLGVCSALAVTTKLETAFVMTLAVMFVTAFSNLFVSLIRHHIPNSVRIIVQMAIIASLVIVVDQILRAYLYDISKQLSVFVGLIITNCIVMGRAEAFAMKSAPIPSFIDGIGNGLGYGFVLITVGFFRELLGSGKLFGMEVLPLVKDGGWYQPNGLMLLAPSAFFLIGFMIWAIRTFKPEQLEAKE", "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": "MPFSHTKIVGPAGRYGARYGMGLRRKITAIEIKQRGKHRCPSCRSLVRLKRLAFGIWQCPKCGFTFAGGAWVPQTVMGKTLTPEELKEVEIQKARWRETGK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family."}
{"protein": "MPVITLPDGSQRHYDHAVSPLDVALDIGPGLAKACIAGRVDGELIDASDKIDTDAQLAIITAKDDAGLEIIRHSCAHLLGHAIKQLWPDTKMAIGPVIDNGFYYDVDIDRTLTQEDIELLEKRMHELADTDYDVIKKKVSWQEARDAFAARGETYKIAILDENISHDDRPGLYHHEEYIDMCRGPHVPNMRFCHHFKLQKTSGAYWRGDSKNKMLQRIYGTAWADKKQLASYLQRLEEASKRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEAFVRMKLKSYQYQEVKGPFMMDRVMWEKTGHWDNYKEAMFTTSSENREYCIKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEEQVRDEVNSCIKMVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADLAAALTENNIEFAYQPGEGAFYGPKIEFTLHDCLDRAWQCGTVQLDFSLPGRLSASYVGESNERQVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQVVIINITDSQSDYVNELTQKLQEAGIRVKADLRNEKIGFKIREHTLRRVPYMLVCGDKEVEAGKVAVRTRRGKDLGSLDVSEVISKLQQEIRSRSLHQLEV", "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": "MILIIDNYDSFTYNLVQYVGVLTDVAVVKNDDDSLGNMAEKADALIFSPGPGWPADAGKMETLIQQFAGQKPILGICLGFQAIVEVFGGKLRLAHQVMHGKNSQVRQTSGNLIFNHLPSKFLVMRYHSIVMDEAVALPDFAITAVATDDGEIMAIENEKEQIYGLQFHPESIGTLDGMTMIENFVNQVNENKESSNEK", "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": "MTVVSPIRVLVVDDSAFARKVLRQVLSSAEGLEVVGVARDGLDALEKVAELSPDVLTLDLVMPGLDGLGVLRALASSAAAPRVVVVSSAGEESELAVAALQAGAVELVNKPTALATERLYELGGELVAKVRTAAGAVARAPPEPAPSPEATSAPVARAAAKSLVVVGTSTGGPQALTRLLSELPVDFPAPLALALHIPTGYTEAVARRLNAHCALEVFEAVDGLELRPGRVVLARSGQHLKLERHGPVTLARLDRQPLRTAHHPSVDVLFESAARSWGSDVVGLVLTGMGDDGVAGARAIREAGGTVLTESESSCVVYGMPRAVKEAGLATDSAPLEGMLALLRRHVR", "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": "MDTRGVAAAMRPLVLLVAFLCTAAPALDTCPEVKVVGLEGSDKLSILRGCPGLPGAAGPKGEAGASGPKGGQGPPGAPGEPGPPGPKGDRGEKGEPGPKGESWETEQCLTGPRTCKELLTRGHILSGWHTIYLPDCQPLTVLCDMDTDGGGWTVFQRRSDGSVDFYRDWAAYKRGFGSQLGEFWLGNDHIHALTAQGTNELRVDLVDFEGNHQFAKYRSFQVADEAEKYMLVLGAFVEGNAGDSLTSHNNSLFTTKDQDNDQYASNCAVLYQGAWWYNSCHVSNLNGRYLGGSHGSFANGVNWSSGKGYNYSYKVSEMKFRAT", "text": "FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ficolin lectin family."}
{"protein": "MKNITFKEKINLSNYTTIKVGGFAEYFSKPNNTDEFINLINWASLNNQKCRIIGAGSNLLINNIFLKGLTICTKKMRSIKIESHSGIVEVEAGVMLPTMSNILAKKGLQGGEWTVGIPGTVGGSICMNAGSKQLSLANNLLSVRVIDTKTLKISEIEKKDINFQYRFSPFQQNNLMIISAKLLFEPKGNIEQLLETTQKNLKKKTDTQPYHLPSFGSVFKNPTNNYAGKLIEELGLKGFKIGGAEISTMHGNFIVNNSFANSKDILDLITVIQQKVLQKKGIFLEPEVRMIGFDYP", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
{"protein": "MAKLTKRMRVIRDKVDVTKQYDINEAVALLKELATAKFVESVDVAVNLGIDARKSDQNVRGATVLPHGTGRSVRVAVFTQGANAEAAKAAGAEFVGMEDLAEQIKKGEMGFDVVIASPDAMRVVGQLGQVLGPRGLMPNPKVGTVTPNVAEAVNNAKAGQVRYRNDKNGIIHTTIGKVDFDSNKLKENLEALLVALKKAKPSQAKGVYIKKVSLSTTMGAGVAVDQSGLNAAAN", "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": "MKNIKIEICAGSFEDAVLAEKAGASRIELNSSLFLGGLTPSLGTLKLVKKETHLEVMAMVRPRAAGFFYSSYEYKTMLEDAKLFIDNGADGLVFGFLKKDGTIDAKRCEALIKIAESRDKVFHRAIDVVPDPLKALDELISLGFTRVLTSGQEPTAYEGADLIAKMVKRAKGRIEILPGGGITEKNASKIIKLTGVDQIHFAALKRREEPSTKANPSIYYGGALYPPEDSIEVAGLDEMTKVIKSL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutC family."}
{"protein": "MSSLTPLLLRSLTGPARRLMVPRAQVHSKPPREQLGVLDITIGLTSCFVCCLLPAGWVLSHLESYKKRE", "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": "MKQLFRQWYDLSEIKKELTTRNWFPATSGNISIKVSHEPLTFLITASGKDKTKTTPDDFLLVDHLGVPVLETELRPSAETILHTHIYNNTNAGCVLHVHTTDNNVITNLYSDAVTLQNQEIIKALDIWEEGATINIPIIENHAHIPTLGENFRKHIQGDSGAVLIRNHGITVWGRDSFDAKKRLEAYEFLFQFHIKLLSIQGGVSNGANSYS", "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": "MEGKVIGIHGPVLDLQFTDYTPFERELIKVRDILVECRALLGEGKVRTVALGPTEGIRRGDKATALGKPMTIKVGEQLIGRVLSGIGAPLDQKEEPEGEERSVFNVPPQVTAVLPVSTVLETGIKALDLLAPFPRGGKIGLFGGAGVGKTVLVMELIHNVAIKHRGYSVFAGVGERTREGQELWEEMRESGVMDHLVMIFGQMNEPPGVRAITPYAAATVAEYLRSQYGGEILLFMDNIFRYAQAGMEVSTLLGRMPSAMGYQPTLFSEVAQIEERINSLAEGAITSVQAVYVPADDITDPAPATIFGHLDSSVVLSRALTEVGIYPAVDPLQSSSKMLDPEVVGYNHVQVAGRVKEFLQRYEELKDIIALLGMEELSPEDREVVLRARKIQMFLSQPFFVAEAFSGAPGKYVPLERTVEGFKAIIDGKLDHVPESALYMIGDISEAGVDV", "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": "MAGPTLLKESGPREVFCGLTSIVWLHRRMPDAFFLVVGSRTCAHLIQSAAGVMIFAEPRFGTAILSERDLAGLADAHEELDRVARELLQRRPEIRTLFLVGSCPSEVIKLDLARAAERLNDELQGRVRVVNYSGSGIETTFTQGEDGALAALVPLLPSSAERQLLLVGTLADAVEDRLIHLFGRLGIDRVRSLPPRQSTALPPVGPGTTVLLTQPFLTDTARLLRNRGATVLTAPFPLGAEGSRRWMEAAAQAFEVAPSHVATVLDPLMERARIALEPHREVLAGKRIFLLPESQLELPLARFLQRECGMELVEVGTPYLNREQMAEELALLPEGTPVMEGQHVELQLDRVRDSAPDLVVCGMGLANPLEAEGIATKWSIELVFSPIHGIDQAGDLAELFSRPLRRRQLIHPGLHPTQPDQPVHA", "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": "MQAIKCVVVGDGAVGKTCLLLSYTTNAFPGEYILTVFDTYSTNVMVDGRPINLSLWDTAGQDDYDQFRHLSFPQTDVFLVCFALNNPASFENVRAKWYPEVSHHCPNTPIILVGTKADLREDRDTIERLRERRLQPVSHTQGYVMAKEIKAVKYLECSALTQIGLKQVFDEAIRTGLTPPQTPQTRAKKSNCTVL", "text": "FUNCTION: During gonad morphogenesis, plays a role in distal tip cell (DTC)-mediated guidance of gonad elongation (PubMed:19023419). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MNYKDTLLMPKTDFPMRGGLPNKEPQIQEQWEANNQYQKALEKNKGNQSYILHDGPPYANGNLHMGHALNKIIKDIIVRYKTMQGFYAPYVPGWDTHGLPIEQALTKKGVDRKKMSIAEFREKCKEFALEQIELQKKDFKRLGVRGDFNDPYITLKPEYEAAQIRLFGEMADKGLIYKGKKPVYWSPSSESSLAEAEIEYHDKRSASIYVAFDVKDTKGVVDQDAQFIIWTTTPWTIPSNVAITVHPDLKYGQYNVNGKKYIIAQALSEDVAEALEWDKDAIQLEKEFTGKELEYVEAQHPFLDRISLVINGNHVTTDAGTGCVHTAPGHGEDDYIVGQKYDLPVISPLDDKGVFTEEGGQFEGMFYDKANKAVTDLLTEKDALLKLNFITHSYPHDWRTKKPVIFRATPQWFASINKVRQDILDAIEETDFKVDWGKTRIYNMIRDRGEWVISRQRVWGVPLPVFYAENGDIIMTKETVNHVADLFEEHGSNIWFEREAKDLLPEGFTHPGSPNGTFTKEMDIMDVWFDSGSSHRGVLENRPELSFPADLYFEGSDQYRGWFNSSITTAVATRGQAPYKFLLSHGFVMDGEGKKMSKSLGNVIVPDQVVKQKGADIARLWVSSTDYLADVRISDEILKQTSDVYRKIRNTLRFMLGNINDFNPDTDVIPEAELLEVDRYLLNRLREFTASTIEHYDNFDYLNIYQEVQNFINVELSNFYLDYGKDILYIEEKNAHKRRSMQTVLYQILVDMTKLLAPILVHTAEEVWTHTPHVKEESVHLADMPKVVEVDQALLDKWNQFMALRDDVNRALEVARNNKVIGKSLEAKVVIGNNDNFKAAEFLQQFEDLQQLFIVSQVEVSDSVDNAEAYQHGDIRIDHAVGEKCERCWNYTEELGSVGELEHLCPRCQEVVKTLV", "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": "MRQKIFFLKRFDSELLYVQGSILKSFQRFSLTLSVSTNNSKYLDFFRTGPSQIATIRSTSFYTISETQGLNRMDM", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MSDMHSLLIAAILGVVEGLTEFLPVSSTGHMIIVGHLLGFEGDTAKTFEVVIQLGSILAVVVMFWRRLFGLIGIHFGRPLQHEGESKGRLTLIHILLGMIPAVVLGLLFHDTIKSLFNPINVMYALVVGGLLLIAAECLKPKEPRAPGLDDMTYRQAFMIGCFQCLALWPGFSRSGATISGGMLMGVSRYAASEFSFLLAVPMMMGATALDLYKSWGFLTSGDIPMFAVGFITAFVVALIAIKTFLQLIKRISFIPFAIYRFIVAAAVYVVFF", "text": "FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family. SIMILARITY: Belongs to the UppP family."}
{"protein": "MSLIEGLLQTSSTVTLLGTVLFLLVLYLRSSGSSSEGQGKEPPGPRPLPLLGNMLQLDLKKPYCTLCELSKKYGSIFTFHFGPKKVVVLAGYKTVKQALVNQAEDFGDRDITPVFYDFNQGHGILFANGDSWKEMRRFALTNLRDFGMGKKGSEEKILEEIPYLIEVFEKHEGKAFDTTQSVLYAVSNIISAIVYGSRFEYTDPLFTGMADRAKESIHLTGSASIQMYNMFPWLGPWINNLTRLKKNIADMKMEVTELVRGLKETLNPHMCRGFVDSFLVRKQTLEESGHMDSFYHDDNLVFSVGNLFSAGTDTTGTTLRWGLLLMTKYPHIQDQVQEEISGVIGSRQTLVEDRKNLPYTDAVIHETQRLANIAPMSIPHTTSRDVTFQGYFIKKDDSEWESPHTLTPSHFLDEKGGFVKRDAFMAFSAGRRVCLGEGLARMELFLFFTSLLQHFRFSPPPGVTEDDLDLTPSVEFTHNPSPHQLCAVSRV", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSNHKLIEAVTKSQLRTDLPTFRTGDTLRVHVRIVEGSRERIQVFEGVVIKRRGGGISETFTVRKISSGVGVERTFPLHTPKIEKIELKRRGKVRRAKLYYLRSLRGKAARIQEIR", "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": "MTWITPKKAIMLAAAAEGGTKLNAFDNALLKMGIGNVNLVKLSSVIPAHIEWLDELPKNIPIGMLLPTVYAHIESDEPGSTISAALGVGISEGNEGGLIYEYAGYCKREEAEDMVRKMVEEGFKVRGWKLKEFKVVSAEITVKEKPAAAVAAVIMFPY", "text": "SIMILARITY: Belongs to the PdaD family."}
{"protein": "MNFKNINKCQLDWLFSTNHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLSIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVVGGVTGVAMSNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGKISGRKYPEILGQIHFWLFFIGVNITFFPMHFLGLAGMPRRIPDFPDAMSGWNAVSSFGSYISFFSALFFFYIVYVTLVYGKKTEN", "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": "MKILIDNNIIFSYSLFKKIGKVNLINSIDINAKNISGFDALIIKSSTNVNENLLKNSNIKFIGSATSGKDHVDVDWLKKNKINFDFAPGCNSVAVAEYVFSSMLYFAYRDKFSLLKKTVGIVGFGNIGKCLNKKLSAIGVKTILCDPILEEKNNIKLKSLNEIVQNSDIITLHVPLTYSGKYPTWHLINKKILLDLKDNCILINTSRGSVIDNNSLLNILKEGKPIRVVLDVWENEPLICSKLLSLIDIGTPHIAGHSLEGKIKGTISIFNSLCNFVGKKNKKYFISSFIDPYEIEYISMKGRIDQSKIYLLSLLSNNILYDDHELRKNFNKKNCFVNLRNSYRKRREWSSLFIKSNNILFSNLLNKIGFNSKFFKEK", "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": "MYQLFRHGIFQMDAEKAHNFTIQCLKLAGNPLFKPILKSIIHAPKGFPKMVMGVNFPNPIGLAAGADKNGDAIDGFGALGFGFLELGTVTPVAQDGNAKPRQFRLIEAEGIINRNGFNNNGIDYLIENVKNARYKGVIGINIGKNKFTPLEQGKDDYIFCLNKAYNYAGYITVNISSPNTPDLRQLQYGDYFDDLLRSIKDRQTILANQYNKYVPIAVKIAPDLTESELVQIADTLVRHKMDGVIATNTTISRDTVMGMKNAEQQGGLSGKPLQHKSTEIIKRLHQELKGQIPIIGSGGIDGLQNAQEKIEAGAELLQVYSGLIYHGPKLVKELVKNIK", "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": "MNSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDFAKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIAAIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTLFAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGNPIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGLGAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILVPLTIEDAQIRQGLEIISQCFDEAKQ", "text": "FUNCTION: Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate (PubMed:15723541, PubMed:30498244). Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth (PubMed:12446648). Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:30498244). SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MIKRYTCQNGVRIVLENNPTVRSVAIGVWIGTGSRHETPEINGISHFLEHMFFKGTSTKSAREIAESFDRIGGQVNAFTSKEYTCYYAKVLDEHANYALDVLADMFFHSTFDENELKKEKNVVYEEIKMYEDAPDDIVHDLLSKATYGNHSLGYPILGTEETLASFNGDSLRQYMHDYYTPDRVVISVAGNISDSFIKDVEKWFGSYEAKGKATGLEKPEFHTEKLTRKKETEQAHLCLGFKGLEVGHERIYDLIVLNNVLGGSMSSRLFQDVREDKGLAYSVYSYHSSYEDSGMLTIYGGTGANQLQQLSETIQETLATLKRDGITSKELENSKEQMKGSLMLSLESTNSKMSRNGKNELLLGKHKTLDEIINELNAVNLERVNGLARQLFTEDYALALISPSGNMPS", "text": "SIMILARITY: Belongs to the peptidase M16 family."}
{"protein": "MGVIEFLLALAQDMILAAIPAVGFAMVFNVPVRALRWCALLGAIGHGSRMILMTSGLNIEWSTFMASMLVGTIGIQWSRWYLAHPKVFTVAAVIPMFPGISAYTAMISAVKISQLGYSEPLMITLLTNFLTASSIVGALSIGLSIPGLWLYRKRPRV", "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": "MIRIGVLGPVGSGKTTLIEFLTEYLVKKEGLSVGIITNDVISSHDALRIYQNLVLKEKLLPKENVIGIVTGGCPHTAIREDPSVNLRALETLMKRTSLDVIFIESGGDNVMSTFSPILADYTIFVLDTAAGDKYPGKGGLGIQESDLLVVNKIDLAPFVGADLEKMRRDAEKIRKDKPTVFISLKTGDGIDDLIKIIRSELELEGLIRS", "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": "MAAKEVKFGNDARVKMLAGVNILANAVKVTLGPKGRNVVLDKSFGSPVITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQSIVVEGLKAVAAGMNPMDLKRGIDKAVIAAVAELKKLSQECSDTKAIAQVGTISANSDESIGEIIATAMEKVGKEGVITVEEGQALENELEVVEGMQFDRGYLSPYFINKPETGSIELDSPFILLVDKKISNIRELLPILEGLAKTGKPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDVAILTGGTVIAEEIGLELEKATLEDLGTAKRVVITKDNTTIIDGSGEHTQITSRVAQIKQQMEDSSSDYDKEKLQERMAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRVASMIADIEVLNEDQKHGVVIALRAMEAPLRQIATNAGQEASVVANTVKNGTGNYGYNAGNDTYGDMLEMGILDPTKVTRSALQFAASIAGLMITTEAMIAEIPQESAPDMGGMGGMGGMGGMM", "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": "MLKTPLYESHIAANAKMIDFSGWSMPINYGSQIQEHNNVREDCGIFDVSHMLAVDIQGSEAEKFLRYLLANDVAKLQENKAQYGCMLNHDAGIVDDLITYKVTDEHFRIVVNAGNRESDVAWFNQNAQNFDVAITPQTDLAIVAVQGPKAVAVIKRVVTKEIAAEIEALLPFSFKFFSKWMVARTGYTGEDGFEVILPATQVKKFWDSLLENGAQPAGLGARDTLRLEAGMHLYGADMDTSTTPLERGLGWSVDLSDEHRDFIGKKAYLAKKAQGVDTKWVGVVLKTKGVLRAGQEIDFDNGEKGYITSGSFSPTLKVAIGLAYVPKQADNPVVNIRGKELEVELVKPKFVKNGKSLI", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. SIMILARITY: Belongs to the GcvT family."}
{"protein": "MASIAPSLKRAHAPLRKALTASSTIRAFATVPPTSSETTKPKRKSYFKDTTVAEFSDFLATSSPAQPLSPAEAFTLRTAEVGPEGKKRTITRLPEWLKTPIPAGNDNFKSIKKDLRGLGLHTVCEEARCPNISECWGGSDKNAATATIMLMGDTCTRGCRFCSVKTNRKPAALDPHEPENTAEALARWGLGYVVLTSVDRDDLADGGAHHFAETIRRIKQKKPSLLVEALTGDFRGDLDMVKVVAESGLDVYAHNVETVEDLTPYVRDRRATFRQSLSVLKHVKEVKGKEGIITKTSLMLGLGEQEHEVMAALEDLRKADVDVVTFGQYMRPTKRHLKVEKYVTPDEFEMWNKRALDMGFLYCASGPLVRSSYKAGEAFIENVLRKRSGEKAMARGTLAKAVALDSETRSSI", "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": "MPVYVDYETPADLAERSLEALEVARDTGTVKKGTNETTKAVERGNADLVIVAEDVSPEEIVMHLPELAEEKGIPVVFVDTQDEVGHAAGLEVGSAAAAVIDAGDADDDVEDIGEKVAELR", "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": "MNDMAVRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGTFVFRIEDTDSARDSEESYQAILDALNWLGLDYDEGPEIGGPYAPYRQSQRRDLYRDVIDRLIAAGEAYEAYSTAEEVEARHLAAGRNPKLGYDNFDRDLTDEQRAAHRAEGRNPVIRLRMPERDITWRDLVRGETTFGAGTMPDFALTRGNGEPLYTLVNPVDDALMKITHVLRGEDLLPSTPRQIALYEALIRIGVADGVPEFAHLPSVLGDGNKKLSKRDPQSNLFLHRDRGFIPEGLLNYLALLGWGIADDRDVFSLDEMVAAFDVVDVNSNPARFDQKKADALNAEHIRLLSEDEFTARLKAYFAAHGHDTGLDDAQFAEAARLVQTRIVVLGDAWGLLKFLDEGAFVLDEKAAAKELKADAVPVLDAALAGLEGVGQWTTGAIEEALKKALLEDLELKPRKAFGPIRVAATGASVSPPLFESLELLGRDRSLARLRAGRDHAAAAA", "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": "MEHPILFLNLLFEKLGLHVVGPEQAKSFGDFLLQPHVTYTWVVMLVLLGLGSMAAKGLEMVPKGAQNFFEVVITGIEDFMISITGEEGRFVFPLIASLGMFILFSNYLGMIPGFFSPTANINTTAACALISVVFTHVIGIKFHGVKYIKHFMGPVWWLTPLIMPIEIIGHIARVLSLSIRLFGNVFGEELVLGILFFLAGFYLAPLPMMFLGLFTGFIQAFIFCLLSMMYFAGAIEHAH", "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": "MMLVFQIALLVLVLYSLLLVVAVPVLYSSASDWSRAKNVILVGSLLWVLMVIGVGVLSFLK", "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": "MADLAKIVEDLSSLTVLEAAELSKLLEEKWGVSAAAPVAVAAAGGAAAAAPVEEEKTEFDVILTEAGANKINVIKEVRAITGLGLKEAKDLVEGAPKAVKEAVSKAEAADLKKKLEDAGAKVDVK", "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": "MPPKKADDGPKQHPIIGRFGTSLKIGIVGLPNIGKSTFFNVLTKSQAAAENFPFCTINPNESRVPVPDDRFEFLCEHHKPASKVPAFLNVVDIAGLVKGASAGQGLGNAFLSHISACDGIFHLMRAFDDDDIIHVEGNVNPVRDIEIIREELRLKDEEMIIAALDKLEKVAVRGGDKKLKPEYDIMCKVKTWVIDEKNHVRYYHDWNDKEIDVLNKYLFLTSKPMIYLINLSEKDYIRKKNKWLIKIKEWVDKNDPGALVIPFSGVLELNLQDMSDEEKQKYLEEKMTQSVLSKIIKTGYAALQLEYFFTAGPDEVRAWTIKKGTKAPQAAGKIHTDFEKGFIMAEVMKFDDFKEEGTEASVKAAGKYRQQGRNYTVEDGDIIFFKFNTPQQSKKK", "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": "MRSPKVKFLTIFTLSILITKMSFASSACFNEAGTMFRIEPNLIKAIALVESNLKKDSIGKNRDKKNNIKSFDYGLMQINQMHIPMLKKRGIIKDERDLLDNPCLNIKIGTEILYKHFSRCGMTWQCLGTYNAGFAMDNQKKRLQYAKKIYIVYTRLNELDNRKALAK", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the IagB/IpgF/P19 family."}
{"protein": "MTYLAVVLNGPKAKNGRKVFDSFLEQNRQMFWNRELTSACESITYMGFMRPGTLFVSGPASQLTVLKDAWARRILKPAMGYTITSLGDLGAIQQVEQMHFVPLGDVICDAVAQLNRQGLAATEQAIRQYVARHCPHVAPPGIEMVRQTITSLLSTGFVYKMADHYFVSVPTNSPMRPPAKAATKTTKTTVECQTGASMMCPQQTSTSSDEHVIEPAKKDHKKCQNSNRRSIFARLFSRGMKPQTIMPSASPIHVGGPPTPPPAAMLPTKNKYPTYHHDLNEECQRKARRRNHPRRGETQKLLSSSSECLKYYPVDMPETRPTRRRARMASPLRSSTPNNSDSAYSISPPHTDSNEEAGSISDSEINHTYININKFRRQNFDSTQFEDLTGATATTSEEPEILGRHIRGVLISNL", "text": "FUNCTION: Probable transcription factor (PubMed:23946438). Required for asymmetric cell division in neuroblasts, perhaps acting by regulating spindle positioning and myosin polarization, and thus the position of the cleavage plane (PubMed:3200316, PubMed:18505863, PubMed:8951066, PubMed:26703426, PubMed:15979607, PubMed:23946438). Required to produce daughter cell size asymmetry in neuroblasts undergoing asymmetric cell division, usually giving rise to one precursor cell and one apoptotic cell (PubMed:29668718, PubMed:15979607, PubMed:23946438). Positively modulates expression of the serine/threonine kinase pig-1/MELK during asymmetric division of the Q.a neuroblast (PubMed:23946438). Plays a role in neural fate specification in several dopaminergic lineages, including the hermaphrodite-specific neuron (HSN)/phasmid neuron (PHB), acting in concert with the kinase, ham-1, and the T-box protein tbx-2 and the homeobox protein egl-5 (PubMed:3200316, PubMed:18505863, PubMed:8951066, PubMed:28659600, PubMed:23946438). SUBCELLULAR LOCATION: Cytoplasm, cell cortex Nucleus Cytoplasm Note=Distributed asymmetrically in the cell cortex in some embryonic cells, including the hermaphrodite-specific neuron (HSN)/phasmid neuron (PHB) neuroblast (PubMed:15979607, PubMed:26703426). Localized to nucleus during interphase and evenly distributed in the cytoplasm of dividing Q.a and Q.p neuroblasts (PubMed:23946438)."}
{"protein": "MLNPIVHRFQYGKHIVILETGIVARQATAAVMVNMADTIVLVTVVGVKQVKPGQKFFPLMVNYQERTYAAGRFPGGFFRREGRPSEGEILISRMIDRPLRPLFPDGFLNEVQVIATVVSINPQVSPDIVAMIGVSAALSISGIPFNCPFGAARVGYINNQYVLNPTIAELVDSSLDLVVASTANAVLMVESEAKQLSEEQMLSAIIFGHEQQQLVIQNINHMVTIVGKPKWSWQAQVIDTNLQLCVTELAESRLNEAFCISDKQERDVCIETIKSDVLSALQQKNETIEEETISNIFANLEKQIARNRILGGKLRIDGRNHKMIRSLDMRTSILPRTHGSALFVRGETQALVTVTLGTERNAQNIDELIGERTDRFLLHYNFPPYCVGEIGLVGSPKRREIGHGRLAKRGILAVMPTANEFPYTVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKAAVAGVAMGLIKEDNNFVILSDILSNEDYIGDMDFKVAGSKNGITALQMDIKTKGITNNIIQLALNQAKDARMHILNMMEQVISMSRTDISPFAPRIHTIKIHPDKIKDVIGKCGSVIRALTEETKTIIDIEDDGTVTVAATDSIKAQQAICRIKDITAEIEVGSIYHGKVTRIVDFGAFIAISSNKEGLVHISQITNKRVEKVADYLSIDQIVLVKVLEVDRQGRIRLSMKDTNLTNK", "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": "MNSPLAPVGVFDSGVGGLTVARAIIDQLPDEDIVYVGDTGNGPYGPLTIPEIRAHALAIGDDLVGRGVKALVIACNSASSACLRDARERYQVPVVEVILPAVRRAVAATRNGRIGVIGTRATITSHAYQDAFAAARDTEITAVACPRFVDFVERGVTSGRQVLGLAQGYLEPLQRAEVDTLVLGCTHYPLLSGLIQLAMGENVTLVSSAEETAKEVVRVLTEIDLLRPHDAPPATRIFEATGDPEAFTKLAARFLGPVLGGVQPVHPSRIH", "text": "FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family."}
{"protein": "MTVERLENGVIVQRNTNEIEISITLDTVHGKLEGSTGVNFFDHLLNTFCHYSGLGLRVSTCESKDGILHHLIEDFGISLGLAFRELFDYTKVRRFGEATVPMNEALVGCYVDLSGRPFFQKNFEFSVEKIEDMPVEGFEEFMCGFVNHARITVHFFKFFGKNDHHISESAMKSFGLAIARALEGSEKKTTKGVID", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MAVVTMKNLLESGVHFGHQVKRWDPRMKKYIFSERNGIHIIDLQKTIVAIREAYEAVRKTTSEGKSVLFVGTKKQAQQTIQKEAERCGMFYINNRWLGGMLTNFSTIKKSLARLKKIEKMEVDGTFDNLTKKEIASLQKEKSKLEKNLGGIKEMKDLPGILFIIDTRKEEIAIREARSLGIPIIAVVDTNCNPEGIDYPIPGNDDAIRAISLFTGVIANAVIEADNEHGLKIIENLQEDEESGDSGVDPYQDREEEITDYSNYTPKDEASGDDEDEEDNSLVNDEDLYDDK", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MKNTFSRLFGFGDKMSELEIQNESHEDINKKIHEEIHEIPIANIIPNRYQPRTVFDDARIDELALTIRTHGLIQPIVVRQYEEDCYEIIAGERRFRAATKLGWEKVPAIIKNLNDTETASVALIENLQREELTAIEEAVAYQKLIELHNLTQEALAQRLGKGQSTIANKLRLLKLPEDIKRSLLEKSITERHARALIPLKNEELQLKVLQEIVEKQLNVKQTEERIAKLLEEVKPKRKAKKKAVSRDMRIAMNTIRQSLQMVAKSGLNVNSEEEEFDEYYQITIKIPKKK", "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": "MANVVVVGAQWGDEGKGKITDLLSEKAHVVVRYQGGVNAGHTLVVGGQTFKLHLIPSGILYPDKRCIIASGTVIDPEVLLAEIDQLHQLGISTDNLFIAETAHVTLPYHRVIDIAEEERRGIYRLGTTGRGIGPTYADKAERMGIRVVDLMYPDQLRERLSWAIPYKNVLLEKIYNLPPLDPEPIIEQYLAYAERLRPYVTDAALLLTQAIEDRENILFEGAQGTLLDLDYGTYPYVTSSHPIAGGACIGAGIGPTSIDRVIGVAKAYTTRVGEGPFPTELKDEIGAYLGATGAEFGTTTGRQRRCGWFDGVIGRYAVRINGLDCLAITKLDVLDGLDEIKVCVAYEYQGREIRHFPSDARVFAQCKPIYETLPGWKCSTKDCRSIQDLPPEAHDYLKFLAQLMQVPIAIVSLGASRDQTIIVEDPIHGPKRALLYPNGGKRAHALMPD", "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": "MKLPKPWWAGGGLLQLTILLSLVGLRVDLDLFLPPPAAALWEELLPLCPTRPASASNPFSASEGWERTPLLPAKGRLLHEVRALGVPFIPRTRVDAWLVHSVATGNADGAHGLLGTAASSAVGDGGQSASAGGGDPRAAHSSPLAAEEEEEKAAEPTAQVPDAGGCGSQENGMLREKSEAVDHSSQQEENEEGVSAQAKSRQQSKTEEHKMACASAREAEKITEARNESHLHWSDTSFSLEDLFQLLSSQPEHSLEGISVEDIPPFLSSVCESVNSSAQNINLSQAISHDVNLHEAMLLYPNNTFRRDPSARSSQAQEPFLQLNPHTNPEQATPAMSLPPFDNQMRNLTSQDLLYDLDSNIFDGINLMSLATGFSPLEVSQLFEEPDSGLSLNSSYNSTSLTNSYRIYDGTVGYNSDLQSLCHDLGAVGGCYPEPHKHCHMDHRTIAGFHVSLECQQVFHDHTYHLQSGASEPTSESFAWSEKSQKTSGCLDNPDRNLSRDEQRAKALHIPFSVDEIVRMPVDSFNSMLSRYYLTDLQVSLIRDIRRRGKNKVAAQNCRKRKLDIILNLEDDICNLQAKKEALKNEQTQCSKAIDIMRQKLHGLHQDVFNRLRDDQGRPVNPSQYALQYSHDGTVLIVPKELISSGHKKEAPKGKRERRN", "text": "FUNCTION: Activates erythroid-specific, globin gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. CNC subfamily."}
{"protein": "MESAALSRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETLDRAAVEGNLPVSGQYSPRDFVLSIQRPRSLIILVKAGAPVDQTIDAFSEYMEPGDCIIDGGNEWYQNTERRISEAEQKGLLYLGMGVSGGEEGARNGPSLMPGGSFQAYDNIKDILEKVAAQVEDGPCVTYIGEGGSGNFVKMVHNGIEYGDMQLISEAYDVLKNVGGLSNEELAEIFTEWNSGELESFLVEITSDIFRVKDEFGDGELVDKILDKTGMKGTGKWTVQQAAELSVAAPTIAASLDCRYLSGLKDERENAAKVLREAGLKEEIGSASSGIDKKRLVDDVRQALYASKICSYAQGMNLLRAKSLEKSWNLNFGELARIWKGGCIIRAVFLDRIKKAYQRNPDLASLVVDPEFAKEMVQRQAAWRRVVGLAVSAGISTPGMCASLAYFDTYRRARLPANLVQAQRDLFGAHTYERTDRPGAYHTEWTKLARKNH", "text": "FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. SUBCELLULAR LOCATION: Plastid, chloroplast Cytoplasm, cytosol. SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family."}
{"protein": "MPTIKQLIRNTRQPIKNVTKSPALRGCPQRKGTCTRVYTITPKKPNSALRKVARVRLTSGFEITAYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYHIVRGTLDAVGVKDRQQGRSKYGVKKPK", "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": "MVKKNSKSAKNASATIARNKRATFEYRIEDKIEAGLQLMGWEVKSIRMGKVNLSDCYVYIKEGEAFMHGCTIQPLNTASTHVVCDPIRTKKLLLKRSEIDKLAGLIERQGYTLIPLSMYWRKGAWVKVEIGLGKGKKDHDKREDTKEREWKIEKARVMKKDKVGA", "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": "MRSSKVIHVVGCHAEGEVGDVIVGGVAPPPGETVWAQSRFVASDNTLRNFVLQEPRGGVFRHVNLLVPPKNKEAVAAWIIMEPEDTPPMSGSNSICVSTVLLDTGIVPMVEPETHMVLEAPGGLIEATAYCKNGKAERIRVKNHPSFADKLDAKLELEGYGTLTVDTAYGGDSFCIVDAHALGFSIKPDEAKDFADLGMKIVKAANQQLGFQHPTNKDWSHISFCQFAAPLTDDNGTPSGANAVAIRPGKIDRSPCGTGCSARMAVLHAKGILKVGDAFVGRSIIGSRFDCRVEAETSIGGRPAIVPSIMGRAFITHTAQLMVDPDDPWQTGYRLSDTWPVWKQD", "text": "FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be involved in a degradation pathway that converts t3LHyp to L-proline, which would allow S.novella to grow on t3LHyp as a sole carbon source. SIMILARITY: Belongs to the proline racemase family."}
{"protein": "MTLEADKQTHGFQTEVKQLLQLMIHSLYSNKEIFLRELISNAADAADKLRFEALSAPSLLEEDPNLRIRVEFDKQAHTITIDDNGIGMSRDEAIAHLGTIAKSGTADFLKALSGDQRKDANLIGQFGVGFYSAFIVADHVDVYSRRAGLTAAEGVHWSSKGEGNFEVATIDKPQRGTRVVLHLKENEQHFAEGWTLRSTLKKYSDHIGLPIEMLKEHHGKEEEKDTPQEAEWEAVNKASALWTRPKNDIKDEEYQEFYKHISHDMTNPLAWSHNKVEGKLEYTSLLYVPTRAPFDLYHRNAAKGLKLYVQRVFIMDQAEQFLPLYLRFIKGVVDSADLSLNVSREILQSGPVVDSMKTALSKRALDMLEKLAKDAPEDYKTFWKNFGQVLKEGPAEDYSNREKVASLLRFASTYDTSGDPSVALTDYIARMKEGQDKLYYLTGESYAQIKDSPYLEVFRKKGIEVLLLVDRIDEWLMNYLHEFDGKSFVDIARGDLDLGNLDSEADKKAQEEIAKTKEALASRIKATLGEDVAEVRVSHRLTDSPAVLAIGEGDLGLQMRQLLEASGQKVPETKPVFEFNPSHPLIEKLDAEQDMDRFADLSRILFDQAALAAGDSLKDPANYVRRLNKLLLELSA", "text": "FUNCTION: Molecular chaperone. Has ATPase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "MALRTRLGEILRPLNAEYGKVAPGWGTTPVMGVFMGLFLVFLVIILQIYNSSIILENVDVDWVTVN", "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": "MIPLRSKVTTVGRNAAGARALWRATGTKENEFGKPIVAIVNSYTQFVPGHVHLKNVGDIVADAVRAAGGVPKEFNTIAVDDGIAMGHGGMLYSLPSREIIADSVEYMVNAHTADAMVCISNCDKITPGMLNAAMRLNIPVVFVSGGPMEAGKAVVVDGVAHAPTDLITAISASANDGVDDAGLLAVEQSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSTLATHSARRALFEKAGETVVKLCERYYGQEDESALPRSIATKKAFENAMALDMAMGGSTNTILHILAAAQEGEVDFDLADIDALSKRVPCLSKVAPNSDYHMEDVHRAGGIPAILGELNRGGLLNKDVHSVFSDDLESWLDEWDIRSGKASEEAIDLFHAAPGGIRTTEAFSTDNRWDSLDTDAENGCIHSIEHAHTADGGLVVLRGNIAPDGAVIKSAGIDEELWTFTGPARVVESQEEAVSVILNKTIQAGEVLVVRYEGPSGGPGMQEMLHPTAFLKGSGLGKKCALLTDGRFSGGSSGLSIGHVSPEAAHGGVIGLIEDGDIITIDIHNRVLDLGVSDEELERRRAAEEASDKPWQPKNRQRVVSKALRAYAKMATSADKGAVRQID", "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": "MARFLVALLATTLVAVQAGGQLGHAAPATAEVFWRAVLPHSPLPDAVLRLLKQPAAGVELLTEATSFVRDAEDRPPFDYRDYSRSPPDDEPSKSTGAASGARDFDYDDYSGGDKLRGAASGARDFDYDDYSGADKLRGATDEYKAPSSSLAGNGASMARGGKAETTTVFFHEEAVRVGKRLPFRFPPATPAALGFLPRQVADSVPFTTAALPGVLATFGVASDSATVASMEATLRACESPTIAGESKFCATSLEALVERAMEVLGTRDIRPVTSTLPRAGAPLQTYTVRSVRPVEGGPVFVACHDEAYPYTVYRCHTTGPSRAYMVDMEGARGGDAVTIATVCHTDTSLWNPEHVSFKLLGTKPGGTPVCHLMPYGHIIWAKNVNRSPA", "text": "FUNCTION: Required for pollen development. Probably synthesized in the tapetum, packaged in Ubisch bodies and transported at appropriate stages to the micropsores."}
{"protein": "MGFGWQGSVSIAFTALAFVVMAADWVGPDVTFTVLLAFLTAFDGQIVTVAKAAAGYGNTGLLTVIFLYWVAEGITQTGGLELIMNFVLGRSRSVHWALARSMFPVMCLSAFLNNTPCVTFMIPILISWGRRCGVPIKKLLIPLSYASVLGGTCTSIGTSTNLVIVGLQDARYTKAKQLDQAKFQIFDIAPYGVPYALWGFVFILLTQAFLLPGNSSRYAKDLLIAVRVLPSSSVAKKKLKDSGLLQQSGFSVSGIYRDGKYLSKPDPNWVLEPNDILYAAGEFDVVEFVGEEFGLGLVNADAETSAERPFTTGEESVFTPTGGAPYQKLVQATIAPTSDLIGRTVREVSWQGRFGLIPVAIQRGNGREDGRLNDVVLAAGDVLILDTTPFYDEEREDSKNNFAGKVRAVKDGAAKEFVVGVKVKKSSEVVNKTVSAAGLRGIPGLFVLSVDRADGSSVEASDYLYKIQPDDTIWIATDIGAVGFLAKFPGLELVQQEQVDKTGTSILYRHLVQAAVSHKGPIVGKTVRDVRFRTLYNAAVVAVHREGARVPLKVQDIVLQGGDVLLISCHTNWADEHRHDKSFVLLQPVPDSSPPKRSRMVIGVLLATGMVLTQIVGGLKSREYIHLWPAAVLTSALMLLTGCMNADQARKAIYWDVYLTIAAAFGVSAALEGTGVAASFANGIISIGKNLHSDGAALIAIYIATAMLSELLTNNAAGAIMYPIAAIAGDALKISPKETSVAIMLGASAGFINPFSYQCNLMVYAAGNYSVREFAIIGAPFQIWLMIVAGFILCYMKEWHQVWIVSWICTAGIVLLPALYFLLPTKVQLRIDAFFDRVAQTLNPKLIIERRNSIRRQASRTGSDGTGSSDSPRALGVPKVITA", "text": "FUNCTION: Na(+)/sulfate cotransporter with a probable high-affinity for sulfate and a proteasome dependent turnover. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the divalent anion:Na+ symporter (DASS) superfamily. Na+/sulfate symporter (TC 2.A.47.4) family."}
{"protein": "MSKQQKILFIDRDGTLIVEPPIDFQVDRLDKLKLEPFVIPSLLSLQDAGYRLVMVTNQDGLGTDSYPQEDFDAPHNMMMEIFESQGVKFDDVLICPHFEEDNCSCRKPKLGMVKEYLQGGKVDFQNSVVIGDRQTDLQLAENMAIRGIQYNPETMGWKQILKDLTVKARVAEVIRTTKETDIKVAVNLDEQGGNDISTGLGFFDHMLDQIATHGGFQMVCKVDGDLHIDDHHTIEDTALALGQALKEALGDKRGIGRFGFSLPMDECLAQCALDLSGRPYLKFDAKFSRDQVGDLSTEMVVHFFRSLTDTLACTLHLSSAGDNDHHIIESLFKAFGRTLRQAIKVEGTELPSSKGVL", "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": "MGDFGTVLTAMITPFKADGSVNYAVAAELAANLVDNGTDTLVVCGTTGESPTLSWDEEYNLFVEVLQTVAGKAKVIAGCGSNSTKEAIAATQKAAKIGVHGTLQVVPYYNKPPQAGLYQHFQAIAQACPELPLLLYNVPGRTGQNLSPETVVRLAEIDNIVGVKEASGNLDQAGEIRRLTPKEFQIYAGDDSLTLPLLAIGAKGVVSVASHLVGNQLQQMIQAFNSGQVTVASDIHLRLLPLFKTLFITTNPIPIKQALKLQGWEVGSTRPPLSDADAEVSQKLEAVMKHLDLI", "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": "MTVDIKTTLVTIPNQNLQIAGYLAEPVAVGQYPVVIVIQEIFGVNSHIRDVTERVAKEGYVAIAPAIYQRQAPGFEEGYTPEGIEAGRKLKDQTSSAEILSDLEATIAYAQTLPNVKPEEVGLIGFCFGGWIVYLGASLPTVKATASFYGAGIPHWAPGTAEPPITYTDKIQGTLYAFFGLEDTSIPMADTEQIEQALTKYQVNHKIFRYPGADHGFFCDQRASYNAEAAADAWQKVKQLFQTELK", "text": "SIMILARITY: Belongs to the dienelactone hydrolase family."}
{"protein": "MAASAEIDAEIQQQLTNEVKLFNRWSFDDVSVTDISLVDYIGVQPSKHATFVPHTAGRYSVKRFRKAQCPIVERLTNSLMMHGRNNGKKLMAVRIVKHAMEIIHLLSDLNPIQVIIDAIVNSGPREDATRIGSAGVVRRQAVDISPLRRVNQAIFLLTTGAREAAFRNIKTIAECLADELINAAKGSSNSYAIKKKDEIERVAKANR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "VLFTPPELLGCGNRCSDDCCKWGRCQPGCTD", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MSKIYDWFEERLEIQSIADDISSKYVPPHVNIFYCFGGITFTCFLVQVATGFAMTFYYRPTVAEAFTSVQYLMTQVNFGWLIRSIHRWSASMMVLMMILHIFRVYLTGGFKKPRELTWVTGVLMAVCTVSFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGQVLLELLRGGVAVGQSTLTRFYSLHTFVLPLFTAVFMLMHFLMIRKQGISGPL", "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": "MTIKLAITPGEPAGVGPDLIITLAQQQWQAMLVVFANAELMRTRANELNIPLTLLPYDASRTDIQPAGSLYIVDIPLQDEVIAGKLNPTNSQYVLDTLHQACQMNLNGEFQALVTGPVHKGVINEAGIPFSGHTEFFAQQSNTPEVVMMLATEGLRVTLATTHIPVTAVSAAITQPKLDNVIRIIDHDLRTKFGIAKPHIFVCGLNPHAGEDGHIGREEIDTIIPALNALRQEGITLTGPLPADTIFNPKYLQQADTVLAMYHDQGLPVLKYKGFSQAVNITLGLPFIRTSVDHGTALDLAATGQADVGSFSIAIKEAISLAKSTQ", "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": "MAGVNLQLRHAYSIAQFVPTVSSPPPLPTQRVRLGTSPSRVLLCNLRANSAAAPILRTTRRSVIVSASSVSSAVDSDSLVEDRDDVGRIPLLEVRDLRAVIAESRQEILKGVNLVVYEGEVHAVMGKNGSGKSTFSKVLVGHPDYEVTGGSIVFKGQNLLDMEPEDRSLAGLFMSFQSPVEIPGVSNMDFLNMAFNARKRKLGQPELDPIQFYSHLVSKLEVVNMKTDFLNRNVNEGFSGGERKRNEILQLAVLGAELAILDEIDSGLDVDALQDVAKAVNGLLTPKNSVLMITHYQRLLDYIKPTLIHIMENGRIIKTGDNSLAKLLEKEGYKAISG", "text": "FUNCTION: Essential protein. Required during embryo development, especially at early stages. Involved in chloroplast differentiation. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ABC transporter superfamily. ABCI family."}
{"protein": "MTKGILGRKIGMTQVFGENGELIPVTVVEASQNVVLQKKTEEVDGYNAIQVGFEDKQAYKKGSKSNKYANKPAEGHAKKADTAPKRFIREFRNLNVDEYEVGQEVSVDTFETGDIIDVTGVSKGKGFQGAIKRHGQGRGPMAHGSHFHRAPGSVGMASDASKVFKGQKMPGRMGGNTVTVQNLEVVQVDTENSVILVKGNVPGPKKGLVEITTSIKKGNK", "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": "METTNFGFIISLLFVGIPTIFLVGLYISTSDGEKSSFFSDSSKGKLGPKS", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbM family."}
{"protein": "MRVLVASRNKKKLAELNRMLEAANVTGIELVGLGDLPEYPETPETGATFVDNARIKTNDGVRHTGLPTIADDSGLAVDALNGMPGVLSARWSGGHGDDKANNDLLLAQMGDVPDERRGAHFVSSCVLQLPAQVAAERGMETEYAVEGRWYGRVLRAEQGEGGFGYDPLFAPDELPEGQEEQLAGKSAGELTAEQKDAVSHRGKALRQLVEILAQLAD", "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": "MTDHIRPLIAGNWKMNGLKASTAEFEAMLAGAAEVTGKADLLVCPPATLLAGFADKARGTRAVAVGAQDCHAKASGAHTGDLSAEMLADAGASAIIVGHSERRADHGESDVVVHQKTEAVWRAGLVAIVCVGETQQQRDAGQTLDILRGQLNLSLPQGSTAANLTVAYEPVWAIGTGLTPTAKDVEQIHAFIRTLLIERFNGEGARMRILYGGSVKPSNAAELMAVANVNGALVGGASLKAADFLAIAKGC", "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": "MTGPAAAPVPDAPASLDVSGLAFAYPDGHQALFGVDFCVARGERVALLGPNGAGKTTLVLHLNGILTGGTGTVTVAGLPVDKRNMAEIRRRVGIVFQDPDDQLFMPTVREDVAFGPAAAGVKGAELEACVDRALTLVGMAEFKDRPPHHLSFGQRRRVAVATVLAMEPEILVLDEPSSNLDPASRRELADILRSLDVTVLMVTHDLPYALELCPRALILSDGAIAADGPTAALLSDDDLMRAHRLELPFGFDPRSVRASG", "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": "MAEPDYIDDDNPELIRPQKLVNPVKTSRNHQDLHRELLMNQKRGLAPQNKPELQKVMEKRKRDQVIKQKEEEAQKKKSDLEIELLKRQQKLEQLELEKQKLQEEQENPPEFVKVKGNLRRTGQEVAQTQES", "text": "SIMILARITY: Belongs to the FAM107 family."}
{"protein": "MNREEQLGVLESLLFAAGDAGLSTEQLTEVMEITHIEALNLLELLSERYNESADRGLILLELAGTFQLATKKAHAEFLRKLVEVPSNTVLSQASLETLAIIAYRQPVTRMEVDEVRGVQTDGPIRTLVAKGLVTDKGRVDGAGRAKLYVTTSEFLDAFGLNSLEDLPKLADPATDEPDQNEMDLFFDRFNQSKEQEEE", "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": "MASEEIIREVYKVLEERRDNPIDSYTSKIMQDSDKKAEDKILEKVAEECGEVLLAAKNDENLVYESVDLIFHTLLILVYKGIEIDEIFEEFARRRH", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MKQKYQYIKNTELDLKDKIFGINKPKNFSSNQVIQIIKKYYGLKKIGHAGTLDPLATGLLLVATNSKTKELNELILENKKYVAEIQFNYQTSTYDAEGEITNYTTRKIHEKTLKEELKFLNSTYWYQQPPVYSAVKIKGKKLYEYARANQEVSVPFKKVYINKVELISFDSISQKTFVSLDVSKGFYIRSFANDIGLRLNNYGYLLNLKRVEVGNYKLDQAYDFFDLVKQVN", "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": "MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRAVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE", "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": "MPSKSLSNLSVTTGANESGSVPEGWERDFLPASDGTTTELVIRCVIPSLYLLIITVGLLGNIMLVKIFITNSAMRSVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWMFGKVGCKLIPVIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGALLRTCVKAMGIWVVSVLLAVPEAVFSEVARISSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFIFCWFPNHILYMYRSFNYNEIDPSLGHMIVTLVARVLSFGNSCVNPFALYLLSESFRRHFNSQLCCGRKSYQERGTSYLLSSSAVRMTSLKSNAKNMVTNSVLLNGHSMKQEMAL", "text": "FUNCTION: Receptor for neuromedin-B (PubMed:1655761). Contributes to the maintenance of basal sigh rate through signaling in the pre- Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR- expressing neurons in the sneeze-evoking region of the brainstem (By similarity). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (By similarity). Contributes to induction of acute itch, possibly through its activation on dorsal root ganglion neurons by the NMB peptide (By similarity). Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6 (PubMed:31601264). Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "METPFWKTKTLEQMSPAEWESLCDGCGKCCLSKLEDEDTGEIYWTSVGCRLFDAQTCRCSDYANRLARVPDCVGLTPQNVRTISWLPSTCAYRLVAEGRDLYWWHRLVSGSAETVHEAGISMRGRVKASETDLAEPEDYFDYMLDDEP", "text": "SIMILARITY: Belongs to the UPF0260 family."}
{"protein": "MDLTAVALLVSLVSVSLSAENAGGKARSCTDVRQFYSGKGFTLNGVPQSEISGEHLRICPQGYTCCTSAMEETLSNLSRREFEGLVREAGRSIQALLNAQYRTFDTYFLELLNGSERWLEEAFVAALGELYRLNAGVFRDLYAELHRYYSGASLNLEEALDEFWMKLLERLLKASDPETASLLSDDFLDCASKQTETLRPFGDAPRELKAKLVRAFIAARAFVQGLNAAGEIVRKVSQVPLSPECNRAIMKLVYCPHCRGLGSVKPCINYCKNVMKGCLANQADLDTEWQSLIETMLQVASSFGAEPSMDTVIYSIPVRISEAVLAMQENMEIYTSKVFKACGDRGEEGTPSSISEEPKKKERTVTALEYKPSPKSAARLEVQVTDVYSKLKEMQLYWIQLPSALCSGKTASSTTGDKCWNGITKASYLPEVMGDGLANQINNPEVEIDITKPDRTIRQQIMLLKIMSNRLKNALEGNDVDFQDTSDDFSGSGSGMCADHLCVRGRPPVFGPKTDRPKLYATGPENKRVKGSGNQIQPSFILLIVFFVSLLLRR", "text": "FUNCTION: Cell surface proteoglycan that bears heparan sulfate. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space. SIMILARITY: Belongs to the glypican family."}
{"protein": "MATGTPAAELRELTEEELVTRLRESKEELFNLRFQMATGQMDNNRRLRTVRHEIARIYTVLRERELGLAVGPDAGDAA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MAQYSTNEFKGGLKIMLDGDPYTIVENEFVKPGKGQAFNRVKVRNLKTGKVIDRTFKSGESVEAADVLETEMQFLYSDGEFFHMMDPETFEQKAAPASAVGDAAKWLKEQAMCTVILWNDEPLTVEPPNFVELRVVETDPGVRGDTSGGGGKPATLETGAVVRVPLFIEEGELLKVDTRSGEYVGRVKG", "text": "FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the elongation factor P family."}
{"protein": "MAIVDLVNAGEQQQMGSKRAAAEDGDGGVDDSREYYCRRGVRHLCDSGITRLPGNYVLPASDRPGQAAGAAAAAGGSVKLPVVDLSRLRVPSERGAVLRTLDAACREYGFFQVVNHGVGGEVVGGMLDVARRFFELPQPERERYMSADVRAPVRYGTSFNQVRDAVLCWRDFLKLACMPLAAVVESWPTSPADLREVASRYAEANQRVFMEVMEAALEALGVGGGGVMEDLAAGTQMMTVNCYPECPQPELTLGMPPHSDYGFLTLVLQDEVAGLQVMHAGEWLTVDPLPGSFVVNVGDHLEILSNGRYRSVLHRVKVNSRRLRVSVASFHSVAPERVVSPAPELIDDRHPRRYMDTDLATFLAYLASAAGNHKSFLHSRRLY", "text": "FUNCTION: Involved in the regulation of shoot development and salicylic acid (SA) homeostasis. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MRDVQSERDERNVPLKHVGIKNLKYPVVVLDKKNKNQHTIAEINMYVDLPKDFRGTHMSRFLEVLNKFHLKIDPKNIKAILDDLKKTLKAQSASIEIMFPYFLQKKAPVTKIESYMEYKCGFKAYDTNEECEFYIVVEVPIQTLCPCSKEISKYNAHNQRALARIEVETSELIWFEDLIELAESSASVPLFTLLKRPDEKYVTEKAYENPKFVEDVARDIALSLKENKKIRWFKVEVESFESIHNHNAYACVNSDTMEV", "text": "FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. SIMILARITY: Belongs to the GTP cyclohydrolase IV family."}
{"protein": "MCDEEVTALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFDQEMGTAASSSSLEKSYELPDGQVITIGNERFRCPESMFQPAFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVMSGGTTMFPGIADRMQKEITSMAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "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": "MEQAPEDQGPQREPHNEWTLELLEELKSEAVRHYPRPWLHDLGQHIYNTYGDTWEGVEAIIRTLQQLLFAHFRIGCQHSRIGITRQRRVRNGPSRS", "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": "MERATVRLLRGGALLRRNFPSCLSSWKTPPHALNSSQSEAQLKATSNGPPLAPLQTFTDEEMMIKSAVKKFAQEQVAPFVSKMDEDSKMEKSVIQGLFQQGLMGIEIDTKYGGTGASFFSSVLVIEELAKVDASVALVCDIQNTLINRMIGKYGTEEQKATYLPKLATEKASSICISETGAGSDSFAMKTRADKKGDYYIINGSKMWISSAEIAGLFVVMANADFSAGYKGITCFLVDGDTEGLHVGKPENKLGIRASSTCPVTFENVKVPKTNILGQVGHGYKYAIGSLNEGRIGIAAQMLGVAQGCFDYTIPYIKERKQFGRRVFDFQGLQHQVAHMATQLEAARLLTYNAARLLEAGRPMIKEASMAKYHASELAGLITSKCIEWMGGVGYTKSYPVEKYFRDAKIGTIYEGTSNIQLNTIAKCISAEY", "text": "FUNCTION: Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (By similarity). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2- methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway (By similarity). Can also act on valproyl-CoA, a metabolite of the valproic acid drug (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MTFDALLLLSFGGPEGPEQVMPFLENVTRGRGIPRERLESVAEHYLHFGGVSPINGINRDLITAIEAELSRRGMQLPVYFGNRNWEPFVEDTVAAMRDNGIRRAAVFSTSAWGGYSGCTQYQEDIARGRNAAGPDAPELVKLRQYFDHPLLVEMFADAIADARDTLPEPLRADARLVFTAHSIPLRAASRCGPDLYERQVGYAAGLVAGAAGYRDYDQVWQSRSGPPQVPWLEPDVGDHLAALAEAGTKAVIVCPIGFVSDHIEVVWDLDSELAEQAAEAGVALARASTPNAQPRFAQLAVDLIDEVIAGRPPQRVPGENPVPGYGSSVNGALCTELCGA", "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": "MGNEASYHSEMGTHFDHDEIKRLGRSFKKMDLDKSGSLSVDEFMSLPELQQNPLVGRVIDIFDTDGNGEVDFREFIVGTSQFSVKGDEEQKLRFAFRIYDMDNDGFISNGELFQVLKMMVGNNLKDWQLQQLVDKSILVLDKDGDGRISFEEFRDVVRTMEIHKKLVVFVDHGQED", "text": "FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. SUBCELLULAR LOCATION: Mitochondrion Note=Localizes in the mitochondria in a SPATA33-dependent manner. SIMILARITY: Belongs to the calcineurin regulatory subunit family."}
{"protein": "MIMGGVRELLLVVMTVGVVKVSCYPVGKSQKQDQVSLQRRLGELSSNDVSIVHALALLRSIGSDAKQAREEYLETNEVESQASPNHGSSPANDALSSEEKLRRVSSDDAATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDATSEAATGPSGDDAMDI", "text": "FUNCTION: In response to egg activation, PSGP is discharged by exocytosis into the perivitelline space, where it undergoes rapid proteolysis into glycotridecapeptides. During fertilization and/or early development the glycotridecapeptides prevent polyspermy or are involved in the formation of a fertilization membrane."}
{"protein": "MIVRTLDECRNSERRVVSDNWESVRMLLKDDNMGFSFHITTIYEGTETHIHYQNHLESVFCMSGEGEIEVVGGETYPIKPGTLYILDKNDEHYLRAYKNKEMVMACVFNPPITGAEVHDENGVYPLVD", "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": "MRFEGLIGARILKRINRFAVQIDVEGRTELAHLHDPGRLLEIVYPGNEVLVRRTDGPKLKWRIEFGKINGRYVLIDSGLHSDIARRFLPEGAVPEVRVGRKRIDFRYGDDYIEVKGCTLMANGIAMFPDAPTKRGLEHLKTLETLASSGYRSHVMMIITRDDVRCFYPNFETDPKFAEAFLRLVPAYVKAHFLTFGFDGLYLRYAGSIGLCADVGHGTNGRL", "text": "SIMILARITY: Belongs to the SfsA family."}
{"protein": "MPTELTLATRRSALALAQSRAFARSLEAAVPDLSLRELEVVTSGDKTQDRSLQDIGGKGLFIKELEEALLDRRADFAVHSIKDVPAEIAPALCLACIPAREDPRDALVTRSGALLAELPAGARVGTSSLRRAVALREARPDLVIEPVRGNVDTRLRKVFDGVFDAVVLALAGLKRLGLEARATEVLSPEVSLPAIGQGALGIECRTADDSVRDVLGTLADAETTICVSAERAVMAAVEGSCRTPVAAYAVRDGGALWLRALLAEPDGSRLRRAERRLSWPGNTREAERLGADLGAELKKG", "text": "FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SIMILARITY: Belongs to the HMBS family."}
{"protein": "MVLLAAKGLSLLDVNPGLVVWTLVTFLVVVLVLKKFAWDVILKALDERAETVQNDIKKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLLEETNGEVKAQKDQAVKEIELAKAKALGQLQAQIVEMTITVAAKVLEKQLKSEDYKAFIETELDKLGKLSA", "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": "MTITDLVLILFIAALLAFAIYDQFIMPRRNGPTLLAIPLLRRGRIDSVIFVGLIVILIYNNVTNHGALITTWLLSALALMGFYIFWIRVPKIIFKQKGFFFANVWIEYSRIKAMNLSEDGVLVMQLEQRRLLIRVRNIDDLEKIYKLLVSTQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0266 family. SIMILARITY: Belongs to the UPF0266 family."}
{"protein": "MQNTIRIIGIDPGLRRTGWGVIETLGNSLRFVASGTVTSDGELDLASRLCQLHDGLAEVVHGYQPHEAAVEQTFVNKDATATLKLGQARGIAMLVPARAGLRVAEYAPNAVKKAVIGVGHGEKQQIHMMLKVLMPKAEFKGNDAADALAIAICHAHNRQAVTSRLAALAG", "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": "MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTELRFQSSAVMALQEASEAYLVRLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA", "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": "MKPMSYWDYIKVEELLALQGGANGDETQVGNDEALFIVVHQVYELWFKLILRELTFARDLLRQDTVPGHQIALGVRSLRRAIAVFEQANQHFRVMETMTARDFLDFRERLMPASGFQSAQLREIEILLGLEDNERIAVCQGGSFKDALKLPNGALSSAAYRVEAREAHGQSLKHCLYAWLSRIPIDGSNEPAAVKRFLRDYIGSVRAESQRRLQTAIDRQLAPAEVERLRARYQADDVGAETFLLAEEDPQADAMTREKRRAVRAAMLFVESYRELPQLAWPRELLESILELEQSMLIWRQRHARMVERIIGRRVGTGGSSGVDYLDQTALRYRVFTDLWTVRSLLLRKSSVPPIRQGASYAFAEEALV", "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": "MHNESPIIRRKSTRIYVGKVPIGDGAPITVQSMTNTKTTDVAATVAQIKALERVGVDIVRVSVPTMDAAEAFKLIKQQSNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGSEERIRSVVDCARHHNIPIRIGINGGSLEKDIQEKYGEPTPEALLESAMRHVDILDRLNFDQFKVSVKASDVYLAVNSYRLLAKQINNPLHLGITEAGGARSGSVKSAIGLGLLLSEGIGDTLRISLAADPVEEVKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIGTVNALEQRLEDLITPMDVSIIGCVVNGPGEALVSTIGVTGARNHSGFYEDGVRQRERFDNEKMIDQLEAKIRAKASMLDANNRIVINMLEEK", "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": "MSDWSIEDARSGYNVTHWSQGFYGIREDGEVTVSPNPQNPDHKVGLNELAKSMVEAGVSLPVLVRFPQILHHRVESLCEAFNDAIKKYDYQNDYLLVYPIKVNQQKTVVEEILASQKSKEVPQLGLEAGSKPELMAVLAMAQKASSVIVCNGYKDKEYIRLALIGEKLGHKVYIVLEKMSELKMVLIEAEKLGITPRLGLRVRLAFQGKGKWQASGGEKSKFGLSAAQVLKVIAELKSANMLDSLQLLHFHLGSQIANIRDIRQGVSEAGRFYCELRQLGASIDCFDVGGGLAVDYDGTRSQSNNSMNYGLNEYANNIVNVLTDLCNEYEQPMPRIISESGRHLTAHHAVLITDVIGTEAYQPENIQEPSEDAPQLLHNMWQSWLEISGRYDQRAIIEIYHDSQSDISEAHSLFAVGQLSLADRAWAEQANLRVCHEVKGLLSNNNRYHRPVIDELNEKLADKFFVNFSLFQSLPDAWGIDQVFPVLPLSGLDKAPERRAVMLDITCDSDGIVDQYVDGQGIETTLPVPAWSADSPYLIGFFMVGAYQEILGDMHNLFGDTNSAVVRIDERGLSQIESVLEGDTVADVLRYVNLDAVDFMRTYEELVNQHIVEEERASILEELQLGLKGYTYLEDF", "text": "FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily."}
{"protein": "ADYLQLAR", "text": "FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRF amide related peptide) family."}
{"protein": "MYFLKKIVNLFSSKIESEDNNVKKDDLTQPRKQSPEARKRRNRRIIFWLIILLIIGTIIGVIIYFSVRKEYDNVIVKSAQTEVVNNKKVLYLNTIRPNSTQITRYTIDEDQLLTARVNILNNTNFQIISNASSLGLSRISFNIVREGVEKFKLGETNIYAPISGNTNNQWNWLTSIITQNAGIPSSGFNPQVIISPLISIIFFIIFLYIILRVSKAQSDSLLGTNKANAKLTKSGVRFSDVAGIAEVKEELIEIVDFLKEPKKYVAAGARIPKGVMLYGPPGTGKTLIAKAVAGEANVPFFQTTGSSFEDTFVGVGARRVRELFEKARKSAPAIIFIDEIDSVAKKRGNSLTAVQDQTINQLLSELDGFDTSSGVIVMAATNRLDTLDDAILRPGRFDRQISVNLPDILEREQILRIHSRNKNLSAKVSLEDIARRTAGFSGAQLENVLNEAALLSVRDKATSIHMNHLDEAIDRVIAGPSRPNKVISEREREQVSYHEAGHALIGLYSPGADVVQKITIVARGRAAGYTLQTPERNENILQNKTELISRVRTALGGRAAEELIYGPNEITTGAANDFYKITNIVRAMVASFGMTDVGLTQYIATEGVDNPYRNSYSEQTALAIDIEIEKIIQREYKIVKEMINEHREELELIVQTLLELETILKPQIDYIHQYKQLPPEVIANKNKREASQKQANSSVEEAKVVDDEESIKDKEKDQKSN", "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": "MFSLQELCRKNIYILPYPLGKHVLQQLGLYWKGHGSLQRIGDDHVLLQQDLIFSINEALRMAAEEGNNEVVKLLLLWEGNLHYAIIGALEGDRYDLIHKYYEQIGDCHKILPLIQDPQIFEKCHELSNSCNIRCLLEHAVKHNMLSILQKHKDQIRLHMALTQILFELACHERKNDIIRWIGYSLHIYHLETIFDVAFAHKNLSLYVLGYELLMHKVNTEAANIDLPNLLSYHLRTAAAGGLLNFMLETIKHGGCVDKTVLSAAIRYKHRKIVAHFIHQVPRKTVKKLLLYAVQARAPKKTLNLLLSSLNYAVHTITKQLVHNVINYSSTLVVKLLLMRRKRKLNLVDAVLARLVKYSTYTDIVQFMGEFSVSPERVIKMAARESRTFLIEMISKAAWGNHPQTLIHHLKHLTNTMKPQSGKDLIIYTIHYIYLNSNMLVAEEEKNIFKLAKFYANHNAVNRFKQICEDYYILDARFKTLILECFEIAVQKNYPRIANIVDDYIRFLFYRGNITEEEIREAYSLKDAEVYVDLKWLQQGEMV", "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": "MAPFVRNLVEKTPALVNAAVTYLKPRLAAFWYYTTVELVPPTPAEIPRAIQSLKKIVSSAQTGSFKQLTVKEALLNGLVATEVSTWFYVREITGKRGIIG", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane. SIMILARITY: Belongs to the ATPase g subunit family."}
{"protein": "MSTIVLILALLLTSLIAVGLLWWLRFRRPHPITAALPFVKLTHRKLTPEERVSIENYLRNQQNKHGFNTQPAFDSHALAASTSSTPMLVLTPQSDNVYSVTRAITRYGVASDEPNKWRYYLDSIEVHLPSAWEQYITQDNDVELIQTQTIPLVISLNGHTLNNHQSENTYQPILPSVSKNASIRKEDSEHIELLNIRKETPEEYALHGPNGLKEACAICIALLLLFFALSGPTVTLPWLVIVAVSLTCWACWYLFRPLSEKDLREVHCLNGTPKRWGLFGESNQGQINNISLGIVDLIYPAHWGPYFVHDLGKKTHIDIYLNRQVVRQGAFLSLHDEMKMFPLQRWGKNLTLIVGSLLVLVLLLIYVPLGLPLKLSVAWLQGAQSQQVTSVAALDKMPLRIGDMLKAQGNGMCYVPPNIQNTRGFVFTPFDCSGIYWNTASPLPQPESETIEKAAALVETINKQLHPQGSDASVNPKLATAIEKSGMILLDDFSDIVLKTQALCSENTDCIRLKNALVNLGNAKNWSALVKRAQSGNLEGMNVLLRPISADVLENLINTAASSFVYRETHLATEALNSPPPGGFLITSDEGKQLVNHPAPTLPLFDYSALEQWRELQRLSALLLDTPFKAEGIITNITTDANGTRHIALHSEPDIVTLGRYLATSLLLLVLIFCLVVNMVLLIQRAMKNRRRMDNIQRYYDDCFNQTLTPPPFLR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the IgaA family."}
{"protein": "MSEIGSSVPVNENRPLLTEDEVEAQANSSTVWPLSRIRVARCEWKLWGSLAFIFGASAYIYSFSRVMKDSFVLSRQLPIAISFLKTCFVLPISVIVTGIVQKLLVTRTISKVFDYTLIAFSFLYLLIGMVLLPFAEKIQPGLYFSRDIFADDKMAYKGFEFLFAIFLIFNEWTTSFVYVCAELFGSLVVQFMFLAFANEALTIRQSTRMMPLFYVISNILLLLSSESTSFYSKKVREWDYKKTCLITNSFFAVFGAMIAVTYLVKKYAENTILKKQLFIRTEGVAKKKGRKSSAGFSESMKLMAQSKFLVAMVMNALFYYAGTNLIESSWKNGISVAADANNMEKRAYSASIVSGEQRVVGALVAIILLTPISTLVQTHGWITMAIVPPLVTLVSSLVIFGSAFFNYSNYPEGKTSVILSSLVKGYKPNFYLECNIGIYCVSGMKIAKYAFYDISKEAISLQIDPLYRPRLKAVYDGLCGKLGKSIGSLYAMFWSVMGYNDVRAAAPITLGMWLIISPIWIYSVIYLNRKYNQSIQTSSPIDLDLFSGKKDLE", "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": "MASSHQGNGTVPNSQTDAPPDSSTKRRWRRNRIACDSCHARRVRCDRQFPCSRCLRSEITCEFTRERRKRGRIARSKLAEMAKNKMETSETPAPAKTMNGIPAPAGTEIPGHVSPASTFHHRSPPANAPTVSAPSVDGRRSQTDPQLPVRRPEIGGNVTEEWLAGTHVSPGSYEFLNGPAFGEGLGPFPHMFDVWNGVDLAAYSAGTSQGSKATNAPSTSTAPLKYPVLQPLMPFVEATLPRKLVFDLLDLYFTSAFSTHMHPVSFLSKDAPRPSSPALLSSMLWVAALDDRAFSLPISPPQRKRICQFLCALTIRLLRPLIHVSFKDQGGAAAAVAAAAAAATNNPAFAGVGQDLPPTTVHHPFEGGGDDRGLVGPAGSLDDVITYIHVASIISSSEQKAASMRWWHAAFTLARELKLNQEIEVMPNGDSQVEGSSPPFGYSLPGWDGADPGPVFNYSNPTRSSLNCVCDRQDQNTITEEHREERRRTWWLLYIMDRHLALCYNRPLALLDAESEDLLLPLDEASWQSGIIHSNSPKSDGPQCLLSADKNKRRLFPNFICHDHSVFGFFLPLMTITGELIDLNQARNHPMLGMRLNGKDAWNVHVSEVLRQLEIYKASLTTFAATTSDPEAPLSAYAHAQSEHLPAEPSLSQAYAWHTQTVISYASYLVHVLHILLVGKWDPVSLIEDKDFWTSSPAFASTISHALDAADSVDQILRYDPDISFMPYFFGIQLLQGSFLLLLIVERLQKEAGEGILNACEVMIRATESCVVTLNTEYQRNFRQVMRSAVAQARGRPVNHSEIRHRRKAVLALYRWTRKGTGLAL", "text": "FUNCTION: Transcriptional activator of the arabinanolytic system. Involved in the regulation of extracellular arabinanolytic genes and in the regulation of the intracellular activities of L-arabinose catabolic genes in the pentose catabolic pathway (PCP) in response to the presence of L-arabinose. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the xlnR/xlr1 family. araR subfamily."}
{"protein": "MAEASQLFKEFKIQSVSEFFRRNAAMLGYTGKIRSLTTVVHEAVTNSLDACEEAGILPYVRVEIEELGREHYKVIVEDNGPGIPEKFITHVFGKMLAGTKAHRNIQSRGQQGIGISGAVMFAQITSGKATRVITSTGGDIIEAWVKIDVDKNEGKIVKKERHPNPKGWRGTRIELEVKNVRYVRSKQGVYWYLKLTAIANPHAHIELIEPDGKLIVFPRSSEEVPKPPVEMKPHPKGVLTDDVYRMAKKTRRNTVRRFLIGEFSRISDKKVDELIKYIAALRLIKTEKDKAVQDQLYERLMNGEVDKVLRSFKGYTKVVKQVAKLMEKPPEKLSWHEAEEIVEAFKYMKFLAPPTHGLRPIGEENIEKGLKGILKPEFVTAVTRPPKVYSGGIPFQVEVGLAYGGEISSGFDLLRYANRVPLLFDAGSCVTTLAARSIDWKRYKVDDLERAPVVLMINVISVHVPYTGTGKQSIANVDEIHNEIRLAIMDAARRLQTYLSGKHRRLYQVKRKKTFEKYVPEIAKALSILTGEPEEEVKNYFLRFIEERFAQSEVEAEEVAENA", "text": "FUNCTION: Relaxes both positive and negative superturns and exhibits a strong decatenase activity. SIMILARITY: Belongs to the TOP6B family."}
{"protein": "MKTFFLIEAGRALQIVAFRPAITTVLFQRFSVSFSCSYFTCCTSQLLRENWLFKFLTAFDHVIRASNDLSTMRFMIMYIYVYIYIYTVLRKRLSCYMLIL", "text": "FUNCTION: May be involved in growth at elevated pH and presence of calcium."}
{"protein": "MRFSPELEQGRLLVRYKRFLADIETDSGELLTIHCPNTGSMLNCMMPGGRVWFSRSNDPKRKLPGTWEISETPQGRLACINTGRANTLVEEALRAGVIRELEGFTALKREVAYGQEKSRVDFRLEYPDGYLYLEVKSVTLGFADSAVAAFPDAVTQRGARHLRELATLAREGVRAVLLYCVNLTGIEAVRPAKEIDPAYAAALREAVDAGVQILAYGVQLTPEAVYIDRHLEVHWPD", "text": "SIMILARITY: Belongs to the SfsA family."}
{"protein": "MKVILKEDFINLGREGDTVEVRDGFARNYLLPKGFAVFSNKHNVEIFNQKRRSILKKQETKKQIANDLKSKLDLVKLEFFMKSNDSGKLFHSINSLNIAEELFKLGFDIERKKIDIHHGTLKTFGTYDVTIKLYEGISSIIKVEIKKEEKQEDKKPLNKKLNKVDEQAERERV", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MRSPVLIINCKNYEEAAGGRIRGLADAAAGAAARYGVRIAIAPPQHLLGIIAGRDLGVLAQHVDDKGTGSTTGYVVPELLKQSGVSGAIINHSEHRVPADQVAGLVPRLRGLGMVSVVCVRDPAEAADLSRYCPDYIAIEPPELIGSGRSVSTERPQVIQEAAEAIRGAGGVKLLCGAGITSGADVRRALELGSEGILVASGVVKSADPAGAIGELARAMS", "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": "MITIPITLRMLIAKYLCLLKPFWLRKNNKTSVLLIIIILAMILGVVKIQVWLNDWNNDFFNALSQKETDKLWQLVLWFPALLGIFVLISVNKTWLIKLLTIRWREWLTDYYLNRWFADKNYYFTQIYGEHKNTDNPDQRIAEDILLLISKTLSLSFGFIQSLSMLITFTVILWESAGTLSFTVGGTEWNIQGYMVYTVVLIVIGGTLFTHKVGKRIRPLNVEKQRSEATFRTNLVQHNKQAELIALSNAESLQRQELSDNFHTIKENWHRLMNRQRWLDYWQNIYSRSLSVLPYFLLLPQFISGQINLGGLMKSRQAFMLVSNNLSWFIYKYDELAELAAVIDRLYEFHQLTEQRPTNKPKNCQHAVQVADASIRTPDNKIILENLNFHVSPGKWLLLKGYSGAGKTTLLKTLSHCWPWFKGDISSPADSWYVSQTPLIKTGLLKEIICKALPLPVDDKSLSEVLHQVGLGKLAARIHDHDRWGDILSSGEKQRIALARLILRRPKWIFLDETTSHLEEQEAIRLLRLVREKLPTSGVIMVTHQPGVWNLADDICDISAVL", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MAVKIRLRRMGAKKNPFYRIVVADSRSPRDGRFIEEIGYYDPIKKPAEVKIDEAKAQDWLKKGAQLSDTAKSLFVKAGIIPGRAKTNEA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MRTIDKRIAPNVRLAATLVARAPALTLAYDARCKSRLAATLDTGEDVALVLPRGTVLRDGDVLVADDGALVRVAAAHEAVLLVRAPDALTLTRAAYHLGNRHTPVEVGAGCLKLEYDPVLADMLTRLGATVERASAPFQPEAGAYGGGHRHGHDATFAEDYALAQQVFDEHHGHSHSHSHDHDHDHDHDHDHQHGPCCSHGHHHGHR", "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": "MLRLSLPPNVSMGFRLVALVALLFSHVDHITADTEAETGGNETTECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVSSPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPASKTEIEMDGKVVNSHVDNFLDGALVLEVDERDQDDEEARREMARILKELKQKHPEKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNMEMAENDPVSKIFFEQGTYQCLENCGTVALTIMRRGGDLSTTVFVDFRTEDGTANAASDYEFTEGTVIFKPGETQKEIRVGIIDDDIFEEDENFLVHLSNVRVSSDVSEDGILESNHASSIACLGSPSTATITIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIIPYKTIEGTARGGGEDFEDTCGEPEFQNDEIVKTISVKVIDDEEYEKNKTFFIEIGEPRLVEMSEKKALLLNELGGFTLTGKEMYGQPIFRKVHARDHPIPSTVITISEEYDDKQPLTSKEEEERRIAEMGRPILGEHTKLEVIIQESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSSLFVLLWLLYIFFSSLEAYCHIKGF", "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:8659820). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle (PubMed:8659820). In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum (PubMed:8659820). SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:10967099). Required for normal embryonic heart development and the onset of heart contractions (PubMed:10967099). 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": "MNAWNTIYERFNPIAFSLGGIEVHWYGLAYACAIVVAFYMALRMIQKDPKRFPIERKEFESYFLWAELGIVLGARIGYVLIYEPNSSYYLTHFWQIFNPFDSHGNFIGIRGMSYHGGLVGFLIASYLYSRKDLKKLLIYLDLIAISLPLGYVFGRIGNFLNQELFGRIVPKDSHLGQIIGIMVDNELRYPSQLIEAFLEGVVVFLMVMWAKKHTKTHGLLIVVYGLGYSLMRFIAEFYREPDSQLGVYFLNLSMGQILSVFMVIVSLGILLYATKNSKKIKEE", "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": "MKAAVITFPGSNCDRDLATAFEKAGADVTRVWHKDTALPEGVDVVGVPGGFSFGDYLRCGAIAARSPIAAAMIRHAERGGYVLGICNGFQVLTETGLLPGALMRNAGLKFICRRVDLRVATADSAFTSGWAAGDAVRFPIAHHDGNYTADPETLARLRGEDRVAFTYLDNPNGSMEDIAGILSANRRVLGLMPHPERAVEEAQGGADGMGLFRALLGGMALV", "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": "MKIWTSEHVFDHPWEMVTTAAMQKYPNPMNPSVVGVDVLDRHVDPSGKLHSHRLLSTEWGLPSIVKSLIGAARTKTYVQEHSVVDPVKKTMELKSTNISFTNMVSVDERLTYKPHPQDPEKTVLTQEAIITVKGVSLSSYLEGLMASTISSNANKGREAMEWVIHKLNAEIEDLAASARGSIRTPMAAAAALVEK", "text": "SIMILARITY: Belongs to the slowmo family."}
{"protein": "MTYRVCFVCTGNICRSPMAEAVFRARVEDAGLGHLVEADSAGTGGWHEGEGADPRTEAVLADHGYGLDHAARQFQQSWFSRLDLVVALDAGHLRALRRLAPTERDAAKVRLLRSYDPAVAGGDLDVPDPYYGGRDGFEECLEMVEAASTGLLAAVREQVEGRAA", "text": "FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. May be involved in the regulation of sulfur amino acid metabolism. SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family."}
{"protein": "MSIPKELRYSQEHEWVRVEGNTVRIGITDFAQSELGDIVFVELPEVGAQLTANEPFGSVESVKTVSELYAPISGKVVAVNEELNDNPEYVNESPYDKAWMIVIEPSDLSEVDNLLTAEQYEQMINQD", "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": "MSRSESKESRKGREESLEKWVNSRKKVEELERELRKEKKKIKRLEDQNPWLGNIKGILGKKDKDGEGAPPAKRARTDQMEVDSGPRKRPLRGGFTDKERQDHRRRKALENKKKQLAGGGKNLSREEEEELKRLTEEDERRERRVAGPPTGGVNPLEGGQRGAPGGGFVPSMQGVPESPFSRHGEGLDTRGDRGFP", "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. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the hepatitis delta antigen family."}
{"protein": "MPRSQRNDNFIDKSFTVMADLILKVLPTNQKAKEAFAYYRDGMSAQGDGEYAEALENYQEALRLEEDPNDRAFILYNMALVYASNGEHNRALEQYEQALALNAKMPQVLNNMAVIHHHLGSIAQEKGESDEADRRFDLAADFWSKAIRLAPNNYIEAQNWLKTTGRGSADVYL", "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": "MGANTFGKLLAVTTFGESHGPAIGCVIDGCPPGLELAAEEFAHDLQRRATGRSRHTSARREADEVEILSGVYEGRTTGTPIALLIRNTDQRSKDYATIVRQFRPGHADYTYWQKYGIRDPRGGGRSSARETTMRVTAGVVAKKWLKQRYGVIVRGFLSQLGEIRPEGFAWDAIEDNPFFWPHAAQVPALEAYMDALRKSGNSVGARVGVVAEGVPPGWGEPIYGKLDGELAAALMSINAVKGVEIGAGFGSAVQKGTEHRDLMTPLGFLSNHAGGIIGGIATGQPIIVSIALKPTSSLRLPGETVDVDGCAVQVITKGRHDPCVGIRAPPIAEAMVALVLMDQALRHRAQCGDVGEMSPCIPEGVGLRNADD", "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": "MKITLSKRIDLLAFLLPCALALSTTVHAETNKLVIESGDSAQSRQHAAMEKEQWNDTGNLRQKVNKRTEKEWDKADAAFDNRDKCEQSANINAYWEPNTLRCLDRRTGRVITP", "text": "SIMILARITY: Belongs to the UPF0482 family."}
{"protein": "MTFADRLSAYTRLIRLDKPIGILLLLWPTLWGLWLAADGMPDPMILVIFILGTILMRSAGCAINDFADRRIDPHVSRTRNRPLAAGLITAREALLIAAGLSLCAFLLILPLNLLTIQLSVPALFLAASYPFTKRFFAMPQAYLGIAFSFGIPMAFAAQTGTVPPLAWLLVLANLFWVIAYDTEYALVDRADDLKIGIRTSAITLGRFDVAGILLCHIIFLSTLTYAGILLQRGIWFYGALLVALGLVIVQYGMIRKREPSRCFQAFLHNNWIGAVIFAGILLDTLFRTDQSF", "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": "MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRDLIIADNVHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGIGNWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLAERLKFYA", "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": "MDWAIKAARKKTQRKPGSTRSIIETLDDLNNLTTDAHSEINQRLYESSEWLRNNVYMNTLKYEDKKMEESLISPENTHNKMDVEFPKMKGEYELSNSQNDAAKDVTKTPRNGLHNDKSITPKSLRRKEVTEGMNRFSIHDTNKSPVEPLNSVKVDANESEKSSPWSPYKVEKVLRESSKTSESPINTKRFDNQTWAAKEEMENEPILQALKKAESVKVKPPPNSGIARSQRRSNMFVPLPNKDPLIIQHIPPTKSSGSIPKVRTVKESPIAFKKKSTINSPAIRAVENSDTAGSTKASSVFDRLSSIPTKSFENKISRGNVGHKYSSSSIDLTGSPMKKVSQKFKSINSTDTDMQEALRDIFSVKNKITKNNSPKGKNSRKSSIPRFDKTSLKLTTHKKLAIIAEQKKKSKHSSDVHKTGSRPHSISPTKISVDSSSPSKEVKNYYQSPVRGYLRPTKASISPNKNKNLTTSQTPHRLKIKEKTLRKLSPNIADISKPESRKSKNYRLTNLQLLPPAEAERDDLKKKFDKRLSGIMRSQQEHHRRKQEKQKRMSHLEQDLKKQTSFSNDYKDIRLKESLAPFDNHVRDTINKNTAFSTDNILATINTVDHREIIGNVTPKIASVNDSLPEINTDSEDEASVTLAAWAKSPYLQEQLIRQQDINPQTIFGPIPPLHTDEIFPNPRLNRLKPRQIVPKRS", "text": "FUNCTION: Required for high-fidelity chromosome segregation during the later part of each cell cycle in association with the protein kinase IPL1. Stimulates IPL1 kinase activity and facilitates its association with the mitotic spindle. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Note=Associates with the mitotic spindle and the kinetochore (PubMed:11724818). SIMILARITY: Belongs to the INCENP family."}
{"protein": "MERLLVLVRHGQSEWNLRNLFTGWRDPDLTERGVAEARAAGRGLKRDGYGFDVAFTSALIRAQRTCALVLEEMGLSEIPILRERALNERDYGDLSGLNKDEARARWGDAQVHAWRRGYDVRPPGGESLKDTAARVLPCYVATILPRVMAGQRVLVAAHGNSLRALVMVLDGLTEAQVPDLQIRTGVPLVYRLNADTTVASKTVLDQDVDAGR", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
{"protein": "MSGPITLPTLRMMLDYVDTPVLVKLKSGLRIKGVLKTYDQHLNIILGDAEEIGETSIRRLGLTLVRGDSVVVITPAA", "text": "SIMILARITY: Belongs to the snRNP Sm proteins family."}
{"protein": "MEQFKGLQKSLYIWTDNAELDKRVEQLKTATGGEVALENVHRLSFASYASSSFDLIVIECAQLTDNYVKLLHMLKPSGKLHLISFIGAAGSLLQEIKLSGFINCSEDSDNTLTAEKPGYETGSSARLSFAKKNSSTLNVWKISGDDDELIDEEDLLDEVDKQKPDPASLKVCSTTGKRKACKNCSCGLADELENEKKQENAAKQASTENAKSSCGNCYLGDAFRCSSCPYLGMPAFKPGEKVQLVDNLLKSDI", "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": "MSDKPAYLTRDGRARLEAELEELVTKGRKEIAERINAAKELGDISESGEYEDAKNQQAHLEGRIREIKSILARAQIIDEENGSNHEVRIGSRVTVRIDGEHEEETWTIVGSTEAKPSEGKISNESPIGAALLGKRPSQQVTVETPSGTMKLTILNIQ", "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": "MMRQGGVMVGARKRWITDWWPNRLNLKILRQNLQNPYGEDYDYVEEVENLDIDAVIRDLKELMRSSQDWWPADFGHYGPLFIRLAWHSAGSYRIFDGRGGARDGSIRFPPRINWPDNINLDKAIRLLWPIKKKYGRKLSWADLIILAGTVAMEDMGVKLFGFALGREDIFEPDESPDWGPEEEMLTAKRGEKEELERPFAATEMGLIYVNPEGPGGNPDPLGSAQEIRVAFRRMGMNDEETVALIAGGHAFGKCHGAGPADYLGPDPSSSPIEMQGLGWKYNYGKGKGSDTFTSGLEVTWSPTPTKFGINYLRILFTYEWELEKSPAGKNQWVAKDAPEIIPDAHDPNKKHRPRMLTADLALRFDPEFSKIARRFLENPEEFEKAFAIAWYKLTHRDMGPKDCYIGKYVPEETFVWQDPLPRRDYELVDEKDVEELKRRILASGLSLSQLVYFAWASASTYRNSDRRGGANGARIRLKPMSVWEVNHPEELKKVIAAYEKIQQEFNEGAKGSEKRISIADLIVLGGIAAVEEAARRAGFSVKVPFIPGRVDAQQEHVDEEFYRVIEPFADGFRNYFRYPERINERDVYTTPEYFLVDKANLLTLTVPEMVVLIGGMRALGANYSHSDYGVLTERPGVLSNDFFVNLLDMSVEWRAADDYRYTFEGYDRKSGELRWRATRVDLILGHHDELRAVAEVYGCDDAKEKFVKDFAAVCAKVMHLDRFDLWRSNRKLYKEITAGLR", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Also displays NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activities. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MASPLSPGSRILIGLVRAYQLVISPLLGPRCRFQPTCSHYAIEALSRFGMIKGSWLALKRVLKCHPLNPGGDDPVPPKPDDNREH", "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": "MSITTTRRRNQDSVCCKATRASIKVEAVSGQTVFEKQKLLHNFDELPEWQKDNDKILTGYVRETLSWKKCLYSLFYWNNETVNIYTHLVPAIVYFVFAITLTNYFLIPVFPSTSWSDYTVINIFLMGAFSCLMCSSCFHCMKQHSEKQSNFWSKLDYLGIISLISCSMIPIIYFGYFDHISYFSLFTIVTLVLATFCTVCVLHDKFNTSTFRPFRAMFFILFGFSGLLPLTTGFFKFGIQGVLNRIKVSFVFWEALFYISGAVIYGFRIPETLAPGKFDFFGSSHQIFHIMVVLGSVCHLKAIIDSYKLMHSHIHP", "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": "MTKNLLVELGLEELPAYVVTPSEKQLGEKMAAFLKGKRLSFEAIQTFSTPRRLAVRVTGLSDKQSDLTEDFKGPAKKIALDSDGNFTKAAQGFVRGKGLTVEDIEFREIKGEEYVYVTKEEIGQAVEAIVPGIVDVLKSLTFPVSMHWAGNSFEYIRPVHTLTVLLDEQEFDLDFLDIKGSRVSRGHRFLGKETKIQSALSYEEDLRKQFVIADPCEREQMIVDQIKEIEAKHDVRIEIDADLLNEVLNLVEYPTAFMGSFDAKYLEVPEEVLVTSMKEHQRYFVVRDQDGKLLPNFISVRNGNAERLKNVIKGNEKVLVARLEDGEFFWREDQKLVISDLVEKLNNVTFHEKIGSLREHMIRTGQITVLLAEKADLSVDETVDLARAAAIYKFDLLTGMVGEFDELQGIMGEKYTLLAGETPAVAAAIREHYMPTSAEGELPESKVGAVLAIADKLDTILSFFSVGLIPSGSNDPYALRRATQGVVRILDAFGWHIAMDELIDSLYALKFDSLTYENKAEVMDFIKARVDKMMGSTPKDIKEAVLAGSNFVVADMLEAASALVEVSKEEDFKPSVESLSRAFNLAEKAEGVATVDSALFENDQEKALAEAVETLVLSGPASQQLKQLFALSPVIDAFFENTMVMAEDQAVRQNRLAILSQLTKKAAKFACFNQINTK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MYIMKQSGWLEVICGSMFSGKSEELIRRVRRATFAKQEVKVFKPTIDNRYSDEAVVSHNGNSLIAIPVSSPKEIFEHISEKTDVIAIDEVQFFSDDIIDVVQTLADRGYRVIVAGLDQDFRGEPFGPVPTLMAIAESVTKLQAVCTVCGSPASRTQRLINGVPASYYDPVILVGASESYEPRCRHHHEVPDKPTKNGQTNNHLAR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thymidine kinase family."}
{"protein": "MLVPKRVKHRREFRGKMRGEAKGGKEVSFGEYGLQATTSSWITNRQIEAARIAMTRYMKRGGKVWIKIFPHKSYTAKAIGVRMGSGKGAPEGWVAPVKRGKVMFEVAGVSEEIAREALRLASHKLPVKCKFVKREAE", "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": "MKKLKASEIRQKYLDFFVEKGHMVEPSAPLVPIDDDTLLWINSGVATLKKYFDGRETPKKPRIVNSQKAIRTNDIENVGFTARHHTFFEMLGNFSIGDYFKQEAIEFAWEFLTSDKWMGMEPDKLYVTIHPEDMEAYNIWHKDIGLEESRIIRIEGNFWDIGEGPSGPNTEIFYDRGEAYGQDDPAEEMYPGGENERYLEVWNLVFSEFNHNKDHSYTPLPNKNIDTGMGLERMASVSQNVRTNYETDLFMPIMNEIEKVSGKQYLVNNEQDVAFKVIADHIRTIAFAISDGALPANEGRGYVLRRLLRRAVRFSQTLGINEPFMYKLVDIVADIMEPYYPNVKEKADFIKRVIKSEEERFHETLEDGLAILNELIKKAKATTNEINGKDAFKLYDTYGFPIELTEEIAVQAGLKVDMTTFESEMQQQRDRARQARQNSQSMQVQSEVLKNITSASTFVGYDTATAQTTLTHLIYNGEEVSQVEAGETVYFMLTETPFYAISGGQVADTGIVYNDNFEIAVSEVTKAPNGQNLHKGVVQFGQVNVGATVSAEVNQNDRRDIQKNHSATHLLHAALKSVLGDHVNQAGSLVEADRLRFDFSHFGPMTNDEIDQVERLVNEEIWKGIDVNIQEMDIASAKEMGAMALFGEKYGDVVRVVNMAPFSIELCGGIHVRNTSEIGLFKIVSESGTGAGVRRIEALTGKAAFLYLEDIQEKFNTMKSQLKVKSDDQVVDKLTQLQDEEKALLKQLEQRDKEITSLKMGNIEDQVEEINGYKVLVTEVDVPNAKAIRSTMDDFKSKLQDTIIILASNVDDKVSMVATVPKSLTNNVKAGDLIKQMAPIVGGKGGGRPDMAQGGGTQPENISKSLSFIKDYIKNL", "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": "MTSTLPNASTPDPSSLQPAVRPGAHGRFGRFGGQYVPETLMPALAELEQAAAQAWNDPAFTDELNRLLKNYVGRATPLYEAERLTAHYRRADGGPRIWLKREDLNHTGAHKINNALGQALLALRMGKKRIIAETGAGQHGVATATVCARFGLECVIYMGAEDMRRQALNVFRMRLLGATVQPVTAGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMLVRDFHAVIGEESKQQCQEAFGRLPDVLMACVGGGSNAMGLFHPFVQDMSVRLIGVEAAGDGVASGRHAATITEGRAGVLHGAMSLLLQDGDGQVMEAHSISAGLDYPGVGPEHSYLREIGRAEYAAVTDQQALDALRLVSELEGIIPALETAHAFAWLEQLCPTLADGTEVVINCSGRGDKDVNTVAEKLGDQL", "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": "MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTNMPWFKGWKVERKEGNADGKTLIDALDAILPPARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYVAGDSKANPPKGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKDASGGKVTKAAEKATKGKK", "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": "MARRPSTDDLRSGPERFMALVKTTVPPVHPAGLPFIGASLALAAAGRRNRWVRGAGLVAAGANAAFFRHPPRVPPTRPGVVVAPADGLICLVEDAEPPAELNLPARPVPRVSIFLSIFDAHVQRIPISGEVVAVEHRPGLFGSAELAAASEDNERNSVVIRTDTGAQVIAVQIAGLVARRIVCDLTTGDKVTIGDTYGLIRYGSRLDTYLPEGTDIQVLPGQRAVGGETILAELP", "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": "MGSAAELTEPTTGTEKLHQPIEVEEDDEQIVDLERKTFRHGKGHDTSVDSSTITNTSSSSSSSFSGDGGTEETPDFHSNGDGEHTDLVNLEVPELETEIVFHQEHDDGKNCIVFFDGEQGSESAGAIPDAHEESQTADLNGEQTQLEPENGSTSEDNERSREIEEVLDGDVSKDLDAVDPLAGEVIEEEVDFEDVEYHDVENMMDKQETHDLYCPNCDSCITKKVILKRRKRKIRRHELGDSKRPHLTEPLFHSEDNLPSLDGGENSANESFVFKCLSCFTIFIPKGVSSKPIPPRQGVEGLKIQPNPQVEATGDSNWFSSIFGLNKKESAIQQGGASSSVLEANPPPRESIVPVVNPSRGNLSPMRKDTTGSAVVQPDAATSIQVAKSNDTSEIVNNGAIVGDGQKFLAPMVEEQTQQKIDNDDSSTADGNHTSDKGRLSPIQPSHGMSILNTVTNGPDGLKVETTIHEEGAPLLFEGKDTPDTSTADFGLTKVTGVMDTGDRGVITGPANPEIDISAGNLLEEGSLREPLMRRVVVQGRKLEILKSIVYGGLLEAITSLGVISSAAGSGASMLNILVLGLANLLGGLILIIHNLQELREEEPIRTTTEDNQTNGREEEEGRYKRLLGRRENFTLHATVAILSFIITGILPPVVYYFSFSEKHNKDYKVASVFGASLFCIVLLAIAKAHVRYPRGSYLKSILYYGSIAVSVSGISYVVGNFLEQLLEKHGWSDGSETPVGQMMLSSLMGRKAGFGYSSSY", "text": "FUNCTION: Not essential for the accumulation of ER body components, including PYK10. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CCC1 family."}
{"protein": "MNVTLFVTCLVDLFHVNVGKATVELLERLGCTIHFPEAQTCCGQPAYNSGYVKEAKEAMKHMIRTFEHAEYIVTPSGSCATMFKEYPHIFKGDGEWEARAKRVADKTYELTQFIVDVLQVEDVGARLEGKATYHTSCHMTRLLGVKDAPLTLLQHVKGLEVVPLPNAHNCCGFGGTFSVKMGPISEQMVDEKIQCIEQVEADYLIGADCGCLMNIGGRIERKGKPIRVMHIAEVLNHR", "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": "MVDLSFNATVFMQMFHFLLMLVVLRLFAYRPLMNVIEQRQAYIADEIEAAEKQKAAAAELRSQLEADLAKAREEAKAIVARATKASDEQAQAIMEQARTEAQRLKEEALAEIGREREKAIAQLKDEVASLAVLVAAKVVKDGLTIDAQHNLVQNAIKEVGQLQ", "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": "MRIAKIGVIALFLFMALGGIGGVMLAGYTFILRAG", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0387 family."}
{"protein": "MSRQFSSQSAFSSRSRRVYSTRSSSGFGGGRQILVSVGQSRRCGGDYGGGFSSRSLYSLGGSKSIFGGLVGRSASGFCQSRGAGGGFGGGFGGGRSFGGGGFGGGYGGGGRFGGGFGGGFGTSNFGLGGFGPSYPPGGIHEVTVNQSLLEPLHLEVDPEIQKIKTQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTSSLEPIFEEFINQLQRQVDVLTNEQLRQNSEIRSMQDIVEDYKNKYEDEINKRTNSENDFVVLKKDVDAAFMAKSDLQSRVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIINAVRTQYELIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNAQRLQAEIANIKKQIEQMHGSISDAEERGERALQDAKQKLQETEEALQQMKEDLARLLRDYQALLGAKLSLDVEIATYRELLEGEESRMSGALQSQVSIWALPSNEGNDLGERLHDPQSQVPVPKLGC", "text": "SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MAGNDTCNNSCDVKTARLWRDAALRSRKLRSSLRQLTLSCVDKRKLILPADLGDVEVLNLGNNSLEEVPDGLQSLSAGNLHVLILRRNKFLNVPTAVYHLGRLTELDISYNRLSCLTEAVGLLGKLKKLCLSHNQLRTLPRQLGMLVDLEELDVSFNQITHLPDTMQGLPSLRTLDLDHNELCSFPQQLFHVPALEELDFSGNKMLGSLPEGIRSMQSLKILWLSSTSLCLLPDSICELVNLESLMLDNNNLHTLPEGFGALQKLKMLNVSSNAFQDFPVPLLQLVDLEELYMSRNRLVVLPEVISCMTKLVTLWLDNNRIRYLPDSIVELSFLEELVLQGNQIAILPDDFGKLSKVNIWKIKDNPLIQPPYEVCMKGISYIAAYQKELAHSQPAVKPRLKLVLLGLKDAGKTLLRQCLTDEQNTSTLVQGYKGIEITNWTADAERGLAFIVYDLAGDQSYDIIKPFFFSPGALYILVVNLKSYVCKHFYTHVGYFIHLITSKVPHAVVCIVGTHIDLCNEKELEEKCLDIHHQIAVQEKRDSETLQTLIQTVDKALSQDFDFRASNPHSAFYGVSDKNLRRKKTHFQYLMNSRLQILSPVLCVSCLDFSNIKRLREKLLSVAEHREIFPNLHRVLPKSWQMLEELHFKPQELWLTWWDSARLGLQAGLTEDRMQSALSFLHESGKLLYFEDNQTLKEYVFHNLTKLIDILNVFFQRDASVLFAKLTSDATADETKVTQFHHYVEGFLLHGLLPTHIIRSLLKPHIKTHQDLQLILELLEKMGLCYCINKPKNKLLNGATVWYKFPCYVKNEAPHAEAWINGTNISEPCLAVEQLQIEYSFPFIFPPGLFARFSVQINSHIVHRSDSKFQIFAYRGKVPVVVSFQPARGALQPGILSIASHASLPNIWTAWQAITPLVEELNALLQEWPSLYYTVHVLCSKCLKRGSPNPHPFPGELLSQPRPDGVTELICPKNGSERLNVSLVYPPTPTMISPCSK", "text": "FUNCTION: Probable GTP-binding protein. Functions in innate immunity and more specifically the inflammatory response as a regulator of the Toll-like receptor TLR2 and TLR4 signaling pathways. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSDSDSDSDYELTLSANALAALEEFKREEQQHQEAFQKLYDETDEDFQKKKKEEGMKLFKEDWQLSQFWYSDDTAAILADAILEGADENTVIAIVSAPSVYAAIQKKPTNEIPTEHIYLFEFDKRFELLAGRDHFFFYDYNKPLDFSDEIKGKVDRLLIDPPFLNEDCQTKSSITAKCLLAPNDNSKTKKGVFKHRLISCTGERMSEVISKVYSDTRITTFLPEHSNGLSNEFRCYANFECSSWKFAS", "text": "FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-79' (PubMed:25446118). Required for replication of Brome mosaic virus (BMV) (PubMed:14671320). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family."}
{"protein": "MNAQPLLPRIQSPADVRRLSRAELKQLADELREFVLQSVSRTGGHLSSNLGTVELTVALHHVFDTPEDRLVWDVGHQTYPHKILTGRRDRMSTLRQLGGLSGFPRRDESEYDTFGTAHSSTSISAALGMALAAQQKGEKRHAVAIIGDGSMTAGMAFEALNNGGMPHAGRVPNLLVILNDNDMSISPPVGALNKYLARLLSGRFYAAAREGAKSVLKSAPTLFELARRFEEHAKGMVVPGTIFEEFGFNYVGPIDGHDLDALIPTLENLRDKPGAQFLHVVTKKGYGYKLAEADPIAYHGPGKFDPQIGLVKPATPPKTTFTQVFGQWLCDMAAADPKLVAITPAMREGSGMVEFHKRFPERYHDVGIAEQHAVTFAAGLACEGLRPVVAIYSTFLQRAYDQLIHDVALQNLPMVFALDRAGLVGADGATHAGAYDIAFVRCIPNMSLLAPADEAETRRALSTAFAHDGPVAVRYPRGSGAGTAVETGFETLPWGRGEVRRQAGGHVRGPRIAILAFGTLLYPALAAAEKLDATVANMRFIKPLDAALVEQLARTHDALVTVEEGCLMGGAGSAVLEALQAAGLQTPVLTLGLPDQFIEHGDPALLLAACGLDSAGIEAAIQKRFCASAPSHLRPVANG", "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": "MSVLALDVARDVAAPRRAEILETLRALADGADATTREIASDDDADALERASCDAYFARARDASEARRACARASEKLRAGGALGVVVDDERTATATTEAMVLAGFTTVTREDDGVVRCVKPNWARGTAFALKSRAVRVNATAADAADAWGASAAADDDELIDESALLTELDVNTAPVKYDDCDVGAGKKACKNCTCGRAEAEAAEEATTAASEETFVSACGNCALGDAFRCAGCPYLGQPAFKDQPGTKVELDLGDDL", "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": "MEPPMEQSGGEQEPGAVRLLDLPWEDVLLPHVLNWVPLRQLLRLQRVSRAFRALVQLHLARLRRFDAAQVGPQIPRAALVRLLRDAEGLQELALAPCHEWLLDEDLVPVLARNPQLRSVALAGCGQLSRRALGALAEGCPRLQRISLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAQRRGAGLRSLSLAVNANVGDTAVQELARNCPQLEHLDLTGCLRVGSDGVRTLAEYCPALRSLRVRHCHHVAEPSLSRLRKRGVDIDVEPPLHQALVLLQDMAGFAPFVNLQV", "text": "FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation. Also mediates ubiquitination of SMURF2 and WWP2 (By similarity). Required for bone mass maintenance. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBXL15 family."}
{"protein": "MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEALMEWLKTRPILSPLTKGILGFVFTLTVTSERGLQRRRFVQNALNGNGDPNNMDRAVKLYRKLKREITFHGAKEVALSYSTGALASCMGLIYNRMGTVTTEVAFGLVCATCEQIADSQHRSHRQIVTTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAERMEVASQARQMVQAMRTIGTHPSSSAGLKDDLLENLQAYQKRMGVQIQRFK", "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": "MEPEAFEICPYDPHHRIPLSRFQYHLASCRRKNPKKAKKMATCKYNACHVVPIKNLEEHEAVCVNRSAVEEEDTENPLKVSPPSSEQNDDTQQVSPCLPSPDIWNVDGANCQHVFVLKTFFPQKVVCENDTKESARETSPQKILRPGQ", "text": "SIMILARITY: Belongs to the UPF0224 (FAM112) family."}
{"protein": "MSGKPQSPENQARQLIVAYQQYQAEAESLVRELGLIQMTAEGLDKAISAIGALSKAAEGQEMLVPIGSGSFAYAKLSSADRVVVNVGGGVSIEKPAEEAMEMLRARRSAISESSKKINEALAKIEQEMARIQAALERLERELQKQGGSEGFVQ", "text": "FUNCTION: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit alpha family."}
{"protein": "MELKIDTHSHTYASGHAYSTLIENARSAKENGLAMFCTTDHAESMPGAPHYWFFANQRVLPRFLEGVAILRGVEANILNTEGEIDLPLSVDPNLDWAIASFHEPVFAPSNKEAHTQALLNVIQGGRIDALGHLGNPHFDFDFHAVLHCAKEHNVAIEINNSTLKGHSRVGSVERCYEIARVGKALGVYFTTGSDAHFCQDVGKLDLASELLDSVGIDSHRVITHSPSQFLDFLELRGRGPIDELASLRQ", "text": "SIMILARITY: Belongs to the PHP family."}
{"protein": "MSTNKITFLTNWEATPYHLPIFLAQTRGYYEREGIEVAILEPTNPSDVTALIGSGKVDMGLKAMIHTLAAKARGYPVTSFGSLLNEPFTGLITLKGNGINDFKDIKGKRIGYVGEFGKIQLDDLCSKFGLSPSDYTAIRCGMNIAPAIINGEIDGGIGIECMQQVELERWCVSQGRPRSDVQMLRIDRLANLGCCCFCTILYIAHDEFIAKHPDKIKAFLRAIHSATLDMLKDPVQTYKEYIHFKREMGSELHREQFERCFAYFSHDISNVPRDWNKVTNYSKRLGIIPQDFEPNCTNGYLTWELDPDEKDPMGKQEAIAEIQDEIKQKGGVFSGNSLRYVEPANL", "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. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the NMT1/THI5 family."}
{"protein": "MKKQFLNYYEILSQVWFNKYTIILVLMTIKIYLFTNSILSNLTNFKAYTESICTSLDTYSTVIASLPEQLSKVINHMVASTLNSMKMQSLKMLMTIITIIKSLIVFYIDIFLGTYICILTAAIGGTVDFALDSTQSVLKSVNETIISVSEDIQDGLNGLSKVINTLLSGVDKVKSFFTNQDTDSTEYVDKVNLSIKALQNIKIPNSVLTDIDNFKDKVPDFNELQNTSKLVSKPFEIITQELNESAHFKNITVDQLKLASTPPVNFCSNSLDIDKFYSNLAKKVQFTSNIIIIVLLIMAMFAIASLVVVEYFKWRKSQRMINEILADKNQESYFVSTRNIMNKYNSSLIYYIEKFVTIPPSRKDNLYWLLSYITTPYSLTVLIIGLAGLFTVMLQFIILQIILKSFKSLTTELTGFKTQIITLMDNATSSYIKETNSYIGSQQKSINDELFGNIRTASTSVNSTINDFLMKMNTTINSVFANTPFSKPVNTLVYCTIGRKLIKIEQGLTWIVENLSVSLPQLPKNLTEDFMTNYSKDNHGIHKLTDNVTSGITFLLDTYKKSLLIELYISSAILGIWILQIIIGLTLIWYRSSSNCKARKPEKIQGEPTIGNPKPLTTEQRKEYGYPHIDPFNEKVDASSSIYSL", "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": "MPSQPSKTLETFDNPRPDHDYTIRIEIPEFTCLCPKTGQPDFATILLEYVPDRQCIELKSLKMYIWSFRDEGAFHEAVTNTILDDLVTVSRPRFMRVTARFNVRGGIYTTVVAERRAPDWEPTTPVALP", "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": "MKHAYIVDAIRTPFGRYAGGLAAVRADDLGAIPIAALIERNPSVNWAQVDDVIYGCANQAGEDNRNVGRMSALLAGLPVEVPATTVNRLCGSSLDAIAMAARAIKAGEAHLIIAGGVESMSRAPYVMGKSEGAFGRTQKIEDTTMGWRFINPKLKAMYGVDTMPQTAENVAEQFGIQREDQDQFAYTSQQRTAAAQAKGYFAKEIVPVTIPQRKGEPVVIATDEHPRASTTLEGLAKLKGVVKPEGSVTAGNASGINDGAAAVLIASDEAVAQYQLKARAKIIASTTVGIEPRIMGFAPAPAIKKLLKQANLTLDQMDVIELNEAFAAQALACTRDLGLADDDARVNPNGGAIALGHPLGASGARLVTTALNQLEQSGGKYALCSMCIGVGQGIALIIERV", "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": "MVLFGVLTMILAIALFSLRIPAIYFNRITIILLLFSALLSYNSLYMNNIGSGVGVFGGLFQVTTITQSIDVFIYLLGALVLLLSEKANRANTLSFNKLNSTLVNKSKGLSVLAEYPLIALFSVLGMSSLISSSDLISMFLSIELQSFAVYILATIYRESESATSAGLKYFLLGSLSSALILLGSSLLYSFTGLTSFEGLYMLCSTTETNTAIEISVLLIMVGLLFKVSAAPFHNWAPDVYDGVPTVVTTWLTTMPKIAFLVFILEFQGFTQLANWSSWTNLLLISSLLSLLIGTIGGLAQYRIKRLLTYSTISHVGFLLLALAINNEESVESFLFYLIQYSLTNINVFFILVAFGYLLGSKGLSIYSPIQLINQLKGQFKVNPLLGLSLAICLFSMAGIPPLVGFFGKQMVLYAATHNGNFFLAFVAILVSVVSAAYYLRIIKVIHFDPVPAPSALSLIKTTEISSDLNVTETNNSLEGSSEELSTSSSLVIATITLLLIFFIINPTPLLNSVHLITLNLFYW", "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": "MKLSMPRFDQAPVLVVGDVMLDRYWHGGTSRISPEAPVPVVKVDQIEDRPGGAANVALNIAALGAPAALIGVTGQDEAADSLANSLQAAGVRSVFQRIAHQPTIVKLRVMSRHQQLLRIDFEEPFATDPLSLGAEVESLLEGVKVLVLSDYGKGALKNHQSLIQAARAKGIPVLADPKGKDFSIYRGASLITPNLSEFETIVGRCADEAELVAKGLQLLLDLDLGALLVTRGEHGMTLLRTGQPALHLPARAREVFDVTGAGDTVISTLAAAIAAGEDLPHAVGLANLAAGIVVGKLGTAAISAPELRRAIQREEGSERGVLGLEQLLLAIDDARAHNEKIVFTNGCFDILHAGHVTYLEQARAQGDRLIVAVNDDASVSRLKGPGRPINSVDRRMAVLAGLGAVDWVISFPEGTPENLLSQVKPDVLVKGGDYGIDQVVGADIVKGYGGTVKVLGLVENSSTTAIVEKIRKN", "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": "MHNGSNGSVEQRDSMPETSREWWPGSLDVEILDQNAQDVGPWNGDFDYAEAFQELDYEALKEDIEEVMTTSKDWWPADYGHYGPLFIRMSWHAAGTYRTTDGRGGSSGGRQRLAPLNSWPDNANLDKARRLLWPVKQKYGRKISWADLLVLAGNVAMESMGFETFGFAGGREDDFKPDESIDWGPEDEMETWGRFNEEDELDNPLGATVMGLIYVNPEGPESTPDPEWSAQRIRKSFGRMAMNDRETAALIAGGHTFGKVHGADTDEHLQAEPEAAPIEQQGLGWHNEHGSGKGGDTITSGIEGPWTDAPTEWDMGYLDFLLDYEWEVHKGPGGAWQWRPKSDELKGVVPDAHDASETVDPMMLTTDVALKRDPDYREIIEDFRENPDAFEDAFARAWFKLLHRDMGPKERYLGPEVPEEDLIWQDPVPDADHDLIGDEEIAELKEAILETDLSVSRLVKTAWASASTYRDSDKRGGANGARIRLEPHRNWEANEPPQLAHALEVLTGIQKNFNDARTDDVRVSLADLIVLGGSAAIEKAAADAGHDVEVPFTPGRTDATQEQTDVEAFEYLEPKADGFRNYIADDPWQDWTPEEFLVDKADLLNLTPAETTVLVGGMRALDATHEQADGYGVFTDRPETLNNDYFVNLLDMGHEWDPVSEDKQHFKIRDRDTGEVKWKATRVDLIFGSNSRFRALSQVYGSGDAEEKFVDDFVDAWTKVMNLDRFDLE", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQNRIKEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFVGWKCQGWPVMTIVGGKIAWQKESALV", "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": "MTNTPSSAPSPLTYRDAGVDIDAGNELVERIKPLVKRSFRPEVMGGLGGFGALFDLSNKYREPVLVSGTDGVGTKLKLAHQLNRHDTIGIDLVAMCVNDVLVQGAEPLFFLDYFATGKLDIDTAAAVVGGIANGCTEAGCALIGGETAEMPDMYAPGEYDLAGFTVAAVEKSELKDGASVAAGDVLIGIASSGPHSNGYSLVRRIYDRAGRPAELELEGGVKLVDALMAPTRLYVKPILSLLKSHGAAIHGMAHITGGGLTENIIRVVPEGLGLDIQASSWTLPPVFQWLQKEGAVADSEMWRTFNCGIGFVLIVAPDQVAAVSEAVKAQGLDHWTIGQVVTAEGAERVHIG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
{"protein": "MAAPQGGYPPQEGYGQPAGYESPSQQAAGLAPAPAQHGGRKKRAYAGEAFELGSGANAGLGGQLPAGGTYGGYPAQPQAAGYQQPVYGADPTQMQAAAQGYAAPAAPAVAQMTQQFGAMGVTDPHLMPPQPVPQAAQAPRPVLNHLYPTDLLTQPFNVAELDYPPPPIVLPQGTSVYPSPTANCPPKYVRSTLNAVPTTHSLLKKSKLPFALVIQPYGALHDSEDQVPVIPDQVISRCRRCRSYINPFVTFLDHGHRWRCNMCNLTNDVPQAFDWDTTLQRPADRALRPDLNHAVVEFVAPQEYMVRPPQPLVYLFLIDVSYASVTNGLLATSARCIKESLERIPNADRRTRLGFIAVDSSLHYFSIPRDGSENSDPRMLVVSDLDEPFLPIPGDLLVTLSECRENIETFLDKLQEMFQNTQNNGCAMGSALRAGYKLIAPVGGKMTVLSSSLPNIGHGALTMREDKKVLGTSKESGLLQTANSFYKSFAVECSKAQVSVDMFLFSSQYQDVASLSNLPRYTGGQTYFYPGWNAARGEDAIKFAREFSEYLSSEIGLEAVLRVRATTGLRMSTFYGNFFNRSSDLCAFPAFPRDQAYVVEVAIDETVTKPVVCMQTAVLHTTCNGERRIRVLTLALPTTQSLADVYASADQQAIATYFSHKAVERALGSGLEPAREALQAKAVELLATYRKELAGGSVSGGGLQFPANLRGLPVLFLALIKNLGLRKSAQIPTDMRSAALCLLSTLPLPLLIQYIYPKMYSLHDMPDNAGLPDEQTGEIVLPPPVNLSSERVVPYGLYLIDDGQTQFLWVGRDAVPQLIVDVFGLPDKSQLRVGKQNLPDLDNDMNQRVRAVIEKSRDHRSKGCGSIVVPHLYVVKEDGEPGLRLWAQTMLVEDRADQGVSLVQWMGNLQEKV", "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": "MAVVIDGKAKAASVTEAVRKSAEALEAEKGVKPGLAVVIVGNDPASHAYVNSKSKMAKQCGFNSIQHTLPEETTQAALLKLVGELNTDASIHGILVQLPLPKHFNSDEIIQSILPEKDVDGLSVLNAGKLATGDLATGLISCTPAGAMLLVRGIHGDDLSGLNAVVIGRSNLFGKPMGQLLLNANATVTMAHSRTKDLVTVCKTADILVAAVGRAAMVKGDWVKPGATVIDVGINRIAAPEKGEGKSKLVGDVAFDEASAVAAAITPVPGGVGPMTIAMLMANTVIAAHRALGKTAPKF", "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": "MRFFAVLLVPLVFAEICPMDKHAICNTGHLSCTCSVSQEDEAPVPEISCNALIARDLETGNFPVVSVEFDLNNSAEALEEFPEDAFRDKISSSLRVDEEDVIVLRTSCVGTDDTLTIQFVILKKDTNSSALPFAIEDLIDAESIATRMKAMGHLSQIANLDVDTIEYTEELVDLEFEPSNLELIFKAILLALIFGFFFVLGVWKLTKKGDEYADDLQKP", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MERSPFLLACILLPLVRGHSLFTCEPITVPRCMKMTYNMTFFPNLMGHYDQGIAAVEMGHFLHLANLECSPNIEMFLCQAFIPTCTEQIHVVLPCRKLCEKIVSDCKKLMDTFGIRWPEELECNRLPHCDDTVPVTSHPHTELSGPQKKSDQVPRDIGFWCPKHLRTSGDQGYRFLGIEQCAPPCPNMYFKSDELDFAKSFIGIVSIFCLCATLFTFLTFLIDVRRFRYPERPIIYYSVCYSIVSLMYFVGFLLGNSTACNKADEKLELGDTVVLGSKNKACSVVFMFLYFFTMAGTVWWVILTITWFLAAGRKWSCEAIEQKAVWFHAVAWGAPGFLTVMLLAMNKVEGDNISGVCFVGLYDLDASRYFVLLPLCLCVFVGLSLLLAGIISLNHVRQVIQHDGRNQEKLKKFMIRIGVFSGLYLVPLVTLLGCYVYELVNRITWEMTWFSDHCHQYRIPCPYQANPKARPELALFMIKYLMTLIVGISAVFWVGSKKTCTEWAGFFKRNRKRDPISESRRVLQESCEFFLKHNSKVKHKKKHGAPGPHRLKVISKSMGTSTGATTNHGTSAMAIADHDYLGQETSTEVHTSPEASVKEGRADRANTPSAKDRDCGESAGPSSKLSGNRNGRESRAGGLKERSNGSEGAPSEGRVSPKSSVPETGLIDCSTSQAASSPEPTSLKGSTSLPVHSASRARKEQGAGSHSDA", "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. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (By similarity). Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cell membrane; Multi-pass membrane protein Cell surface Apical cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with FZD3 at the apical face of cells (PubMed:16495441). Localizes to the endoplasmic reticulum membrane in the presence of LMBR1L (PubMed:31073040). SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family."}
{"protein": "MSEENTTNNEAAAAEGKAPAGFGIKRVFTKDLSFEVPAGLGAFSLQGQPNVGQDLNTQINRVDDTHYEVVLKVTVTVKMGEDKVAFLAEVHQAGIFQVVGIEGPQLQQVLSTACPQILFPYVRETIDSLAVRGGFAPVLLPQINFDALFVQAVAQAKAQADSQAEADA", "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": "MAKAHKDVKKIVLAYSGGLDTSIILKWLKNEYGCEVIAFSADLGQGDELAPIRDKAIATGADKVYIDDLKEEFVKDFVFPMFRANAIYEGHYLLGTSIARPLIAKRQMEIAKIEGADAVSHGATGKGNDQVRFELAYYHFDPAITVVAPWREWKLNSRQALVNYARKNGIPIPVTKKRPWSSDRNLLHISFEGGILEDTWAEPPENMYVLTKAPEKAPNKPQFVEIEFKNGNAVAVDGEKMSPAQLLAHLNYIGGEHGIGRVDLLENRSVGMKSRGVYETPGGTILREAHSAVEQITMDREVMRIRDSLIPEYARQVYAGYWFSPEREMLQTLIDDSQKCVNGVARVKLYKGHCRTVGRKSETNSLFNLDFATFEKDQVFNQADATGFIKINSLRLRIRSLMQGKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
{"protein": "MRRRKAPVREVMPDPIYGNKIITKFINSLMYDGKKSVATEIMYGALKTIDAKGGDLKGINVFNDAIDNVKPIMEVKSRRVGGATYQVPVEVRPARQQALAIRWIISFARKRSERTMMEKLAAELLDAANSKGASFKKKEDTYKMAEANKAFAHYRW", "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": "MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGVVEYAGEIVLARDAEPEHDPGLVLRVAAASADTGLPIGAATLSRLAASVPDLPTPWPQEALDDLLVVLSAGPTTVATIEALDRTGLWGRLLPEWEPIRDLPPRDVAHKWTVDRHVVETAVHAAPLATRVARPDLLALGALLHDIGKGRGTDHSVLGAELVIPVCTRLGLSPPDVRTLSKLVRHHLLLPITATRRDLNDPKTIEAVSEALGGDPQLLEVLHALSEADSKATGPGVWSDWKASLVDDLVRRCRMVMAGESLPQAEPTAPHYLSLAADHGVHVEISPRDGERIDAVIVAPDERGLVSKAAAVLALNSLRVHSASVNVHQGVAITEFVVSPLFGSPPAAELVRQQFVGALNGDVDVLGMLQKRDSDAASLVSARAGDVQAGVPVTRTAAPPRILWLDTAAPAKLILEVRAMDRAGLLALLAGALEGAGAGIVWAKVNTFGSTAADVFCVTVPAELDARAAVEQHLLEVLGASVDVVVDEPVGD", "text": "FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory protein (GlnB), 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 protein 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 protein, and plays an important role in the regulation of nitrogen assimilation and metabolism (By similarity). 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. FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory protein (GlnB), 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 protein 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 protein, and plays an important role in the regulation of nitrogen assimilation and metabolism (Probable). SIMILARITY: Belongs to the GlnD family."}
{"protein": "MQNRLTIKDIARLSGVGKSTVSRVLNNESGVSQLTRERVEAVMNQHGFSPSRSARAMRGQSDKVVAIIVTRLDSLSENLAVQTMLPAFYEQGYDPIMMESQFSPQLVAEHLGVLKRRNIDGVVLFGFTGITEEMLAHWQSSLVLLARDAKGFASVCYDDEGAIKILMQRLYDQGHRNISYLGVPHSDVTTGKRRHEAYLAFCKAHKLHPVAALPGLAMKQGYENVAKVITPETTALLCATDTLALGASKYLQEQRIDTLQLASVGNTPLMKFLHPEIVTVDPGYAEAGRQAACQLIAQVTGRSEPQQIIIPATLS", "text": "FUNCTION: Repressor of the treBC operon. It is able to bind trehalose- 6-phosphate and trehalose."}
{"protein": "MIIAIDGPSASGKSSIARELGVRLNYKFISSGHLYRIITLIAQRSLMNSCDFISEDSLLNLILENDISFNNFAFLLNGENVENQILNDKIDFQVSFYSSYVGIRNIVNKKLREVVKFSDDNYIIEGRDITTVVFPESEFKIYLDASVKVRALRRYKQRNGNETLEELERTLKRRDDVDKKKQYGKLKLSKGVFYLDTSYKGLDDVCNIIIEKFNLKKVRER", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily."}
{"protein": "MKKLALALDVNDINQALEIVDEIQDKIIIKIGYNLFIKGGINFVKQIKDRGFDIFLDLKLHDIPNTVYNGVKAVSEIGVNYLTIHSLGGQEMIQQAVKAKEGTDLKILAVTILTSHDENYPKLLGSSLSVPDLAYRLADMAVSNGSDGIVCSSHEVKFLKEHIQKPFIAVVPGIRLTKEKTDDQTRIATPEEALRDGADIIVVGRPILKAEDRNKIIKEMLSVIEEL", "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": "MGLCCGSTDRVTKYSKEDIQQPTESEPLKYDPDFKGPLSKRSCTDLPCLFLFVTFLCAWGYVAYYAVQHGDLNRLLVPIDSDGRKCGVDSEVRDEPYLVFFNITECAKIDVPISGCSTTQVCVSQCPNQDFDFESANCNPSNVNEIRSKLICKQNVKKSDLTTCQIIRQYIKSQRCAQTMQKSTPLVNRCVSNIPEGQCTLIPKQFRQQPPITSTKFQTSAEQCKEQRELENILEEKISKLQSFLARYVNNLISVLTKNNSVHQLKYLNYHLVLQTLKKGNLKHNPLIITPYLITIHNITVLLTFQMIVEDILESWRMILVFIACSVLASLILIAMLRWIAKPLVWISIIGVITALSYGVYYSFRQYQQIRANPVAAHVNVSPNLSSLVNSWFKSDQTWLWILIALSVILIVLLLVVLVLRKRIVIAIALLKEGSKAVSASFSTVFFPLVPWILQAVVIVFSLLVLLFLASIGVPVYKVNGLNSSLTCVCTNGYMEGDICDPVAFNENCRDTSRIYDQERCLDAACHFQEVDTPGIVRFFHALNVIGFFWCICFVSAFSEMVLAFTFATWYWTRQKSRLPFFVLTRGVTHTVYYHLGTLAFGSLIIAICKIIRAILEYVDHKLKRYDNGFTRAVLCCCRCFFWCLESFLKFLNRNAYIMCAIYGKNFCSSAKDAFSLLTRNVLRVIALDKVTGFLFFLSKLLLASGMAAVTYTYFDSDLPKMQLNYPFVPAVLVFIGTFIIASIFFSVYSVAVDTLFLCFLEDIERNDGSAERPFYMSRGLQKILGKKQK", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CTL (choline transporter-like) family."}
{"protein": "MTASSAKPASSVDSFFSATLAEADPEIAAAIKGELGRQRHEIELIASENIVSRAVLEAQGSVMTNKYAEGYPGARYYGGCEWVDVAENLAIDRAKKLFGANFANVQPNSGSQMNQAVFLALLQPGDTFMGLDLAAGGHLTHGSPVNMSGKWFKAAHYTVRRDDHLIDMDAVAKQAEEVKPKLIIAGGSAYSRPWDFKRFREIADHVGAYLLVDMAHFAGLVAGGAHASPVPHAHIVTTTTHKSLRGPRGGLILWNDEQFTKKLNSAIFPGLQGGPLMHVIAAKAVAFAEALRPEFKTYAKNIVENAKALAESLRAQGFDIVSGGTDNHLMLVDLRPKGLKGNVSEKALVRAGITCNKNGIPFDPEKPFVTSGLRLGTPAATTRGFGVAEFQQVGSLIAEVLNAIAQAPDGSAPLVEAAVKAKVKALTDRFPIYQ", "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": "MRSLIYRQLLTNSYTVDLSDEIESIGSKNTQNVTINPGPFAQTGYAPVNWGPGEVNDSTTVEPTLDGPYQPTSFNPPVNYWMLLAPLNAGVIVEGTNNTNRWLATILVEPGVASTTRTYTLFGIQEQITVENSSNTKWKFIDLMKTTSSGTYTQHSPLLSEPKLYGIMKHGGQLWTYNGETPNAITNGYPTTNYDSVNMTSFCNFYIIPRSQESVRTGYINNGLPPIQNTRNIVPVSISSRSIIHQRAQANEDIIVSKTSLWKEMKYNRDITIRFKFANAIIKSGGLGYKWSEISFKPANYQYTYTRDGEEVNAHTTCSVNGVNDFSFNGGSLPTDFVISRYEVIKENSYVYVDYWDDSQAFRNMVYVRSLAADLNDVLCTGGDYSFALPVGQWPVMTGGAVSLHSAGVTLSTQFTDFVSLNSLRFRFRLSVEEPHFSITRTRVTGLYGLPAANPNNNNEYYEVAGRFSLISLVPSNDDYQTPIANSVTVRQDLERQLGELREEFNALSQEIAMSQLIDLALLPLDMFSMFSGIKSTIDAAKSMATNVMKKFKKSGLATSVSTLTDSLSDAASSISRGSSIRSIGSSASAWTDVSTQLIDVSSTVNTISTQTSTISRRLRLKEIATQTEGMNFDDISAAVLKTKIDRSTQIAPATLPDIVTEASEKFIPNRAYRVMDNNEVLEASTDGRLCAYRVETFEEIPFDVQKFADLVTDSPVISAIIDFKTLKNLNDNYGISREQAFNLLRSDPRMLREFINQDNPIIRNRIEQLILQCRL", "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": "MRCLPVFVILLLLIASAPSVDAQLKTKDDVPLASFHDNAKGTQHKRIINWCCLIFYQCCLRR", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin T superfamily."}
{"protein": "MLLARAFARRSLRAGLWCRQKHTLPDLPYDYGALEPTISAEIMQLHHSKHHQTYVNNLNVAEEKLAEAKEKGDVSTIISLAPALRFNGGGHINHSIFWQNLSADGGEPEGELLAAINRDFGSVENMKNQLSAQTVAVQGSGWGWLGYIAEGALQIATCPNQDPLEATTGLVPLFGIDVWEHAYYLQYKNVRRIMLKPSGISLIGRISLQGSMQQSKNATSCSGA", "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": "MERDEEASGPMMEMCTNGGEETSNRRPIISGEPLDIEAYAALYKGRTKIMRLLFIANHCGGNHALQFDALRMAYDEIKKGENTQLFREVVNKIGNRLGEKYGMDLAWCEAVDRRAEQKKVKLENELSSYRTNLIKESIRMGYNDFGDFYYACGMLGDAFKNYIRTRDYCTTTKHIIHMCMNAILVSIEMGQFTHVTSYVNKAEQNPETLEPMVNAKLRCASGLAHLELKKYKLAARKFLDVNPELGNSYNEVIAPQDIATYGGLCALASFDRSELKQKVIDNINFRNFLELVPDVRELINDFYSSRYASCLEYLASLKSNLLLDIHLHDHVDTLYDQIRKKALIQYTLPFVSVDLSRMADAFKTSVSGLEKELEALITDNQIQARIDSHNKILYARHADQRNATFQKVLQMGNEFDRDVRAMLLRANLLKHEYHARSARKL", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. In the complex, it plays a central role in CSN assembly. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the CSN1 family."}
{"protein": "MLTFTKRCDDHGKTPDHSLSLPFETRQKSRFRAQFEDGTPVGVVLDRGLILRHGDVLESDEGVRVRIEAAPEPVSQVRGTDPLLLARACYHLGNRHVVLQIDADGLRYLHDHVLDDMVRGLGLTVGFTHAPFEPEAGAYAGGHAHGHGGHGHHHAHGHEH", "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": "MHPRYSPAPPPQQQQQMGGPPHQQQGGGGGGGGSMRGPSNAQQLPPQIPRSQNYSNGSSSSAAAAPLTSRSAFPGAPLTASAVALKGALPQRPPAMTSPAAAAAGAALAAGAPYRGAASWTPQGYAPAAAAAAAAVAQQAAYRYTAPLPQPAYAAYTPHTATTPATTTYGQRVPTAASPSNTNSSSSSNTGSQSGTLSTSLSNTTNTNTNMGPNGTVQNQNQQGGEQLSKTNLYIRGLQQGTTDKDLVNMCAQYGTIISTKAILDKTTNKCKGYGFVDFEQPAFAECAVKGLQGKGVQAQMAKQQEQDPTNLYIANLPPHFKETDLEAMLSKYGQVVSTRILRDQQMNSKGVGFARMESREKCEQIIQMFNGNTIPGAKDPLLVKFADGGPKKKNLFKTPDPNARAWRDVSAEGIPVAYDPTMQQNGVSVNVGTPIGVPYSRFSAPQVGGYPVAGSQWIPGYMMTTQVDDQTSYSPQYMQMAAAPQLGVTSYKPEAVNQVQPRGISMMVSGDTGVPYGTMMPQLATLQIGNSYISPTYPYYAPPPTIIPTMPMTDSEQASTAASPDEAYTQYPHQAAPK", "text": "FUNCTION: Has a role in the perception of gravity."}
{"protein": "MRIKDTLNLGKTKFKMRGNLPVREAEWEKEWEDNHLYEQRLKLNEGHPRFDLHDGPPFANGNIHMGHALNKISKDIIVRYKNMNGYYAPYVPGWDTHGLPVEQQLAKKGIDRKTMDRAKYRELCRQYAEEQVQKQMTDFKRLGVMADWDNPYITLQHEFEGQEIRVFGEMYKKGYIYKGKKPVYWSWSSESTLAEAEVEYKDVEANSIFVAFPVVDSKGIIDPKDTYFVIWTTTPWTIPANEAICVNPKFDYSVVQVGDKKYVVATGLLDKVAEEIGWDDYKVVQTVKGADMEYMKAKHPLYDKESLVTEGFHVTLDDGTGLVHTAPGFGADDFNVGQKYDLPVFSPVDAHGRYTDEVPELEGMFYQDVDKLMVEKLKDAGALLKLKVFTHSYPHDWRTKKPVIFRATTQWFASIAPFRDQILEQIDNAKFIPSWGKTRLYNMIKDRGDWVISRQRAWGVPLPIFYAEDGTPIVTPETIEHIAEIFDKEGSNAWYTHTAKELLPEGFTSEHSPNGEFTKEKDILDVWFDSGSSWSGVMEKRDGLHYPADLYLEGSDQYRGWFNSSLITSVAVTGKAPYKEVLSQGFVLDDKGHKMSKSLGNVISPNDVIKRMGAEIIRLWVAQADTTSDVAVSMGILQQSAESYRKIRNTFRYMLANTSDFDPKENGVAYDDLRSVDQYMEIKLNDLVAECLAAYDKFDFTTVFKKIFNFISNDLSAFYLDFAKDVLYIEGKNSLERRSMQTVIYDAAVKLTKILTPILPHTMEEIWGFLKEPEDYVQLANMPKVENYTNHDELLENWGKFMNLRDDVLKALEDARNKKLIGKSFEAAVTIYPDKETKAMLDDLDADFRQILIVSKLTIVDGEAPENAEKLNNASIVVEHAEGEVCPRCRMIRTDIGEDPKLPELCERCAKIVEEDFPEAAQEGLEE", "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": "MAASTQCFLHQYHALRSSPARTSSVSSPKPNQLICRAQKQDDASNAAVSRRLALTLLIGTAAIGSKVSPADAAYGEAANVFGKPKENTDFLPYNGDGFKLQVPAKWNPSKEVEYPGQVLRYEDNFDSTSNLIVAVTPTDKKSITDYGSPEEFLSKVDYLLGKQAYFGKTDSEGGFESGAVATRNLLEASSATVGGKEYYYLSVLTRTADGDEGGKHQLITATVNDGKLYICKAQAGDKRWFKGAKKFVENAATSFSIA", "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": "MIDIKELKFDEKGLIPAIVQDYYTKQVLMLAYMNEESLKLTLEKGETYFFSRSRGKIWHKGETSGNTQKVKKIFYDCDEDALLIQVEAKGPACHTGNISCFYRSFDEETEDGIEILNKLYERIKGRKINPVEGSYTNYLFEKGIDKILKKVGEEATEVVIASKNDSKDEIVYEVSDLIYHLMVLLVEKNITLNDIYNELERRYKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family."}
{"protein": "MVHKPVLLNEVVEALSPKDGSVYVDATFGGGGYSRRILETAQCVVYAIDQDVVVKKYFDELLQSFPGRLNLAISRFSKLREVVLSFGVDKVDGVVFDLGTSAMQLADASRGFSFMNSGSLDMRMCSSALRDAAMFVNTVPEKEMADVIYQYGGERYSRRVARAIIDARRKCRINNTGDLATIIRSAVPRSRVHPIDPATRTFQAIRIWVNNELEELQAGLEAAAEVLKIGGKILVTSFHSLEDRVVKHKFRSLCDMGFSLINKKAIMPTDEEVKNNPRSRSGKLRAIARVE", "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": "MIKYYNRKNKDYDIEKVAGEKYLNWTYSSPIGMNLLEVFIKKKFFSKIYGFYCDRRLSHKKINKFINDFKIDMSLSENQSSNFKCFNDFFTRKLKKEARPIKTDKNLLISPGDGKILAYENLNLNSVTEVKGINYSFYELINNDSLAKEYDNGTCLVLRLCPTDYHRFHFIDNGICENTIKLKGFYYSVNPIALSKIPSVFCKNKREYSIFHSENFGDIIFMEVGATCVGSIIQTYKPNTKILKGDEKGYFKFGGSTVILFFKKNTIKIDNDILNQSKLGYETSVVMGESIGIKK", "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": "MSTTDDTHNTLSTGKCPFHQGGHDRSAGAGTASRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYSALKGDLKALLTDSQPWWPADWGSYVGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLTHRHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAAAASHVGADPEAAPIEAQGLGWASSYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSPAGAIQFEAVDAPDIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKARYIGPEVPKEDLIWQDPLPQPLYQPTQEDIINLKAAIAASGLSISEMVSVAWASASTFRGGDKRGGANGARLALAPQRDWEVNAVAARVLPVLEEIQKTTNKASLADIIVLAGVVGIEQAAAAAGVSISVPFAPGRVDARQDQTDIEMFSLLEPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTVLVGGMRVLGTNFDGSQNGVFTDRPGVLSTDFFANLLDMRYEWKPTDDANELFEGRDRLTGEVKYTATRADLVFGSNSVLRALAEVYACSDAHEKFVKDFVAAWVKVMNLDRFDLL", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MASAATEGEKGSPVVVGLLVVGNIIILLSGLALFAETVWVTADQYRVYPLMGVSGKDDVFAGAWIAIFCGFSFFVVASFGVGAALCRRRYMILTYLLLMLIVYIFECASCITSYTHRDYMVSNPSLITKQMLTYYSADTDQGQELTRLWDRIMIEQECCGTSGPMDWVNYTSAFRAATPEVVFPWPPLCCRRTGNFIPINEDGCRVGHMDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTTL", "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": "MDDHKTASPPRERSYETPPAERPITDAEAARAAALSANEHIKIASGYLRGTLADGLLKHATGAISDDDGQLVKFHGMYLQDDRDLRAERTKKKLEKAYSFMIRLRIAGGVVSPKQWLALDEIARTYANGTLRATTRQTFQYHGVIKSNLKRTMQAIDAVLLDTIAACGDVNRNVMAATNPAQTGAHKAAYQLAKTISDTLLPKTNAWREIWLDGERVVGGEDEAVEPIYGKTYLPRKFKIVVAVPPSNEVDIFAHDLGFIAILDKKNKLKGWNVTVGGGMGMTHGETDTFPRTADVMAFCEPEDALKVAEAVMTVQRDWGNRKSRKNARLKYTIERYGLAAFRAEVERRVGRKLQDPKPFRFESNGDRYGWVEGEDGRHHLTLYLPSGRIKDVEGGPRYLSGLRRIAEVHQGDFRLTGNQNVIVANVPADRKSEIDALVAEYGLNLGVTALRRNSLACVALPTCGLALAESERFMPGLLTELEESLAAHGLQDEDITIRMTGCPNGCARPYIAEIGFVGRGPERYNLYLGAAFDGSRLSKLYAEDVAAKDIRATLDPLFAAYARDRQPGERFGDFVIRAGFVAKTINGPDFHDRTGALKAVA", "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": "MTKRTFGGTSRKRKRVSGFRVRMRSHTGRRVVRTRRKRGRSRLTV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
{"protein": "MEEKRVKCKKKLTSTIGTWKYIQACIFFAIILISNFYGLKSFTDGFLLRRAVLNQTSLCENPPADVREWKNSSGCWAPKIFERAVIVIIDALRYDFLIPYNDSNYYHNAFTTPYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPTFIDLGSNFAGTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLFHDYLNETLSQPAFSFNVPDLHGVDNKVNQYVFDYIKDANFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYSKKPTFGYLKQPGKVLSANQVDLVPTLSLLLGNPIPYGNLGTLIPEPFYYYGDEYLSKAQKINIGQLNRFFSEYDLDASDFLSSSVHKNNNSYLDQYFLDFDYARDAFSYFKAIWAEFSLFPMIIGFLLLIIGGFNLALLMQDKSVIFRMSANMAPSVMKCLPVCLILILANNELHSPFPAEFYVLLPSFYILLNSFNQKLMEYFKGFVKLDYFSIFITFLHVCSFGSNSFTVWEDRLCHFLIITIGLVMFCKCFSEMSPLFACSTYSALAFILLQVISSYVTNCREEQGAFCVSTYISTPDNSLRTLIVLALMALSSIILPLILQLHLRRVLGLSLKLYHLSILYFFELISSIFWIAHHVFANDALLEKQYHHVLYSLANTYVICILGVLIWQFFLLSRSKFAKINVIERSYFVFALLYSFLSFLQRPLGHLSLFSCFLQILLLIQLKQWQPSVGHNFFSVTLGLLGLSHFFTTGNQAAISSLDWNFAFIHSKSAENQAISAIFMFLHTVGAPILTCISIPLFSFEPLSKKNRFLINLFRFSFSFILYNLLISTSTVFFAGFFRRHLMVWKVFAPRFMLSGILLVTHQLFVLIQCFGSSVVKFPEDAE", "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 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily."}
{"protein": "MVRPHLLKKKILGRVWWLMPVVLALWEAEVGGSLEVRSLRPAWPTW", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MASHDSYTGRLPGAFMNPGTSSFTEFLASYNPDLLPGRHMTALAGGMPGNVEAPHATTIVAVTFPGGVVMAGDRRATAGNMIAQRDVEKVFRADEFSAVAIAGTAGIGMEIVRLFQVEIEHYEKMEGRTLSLEGKANRLATMIRANLGMAMQGLVAVPLFAGYDTEREVGRIFSYDPAGGRYEEHEHHSIGSGSVFARGALKKLWRPDLSAQDAALVCVQALYDAADDDSATGGPDLIRKIYPVVATVTADGFRRLPEEEVGELARIVVDGRHDSPGGPTAPLR", "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": "MKTQVEHAVDGIITEQMATVAHDEDLSPEYIRTMVAEGKIVIPNNSNSTPKPVGIGKGLRTKVNASIGTSSDIVNYQAEVRKARIAEQAGADTLMELSVGGNLDRVRREVLAAVNLPVGNVPLYQAFCDATRKYGSADKLDPEELFDLIEQQCEDGLAFMAIHCGINRYTIERLRKQHYRYGGLVSKGGTSMVSWMEHNNRENPLYEQFDRVVAILKKYDVCLSLGNGLRAGAIHDSHDRAQMQELIINCELAQLGREMGCQMLVEGPGHMPLDEVEANILIQKRMSNEAPYYMLGPISTDVVPGFDHISSAIGAAQSARYGADLICYITPAEHLALPNEDDVRSGVEAARVATYIGDMNKYPDKGRQRDKAMSKARRDLQWDKQFELALMPEQARQVRDSRLPEEEHSCTMCGNFCAANGSKTLFDGDLQGDKC", "text": "FUNCTION: Catalyzes the complex 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 dimethylbenzimidazole (DMB), the lower axial ligand of vitamin B12 (cobalamin). SIMILARITY: Belongs to the ThiC family. 5-hydroxybenzimidazole synthase subfamily."}
{"protein": "MFRYLTAGESHGPQLTAIIEGIPAGLKLSEESINVDLARRQGGYGRGGRMAIEKDQVEILSGVRWGKTIGSPITLCVKNRDWTNWQEKMSPQERFRDDNIHVTRSRPGHADLPGAMKYDHKDVRNILERSSARETAVRVAVGSVAKALLQHFEIYLCGYVAELGGIKAKRPELCPAELRATIAKSELYTCDSAVEGEMKKLIDEVKAAGDTVGGVVEVIASGVPAGLGSHVQWDRKLDARIAMAMMSIQAFKGVEIGLGFEAAARKGSNVHDEIFYDQSRASQGSMTGYYRLTNNAGGIEGGITNGEDILVRAAMKPIPTLYKPLRSVDIVSKEPFEATVERSDVCAVPAASVVAESVLAIELADAFMVKFGGDSIEEMQRNYAGYLEYLKNF", "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": "MVRPQDTVAYEDLSEDYTQKKWKGLALSQRALHWNMMLENDRSMASLGRNMMESSELTPKQEIFKGSESSNSTSGGLFGVVPGGTETGDVCEDTFKELEGQPSNEEGSRLESDFLEIIDEDKKKSTKDRYEEYKEVEEHPPLSSSPVEHEGVLKGQKSYRCDECGKAFYWSSHLIGHRRIHTGEKPYECNECGKTFRQTSQLIVHLRTHTGEKPYECSECGKAYRHSSHLIQHQRLHNGEKPYKCNECAKAFNQSSKLFDHQRTHTGEKPYECKECGAAFSRSKNLVRHQFLHTGKKPYKCNECGRAFCSNRNLIDHQRTHTGEKPYKCNECGKAFSRSKCLIRHQSLHTGEKPYKCSECGKAFNQISQLVEHERIHTGEKPFKCSECGKAFGLSKCLIRHQRLHTSEKPYKCNECGKSFNQNSYLIIHQRIHTGEKPYECNECGKVFSYNSSLMVHQRTHTGEKPYKCNSCGKAFSDSSQLTVHQRVHTGEKNLMNVLSVGKPLVSVPLLITTSELMLERSPQVWLGHLLKAWFSETDSKDL", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MAAPVDLELKKAFTELQAKVIDTQQKVKLADIQIEQLNRTKKHAHLTDTEIMTLVDETNMYEGVGRMFILQSKEAIHSQLLEKQKIAEEKIKELEQKKSYLERSVKEAEDNIREMLMARRAQ", "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. SIMILARITY: Belongs to the prefoldin subunit beta family."}
{"protein": "MLHQLTLAEIARALADKQFSAEELTRTLLGRIRQLDPQLNSFISITDDLAIAQAKAADERRANGENGALLGAPIAHKDLFCTQGVRTSCGSKMLDNFVSPYDATVVEKLTAAGAVTLGKLNMDEFAMGSSNQSSHYGAVKNPWSLDRVPGGSSGGSAAAVAARLLPAATGTDTGGSIRQPAALTNLTGIKPTYGRVSRWGMIAYASSLDQGGPLARTAEDCALMLGVMAGFDPKDSTSVEQPVDDYLAALQKPLSGLRIGLPREYFGAGLDSRIADAVLAVVEELKTLGATVKDISLPNMQHAIPAYYVIAPAEASSNLSRFDGVRYGYRCDAPQNLEDLYKRSRAEGFGSEVKNRIMVGTYALSAGYYDAYYLQAQKIRRLIKNDFVSAFAEVDVILGPTTPNPAWKIGEKNDDPVSQYLEDIYTITANLAGLPGLSMPAGFVDGLPVGVQLLAPYFQEGRLLNVAHQYQQVSDWHTRTPAGF", "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": "MTRRCDITGKSVLSGNNVSHANNKSRRRFLPNLQDSALQSDALGHSVKLRVTPRGLATIEQKGGLDAFLLDTPNRKLTDEARTLKRRVAKAAARREAKSA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MTDLSDIRREYTKGGLRRSELPEDPMALFERWMEQAKAAELTDPTAMCVATVDELGQPYQRIVLLKRFDEQGFVFFTNLGSRKATQLKHNAHISLLFPWHPLERQVAVTGIAEPLSTAEVLKYFVTRPKDSQIAAWVSAQSSKLSARQVLEAKFMEMKQKFSAGEVPLPSFWGGYLVRPASIEFWQGGEHRLHDRFIYEKTAAGWDIERLAP", "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": "MLGDYRSGKTAIFNEIVGRKFGSYTNPSTFDYFYKEIMVDNELVGCNIWDTAGHEKFTTNLNKSFYRDVNCCVLCFDLHFEDSFKNLNKWMNEFHSKCLENGLENMELLPPFVLIGTKSDIPRTDISISNERIEQWCKNIEGQGIIDKVHYFETSAKLSQNIIMPFNTITKLALNYSNSIQKIK", "text": "SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MAADVFMCSPRRPRSRGRSVLLKPQVPEDDDDSDTDEPSPPPPSGVATSARAHASAAPLPPRAGPGREEPPRRQQIIHSGHFMVSSPHREHPPKKGYDFDTVNKQTCQTYSFGKTSSCHLSIDASLTKLFECMTLAYSGKLVSPKWKNFKGLKLQWRDKIRLNNAIWRAWYMQYLEKRRNPVCHFVTPLDGSVDVDEHRRPEAITTEGKYWKSRIEIVIREYHKWRTYFKKRLQQHKDEDLSSLAQDDDMLYWHKHGDGWKTPVPMEEDSLLDTDMLMSEFSDTLFSTLSSHQPVAWPNPREIAHLGNADMIQPGLIPLQPNLDFMDTFEPFQDLFSSSRSIFGSMLPPPSSLPAADPSSPPSQGNILPNTALPPASLPNSLITSSAAPSLDPTEGQGCERTSQTVDPFIQPADFGPSEPPLSVPQPFLPVFTMTLLSPGPAPAPVPTALPLVPSPAPTLNPPTPPAFLQPQKFAGVSKSTPVITHTASATLTHDASATTFSQNQGLVITAHHPTPSSSPCALALSPVPQPPAVGPPQPHLTFIHPKPVSLTGVRHKQPPKIVPAPKPEPVSLVLKNACIAPAAFSGQPQKVIMTSAPLKREGILASTVSPSNVVIASAAITRASGVTEFLSHSTSSQPSPVSRLFSPSTVQDSLVKGEQVSLHGGSPQVPATGSSRDCPNSGQASPCPSEQSPSPQSPQNNCSGKSTDPKNVAALKNRQKHISAEQKRRFNIRMGFNTLNSLISNNSKQTSHAITLQKTMEYITKLQQERMQMQEEARRLREEIEELNTTIISCQQLLPATGVPVNCRQLDHMRDMFDEYVKSRTLQNWKFWIFSMIIKPLFESFKGMVSTSSLEEFHRTALSWLDQHCSLPVLRPMVLSTLRQLSTTTSILTDPSQLPEQASEAVTRMGKRSGES", "text": "FUNCTION: Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion outer membrane Note=Predominantly cytoplasmic but shuttles between cytoplasm and nucleus when associated with MLX. Also associates with the outer mitochondrial membrane and may shuttle between the outer mitochondrial membrane and the nucleus."}
{"protein": "MMGGRGTGGKWPSAFGLLLLWGVAASALPLESGPTGQDSVQEATEGRSGLLTFLAWWHEWASQASSSTPVGGGTPGLSKSQERPPPQQPPHLDKKPCKNFFWKTFSSCK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatostatin family."}
{"protein": "MPSVKIKENEPFDVALRRFKRSCEKAGILSEVRRREFYEKPTSERKRKLAAAVKRHAKKVQREQRRFERLY", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
{"protein": "MMIEVLKSKIHCARVTEANLNYMGSITIDEDLLDAANMIPGEKVYIADNNNGERFETYIIKGERGSGKICLNGAAARKVQPDDIVIIMSYALMDFEEAKSFKPTVIFPDPATNSVVK", "text": "FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family."}
{"protein": "MSRRFNPLEDPPSASSSDEEGKEIARNSSSDDEDDVSSENPSPLKTTLDAVSDSESGSDEETDSDSELEKKKDQVVTNPVDVKRAKKVKTSEKSGAKRSLEVDEAAVSMDVKRAKKVSGEEEKKKSGGGGEETKKTYFQRLWTEDDEIVVLQGLIDDKKDTGVSNTNKVYELVKKSISFDVSKNQLMEKLRALKKKYENNLGKAKDGVEPTFVKPHDRKAFELSKLVWGGIRMALASGMKSNEKSKKSSKFESVKHELDSSLPNSKNNCEDEVMDEGEVSFTKSSLVRSIVGLGMDELTAQQGLSKLASKDMKRFYEQWKAMQAREFEFFLQKHGFLFEVLSKISEAFGSNA", "text": "SIMILARITY: Belongs to the GeBP family."}
{"protein": "MASMGLQVLGISLAVLGWLGIILSCALPMWRVTAFIGSNIVTAQTSWEGLWMNCVVQSTGQMQCKMYDSMLALPQDLQAARALMVISIIVGALGMLLSVVGGKCTNCMEDETVKAKIMITAGAVFIVASMLIMVPVSWTAHNVIRDFYNPMVASGQKREMGASLYVGWAASGLLLLGGGLLCCSCPPRSNDKPYSAKYSAARSVPASNYV", "text": "FUNCTION: Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney (PubMed:20921420). Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts (PubMed:20921420). Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein Note=CLDN4 is required for tight junction localization in the kidney (PubMed:20921420, PubMed:25831548). SIMILARITY: Belongs to the claudin family."}
{"protein": "KDGYPVEVTGCKKSCYKLGENKFCNRECKMKHRGGSYGYCYFFGCYCEGLAESTPTWPLPNKSCGKK", "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": "MSLPIEQYPELLAQKVDNLTALLAPFNPPPFDIFASETSHFRMRAEFRVWHQKNEQGENDLYHIMFDPTTKQRYRVDQLPIANQLINTMMQKLLTQIQGIPVLTHKLFQVDYLTTLSGEIAISLLYHKKLTDEWLAQAKLLKQRLSEPGLTVHIIGRASKQKIAIDCDYVKEKLNVAGKTLIYRQVENSFTQPNAKMNINMLEWAQKCTANSQDSDLLELYCGNGNFSIALAGNFRKVLATEICKSSVHSAQYNIAQNGIDNLQIIRMSAEEFTQAINGVRQFNRLQGIDLSAYQCNTIFVDPPRAGLDQATLNMVQNYPRILYISCNPATLADNLRQLTTTHRIERVALFDQFPYTHHIESGVWLIRK", "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": "MSKIESALQAAQPGLSRLRGGAGGMGYRAATTQAEQPRSSLLDTIGRFAKAGADMYTAKEQRARDLADERSNEIIRKLTPEQRREALNNGTLLYQDDPYAMEALRVKTGRNAAYLVDDDVMQKIKEGVFRTREEMEEYRHSRLQEGAKVYAEQFGIDPEDVDYQRGFNGDITERNISLYGAHDNFLSQQAQKGAIMNSRVELNGVLQDPDMLRRPDSADFFEKYIDNGLVTGAIPSDAQATQLISQAFSDASSRAGGADFLMRVGDKKVTLNGATTTYRELIGEEQWNALMVTAQRSQFETDAKLNEQYRLKINSALNQEDPRTAWEMLQGIKAELDKVQPDEQMTPQREWLISAQEQVQNQMNAWTKAQAKALDDSMKSMNKLDVIDKQFQKRINGEWVSTDFKDMPVNENTGEFKHSDMVNYANKKLAEIDSMDIPDGAKDAMKLKYLQADSKDGAFRTAIGTMVTDAGQEWSAAVINGKLPERTPAMDALRRIRNADPQLIAALYPDQAELFLTMDMMDKQGIDPQVILDADRLTVKRSKEQRFEDDKAFESALNASKAPEIARMPASLRESARKIYDSVKYRSGNESMAMEQMTKFLKESTYTFTGDDVDGDTVGVIPKNMMQVNSDPKSWEQGRDILEEARKGIIASNPWITNKQLTMYSQGDSIYLMDTTGQVRVRYDKELLSKVWSENQKKLEEKAREKALADVNKRAPIVAATKAREAAAKRVREKRKQTPKFIYGRKE", "text": "FUNCTION: Component of the cylindrical core that assembles on the inner surface of the capsid during capsid formation and plays a role in viral DNA ejection into the host cell. The inner core is composed of stacked rings of gp14, gp15 and gp16 proteins. Following binding to the host cell surface, the internal core is disassembled and gp15 is ejected along with gp14 and gp16 into the infected cell. Gp15 probably remains associated with gp16. The gp15-gp16 complex binds to both the viral DNA and the host inner membrane, probably escorting the leading end of the genome through the periplasm and controlling the extend of DNA translocated into the host cell. SUBCELLULAR LOCATION: Virion Host periplasm Note=The gp15-gp16 complex spans the periplasm and the cytoplasmic membrane. SIMILARITY: Belongs to the T7virus internal virion protein gp15 family."}
{"protein": "MTQQLEQIIDQAWENRADFSPKNAPADLRNAVAQVIAQLNEGTLRVAQKDSGAWVVNQWVKKAVLLSFRLEDNIAMPSGEYMQFYDKVPTKFANYTAEDFAKGGFRVVPPAVARHGSFIGKNVVMMPSFVNIGAYVDEGSMVDAWATVGSCAQIGKNVHLSGGVGIGGVLEPMQANPTIIEDNCFIGARSEIVEGVIVEENSVISMGVYIGQSTKIYDRATGEVTYGRIPAGSVVVSGNLPSADGKYSLYCAVIVKRVDAKTRAKTGINELLRD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
{"protein": "MGRLFGTDGVRGVANADLTAELALGLSVAAAHVLAEAGTFEGHRPVAVVGRDPRASGEFLEAAVVAGLASAGVDVLLVGVLPTPAVAHLTGALGADLGVMLSASHNAMPDNGIKFFARGGHKLADDLEDRIEAVYEEHRTGAPWDRPTGAGVGRVTSYGEGADQYVAHLMSVLPNRLDGIKVVLDEAHGAAARVSPDAFTRAGAEIITIGAEPDGLNINDGCGSTHLAKLRAAVVEHGADLGIAHDGDADRCLAVDHTGAEVDGDQILAVLALAMRERSALRSDTVVATVMSNLGFKLAMEREGLSFVQTAVGDRYVLEEMKEHGYALGGEQSGHVIILDHATTGDGTLTGLLLAARVAQTGRTLQDLASVMERLPQVLVNVPDVDRARVKTSAELATAVAEAERELGATGRVLLRPSGTEPLVRVMVEAADIEQARSVAGRLADAVKSALG", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MHYYVLFTFLTLDLAPVALSLSTCSALDMDQFMRKRIEAIRGQILSKLKLNSPPEDYPEPGEVSQDVISIYNSTRDLLQEKANERATSCERERSEDEYYAKEVYKIDMLPYYTSENVIPPSYTTPYFRIVRFDVSSMEKNASNLVKAEFRVFRLMNTKARVSEQRIELYQILKSKDLASPTQRYIDSKVVKTRAEGEWLSFDVTEAVNEWLHHKDRNLGFKISLHCPCCTFIPSNNYIIPNKSEELETRFAGIDDAYMYAGGDSKSKTGRKKHTGRTPHLLLMLLPSYRLESQQSSRRKKRALDAAYCFRNVQDNCCLRPLYIDFKKDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLDSLTILYYIGNKPKIEQLSNMIVKSCKCS", "text": "FUNCTION: [Transforming growth factor beta-2]: Multifunctional protein that regulates various processes such as angiogenesis and heart development (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-2 (TGF-beta-2) chains remain non-covalently linked rendering TGF-beta-2 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as ltbp1 and lrrc32/garp, that control activation of TGF-beta-2 and maintain it in a latent state during storage in extracellular milieus (By similarity). Once activated following release of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (tgfbr1 and tgfbr2), which transduce signal (By similarity). FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-2 and regulates its activation via interaction with 'milieu molecules', such as ltbp1 and lrrc32/garp, that control activation of TGF-beta-2. FUNCTION: [Transforming growth factor beta-2 proprotein]: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix. SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MKKKNSIIFVFMILFFNSTVQSQSFKKNYFTERYTLYEKSNKELRKENFDNAISILEKIKKNNNTANISNDKIQIDLIYAYYKILNFDQARKNIEEFMYFYPNHPNIDYVVYIQCLISMSLDKNRFFSVFPINYYKNDYFYAKNAFFQLKYFIYQYPKSRYVVNAKKNLIYIKNRLSEHDLSILKFYFFHKEYIAVINRGEEMLQRYSETPSARKALIYIEKSYYALKIFDTAKKISKIILLNKIQ", "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 BamD family."}
{"protein": "MSNTSNSDPNSDIPFASSNVTLPSYNQNPRRKRTKLTNNEVGSSSSSPRPKPVTQPDPDASQIARPCTECGKQFGSLKALFGHMRCHPERQWRGINPPSNFKRRINSNAASSSSSWDPSEEEHNIASCLLMMANGDVPTRSSEVEERFECDGCKKVFGSHQALGGHRATHKDVKGCFANKNITEDPPPPPPQEIVDQDKGKSVKLVSGMNHRCNICSRVFSSGQALGGHMRCHWEKDQEENQVRGIDLNVPAATSSDTTLGCSLDLRLGL", "text": "FUNCTION: Mediates the regulation of male germ cell division by DUO1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSQVTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSVGLSVTKPYVIMLLEDGKEPWMMEKKLSKAYPFPLSHSVPASVNFGFSALFEHCSEVTEIFELSELCVFWVLHFLSNSPNSTVEAFSRSKKKKKKKKKRQCFAFLIYFRLGIKMGKQGIINKEGYLYEDSPQPVTMEKVVKQSYEFSNSNKNLEYTECDTFRSTFHSKSTLSEPQNNSAEGNSHKYDILKKNLSKKSVIKSERINGGKKLLNSNKSGAAFNQSKSLTLPQTCNREKIYTCSECGKAFGKQSILSRHWRIHTGEKPYECRECGKTFSHGSSLTRHQISHSGEKPYKCIECGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLLIQHLRIHTQEKRYECRICGKAFIHSSSLIHHQKSHTGEKPYECRECGKAFCCSSHLTQHQRIHSMKKKYECNKCLKVFSSFSFLVQHQSIHTEEKPFEV", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MSQFIRHYLLSLQFFTRIPVTGRLANWVGFSPAMLRASAGHFPGVGVLVGALVAAFTALLLFVLPRTGSTPLVAAALGTALGVLLTGAFHEDGLADVFDGLGGSAERERALVIMKDSRVGAFGAIAVMLALLCKVALLALLGAVSATLMVAALFVAHVLSRTWPLLTIRLLPHVGDAAGSKSKPLADQISVAALLTGFIWCFMALALVISTQSATEYIAINLTDTALLQALLSAVVASCVAWAVMARWFWRRLQGFTGDCLGATQQVCELAFYLGLAVGL", "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": "MAIKDAIEKIVSYFDADEVTDHEDVAKERPVKVQKTEQTPSQQQRKPERPQETVPPRRQHIKSDVQETQVLRSLSLSRSQVNQGSQQMNTTKTTIAIKYPKKYEDAQEIVELLIENECVLIDFQYMLEAQARRCLDFIDGASKVLTGNLQKVGSSMYLLTPINVVVDIEEIGLSHGNQESTFDFDMKRR", "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": "MKVSTAAFAVLLTAAAFCTPASASPYASDTTPCCFAYLSHPLPLTHLQEYFYTSSKCSMPAVVFVTRRKRQVCANPQKKWVRDKGINSLEMN", "text": "FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. May also be an agonist of the G protein-coupled receptor GPR75. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MAEWQTECMLPPTQPGFEGVGPHPGRVLQNTSGNIQSYSDTLAHTDPTGRDDHFSHYGFKYPHQPPVPTHPMPTTTGLHPQQVINNRFHTKKLRRLQSLGPNLIGPRRTRSYLKSQKYIEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIYKTTGKRRSRKQVSSHLQVLDSFLKGDPDWERLVREQPADRSNGQPPSAGPRWRNSLELPFSSHYNSHNYPSYHDSLRPVQSYSGELPPPHVVFHPNLHAEATNINKIYGLSFDMWVSAPNQPGGIESAFHLYTRLQGDQRHPAPPKRLENIPNWRTSFPHLNSVMADVNNPLNCDIILLEANLRLMDDFPPSGSKLGIQLELDFTQPPNGDALTNQMENWSCSTYIYEEGQNIYRARQDLPKQQSNKVKPPFESTWWAKRFTELTEIAKDRQLNELADRQTRDYFRTLTAVQEIRATPSSRRVSNQYPDNSQDDSKRMAILLWQFRQTRSNEVGTTTWRRVTSPSSDRNTIPSPKPVTGIDLPPLSFYANSLARPAPSIYQAPQSHDLVHHNGTSQPQWSMYQPPQDSIFNANGGFDLLNSITKPEGGLHDKTAVTSVLDTYPNLQPEVSQPTSLNGSNGGPGMLSIPDMSLSHTNLNAYNLSGHDNHYGTPQHPGVSVPDNSHVLNNGIFGSSTQSIDDMSQTHAPWPTPTSSITDVGSSNYSHLQFSDHHVPSVSRESHQPNHFEVLLGPDDLIVGSMPGDPGINGAAHGHMNHTYTENNAVEAA", "text": "FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:19850144). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Controls expression of wetA (PubMed:19850144). SUBCELLULAR LOCATION: Nucleus Note=localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). SIMILARITY: Belongs to the TEC1 family."}
{"protein": "MAAEEGQVIGCHEIDVWAVQLDTAKQSNKLIVIDFTASWCPPCRMIAPVFADLAKKFMSSAIFFKVDVDELQNVAQEFGVEAMPTFVLIKDGNVVDKVVGARKEDLHATIAKHTGVATA", "text": "FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily."}
{"protein": "MDVDLASVEVVFAQKLACGEPATRQRALRVLHDWIRDQSAKKHFDDADLMRLCKGLHYVMWMQDKMILQEELADRIGGLINIFTSEEEKVRFVACFLKSLSKEWPHIDRWRMDKFLMEVRRMVRACFTHLAELKWKKDIRDEYWKVFQETTISTDKSFNEALKFHFASILLDELDAAGGLTKKQVTACLKPYIELLGNKDISEYLFTSLYEEIFKTILQQKSDLITAVEEGEEMDQGGIEFSYKEIGALLFEVGKQEHLNAKRRKKIYDLVKKFDKSSRGQDPLHFETPVPKERLTRHDYEEAEKKAIVLANSFKQERKSSRKVKSQIKKRAREAAEAARQENGDDVPDDEIAEVKKGNGKKTAVPKVKKGRPLLKAKGVGKKRMVGGLKRKAGKKN", "text": "FUNCTION: May be involved in the generation of 28S rRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRP1 family."}
{"protein": "MVPAWLWLLCVSVPQALPKAQPAELSVEVPENYGGNFPLYLTKLPLPREGAEGQIVLSGDSGKATEGPFAMDPDSGFLLVTRALDREEQAEYQLQVTLEMQDGHVLWGPQPVLVHVKDENDQVPHFSQAIYRARLSRGTRPGIPFLFLEASDRDEPGTANSDLRFHILSQAPAQPSPDMFQLEPRLGALALSPKGSTSLDHALERTYQLLVQVKDMGDQASGHQATATVEVSIIESTWVSLEPIHLAENLKVLYPHHMAQVHWSGGDVHYHLESHPPGPFEVNAEGNLYVTRELDREAQAEYLLQVRAQNSHGEDYAAPLELHVLVMDENDNVPICPPRDPTVSIPELSPPGTEVTRLSAEDADAPGSPNSHVVYQLLSPEPEDGVEGRAFQVDPTSGSVTLGVLPLRAGQNILLLVLAMDLAGAEGGFSSTCEVEVAVTDINDHAPEFITSQIGPISLPEDVEPGTLVAMLTAIDADLEPAFRLMDFAIERGDTEGTFGLDWEPDSGHVRLRLCKNLSYEAAPSHEVVVVVQSVAKLVGPGPGPGATATVTVLVERVMPPPKLDQESYEASVPISAPAGSFLLTIQPSDPISRTLRFSLVNDSEGWLCIEKFSGEVHTAQSLQGAQPGDTYTVLVEAQDTDEPRLSASAPLVIHFLKAPPAPALTLAPVPSQYLCTPRQDHGLIVSGPSKDPDLASGHGPYSFTLGPNPTVQRDWRLQTLNGSHAYLTLALHWVEPREHIIPVVVSHNAQMWQLLVRVIVCRCNVEGQCMRKVGRMKGMPTKLSAVGILVGTLVAIGIFLILIFTHWTMSRKKDPDQPADSVPLKATV", "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": "MFRPQVVGVTGRTDLGRAVRVAERVCRLCDREGFEVLVDDSLGIGEYPRVNLKDMGKEVDMIITIGGDGTILRVSRITSEYEVPILGVNLGKFGFLTEVSESGLKEAVSRLARGDFNLEEHRKLRIKIGGSDEGDALNEVTVITSRPAKMIRYRLSIDGFELETTWADGVLVATPTGSTAYSLSAGGPIVEPQVECSIITPLNPFKLEARPMVVSMDRRVEIDVDDPERAEVVVDGQEYMNLDGTVSVTRSPNVARFIRFGSTYFERLKEKFLRWD", "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": "MGKAIFITGTGTEIGKTVATSFLAFAFQKMGLNTKIFKPIQTGLAEDGVSFADQYWYEKVVGLAQSEGLYYMEPAVSPHLAATLTNTTIDPALIVEKIEQWKRQYDIVLVEGAGGLAVPLIEKEQGFYMTNDLIREYNIPIIIVSLAGLGAIHHTVTTVSYAQQQGIRILGLIFNQFNAESIIHVNNIETIKKMLDLPVIATLPSLAKVTKHTMMALAERWLENNEQKQLLQEVLSVAI", "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": "MTMEPNSTTSDHILDWLEGSVSFFPSFLDEPCNNSGYIQEYHLWDQYQTDANTGSSPNATNSTTATIVATSATSTTSLEPCGSNNNQPLSDLPKKRNATDESSLKPPQNKNKRIKTRPMNEPENGDAVRKNKKGGAKANGSNCNSGNSKEGRWAEQLLNPCAAAIAGGNVNRVQHLLYVLHELASPTGDPNHRLAAHGLRALTHHLSSSSSSPTSSGTITFASTEPRFFQKSLLKFYEVSPWFSFPNNIANASILQVLAEEANITSRTLHILDIGVSHGVQWPTLLDALSRRSGGPPSVVRLTVVTAENDQNMETPFSKAPPGYNYYPRLLGYAQSININLQINRIENHSLQTLNAQSISASPDEILIVCAQFRLHHLNHNSPDERSEFLKVLRNMEPRGVILSENNTECCCSGCGNFAAGFTRRVEYLWRFLDSTSSAFKGRESDERRVMEGEAAKALTNQREMNEEKEKWCGRMKEAGFAGEVFGEDAVDGGRALLRKYDSNWEMKVEEKNTSVGLWWKGQPVSFCSLWKLDGNDQGGTS", "text": "FUNCTION: Transcriptional regulator essential for Nod-factor-induced gene expression (PubMed:17071642) (Probable). Acts downstream of calcium spiking and a calcium/calmodulin-dependent protein kinase required for activation of early nodulation gene expression (PubMed:17071642, PubMed:24329948). Acts as a common symbiosis gene that positively contributes to the early steps of the arbuscular mycorrhizal fungus and rhizobial infection processes in roots (PubMed:23926062). Transcription factor involved in the positive regulation of the beta-carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones in roots (PubMed:23926062). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MKPRMCLILFIALMRVMSIVSAQSSCTNVLISMAPCLSFITQNTSLPSQQCCNQLAHVVRYSSECLCQVLDGGGSQLGINVNETQALALPKACHVETPPASRCHSGSSVNSHSEHGNGSKTVPREKSSSDGSIKFSFPLLAILFTASYITLIYAKY", "text": "FUNCTION: Probable lipid transfer protein. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the plant LTP family."}
{"protein": "MKTKMITREGYNKLKQELDYLWKEHRPEITQKVSWAASLGDRSENADYTYNKRLLRQIDRRVRFLSKFLPEVKIVDYAPQQEGKVFFGAWVEIENEAGEVMKFRIVGPEEIYGDAKGYISIDSPMARALLKKEVDDEVQVPTPSGIKEWFINSIEYDKGE", "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": "MLRNGVQRLYSNIARTDNFKLSSLANGLKVATSNTPGHFSALGLYIDAGSRFEGRNLKGCTHILDRLAFKSTEHVEGRAMAETLELLGGNYQCTSSRENLMYQASVFNQDVGKMLQLMSETVRFPKITEQELQEQKLSAEYEIDEVWMKPELVLPELLHTAAYSGETLGSPLICPRELIPSISKYYLLDYRNKFYTPENTVAAFVGVPHEKALELTEKYLGDWQSTHPPITKKVAQYTGGESCIPPAPVFGNLPELFHIQIGFEGLPIDHPDIYALATLQTLLGGGGSFSAGGPGKGMYSRLYTHVLNQYYFVENCVAFNHSYSDSGIFGISLSCIPQAAPQAVEVIAQQMYNTFANKDLRLTEDEVSRAKNQLKSSLLMNLESKLVELEDMGRQVLMHGRKIPVNEMISKIEDLKPDDISRVAEMIFTGNVNNAGNGKGRATVVMQGDRGSFGDVENVLKAYGLGNSSSSKNDSPKKKGWF", "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. SIMILARITY: Belongs to the peptidase M16 family."}
{"protein": "MAINAQEISALIKKQIENFQPNFDVTETGIVTYIGDGIARARGLDNAMSGELLEFENGAYGMAQNLESNDVGIIILGDFSAIREGDVVKRTGKIMEVPVGEALIGRVVNPLGQPVDGLGDIETTGFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRRYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYQGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDDLGGGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAATQAKLNRGRRTVEILKQPLHKPLPVEKQVVILYALTHGFLDDVPVDDILAFEEALYDYFDVHYNDLFETIRTTKDLPEEAALDAAIKAFKEHSNFKS", "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": "MDSNTVSSFQVDCFLWHVRKQFADQELGDAPVRDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILEEESDEALKMTIASVPASRYLTDMTLEEMSRDWFMLMPKQKRAGSLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTDEDVKNAIGVLIGGLEWNDNTVRVSETLQRFAWRSSNEGGRPPLPPKQKRKMARTIESEV", "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": "MASETEKTHALLQTCSTESLISSLGLGAFCLVADRLLQFSTIQQNDWLRALSDNAVHCVIGMWSWAVVTGIKKKTDFGEIILAGFLASVIDVDHFFLAGSMSLKAALTLPRRPFLHCSTVIPVVVLTLKFTMHLFKLKDSWCFLPWMLFISWTSHHIRDGIRHGLWICPFGKTSPLPFWLYVIITSSLPHICSFVMYLTGTRQMMSSKHGVRIDV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MSFIPNTEAEALSALFSRRSVLGATAAGGLLATPLAAFAQSGAASGPGEAEITVDQARQEPIPIVVPNFGAGLGEQISGVITSDLNGTGLFKVMSGSVPPGSTPDFSALKAQGARAAVAGQAVGAGSVRVEMRLWDVLSGQQLQGTAYTASNSNWRRIAHIIADVIYERMLGEKGYFDTRIAYIARTGPRHHQITRLALMDQDGANERMLTGGEWLTLTPRFNPVRDQIAFMSYANNRPRVYLFDLASGRQQILGEFAGISFAPRFSPTGGSVVLSATRGGGSDIFVVDLASRAKRQITNSNGAIDTSPCFSPDGSQIVFNSDRGGSPQLYIMSASGGAAKRISYGSGQYGSPVWSPRGDLIAFTRIGSGGFSLGVMNPDGTGERILTQGFTVDGATFCPNGRVLAFCRQSASGAGGAGFASGIGTIDITGFNERPIRISTGASDPAWSPRNG", "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": "MKETITKQLIAVQQASREIITLTDETINSLLCALADSIPSHQEAILQANQKDIERMDPADPMVDRLLLNASRLDAIAADIRNVASLPSPLDALLEERVLPNGLNLKKVTVPIGVIGIIYEARPNVTFDVFALCLKSGNATVLKGGSDAMYSNIAIVELIHSVLKQHGINPDTLYLLPAEREAAAVMLNAVGYIDMIIPRGSQKLIDFVRNNAKVPVIETGAGIVHTYFDKSGDLDLGKHIIFNAKTRRPSVCNALDTLVIHQERLADLPALVEPLQEKQVMLFADEAAFQALQGSYPDDLLHQAEPEHFGTEFLSLKMSVKTVSSLEEALEHITRYSSRHSEAIIATDPETTATFLKRVDAAVVYANTSTAFTDGAQFGLGAEIGISTQKLHARGPMALKELTTYKWIIEGNGQTRPA", "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": "MIGKLTGTVTDLCQESLILDVGGVGYNVFTTRRLIDSLRTGQNLSLYIEHYFLENINKLYGFECRKSQEVARMLSKVKGINYKIALSLLNHLELGELILAIQNKDESRLKIKGIGEKLVKRIITETYEDFLKLDSHLSGIASSTNVHIASEAVSALVKLGFQHKPSHKVVMEIMTKRPAIEIAELITLALKML", "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": "MGLLEGKRALITGVANERSIAYGIAKSFHREGAQLAFTYATPKLEKRVREIAKGFGSDLVVKCDVSLDEDIKNLKKFLEENWGSLDIIVHSIAYAPKEEFKGGVIDTSREGFKIAMDISVYSLIALTRELLPLMEGRNGAIVTLSYYGAEKVVPHYNVMGIAKAALESTVRYLAYDIAKHGHRINAISAGPVKTLAAYSITGFHLLMEHTTKVNPFGKPITIEDVGDTAVFLCSDWARAITGEVVHVDNGYHIMGVFGREEEIKKEVYGD", "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": "MLKEFREFAMKGNVVDLAVGVIIGAAFGAIVTSLVGDVIMPLIGAVTGGLDFSNYFTPLSKAVTATNLADAKKQGAVLAWGSFLTLTINFIIIAFVLFLVIRAINTLKRKEEAAPAAPPKPSAEVELLTEIRDLLKKS", "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": "MDLPLFVIALILGIVEGLTEFLPISSTGHLIIIGDLLGYNDATSKVFKIVIQFAAILAVCWDYRERLARVAAGVGSEPAAQRFVGLLFIGFLPAAVLGLMFHSTIKSLLFNPLTVATALVVGGVLILWLERRAYHPRINAVDEMRWADALKVGFAQAAAMIPGTSRSGATILGGLVFGLSRKAAAEFSFFLSIPTMFAATVYDLYKNRDLLHMGDLPVFAIGFVASFFAAMFAVKAFIRFISNHTFIAFAWYRIVFGLVVLATWQLELVEWSEP", "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": "MVPLKLQALFCLLCCLPWVHPFHWQDTSSFDFRPSVMFHKLQSVMSAAGSGHSKIPKGNGSYPVGCTDLMFGYGNESVFVRLYYPAQDQGRLDTVWIPNKEYFLGLSIFLGTPSIVGNILHLLYGSLTTPASWNSPLRTGEKYPLIVFSHGLGAFRTIYSAIGIGLASNGFIVATVEHRDRSASATYFFEDQVAAKVENRSWLYLRKVKQEESESVRKEQVQQRAIECSRALSAILDIEHGDPKENVLGSAFDMKQLKDAIDETKIALMGHSFGGATVLQALSEDQRFRCGVALDPWMYPVNEELYSRTLQPLLFINSAKFQTPKDIAKMKKFYQPDKERKMITIKGSVHQNFDDFTFVTGKIIGNKLTLKGEIDSRVAIDLTNKASMAFLQKHLGLQKDFDQWDPLVEGDDENLIPGSPFDAVTQVPAQQHSPGSQTQN", "text": "FUNCTION: Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response (PubMed:10066756, PubMed:18434304). At the lipid- aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10066756, PubMed:18434304). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position. Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups (By similarity). Hydrolyzes and inactivates platelet- activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3- phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells (PubMed:10066756, PubMed:18434304). Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in lipoprotein particles and uncontrolled pro-inflammatory effects (By similarity). As part of high-density lipoprotein (HDL) particles, can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall (By similarity). Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space Note=Associates with HDL particles in plasma. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MDEDGGGEGGGVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDEFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFIAMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK", "text": "FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays a role in the epithelial polarization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein Cell junction, adherens junction Cell junction, tight junction Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate."}
{"protein": "MSEYTNEHFNNRELSWLDFNERVLEEAMDERNPLMERLKFLAIFSSNLDEFYMVRVGGLKDEVLAGFNRPEDKTGLTPKQQIKSISMRAQELVETQYATYKKITKQLSNQHVRFLRTKHLNKTQQDFVKEYFRTHVFPVLTPIAVDAYRPFPMLLSKSLNIAVEIASNGEGKKRLALVQVPSVLPRYLELPTDDEEHTDLILLEDLIIQFIDSLFKGFVVESTMPFRITRNADMPFHEEGSRDVLKQIEKELKKRRYGVAIRLEVQQRSLRKELLFMLQDVLDLHDRDIFIVDGPIDLTFLFGIYNQIGMEYDDMINETLIPFIPEGLESGKDLFQSIAKQDYLLHHPYHSFDPIVRFIVQAAKDPNVLAIKQTLYRVSGDSPIIKALTDAAESGKQVTVLVELKARFDEEKNIQWAKQLEKAGAHVIYGYKELKTHSKITLVVRILEGGVLQRFIHLGTGNYNDSTAKLYTDIGLLTTNEELAEDATNFFNWLSGYGERPSWHQFETSPDDMKDFFLNKIDDEIKLHEKYGNGRIVAKMNSITDRAIITKLYDASSAGVKIDLIVRGICCLRPGIKGVSENIKVISIIDRYLEHSRIFYFYQNGKEDLYCSSADWMTRNMKKRIEILFPILNASHKTYIKDMMALQLVDNVKARRQRSDGRYVYVKRETNEEEIQSQIIIHQYTGGRWNNIPSVFEREPSNWAEREVLRLRAENEKMTDD", "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": "MTALNHWQPSADIKNLLKRAKIIAEIRQFFTERGLLEVETPVLSEFGVTDLHLSTFSTEFLAPFGEQSKTLWLSTSPEYHMKRLLAAGSGPIFQISKVFRNEEAGNRHNPEFTMLEWYRPHFHMHRLINEVDDLLQQILDCPPAESLSYQFVFQEYVGLDPLSAERSELIEAARKHNFMAEDNEDRDTLLQFLFSEVVEPQIGKERPIAVYHFPSTQAALAQVSPEDQRVAERFEFYYKGLELANGFHELADAQEQRHRFELDNQQRQKCELPTREIDERFLAALEAGMPDASGVALGIDRLMMIALDCEKINDVISFAVDNA", "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": "MKDVIKDLSELRMSYEKGELHEAQVDTHPHEQFLQWFNHALQSNLHEPYAMSLATCNRQGRPHVRTVLLRGATAQGYDFYTNYDSQKGIDLAENPYAELLFYWPSLERQVRIGGIVNKISEHESTDYYHKRPRDSQIAAHISTPQSGIIANREELQQRFNRLYEQVGQQTVLSKPEFWGGYRLQADYYEFWQGRPNRLHDRLSYQNTDGTWVVQRLMP", "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": "MSGDFDTIRDASSPDEVQLVRLLEEKIKSLQIEIENLRKELNYYKAEMEKMLSPPLIEAVVLDVLPDGRVLVRSSSGPNLVVNIASHIDQKLIKPGISVALNQRGSTILEVLPQKEDPIVKTMEIIERPNVTYSEIGGLEEQIRELREVVELPLKNPEIFREIGVEPPKGVLLYGPPGTGKTMLAKAVATESNAVFIHVVASEFAQKFVGEGARIVRELFEMAKRKAPSIIFIDEIDAIGAKRIDIGTSGEREIQRTLMQLLAELDGFDPLDNVKIIAATNRIDILDPALLRPGRFDRIIEVPLPDFKGRTEIFNIYLKKMKIEDNINLELLSQLTEGFSGADIKNVCVEAAYMAIRDGRNKVTMNDLVEAINKINVKRNKMESMKERREKYS", "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": "MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQLQPSGNNRRGWNTTSQRYSNVIQSSSFSKSTPWGGSRDQEKPSFGSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFVSPGFPVNNSSSDNAQNFSFKTNSGFAAASSGSPAGFRSSPAFGAAASTSSAISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAPAFGGGSSVAGFGSLGSHSHAAFSKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQFQSKKFTLGKIPLKPPPLELLNI", "text": "FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Excluded from the nucleolus."}
{"protein": "MKPPILIIIMATIMTGTMIVMLSSHWLLIWIGFEMNMLAVIPVLMKKYNPRTMEASTKYFLTQATASMLLMMGVTINLLYSGQWVVSKISNPAASIMMTIALTMKLGLSPFHFWVPEVTQGITLTSGMILLTWQKIAPMSVLYQISPSINTNLLMLVALVSVLVGGWGGLNQTQLRKIMAYSSIAHMGWMAAIIIYNPTMMILNLVLYILMTLSTFMLFMLNSSTTTLSLSHMWNKFPLITSIILILMLSLGGLPPLSGFIPKWMIIQELTKNNMIIIPTLMAITALLNLYFYLRLTYSTALTMFPSANNMKMKWQFEHTKKTILLPPLIITSTMLLPLTPMLSILD", "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": "MKNVDDLIASAAELADRGLSKGEIADELNVSRETASWLVERSGAATEPEPRAEPEGPDDIHVDWNAIGSGGKRLTYVGRALADLLMETNGEADVTVGIEKAGVPLATSVSRELETTLGAYSPAKHQWDEGDLEDLGGGFSRNFSPVEGRDCFIVDDTVTSGTTLRETIDAIRSEGGEPLACVVIVDKQGVEEIDGVPVHSLINVVRVGEQ", "text": "FUNCTION: May have some orotate phosphoribosyltransferase activity, but not enough to ensure growth in the absence of the physiological OPRT. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MATPMIAGAAVAAAAVAGRYGILAWQAFKARPRVPRMRRFYEGGFQSSMTRREAALILGVRESVVADKVKEAHRRVMVANHPDAGGSHYLASKINEAKDMMLGKSNNSGSAF", "text": "FUNCTION: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM14 family."}
{"protein": "MWLELILASVLGFVIYWFVSRDKEETLPLEDGWWGPGSKPSAKEDESIRPFKVETSDEEIKDLHQRIDRFRASPPLEGSRFHYGFNSSYLKKVVSFWRNEFDWRKQVEILNQYPHFKTKIEGLDIHFIHVKPPQLPSGRTPKPLLMVHGWPGSFYEFYKIIPLLTDPKTHGLSDEHVFEVICPSIPGYGFSEASSKKGLNSVATARIFYKLMSRLGFQKFYIQGGDWGSLICTNIAQMVPNHVKGLHLNMSFISRNIYSLTPLLGQRFGRFLGYTEKDLELLYPFKEKVFYNIMRESGYLHIQATKPDTVGCALNDSPVGLAAYILEKFSTWTKSEYRELEDGGLERKFSLEDLLTNIMIYWTTGTIVSSQRFYKENLGQGVMVHRHEGMKVFVPTGYSAFPSEILHAPEKWVKVKYPKLISYSYMERGGHFAAFEEPKLLAQDIRKFVSLAELQ", "text": "FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water. May play a role in the metabolism of endogenous lipids such as epoxide-containing fatty acids. Metabolizes the abundant endocannabinoid 2-arachidonoylglycerol (2-AG) to free arachidonic acid (AA) and glycerol (By similarity). SUBCELLULAR LOCATION: Microsome membrane; Single-pass type III membrane protein Endoplasmic reticulum membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the peptidase S33 family."}
{"protein": "MPRSTARAAWKRELAATLALGLPLVLTNLAQMAMTVTDVIFIGRLGSQALAASALGANLFTAIEFFGLGLVAATAPMVAHALGRRGNAVRDVRRTVRQGLWTAVIYSVPGCLLLWHGEAILLAIDQPPELAAQAGAYLRALMWAMPPFLGFLVLRSFVAALQRPRSAFLIALAAIVLNVFGNWVLVFGNLGAPALGLVGAGLASALATLGLFLGMVGVVCLDRRFRRYHLFGDVWQPDWQRLAEFWKLGLPIGAATAFEVTIFNAAAFLMGWLGEPELAAHAIAIQIASVTFMIPYGIAQAATVRVGHAYGARQPDQVARAGWCAFSLGIGSMAIAAALMLLAPGLLVSAFLDIGDPANAQVLRLATAYLAVAALFQIVDGAQVLGAGMLRGLHDTRVPMLYAALGYWGVGLPSGAALAFWAGWRGVGVWSGLAIGLALVAVLMMQRWLRRDRVGLLRRA", "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": "MANEFNYGTGRRKTATARTRLYAGSGQIVVNGRPFEDYFPRKSLQMIIRQPLVLTKNVERFDIKVNVCGGGVTGQAEAVRHGISRALLELEPELRGALKRAGFLTRDARKKERKKYGQRAARARYQYSKR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MDGDGLGRLIGSEIHGFHTLQDLDVQTMLEEAKSRWLRPNEIHAILCGRIILFDRKMLRNFRKDGHNWKKKKDGRTVKEAHEHLKVGNEERIHVYYAHGEDNTTFVRRCYWLLDKARENIVLVHYRDTQEAATTSGDSISSPISVSEQTFPNRVAAEDIDTVVRNHDISLHDINTLDWDELLVPTDLNNQSAPTVDNLSYFTEPLQNAANGTAEHGNATVADGSLDALLNDGPQSRESFGRWMNSFISESNGSLEDPSFEPMVMPRQDPLAPQAVFHSHSNIPEQVFNITDVSPAWAYSSEKTKILVTGFLHDSYQHLERSNLYCVCGDFCVPAEYLQAGVYRCIIPPHSPGMVNLYLSADGHKPISQCFRFEHRAVPVLDKTVPEDNQDSKWEEFEFQVRLSHLLFTSSNKLNVLSSKISPHNLRDAKKLASKTNHLLNSWAYLVKSIQGNKVSFDQAKDHLFELSLKNRLKEWLMEKVLEGRNTLDYDSKGLGVIHLCASLGYTWSVQLFSLSGLSLNFRDKQGWTALHWAAYYGREKMVAALLSAGARPNLVTDSTKDNLGGCMAADLAQQNGYDGLAAYLAEKCLVAQFRDMKIAGNITGDLEACKAEMLNQGTLPEDEQSLKDALAAYRTAAEAAARIQGAFREKALKAARSSVIQFANKEEEAKSIIAAMKIQNAFRKYDTRRKIEAAYRIQCRFQTWKIRREYLNMRRQAIRIQAAFRGLQARRQYKKILWSVGVLEKAVLRWRQKRKGFRGLQVAAEEDSPGEAQEDFYKTSQRQAEERLERSVVRVQAMFRSKKAQQDYRRMKLTHEEAQVNHLTFLNLSFGKKNSNRR", "text": "FUNCTION: Transcription activator that binds calmodulin in a calcium- dependent manner in vitro (PubMed:12218065). Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CAMTA family."}
{"protein": "MTSEQFEYHLTGKEILEKEFKTGLRGYNPEDVDEFLDMVIKDYSTFTQEIEALQAENIRLVQELDNAPVRTTTQPAPTFQAAAQPAGTTNFDILKRLSNLEKHVFGNKLDDNE", "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": "MPAAIDKDENIQKEGKRIELVKDSPKQFAASGAAAVSAQPNSDKLADVSPLHAERTVAQAQEASVSSFNEEEVIHDLQHYLPSQAPLKDFIHHNTLHAFQNYPFHEGTRRAKKIFGYFPSLQLREYRDLYEAGRIRKDILERVISEQKGAQHLEDWMQRLLEKEYDDSVSPRIGKLRANWKRHYPIDLDLMVHPLLFRILCSYLDQGISIWGFPIGHKGFLAALKEMEEKSFASFFKTKRAKKLLVSGNCKMADLLKLLVGDETLYAQYLFDQQFAHPGWSGMVASVEAQPASLLNPKNITVHDLVVFELLLEIDALDSYFGESWEPIAHILEERPEPLFADVPETEVDTVFSLWHDAFEWTYYDQVLTGIALQDKTWERKIENRSFQTYFCIDDRLTSFRRYLEQLDPDCETFTTAGFFNVELYYQPENGKFYTKCCPAPVFPKFLVKEIGNKQKIKKEVHFSKLTHSLFQGWFISQTIGFVSALRLALNVFKPGSMPAGASSYTHVDKNATLTIENKDPNDKENGLQIGFTIDEMVQRVQGVLTSTGLNGVDKTFAPIVYMIGHGASSVNNPHYTAYDCGACGGRPGSVNARTFCYMANHPKVREALKERGIIIPPTTQFLPGLHDTTRDEVAFFDEEILSEENAGKHRRNTLVINEALDLHAKERSRRLVSIDTKMSPKEIHEEIRRRSVSLFEPRPELNHATNAVSIIGRRSITENLFLDRRASTSTYDYRTDPEGKFLTMSMGPIALVMGGIDLEYFFSRTDNHKMGAGTKLPHNVMGLIGVANGADGDLRTGLPSQMIEIHDPVRLLVIIEHYPDVALKVIKSQTANYSFYENYWVHCLALHPDTGELWLYKDGSFSKIYKPLLNDLETVSDLSALMERAKKAESIETLDAVQENLPVYFIEKKERVKK", "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": "MSRVGKLPIEIPVGVEVCVNGRTVSITGPKGSLYLDIAEQIGVSVSDGKVLVSRSDDSRTARALHGLTRALIANNVHGVLHGYTKTLEIVGTGYRVSKKGENLELALGFSHPVFVDPVPGVSFGVEGNSKIIVSGIDKQAVGEAAASIRKLSKPEPYKGKGIRYSDEIVRRKVGKAGK", "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": "MQQIQRDIAQALQVQPPFQSEADVQAQIARRIAFIQQCLKDAGLKTLVLGISGGVDSLTAGLLAQRAVEQLREQTGDQAYRFIAVRLPYQVQQDEADAQASLATIRADEEQTVNIGPSVKALAEQLEALEGLEPAKSDFVIGNIKARIRMVAQYAIAGARGGLVIGTDHAAEAVMGFFTKFGDGACDLAPLSGLAKHQVRALARALGAPENLVEKIPTADLEDLRPGHPDEASHGVTYAEIDAFLHGQPLREEAARVIVDTYHKTQHKRELPKAP", "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": "MAQDVIANGGTPEIGNLATPINSSPFTRTFINALPIYRRGLSSNRRGLEIGMAHGFLLYGPFSILGPLRNTETAGSAGLLATVGLVVILTVCLSLYGNAGSGPSAAESTVTTPNPPQELFTKEGWSEFTSGFILGGLGGAFFAFYLASTPYVQPLVKIAAGVWSVH", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PsaL family."}
{"protein": "MLSSFFLTQHLEAGTDEAGRGCLAGPVTAAAVILPENFESKILNDSKQLSEKTREQLKPIIEALAISFSVTHLDPLIIDEINILNASLKAMQECVLQLNPTPLYIIADGNRPLLSKNSFKKCSGKIFTNREIEILQSIPSSSIIKGDSKYLSIAAASVLAKTYRDEYMNTIHEEFPMYNWKKNKGYPTKEHREAIRKYGVTKYHRMTFRLLPEQTVLDL", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MLTDIEISRQASLQPIESIATAFGILPHELSPYGRTKAKVDLAITNRIKDNKHGKLVIVTAVTPTPFGEGKTVTSIGLTQGLQAIGKKSCACIRQPSMGPVFGIKGGAAGGGLAQVVPMEDLNLHLTGDIHAVTSAHNLAAAAIDARLYHEQRLGCEAFREQSGLAPLDIDPEKILWRRVVDQNERSLRTITVGLGEVNGPVHQGGFDISAASELMAILALSRDLKDLRARIGRIVLAQNKQGDYISAEDLGVAGAMTAIMSQAISPTLMQTLSGAPCLIHAGPFANIAHGNSSIIADDIALRLADIVVTEGGFGSDMGFEKFCNIKTRQSGNAPDAAVLVVTVKALKSHNPDAGSEMDKLAAGYANLSWHISNVAKYGLPLVVAINRFAEDTQEELEWLKARVLQEGVFACEVCEAFTQGAEGAMALARAVVRATEQPSQFRYLYETKQSIEAKLLTIAEAGYGANGISLSDTAKAQLAQLQRQGFDKLALCIAKTPMSVSHDPKLKGAPQGFELPIAELKLNAGAGFITALVGKVMTMPGLGIRPGYLNIDIDERGEITGLA", "text": "SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family."}
{"protein": "MLQVYLVRHGESEWNAARRIQGQSDSPLTETGEHQARLVAQRVKSESITHIITSDLGRTRRTAEIIAKVCGCEIILEPRLRELHMGVLERRNIDSLTSEEEKWRKKVLDGTPGGRIPKGESMDELAVRMRAALENCRNLPVGSRPLLVSHGIALGCLVGTILGLPAHAERRLRLRNCSLSRVDYQHSPWLASGWIVETAGDITHLDTPALDELQR", "text": "SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB subfamily."}
{"protein": "MPIDTPYEDLLRLVTERGTPKSDRTGTGTRSLFGHQMRYDLSAGFPLITTKKVHTKSVIYELLWFLRGDSNVRWLQEHGVTIWDEWASETGDLGPIYGVQWRSWPTPSGEHIDQISSALELLKSDPDSRRNIVSAWNVGEIPQMALPPCHAFFQFYVADGKLSCQLYQRSADLFLGVPFNIASYALLTHMMAAQAGLDVGEFIWTGGDCHIYDNHTEQVALQLSREPRPYPELVLAPRDSIFDYTYEDIAIVNYDPHPAIKAPVAV", "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": "MTELSGQPPKFGGSTGGLLSKANREEKYAITWTSASEQVFEMPTGGAAIMNEGENLLYLARKEQCLALGTQLRTKFKPKIQDYKIYRVYPSGEVQYLHPADGVFPEKVNEGREAQGTKTRRIGQNPEPVTIKFSGKAPYEV", "text": "FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin- oxidoreductase in photosystem I (PS I) reaction center. SIMILARITY: Belongs to the PsaD family."}
{"protein": "MQSTSAQSSASHPERVFNFSAGPATMPESVLREVQDEMLCYPGAGASIMEISHRDKLFVDVLHDAESTIRELLNVSDDYSVMFMQGGATLQFSAIPANLLRGSGKRAQYVLTGSWGKKAVKEAKKEGDVDVLFDAAESNYDHIPSASDLACPDDAAYMYYCSNETIQGVQFPTEPNCPDSVPLVSDASSDFLCRPLPIEKYGLLYACAQKNAGPAGVSVVIMRKDLLDKADPNIPGYLHFKNHHDNDSEWNTPPTFAIYVLGKVARWLRDDMGGLEKMESINHEKSQQLYSVIDSSNGFYRGHAQTDCRSLMNVTFNLPSDELTAKFIAEAAEHKLAALKGHRSVGGIRASIYNAMPREGVNALASFMNNFASKNS", "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": "MVTIRLARGGAKKRPFYQVVVTDSRNARDGRFIERVGFFNPIAAGQAEALRLDLDRIEHWLGLGATVSDRVSSLIKDAKKAA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MAAEPTARLSLLSDLTPPSLERTWLTAPHPTLPIVATCSSDKTVRVYSLTNFRLLSTISGGHKRSVRTCAWKPHVKGESVLATGSFDATVGIWRRWDSYGQTERGAADWGVGDSAGSGTQAKGLADGYGAGGDEENENEDEDEEWRFAVLLDGHDSEVKSVSWSPSGMLLATCSRDKSIWIWEDLDDGDNNFETVAVMQEHQGDVKCVAWHPAEDCLASASYDDTIRLWREDLDDWGQVACIKGHQGTVWCVDWEGVDSVPCGAAADLAEQWRATHALSGPRLVSCSDDRTVRIWRRQPKEPRAQQNTSPFGSSGIPSIIRPTGTDETWEEECTLPQAHDLSVYTVAWSKRTGLLASVGADGRIVVYAERFVGGDSATQAMETEPSADAAEGAPAPSTEWTVIATMDGAHDIYEINHVAWAKRADRGKAEGEDEEVLVTTADDGGVKVWTIAR", "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": "MKFLTSLLLLFVVVMVSAVNLSMAKESANQLTERLQELDGAAIQEPAELNRHKRLTCEIDRSLCLLHCRLKGYLRAYCSQQKVCRCVQ", "text": "FUNCTION: Sapecins, which are potent bactericidal proteins, are produced in response to injury. Sapecin B is cytotoxic to Gram-positive bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the invertebrate defensin family. Type 1 subfamily."}
{"protein": "MNIKSLLLGSAAALVAASGAQAADAIVAPEPEAVEYVRVCDAYGAGYFYIPGTETCLRVHGYVRYDVKGGDDVYSGTDRNGWDKGARFALMFNTNSETELGTLGTYTQLRFNYTSNNSRHDGQYGDFSDDRDVADGGVSTGTDLQFAYITLGGFKVGIDESEFHTFTGYLGDVINDDVVAAGSYRTGKIAYTFTGGNGFSAVIALEQGGEDVDNDYTIDGYMPHVVGGLKYAGGWGSIAGVVAYDSVIEEWATKVRGDVNITDRFSVWLQGAYSSAATPNQNYGQWGGDWAVWGGAKFIAPEKATFNLQAAHDDWGKTAVTANVAYQLVPGFTITPEVSYTKFGGEWKDTVAEDNAWGGIVRFQRSF", "text": "FUNCTION: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the alphaproteobacteria porin family."}
{"protein": "MFSFYFNDNKITKLLMVGYGSTGKSVCDFLANFIDITVDISQNDDEFVNYDLGSYDLITVSPGIPLNKSPYRVLTKFKDKIVSDIDIFYQYIKDTKAKTIAVTGSNGKSTVVTMTDFVLKDLGYKSILVGNIGTPALNKIGEKFDYCVVEVSSFQIDLFNCVRFDLGCIINVSPDHLDRYQNFEQYKQSKLNLAKFSNDFFVYDVHNNGIKYAGEYQIIRGAIYRNSTKLLDIAETKLFGEHNLENIIVVLNILDRLGLDINQAIDSIKKFKGLEHRCKIVKKVNGTTYINDSKGTNVGATIAALNSITNSKNIILLLGGVAKGGDFSLMIKSLDKYVKYVYIYGADKEYIESYIKGYCKYQLCNNMKQAFELASQKANSNEIVLLSPACASFDEFSGYAQRGEVFQNLVAQLEQKS", "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": "MLRIPVRKALVVLSKSPKGCVRTTATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSKKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQTFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARLRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKVLFLLGADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDDIEGANYFQQANELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQAVEEPSIC", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (By similarity). Essential for catalysing the entry and efficient transfer of electrons within complex I (By similarity). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MSIATSLGFPRIGRRRELKSALEAHWAGELSEAGLQEAARLLRAESHSLQQGLGIGHIPSNDFALYDHVLDTACMVGAIPPGYGWRGGEVTLPTYFALARGTGGGDAAAGLPALEMTKWFDTNYHYLVPRLAAGQHFAVTANRPLALFREALARHRRTRPVLLGPVSFLLLAKTDDGSDPLDLLDRLLPCYAQVLAELAAEGCAWVQMDEPVLALDLAPKARAALRHAYETLARGATPRLLLASYFAPIADNLPTALALPVAGLHLDLVRGRDDLAPVLAAIGPATWLSLGLVDGRNVWRADLRAALATAREAARALGGSERLMIAPSCSLLHVPVDLAQEDRLDPAIRPWLAFATQKLAEVATIARGLDEGEGAIAEALEASDAALRTRRDSARVHRTDVAARLLGATPEMERRPAPHAARRARQRQRLPLPAFPTTTIGSLPQTSGVRRTRAALARGEIGAAEYDEAIATWTEDAIRLQERIGLDVLVHGEFERNDMVKYFGEQLDGFAFTRHGWVQSYGSRCVAPPIIWGDVARPRPMTVRWARHAQSLTARPVKGMLTGPVTMLQWSFVRDDLPRETVCRQIALALRDEVADLEAAGLAIIQVDEPAFREGLPLRTADREAYLRWAVSCFRLATAVVRDDTAIHTHMCYAEFQDIMPAIATMDADAISIETARSRMELLEAFAGHGPSAYPAEIGPGVWDIHSPRIPPEEEILALLRLARRKLADDQLWVNPDCGLKTRNWREVIPALENLVGAARRLRAEAIPA", "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": "MKAVVLTLAVLFLTGSQARHFWQRDEPRSSWDKIKDFATVYVDTVKDSGREYVAQFEASAFGKQLNLKLLDNWDSLSSTVSKLQEQLGPVTQEFWDNLEKETEGLREEMNKDLQEVRQKVQPYLDEFQKKWQEEVERYRQKVEPLGAELRESARQKLTELQEKLSPLAEELRDSARTHVDTLRTKLAPYSNELQQRLAARLESIKEGGGASLAEYQAKAREHLSVLSEKARPALEDLRQGLLPVLESFKASVQNVLDEATKKLNTQ", "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": "MDRILTKEEKQALISLLDLEPQYWGDYGRMQKCYKKKCLQLHPDKGGNEELMQQLNTLWTKLKDGLYRVRLLLGPSQDPNASTSTSRPGEFYNPDTGGYWSYSYGSAGYSDQQKKYWEEFFSKWDVNEDLTCQEELSSSEDEFTPWHPNPPPSPVSISSDSSSSSCDEEYPRNSSRKRKRVHANGSPNTPIQPNKRAHTPGGGRTTIRGDTDIPRTPARESQSTFGSYFNSTEELEEEISQTQQSHHNTTPKKPPPTVSPDDFPTILRGFLSHAIFSNKTQNAFIIYSTKEKCEVLYEQIDKYNPDYKGIFIMKQTEAFVMFMTPGKHRVAAVKSYCCKFCTVSFLLCKAVTKPLELYNCVAKCDDFQILKENKPGLYHFEFCDEKKEVKQIDWNFLTSFAVENELDDPLVIMGHYLEFSQCESSCKKCAEALPRMKVHWANHSQHLENAELFLHCKQQKSICQQAADNVLARRRLKVLESTRQELLAERLNKLLDQLKDLSPVDKHLYLAGVAWYQCMFPDFEMMLLDILKLFTENVPKKRNVLFRGPVNSGKTSLAAAIMNLVGGVALNVNCPADKLNFELGVAIDKFAVVFEDVKGQTGDKRHLQSGLGINNLDNLRDYLDGSVKVNLEKKHVNKRSQIFPPCIVTANEYFFPQTLYARFHKVYNFEVKDFLAKSLEENSYMGRHRVCQSPLTMLIALLWNVPTENFDKSLKEKVETEKKVLSDMCNFTTFAEMCLNIQRGADPLEAL", "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 (By similarity). SUBCELLULAR LOCATION: Host nucleus."}
{"protein": "MAEAFAGTWNLKDSKNFDEYMKALGVGFATRQVGGMTKPTTIIEVAGDTVTLKTQSTFKNTEISFKLGAEFDETTADDRKVKSLITIDGGKMVHVQKWDGKETTLVREVSGNALELTLTLGDVVSTRSYVKAE", "text": "FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MQAKKRYLILFSAGVCLILLFYLQGPASRRTPKRGDDPHPHWPHFSDPLRAFIPWDQTETEDYNVRASPRHKRDDSTGADKCRMDSCFDFELCKRNGFKVYVYPQQKGEKISESYQNILSSIEGSRFYTSDPGQACLFVLNLDTLDRDQLSPQYVHNLKTKIQNLNLWNNGRNHLIFNLYSGTWPDYTEDLGFDIGQAMLAKASISTESFRPNFDISIPLFSKDHPRTGGERGFLKYNTIPPFRKYMLVFKGKRYLTGIGSDTRNALYHIHNAEDVVLLTTCKHGKDWQKHKDARCDKDNAEYDRYDYKEMLHNSTFCLVPRGRRLGSFRFLEALQAACVPVMLSNGWELPFSEIIDWRTAAVIGDERLLLQIPSTVRSIHQDRILSLRQQTQFLWEAYFSSVEKIVLTTLEIIQDRVLQHSAHSTLMWNRLPGGLFTLPQYSSYLGDFPFFYALLGIKPHQKFTAVIHAVTPLVSQSQPIFKLLVAVAKSQFCAQIMVLWNCDKPLPSKHRWPATSVPVIVIEGESKVMSSRFLPYENIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWDSNKERWGYTSKWTNDYSMVLTGAAFYHRYYNYLYTHYLPGSLKGLVDQLSNCEDILMNFLVSAVTKMPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQTCMNKFASWFGTMPLVHSQMRLDPVLFRDQVSILRKKYRDIERL", "text": "FUNCTION: Glycosyltransferase required for the biosynthesis of heparan- sulfate. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 47 family."}
{"protein": "MLKEFREFALKGNVVDMAVGIIIGGAFGALVNSLVNDLLMPPLGLLLKGVDFSNLFVVLKEGTPPGPYIALADAKTAGAVTLNYGLFVNALIGFLIMAFAVFLLVRSINRLRSLSEKSAAPAVAPQTKECPFCFSIIPLKAVRCPNCTSQL", "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": "MAVKIKLTRLGKIRNPQYRVAVADARTRRDGRAIEVIGRYHPKEEPSLIEINSERAQYWLSVGAQPTEPVLKLLKITGDWQKFKGLPGAQGRLKVAAPKPSKLEVFNAALAAADGGPTTEATKPKKKSPAKKAAKAAEPAPQPEQPDTPALGGEQAELTAES", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MTMIKLEQIFWHVWINGDLVPYQFARIHVLTHSLHYSGSVFEGERAYNGKVFKLKEHTERLIKSAEALGLKVPYSVDEIIKAHELVIKQNNIKDAYIRPLIWCGDESLNITNPDLSTNLLIAGIPSMPRSFEKGINLHVGRWRKAIPDSTPVQSKSAAQYNMAITSKKEAKALGYDDALLLDYEGYIAECTTTNIFFVKDKTLYTPIADRFLNGITRQTIIEIAKDLGLEVKEERLKLEQIENFTGCFVTGTAIEVQNIDSIDLGNKKITFDDHQIADRLKKEYGRIVRE", "text": "FUNCTION: Acts on leucine, isoleucine and valine. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MGCCGCSGGCGSGCGGCGSGCGGCGSGCGGCGSGCGGCGSGCGGCGSSCCVPICCCKPVCCCVPACSCSSCGSCGGSKGGYGSCGGSKGGCVSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCVSCGGSKGGCGSCGGSKGGCVSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGCSQCSCCKPCCCSSGCGSSCCQSSCCKPCCSSSGCGSSCCQSSCCKPYCCQSSCCKPCCSSSGCGSSCCQSSCCNPCCSQSSCCVPVCCQCKI", "text": "FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated protein (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 5 family."}
{"protein": "MRRDEYFEKLLEVIEELKIEAEEKPIIVEGKRDVESLEKLGVEGTFIIIAKTPIYLIADELVRKRVKEVILLTDFDRRGRMLAKAIIEEFRHRGIKVNTKIRHEIFIYTNSGIRDIESLFSYVNKRLF", "text": "SIMILARITY: Belongs to the UPF0292 family."}
{"protein": "MIFETLDEFAGAVPPMRGLIGLDLGTKTIGVALSDRLLTSASALETVKRKKFGVDADALAGLIAKHEVGGIILGLPRNMDGSEGPRAQATRAFALNLSRRGDFAHLALGFWDERLSTVAAERALIAADTSRKRRSEVIDAVAASYILQGALDRLRHLRAV", "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": "MGLDSPDMRPELSQYKHLSAGKVREIYEIDEHHILMVASDRISAYDFILDTEIPDKGRVLTAMSQFFFDAIDFPNHLAGPIDDPRIPEEVLGRAMVCKKLAMMPFECVVRGYLTGSGLEEYRQTGTVCGITLPEGLVESSRLPEPIFTPATKADVGDHDINVSFDVVEERLGEARANQLRDASIAIYSRAAEIALERGVILADTKFEFGLDENGELVLGDEVLTPDSSRYWPAEGYEAGHVQPSFDKQYVRNWLTGPKSGWDKNSGVQPPALPGSVVEATRERYIEAYELISGNKFSTWIGCCV", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MQELNQIFNTIKDIAKEISEVIKYADLGYTTHENATGDTQLKLDVKSDEIITAKFKQLSCVKALISEEKEDELEINKNAKFIIAYDPLDGSSLVDVNFAVGSIFGIYEDEVKPENLIAAAYSIYGPRLELVIAEKKGALPKFYRLGKDGEFKFVKELELKEKGKLNATGATQKGWSQTHRNFINELFNEGYRLRYSGAMVSDLHQILLKGGGLFSYPATSDHPNGKLRVVFEVLPFAFIYENAKGATTDGKNQTLFDIKIEKIHQTTPCFFGSRDEISLLHKFYEQK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
{"protein": "MKPNYNVDRAPKRSDEPVWWSLFGAGGTWFAMITPVTVLVLGILVPMGVINAEALSYDRVVSFATSIIGALFIIATLALPMWHAMHRVHHGMHDLKFHTGVVGKIACYAVAGLISALAVVFIFML", "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": "MSKSLVIVESPAKAKTINKYLGSQYVVKSSVGHIRDLPTVGSSTGEKAKPISTKGMDAEEKAKIKAEKERNALVKRMGIDPYHDWKANYQILPGKEKVVSELKSLAKKADHIYLATDLDREGEAIAWHLREVIGGNDDRFSRVVFNEITKNAIKQAFEKPEQLNMDRVNAQQTRRFLDRVVGFMVSPLLWKKVARGLSAGRVQSVAVKLLVEREREIKAFQPEEYWEVAVLTNNQNKQAIRLDVTDYKGKKFDPKNQKEAQSAVDFLNVSDYVVTDLETKPTSSRPRAPFITSTLQQTASTRLGFGVKKTMMLAQRLYEAGYITYMRTDSTNLSQDALNMARTYIENHFGAQYLPEKPNFYSSKENAQEAHEAIRPSDIRALPESLEGMEKDAVRLYDLIWCQFLACQMPPAQYDSSTLTVTAGDYTLKAKGRILRFDGWTKVLPQIGKNPEDQELPSVTVSEKLALKEVQPTQHFTKPPARFTEAALVKELEKRGIGRPSTYAAIISTIQERGYVRTENRRFYAEKMGEIVTDRLNESFGELMNYDFTANMEDTLDKIASGSVNWKTELNQFFKDFSSQLSKAELDELEGGMRPNSLVETDIKCPTCGRNMAIRTASTGVFLGCTGYALPPKERCKTTINLIPEAELLNVLDESSETKALMDRKRCTKCGTAMDSYVIDAHRKIHICGNNPNCDGYLIEEGSFKIKGYDGPVVECDKCGADMHLKLGRFGKYMGCTNCDNTRKILKNGEVAPPKEEPVHFPELKCEKSDAYFVLRDGASGVFMSAHNFPKSRETRPVKIAELVQYRERLPEKLAYLADAPQKDPEENEAIVRFSRKEKKQYVTSEKEGKATKWIVDFTNGKWVERKK", "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": "MNEELQNQFMALDVYNQQVQKLQEELSNIDMMIMELLRSIESMEGLKSSKEILLPLGAGAFIKAEAQNPEKIILSVGVDVLLEKDVDEVIVDFQKSVKELEETKELVNTQIQKTNQEIVKLRSELEKRAAAIEQRNAQMRPKTN", "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": "MSLLDYFKSSKSKTASVAKERLQILVAHERYYRNKPSYLPQLQEELMQVIRKYVQVDQDAISVKFEQDDNQETLELNITLPDTQNPRNTQQDMIRNAL", "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": "MKLAIVPFFRELTWSQVRNLFHFAARRLTEERLPQVAGSLTFTTVLALVPILTIALAIFTTFPLFNTFRTSLEAYFVHNLMPKGIANTILGYLTQFSSKATRLSAFGAVALIVTAVAMMLMIDRVFNQIWRVKTKRPIVQRILVYWAIVTLGPLLIGASMTFTSYLFTATDGVVRGVPFVGAVFYTSISILLSMVAFTSLYIVVPNRLVEWRDAVVGGLLAAIAFEIVKRLFAAFVIKVPTYTVVYGAVAAFPIFLVWVYLGWLITLAGAVVTAALPIVKYERWWHVPQPGSAFVDAMALIAVLYEARASADSAVVDTKLLRDRTQLGFDESEALLEKMLDAGWVARLKSEGPKRMQWGKRITDGLDRWVLLANPEYLTLADVYRVFVFDAGGNEMLAKKVECAVEQGLYQSLANYFRESSEGDLPGQHLPVHQP", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0761 family."}
{"protein": "MALYFVYLSTLLALILLGDNWAAGTYASRYTQHVDENQSGAAAQSGSKVTSRHRNWCAYVVTRTVSCVMEDGVETYVKPEYQRCAWGQCSHVVLYRTYRKPRYKVAYKVVSEMEWKCCHGYSGDDCSDGSSAIHDSRARPTGEEGRSDSDRIRQLEEQIQSLNKNLHNLQKKIYEESQREGISGGNNLADAAQPGMKETIHSIQTKLDMLDNMTRVHDKTLTNINNHLVGGNGIENELDSRYGTLKEEILRELERRVTLSCSSCQTGVESIQRQHQEDRERIRELEKHISVMEQHHQQTLDLLSRSQSCCDSLDRKLSAIDRKVSSTAETYDILRGRLEKELRSNGNGGRGKAMEEKLNNRLRDLERRLNGTVRKTEQKCSHTETSMKEFVQREIGQIKNSVLGRNDDHGYRISTVEIDIQDLKRFINDHKNNLERLGNKTNDLDSGLKSAIHLCTETCAAKGSETEDTVKSLEWKVVANEEDIKKFDTKLKDISVSGDSLLDRVIDLSNDVQKIKDLTGQNGEHFNQIVTDVENLGRDCDVCSSIDGELQKIRNVTSYAFDKFQAELTVLGRKVFSDEHVCSQVCSNLQEEVGKLKEEVEKCTGQCMISMADHQRNVDNQNTVTRKLGKDLKSIQGELTGILQIFNSINDTLKGLRNTIQKHGNNITDLNTSKGKIYLELDQLYDDLNKHKVDSKGHFDSISSFNSNLMTEMGECRLSREGLDKRLSKMEDVCGRLDTLSENLKTIKDGLSKHVSGLWTCVNDLNSTVISHSETISRIHNVHLENIQGRMNNLNSSIRNVLKEFQIFTEQDFTGPPGLPGPQGEKGSKGPPGPRGPLGKEGPQGRVGPVGPPGLRGEQGPPGKDANVPRLSFSAALTRPQASSGTIIFNKVFINERKAYNPKTGVFTAPVRGRYFFSAVLTGHKNVKIEAVLSKSNFGIARGDSAGYQPEGLEKPMAEARHTPGSLVIFNIVLPLQEGDTICIDLVTGKLAHSVEPLTIFSGMLLYEESEDRL", "text": "FUNCTION: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
{"protein": "MKTSQLFYKTSKNANKEASVLSYELLEKAGYIFKTAKGIYTYTPLFWRVALKMMDIIREELNAIGGQELVLPILHPAELWQKTGRWEAFRSEGLLYTVKDREDKEFCLAPTHEEIVSMFVSQWLSGRKQLPIHLYQIATKFRDEIRPRFGLMRAKEFLMEDSYTFSDSPEQMNEQYAKLRQAYQNIFDRLEIQYVIVEADGGKIGKGKSEEFHVLSSLGEDTLCVSGHYGANIEAAVAQPPQYTYDKDYLPIEEVDTPDVRTIENLQDFFSVPPYRIMKTLVVKLSYGEKEKFTAIGIRGDRQINLTKIGSKLNADACSLASDEEIQKHLGVEKGFIGPLNCPIDFYADETTQCMTNFICAGNVKDKHYKNVNWDRDIPRPEYADFLLAEAGDLCPTNNHAPYEIFEGVEVAHIFNLGTRYTEGFDVVFQDEQGKPQSCWMGTYGIGIGRTLAACIEQLADDRGIVWPKAIAPFDISILYNGGDTACEEAAEKIYKELQGYGYAPLLDDRNERLGFKLKDSDLIGIPYKLILGKTFLNSGMLEIESRSIEKFSVEPKDFVHWCKRHLPSPRVFSPIP", "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": "MAIGFICSSPDAELFSEKSRMSSSVLLGCLLCCMDWSAAVPGKTEPFRKLFDAIMIKKLKSCSAAYPSDLDEGSMCDMADASPTSLELGLSKLDKES", "text": "SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. Highly divergent."}
{"protein": "MTATTTAQPSGPVPPASPTAARRLLLVHAHPDDEVITTGATMAAYAAEGAHVTLVTCTAGEEGEVLVPELAHLAADREDRLAEIRVVELANAMTALGVADHRFLGGVGCYRDSGMMGTPANDKPHAFWRADLDEAAAHLVKVVREIRPQVLVTYDENGGYGHPDHIQAHRVAMRAAELAADPAFAPEHGAVWDVAKIYWTAMPESVLAEGIQALKEAGDTSGFIAVESVEDLSFGTDDALVTTTIDGTAYMENKREGMRAYPTQISMGQGFFALSNSIGMEFMAHEFYQLVKGAAEGSDTGLEKDLFAGLGIADGTAAGVSQG", "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": "MAKTAKSKQSVDVADLTKAQAKVEWKRLALELETHDRLYYQEDAPKISDAAYDELRRRFNAIEKRFPELVSRDSPSQTVGAAPSGRFKKVRHAVPMLSLDNAFAEEDVRDFVGRIARFLKLAEDDRIAFSAEPKIDGLSMSLRYEGGQLVTAATRGDGAEGEDVTANIRTLKDVPQKLHGRNLPDICEIRGEVYMTKQAFLALNERQKEAGDTIFANPRNSAAGSLRQKDPTITASRPLGFFAYAWGDMSAMPAETQSGMIKWFEHCGFTTNPLTKLCHSVEELIAFHRAIEEQRAELDYDIDGVVYKVDRIDWQERLGFVSRTPRWGIAHKFPAERAMTVLKDIEIQVGRTGSFTPVGKLEPVGVGGVIVQNVTLHNEDYIKGIGNKGEVLREGRDIRIGDTVVIQRAGDVIPQVVDVLIDKRPADAEVFAFPRKCPCPLHTDVVREETAAGEEGSRARCTGEFACPYQKIEHLKLFASRRAFDIDGLGEKQIQFFFDEGWVKEPADIFTLQKRNAKLKLEEVEGYGETSVRNLFNAIEARREMALERFIYALGMRYVGETTALALARGYGSWEAFHDACLKVANGDEEAIAEMDALDQIGETVIKSVAAYFGEDHNRGIVERLTREVKILDAEKPKRNSPIATKTVVFTGTLEKMTRDEAKATAERLGAKVSGSVSKKTDYVVAGPGAGSKLKDAEKHGVKVLTEDEWLQLIGE", "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": "MEVNSKPGILKRIAGPVVTAVDLDAHMYDVVKVGNEELMGEVIKIDGADTVIQVYESTTGIRPGEPVINTGLSLAVELGPGLLTSIYDGIQRPLEVLIQKMGNFIARGVTAPGLDHEKKWTFKPVVHVGDNVVPGQIVGEVQETRSIVHKIMVPPLAKGGKVTKINAGDFTVDEIVIELDSGESFPMMQKWPVRVPRPYVEKHSPSIPLLTGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELQDPKTGNSLMERTILIANTSNMPVAAREASVYTGITLAEYFRDMGYDVALMADSTSRWAEAMREICSRLEEMPGEEGYPAYLSSRLSEFYERAGLVEPLAGGSGSVSVIGAVSPAGGDFSEPVTQNTLRIVKVFWALDANLSRRRHFPAINWLQSYSLYMAQLNDYYDEKVSPDWNKLRSWFMEVLQKEAELQEIVQLVGSDALPETEQITIEVARMMRELFLQQNGFDPVDTYCDLPKQLDMFKMIRTYADLAYAAQAAGVPPSQILAVKAKNEMPQVKFTKDYKPVLDKIYAGMEAEFKALRA", "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": "MPPYISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKTVVTQRRAAVAIAGCWILSLVVGLTPMFGWNNLSEVEQAWIANGSVGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPTCQKPSILIYIAIFLTHGNSAMNPIVYAFRIHKFRVTFLKIWNDHFRCQPKPPIEEDIPEEKADD", "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": "MELKFSTFLSLTLLFSSVLNPALSDLCNPDDKKVLLQIKKAFGDPYVLASWKSDTDCCDWYCVTCDSTTNRINSLTIFAGQVSGQIPALVGDLPYLETLEFHKQPNLTGPIQPAIAKLKGLKSLRLSWTNLSGSVPDFLSQLKNLTFLDLSFNNLTGAIPSSLSELPNLGALRLDRNKLTGHIPISFGQFIGNVPDLYLSHNQLSGNIPTSFAQMDFTSIDLSRNKLEGDASVIFGLNKTTQIVDLSRNLLEFNLSKVEFPTSLTSLDINHNKIYGSIPVEFTQLNFQFLNVSYNRLCGQIPVGGKLQSFDEYSYFHNRCLCGAPLPSCK", "text": "FUNCTION: Inhibitor of fungal polygalacturonase. It is an important factor for plant resistance to phytopathogenic fungi. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. Secreted, cell wall. SIMILARITY: Belongs to the polygalacturonase-inhibiting protein family."}
{"protein": "MKFHIITLGCPKNQVDSEGMSSILAAQGHTPVAHADDADVVVVNTCSFIAAAREETLDVLREVAARKTPGQYLVAAGCMAESHSALVAAAPGVDALLSTREWMRIGDVVDTLQREPAVAASSAAREIIPLSSAPASSDDLRVPGAYADWRTAPIRRRITGPSAYLKISDGCNLRCAFCTIPSFKGDMRSKAVGAILGEAQELADAGVKEIVLVAQHLTDYGRDLGLKDGLALLLDELCAVLPKDRWVRLMYAYPHGISERLIATMARHPQICHYLDMPLQHAHPETLRRMHRPPDSDRTRRLIADLRAAMPDIALRSTFIIGFPGETSAEFRALTAFLEEVQFDRVGVFRYSREPGTPAAALPDQIPQRVIERRWHTIMRLQQGISRQRNRRWVGRVIRVLVEGQGQTDDGRLLSVGRSFRDAPEVDGQVLFWGTAATGTFVDVRVTQALDYDLWGEMVEAPADDARSENGT", "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": "MRVLGLISGTSADGIDVAIAEIQGFQADLSVALLAFETIAYEPSLRDRILEVAAGFPLSVAELTALDAAIAQAFATAAQTLIQQHGAVDLIGSHGQTVYHQPLQAGQLGWSVQLGWGAAIAQQTGITTVSNFRSADLALGGQGAPPVPAVDLWLLGSDSENRCVQNIGGIGNLTWLPRRDHPDWQSEVRGWDTGPGNSLLDLAVQKLSQGRLSYDDGSQWAATGQIDQVLCDRWLQEDDYFRLPPPKSTGRERYGWQFLETWAAELDRLTAADQLATLTEFTAASIVNNYRHFLPALPDRVLVCGGGLHNQFLLQRLQQQLPTVKIASTDDFGVNSQAKEAIAIAVLAYWRQHNVPGNLPAVTGASGPALLGDVFART", "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": "MTIDSGFNHITVLLDEAVEALALRADGCYLDGTFGRGGHSRLILSKLGPQGRLLGFDKDPQAIATGQALAAEDGRFVIVQRSFAELGAEVAERGLAGKVSGILLDLGVSSPQLDDPERGFSFLNDGPLDMRMNPDQGISAAEFIATAPVEEIARVFKEYGEERFAGRMARAVVERREKQPFTRTADLAEVLKVANPAWEKGKNPATRAFQGLRIHVNNELGDLEAGLEAALDALEVGGRLAVISFHSLEDRIVKLFMRKLVKGEADNLPRNLPVQHKVFEPKIRLIGKAQFASEAELKANPRSRSAVMRVAEKLR", "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": "MSKKLGNNSKKIAFVHPDLGIGGAERLVVDAAVGLQELENEVTIYTSHCDKKHCFEEVSSNLLDVEVYGDFFPTNVLKRFHILFAIIRQFYLVLALIFTGKIKQYDYFIVDQLSFCIPLLCCFSRPECKILFYCHFPDQLLALKGGFLKRFYRMPFDLIEEWTTGISDQIVVNSKFTKGIFHKTFKGLKNIEPGVIYPCVDLNSATDTEEDKLMDEEVNEFFKGGKFFLSVNRFERKKNIGLAIQSFAKFKAQLPKNVSEDNRIKPRLVVAGGFDPRVLENVEYLQELNGLSESLNLKCFTIRGKLLIIPPATDILFLPSIKSSLKKSLIKNAELLLYTPSFEHFGIVPVESMLFKTPVLSANNGGPLESIVHFTSDNIATATGYSQEPNDELWSKTMHTFYTELDEATKLKLGENGLTRVHELFSRHQMSEAFMQNLIQSNSKDEEKGILYGILKMWRIELLFVLISYYLVRLYK", "text": "FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase group 1 family."}
{"protein": "MIALIQRVSQAKVNVKGETIGKIGKGLLVLLGVEKEDNREKADKLAEKVLNYRIFSDENDKMNLNVQQAQGELLIVSQFTLAADTQKGLRPSFSKGAPPALANELYEYFIQKCAEKLPVSTGQFAADMQVSLTNDGPVTFWLNV", "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": "MAFDLDTIRSAAQRVASSHGLDVVDVEYQGGAKHRMLRIFIEKNAEERAKLAAQSSGRVETIEVHEEMPREGMNPEHFSGVTHEDCSAFSTDFGTLLDVEELMPGASEYTLEVSSPGLDRKLQSRADYERFAGSLVKLSTFEPVNGNRHWQGRMAGLDGDTLRLDLTAMKQKGKGKEKKSAAETVEIALGNVEKAQLIPEI", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MKHNQNIDFVSIVIPVYNEEASLPELLSRTLAAADSMGKHYELVLIDDGSRDNSANIIEAAAAEPDSHVVGIILNRNYGQHNAIMAGFEHVRGDLIITLDADLQNPPEEIPNLVAKAEEGYDSVGTVRRHRQDSALRRYPSKLINKLVKRSTGVEMNDYGCMLRAYRRHVVKAMLECHERSTFIPILANGFARHTAEIDVHHSERSQGESKYGFMNLINLMFDLLTSMTTAPLRMLSIVGGGIASFGILFGLFLILLRLIYGAEWGVDGVFPLFSILFIFIGAQFVGLGLLGEYIGRIYSDVRARPRYYVQDILVGEATKGARISDENKNN", "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": "MPSHPNFIFRWIGLFSDKFRRQTTGIDENSNLQINGGDSSSSGSDETPVLSSVECYACTQVGVPAFHSTSCDQAHAPEWRASAGSSLVPIQEGSVPNPARTRFRRLKGPFGEVLDPRSKRVQRWNRALLLARGMALAVDPLFFYALSIGRTTGPACLYMDGAFAAVVTVLRTCLDAVHLWHVWLQFRLAYVSRESLVVGCGKLVWDPRAIASHYARSLTGFWFDVIVILPVPQAVFWLVVPKLIREEKVKLIMTILLLIFLFQFLPKIYHCICLMRRMQKVTGYIFGTIWWGFALNLIAYFIASHVAGGCWYVLAIQRVASCIRQQCMRTGNCNLSLACKEEVCYQFVSPTSTVGYPCLSGNLTSVVNKPMCLDSNGPFRYGIYRWALPVISSNSLAVKILYPIFWGLMTLSTFANDLEPTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLHAVMAKKRKMQIRCRDMEWWMKRRQLPSRLRQRVRRFERQRWNALGGEDELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGDELLSWCLRRPFLDRLPPSSATFVCLENIEAFSLGSEDLRYITDHFRYKFANERLKRTARYYSSNWRTWAAVNIQMAWRRRRKRTRGENIGGSMSPVSENSIEGNSERRLLQYAAMFMSIRPHDHLE", "text": "FUNCTION: Acts as cyclic nucleotide-gated ion channel. Permeable to potassium and calcium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Could also transport lithium, cesium and rubium and displays a strong selectivity against sodium. Seems to directly participate in pathogen-induced calcium influx. May function in homeostasis, re- establishing ionic balance after defense action and/or other stimuli. Could mediate the initiation of the developmentally regulated cell death programs. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family."}
{"protein": "MPQNEYIEQHIKKHGRRLDHEERKRKREAREAHKISEKAQKLTGWKGKQFAKKRYAEKVAMRKKIKAHEQSKLKGAAKPLEDSGEALPAYLLDREQANSAKAISSSIKQKRLEKADKFSVPLPKVRGISEEEMFKVVKTGKSKTKSWKRMITKHTFVGEGFTRRPVKMERIIRPSALRQKKANVTHPELGVTVFLPILGVKKNPQSPMYTQLGVLTKGTIIEVNVSELGMVTSGGKVVWGKYAQITNEPDRDGCVNAVLLV", "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": "MAIKKYKSTTNGRRNMTTIDYSAVLTTKNNPEKSLVVSKNSKAGRNNRGLITTRHKGGGHKQKYRIIDFKRNKRDIFGTISTIEYDPNRNAFICLINYVDGEKRYILFAKGMQVGMKVVASENADIKVGNVAPLKNIPEGTLLHNVELKPGKGGQIARSAGSSVQLLGKDDDGKYVTLRLSSGEVRKVLAECYATIGEVGNEEYNLVNWGKAGRNRWRGIRPTVRGSVMNPNDHPHGGGEGRAPIGRKSPVTPWGKKALGVKTRNTKKTSEKLIVRKRSNKK", "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": "MPLGLRGKKKAAKSKETARLVEGERSGGSQGVPGPPAPARRLVFHAQLAHGSATGRVEDFSSISELYAKIAGVFEIAPSEILFCTLNTPKIDMGKLLGGQLGLEDFIFAHVKGIKKEVNVYKSEDSLGLTITDNGVGYAFIKRIKDGSTIDSVKTICVGDHIECINGENIVGWRHFEVAKKLKELKKEELFTLQLIEPKKAFEIGPRSKAGKTSTEKIGTSRGTLRLRSKGPATVEDLPSEAKAKAIEKVDDLLELYMGIRDIDLATTMFEAGKDKSNPDEFAVALDETLGDFAFPDEFMFDVWGAISDVKQGR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GIPC family."}
{"protein": "MSQRVSDQVMADVIAETRSNSSSHRHGGGGGGDDTTSLPYMHKVGTPPKQTLFQEIKHSFNETFFPDKPFGKFKDQSGFRKLELGLQYIFPILEWGRHYDLKKFRGDFIAGLTIASLCIPQDLAYAKLANLDPWYGLYSSFVAPLVYAFMGTSRDIAIGPVAVVSLLLGTLLSNEISNTKSHDYLRLAFTATFFAGVTQMLLGVCRLGFLIDFLSHAAIVGFMAGAAITIGLQQLKGLLGISNNNFTKKTDIISVMRSVWTHVHHGWNWETILIGLSFLIFLLITKYIAKKNKKLFWVSAISPMISVIVSTFFVYITRADKRGVSIVKHIKSGVNPSSANEIFFHGKYLGAGVRVGVVAGLVALTEAIAIGRTFAAMKDYALDGNKEMVAMGTMNIVGSLSSCYVTTGSFSRSAVNYMAGCKTAVSNIVMSIVVLLTLLVITPLFKYTPNAVLASIIIAAVVNLVNIEAMVLLWKIDKFDFVACMGAFFGVIFKSVEIGLLIAVAISFAKILLQVTRPRTAVLGKLPGTSVYRNIQQYPKAAQIPGMLIIRVDSAIYFSNSNYIKERILRWLIDEGAQRTESELPEIQHLITEMSPVPDIDTSGIHAFEELYKTLQKREVQLILANPGPVVIEKLHASKLTELIGEDKIFLTVADAVATYGPKTAAF", "text": "FUNCTION: High-affinity H(+)/sulfate cotransporter that mediates the uptake of sulfate by plant roots from low concentrations of sulfate in the soil solution. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family."}
{"protein": "MEAIKGSDVNVPDAVFAWLLDGRGGVKPLEDNDVIDSQHPCWLHLNYTHPDSARWLASTPLLPNNVRDALAGESSRPRVSRMGEGTLITLRCINGSTDERPDQLVAMRLYMDERFIVSTRQRKVLALDDVVSDLQEGTGPVDCGGWLVDVCDALTDHASEFIEELHDKIIDLEDNLLDQQIPPRGFLALLRKQLIVMRRYMAPQRDVYARLASERLPWMSDDHRRRMQDIADRLGRGLDEIDACIARTGIMADEIAQVMQESLARRTYTMSLMAMVFLPSTFFTGLFGVNLGGIPGGGWRFGFSLFCILLVVLIGGVTLWLHRSKWL", "text": "FUNCTION: Zinc transporter. Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family."}
{"protein": "MISSRIGGAGGVELSRVNQQHDTVPAQTAHPNAVTAGMNPPLTPDQSGSHATESSSAGAARLNVAARHTQLLQAFKAEHGTAPVSGAPMISSRAALLIGSLLQAEPLPFEVMAEKLSPERYQLKQFQGSDLQQRLEKFAQPGQIPDKAEVGQLIKGFAQSVADQLEHFQLMHDASPATVGQHAKADKATLAVSQTALGEYAGRASKAIGEGLSNSIASLDEHISALDLTLQDAEQGNKESLHADRQALVDAKTTLVGLHADFVKSPEAKRLASVAAHTQLDNVVSDLVTARNTVGGWKGAGPIVAAAVPQFLSSMTHLGYVRLSTSDKLRDTIPETSSDANMLKASIIGMVAGIAHETVNSVVKPMFQAALQKTGLNERLNMVPMKAVDTNTVIPDPFELKSEHGELVKKTPEEVAQDKAFVKSERALLNQKKVQGSSTHPVGELMAYSAFGGSQAVRQMLNDVHQINGQTLSARALASGFGGAVSASSQTLLQLKSNYVDPQGRKIPVFTPDRAESDLKKDLLKGMDLREPSVRTTFYSKALSGIQSSALTSALPPVTAQAEGASGTLSAGAILRNMALAATGSVSYLSTLYTNQSVTAEAKALKAAGMGGATPMLDRTETALNNIRHPNRESLPHTFQKSTLSGIPRVAENAYHMGRGALQLPTQMAVDTVRVVDEGVLNAVASAREALKQPTKDDDALRALEEGLLDPR", "text": "FUNCTION: Involved in the suppression of basal resistance and promotion of disease symptoms in plants. Mediates the ubiquitination and degradation, via the host proteasome, of a low-abundance immunity- associated protein in Arabidopsis thaliana. May be involved in the inhibition of a host vesicle trafficking pathway. SUBCELLULAR LOCATION: Secreted. Host membrane. Note=Secreted via the type III secretion system (TTSS). Localized to the plant endomembrane."}
{"protein": "MAKLQQLVQAIQSGTIKTELPDVRVGDLVRIGVSIQEGNKQRIQPFEGTVISKHQAGANSTVTVRKSLQGIGVERVFPLYAPCVANLQVLRRAQVSRAKLYYLRSRTGKATRLKEKFETLPQIWMNQNQH", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family."}
{"protein": "MGLQRGMPLAQLGEPFGITPSSIENVSPGIDQCKDHRMDVSMRSDPTDCSSDTTNTFHSSIHIIQPPPNNGFRLMNWKTDSSSETEIDIGDVRKCGEKADPRQFELLKVLGQGSFGKVFLVRKVRGRDSGHVYAMKVLKKATLKVRDRQRTKLERNILAHISHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEDDVKFYLAELTLALEHLHSLGIVYRDLKPENILLDADGHIKVTDFGLSKEAIDSEKKTYSFCGTVEYMAPEVINRRGHSMAADFWSLGVLMFEMLTGHLPFQGRDRNDTMTQILKAKLSMPHFLTQEAQSLLRALFKRNSQNRLGAGPDGVEEIKRHAFFAKIDFVKLLNKEIDPPFKPALSTVDSTSYFDPEFTKRTPKDSPALPASANGHEIFRGFSFVSNAVMEERKLIAKSVRSVPTAKTNPFTDDYEILEKIGNGAHSVVHKCQMKATRRKYAVKIVKKAVFDATEEVDILLRHSHHQFVVKLFDVYEDETAIYMIEELCEGGELLDKLVNKKSLGSEKEVAAIMANLLNAVQYLHSQQVAHRDLTAANILFALKDGDPSSLRIVDFGFAKQSRAENGMLMTPCYTAQFVAPEVLRKQGYDRSCDVWSLGVLLHTMLTGCTPFAMGPNDTPDQILQRVGDGKISMTHPVWDTISDEAKDLVRKMLDVDPNRRVTAKQALQHKWIGQKEALPDRPIQSEQVGELDMQNVKVALEQTYKAIASAPSVQLRPVGSSALAKRRMKEILYANYTKNVSANA", "text": "FUNCTION: Serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of transcription (By similarity). Suppresses germline tumor formation by preventing the dedifferentiation of secondary spermatocytes probably downstream of mpk-1 (PubMed:22820175). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily."}
{"protein": "MEYKDIATPSRTRALLDQYGFNFKKSLGQNFLIDVNIINKIIEASHIDCTTGVIEVGPGMGSLTEQLAKNAKKVMAFEIDQRLIPVLKDTLSPYDNVTIINEDILKADIAKAVDTHLQDCDKIMVVANLPYYITTPILLNLMQQDVPIDGFVVMMQKEVGERLNAQVGTKAYGSLSIVAQYYTETSKVLTVPKTVFMPPPNVDSIVVKLMQRQEPLVQVDDEEGFFKLAKAAFAQRRKTINNNYQNFFKDGKKNKETIRQWLESAGIDPKRRGETLTIQDFATLYEQKKKFSELTN", "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": "MTLKITRRAYAEMFGPTTGDRVRLADTDLIVEVERDYTIYGEEVKFGGGKVIRDGMGQSQRESKDCADTVITNALIIDHWGIVKADIGLKHGRIAAIGKAGNPDIQPGVTIVIGPGTEIIAGEGMIVTAGGVDTHIHFICPQQIDEALNSGVTTMIGGGTGPATGTYATTCTPGPWHLQRMLQAADAYPMNIGFLGKGNGSLPGALREQIDAGAIGLKLHEDWGSTPAAIDCCLGVADDTDTQVAIHTDTLNESGFVEATIAAFKGRTIHTYHTEGAGGGHAPDIIRVCGESNVLPSSTNPTRPFTVNTLDEHLDMLMVCHHLDASIAEDIAFAESRIRRETIAAEDILHDLGAFSMLSSDSQAMGRVGEVILRTWQTAHKMKAQRGKLAGDPNDARGGHDNFRVKRYVAKYTINPAITHGIAHEVGSIEVGKWADLVLWKPAFFGVKPSLILKGGMIASAAMGDANASIPTPQPVHYRPMFAAAGGALARSSLSFLSQSAAQAGVAERYGLAKTTAVVRGTRAVTKAQMIHNDWQPSITVDPETYQVVADGMLLTCEPAEVLPMAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "MEGKEEDVRLGANKFSERQPIGTAAQSDKGYKEPPPAPLFEPGELTSWSFYRAGIAEFMATFLFLYITILTVMGVVKSNSKCSTVGIQGIAWAFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRALFYMVMQCLGAICGAGVVKGYQKGLYESNGGGANVVAPGYTKGDGLGAEIVGTFILVYTVFSATDAKRNARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNKKHAWDDHWIFWVGPFIGAALAAIYHQIVIRAIPFKSRP", "text": "FUNCTION: Water channel required to facilitate the transport of water across cell membrane; mercury-insensitive (By similarity). Promotes primary root elongation and root hair formation (PubMed:24606771). Contributes to the tolerance to multiple abiotic stresses including salt (NaCl), cold and water deprivation, by modulating cytosolic K(+)/Na(+) ratio, maintaining osmotic balance, and reducing membrane injury (e.g. oxidative injury) (PubMed:24606771, PubMed:34512687). Regulates also the expression of abscisic acid (ABA)-responsive genes during dehydration and salt stresses (PubMed:24606771, PubMed:34512687). 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": "MPQNEYIEQHIKQHGRRLDHEERKRKKEAREGHRVAKDAQTLKGWRAKQFAKKRYSEKVSMRKKIKAHQESKVKGPSTPKQDEGEALPTYLLDRQTNNTAKALSSSIKQKRLEKADKFSVPLPKVRGISEEEMFKVIKTGKSKTKSWKRMITKHTFVGEGFTRRPVKMERIIRPAALRQKKANVTHPELGVTVFLPILGVKKNPQSPMYTQLGVLTKGTIIEVNVSELGLVTAGGKVVWGKYAQITNEPDRDGCVNAVLLV", "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": "MKYRDLRDFIAQLEALGELKRIGVEVDPHLEMTEICDRTLRAGGPALLFEKPKGHTMPVLGNLFGTPRRVALGMGEDSVEALREVGKLLAFLKEPDPPKGLKEAWKTLPIFKKVLDMAPKKVGSASCQDLVREGADVDLSSIPVQTCWPGDAGPLITWGLVVTKGPHKERQNMGIYRQQVIGPNRVIMRWLSHRGGALDFRDWCEKYPGEPFPVAVALGADPATILGAVTPVPDSLSEHAFAGLLRGSRTELVKCLGSDLLVPASAEIVLEGVIHPGDTAPEGPFGDHTGYYNEVDQFPVFTIERITSRRDPIYHSTYTGRPPDEPAILGVALNEVFIPILQKQFPEIVDFYLPPEGCSYRLAVVTMRKQYPGHAKRVMMGVWSFLRQFMYTKFVIVTDADVNARDWQDVIWAMTTRMDPARDTVMIENTPIDYLDFASPVSGLGSKIGFDATNKWPGETTREWGTPIVMDEAVKRRVDEMWETLGL", "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": "MDIILGVVMFTLIVLALVLVILFAKSKLVPTGDITISVNDDPSLAIVTQPGGKLLSALAGAGVFVSSACGGGGSCGQCRVKVKSGGGDILPTELDHITKGEAREGERLACQVAMKTDMDIELPEEIFGVKKWECTVISNDNKATFIKELKLQIPDGESVPFRAGGYIQIEAPAHHVKYADYDIPEEYREDWEKFNLFRYESKVNEETIRAYSMANYPEEHGIIMLNVRIATPPPNNPDVPPGIMSSYIWSLKEGDKCTISGPFGEFFAKDTDAEMVFVGGGAGMAPMRSHIFDQLKRLHSKRKMSFWYGARSKREMFYVEDFDMLQAENDNFVWHCALSDPLPEDNWDGYTGFIHNVLYENYLRDHEAPEDCEYYMCGPPMMNAAVIGMLKDLGVEDENILLDDFGG", "text": "FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NqrF family."}
{"protein": "MGVVHDVWLVTKELLEATALPWPSEEREERLAAVDRLLLEREELLRKLRPPYSEEEQELGREIIVWNQEIEARLLRVCEEIRRDLRMTGAKRQANARYVHPYEQPLSFDGMFYDKRR", "text": "FUNCTION: May act as an export chaperone for the filament capping protein FliD. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the bacillales FliT family."}
{"protein": "MKAGALELGHASKTTKSGVNRGMSILDLFIRIIAIIATLGSAIAMGTTNETLPFFTQFVRFKAKYSDLPTFTFFVVANAIVSAYLVLSLGLSIYHIMRSRAQATRIALIFFDAAMLGLLTGGASASAAIVYLAHKGNRKTNWFPICQQYDSFCHRTSGSLVGSFAGSVLIILLIFLSAIALSRQSLNH", "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": "MLQKTGRGLLAFLLIVLEWTQPSLPSPLRPICDLRVLNHFIKEAQDAEAAMKLCSEGCTLSDSVIVPQTTVEFDVWEKKSALAKAQEVQSGLWLLQEAFNFLRTSVTNTALHSHIDNSVRNLLSVNAVLRSLNIQEFTPPASAAEIEGTWRVSTATELLQVHINFLRGKVRLILLDAQACQQDVS", "text": "FUNCTION: Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the EPO/TPO family."}
{"protein": "MAVYTDVAADELADFLSQYDLGELLSYKGIAEGVENSNFLLHTTKGSFILTLYEKRVAKNDLPFFLALMTHLAEHGVNCPLPVKGRDGEALRELSGRPAAIITFLEGVWPRKPNAAHCAGVGEGLARMHLAGANFAIRRANALSVAGWRPLFDAAASRADEVQPGLRAFLAAELDYLASGVWPTNLPEGVIHADLFNDNVFFLGDKLSGIIDFTFACNDMLAYDVAICLNAWCFEPDHSFNVTKARAFLNAYGRVRKLSEAEEAALPLLARGAAIRFLLTRLVDWLNVPPGALVRPKDPLEYVRKLRFHQSVSSVRDYGLMPSGLVA", "text": "SIMILARITY: Belongs to the pseudomonas-type ThrB family."}
{"protein": "MNFSIKSVIFLAIVALATLVSASTNPKVTNKVYFDIKQGDKDLGRIVLGLYGEVVPKTVENFRALATGEKGYGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFADENFKLRHTGPGILSMANAGRDTNGSQFFITTVTTSWLDGRHVVFGKVIEGMDVVTAIETTKTLPGDRPATPVIIADCGELPVSNNNDAKAEL", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B subfamily."}
{"protein": "MGKVPSSFRSMPANLLVRKTTPSPPAPPRDFRNRTAVGGDSAKLPQNTQAPREPSLRNPFKSPNLSDAKSLFNSIAATSRIPLDLKFHNSVLQSYGSIAVVNDTVKLFQHILKSQPNFRPGRSTFLILLSHACRAPDSSISNVHRVLNLMVNNGLEPDQVTTDIAVRSLCETGRVDEAKDLMKELTEKHSPPDTYTYNFLLKHLCKCKDLHVVYEFVDEMRDDFDVKPDLVSFTILIDNVCNSKNLREAMYLVSKLGNAGFKPDCFLYNTIMKGFCTLSKGSEAVGVYKKMKEEGVEPDQITYNTLIFGLSKAGRVEEARMYLKTMVDAGYEPDTATYTSLMNGMCRKGESLGALSLLEEMEARGCAPNDCTYNTLLHGLCKARLMDKGMELYEMMKSSGVKLESNGYATLVRSLVKSGKVAEAYEVFDYAVDSKSLSDASAYSTLETTLKWLKKAKEQGLVP", "text": "SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MQPFIHENFLLQNKHAEVLYHDYAKSLPIIDYHCHLSAKEIAEDRRFHDMTELWLEGDHYKWRAMRALGVEEKYITGNASPEEKFQAWAKTVPYCIGNPLYHWTHLELKRYFQVDALLNERTWREIWNHCNDLLRQEGFSARSFMVKSNVEWIGTTDDPLDDLADHQAIAQDPSFLVKIVPSFRPDAVIEINRPSFLDYVGKLGEALACRFMITISCCKPLENRVRYFHEKGCRMADHGLESMPYSECGWKEANDIFQKRKNGFVLSREEEEKYKTSTLCFLARLYHSLGWVMQLHIGSIRNTNEKMFRRLGPNTGYDSIHDFFLAQPLNAFLNELERRDQLPKTIVYTLNPAYNYVVASTVGNFQSEGVKGKVPIWRSLGGFNDSFKMAFIRHLTDLANVGVFSTFVGMLTDSRSFVSYVRHEYFRRIVCNLIGSWIEKGEVPQDYDFLGKIVQDVCYFNAKQYFQVGVSGG", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family."}
{"protein": "MFKNTFQSGFLSILYSIGSKPLQIWDKKVRNGHIKRITDNDIQSLVLEIEGTNVSTTYITCPADPKKTLGIKLPFLVMIIKNLKKYFTFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDDGWNQIQFNLSDFTRRAYDPCKLSYPKGLLLRQTLLRG", "text": "FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility (By similarity). Involved in the regulation of the size and morphology of cilia. Required for axonemal microtubules polyglutamylation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, cilium axoneme Note=Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme. SIMILARITY: Belongs to the CFAP20 family."}
{"protein": "MDDVIVVTSDYVPGHRIVKILGVTWGLTVRSRGLGGNLVAGLRTIAGGEIKEYVTLLNDARETALQRLISSAKAMGATAVINMRFDTSDMAQAMTEIVAYGTAVVTEPVENSQNVTLS", "text": "SIMILARITY: Belongs to the UPF0145 family."}
{"protein": "MDERPVLFFDSGIGGLTVLREARVLIPEIQFIYVADDAGFPYGNWEENILKEHILNIFTNLLTRYNPALCVIACNTVSTLMMADLRQKFPHVPFVGTVPAIKSAAEQTKSGFISVLATPGTVKRAYTNELINSFAGQCHVQLVGSEKLAGFAEDHLRGKTIDSEALRKEILPCFVKKNGKCTDVIVLACTHYPFLINFFREQALWSVEWIDPAKAIAKHIRSLLPLSEKIHQKPIKKYQDFALLTSKNITASTEHLLKGFGLKLMKRVDFRIRDQ", "text": "FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family."}
{"protein": "MINPIVKTIELPDGRTITLETGKLAKQADGSVMLRMGNTMLLATVCAAKDAVPGTDFMPLQVEYKEKFAAFGRFPGGFTKREGRASDYEILTCRLVDRALRPLFPDNYHAEVYVNIILFSADGVDMPDALAGLAASAALAVSDIPFNGPISEVRVARIDGQFVINPTFDQLEKADMDLMVAATYDNIMMVEGEMHEVSEAELLEAMKVAHEAIKVHCKAQMELTEEVGKTVKREYNHEVNDEELRKAVREACYDKAYAVAASGNNNKHERFDAFDAIREEFKAQFSEEELEEKAPLIDRYYHDVEKEAMRRSILDEGKRLDGRKTTEIRPIWCEVGPLPGPHGSAIFTRGETQSLTSVTLGTKLDEKIIDNVLEHGKERFLLHYNFPPFSTGEAKAQRGVGRREIGHGHLAWRALKGQIPADYPYVVRVVSEILESNGSSSMATVCAGTLALMDAGVKIKKPVSGIAMGLIKNPGEEKYAVLSDILGDEDHLGDMDFKVTGTRDGITATQMDIKVDGLSYEILERALNQAKEGRMHILDKITETIAEPRADLKDHAPRIETMTIPKEFIGAVIGPGGKIIQGMQEETGAVITIEETDGMGRIEVSGTNKKCIDDAMRMIKAIVAVPEVGEVYKGKVRSIMPYGAFIEFLPGKDGLLHISEIDWKRLETVEEAGIKEGDEIEVKLIDIDPKTGKFKLSRKVLMPRPEKK", "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": "MGHPLLLPLLLLLHTCVPASWGLRCMQCKSNGDCRVEECALGQDLCRTTIVRMWEEGEELELVEKSCTHSEKTNRTMSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTFSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPSCPGSSGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGHQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTYEPKNQSYMVRGCVTASMCQRAHLGDAFSMHHINVSCCTESGCNHPDLDIQYRKGAAPQPGPAHLSLTITLLMTARLWGGTLLWT", "text": "FUNCTION: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form (By similarity). SUBCELLULAR LOCATION: Cell membrane Cell projection, invadopodium membrane Cell membrane; Lipid-anchor, GPI-anchor Note=Colocalized with FAP (seprase) preferentially at the cell surface of invadopodia membrane in a cytoskeleton-, integrin- and vitronectin-dependent manner."}
{"protein": "MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGTPEGSGGNSSSSTSSGGGGGGGSNSGSSAFNPQGEPSEQPYEHLTTESFSDIALNNEKAMVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPTSSSSAPSPAASSSSSASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPATKGGFQVPMIPDYLFPQQQGDLSLGTPDQKPFQGLENRTQQPSLTPLSTIKAFATQSGSQDLKALNTTYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASPAASSLSSYPSPVATSYPSPATTSFPSPVPTSYSSPGSSTYPSPAHSGFPSPSVATTFASVPPAFPTQVSSFPSAGVSSSFSTSTGLSDMTATFSPRTIEIC", "text": "FUNCTION: Transcriptional regulator (PubMed:8336701, PubMed:8703054, PubMed:15958557). Recognizes and binds to the DNA sequence 5'- GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (PubMed:8703054, PubMed:15958557, PubMed:2028256, PubMed:8939742). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia (PubMed:11100120, PubMed:15958557). Plays a role in the regulation of cell survival, proliferation and cell death (PubMed:15265859, PubMed:15958557). Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation (PubMed:15958557). Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy (PubMed:15265859). Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia (PubMed:11100120). Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary (PubMed:8703054). Regulates the amplitude of the expression rhythms of clock genes: BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription (PubMed:26471974). Regulates the rhythmic expression of core-clock gene BMAL1 in the suprachiasmatic nucleus (SCN) (PubMed:29138967). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family."}
{"protein": "MTYAIIENSGRQFFTEPGKFIDINHIKAEVGDIIYFNRVLLLKSNNLIEIGYPFINNIKVKAKILKHFKDKKIRVYKMNPKKGTRKTKGYRSLCTRVLIESIENTENIIN", "text": "FUNCTION: This protein binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MKLSESVMAQNSVSFQKLQEQCEEQELEAPGGIASPQVYNQLLALYLLHNDLNNARYLWKRIPSAIKSSHSELGGIWEVGQKIWQRDFPGIYTSISAYQWSENIQQIMEAVRDATQQRAFGLVSQAYTSISADDFAAFVGLPVEEAVKGVLEQGWQADSATGMVMPKKPDSAPLSLIPNEQQLARLTDYVAFLEN", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CSN8 family."}
{"protein": "MDSKLRSLLSDHSRYVESFRLFLQNSTEHQCMQHFIESKLPNIISSIGNDKPVIDVLGVGSGSGEIDLQMIAKIQARWPGVPINNQIVEPSAEQIFGYKERVAKAPNLENVTFSWHRQTSSEFESQVNEDKQMRKFDFIHMIQMLYYVKDVLGTLKFFKSCLAPSGKLLIILVSGNSGWATLWKKYGQRLPLNDLCLYITAGDIAEMLSSMGARFQSHELQSDMDITECFIEGDRDGELLLDFLTETCDFKRNAPADLRDQIICDLKSPGCSTTKDGKVIFNNNLSVIVVEAD", "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": "MIKGIGIDITEIERVKKAATAHSQFIQHVLTPTELEQYSQFSGQRSVEYLAGRWSLKESFAKAYGTGIGANLGFHDIEIIDNQYGAPIVTKSPYNGNAHASVSHTATLVMTEVILESENK", "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": "MIGSEIRMAKLFDKGRALVVALDHGLVMGPLKGIENPVEVVAKIAKNGPDALQMTPSMVKLVKENFFSRGSPMLITRLDTANVWRQKYKVYNEGYYASIYTVKDAISAGADAVVTYLVVGYGNDTVEGYNLSVLSSLRKEANDYGIPFIVEPLYVTKDNPDSVKEVDLVKYVTRLASEIGADILKVDYTGNKESFRQVINVAFSPILIRGGPKTNTTEEFLRMLRDALEAGAKGVTVGRNLWQAEEPDKLAKAISKVIHENADIGEALKILK", "text": "SIMILARITY: Belongs to the DeoC/FbaB aldolase family."}
{"protein": "MSFMLYLDKADFILSQPPPSNNQEKKKILKNRITNSFSLIMFSGNNCTYCQELKPIFKKLVGTIPNCQIGTVNVSLQPELAELSQQTTTPIRYVPLILFYINGTPFKEFGGNYTEDNLRQFVKEVSIKAYEIIGTPQQEEGSISQHSVGKAVSKRVCYLNFDNAYNGTPPPSFD", "text": "SIMILARITY: Belongs to the IIV-6 196R family."}
{"protein": "MNFDMSKLVQQAQKMQEQMKKAQQERENMEVIGESGAGLVTVTMTGKYDVKSVSIDNSLMSEDKEILEDLIAAAVNSAVKKVEENSTASSDIYKMAKDAGIDLPSGINFPFK", "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": "MRVLLASLLIFGACWAGPVVNTNYGKVEGFEYGAAEVFLAIPFAKPPVDNLRFEKPEAPEPWEDVYQATQFRNDCTPHYRLVAQFSSYSGEDCLTLNVIKPKTIEKKLPVLFWVHGGGYEIGSGSQHGYEFFADRYTSQGVIVVTIQYRLGFMGFFSEGTSDAPGNYGLFDQAAALRFVKENIGNFGGDPDDITIWGYSAGAASVSQLTMSPYTHDLYSKAIIMSASSFVGWATGPNVIDTSKQLAEILGCPWPGAKECMKKKTLHEIFDAVETQGWTTGTIDILRWSPVIDGDYLPKNPENLINDAPIKPTLIGMSNKEGSYFATMNMGRVIADFGLSPEEIPKVDEDFISEIIDRKLLYNNRYGENRQKVWDQILDYYTKQGKPERDLNGFYVDRYAELLSDITFNVPILREITARVERKTPVWTYRFDHYNEQIWKKYIPEQAKGSPHANEYHYLFNMPVMAQIDFKKEPESWLQRDLIDMVVSFAKTGVPHIQDVEWRPVSDPDDVNFLNFQSSGVSVKHGLFQEPLDFWNNLREREGFDLVDPAYSKTTSNSEKDEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MSHVRSAPAGKSGGGGGSTPAKRGRPFGSTTGSGAAAAAAAAAIGDAAAPAALVGPSLQVLTALSDQNNKRIVLALQSGLKSEILWALNALTVLSFKEKDDLRRDTTPLAKVPGLLDALLQVIDDWRDIAMPKDHTKPPRVRTLGVNTTLSGFGHENVEKVYSDTTTPSDDQTKTADSTVTKKRSAGFLFDEEGLFNVDDEGRTEKQQCAVAASNIIRNFSFMPENETVMVQHRHCLETVFQCLEDQNTEDDELITNMLETLVNLAPVLDLRIFSSSKPSFIKITEKRAVQAIMGMLASSIRVWHCAAAELIGRLIINPDNEPFLLPAIPQIYKRLVDLLSVPAVDAQAAAISALYNVAEVNMDFRLKLASERWAVDRLLKVVKTPHPVPEVCRKASMIVESLVSEPQNRMHLLVHENTFAEILTSEGKYSDTFARILYELTARPSNKVTAGQAIWGNIN", "text": "FUNCTION: Plays critical roles in both embryo and endosperm development (PubMed:32808364). Required for free nuclei division and cellularization in early endosperm development, by preventing premature cell death in the endosperm (PubMed:32808364). Involved in the regulation of pattern formation and organ differentiation during embryogenesis, by regulating genes involved in the early stages of seed development (PubMed:32808364). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPPSMLVKDEYVHDFEGQPSLPTEGHSIQTIQHPPSNRASTETYSAPALLAPSESNATSTTNFPNIPVASTSQPASILAGSHSEGLLQIASGPQPGQQQNGFTAQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD", "text": "FUNCTION: Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation. SIMILARITY: Belongs to the dwarfin/SMAD family."}
{"protein": "MRATAAKKVFIKTYGCQMNVYDSQRMGDALAADGYTATDAIDEADLVLLNTCHIREKAAEKVYSELGRIRDMKAERAIAGRELLIGVAGCVAQAEGAEIIRRSPAVDLVIGPQTYHRLPDVLARVRGGEKIVETDYAIEDKFDHLPQPKRAEVIKRGVTAFLTVQEGCDKFCTFCVVPYTRGSEVSRPVAQIVAEAERLAEAGVREVTLLGQNVNAWHGQGENGEEWGLGRLLFRLAEIPGLARLRYTTSHPRDMDDELISAHRDLPSLMPYLHLPVQSGSDRILKAMNRRHTARDYLALLDRIRAARPDIALSGDFIVGFPGETEADFEATMELVRQVNYASAFSFKYSPRPGTPGAEMPDHVPETLKDERLQRLQALLLKQQQGFGSSLVGSTIDTLIEKPGRQAGQKVGRTPWLQPVIVDEKAGEIGDIIQVRITKTGYNSLFAELA", "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": "MVSNGHFAYAEDDPVASYEHGVQVVDEDKEFNPNLSKYLAYEGVTPAGFNYHLISVFGSQSTGKSTLLNYLFGTHFSVMSETERRQTTKGIWMSKNKRQDCERENSLPHLQNNRMADNILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNMQLFLKDKKSTPRSLLFFVIRDFLGTTPLQNLQNTLMQDLQRIWTSLSKPPGLENSTIEDYFDFEFAALPHKNFQTDKFVAEVKKLSMRFREGHRDPSKGNKTEGGIFLSEYHRRIPADGFAVYAEGIWDQIVNNKDLDLPTQQELLAQFRCDEISREVLVAFDEAVVPFETKQAEAAQSGNPEVFAGLGPAMKNARVKTLSAFETEASRYHKRVFQMKRAELEDKMDTRLKVLFSGQLTAAHKSGIAQFSDAVSAAVKAGQKKGASYDFADIVNKEKRIALERFEDDAKATVIEGACWSNYTQELALYQKDLEKISAQLRKDEMRRLATRVERWVRSRLGESVGLEFNALGSGRGGSGAPETGDKPSEDTIWDRIWSIFVATVLEAEQRFTERASSFDASLEEVDVGLWRLRRKAWGVLRSKIDEEMMEGNLLLKLRENFEDKFRYDSAGVPRIWRPTDDIEGLYTKARESTLTLIPLLSRFRLQETNATPQLDRWVGYTPSAATPADEEDLVPIGGVDDDGKSLEEEMTMLSETKRQDLTVRFKKAADGVYVEAKRSAIGGMTQIPVYFYILLLALGWNEIIAVLRNPVYFFMLFLCSVAAYIIYQLNLWGPMVKMAEAASHQAVEEGKKRLRDLLEPSDIGHHGMKYKNGTEQYEMSHVRSGRNATKINERDDDDEVEGEETW", "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": "MSRPRRRGRDVHGVLLLDKPQGVSSNDVLQKVKRIFNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGNVIEERAIGFSATDLELALESFRGTTQQVPSMYSALKYQGRKLYEYARQGLTVPREAREITVYELQFIRWEGDELELEIHCSKGTYIRTIIDDLGEQLGCGAHVIYLRRLQVAIYPTERMVTLEQLAALAEQAQTQEHSLSLSLDSLLMPMESPVIDFPEVNLPPVVAGYLKLGQAVQAANAPLNGMVRITEGDAHKFIGMGEIDGDGRVAPRRLVVEFPV", "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": "MNKQVVAKRYASALFEIAKEQQLLDQLEQELRVVKQVFAQNETLLSVLNHPKIALAKKKALVQEAFANISTVLQHTLMLLLDRHRIDIVNDLADAFIALANEARGVAEAIVYSARPLTEDETNALADVFAKKVGVDTLRITNIIDKDVIGGVKVRIGNRIFDGSVSGKLARLQRQLTR", "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": "MNDTVHKHITVLLHEAVDGLAIKPNGIYIDGTFGRGGHSRLILSKLSEQGRLIATDRDPRAIAEANTIDDTRFQIVHTAFSAIPDVCEQLGLTGKIDGILLDLGVSSPQLDDAERGFSFMRDGPLDMRMDTTKGLSAAEWLAQVSADDLAWVLKTFGEERFAKRIAQAVVSYNKSVTDKISRTLQLAQIIADAVPFKDKHKHPATRSFQAIRIFINSELDELEKALQSALSVLAPEGRLSIISFHSLEDRMVKQFMKKNSKGMDVPKGLPILESELNKNIPLKIIGKAIMPSEAEIEANPRSRSAVLRIAEKR", "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": "MITEALKKVIEFKDLDEKEAEAVMKDIMSGNAKPTQIAAILTALRMKGETIEEITAFAKIMREFSLKINPNVPKLLDTCGTGGDNLNTFNISTATAFVVSAYVPVAKHGNKAVSSKSGSADVLEALGVNLNVPIERVKESIEKIGIGFLFAPHFHPAMKFATPVRKELGIRTVFNVLGPLTNPANANYQLMGVYDEKLTEKLANVLKNLGLKGALVVHGSGMDEITTIGKTKISELRNGEIKSYYIEPEDFGIKKAKLEDIRGGDAEENAKIIGEIFEGEEVGAKRDIVVLNAAFALYIAEEAKDVEEGIKLAEKSIDEGKALKKLEDLIEFYREG", "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": "MDPIRKPAWLQKKITPAAHAEMEGLLKELRLNTVCQQARCPNITECFGKRQATFLILGRICTRLCSFCSVSKETPLPLEPGEAASVAEAVKRLGLSHVVITSPTRDDLSDGGASVYAETVARIRSVSPRTKVELLIPDFRGERAALAAVVESAPDILGHNLETVPRLYSIRSGADYQRSLDLLAQARRMAPDLNTKSGLMLGLGEEEAELYAVMEDLLKAGCGYLSLGQYLAPSRMHHPVQRYVEPELFEKYKEKALAMGFEHVESAPYVRSSYHAENYLEVKSPPPEGEG", "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": "MAAVGVDSRRPETAMEETCNVKGAAAKQGEGLKQYYLQHIHELQRQLRQKTNNLNRLEAQRNELNSRVRMLREELQLLQEPGSYVGEVVKVMGKNKVLVKVHPEGKYVVDIDKSIDITKITPSTRVALRNDSYVLHLVLPSKVDPLVNLMKVEKVPDSTYDMIGGLDQQIKEIKEVIELPIKHPELFESLGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSARMESGSGNGDSEVQRTMLELLNQLDGFEASNKIKVLMATNRIDILDQALLRPGRIDRKIEFPNPNEESRFDILKIHSRKMNLMRGIDLKKIAEKMNGASGAELKAVCTEAGMFALRERRVHVTQEDFEMAVAKVMKKDTEKNMSLRKLWK", "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. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MRTSQFLLATQKETPSDAVVVSHQLMLRAGMIRKLASGLYTWLPMGLRVLRKVEAIVREEMDAAGALEILMPGIQPAELWQESGRWEQYGPELMRLVDRHNREFCLGPTHEEVITDLARNELNSYKQLPINMYQIQTKFRDEIRPRFGLMRGREFVMKDAYSFHADHESLQVTYDRMHLAYSNIFTRLGLKFRPVEADNGSIGGAGSHEFHVLAESGEDDIVFSDGSDYAANIEKAEAIPREKTRPAATEELRLIDTPNTKTIAQLVEGFGLPIEKTVKTLVVHAAEEGKLIALIIRGDHELNEIKASQLEQVANPLVMASEAELRDAIGAGAGSLGPLNLPLPCIIDRSVELMSDFSVGANIDDKHYFGVNWERDLPVPTVADLRNVVAGDPSPDGKGTLEIKRGIEVGHIFQLGTKYSEAMKCQVLGENGKPVNLAMGCYGIGVSRVVAAAIEQNSDENGIIWNDTLAPFQIALVPLRYETDAVREATDKLYADLTAAGFEVLLDDRDKKTSPGIKFADMELIGIPHRIVVSDRGLAEGNLEYKSRTESQPQAIAVADVLSFIQGKVNR", "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": "METTVRKQKKNLETKKTSIYSLQLHEMQDWLKEQGEPKFRAGQIFDWLYKKRVKNYEDMSNLSKGLREKLSNSFDITTLNTLVKQTSSDGTIKFLFQLYDGYSIETVLMRHEYGNSICVTTQVGCRIGCTFCASTLGGLKRNLEAGEIVAQVVEVQRALDESEERVSSLVVMGIGEPFDNYDNLMGFLRIINHEKGLHIGARHMTVSTSGIIPKIYKFAEEDLQINFAISLHAPNSELRSKLMPINRAYKLPDLMEAIKYYVNRTGRRITFEYGLFGGENDQVEHAEELAALLKGVKCHVNLIPVNYVPERDYVRTPREQIFLFEKTLKDRGVNVTIRREQGHDIDAACGQLRAKERKEETR", "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": "MSSKNGVVRSCLGSMDDIKKVFQRFDKNGDGKISVDELKEVIRALSPTASPEETVTMMKQFDLDGNGFIDLDEFVALFQIGIGGGGNNRNDVSDLKEAFELYDLDGNGRISAKELHSVMKNLGEKCSVQDCKKMISKVDIDGDGCVNFDEFKKMMSNGGGA", "text": "FUNCTION: Calcium-binding protein that may positively regulate abscisic acid (ABA) inhibition of germination and seedling development. May be required for photoperiod-induced flowering and function in ion homeostasis."}
{"protein": "MFEKPVVKSFQYGNHTVTLETGVMARQATAAVMASMDDTSVFVSVVAKKEAVAGQDFFPLTVNYQERTYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPSAFKNEVQVIATVVSINPDVNPDMITMIATSAALSIAGVPFNGPIGAARVGHINGELVLNPSNTELANSKLDLVVSGTEAAVLMVESEADNLSEEEMLSAVVFGHDQQQVVIKAINEFAAEVATPSWNWEAPVVNAELKAQVAELAETRLSEAYQITEKMARYEQVGAIKSEVVAALLVQNEALDEREIRGMLGALEKNVVRSRIIAGHPRIDGREKDMVRALDVRTGVLPRTHGSALFTRGETQALVTATLGTQRDAQIIDSLMGEKKDHFLLHYNFPPYCVGETGFVGSPKRREIGHGKLAKRGIAAVMPSVEEFPYTVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKASVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTNAGITALQMDIKIEGITKEIMQIALNQAQGARKHILTVMDEAISGAREDISQYAPRIHTMKISSDKIKDVIGKGGAVIRALCEETGTTIEIEDDGTIKIAATEGAAAKEAIRRIEEITAEVEVGKIYPGKVMRIVDFGAFVTVLGPKEGLVHISQIAEERIEKVADHLQVGQEVQTKVLEIDRQGRIRLSIKEATAELNPVAATEVKDAE", "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": "MTDINTVLAELKRGTDEILSEADLIEKLKENRPLKVKLGADPTAPDIHLGHTVVLNKLRQFQQLGHEVYFLIGDFTGMVGDPSGKNATRPPLSREDVLRNAETYKEQIYKILDPQKTKIVFNSEWLSKLGTXGMIRLASNYTVARMLERDDFKKRFGNNQPIAIHEFIYPLLQGYDSVALDADVELGGTDQKFNLLVGRELQKSAGKKPQVAITLPLLVGLDGEKKMSKSLGNYIGVTEAPSDMFGKVMSISDELMWDWYNLLSFRPLNEIAQLKSEVENGKNPRDVKILLAKELIARFHNEEAANAAEQEFINRFQKGAMPDEMPEFTFSGEMGLATLLKEAGLVPSTSEAIRSAQQGGVKINGEKVDNVKDNAPKGTNVYQVGKRKFARVRLNKVDTVK", "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": "MTKILPVSTISIFRIILILPQINMELLPTKAWLVLDDVKEINEPTKPVQFPLDQASLDCIAKMMAYVDASYNGDAEKYGIIPGIGIAANQIGYWKQMFYIHLMDGGVEHKCLLINPKIINLSANKSFLKSGEGCLSVPKMHQGYVIRHEWITITGFDWLQQKEITITATGLFGMCLQHEFDHLQGRFYYHRINPLNPLFTNKEWKVINPALPSDSE", "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": "MNFTGAHILSIQQFQREDINRIFDVADAMEPYALRRRVTRVLEGAILGNMFFEPSTRTRVSFGAAFNLLGGNVRETTGFESSSLTKGESLFDTARVLSGYSDVICMRHPAAGSVAEFAEGSRVPVINGGDGPNEHPTQALLDLYTIRKELRSKGRGIDDLRIAMIGDLKHGRTVHSLCKLLGLFNNVSITLVSPKELAMPDYIVEDLRQAGHKVTITDDLPTSITHIDIAYSTRIQEERFASKEEADSYRGRFRLNQAIYTQFCEPNTVIMHPLPRDSRAEANELDNDLNTNPNLAIFRQADNGVLVRMALFALVLDVADQVDKYAREVRWFSSLRAN", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
{"protein": "MNLQHHFLIAMPLLQNTYFERSVIYVCEHNENGAMGLMINQPVARFTLERLLKKLNISSVHDAGHLNKPVMSGGPLSDDRGFILHSPQSGFNSSIHVSDDTMITTSKDILKTLGTKKQPKNIMVAVGYTGWQKGQLEQELIDNVWLTTKADTEILFNTLIPNRWYEAASKLGINIFHIAQQAGHA", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
{"protein": "MAKEELLEMEGLVDEILPDSRYRITLDNGHKLIAYTAGRVKKNHIRILAGDKVSLEVSPYDLSKGRITFRHIDKKQSFAGAPYRRH", "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": "MIDIKLIRQNPDFVKEALRKRGEDPAVIDEILKIDADWRATITKTNELRSRRNEISKNVARLKKEGKNAEAEALIEEGKRLGEEIKALEEKEKELQEKLNYLLLMVPNIPHESVPVGEDESQNVEVRRWGEPREFDFTPLAHWDLGPAWGLMDFSRASKLSGSRFTVMYGKLARLERALINFMLDVHTKEHGYTEVWVPHLVKRETITITGQLPKFEEELYLAERDDLFLIPTAEVPLAALHSGEILEEKELPKKYVAYTPCYRREAGSYGKDVRGMIRQHQFDKVELVWVTTPKRSFEDLEQLVKDAETILQKLELPYRVVSLCTGDLGFTSAKTYDIEVWLPSYNAYKEISSCSNVTDFQARRGNMRYRRRSDGKLEYVHTLNGSGIAVGRALVAILENYQQPDGSVRVPEVLVPYTGFEVIP", "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": "MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK", "text": "FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 14 (Hntx-1) subfamily."}
{"protein": "MVKALMVQGTASDAGKSIIAAGLCRIFKQDGLEVVPFKSQNMALNSFITKKGDEMGRAQVVQAEAAGKEPDVRMNPVLLKPTSDRKSQVVFLGRVLRDMDAVEYHEYKQQLLPKIKEVYDELGAENDIIVIEGAGSPAEINLNDRDIVNMGMAKLVDAPVILVADIDKGGVFASIYGTIELMPPEDRKRIKGVIINKFRGDVALLQSGIDMIEELTQVPVIGVVPYAQLDIDSEDSVALVQKSRRFDSRKSLDIAVVSLKRLSNFTDFHSLEIQPDVSVRYVQPGDAIGRPDLLILPGSKNTIEDMNYLCESGLEAEILECLEQGVRIFGICGGYQLLGQKISDPLHLESDLEETRGLGILETETVLQPVKRTTQVRALHEGQELEGYEIHMGETQLADRLEPFSIIKEQNGEATERPDGAVAYGGQVQGTYLHGVFDNLEWTRQYLNELRLAKGLEPLEDQLVSIKDFKDREYDKLADVLRQSLDMEQIYQIINREEK", "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": "MRIKIFMLVTAVVLLCCSGVATAAPKTYCEELKGTDTGQACQIQMSDPAYNINISLPSYYPDQKSLENYIAQTRDKFLSAATSSTPREAPYELNITSATYQSAIPPRGTQAVVLKVYQNAGGTHPTTTYKAFDWDQAYRKPITYDTLWQADTDPLPVVFPIVQGELSKQTGQQVSIAPNAGLDPVNYQNFAVTNDGVIFFFNPGELLPEAAGPTQVLVPRSAIDSMLA", "text": "SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the RsiV family."}
{"protein": "MAQITFKQEPITLLGSQVKTGETAPEFTLLDNDLNEVNLSTYDGQKKLISVVPSIDTGVCDQQTRKFNEEASQEDGVVLTVSVDLPFAQKRWCASNGLDNVITLSDHKDLSFGKNYGVVMEELRLLARSVFVLDKNNKVVYSEIVSEGTDFPDFESALEAYRNI", "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": "MNDNYMINPKKELSQCFIHSTDITDKIVNYAGNISNFSIIEIGPGLGTMTYSILKKNPKKLISIEKDSRLLPIHDKIIKKFQGKYEFILSDALDIDLRNIAKPPVKVIANLPYSIATLLLIKWINYINFFHSFTLMFQKEVADRIIAQPNNKNYGTLSILTQLFADVYKMQDFGPEIFSPKPKVFSSVINIVVLPQPRFDVNYDKLRKIVKITFNQRRKMIRSTLKQITNNTDEILHSLNIPNNLRPENLSIKQFCDIANCI", "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": "MLSEFKTFIMRGNVLDLAVGVIIGGAFTGIVKSLTNNLISPIITFFTGGTSDLQNLKLVVTKELTFKYGAFLNDVINFLITAFVVFLLVKFVNRILRTNKKEEVKANPELEVLAEIRDLLEAQKKA", "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": "MDFSKFLADDFDVKEWINAAFRAGSKEAASGKADGHAATLVMKLQLFIQEVNHAVEETSHQALQNMPKVLRDVEALKQEASFLKEQMILVKEDIKKFEQDTSQSMQVLVEIDQVKSRMQLAAESLQEADKWSTLSADIEETFKTQDIAVISAKLTGMQNSLMMLVDTPDYSEKCVHLEALKNRLEALASPQIVAAFTSQAVDQSKVFVKVFTEIDRMPQLLAYYYKCHKVQLLAAWQELCQSDLSLDRQLTGLYDALLGAWHTQIQWATQVFQKPHEVVMVLLIQTLGALMPSLPSCLSNGVERAGPEQELTRLLEFYDATAHFAKGLEMALLPHLHEHNLVKVTELVDAVYDPYKPYQLKYGDMEESNLLIQMSAVPLEHGEVIDCVQELSHSVNKLFGLASAAVDRCVRFTNGLGTCGLLSALKSLFAKYVSDFTSTLQSIRKKCKLDHIPPNSLFQEDWTAFQNSIRIIATCGELLRHCGDFEQQLANRILSTAGKYLSDSCSPRSLAGFQESILTDKKNSAKNPWQEYNYLQKDNPAEYASLMEILYTLKEKGSSNHNLLAAPRAALTRLNQQAHQLAFDSVFLRIKQQLLLISKMDSWNTAGIGETLTDELPAFSLTPLEYISNIGQYIMSLPLNLEPFVTQEDSALELALHAGKLPFPPEQGDELPELDNMADNWLGSIARATMQTYCDAILQIPELSPHSAKQLATDIDYLINVMDALGLQPSRTLQHIVTLLKTRPEDYRQVSKGLPRRLATTVATMRSVNY", "text": "FUNCTION: Required for normal Golgi function. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COG7 family."}
{"protein": "MNLFDQFLTPSLLGISLLMPALLMTTILLLNPKNQWLSHPTTTIKSWFINQAAKQIMTPINPTGHKHSLILISLLILLSLTNLLGLLPYTFTPTTQLSMNMAIALPLWLVTVLIGLRTQPTTSLAHLLPEGTPMLLIPILILIETISLLIRPIALGVRLTANLTAGHLLIQLISIATLNLWFMMPPLSLLTSTVLILLLLLEFAVAMIQAYVFVLLLSLYLQENS", "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": "MASQGTKRSYEQMETGGERQNATEIRASVGRMVGGIGRFYIQMCTELKLSDNEGRLIQNSITIERMVLSAFDERRNRYLEEHPSAGRDPKKTGGPIYRRREGKWVRELVLYDKEEIRRIWRQANNGEDATAGLTHLMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGVNDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRAMMDQVRESRSPGNAEIEDLIFLARSALILRGAVAHKSCLPACVHGLAVASGYDFEREGYSLVGIDPFRLLQNSQVFSLIRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGARVLPRGQLSTRGVQIASNENMETMSSSTLELRSKYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERATIMAAFTGNAEGRTSDMRTEIIRMMENARPEDVSFQGRGVFELSDEKATNPIVPSFDMSKEGSYFFGDNAEEFDS", "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": "MNVELQLDPRRTVPAWLAYGTPVLTVLAALAVGGVALVALNVDPVDAYGVMFVETLTSQFGLTEVLVRAVPLILAGLAVYLPLKAGLFNIGAEGQLLLGALAGTWVAVNVSLPAVALLPLMFLAACVAGAFWAGIPAWLRAKWDVNEIITSLLLTFVAQELQSYLLRGPMQGGTGNFPQSARFSDAATLPPLAGLVPGGESIPLFADVHAGLLVAVAAVVATYVVMTKTRLGFEVTFVGSNDEAARQAGMSRHTVYLFVFLLGGAFAALGGIAEIAGSQGRFRAAFAPGYGFTAIPIALLGRNSAVKVTLAGLFFAVLFVGGSSVEVAFGVPAALVEIIQALVILFLITSEFFKRYRVGIAFDRRGNDAPADATGGDARW", "text": "FUNCTION: Part of an ABC transporter complex involved in glucose import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family."}
{"protein": "MSLFDWFADRRKGQFVGKVTQESEESDGLWEKCPECGQVVYRKDLIDNCSVCSNCGHHNRIDSKERIRIISDPNTFKSINNNLTPVDPLGFKDRRAYADRLRESQASTGLKDGVLTGTCEVNSIPMALAVMDFRFMGGSMGSVVGEKITRLIEHSTKEKLPLLIVCASGGARMQEGMLSLMQMAKISGALERHRDAQLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLQDHGFVDTIVPRTELKETLAKILRLHKTQEVKLQTNA", "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": "MIVRSFSDIENTDRHVKAASGTWESKRIVLAKEKVGFSLHETVLYAGTETSMWYANHIEAVLCTEGEAELTNDETGETHWITPGTMYLLDGHERHTMRPKTDFRCVCVFNPPVTGREDHDENGVYPLLTEEA", "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": "MLKLRVIPCLDVKDGRVVKGVNFVSLRDAGDPVEQAKLYDAAGADELTFLDITASVENRDTILDVVRRTAEAICLPLTVGGGVRTCEDMRRLLLAGADKCAVNSAAIKNPDLIREASERFGSQCIVVAIDARSNGKGGWEVYAKGGREPTGLDVVEWARKMQDLGAGEILLTSMDRDGTRAGFDLDLLRAVCGAVTVPIVASGGVGELQHFVEGAEVGASGLLAASVFHFGQFRIDEVKNALNKAGLPVRLGE", "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": "MTEITAEGNASTTTTVIDNKNGCIPKSPGKVLKRSVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVNDAVEETTDWIYGFFSLLSDIISSEGDEDDEDADEDIDKGEIEEPPLKRKEIHQEKAEKEEKPEKKIQTKASHREREKGKEKLKGEKPEKTATHKEKLEKKERPETKMMAKEDKKIKTKEKTEEKAKKEMKVGKQEKVKPTAAKAKETPKTPPKARKKDDKEMPAVHEQKDQYAFCRYMIDMFVHGDLKPGQSPVMPPPSLTPSKPALSTTALEEKEKEEKKKMEKKDTSDTKKKEKEVKKKSEETTIDGKGKEPGKPPETKQMTAKLTTQAAARKDEKKEESKKMRKPTEEQPKGKKQEKKEKHIEPAKTPKKEHPGPSEKLKKAKAEQAKEEIAAASTKKALHGKKEEKAKTVEQEVKKEKSGKSSSDLKDKEVKKEKSGKSSSDLKDKEPQLKNEEKSKPQVKKEAKLASSDKGQTRKQNITRPEQVIPHVKPEKAEHQEKGHPSIKKDKPKPSSKGAPEVPDSGKKKIEKSEKESKVPTREENLQVYNVTKAEKPGKIPKDSKEAPASKKDKEDSKEAPTSKKDKEDSKDVPHSKKDKEVTDDVSSPKKQTRPISFFQCVYLNGYNGYGFQFPVTPVQQPGENPGKTNSPGQKQQEQ", "text": "FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact. Required for normal skeletal muscle strength (PubMed:19843516). Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Single-pass type II membrane protein."}
{"protein": "MERTFIMIKPDGVQRGLVGEVIGRFEAKGFTLVGLKLMSVSKELAEEHYDVHKERPFFGSLVEFICSSPVVAMVWEGDGVVASARKLIGATNPLSAEPGTIRGDFGVSVGRNLIHGSDAIETAQREISLWFNEKELSSWEPTAKTWLYE", "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": "MGLPQIHRLKHRQDFQAVYGTGKRYHGSHLTLISLEDSCPDAPGPSRFGISISKKVSKKAVVRNRLKRQIRAVIRELLPEIAAGWRGIIIIRPGAIECNYEHFLRELKQLLVKANIIHGH", "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": "MKFNSDEIASVLQAEIEQFDNKIDVREVGTVLEVGDGIARVYGLSGVMAGEMVEFANGSIGLAFNLEENSVGVIILGDYLTIEEGQEVKALGTLLSVPAGDAVIGRVLDPLGNPLDGKGPVQTDITRPVEIIATGVAERKPVTEPLQTGIKAIDSMTPIGRGQRELIIGDRKTGKTAIAIDAILNQKGQGVKCFYIAIGQKDSAVASVVDVLERHGAMEYTTVIAAGASAPAPLQYVAPYAGTAMAEHFMFNGGHALVVYDDLSKQATAYRQMSLLMRRPPGREAYPGDVFYCHSRLLERSSKLSDELGGGSITSLPIIETLEGEVSAYIPTNVISITDGQIYVQPDLFFSGVRPAMNPGISVSRVGGAAQTKAMKKVSGGLRLQLAAFRALEAFAQLGTDLDPATQAELDRGYRMVELLKQPQYQPLSVAEQVISIYAGTNGHLDDVAVKEVQRFEKELLQYVHDKHSSLISDLTATPALSDEIAERIVAAVKEFKTVYKPATPAA", "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": "MTEPAPTRIYVDADACPVKDEIYKVAERHGLPVSVVAGAFIRVPAHPLIERIAAGSGMDAADDWIAERVQPGDIVVTADVPLASRCVKAGAEVLAPNGKPFSEASIGMTLAVRNLMTDLRSSGEVTGGPRAFSPRDRSTFLAALDTTIRRIARRRASPPAQQQN", "text": "SIMILARITY: Belongs to the UPF0178 family."}
{"protein": "MAIHLYKTSTPSTRNRAVDSQVKSNPRNNLIYGQHRCGKGRNARGIITARHRGGGHKRLYRKIDFRRNEKDIYGRIVTIEYDPNRNAYICLIHYGDGEKRYILHPRGAIIGDTIVSGTEVPIKMGNALPLTDMPLGTAIHNIEITLGKGGQLARAAGAVAKLIAKEGKSATLKLPSGEVRLISKNCSATVGQVGNVGVNQKSLGRAGSKCWLGKRPVVRGVVMNPVDHPHGGGEGRAPIGRKKPATPWGYPALGRRSRKRNKYSDNLILRRRSK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "MARWNVCSYCGREFEPGTGKMFVRNDGRVLFFCSSKCEKYYFMGRNPRKLKWTKAFQEARLQRAKRK", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
{"protein": "MSSMPNHQKVVLVGDGAVGSSYAFAMAQQGIAEEFVIVDVVKDRTKGDALDLEDAQAFTAPKKIYSGEYSDCKDADLVVITAGAPQKPGESRLDLVNKNLNILSSIVKPVVDSGFDGIFLVAANPVDILTYATWKFSGFPKDRVIGSGTSLDSSRLRVALGKQFNVDPRSVDAYIMGEHGDSEFAAYSTATIGTRPVRDVAKEQGVSDEDLAKLEDGVRNKAYDIINLKGATFYGIGTALMRISKAILRDENAVLPVGAYMDGQYGLNDIYIGTPAVIGGTGLKQIIESPLSADELKKMQDSAATLKKVLNDGLAELENK", "text": "FUNCTION: Catalyzes the conversion of lactate to pyruvate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family."}
{"protein": "MLDILIYPVSGVMKLWHLLLHNVAGLDDSLAWFFSLFGLVITIRAIIAPFTWQMYKSGRTAAHIRPHRAALREEYKGKYDEASIRELQKRQNDLNKEYGINPLAGCVPGLIQIPIVLGLYWALLRMARPEGGLENPVFQSIGFLTPEEVESFLAGRVSNVPLPAYVSMPTEQLKYLSTTQAEVLSFVLPLFITAAILTAINMAMSMYRSFQTNDYASGFSNGMLKFMIVMSILAPIFPLSLGLTGPFPTAIALYWVSNNLWTLLQTIIMMVILERKYPLTDDFKVHHLEQRDIYRAKQKEKRIFLWTRRKNRALMILTPWNASTLHATNVELTKTRTAEINEAKQARKEIANKRRETQREMNRAAMQRLKQRRAEVKAKKKGLIDASPNEDTPSENEETKLSSPQVEPTTTAEPNREPSQED", "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": "MIIKNASHEITAVKPIQYPVTGFPEIAFVGRSNVGKSSIINTLVNRKSLARVGSTPGKTRQINFFDVNGEFYLVDLPGYGFANVSKEMKASWQNLIETYLYSRKENFLKMVVMLVDIRHSPSKDDIIMYQWLKGFGLDTLIIANKVDKISRGQIHVRINDIRKVLQLDDAEKVIPFSAENRFGLEKVLAEFDNVLSIPGEEQKD", "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": "MKDVTIIGGGPSGLYASFYAGLRDMSVRLIDVQSELGGKMRIYPEKIIWDIGGIAPKPCHEILKDTIKQGLYFKPEVHLNERVVDIRKKSERHFEVETEAGEIYTSKAVIIAIGAGIINPKQLDVKGVERYQLTNLHYVVQSYRRFKDKDVLISGGGNTALDWAHDIAKIAKSVTVVYRKEDVSGHEAMKTLVTDLNVKLCPKTRIKYLVGNDDETHISEVVLEHVESGDTHAVKFDDVIISHGFDRCNTLLSETSSKLDMHDDCRVKGFGNTTTSIPGIYACGDIVYHDAKSHLIASAFSDGANAANLAKTYIQPDANAEGYVSSHHEVFKEANKTIVNKHLY", "text": "SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family."}
{"protein": "MNNKLTERQILILKAIINEYISTATAVGSKIILEKYFNNEVSSATIRNEMSVLEKEKYIEKPHTSAGRIPTIKGYQYYEANLAETKISERLKQKLMAILNKRYHSIDEVIEQSVEFINNVTNLPSVITKFKSYDLLKRMDLIKINNNTAIILIVSSSGEVIKKTIKYQNSIQYNDVSTCVQIFNDRLVDTPFIELKEKLTAIKEIVRTKVHEYEFVMQRIVNYIFDINEKSTINIKGTKKLVIHPEFHDHNKLSEILNLLENTSIWEQISFMQQKTGKSVITFGQDIGIEGISVASTLIETEQNKHQIAIVGPNRMEYGKIKGLLNILKEQVEKIDHLNLPLEEINKES", "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": "MEMKKKINMELKNRAPEEVTELVLDNCLCVNGEIEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDGFDQEDNEAPDSEEEDDDDEDGDEDEEDEDEDEAGPPEGYEEEEDDDEDEAGSEVGEGEEEVGLSYLMKDEIQDEEDDDDYVDEGEEEEEEEEEGLRGEKRKRDAEDDGEEDDD", "text": "FUNCTION: Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the ANP32 family."}
{"protein": "MSGKASTEGSVTTEFLSDIIGKTVNVKLASGLLYSGRLESIDGFMNVALSSATEHYESNNNKLLNKFNSDVFLRGTQVMYISEQKI", "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 involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. In association with PAT1, LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers oligoadenylated RNAs over polyadenylated RNAs. 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. Component of a nucleolar LSM2-LSM7 complex, which associates with the precursor of the RNA component of RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It may play a role in the maturation of a subset of nucleolus-associated small RNAs. 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. In association with PAT1, LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers oligoadenylated RNAs over polyadenylated RNAs. 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. Component of a nucleolar LSM2-LSM7 complex, which associates with the precursor of the RNA component of RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It may play a role in the maturation of a subset of nucleolus-associated small RNAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=LSM1 and LSM8 act competitively with respect to the localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the cytoplasm under conditions of stress. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=LSM1 and LSM8 act competitively with respect to the localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the cytoplasm under conditions of stress (By similarity). SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily."}
{"protein": "MLKRYLVLSVATAAFSLPSLVNAAQQNILSVHILNQQTGKPAADVTVTLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEIPVEFHINKVNEHYHVPLLLSQYGYSTYRGS", "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": "MLQSNEYFSGKVKSIGFTSSSTGRASVGVMAEGEYTFGTAEPEEMTVISGALNVLLPGETEWKVYTAGQVFNVPGHSEFHLQVAEPTSYLCRYLK", "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": "MDSFLRLLIHGASGRMGQSLLRLASEDPSFQVTAAVVGNAPHRHVSDGVPFFAAAELAAVPAFDVAIDFSLPQGFSSLLALCVARAVPLVSGTTGLDSRQHEALVMAGARIPLVWGSNFSVGMAALVNLVERAGDALSGWDCDIVESHHVHKQDAPSGSALTLGEAVACKGIAPRYTSLRAGDIVGDHLVQFTGLGERIELVHRATNRDVFARGALCVARRVVGRVPGCYRVRDLIM", "text": "FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapB family."}
{"protein": "MALLQISEPGMAPAPHQRRLAVGIDLGTTNSLVAAVRNSVPEVLPDEAGRALLPSVVRYLEKGGRRIGHEAKEQAATDPRNTIVSVKRFMGRGKAEVEGAANAPYEFVDAPGMVQIRTIDGVKSPVEVSAEILATLRYRAEDTLGDELVGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDNAAEGLYAVYDLGGGTFDLSILKLTKGVFEVLAAGGDSALGGDDFDHVLFGHVLAQAGIDAKALAPEDVRLLLDRVRVLKEALSSAPQASLDVTLSNGARLVQTISHDTFASLVEPLVQRTLTPTRKALRDAQVTPADIKGVVLVGGATRMPVIRDAVAKYFGQPPLVNLDPDQVVALGAAIQADLLAGNRGSGDDWLLLDVIPLSLGVETMGGLVEKIIPRNSTIPIARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMTAGAARIRVTYQVDADGLLSVFAREQHSGVEASVVVKPSYGLADDDIAKMLEDSFKTAEIDMRARALREAQVEAQRMIEATQAALSADGELLDDAERTQVDALVAALRTIAQGDDADAIETATKALADGTDEFAARRMDKSIKRALSGRRLDEI", "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": "MNETLSGVVTRVTGATYIVETGDGPKVRCRTVPSTVSENEGSNLVAVGDRVEFRPKASETEMAEGVIVRVEERRSVLERRREVRRNRSKEKEQVIAANIDQIVLITSFDDPPFNSRLVDRYLVFAESEHLPLLIVVNKIDLDEEGMVEEDLEVYRNLDCNICLVSAEDGRGIEELRELLRDRLSAFSGHSGVGKSTLINLLVGREELRTAETSGKTGKGVHTTTSSAMFQLPGGGYVIDTPGIREFNLAGITRENLRFYYTEFLRFMPECAFSSCSHTVEPGCAVIAAVESGRIDAERYESYLALLDSLDE", "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": "MENTFKLLFETIGERKRNPLPESYTNYLFSKGEDKILKKIGEECTEVIIASKNNDKEELVKEMVDVLYHCFVLLAEKNISLEDIMAEVTERNGKLSRVGDRREIDTL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSVRIF", "text": "FUNCTION: Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release. SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted Note=May be secreted by a non-classical secretory pathway."}
{"protein": "MCGIIGLAFAEGNSVAGALVRGLKRLEYRGYDSMGVAVIEPPGRLVVRKAAGKIGEVVRRTGVLSLRGRVGIGHTRWATHGPPNDVNAHPHTDCGGRVAVVHNGVIRNYASLRRELEARGHRLVSETDTELVAHLIEEYLGRGYSFLEALSLLGRVLRGSYALALLHLGEPDKVYFLRYKSPLVVGLGEGVNAVASDITAVLDVARDVIVLEDGEFGWISPEGVAIYRPRGDGGFEPLPPGALEERVKRVEWTPESASKAGYPHFMLKEIYEQPRALAETFEGIIEDPALLRAAGLVAGAGRLLIVGAGTSFHAGLVGHYYLSRLAGILGHPVVASEHKVYTPGVDGETVVVAVSQSGETYDTLEAVREWRGRGARVIGVTNVVGSALDREADVTLYLRAGPEIGVAATKTFLAQTILLQTLSIAAAGEAGRLTSGETRELTGVLEGAPDAARRAILASEGAAREAASLLKGAGSMYIIGRGLGGRLAMEAALKVKEVSYIHAEAYPAGESKHGPIALVEPGFKVYVVATSDSPEVMGNAIEMKARGASVTVVAPSDLQLDTPEGIEVLKMPPTGGETLLDPYSLTPYFQLLAYHLAVARGYDPDKPRNLAKTVTVE", "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": "MWLTKLVLNPASRAARRDLANPYEMHRTLSKAVSRALEEGRERLLWRLEPARGLEPPVVLVQTLTEPDWSVLDEGYAQVFPPKPFHPALKPGQRLRFRLRANPAKRLAATGKRVALKTPAEKVAWLERRLEEGGFRLLEGERGPWVQILQDTFLEVRRKKDGEEAGKLLQVQAVLFEGRLEVVDPERALATLRRGVGPGKALGLGLLSVAP", "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 enzyme processes pre-crRNA into individual crRNA units, but may not actually undergo enzyme turnover, retaining the crRNA product (PubMed:21572442). Generates a 2',3'-cyclic phosphodiester. SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family. Subtype I-E/Ecoli subfamily."}
{"protein": "MANVVVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTVVVNDQTFKLHLIPSGILYPNTDCIIGSGTVIDPKVLIEELDMLDKLGVSTSHLFISESAHVTMPYHRMIDQASEERRGDHKIGTTGRGIGPTYADKSERTGIRILDLMDPEGMKKQLRWTVNYKNVILEKLYNLPHLDPEEVIAEYQVYADRLRPFVADCSLKIYDAYQQHRNILFEGAQGTLLDLDHGTYPYVTSSNPVAGGACVGTGVGPTMIDRVIGVAKAYTTRVGEGPFPTELHDEMGVALCERGAEFGTTTGRRRRCGWFDAVIGRYAVRINGLDCLAVTKLDILDEVDEIKVCVAYEIDGHESKDFPTNARQFSRCNPVYKTLPGWKQSTIHCRTLEDLPPKALDYLKFLASIVEVPIAIVSLGAERDETIIVEDPIHGPKRALLYSNGESQAMSA", "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": "MPFYKQPWVFSKVFVLAMAKPPSFGCCFFLLFFSFLSSSFVSFALTDTEAAFIVQRQLLTLPDNGELPDDIEYEVDLKATFANTRLKRAYIALQAWKKAIFSDPFNTTGNWHGPHVCGYTGVVCAPALDDSDVTVVAGVDLNGADIAGHLPAELGLMTDVAMFHLNSNRFCGIIPKSFEKLKLMHEFDVSNNRFVGPFPNVVLSWPDVKYFDLRFNDFEGQVPPELFKKELDAIFLNDNRFTSVIPESLGESPASVVTFANNKFTGCIPKSIGNMKNLNEIVFMDNDLGGCFPSEIGKLSNVTVFDASKNSFIGRLPTSFVGLTSVEEIDISGNKLTGLVPHNICQLPNLVNLTYSYNYFSGQGGSCVPGGSRKEIALDDTRNCLASRPEQRSAQECAVVINRPVDCSKDKCAGGSSTPSKPSPVHKPTPVPTTPVHKPTPVPTTPVQKPSPVPTTPVQKPSPVPTTPVHEPSPVLATPVDKPSPVPSRPVQKPQPPKESPQPDDPYDQSPVTKRRSPPPAPVNSPPPPVYSPPPPPPPVHSPPPPVHSPPPPPVYSPPPPPPPVHSPPPPVFSPPPPVYSPPPPVHSPPPPVHSPPPPAPVHSPPPPVHSPPPPPPVYSPPPPVFSPPPSQSPPVVYSPPPRPPKINSPPVQSPPPAPVEKKETPPAHAPAPSDDEFIIPPFIGHQYASPPPPMFAGY", "text": "FUNCTION: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization. SUBCELLULAR LOCATION: Secreted, cell wall."}
{"protein": "MSLLCYNKGCGQHFDPNTNLPDSCRYHPGVPIFHDALKGWSCCRKRTVDFSEFLNIKGCTVGLHCAEKLPEVPPQPEGPATSSLQEQKPLNTIPKSAETLFRERPKSEMPPKLLPLLISQALGVALEQKELDQEPGAGLDNSLIWTGSSCQNPGCDAVYQGPESDATPCTYHPGAPRFHEGMKSWSCCGIQTLDFGAFLAQPGCRVGRHDWAKQLPASCRHDWHQTDSVVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKADPGSWAQLEHPDSLAEKARAGVLLEMDEEESEDSDDDLSWTEEEDEEEEEAMGE", "text": "FUNCTION: May play a role during maturation and/or organization of muscles cells."}
{"protein": "MLPFCFEMTSMSYIGRFAPSPSGPLHFGSLIAALGSYFQAKSQHGQWLVRIEDLDPPREMPGAADLILKTLETYHLFWDGEVVYQSQRHHLYQAQIDHWLQSGQAYYCQCSRKQIKEMGGYYNGHCQELHLDAGAIRLKMTQPITHFDDLRHGQMHIPLELAQEDFIIKRRDGLFAYNLAVVLDDIDQGVTEVVRGADLIEPTGRQISLYHMLGQVPVRYLHLPLAMDKNGNKLSKQNHATGIDLTHPASMILEAMAFLGFAIPKELHQANLDEILRWGVQNWRLNQLPESLEITARFSNGTA", "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": "MVKDFSSQHPLGDVSPSQYKSEVRNLSFYYGSFLALKNINMMLHEKKVTALIGPSGCGKSTFLRCFNRMHDLYPGNRYMGDIILHPDNVNILSRSVDPIEVRMRISMVFQKPNPFPKSIYENVAYGLRVRGVRRRAILDEKVEDALRGAALWDEVKDRLHQLAYNLSGGQQQRLCIARALATDPEILLFDEPTSALDPIATASIEELIADLKDKVTILIVTHNMQQAARVSDYTAYMYLGEVIEFGVTDTIFIKPKNKQTEDYITGRFG", "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": "MLKIVSKPSFNRIALMGREGVEGVPETLAALKDYLVSLNREVILEENAAHMIDGSRLLTVPANDLKKKADLLIVVGGDGSLLNAAHIAVPQQLPVLGINRGRLGFLTDIPPNELTQISDILDGHYREEVRFLLEGTVEEGDEIVAQGIALNDIVLLPGNAPKMIEFDIFINDEFVCNQRADGLIITTPTGSTAYALSGGGPILHPQLNAMALVPMFPHTLSSRPIVVDAESQIKITISPENDVSPYVSNDGQERVSIKPGGNVYTRKYHYPLHLIHPTDYNYYDTLRRKLDWEKRAAKV", "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": "MQILHTMLRVGDLDRSIKFYQDVLGMRLLRTSENPEYKYTLAFLGYEDGESAAEIELTYNWGVDKYEHGTAYGHIAIGVDDIYATCEAVRASGGNVTREAGPVKGGSTVIAFVEDPDGYKIEFIENKSTKSGLGN", "text": "FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. SIMILARITY: Belongs to the glyoxalase I family."}
{"protein": "MEIFVTGLLLGASLLLAIGPQNVLVIKQGIKREGITAVIIVCLLSDVVLFTLGTLGVGLISDTAPIILDILRWCGIAYLLWFAVMAARDALRARTEVTFVEHSEPVAAASASGGGVTTKQRPRLRITSGTRQVWVRPMLMAIVLTWLNPNAYLDAFVFIGGVGAQYGETGRWIFAAGAFAASLVWFPLVGYGAAALSRPLSSPRVWRWINIGVAVVLTGLAVKLILMG", "text": "FUNCTION: Catalyzes the efflux of L-lysine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LysE/ArgO transporter (TC 2.A.75) family."}
{"protein": "MRVSAVAVAAPASGSGKTTIATGLIGALRQAGHTVAPFKVGPDFIDPGYHALAAGRPGRNLDPVLVGERLIGPLYAHGVAGADIAVIEGVLGLFDGRIGPAGGAPAAGSTAHVAALLGAPVILVVDARGQSHSVAALLHGFSTFDTATRIAGVILNRVGSARHEQVLRQACDQAGVAVLGAIPRTAELELPTRYLGLVTAVEYGRRARLAVQAMTAVVARHVDLAAVIACAGSQAAHPPWDPVIAVGNTARQPATVAIAAGRAFTFGYAEHAEMLRAAGAEVVEFDPLSETLPEGTDAVVLPGGFPEQFTAELSANDTVRRQINELAAAGAPVHAECAGLLYLVSELDGHPMCGVVAGSARFTQHLKLGYRDAVAVVDSALYSVGERVVGHEFHRTAVTFADSYQPAWVYQGQDVDDVRDGAVHSGVHASYLHTHPAATPGAVARFVAHAACNTPRA", "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": "MTGPSGAGRSTAINVLEDLGFEAIDNLPMGLLMRLLDGPALRRPLALGLDARNRDFSTEGFLDLSKRLASLEGFQVTTLYLDCSADILLRRFSETRRRHPMSPGSSPLEGVEHELELLRPIREAADTLIDTTALNVHQLRREVERWFAPSGGSMLAISVESFSYKRGLPRGLDMVFDCRFLANPHWQPDLRAADGRDPAVAAYVHADPQYLPFFTRVTDLLQSLLPAFRSEGKAHLSVGFGCTGGQHRSVALTEAVAKALAEAGGQVSIRHREMERRKPDARPD", "text": "FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family."}
{"protein": "MMNMRKTHPLMKIINNSFIDLPTPSNISSWWNFGSLLGLCLITQIITGLFLAMHYTSDTLTAFSSITHICRDVNYGWLIRYTHANGASMFFMCLFLHIGRGLYYGSYLFYETWNIGIILLIITMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGSFSVDKATLTRFFAFHFIFPFIIVAMVMIHLLFLHEAGSNNPTGITSESDKISFHPYYTLKDMLGMMFMFLILMSLVLFYPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALFMSILILFLLPYLHTSKHRSMVFRPVSQCIFWLLVSDLLILTWIGSQPVENPFITIGQLASIYYFLSILILIPLAGLIENYMFKW", "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": "MPVADTSQLISGVAERYASSLFELALDAGSIEAVGADLTRIQALIDGSDDLKRLIVSPVFSADDQFKAISALVEKFGFSGLVGNFLKVVARNRRLFVLPGIIKAFRLLAARHKGEITADVTSAHALTLAQEIELKAALKGVTGKDVAVNVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG", "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": "MKIAVIGQSLFGREVYRELLKEGHQVVGVFTIPDKNGKADPLGADAEKDGIPVFKFPRWRVKGQAIPEVVEKYKALEAELNVLPFCSQFIPMEVIDCPKHGSIIYHPSILPRHRGASAINWTLMQGDKIGGFTVFWADDGLDTGDILLQRQCEVLPDDTVNTIYNRFLFPEGVKGMVEAVRLIAEGNAPRIKQPTEGATYDPMQKKENAKINWDQPAEDIHNFIRGNDKVPGAWTVVDDQQLTFFGSSFTRNGPAPDGQPLEIPGASRPALVTKTGLVLFGNDGERLTVKNIQFEDGKMIPASQYFKTADSAALQLSEEEQKVSEEIRAAWRRILTNVSEIEDSTDFFKAGAASMDVVRLVEEVKLKCNGLQLQNEDVYMATKFEEFIQMVVRRMRGEDGEEELVIDYVEKEINNMTVKIPHQLFINGQFMDAEGGKSYDTINPTDGTAICKVSLAQISDIDRAVAAAKEAFENGEWGKMNPRDRGRLLYRLADLMEEHQEELATIESIDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGRTIPINQARPNRNLTFTRREPIGVCGIVIPWNYPLMMLAWKTAACLTAGNTVVLKPAQVTPLTALKFAELSVKAGIPKGVINILPGAGSLIGQRLSDHPDVRKIGFTGSTPIGKQIMKSCAVSNVKKVSLELGGKSPLIIFHDCDLDKAVRMGMSSVFFNKGENCIAAGRLFLEESIHDEFVKRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLIEYCQTGVKEGGKLVYGGKQVERPGFFFEPTIFTDVTDEMFIAKEESFGPVMIISKFNDGDIDGVLKRANDSEFGLASGVFTKDINKALYVSEKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKAVTIEY", "text": "FUNCTION: Cytosolic 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide. May also have an NADP(+)- dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: In the N-terminal section; belongs to the GART family. SIMILARITY: In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily."}
{"protein": "MGAQWKVKHKEAAANAKGKIFGKLVKEITIAARNGADTATNAHLRLVVEQAKKASMPKETLDRAIKKGAGLLGETVQYHRVTYEGFAPHQVPLIVECVTDNINRTVAEIRVAFRKGQLGASGSVAWDFNHVGMIEASPDTPDADPEMAAIEAGAQDFEAGEEGATLFLTDPTDLDAVQKALPEQGFTVLSAKLGYQPKNPVSGLSDEQMAEVEAFLEGLDNHDDVQDMFVGLAG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family."}
{"protein": "MTTDHAGKKVDVVVVGNVDGEHVGVEQARHDLHEEAAAAAAADHHATRGLAIGFLIREVMVEGLASFLVVFWSCVAALMQEMYGTLTFPMVCLVVAMTVAFVLSWLGPAHFNPAVTITFAAYRRFPVWPKLPLYVAAQLAGSLLACLSVNAVMRPRHDHFYGTAPVVVHGTRLPFLMEFLASAVLMIVIATVATDGTAGKTVGGIAIGAAVGGLGLVIGPVSGGSMNPARTLGPAIVLGRYDGVWIYVVAPVAGMLVGALCNRAVRLSHRIVAFLCGTSVGIAGSP", "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": "MAKIVLCMVLLAFGRQVYGASLVPAPISEQDPELATCELQLSKYRRFILQAILSFEDVCDAYSSRPGGQDSDSEGWPFRHYAPPPTSQRGEIWAFFRLLMAQFGDKEFSPIIRDAVIERCRIKSQLQRDEKRNSVVLGKKQRFHSWGGKRSPEPPILPDY", "text": "FUNCTION: Acts through intracellular calcium in Malpighian tubule stellate cells to raise chloride conductance. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MPGPMNKRDLEPGIITDLAGRTTYGDYLQLDRLLSAQVTRSQPPHHDELLFIIQHQTSELWMKLLIHELGACIRYVQADRLEPSFKIFARVAHIQRMLFEQWSVLETLTPNEYLEFRDTLGSSSGFQSFQYRAVEFLLGNKDAQALMPFRHVPAIHGELERLFESPSLYDEFLRHLSRMGHPVPQSHVQRDWRKPYEKSPEVVEVFRRIYQDAEAHWDAYEMCEKLVDTEERFQLWRYRHMMTVMRIIGFKQGTGGSSGVGFLRKALDLRFFPELWDVRTELTPPPPRHRP", "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": "MNVFPKKIMLLGSGELGKEVAIAAKRLGCYVIACDRYNDAPAMQIADQFNVFNMNNGSELKEVIYKCNPDIIIPEIEALAVDVLKEIEQKITVIPNSRATAITMNRDKIRDLASNELNIRTAKFSYAVNQSELDLHAETIGYPLLIKPVMSSSGKGQSLVKNKNDLAQAWNLAIEKSRGKSNKIILEEFIDFDLEITLLTIRQSNGKTLFCAPIGHEQKNGDYQCSWQPAELTESVLEKAQQIAKRVTDNLGGVGLFGVEFFIKGEEVIFSELSPRPHDTGLVTLISQNLNEFELHLRAVLGIPIPEIVCHEASASRVILASMETTDVAFTGLEQALSQSNTNVFMFGKPSSTEGRRMGVAVAKAETIDEARIKADNAAQSVQFINE", "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": "MAQAWAFLLPVLFFGSYVTNLFLPTYASSPLCSGDGGRSFLCAQAPKDKDPSPASTMYKTAFHFQSAKNWMNDPSGPMYFNGIYHEFYQYNLNGPIFGDIVWGHSVSTDLINWIGLGPALVRDTSSDIDGCWTGSVTILPGGKPVIIYTGGDIDQHQVQNIAFPKNRSDPYLREWIKAANNPVLRPDEPGMNSIEFRDPTTGWIGPDGLWRMAVGGELNGYSAALLYKSEDFLNWTKVDHPLYSHNGSNMWECPDFFAVLPGNNGGLDLSAAIPQGAKHALKMSVDSVDKYLIGVYDLKRDAFVPDNVIDDRRLWLRIDYGTFYASKSFFDSNKGRRIIWGWSRETDSPSDDLEKGWAGLHTIPRRIWLADDGKQLLQWPVDEIEFLRTNEINHQGLELNKGDLFEIKEVDTFQADVEIDFELASIDDADPFDPSWLLDPEKHCGEVGASVPGGIGPFGLVILASDNMEEHTEVYFRVYKLQEKYMVLMCSDLRRSSMRPDLEKPAYGGFFEFDLAKERKISLRTLIDRSAVESFGGGGRVCITSRVYPAVLADVGRAHMYAFNNGSATVRVPQLSAWTMRKAQVNVEKGWSAIQNRGSI", "text": "FUNCTION: Hydrolyzes inulin-type beta-(2,1)-fructans. May play a role as a beta-(2,1)-trimmer during graminan biosynthesis (By similarity). SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
{"protein": "MKRYILATVIASLVAAPAMALAAGNNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS", "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": "MEQIKLDSIADAIEAIRKGEVIIVVDDEDRENEGDFICAAECVTPEIINFMSKEGRGLICAPISEARCTELKLDLMVGSNTATHETPFTVSVDLLGNGCTTGISASDRSKTIRALVDPDTKPEDLGRPGHIFPLKAKDEGVLRRVGHTEAAVDLARLAGFKPAGVLIEIMSEDGSMARLPELKQIATKFNLKLISIKDLIEYRLTHESLVKREIGVDMPTNLGDFDLIAFRQISTGEVHLALIKGTWEKDEPVMVRVHSSCVTGDIFGSCRCDCGPQLHKAMEMIQQEGKGVILYMNQEGRGIGLLNKLKAYKLQEQGRDTVEANLELGFKMDQRDYGTGAQILRDLNISKLRLITNNPVKRAALAGYGLEITEAVPIEIPSNPHNLEYLKTKRDKMGHTILKKD", "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": "MKLKNQDKHQSFSSNAKVDKISTDSLKNETDIELQNINHEDCLKMSEYENVEPFVSASTIQTGIGIAGKILGTLGVPFAGQVASLYSFILGELWPKGKNQWEIFMEHVEEIINQKISTYARNKALTDLKGLGDALAVYHDSLESWVGNRNNTRARSVVKSQYIALELMFVQKLPSFAVSGEEVPLLPIYAQAANLHLLLLRDASIFGKEWGLSSSEISTFYNRQVERAGDYSDHCVKWYSTGLNNLRGTNAESWVRYNQFRRDMTLMVLDLVALFPSYDTQMYPIKTTAQLTREVYTDAIGTVHPHPSFTSTTWYNNNAPSFSAIEAAVVRNPHLLDFLEQVTIYSLLSRWSNTQYMNMWGGHKLEFRTIGGTLNISTQGSTNTSINPVTLPFTSRDVYRTESLAGLNLFLTQPVNGVPRVDFHWKFVTHPIASDNFYYPGYAGIGTQLQDSENELPPEATGQPNYESYSHRLSHIGLISASHVKALVYSWTHRSADRTNTIEPNSITQIPLVKAFNLSSGAAVVRGPGFTGGDILRRTNTGTFGDIRVNINPPFAQRYRVRIRYASTTDLQFHTSINGKAINQGNFSATMNRGEDLDYKTFRTVGFTTPFSFLDVQSTFTIGAWNFSSGNEVYIDRIEFVPVEVTYEAEYDFEKAQEKVTALFTSTNPRGLKTDVKDYHIDQVSNLVESLSDEFYLDEKRELFEIVKYAKQLHIERNM", "text": "FUNCTION: Promotes colloidosmotic lysis by binding to the midgut epithelial cells of certain coleopteran and lepidopteran species. Active on Plutella xylostella and Bombyx mori. SIMILARITY: Belongs to the delta endotoxin family."}
{"protein": "MADEQQRRAQDGGSARDRHVPVMMERTLELLAPALSKGPAVVVDATLGMGGHSEALLAAHPELTLVGLDRDPDALRLAGERLAPHSDRVHLVHAVYDEWAEALAGLSLSKVDGALFDLGVSSLQLDETDRGFAYAHDAPLDMRMDSGAPRTAADVLNTYSAGELTRVLREYGEEKFAARIAAAIVRERAKAPFDRSGRLVELLYDAVPAASRRTGGHPAKRTFQALRIEVNAELEVLGRALPAALDSLAVGGRMVVMSYHSLEDRMVKRAFAERAKSKTPVDLPVELPGHGPEIRLLTRGAELASDAETAANPRAASVRLRAAERIKEAV", "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": "MSYKLMLVENDIVLSKAIQEYLIDQGFNVYIANNGLEALNLAYQYNFDLIISDIMMPLVNGYELLAKLKKNKALSKIPVIFLTAKGMTKDRIKGYDMGCYGYLSKPFDPNELLSIINNLIARDVLKEASLQNSATSNQQLNHKIRLTPREKSILDLVVDGLTNKEISTILNTSVRNVEKYVSRLLHKTNMKNRTLLVKYSINNNLLNNEINERANDGTRTRE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL", "text": "FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity). SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side. SUBCELLULAR LOCATION: Mitochondrion inner membrane Lipid droplet Note=Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid- deplete conditions. SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Cytoplasm Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily."}
{"protein": "MATPHINAVEGAFAETVLFPGDPLRAKYIAETFLENVEQVTDVRNMLGFTGTYKGKRISVMGSGMGIPSCSIYAHELIKDYGVKNLIRVGTCGAISTDVKVRDVIIGMGACTDSRVNRLRFKDNDFAAIADYSLLSAVVDSAKAHGTKIRVGNVFSADLFYTPDPQMFDVMEKMGILGVEMEAAGLYGVAHELGAKALCVVTVSDHIRTGEKTTSDERQTTFSDMIIMTLDAALTL", "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": "MKPTILLYDSGMGGLTIYDAIRENLPDAHYLYCFDNAYFPYSEKSEAVLIELAVGIVQKIAENYPLDMVVVACNTASTVVLPALRERFAMPIVGTVPAIKPAAQISQTKTIGLLATKGTVTRPYVDELIERYAKDCVVERIGSTDLVEIVEEKQQTGSVDMRRLQKVVEEWQSHPTLDTVILGCTHFPLVKEELQQLLPRVSFFVDPGNGIANRVVSLLQDVKRNVNNENKENQAFCTQNSENFLKREKVMQNWGFKRLNILNFVEK", "text": "FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family."}
{"protein": "MSNEFTHINADGNAHMVDVTEKAVTEREARAEAYIEMAADTLEMIMSGSHHKGDVFATARIAGIQAAKKTSDLIPLCHPLMLTKVEVELEAQPEFNRVRITSLCKLSGKTGVEMEALTAASVAALTIYDMCKAVQKDMVISQTRLLEKRGGKSGHFKV", "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": "MEHIYQYTWIIPFIPLTVPLLIGAGLIIFPTTTKNLRRMWAFPSILLLSLVMLFSTKLSIQQINSHYIYQSVWSWTINNDFSLEFGYLVDPLTSIMSMLITTVGILVLIYSDNYMVHDQGYLRFFAYLSFFNTSMLGLVTSSNFIQIYIFWELVGMCSYLLIGFWFTRPIAANACQKAFVTNRVGDFGLLLGILGLYWLTGSFEFRDLFEIFNTLIYNNEVHFLVGTVCTFLLFAGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLFPLLIVTPFILNLIALVGIITLFLGATLASCSKDIKRGLAYSTMSQLGYMMLALGMGSYRAALFHLITHAYSKALLFLGSGCVIHSMEAIVGYSPDKSQNMVFMGGLKKHVPITKTAFLLGTLSLSGIPPLACFWSKDEIINDTWLYSPIFAIISWATVGFTAFYMFRIYLLTFEGHLNVHFQNYNGKKSSSVYSISLWGHEGLKPINKNLSLFTLLPIKNNESFYKNPHGDIKKTIQSFLITNNCDNKKIVPYPHESGNTMLFPLLVLIIFTGVIGFIGIPFDQENMDFDILSSWLTPSVNLLHLKLNNKNSFDWSEFLTNATLSVSIAYSGIVLASFLYKPIYSYSSLQNFALINLFAKRHPKRFFSDKIKNVIYDWAHHRGYIDAFYTRYIIRSVRGLSQFINFFDRRVIDGIPNGLGVTSFFVGEGLKYVGGGRISSYLFLYLLYASIFLLIYYFDFTNININFTDQ", "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": "MAYPVQLGFQDAASPIMEELLYFHDHTLMIMFLISSLVLYIISLMLTTELMHTNTMDAQEVETVWTILPAAILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYEDLCFDSYMTPSSDLKPGELRLLEVDNRVVLPTELAVRMLISSEDVLHSWTVPSLGVKTDAIPGRLNQATLMASRPGVYYGQCSEICGANHSFMPIVLELVPLKHFEEWLLSML", "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": "MVYRKSENGLIAGVDEVGRGCLAGPVVACAVILTENLAIPGDSKVLSRAVRLSWYEEIISNSYNAIGMSSVKEIETMNILNATLLAMERALERLPVVPTTVLIDGRDIINNAAKYKEVKSVVSGDKIYGEIKAASIVAKVTRDRLMEGLDLTYPYYRWKFNKGYGTKEHLEALAKYGVTDHHRRKFAPVKRMLLR", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MGSEKEQRPEAHLPEEGEGAKPWRVDGSKDSQITPREDHGQESLLAGLHGTHPPKTRQKVTAQAGGPGDPMLFSSPETDEKLFICAQCGKTFNNTSNLRTHQRIHTGEKPYKCSECGKSFSRSSNRIRHERIHLEEKHYQCAKCQESFRRRSDLTTHQQDHLGQRPYRCDICGKSFTQSSTLAVHHRTHLEPAPYICCECGKSFSNSSSFGVHHRTHTGERPYECTECGRTFSDISNFGAHQRTHRGEKPYRCTLCGKHFSRSSNLIRHQKTHLGEQDEKDFS", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MKIPEAVNHINVQNNIDLVDGKINPNKDTKALQKNISCVTNSSSSGISEKHLDHCADTVKSFLRKSIAAQSYSKMFSQGTSFKSLNLSIEAPSGARSSFRSLEHLDKVSRHYLSEIIQKTHPLSSDERHLLSIIINSDFNFRHQSNANLSNNTLNIKSFDKIKSENIQTYKNTFSEDIEEIANHDFVFFGVEISNHQETLPLNKTHHTVDFGANAYIIDHDSPYGYMTLTDHFDNAIPPVFYHEHQSFFLDNFKEVVDEVSRYVHGNQGKTDVPIFNTKDMRLGIGLHLIDFIRKSKDQRFREFCYNKNIDPVSLDRIINFVFQLEYHIPRMLSTDNFKKIRLRDISLEDAIKASNYEEINNKVTDKKMAHQALAYSLGNAKSDMALYLLSKFNFTKQDIAEMEKMNNNMYCELYDVEYLLSEDSANYKVLEYFISNGLVDVNKRFQKANSGDTMLDNAMKSKDSKTIDFLLKNGAVSGKRFGR", "text": "FUNCTION: ADP-riboxanase effector that mediates arginine ADP- riboxanation of host caspases (PubMed:34671164, PubMed:35338844). ADP- riboxanation of host apoptotic caspases (CASP3 and CASP9) prevents their activation, thereby inhibiting host cell extrinsic and intrinsic apoptosis (PubMed:35338844). Does not catalyze ADP-riboxanation of host CASP4/CASP11 or CASP8 (PubMed:34671164, PubMed:35338844). In contrast to Ospc1 and OspC3, not able to inactivate host calmodulin (PubMed:35568036). SUBCELLULAR LOCATION: Secreted Note=Secreted via the type III secretion system (TTSS). SIMILARITY: Belongs to the OspC family."}
{"protein": "MKKLFKKKKGVSPHMYMLPEESNSNTATNAPSYSVGGTTANSYSSNSYNDNNNSNSTYGSSNNYGNYGSSNNYGSYGASNTYGSNGSSNNYGNYGATNSNGDAGYSITPIRNDPYARKDMPPMKSSAAVTERPSMHRSAPSQDTLDLKKQELFAGARIQNDDESTTDTIPHNDDGTEGDEYGEGYRDGYEEDQEVEAIKQKIQFVKQDSLSSTRNALLMAGNAEQMGLATLANLGEQTEKIATAEKELDISKIHAKRAEEQARELKTLNRSMFAIHVPKPWGKAKRVAAEEARLAAKRDAERQDEMLNRQFAYRSQKRIDQAMKDNMKSNKKKGDSKGVSILERSHYQFEPDAEDDAMEKEIDGNLDQIGALATRLKGLAYATGQEIDSQNARLGSIHDKSDRLDTDVYLNVERLRHIH", "text": "FUNCTION: Has a role in cell separation, a final step of cytokinesis and in the assembly of the forespore membrane. May have a role in the transport of secretory proteins to these growing sites. SIMILARITY: Belongs to the SNAP-25 family."}
{"protein": "KEGYPVDWGNCKYECMSDAYCKDLCVDRKAKSGYCYKLNWFCYCEGLPDDSPIKTNGHCRPGGRRK", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MAEEQAAAQEQQPAFGIEKVYVKDLSLEIPHAPQIFIQREAPQVSIELSNATAQLEEGIYEVVVTVTVTSKIADKTVFLVEVAQAGIFQIRNVPQENIDIILGVTCPNIIFPYARETISDVVTRAGFPPVLLNPVNFEALYAQQKQEQAKANGATTH", "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": "MAKLALGHHREATDPGCLRAVVAELLLTFLFVFSGVGSAMAAAKLGGGGDTIMGLTAVAAAHALVVAVMVSAGLHVSGGHINPAVTLGLAAGGHITLFRSALYAAAQLLGSSLACLLLAALTGGEEAVPVHAPAPGVGAARAVAMEAVLTFSLLFAVYATVVDRRRAVGALGPLLVGLVVGANILAGGPYSGASMNPARSFGPALAAGEWADHWIYWVGPLIGGPLAGLVYEGLFMGPPGHEPLPRNDGDF", "text": "FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. May be involved in transport from the vacuolar compartment to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC 1.A.8.10) subfamily."}
{"protein": "MTQPSAIDDILAEHAGLETQLADPTLHNDPSAARRVGKRFAELAPIMATYRKLESARADLTAARELAADDASFAAEVPELERQVDELEQALADLLAPRDPHDGDDVVLEVKSGEGGEESALFAADLARMYMRYAERRGWRVEVLDATVSDLGGYKEATLSIKSRDAARDGVWSRFKFEGGVHRVQRVPVTESQGRIHTSAAGVLIYPEPDEVAEVQIDESDLRIDVYRSSGKGGQGVNTTDSAVRITHLPTGIVVTCQNERSQLQNKARAMQVLAARLQALAEEQAEQEAAAGRASQIRTVDRSERIRTYNFPENRITDHRIGYKSHNLDAVLDGDLDALLDALGKADREARMAAE", "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": "MICKNSIVTSSSKLFYKMFFIAISIEILEYNYIYPLCIEIAQHSGNIKIALCLKEILQKKKYNLILLKIASIVISNFLSTNTYSFIYTPYDVEILFSNLLLEKYEKDKEMSYMIDVFTKLSHLKQNIIYPYLFNQLKHDCNKKHIFLLLKKIDYTDISTFTHSIFIK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MQSLAGKKILLGISGGIAAYKCAELTRRLVERGATVQVVMTHAAKEFITPLTMQAVSGRPVSDSLLDPAAEASMGHIELAKWADLVLLAPATADLIARMAAGMGNDLLTTLILATSAPVAIAPAMNQQMYRNIATQENLQTLIRRGYLTWGPAAGEQACGDVGPGRMLEPMELVAHCENFFAPKILVGKRVLITAGPTREALDPVRYITNHSSGKMGFALAKAAAQLGADVTLVSGPVHLPTPVGVNRIDVQSGLEMHSAVMKEATSHQIFIACAAVADYRPQTVAEQKIKKSRDNDTLTIEMVKNPDIVASVAALTENRPFTVGFAAETQDVETYARSKLVRKNLDMICANDVSIAGQGFNSNDNALTLFWKEGQHSLPLTSKDALASAVMHLIHEQM", "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. 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": "MQGVYPAIITPLKENKVDYDGLRNNIDFLIENGVSGVIPVGTTGESPTLTPLEHEKVVEKVVEFVDGRVEVIAGTGSNSTSEALEFSQYAEDVGVDGVLLITPYYNKPTQEGLKRHFGEIANSINVPIVLYNVPSRTALNIEPETIKYLFNEYSNISAVKEANPNLSQVSEVLDSCDIDILSGNDELTLPIISLGGKGVVSVIANIAPKEFVQMVDFANAGKFDKAKEIHYKLFPLMKLMFVETNPIPIKTAMNMLGMPSGELRLPLCEMAESNKLKLQNALNNLGLLK", "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": "MASLRELKGRIESTKKTKQITGAMQLVSASKMSKAEQNARGFVPYADKLQEVVSSIANANTDAQHPMLMKREVKKTGYLIITSDRGLVGAYNSHILKNLVNTIEKNHTSKDEYTIIVLGRKGYDYCRKRGLPVSKSVLGVPDHPTFADVKELASETVQMYADGDIDELNIIYNHYVSAISQVVTNKQLLPIDNLDESGAATSDYEFDPNQEQILEVLLPQYAESLIFGALLDGKASEHAASMTAMRSATDNASDLIDDLSLSYNRARQAAITQEITEIVGGVAALE", "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": "MNEKHLTYADSGVDIEKEESTIKALTNGMTYKREGIGAPLTSIGHYAGLIDFGEYALAMATDGVGSKVLIANEMKRWNTVGIDCIAMNVNDLLAIGAEPISFVDYLALEKHSDDFASQIGEGLVKGAEISRMSIVGGETATLPEIVNGFDLAGTCLGMVKKEEVITGEKVRLGDVLVGIPSNGVHSNGYTLVRDIIKESGHSYHEDFSYNTETTIGDELLIPTRIYMEVLDVIKECDVHGLAHITGSGLLKLKRVTGLGFDFTDPIEPGNIFKFLQEEGNVDDLEMYRTFNMGMGFLIILPEADAEKAAEMTGGKIVGKIVESGIRVRDLEIV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
{"protein": "MTATNHPKLFKRPVDGVLLLDKPGGMTSNEALQRVKRLFHAKKAGHTGSLDPLATGLLPICLGEATKFSQFLLGADKSYSVKGRLGVRTASGDSESPILTERPIPKLTKRALEKTLSAFRGVIDQTPSMYSALKHKGQPLYKLARQGIEVERKTRQVTIYELTLLDWDNESIELYVHCSKGTYIRTLLDDVGEALGCGAHVVALRRLRVAHYHEDQMIKLAHLEREYDKANYTGLDRYLLPLETMVSHFPAIKLSSSTAFYLQQGQAVMVPNAPTHGFVRLRDQNDQFIGIGEILSDARIAPRRLIQKR", "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": "MTSRFGHSQHPRRGRSARARAGRREGVQSNFPATQVLERSAHSLPARQRTALVMAGGTGGHIFPGLALAEALRERGWQVHWLGTPGSMEERLVPPRGFAFEPIDFSGVRGKGLKTLLALPLRLARACLQARAVVRRLQPDVVIGLGGYVTFPGGIAARLARKPLLLHEQNSVPGMANKLLSRLATRVYTAFPNVLPDAQWVGNPMRRAFTRQPRPERRLAGREGPLRLLVVGGSLGAKALNDIVPQALAWIHEQDRPIVTHQSGESQIEALRRSYAAAGVEATLTPFIEDTAAAFAEADLVLCRAGASTVTEIAAVGAAAVFVPFPHAVDDHQTTNAQYLVKVGGGWLVQQADLTAHGLAEMLQNMKRQDLLAKAQKARTMRKINATRDIVAACERLAR", "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": "MLNNTMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGASNVHLVYGHGGDLLKKTLSDDKLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLIAVETLTRLREAKPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDASDEQRQIQEINTGILIANGADLKRWLSKLNNNNAQGEYYITDIIAMAHHEGHEITAVHPTRISETDGVNNRLQLSRLERIYQAEQAEKLLLAGVMLRDPARFDLRGTLAHGRDVEIDTNVIIEGQVTLGHRVKIGTGCVIKNSVIGDDCEISPYSVVEDARLDAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDSQLVAPVTIGKGVTIAAGTTVTRDVAENELVLSRVPQVNKQGWQRPVKKK", "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": "MRKIKGLRWYMIALVTLGTVLGYLTRNTVAAAAPTLMEELNISTQQYSYIIAAYSAAYTVMQPVAGYVLDVLGTKIGYAMFAVLWAVFCGATALAGSWGGLAVARGAVGAAEAAMIPAGLKASSEWFPAKERSIAVGYFNVGSSIGAMIAPPLVVWAIVMHSWQMAFIISGALSFIWAMAWLIFYKHPRDQKHLTDEERDYIINGQEAQHQVSTAKKMSVGQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKVYGFNLKEIAMFAWMPMLFADLGCILGGYLPPLFQRWFGVNLIVSRKMVVTLGAVLMIGPGMIGLFTNPYVAIMLLCIGGFAHQALSGALITLSSDVFGRNEVATANGLTGMSAWLASTLFALVVGALADTIGFSPLFAVLAVFDLLGALVIWTVLQNKPAIEVAQETHNDPAPQH", "text": "FUNCTION: Transport of aldohexuronates such as D-glucuronate and D- galacturonate (PubMed:783117, PubMed:6343797). Under anaerobic conditions, can play a critical role as a D-glucose transporter in the absence of sugar-PTS system (PubMed:32038601). FUNCTION: Transport of aldohexuronates such as D-glucuronate and D- galacturonate. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Phthalate permease family."}
{"protein": "MGPAGCAFTLLLLLGISVCGQPVYSSRVVGGQDAAAGRWPWQVSLHFDHNFICGGSLVSERLILTAAHCIQPTWTTFSYTVWLGSITVGDSRKRVKYYVSKIVIHPKYQDTTADVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRDYHSALQEAEVPIIDRQACEQLYNPIGIFLPALEPVIKEDKICAGDTQNMKDSCKGDSGGPLSCHIDGVWIQTGVVSWGLECGKSLPGVYTNVIYYQKWINATISRANNLDFSDFLFPIVLLSLALLRPSCAFGPNTIHRVGTVAEAVACIQGWEENAWRFSPRGR", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MAFPQRKRTPSFSSSVLDSVYRSIDESDGLQSDLKGSINENVSSSSSSPSPNKKDDKLTTLRRAIMDEEHWLYARSSTTTTNSSDSSSFSSSEAESYRTKRRLRKLAEQGKRSGDERQRTKRTVMDNDSRLFSKSDDDKKPKAVKIIEELKRSKQPVSPGARLTSFLNSIFQSNAKKVKLCSVGKTTDVKSSSSKSCFSRTRNKTDNNNNNCKKLERSIRFYPVRVTIDGDCRDYAQKHITRVRKPIPEFTAKKSVKEEIKTNDHHTEFTCITRNIGLKDFVRSNKYEGKEEEEDAWSHSSSDLFELDSYRIGMGRYLKELPVYETTDFKTNQAIARSLLL", "text": "FUNCTION: Involved in auxin transport. Regulator of the auxin signaling pathway. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the BIG GRAIN 1 (BG1) plant protein family."}
{"protein": "MKYQKPKGTADILPPFSKEWQFVEQNARETFALYNYEEIRTPIFEKFEVFSRSAGDTSDIVTKEMYDFDDKGGRHIALRPEGTAGVVRAFVENKLYGPEHQKPVKVYYMGPMFRYERPQSGRLREFHQIGVEAFGSDSPKIDVETIMMGMDFLKKLKVSGLKLVINTLGDKESRDRYRQALIDYLEPHFEELSDDSKARLHKNPLRVLDSKDKNDQKIVENAPEILDFLTEDAQKHFTSVKEELDTLGVDYVVDSSMVRGLDYYNHTIFEIMIADSPLGKGDVTICAGGRYNGLVEELGGPEVSGVGFGLGVERLLLLLNAETQTTLQSKQLDFYVVGIGDLVQNDVLKVVHELRQMNFVTEQDYLDRKPKAQFKSADKLNAKYVVTIGESEMNDRIFKLKDMHSGEERTVALSEINTLKDLLK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MEMKQISETTLKITISMEDLEERGMELKDFLIPQEKTEEFFYTVMDELDLPENFKDSGMLSFRVTPRNDRIDVFVTKSEINKNLNLEDLSDFDDISKMSPEDFFNTLEETMREKGDAAALDKLAEIEKREEEKTQQEKGETKEKRDYVHFVLDFPNIQQVINFAKTVDYDVEASELFKESDAYHMTVLLNLEDKPDYYADLMFARMLEHAGRGTKTRAYLLEHGVQLIKADALQELQMIG", "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": "MNQNREVRTRFAPSPSGFLHVGGARTALFNYLYAKSQGGKFILRIEDTDQNRSTEDSFKIILESLKWLGVRWDEGPEIGGEYGPYIQSQRLDIYKEYTEKLLKEKKAYRCFCTQEELEAKKKQAEAMGVPYVYDGLHANMSDEEVEEKLKQKIPYSIRFKTPSKTLIVDDIIQGKVKFETKLIGDFIIVKSDGFPSYNYAVVVDDALMKITHVIRGVGHLSNTPRQILLYEALDYEIPEFAHASEIVGMDGKKLSKRAGATSILAFRDLGYLPETFRNYMALLGWTSSDGREFLPEGELEKIFDVHRCSKSPSTFDVFKKPKGGEDEVVTNFSDLTQIAEAMNPKSKLNWLSNRTIRDLKISKVLESLLPFLKDRKDIPEEVKNINSPALTSIIESIRVYLDNLAQAPDYIAEFFVTDLKIQSQEATGFMKDGDGPKVVKEFYGILKNSDPKTDENYKDLMSKVGEVTGQKGKTLYMPIRVATTGKSVGLELPILFPLLGKEKLLQRIEKTAKEAGIPLST", "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": "MNKLPHETRVVIGMSGGVDSSVAALLLKEQGYDVIGIFMKNWDDTDENGVCTATEDYNDVIEVCNQIGIPYYAVNFEKQYWDKVFTYFLDEYRAGRTPNPDVMCNKEIKFKAFLEHAMALGADYVATGHYARVAYMDGEYKMLRGVDDNKDQTYFLNQLGQEQLSKTMFPLGELKKPQIREMAKEAGLATATKKDSTGICFIGERNFKDFLSNYLPAQPGVMQTLSGEVKGKHDGLMYYTIGQRHGLGIGGNGDPWFVVGKNLKENILYVDQGFHNELLYGDEVIATNVNWVSDRAKEKEFKCTAKFRYRQEDNGVTVQIVDENTIRILCDEPIRAITPGQAVVFYDGDECLGGATIDEVYRSGEQLDYLG", "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": "MDARRKHWKENMFTPFFSAQDVLEETSEPESSSEQTTADSSKGMEEIYNLSSRKFQEESKFKRKKYIFQLNEIEQEQNLRENKRNISKNETDTNSASYESSNVDVTTEESFNSTEDNSTCSTDNLPALLRQDIRKKFMERMSPKLCLNLLNEELEELNMKYRKIEEEFENAEKELLHYKKEIFTKPLNFQETETDASKSDYELQALRNDLSEKATNVKNLSEQLQQAKEVIHKLNLENRNLKEAVRKLKHQTEVGNVLLKEEMKSYYELEMAKIRGELSVIKNELRTEKTLQARNNRALELLRKYYASSMVTSSSILDHFTGDFF", "text": "SIMILARITY: Belongs to the CCDC160 family."}
{"protein": "MKNNKSVIIWLLSGCFLVFIMVVVGGITRLTNSGLSMTDWHLVTDTFPPLTEAKWEETFEKYKLFPEYQKINIHNDFTLSDYKFIYFWEWFHRFIGRIIGLVFIIPFIYFLIKKKLNTETLRKCAILLGMGAFQGFLGWFMVKSGLIDAPDVSHFRLSLHLTFAFITFAYTLWVALDLIYPEKKQVILPLRNIARITLAIIILQIIYGGFVAGLNAGLIHNHWPLMSDGQFFHESIILEKESWFARFTEGKSGVQFVHRTIAYFVAGLIVFLTFKSKKHTLSLEQKNGLNALLIIVFIQFTLGVLTLLYSVPLWLGVIHQAMAFILLATTTYTLHRFSK", "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": "MTWRDEIARRVRGEHLRDAPLAPRTAVRVGGPADLLCRPADGDALSALLRAVRELGVPLSVLGGGANTLVADAGVRGVVLRLPQEFPGESTDGGTLVLSAGAPISRLPARAHAHGLVGMEFLGGIPGTLGGAAAMNAGTRLGEMKDVVTRLELATPDGTGFVPASALGYAYRTCRLPPGAVIARVEVRLHAGDVAASEALMREDRERRRATQPLDRPTFGSTFTNPPGEYAGRLVEAVGLKGHRVGNAIWSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLMGEFLDEDLEGLDGHAAAGGGPGAASGGVRPPEAT", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
{"protein": "MADTGYYAGYQDDVDVDEHKRHQALYLIGIILLVTVCLIVLWVCIMLACYVPGFLKKTLEAWLNSSSLMKRRVASTLTRTPFEATGPERERNWDARRQSTTVNPASQPNTGSVF", "text": "FUNCTION: May transport viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier (By similarity). SUBCELLULAR LOCATION: Host cell membrane; Single-pass membrane protein Note=The hydrophobic region is responsible for the localization of the protein to the cell periphery. SIMILARITY: Belongs to the nanovirus movement protein family."}
{"protein": "MAEAIRSDWSVDEVEALLRLPLLDLVGRANGVHRAHHAPDDIQKASLLSIKTGGCPEDCAYCPQSAHHREVELTREKLMNPDHVVSLARRAQRAGAERFCMGAAWRQVRDGAEFDNVLAMVRGVRALGMEACVTLGMLRPHQAQRLAEAGLTAYNHNLDTSPEFYGQIIGTRTYQDRLDTLAYCRDAGIELCCGGIIGMGESLRDRAAMLQVLANFAPHPESVPINALIPIEGTPLAHRERVGIFDLVRMVATARIIMPLTRVRLSAGRSDFSAAEQALCFLAGANSVFYGDVLLTAPNAGTGADAELFAALGALETA", "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": "MARIAGVDLPRDKRIVVALTYIYGIGNATAKKICADAGVSEDVRSKDLTPEDQEKLRTEVDKYRVEGDLRREVSMNIKRLVDIGSYRGIRHRRGLPVRGQNTKNNARTRKGTKRNR", "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": "MPATALSLPLDEIRYDERGLVPAIVQDYLDGTVLMLAWMNRESLQKTLETGRTWFWSRSRQELWPKGETSGHVQWVKSIRYDCDSDALLLTVEQVGHIACHTGERSCFHRHGAKGESIEPPPADTLSQVYNIVCQRRDFPQLQSYTSSLFTAGDNKILKKLGEETAEVVMACKDDDPEAIASEVADLFYHTLVALAYHRVSLRQVYEQLQLRRR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family."}
{"protein": "MTIKKLILVRHGESEWNKENRFTGWADVDLSEKGRVEAQQAGNLLKKKGFSFDFAYTSVLRRATNTLSLILDVLQQQNLPIEKSWRLNERHYGALQGLNKSETAAKFGSEQVKQWRRGFSTLPPALNLNDPRAPANDSLYATLNKNDLPLTESLATTVDRVVPYWDEVVKPRIIDGKRVIIVAHGNSIRALVKYVDHLSEEEIMEINIPTAVPLVYEFNSSLQPINHYYLGNAEEITQKVAAVAAQGKA", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
{"protein": "MTTGDLVNIHPTELKFPFELKKQSSCSMQLTNKTTTQCVAFKVKTTNPRKYCVRPNTGVVLPGDSCNVTVTMQAQKEAPLDMQCKDKFLVQTVVVSDGTTSKEVLAEMFNKEAGRVIEDFKLRVVYIPANPPSPVPEGSEEGNSPMASLNDIASQSASLFDDVSRTFEETSEKSSEAWSMISKLTEEKTSATQQSQKLRLELEMLRKETSKKQSGGHSLLLMLLVGLLGCVIGYLLNRI", "text": "FUNCTION: May play a role in vesicle trafficking. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family."}
{"protein": "MPRVKGGPVTRRRRKKVLKLAKGYFGAKHALYRVANQQVMKSLMYAYRDRRQRKRDFRKLWIARINAAARQNGLSYSRLMHGLKLAGVEVNRKMLADLAVNDQAAFAQLADLAKANLNK", "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": "MTNIRKTHPLTKIINNSFIDLPAPSNISAWWNFGSLLGICLIIQILTGLFLAMHYTSDTATAFSSVTHICRDVNYGWIIRYMHANGASMFFVCLFLHVGRGLYYGSYMFPETWNIGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFAFHFILPFIISALAAVHLLFLHETGSNNPSGIPSDSDKIPFHPYYTIKDILGALFLILTLMLLVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILVLAIIPLLHTSKQRSMMFRPLSQCLFWLLVADLLTLTWIGGQPVEYPFITIGQLASILYFMILLVLMPIASIIENNLLKW", "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": "MTNFLIVVATVLVMELTAYSVHRWIMHGPLGWGWHKSHHEEHDHALEKNDLYGLVFAVIATVLFTVGWIWAPVLWWIALGMTVYGLIYFVLHDGLVHQRWPFRYIPRKGYARRLYQAHRLHHAVEGRDHCVSFGFIYAPPVDKLKQDLKMSGVLRAEAQERT", "text": "FUNCTION: Catalyzes the hydroxylation reaction from beta-carotene to zeaxanthin via beta-cryptoxanthin. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MLGLRLIVGLGNPGSEYIKTRHNAGFRFVDGLVQREGQCWALESKLFAYVARVFIAGQWVWLLRPVTFMNLSGKSIFAGLNFWKIKPEQMLVAHDELDFPPGAVRLKFDGGHGGQNGLRDITKLLGHGRFHRLRVGIGHPGHKERVVSWVLGCPTCDENIAIDAALERASVVLPLAVAGDFDGAMKKLHTVV", "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": "MIKIQPEEISSVIRKQIEQYNQEVKVVNTGTVLQVGDGIARIYGLAKAMAGELLEFEDGTVGIALNLESNNVGAVLMGDGFSIQEGSRVKATGKIAQIPIGESYIGRVVDALARPIDGKGDIPSSETRLIESPAPGIISRRSVYEPLQTGLVSVDAMIPIGRGQRELIIGDRQTGKTAVAIDTILNQKGQNVICVYVAIGQKASSVAQVVSTLEENGAMAYTIIVAENANAPATLQYLAPYTGATLAEFFMYSGRHTLVIYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSNALGEGSMTALPIIETQAGDVAAYIPTNVISITDGQIFLSADLFNSGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGRRLRELLKQAQSSPLPVAQQVLTIYAGVNGYLDSIAIEDVKKFLAGLRNYVITSKAAIINNINSSKAVTPETEGMMKEAINEYKKVFAAGA", "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": "MSSKPKPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAFVDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFGTKREGNHKPETDYLKPPK", "text": "FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. FUNCTION: Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (By similarity). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid- derived suppressor cells (MDSCs) plays a role in suppression of T cell- mediated antitumor immunity. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic granule. SIMILARITY: Belongs to the arginase family."}
{"protein": "MQAILALDQGTTSSRAIVYDAHGGVLGTAQQDFPQYFPQPGWVEHDPGEIWQSQYRVMIQAVERAGIPWSAIAGLGLTNQRETTLLWDRATGEPLHRAIVWQDRRTARLCDDLRRDGHERLFRERTGLLLDPYFSGTKLRWLLDHVPGARRRAEAGELAFGTVDSWLIWQLTGGRLHLTDASNASRTLLCNIHSGDWDPDLLAALDIPAALLPEIIDSSGVCGTTCCAGVPEGIPIAGVAGDQQAALYGQGCHEAGLAKCTYGTGAFLLMHTGERPIASANRLLTTVAWRIGGRTAYALEGSVFIAGAVVQWLRDGLGLIRSSDEIEALARQVPDTGGVYLVPAFAGLGAPHWDPDARGILVGMTRGTERPHIARAALESMAFQATEVIGAMEVDAGLAVKELRVDGGASANDLLMQFQADLLGAPVLRPADTEATAAGAAALAARAVGLNGARPSAEAAFTAFSPRLSRYEVEQRMATWQRAVRRAGGWARDDD", "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": "MAVQGSQRRLLGSLNSTPTAIPQLGLAANQTGARCLEVSISDGLFLSLGLVSLVENALVVATIAKNRNLHSPMYCFICCLALSDLLVSGSNVLETAVILLLEAGALVARAAVLQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVVFSTLFIAYYDHVAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRPVHQGFGLKGAVTLTILLGIFFLCWGPFFLHLTLIVLCPEHPTCGCIFKNFNLFLALIICNAIIDPLIYAFHSQELRRTLKEVLTCSW", "text": "FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH (PubMed:1325670, PubMed:8463333, PubMed:1516719, PubMed:11442765, PubMed:11707265). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (PubMed:1325670, PubMed:11707265, PubMed:16463023, PubMed:19737927). Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes (PubMed:31097585). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MNALKRLGTTLAKNGDQIIEGTKELDQISVKYFLGNTRVSNNEKSLVSISSNKSRLNFNQLIKDNAHLIGKGSQYQRKVVKHYLSPLIGHKLRRQDIHNDYNKQLSHTDHIITPTDRKREAFSSMELAVDILPLLIKSTKKPVTKPAKRRLFKPYYTKEVPPIPDFKGDMKLFEDYIALLTHTKFLYKNSSSSNGIIPKILRVLIHPSNLNTIDLRSVQCYNDILYFYSKKYDFATCRELFAQMKVEGCKPNTTTYNILLLNLVKKVHMRKIRSIKNELLFYLRNMQKNGIFCDTVTWNTCYNFLNDEMSRDLYIEKLIDCGVPLTSELVYSVVRNSSKAHISTKTKYILDMFGEDGESFVNLKFVNLLISDLVLDHNVERAWSVLRYFELKQLKFVNQPKFLINSETMNTFLRYFAEQGRIDLCFLTYNYFVKDLVGPNKIRPNVNTFDMLMKSLVKNGYTETLPTVFEVICALSERYGIKIRNDGYWSLKCKAIIKFQYKSSSCEKNKTELLNKLNNFSWGKQLPLFTTKVWKNGNSEVRKICRMLGSIPIPLRKSRKLGDKETVDRSQNRSVSEKKKAYRNRIKYIAIGNAMARRIPYANNWHQSFKDEVTKRGLLASER", "text": "FUNCTION: Required for respiration. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side."}
{"protein": "MIKISIDAMGGDFGPEVVIPGAAKALERHPDIRFIFFGLPAQVEPVLARYPKLKAASEFRASQVAISMDDKPSQALRAGRGKSSMWQAIEAVKTGDAQACISAGNTGALMAMSKFCLRMMSDVERPAIAGIWPTLRGESIVLDVGATIGADARQLVDYAVMGAGMARALFEVRKPTVGLLNVGTEEVKGLDEIKEAGQILRDTPLDGLAYSGFVEGNDIGKGTVDVVVTEGFTGNIALKAAEGTARQMGELLRQAMRRTLLAKIGYVFAKGAFDRLREKMDPNKVNGGVFLGLSGIVIKSHGSANAEGFCSAVEVGYDMVRNRLLEKIEADLAHFHHSHPHVSNDGGEAAKA", "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": "MNGTEGLNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSVLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYIPLNLAVANLFMVFGGFTTTLYTSLHAYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGLALTWVMAMACAAPPLVGWSRYIPEGMQCSCGIDYYTSRQEVNNESFVIYMFVVHFTIPLVIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVVAFLICWVPYASVAFYIFTHQGSDFGPIFMTIPSFFAKSSSIYNPVIYIMMNKQLRNCMLTTLCCGRNPLGDDEASTTASKTETSQVAPA", "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": "MTATEQQQDDFSNVSWSEHVHDQQTRSVPDAEEPGHDMNAPGTGLERDAPSLGNEKLECTVDTPIKENDGTKDAFVSYLITTHSTFSSFQRSTTTVRRRFTDFVFLYKQLTRDYPAAAVPPLPDKQRMEYVRGDRFGSDFTTRRANSLQRFLSRLSLHPTLRRAPILHTFLESPDWNATMRSRGSRVSSASDPGSAGVFDNFADTFINAFTKLHRPDRRFLEVKEKSDKLDDDLGHIEKVIARVARREADLEVDLRDLAEQFQKLIPLEPHVEPAVHGFSASIEDTASHLRKLKDMTDQDYLGSLRDMQAYSIALKNLLKAREQKQLDYEQLTEYLNKSTTERDTLQSGHGGGSGAGSFLRAKIEDVRGVDHEQARRERTRKLELRVEELTHEVESARKTSDMFDDEVVKEVADFERIKRIEMKAQLGSLADSHIEFYGEVASIWEKYVEEMEKQGITSA", "text": "FUNCTION: Sorting nexin involved in the separation or division of vacuoles throughout the entire life cycle of the cells (By similarity). Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), mitophagy, and pexophagy (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence (PubMed:28894236). Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant (PubMed:28894236). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein Note=Endosome and other perivacuolar punctate structures (By similarity). Associates to phosphatidylinositol 3-phosphate, necessary for peripheral membrane localization to the perivacuolar punctate structures (By similarity). SIMILARITY: Belongs to the sorting nexin family."}
{"protein": "MIEFRQVSKSFHKKKQTIDALKDVSFTVNRNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDITNYSEKGMREIKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTVIQTEPSTSLIRRLNDEQVGGFKDYKIFVEETQVTQPIINDLIQICGREVKILFSSMSEIQGNTVCYMWLRFNIDQQFDDTAINQYFKEKNIQFEEVH", "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": "MQTTHLTETHFADLPINEQVVKALSAANFSHCTPIQALSLPPLLEGNDIAGQAQTGTGKTIAFLVATFHYLLSNPQPTKKQPRAIIMAPTRELAVQIFNDAELLSQHTGLSLGLIYGGEGYQSQREKLEEGVDIIIGTTGRIIDYYKQNIFSLAGIQVAVLDEADRMFDLGFIKDIRYLFNRMPKPTERLSMLFSATLSYRVQELAYEHMDNPTHVQVEPERKTGTRIKEELFYPSDEDKMALLLSLMEEEWPDKAIVFANTKHSCEKVADWLQADGHRVGLLSGDVPQNKRLKILEDFTSGKLDILVATDVAARGLHIPMVSHVFNYDLPDDAEDYVHRIGRTGRAGQSGSSISFACERYALNLPAIETYIEHAIPVTEYQADALLRDVTPPKPRHKKRMQNGRNPQKRQSSGSRNRRKP", "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": "MSQKGSVKKAVLAYSGGLDTSIIVRWLIEEYGCEVIAFAADVGQGKELDGIPEKARQTGASKCYVEDLREEFVRDFVFPMFRANAIYEGRYFLGTSIARPLISKKQMEIALAEEAEAVCHGATGKGNDQIRFELAYYHFNPEIKIIAPWREWDLNSRESLIAYANKHGIPVPVTKKRPWSSDRNLLHISFEGGVLEDPWAEPPEDMYLLSVSPEQAPDKPEYVEIEFRNGDPVSINGESLSPAQLLAHLNELGGKHGIGRADIMENRFVGMKSRGVYETPGGTILEEAHRGVEQITMDREVLNLRDSLIPRYATMVYNGFWFAPEREAMQAMIDETQKTVNGVARVKLYKGHCRVVGRKSETNSLFDPEVATFEADEVYNQADAEGFIRLNALRLRIRSAMQKKHG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
{"protein": "MATVMAATAAERAVLEEEFRWLLHDEVHAVLKQLQDILKEASLRFTLPGSGTEGPAKQENFILGSCGTDQVKGVLTLQGDALSQADVNLKMPRNNQLLHFTFREDKQWKLQQIQDARNHVSQAIYLLISRDESYQFKTGAEVLKLMDAVMLQLTRARNRLTTPATLTLPEIAASGLTRMFAPALPSDLLVNVYINLNKLCLTVYQLHALQPNSTKNFRPAGGAVLHSPGAMFEWGSQRLEVSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKISVFSSYWSYRPF", "text": "SUBCELLULAR LOCATION: Nucleus envelope Presynapse Cell projection, axon Perikaryon Cell projection, dendrite Cytoplasmic vesicle, secretory vesicle, synaptic vesicle Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. SIMILARITY: Belongs to the rogdi family."}
{"protein": "MNKRRAKGKSHSIRPARAGAPKWVRLTREEVEMLVEELAKRGYTPSMIGIILRDQYGIPLVKQIVGKKVTQILEERGLAPQIPEDLFNLIRKAVNVRRHINEYPRDKTAKKGLEEIESKIRRLTRYYKGIGKLPQEWVYDPAKAELLVAGAS", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MTVPENAQHTAPDQTQHTAPDRTRQAQQAAPDTAGRRLIELMAGFWKTQAIYLAAESGLVDAIAAAGRAPAVELANRTGTDPDALGRLLLFLESLDVVSGEDPAGYALTPVGELLRTGTQDSMRDHVRIYGSHFYRAWGALDHSLRTGRSAFTEVYGSDLFRYLNQHPDLSLTYERAMVAGTPFFAQVPEVHDFSGARLIVDVAGGHGALLHEILKSCPEPRAVLFDAPHVIAETADRPIASEHGDRVTLVPGDFFEGVPQGGDVYLLSRILHCFDDEACLRILAHCRSAMAPGGRLVVVERLLTRGTGSSLAQGYNMHMLVVLGGGRERDEDAYRTLLEKAGFQLDSVTTLPLETHLMAATLRR", "text": "FUNCTION: Part of a gene cluster involved in the biosynthesis of cremeomycin, a light-sensitive o-diazoquinone with antibacterial and antiproliferative effects (PubMed:26278892, PubMed:26689788). Catalyzes the methylation of the C4 hydroxyl group of 3-amino-2,4- dihydroxybenzoate (3,2,4-ADHBA) to form 3-amino-2-hydroxy-4- methoxybenzoate (3,2,4-AHMBA) (PubMed:26278892). In vitro, can also catalyze the methylation of 3-amino-4-hydroxybenzoate (3,4-AHBA) (PubMed:26278892, PubMed:26689788). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MKFSLKDLFGLVVSFGLIFLALTIGSGIQHWTGTSVPGSVIGMLVLFVSMAIGLVKVEWVKPGASLLIRYMILLFVPISVGLMEHFDMLIANALPIIASAIGGSLIVLVSLGWLLQRILGKEA", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0299 family."}
{"protein": "MLNTLMTHLINPLAYIVPVLLAVAFLTLIERKVLGYMQLRKGPNVVGPYGLLQPIADGVKLFIKEPVRPSTSSPFLFLAAPVLALTLAMTLWAPMPMPHPVTDLNLGILFILALSSLAVYSILGSGWASNSKYALIGALRAVAQTISYEVSLGLILLSVIIFSGGYTLQTFNTTQESIWLLIPAWPLAAMWYISTLAETNRAPFDLTEGESELVSGFNVEYAGGPFALFFLAEYANILLMNTLSAVLFLGASHIPNMPELTTINLMTKAALLSILFLWVRASYPRFRYDQLMHLVWKNFLPLTLAFVLWHTALPIALAGLPPQL", "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": "MSQLVQFIDGQWLAGAGKPFESKDPAKNQVIWQGEAASAAQVEAAVKAARHAFYHWSDLALDYRLAIVRRYADLLGEHKEALALTIARETGKPLWETRTEVAAMQGKIAISIRAHDERTGTVENPMPGAKAFVRHKPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELTPMVAEAMLKIWQEAGLPKGVLNLVQGEVDTGKALAGNPDIDGLFFTGSSRTGHFLHQQFAGQPGKILALEMGGNNPLIVKDVSDIDGAVHAIVQSAFITSGQRCTCSRRLFVERSVQGDALVKRLVEVVGQIKVGLYDAAEQPFMGAMISEKAALGMVEAQANLQRLGGESLLTLTHLEAGTGFVSPGIIDVTAVSALPDEEYFGPLLQLIRYDDFDAAIDQGNATSFGLSAGLLGDSEADWQHFFKRIRAGIVNWNKPITGASSAAPFGGIGASGNHRASAYYAADYCAYPVASVEDSKAAMPDQLSPGLTF", "text": "FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD subfamily."}
{"protein": "MIEQQTGSRIRVEALAVAGQEQAEHWAQRLGLPLHDAEADFALQSTDDGLQLQQLGDDAPGAVRVDFVEGAVAHRRLFGGGTGQMIAKAVGIQPGVRPSVLDATAGLGKDAFVLASLGCELSLIERQPIIAALLEDGLARGRDDRDVGSIVARMHLLTGNSIEIIRGWTAEPPQVIYLDPMFPHREKNALVKKEMRLFRPLVGDDMDAPALLEAALALATHRVVVKRPRKAPCIDGPKPGYALDGKSSRYDIYPKKALKPKAVTDDSGA", "text": "FUNCTION: Specifically methylates the guanosine in position 1516 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family."}
{"protein": "QHWSLCHAPG", "text": "FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the GnRH family."}
{"protein": "MTKTLPKDFIFGGATAAYQAEGATHTDGKGPVAWDKYLEDNYWYTAEPASDFYNRYPVDLKLSEEFGVNGIRISIAWSRIFPTGKGEVNPKGVEYYHNLFAECHKRHVEPFVTLHHFDTPEALHSDGDFLNRENIEHFVNYAEFCFKEFSEVNYWTTFNEIGPIGDGQYLVGKFPPGIQYDLAKVFQSHHNMMVSHARAVKLFKDSGYSGEIGVVHALPTKYPFDANNPDDVRAAELEDIIHNKFILDATYLGKYSDKTMEGVNHILEVNGGELDLREEDFAALDAAKDLNDFLGINYYMSDWMQAFDGETEIIHNGKGEKGSSKYQIKGVGRRKAPVDVPKTDWDWIIFPQGLYDQIMRVKADYPNYKKIYITENGLGYKDEFVDNTVYDDGRIDYVKKHLEVISDAISDGVNVKGYFMWSLMDVFSWSNGYEKRYGLFYVDFETQERYPKKSAYWYKKVAETQVIE", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MFMSTDEVRRAFLSFFESKGHQIVESSSLVPANDPTLLFTNAGMNQFKDCFLGLEKRAYTRATTAQRCVRAGGKHNDLENVGFTARHHTFFEMLGNFSFGDYFKEDAIQYAWEFLTDVLQLPKERLLVTVYETDDEAFDIWNKKVGIPADRIIRIGDKKGGKKFDSDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRFIEIWNNVFMQFNRHADGTMEPLPKPSVDTGMGIERISAIMQGVHSNYEIDVFQTLIKAAADAIGYQDLTNQSLRVVADHIRSCAFLIVDGVMPSNEGRGYVLRRIIRRAVRHGNKLGAQGAFFHKLVGPLAEVMGTAGVELKKQQALVEKVLRIEEENFGRTLDRGMSILNDALDQLSGQVLDGETVFKLYDTYGFPADLTNDVARERGFSIDEAGFEQAMEEQRQRAREAGQFGTDYNSLIKSATNTEFCGYTASRGQSVVREMFVEGAEVSTLSAGDKAIIVLDNTPFYAESGGQCGDTGVLKTDAGIFHVEDTQKLGNAIAHHGVLAQGVLATGDQVDAIVDEKRRAAISLNHSATHLLHAALRKVLGEHVAQKGSLVRAETLRFDFSHLEAMTAAEIKEVERLVNQEVRRNHSIETNIMNIDEAKAKGAMALFGEKYDDQVRVLSMGDFSTELCGGIHASNTGDIGLFKIISEGGIAAGIRRIEAVTGEGALDYLDAQQAQHDAKVSEMAAKAKLLEKEIQQLKDKLAAKESAGLINQVKQIAGVNVLVAQLNGADNKALRGMVDDLKNQLSSGIIMLGNVAEGKVGLIAGVTNDLTNKVKAGELVNMVALQVGGKGGGRPDMAQAGGTDAHALPSALESVDAWIAERL", "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": "MAGKGVGSRLSTLFLLVLLVITIGMMQVQVAEGRMCKTPSGKFKGYCVNNTNCKNVCRTEGFPTGSCDFHVAGRKCYCYKPCP", "text": "FUNCTION: Plant defense peptide. Has antifungal activity against B.cinera, F.oxysporum, F.solani and H.annosum with IC(50) values of 0.4 ug/ml, 2.9 ug/ml, 0.9 ug/ml and 1.4 ug/ml, respectively. Has modest antifungal activity against C.albicans and T.reesei. Causes thickening of F.oxysporum hyphae and an increase in their branching. Lacks antibacterial activity against the Gram-negative bacteria E.coli and E.carotovora. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MGIARILSAVLFLSVLFVVTFPALLSADHHDGRIDTCRLPSDRGRCKASFERWYFNGRTCAKFIYGGCGGNGNKFPTQEACMKRCGKA", "text": "FUNCTION: Serine protease inhibitor that inhibits trypsin and blocks voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family. 02 (native) subfamily."}
{"protein": "MPEYRSKTSTHGRNMAGARALWRATGVMETDFGKPIIAVANSFTQFVPGHVHLHNMGQLVAREIEKAGAIAKEFNTIAIDDGIAMGHSGMLYSLPSRDLIADSIEYMVNAHCADALVCISNCDKITPGMLIAAMRLNIPTIFVSGGPMEAGKVIGVANIQPERRLDLIDAMIESADDNVSNRQVEEVEQNACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSYLATHVGRKELFLEAGRMIVEITKRYYEQNDETVLPRSIATKKAFENAMTMDIAMGGSTNTILHLLAVANEAGVDFKMADIDRLSRVVPCICKTAPNNHDYYMEDVHRAGGIFAILKELDKAGKLHTDVHTIHAPTLKDAIEKWDITNPENTRAIERFKAAPGGVRTTQAFSQNRMWKTLDLDREKGCIRDVAHAYSQDGGLAVLFGNIAERGCVVKTAGVDESILKFTGRARVFESQEDAVEGILGNQIVAGDIVIIRYEGPKGGPGMQEMLYPTSYLKSKGLGKACALLTDGRFSGGTSGLSIGHASPEAAEGGAIGLVHEGDTVEIDIPNRSIHLAISDEELAARRAEMEARGSKAWKPENRDRYVSAALRAYGAMATSADKGAVRDVAQIER", "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": "MTDTLPTVSRRGLMLVMSSPSGAGKTTISRALLERDPAIGMSVSATTRAPRPGEVDGKDYHFVTVEKFHEMVEKREFLEHARVFDNFYGTPRGPVDEILRSGRDVLFDIDWQGTQQMAQNARADLVSVFVLPPSVEELERRLRGRAQDSDEVVRKRMAKAGDEMSHWPEYDYIVVNIDLDKSIAAVQAILAAERLKRERQVGLPDFVTQLRGGE", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family."}
{"protein": "MSRTYKATGINLKSMPFGEADRLLTILTREQGLVRAVAPGCRKPKSKLGGRSALFVVNDLMLVQGRSLDKIAQAETLESYPGLSQNLAKLTTSQYLAELTLYQALSGQPQTELWDLFCQQLTQLQNATLAQVPCCLIHGTLKLLAGAGIAPQVHACCVTHQPLDPPTSNPTWRVGFSAGAGGTVTLTGPPRPRTAIQQAAEQAIAYPLGADYRVQGKLSAQELALLQDLNPAEIQPASPLPLPLIATYPLVIWQGVESALRHYAEAYFDRPIRSAALIDTCFTPLPDLTSVPS", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family."}
{"protein": "MADKFDANDETRTVYAVVYDNDQPVSTGQFLAETKIEARLTRIVTLADYCGCGYGAKVTEALETYTRREGFYQLTIHSELTAQTFYENLGYQTYGPKCLEDGEYCQSLAKTILKWEKNMDIAMLIAIVGGLLGCYLYLTKNN", "text": "SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MPELPEVETVRKGLNQLTLNQEITGGDVLLNRTIAYPFSVGEFVDGIEKNAIATWHRRGKYLLAELSSPCSTSWLGVHLRMTGQLLWLHRDEPLHKHTRVRLFFGDQQELRFVDQRTFGKIWWVPPGVAVESIITGLAKLAADPFSPEFSVEYLASKLKNRRRPIKTALLDQSVVAGLGNIYADEALFKSGILPETLCIDLQLKQIELLRTAIIQVLETSIEAGGTTFSNFLNVKGTNGNYGGVAWVYNRAGEPCRVCGMPIQRIRLAGRSSHFCSECQTLRGVENRERRD", "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": "MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQEALKESGLTAKDIDAVAYTAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGATADLGVSVRPRWPLAELPAA", "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": "MGPVSVLPKPQSISTWEGDLAKMTHLQAGLSPDTIEKARLELNENPDVLHQDIQQVRDMIITRPDIGFLRTDDAFILRFLRARKFHQADAFRLLAQYFQYRQLNLDMFKNFKADDPGIKRALIDGFPGVLENRDHYGRKILLLFAANWDQSRNSFTDILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASKLTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLIKPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGTLPPYDMGTWARTLLGPDYSDENDYTHTSYNAMYVKHTCSNLERECSPKPMKRSQSVVEAGTLKHEEKGENENTQPLLALD", "text": "FUNCTION: Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Early endosome membrane; Peripheral membrane protein Cytoplasmic vesicle, clathrin-coated vesicle."}
{"protein": "MAKLTPMMEQYIQIKNEYKDAFLFYRLGDFYELFYEDATRAAQELEITLTKRAGGKGDPIPMCGVPYHSAENYIKTLIDRGYKVAICEQVEDPKTAKGVVKREVVQMITPGTVMESTMLTDGENNYIGSLSHFQDGSYVIVYNDLSTGENRLAFINDGWDAVIHEFYNQPIKEIVISSNLPEELQIQLKERLNVTLSYQDEVTFNAEFRELSENLNDERLMKAFSRLLNYIQTTQKRSLHHLQKAEVIELKKYMSLDMYSKRNLELTETIMKKSKHGSLLWVLDKTVTAMGARTLKKWLERPLLSKQKINERLEVVQGFYDGFMERESLRDLLKSVYDLERLSGRIAFGNVNARDLIQLKQSLSRIPAIQETLRQFDQPEITRLAEMLIYPEQMVESLEKSIVDEPPISIKEGSLIKEGYHDQLDTYRDASRNGKKWIAQLEHQEREETGIRSLKVGYNRVFGYYIEITKPNLHLLPEGRYERRQTLTNAERFVNEELKEKEKLILEAEEKSVELEYDLFIQIRDQIKEEIPLIQQLAHIISQMDVLQSFATVSESNNYVRPDFNDEQLQVTKGRHPVVEQVMKDGTFVPNDVVFDKSQNMLLITGPNMSGKSTYMRQVALTSIMGQIGCFIPAEQATLCVFDQIFTRIGAADDLVSGQSTFMVEMLEARHAISNATDRSLILLDEIGRGTSTYDGMALAQAIVEYIHHNIAAKTLFSTHYHELTALEDSLHHLKNIHVRAEEHEGNVVFLHQIKEGAADQSYGIHVAKLADLPNELIERASVILEELEDDSNKKPTPTKDKLESGQLSFFIEESNKKKAEMPKQEKTHNNQEQSVIEDLKNVNVLDLTPLEAMNELYRLQKGLKQY", "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": "MEQESELLSLNTLARILTLYFSSEKGTKITPSALELITQYLRIYSKEAVCRAYEEKKNSIMSSSENEDIVLELEDLENGIAAQLALDFS", "text": "FUNCTION: Component of a FANCM-MHF complex that promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (Probable). FANCM-MHF promotes non-crossover recombination (PubMed:22723423). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CENP-X/MHF2 family."}
{"protein": "MITEDEVNKLLSENEALFRFMGAKFEKIERGVAKLSFEYKEELSRIGGMLHGAIIFAAMDYSGSYAVRTLDVKEAYTLEFNVIFLKAMKTPPFTFLARVVRETKRYAYVEVEGFDGNNELCAKGNGIWHLIRD", "text": "SIMILARITY: Belongs to the thioesterase PaaI family."}
{"protein": "MKNPTLLPKLTAPVERPAVTSSDLKQASSVDAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAADGAE", "text": "FUNCTION: Both kawaguchipeptin A and B, which only differ by post- translational modifications, have antibacterial activities, since they inhibit the growth of the Gram-positive bacterium S.aureus at a concentration of 1 ug/mL."}
{"protein": "MNKYLEYPEVESKETPPQKLVVLLHGIGSDGHDLIGLVPYIKNDLQNCHFISPHGIEDYDMMPYGRQWFSLRDRSPHIIATLIANNISKLEDIIREKQTELNLTNKDTVIIGFSQGTMIGLYLTLVQQAPFFCTIGFAGALIPPMKINNKLTPICLIHGALDQVIDVSEMYNASNYLSKLNIEHSVHKLTSLAHSIDGRGLEIAINFINTCHNMV", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2 family."}
{"protein": "MDAVAFEDVAVNFTQEEWALLGPSQKNLYRYVMQETIRNLDCIRMIWEEQNTEDQYKNPRRNLRCHMVERFSESKDSSQCGETFSLIRDSIVNNSICPGEDPCQSAECEEVIMGHLSLNSHIRVDSGHKPHEYQEYGEKPHTHKQRGKAFSYHHSFQSRGRPHTGKKRYECKECGKTFSSRRNLRRHMVVQGGNRPYKCKLCGKAFFWPSLLRMHERTHTGEKPYECKQCSKAFPFYSSYRRHERMHTGEKPYECKQCSKALPDSSSYIRHERTHTGEKPYTCKQCGKAFSVSSSLRRHETTHSAEKPYECKQCGKTFHHLGSFQIHMKRHTGDRPHKCKICGKGFDRPSLVRYHERIHTGEKPYECKQCGKTLSHSSSFRRHMIMHTGGGPHKCKICGKAFVYPSVCQRHEKSHSGEKPYECKQCGKALSHSSSFRRHMVMHTGDGPNKCKVCGKAFVYPSVCQRHEKTHWRETI", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MAVFKVLTPADIVAFSTGLIAGVDEVGRGPLVGDVVTAAVILDPNQPISGLNDSKKLSEKRREALFDEICEKALCYHIGRASPAEIDELNILHATMLAMQRAVAGLNLAPKLVLVDGNRSPFFSHNSQSIVSHSIIKGDGLIASISAASIIAKVTRDREMDALDAAYPQYGFAKHKGYPTKAHFEAIAEHGVFDQYRKSFKPVKALLEG", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MGLSRTMTAIQLNSSIPLGLPVPPHTPHAISVSLPTWSETVAYKEGIKHINDALLNGYPRMFIQLNVRKLSSLLEQKFGINGERCMLFPTYKVAEQCQLFMQARSVGARIVGLLICPEGKQNNRVIECKEPANLSESTSSASTNLYVVLFPPDMFSIANQFWQHSGQGISSRLTDHCLSILTENAAHANGSSLSPLTFPGNSHVAPEQLEVGHDVDLEGRCGGPLLADAAIAKQVLRQRIAGLLIRYGSCDYRAELCVGKKNLEGNQNSRDFADVTENDVYLFPTGMTAIWNAHQLALAVRPTAKSVCFGFPYSDTLKVLQKWGPGCHFFAGGTDSEIDELEIILEQEFARDSTKPPVLALFTEFPSNPLLCSPNLLRLRALADKYDFLLAIDETIGNFVNVEVLPYADILLTSLSKIFSGNANVMGGSLVLNPNGRHYTALKAHIAAHYQDIYYPEDAIHMEWNSRDFEQRIKIIDDNAEAICDFLRPHSVAAGATNAVIKEVFYPKYITPENYERCLTKGTNHDLSSSPSNGGGGYGGLFSLTFTSGAASAAFYDALSCFKGPSLGTNFTLACTYTLLAHFKELEWAAQYGVEAGLVRISVGTENTEALLRTIEAALGAAKEAKGL", "text": "FUNCTION: Cystathionine gamma-synthase-like enzyme; part of the gene cluster that mediates the biosynthesis of the psychoactive metabolites ibotenic acid and muscimol (PubMed:32233056). The first committed step is glutamate hydroxylation by the 2-oxoglutarate-dependent dioxygenase iboH, and the last step is decarboxylation of ibotenic acid to muscimol by the decarboxylase iboD (PubMed:32233056). The order of the intermediate reactions is somewhat ambiguous (Probable). IboA likely activates the carboxylic acid at position 5 to introduce an amide bond, and the flavin monooxygenase iboF generates the N-O bond (Probable). There are several options for the latter step (Probable). One option is that iboF directly hydroxylates the amide nitrogen formed by iboA to produce a hydroxamic acid species (Probable). Another option is that iboF hydroxylates an external N-containing compound, whose resulting N- O bond is subsequently introduced into the hydroxyglutamate scaffold (Probable). The paralogous PLP-dependent cystathionine gamma-synthase- like enzymes iboG1 and iboG2 are likely involved in substitution of the OH group at position 3 by the O-N moiety (Probable). The first cyclic intermediate is most probably tricholomic acid which is likely desaturated to ibotenic acid by the cytochrome P450 monooxygenase iboC (Probable). SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
{"protein": "MIRALFAAAKKIVIKIGSNTLAQADGTPDEEFLAECARACAALMRDGKQIVVVSSGAQVAGISALHCLSSPPQGAGLERHESRGVIPGDGASCKQALCAVGQAELISRWRSAFAAHQQCVGQFLCTKEDFTDSDRAAQVRYTLSFLLERRVVPILNENDALCCSDVPSVPADRRVSLSPQKRIGDNDSLSAFVALLWQADLLLLLSDIDGVYDKDPKAHTDAQHVPLVTDVSALVGKTSMGSSNVFGTGGIATKLDAARLVTRAGIPLVLANGRHLDPILSLMRGDARGTLFVPVS", "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": "MEYFNVGKIVNTQGLQGEMRVLSVSDFAEERFKKGSQLALFDDKDRFVQEVTIVSHRKQKHFDIIKFKDMYHINAIEKYKGYTLKVSKDNQGDLQEGEFYYHQIIGMAVYEKDVLIGHVKEILQPGANDVWIVKRQGKRDLLLPYIPPVVLNVDVPNKRVDVELMEGLDDED", "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": "MFRGKKYQEAAKLVDKTKLYDPEEAIELALKTSYAKFDETVEVHVRLNVDPRHADQQVRGTVVLPNGTGKSVRVLVFAKGDKAKEAEEAGADYVGAEELVAKIQNEGWTDFDVCIATPDMMGLVGRLGKILGPKGLMPNPKSGTVTMDVAKAVKEAKAGRVEFRLDKTAIIHCPIGKVSFGKEKLLENYRTLIEAIIKARPAAAKGQFIKSITVATTMGPGIKINPLKPL", "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": "MLTYLEQKINYEFKDKTLLLEALTHSSWAHEGKNEKVSNERLEFLGDSVLSLVISEYLYKNRKDLEEGSLSKYRAEIVCEPSLARCARKIELGSFLRMGKGEEISGGRDRDSILADAMEALLAAVYLDGGLEAVRRVILDLFKEIIDEVLKGIIYRDYKTRLQEVVQSMEVGKITYELVEEIGPDHNKTFVTQVKIGDVVLGIGQGKSKKESEQAAAMEALSKLGILK", "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": "MEFWSELQSYQSLRRLLELASARTSSCWRFIFGSTLTNVIYRAKEDYSSRFAELLSFNPGIFASLNLGHHSFFQEIVIKNLDFSSPGRTVSGLAFICFILDQWSAQTHLSEGYTLDYMTMALWRTLLRRKRVLGCSPAQPPHGLDPVREEEEEEEEEENLRAGLDPQTEL", "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": "MPETEHETCSKEWLQSQLRSLDSKDLILLDCRGSHEYSESHIRGAVNLCIPSIVLRRLAVGKIDLASTIKSPELKQRIQSGYKLCWFILYNGEGVPGQNQEIAGAGSLAVAMDSIISILHRRLKQDGCRVVALQDGFNNFRQAFPEWCEDDNQTHSKEIESSRNVQTDQLMGLRSLRISTTQSDSACSSSAESSDCESSSHHHHHHSHHNYNEAPVEIIPGLLFLGNATHSCDSEALKKYNIKYVLNVTPDLPNKFKESGDIKYLQIPITDHYSQDLAIHFPDAIQFIEEARSASSVVLVHCLAGVSRSVTVTLAYLMHTRGLSLNDAFAMVRDRKPDVSPNFHFMQQLLSFESQLRLRPGSRFSCSCIAPDCNCMQTTGFMATHLANATGVSPDSGIEFDRWTPSDTGLK", "text": "FUNCTION: Negatively regulates the activity of members of the MAP kinase family in response to changes in the cellular environment. Has a specificity for the ERK family. Acts as negative regulator in a variety of developmental processes including cell differentiation and proliferation controlled by the Ras/ERK pathway. Suppresses the photoreceptor cell differentiation and wing vein formation. Required for proper oogenesis and early embryogenesis. Functions autonomously in a subset of photoreceptor progenitor cells in eye imaginal disks. Appears also to be required in surrounding non-neuronal cells for ommatidial patterning and photoreceptor differentiation. Plays a role in the maintenance of epithelial integrity during tracheal development. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MKYNQYSYIGTSVSQAEKELKELGFQISSQKTNKANLATFVSQVYFHNPDKDDVFKSIIADSQTDLATFLHSDRELTEEIFYTIALQLLEFTPYIDFDEAKTFIKHSHFPIIFQPKHFLLNFYQLLGTRTKNGMTLIDKLVSQGFLPADNHYRYFNGKSLATFDTNALIREIVYVEAPLDTDKDGQLDLIKVNIIRPQTKAKLPVVMTASPYHQGTNDKGADKKLHQMEGELTVKKAATITVTDSHFQALQVPSSNLPISPAQESFSYIDSYTLNDYFLARGFANIYVSGVGTKDSDGFMTSGDYAQIESFKAVIDWLNGRTTAYTSHKRDKRVMADWTNGLVATTGKSYLGTMSTGLATTGIKELKVIIAESAISSWYDYYRENGLVCSPGGYPGEDIDVLTELTYSRNLAAGDYLRNNAQYQKMLAEQVKQIDRTSGDYNQFWQDRNYLPHAHKIKAHVVYTHGLQDWNVKPNQVYYIFNALPEEIQKHIFLHQGQHVYMHNWQSIDFRESMNALLSEELLGLQNHFQLPTIIWQDNSQVQTWKKLNNFGSHQTRQFSLGQEKKIIDNHYPSSDFKLYSDDYHAFKHDLFLKKANEIAIDLPIQEDMLVNGQIKLNLTLKSSSNKGLLSAQVLDYGQKKRFSDLPTILEHNSIDNGQNFSREALRELPFKKAPYRIITKGVLNLQNRTDLLTIEDIFPNKWMTITFNLQASLYQLQKGDSLRIVLYTTDFEQTVRDNSNYILVVDLAKSTIEIPIA", "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": "MGQKVNPIGLRIGITRGWDSIWFSQSDYKKNLHEDIKIRKFIQSRFSNAGVVKVVIERFPEKINVNLHTAKPGIVIGQKGSNIEAVKKILKTMTEKPVNLNIIEVKKPETVAQCIAESIALQIEQRQPFRRVMKQELRRAMRGGVEGIKILISGRLNGADMARRENYKEGRIPLHTLRAKIDLGFKEAKTTFGQIGVKVWTYSGDFIQSKEESEEDKYAVKRRTS", "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": "MQAFVQFLGSNPYILLFLTIGLAVWVGKFSIKGYGLGAVAAAIVVGCLVATVGAAYGVKFHLDEFAKSLLYYLFMYGVGLRVGPSFVNALNKESINYAILAIIAPILGLAIVVLGTQFFGLPLGAAGGMLAGSQTMSAAIGSAEQAVSAGVLSLGSESPEQISAMIALSYGITYIWGTVGIILLCKYLPRIWGVDAKAAALEFEKAHGVPNVDDAGLTAFHPFDLRAYRVENPESIGKTVQQFRTRFPQYQVVNVERGDQLLGPSAETVLQQGDVVALGGRLEEMTANMGMLGPEVPDARALNIPLDQAEILVTNKEVTGRPLKTFRGSELAGQIQLQRVERSGVPLPIGLETTLQKRDVLFVTGLQPAVSKAGEIFGVIARHSSATDLLTLSFGMILGFLIGLIEVPAFGAKVGLGNAGGLLLSGIIVSSISSRLRFFGNTPNAARNILEDLGLIGFVAIVGINAGADLLTQLTGAIALKIFIVGFLASTIPPIIVWAIGFHIMKINPALLMGATAGARSHSGPAREAAKEVGSSVPWLGFPVGYAVSGVLLTVFGYFAMVLAH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family."}
{"protein": "MTTPRNSVNGTFPAEPMKGPIAMQSGPKPLFRRMSSLVGPTQSFFMRESKTLGAVQIMNGLFHIALGGLLMIPAGIYAPICVTVWYPLWGGIMYIISGSLLAATEKNSRKCLVKGKMIMNSLSLFAAISGMILSIMDILNIKISHFLKMESLNFIRAHTPYINIYNCEPANPSEKNSPSTQYCYSIQSLFLGILSVMLIFAFFQELVIAGIVENEWKRTCSRPKSNIVLLSAEEKKEQTIEIKEEVVGLTETSSQPKNEEDIEIIPIQEEEEEETETNFPEPPQDQESSPIENDSSP", "text": "FUNCTION: B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes (PubMed:3925015, PubMed:7684739, PubMed:12920111). Functions as a store-operated calcium (SOC) channel component promoting calcium influx after activation by the B-cell receptor/BCR (PubMed:7684739, PubMed:12920111, PubMed:18474602). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell membrane; Lipid-anchor Note=Constitutively associated with membrane rafts. SIMILARITY: Belongs to the MS4A family."}
{"protein": "MEIDLNADLGEGCGSDEALLDLVTSANIACGWHAGGAQAMRDCVRWAVEKGVSIGAHPSFHDPENFGRKEMDLPASEIYAGVLYQLGALSAIAQAEGGRIAHVKPHGALYNQAAREPEIADAVVSAIHDFDPSLAVFGLAKSGFVDAAQQAGLVAVEEVFADRGYRADGSLVPRSQPGALVDDENEMLARTLEMVRGQRVRAVTGEWVPLNAQTVCLHGDGPHALAFAKRIRDALEAAGIDVHAPGALHAGERA", "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": "MATLEQRLTELLDAPIVALGYELWGIEFIRAGKHSTLRVYIDHANGISVDDCAEASHQVSALLDVEDPITTEYYLEVSSPGMDRPLLKPEHFARYIGQVATVTLRMAVNNRRKYKGTIKQVDGEMITLTIDGRDEILAFANIQQANLIPNFD", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MKLNTIQRKKFRVTGKLKKVASSDRLRLSISRSAKNISAQIIDDVKNITLVSCSSVEKDIRSMDKVNKTEISKIVAEKLAKKAQEKKISKIFFDRGIYKYHGRVKVFAETLRKNGMEF", "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": "MELELLFQNVVNSFAFYNNQVAVAVSGGVDSIVLLHLMTNWAKKNKLSLPTALTVNHGLRPESQKEADFVVSYAKELGAKESFILNWEKQNIKGNIQLQARKARYKLLAEWCKNNNVKYLLVAHHKDDQAETFLLRLERGSGVDGLSSMDYKSFLNGIYIFRPLLNFSRSEIEKYAKLHRLKWIEDRSNYDLKYRRTLYRNLLKASDNQEILTERICLTALHMKRAAKALMHYTRLAFNDCVNVHDLGYIEIKLSEFYQLPEEIALRLLLYSIMAIASKHYKPRYNSLIVIFNKILQKDSNVNCTLSGCKIRKHGENILIIRESSKIQEITLNLPLNEPTQWDNRFSCTILGNQECSVIIAPLKKTQKVPEFLKDYNCCPEVFYSLPVVLKDGKVLAYPDVNYNGKNTNDDKVQCIINSTIKQNLVSLISI", "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": "MNPPILERDPSDPQKEKKEGVNPVLKLVLELGPLLVFFFANARGEWLVQKFPVLGEFGGPIFVATGLFMAATAIALIASWLLTRTLPIMPMVSGVVVFIFGALTLYLQDDIFIKMKPTIVNTLFGGVLLGGLYFGRSLLGYVFDSAFRLDAEGWRKLTFRWGLFFLFLAVVNEVVWRNFSTDAWVTFKVWGIMPITLLFTFSQMPLILRHSLDDKASGEEKAGK", "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": "MNSLFASTARGLEELLKSELEALGAHACKVVQGGVHFQGDDRLLYQSLLWSRLASRILLPLNEFRVHSDLDLYLGVQAIDWTSIFGVDKTFAVHFSGVNEEIRNSQYGALKVKDAIVDSFTRKIEQRPTVAKQQPDIRVNVFLQRDMASVALDLSGEGLHQRGYRDLTGQAPLKESLAAAIVQRSGWQPGTPMLDPMCGSGTLLIEAAMIASDRAPGLHRQHWGFTAWNGHNVDLWREVITEAQVRARRGLQETTSRFFGSDIDRRVIEMARGNARRAGVAELITFNVNDVAKLTNPLPEGPTGTVVCNPPYGERLESEPALIALHNMLGRIMKSAFGGWQLSLFSASPELLSCLQLRAERQFKAKNGPLDCVQKNYQLAENPLGAGGVQVAEDFANRLRKNLKKLDKWAKQQGIECYRLYDADLPEYNVAVDRYGSKVVVQEYAPPKTIDAQKARQRLFDVINATLAVLELPSNQLILKTRERQKGKNQYEKLAQKGEFLLVEEFNAKLWVNLTDYLDTGLFLDHRIARRMLGEMSKGKDFLNLFAYTGTASVHAGLGGARSTTTVDMSRTYLEWAEKNLRVNGLTGKQHRLIHADCLSWMQNADEQFDVIFIDPPTFSNSKRMENTFDVQRDHLALMQDLKRLLRRNGTIMFSNNKRGFQMDMAGLSALGLEAKEITAQTQSQDFARNRQIHNCWLLTHAGEGK", "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": "MADKEAKKVPSVPESLLKRRQAYAAAKAKRLKRLLAQKKFRKAQRKIIYERAKAYHKEYRHMYRQEIRMARMARKAGNYYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVHDLIYKRGYGKINKKRIALTDNSLIRKRLGKLGIICMEDVIHEIYTVGKNFKVVNNFLWPFKLSSPRGGMKKKTIHFVEGGDAGNREDQINRLIRRMN", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MTKESIPNELLNLLNEEEIIMFRELQIKIQELNYKTNLTRLIEGDDYWISQVYDSLWTFKENTNKNFDNKKFIDIGSGCGFPGFAYAITHPNSEIYLVDSSKKKTDSLKEIIKSIKFKNDIFVINDRIENIGRQSSFKNGFNIATARAVSNPSTVSEYILPMLKSNGLGILYCGKWTNEDNKNLEKTLNVLEGQILEIKSNFLPREKGMRNVIFIEPKASCPDIYPRSIGKAEKYPLKG", "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": "MSWNNIGVVEMTPILFQFLLSSLCVFLLFVFIRFLNDIWWTPIRLQRVFRQQGIRGPSYGFLYGNTKEILNMRKESMSRPMDYLSHNIFPRLQPHLYSWLNIYGKNFLNWYGPRAQFVVTQVDFVKETMIKDQAYPKMDPEWFAKKLLGDGIVTSKGKKWAKHRRLANHAFHAESLKSMTPAMIASVEMMLKRWKQHEGREIDVFQEFKILTSEVISRTAFGSSYLDGKDIFDRLTQLGIIITRNSYKVKLPGISLFYKSNDEIEAEKLDQGLYDSILRIMEKREKESTMSGEVGSFGTDFLGLLMKAMNDADEKNRITAQDVVDECKTFYVAGQETTTTLLAWVIFLLGIHTDWQEKARQEVLNLFGQEIPNSDGLAKLKTVNMIINETLRLYPPVIFLTRKVKEETKFGKLTLPANVHIVVPTLALHHDEQIWGDDALLFKPERFSQGVAKATNNNAAAFFPFGLGPRSCVGLNFATNEAKIALAMILQCYSFALSPTYIHSPVQILTVRPQHGLQVMLQPL", "text": "FUNCTION: Probable heme-thiolate monooxygenase. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MAHKKAGGSTKNGRDSESKRLGVKRFGGESVLAGNILVRQRGTKFHAGANVGIGKDHTLFATSEGKVSFDVKGSKNRKFVSVITD", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MANQISQHLQVALVAGETSGDLLAGLLLDGLREQWPLMTAVGIGGPQMARRGLVAWWGHDKLSVHGFGWEVLRRYREIVGIRRQLKTRLLRQQPDVFIGVDAPDFNLDLEQDLKAQGIKTVHFVSPSIWAWRPERVEKIRRSVDHVLCIFPFEPALLARHGIAATYVGHPLANVIPMEPDRSAARAALGLADGDQVVAILPGSRQSEINHLALRFFQAAALINKAHPAIKFIVPAIPALRAGIEHAARASGMQAHLQIIAGQSHTVLAACDVTLIASGTATLEAALFKRPMVIAYRMGWLSWQIMRRKQLQPWVGLPNILCQDFVVPELLQDAATAQALADAVLLWIDAKASHPAKIAALQQKFTALHTELQRDTPRLAAHAIQQVLQG", "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": "MIALPRNRRPLFLAVFAYCAALLAFGLYLQHYQGIEPCPMCIMQRYAFALVGVIALVAGLHGPRGAGVRVYGGLLLLTALAGGSVAARQTWMQLYPPEIPECGPGLEYMLESFPLTSALPMIFRGAGDCSAIDWTFLGLSLANWSLLNFGAAALLALWLLFGRRVR", "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": "MTTIAFLGLGNMGAPMSANLVGAGHVVRGFDPAPTAASGAAAHGVAVFRSAPEAVAEADVVITMLPTGEVVRRCYTDVLAAARPATLFIDSSTISVTDAREVHALAESHGMLQLDAPVSGGVKGAAAATLAFMVGGDESTLRRARPVLEPMAGKIIHCGAAGAGQAAKVCNNMVLAVQQIAIAEAFVLAEKLGLSAQSLFDVITGATGNCWAVHTNCPVPGPVPTSPANNDFKPGFSTALMNKDLGLAMDAVAATGATAPLGSHAADIYAKFAADHADLDFSAVIHTLRARADA", "text": "SIMILARITY: Belongs to the HIBADH-related family."}
{"protein": "MNHLANNYGYYPQDCRTQYSRMNSAEAELTSLPVHVSLQDRELWDKFSSIGTEMLITKSGRRMFPSCKVTVTGLNPKVKYVVIMDMVPFDNHKYKWNKDCWEVNGSSDPHLPNRFFIHPDSPAPGQKWMQYPISFHKLKLTNNTLNSNGLVVLHSMHKYQPRLHIVQSPDPCTPHNPGAYLRFTFPEAAFIAVTAYQNQEITKLKIDNNPFAKGFRDNGLNRKRFRDKGTQEMQDTDRQVKLDLTANECAAGMSQMVEDVDVSVSSSVDCRDTQNSSSVSLNPFISAFTNPSSAGGAAAHQTHTLLSLSNRHFSSPRESNLNSVCAALPVSQLSTGHTSFSRLNPQETHHNSRPKIQLQPPHPSLQCHDLDVRLPLPPKLSRVQLSESALRNLEMSPLSDCANPRPLTNILNRSCFRASTPSGKLLPNPPQPEQFLRGSEREIYPAVQEYTDQQFTLNSQTEHRPHMRPLTEY", "text": "FUNCTION: Probable transcriptional regulator involved in developmental processes. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "AIAAVITFLILFTIFGNALVILAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFRRTWCEVYLALDVLFCTSSIVHLCAISLDRYWAVSRALQYNSKRTPRRIKCVILTVWLIAAAISLPPLIYKGDQGPQPRGRPQCKLNQEAWYILSSSIGSFFAPCLIMILVYLRIYLIAKRSNRRGPRAKGAPREGEPKQPHPLPAGPSALANSPTLASSLAVTGEANGHSEPPGEKERETPEDPGTLTLPPSWPVLPNSGQGQKEGVCGASPEEEEECGSPAVPASPALACSPPLQQPKGSRVLATLRGQVLLGRGVGTAGGQWWRRRAQLTREKRFTFVLAVVIGVFVLCWFPFFFSYSLGAICPQHCKVPHGLF", "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": "MNINKIALIYNHNSKHLAIIEEIKQLYNYCKIEEAEVIIVIGGDGELLHNIHRYMHLNIPFYGVNLGSLGFLMNPLDTKKLLQNIHESTVSILNPLLMQVEDTSGQIYTALAINEVSIFRKTNQAAKFRIEVNGIERMSELVADGALVATPAGSSAYNLSASGPILPLESNMLCLTPICSFRPRRWHGALLLSSATIKFEILNTNKRPVNATADFQEFNNITNVTVKSTKDKPVKLLFNKNHTLEDRIIKEQFGG", "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": "MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPASGRRGMRSGPLAPVQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITAPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPTAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTPEEKATSREYAKKGARS", "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": "MSEHKKLLKNGMWDNNPALVQLLGLCPLLAVSSTVTNALGLGIATLLVLVGSNVTVSLIRNYVPKEIRIPVFVMIIASLVTCVQLLMNAYAYGLYLSLGIFIPLIVTNCIIIGRAEAYASKNDPLPAALDGFWMGMGMTTVLVVLGAMREIIGNGTLFDGADLLLGEWASALRIQVFQFDSSFLLALLPPGAFIGVGLLIALKNVIDTQLKARQPKQEKPAIERARVTNA", "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": "MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVLVSPGYTHLRDEYFPNAHQFNIHRWNKDSASSYSVGEEVDYGFGAISKGVSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFTSMVTLPTGPAKIIWEKRNPEQKI", "text": "FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:369554, PubMed:105731). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (PubMed:32679672). Starting from lanosterol (lanosta- 8,24-dien-3beta-ol), it catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of the sterol in the form of formate, and converts the sterol to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien- 3beta-ol, which is critical for ergosterol biosynthesis (PubMed:369554, PubMed:105731, PubMed:3543000). Can demethylate susbtrates not intrinsic to yeast, such as eburicol (24-methylene-24,25- dihydrolanosterol) at a similar rate to lanosterol, and at a lower rate the 24,25-dihydrolanosterol (DHL) to 4,4-dimethyl-8,14-cholestadien- 3beta-ol (PubMed:3543000, PubMed:1872829). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MKREILLERIDKLKQLMPWYVLEYYQSKLAVPYSFTTLYEYLKEYDRFFSWVLESGISNADKISDIPLSVLENMSKKDMESFILYLRERPLLNANTTKQGVSQTTINRTLSALSSLYKYLTEEVENDQGEPYFYRNVMKKVSTKKKKETLAARAENIKQKLFLGDETEGFLTYIDQEHPQQLSNRALSSFNKNKERDLAIIALLLASGVRLSEAVNLDLRDLNLKMMVIDVTRKGGKRDSVNVAAFAKPYLENYLAIRNQRYKTEKTDTALFLTLYRGVPNRIDASSVEKMVAKYSEDFKVRVTPHKLRHTLATRLYDATKSQVLVSHQLGHASTQVTDLYTHIVSDEQKNALDSL", "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": "MSAVDAAAGAADGAHLAAGTVVGVVGPTAAGKSALSVALAHALDGEVVNADSMQLYRGLDIGTAKLTTDERAGVPHHLLDIWPVTEPASVAEYQRLARAAVDDILARGRVPLLVGGSGLYLRAVLERFEFPGTDPVLRQRLEAELAQAGPAALHERLRAVDPDAAANILPGNGRRIVRALEVVELTGAPFTAALPDPSPYYRSVQVGVDLDTARLDERIALRVDRMWADGLVAETRLLADQGLAEGRTASRALGYQQVLRFLAGELTESEAYQETIRATRRFVRRQRSWFRRDPRITWLDSAGSGLVAEALRVVRPAAR", "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": "MTKKKVVIGMSGGVDSSVAAYLLKEQGYDVIGVTMQIWQEDKEYEEREGGCCSLSAVDDARRVAQKLDIPFYVLNFRDSFKRNVIDYFVDEYIQGRTPNPCIACNKYLKFDELLQKAKGIGADYVATGHYAKIEERDGRFQLIRSKDDRKDQTYALYNLTQEQLEHTLMPCGEFTKDKIREIAKEIGLDVHNKKDSEEICFIPDNNHGRYICEAAPNKVRPGNFVDKYGNVLGKHKGIVYYTIGQRKGLGLALGRPVFVTDINPVTNTVVVGPEEDIFKTDLVCKDINFISIDKLEGPMEVEAKIRYSARPAKATISPMENGRVKVSFEDKQRAITKGQSVVFYKDDLVVGGGIIESLL", "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": "MFSSSIRLIVSGFHRTQPLKSPVNSPSVFISVPKFFNSESKSTGTGSRSVAMSSVEKTGSDSGAIENRASRMREKLQKELEPVELVIEDVSYQHAGHAGMKGRTDDETHFNVKIVSKGFEGMNLVKRHRLVYHLLREELDTGLHALSIVSKTPSESPSKD", "text": "FUNCTION: May act either alone or in interaction with glutaredoxin as a redox-regulated transcriptional regulator, or as a factor regulating Fe-S cluster biogenesis (Probable). The glutaredoxin-BOLA1 heterodimers bind a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bolA/yrbA family."}
{"protein": "MKKRAIVLLSGGLDSATVLAMANAQGFETYALSMRYGQRHSSELEAAKKVAAALGAVRHEIVDLDLRRFGGSALTDDALEVPTTGVQEGIPITYVPARNTIMLSLALGWAEAVGARDLFFGANAVDYSGYPDCRPEYVAAYETLANLATKAGVEGDHIRVNAPIIAMTKAEIIQAGARLGVDYSLTVSCYQADDEGRACGVCDSCRIRRAGFEAAAVPDPTRYR", "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": "MPTLKDIRVRIKGVTSTQQVTKAMKMVAAAKLRRAQERAVMARPYAAKLSEMLGSLSAKVDTSENPLLSGRSEVRGALVILITSDRGLCGGFNTNIIKVAQRVVNNEYGELNAAGRLSMICAGTRGFDFFRKRGYTILKGYPSVFQNLDFSTAQEIAETASSMYLKGEVDKVVVVYNEFKSVLAPVLKAETLLPISSEENEGDRGGDYIYEPSPSAIISELVPKHLNTQVWRMMLESNAAEQAARMTAMDSATENAKELLRTLNISYNRARQAAITKELSEIVGGADALQN", "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": "MKLKTNIRHLHGSIRVPGDKSISHRSIIFGSLAEGETKVYDILRGEDVLSTMQVFRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNMGNSGTSIRLISGVLAGADFEVEMFGDDSLSKRPMDRVTLPLKKMGVSISGQTERDLPPLRLKGTKNLRPIHYELPIASAQVKSALMFAALQAKGASVIIEKECTRNHTEDMLKQFGGHLSVDGKKIIVQGPQKLTGQKVVVPGDISSAAFWLVAGLIVPNSRLVLQNVGINETRTGIIDVIRAMGGKLEITEIDPVAKSATLIVESSDLKGTEICGALIPRLIDELPIIALLATQAQGVTVIKDAEELKVKETDRIQVVADALNSMGADITPTADGMIIKGKSALHGARVNTFGDHRIGMMTAIAALLVADGEVELDRAEAINTSYPSFFDDLESLIHG", "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": "MGKIIGIDLGTTNSCVAVMDGDKARVIENAEGARTTPSIIAYTDNETLVGQPAKRQAITNPKNTLFAIKRLIGRRFESEEVQRDIKIMPFEITRADNGDAWVNVKGDKLAPPQISAEVLKKMKKTAEDFLGEAVTEAVITVPAYFNDAQRQATIDAGRIAGLDVKRIINEPTAAALAFGLGSTKENQVIAVYDLGGGTFDISIIEIDNFDGEQTFEVLATGGNTHLGGEDFDNRVIDYIIDEFKKEQGVDLRNDPMALQRVKEAAEKAKIELSSAQSTEVNLPYITADATGPKHLAINVTRAKLEALVEDLVASSIESLKTVLKDAGKSVNEINDIILVGGQTRMPLVQQKVAEFFGKEARKDVNPDEAVAIGAAVQGGVLKGDVKDVLLLDVTPLSLGIETMGGVMTVLIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKQASANKSLGQFNLEGINPAPRGMPQIEVTFDIDANGVINVSAKDKNTGKEQQIRIQASSGLSDEEIEKMVRDAEANAEADKKFEELVQARNQADGIAHATRKQIEEAGDALNADDKAKIEAAIADLEKAAKGDDKAEIDAKTEALIKASEPLMQAAQAKAQAGEQPQQSAKDDGVVDAEFEEVKDNK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MKQLSSAEVRQLFLDFFKEKGHTIEPSAPLVPNNDPTILWINSGVATMKKYFDGSVIPDNPRMANAQKSIRTNDIENVGKTARHHTFFEMLGNFSIGDYFKEGAILFAWEFLTSPKWIGFDPDKLYVTVYPEDEEAKTLWREKIGLSEDHIVEIEDNFWDIGIGPSGPDSEIFYDRGPAFGDDESDPELYPGGENERYLEIWNLVFSQFNHNPDGTYTPLPKQNIDTGMGLERMVSIIQDAPTNFETDLFMPIIREVEQISGVKYGHSQENDVAFKVIADHIRTVAFAIGDGALPSNEGRGYILRRLLRRAVRYAKVLTINEPFMYKLVPVVGKIMNSFYPEVENQTDFIQKVIRTEEERFHETLNEGLAILETILKNAKETNEQTIKGADIFKLYDTFGFPVELTEEYAEDHGLKVDHAGFEAEMKEQRDRARSARADVKSMQVQGELLANLTDKSEFVGYNTTEHVSEILYLIQDDTLVDEVASGSEAQVIFKETPFYAESGGQVADKGTIESETGVAYVEDVQKAPNKQNLHRISVKEGVLKTGDTVKLAVDKVKRRETIKNHTATHLLHRALKDTLGEHVNQAGSLVSPDRLRFDFSHFGQITEEELTKMEEIVNEKIWEQINVIIEEMPIAEAKELGAMALFGEKYGEVVRVVQVGKYSIELCGGVHVRNTADIGLFKIVSETGIGAGTRRIEAVTGKEAYRFVTEQENTLKQTANLLKTTTKETPQKVEQLQADLREVRRENESLLSKLASAASADIFESPEEIGGVKVIAKQVNAKDMNQLRQFVDNWKDKKIGGVLVLGAVQGDKVNLISAVSEDAIKAGYHAGKLLKEVATRCGGNGGGRPDMAQAGGKNPAELGTALDYVSTWVKEQQA", "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": "MSDSAPEIETPVEEAPKAASPAKSPAKSPGRAKKAKKDGSDKPKKPKAIPTHPPVSEMVVNALKTLNEKGGSSVIAIKKFLVATYKVEIEKLLPFIKKFLKGAVLKGEVLQVKGTGASGSFKMPPPAKKVDRPESAPKKKATKTKTRVERKEKKVVAKKPKPAVEKKAAKPAAKKAAAKPAAKKAAAKPAAKKPAAKASPKKAAAKPKAKPTPKKSTPAKPKAAARKPAKKSK", "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": "MSGDLSRCLGKGSCPPGPVPEGVIRIYSMRFCPYSHRARLVLKAKGIRHEVININLKSKPDWYYTKHPFGQIPVLENSQCQLVYESVIACEYLDDVYPGRKLFPYDPYERARQKMLLELFCKVPPLSKECLIALRCGRDCTDLKVALRQELCNMEEILEYQNTTFFGGDCISMIDYLVWPWFERLDVYGLADCVNHTPMLRLWIASMKQDPAVCALHTDKSVFLGFLNLYFQNNPCAFDFGLCNPIIR", "text": "FUNCTION: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). SIMILARITY: Belongs to the GST superfamily. Omega family."}
{"protein": "MHQLFRLVLGQKDLSRAGDLFSLDDAEIEDSLTEALEQIKVISSSLDYQTNNNDQAVVEICITRITTAIRETESIEKHARALVGLWDSCLEHNLRPAGKDEDTPHAKIASDIMSCILQNYNRTPVMVLAVPIAVKFLHRGSKELCRNMSNYLSLAAITKADLLADHTEGIVKSILQGNAMLLRVLPAVYEKQPQPINRHLAELLALMSQLEQTEQYHLLRLLHVAAKRKDVEVVQKCVPFLIRNLKESTYNDIILNILIEIAGHEPLALNSFLPMLKEIAEQFPYLTGQMARIFGAVGHVDEERARSCLRYLVSQLANMEHSFHHILLLEIKSLTDAFSSILGPHSRDIFRMSNSFTNIAKLLSRQLENSKAESGRRRTGTEVSFPEKFREPKTMEPKSEDHEKLQVKIQAFEDKINAESHTPGSVRRYSLDHVSKEERKNVRFSRSRSLALNTVLTNSVNVEDGEIEGKTGMHASISLSEIDPPGHGIGKVPFKTDTHGSQLRNSSASHPSIIHSEPENMPETFKENVQEEIPEAAISPVEYQDKLYLHLKENLSKVKAYALEIAKKVPIPDQCTIEDNTRSCVAKLFFTCSLKGHYCLYSKSSFTLVSQAPQPWIQIMFLFQQSLFPEPLSIQSGSVQFLKALWEKTQGTGTHSFEVAMTESTFPQQKDLDQLQLHLEEVRFFDVFGFSETAGAWQCFMCNNPEKATVINQDGQPLIEGKLKEKQVRWKFIKRWKTRYFTLAGNQLLFQKGKSDDPDDSPIELSKVQSVKAVAKKRRDRSLPRAFEIFTDNKTYVFKAKDEKNAEEWLQCINVALAQAKERESREVTTYL", "text": "FUNCTION: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the MELT/VEPH family."}
{"protein": "MNYNNKKTLKDIDVKNKTVLVRVDFNVPIQNGVITDDNRIIAAFPTINYLLENDAKIVLFSHLSRIKSKEDKLKKSLAPVAKRLEELLNKQVKFINQTRGQELEKAISSLQSKEIILVENTRFEDVLDDQVVKYESKNNSELGKYWASLGEVFVNDAFGTAHRAHASNVGIASNIKVSAIGFLVEKELKMLFQAVNEPKKPFIAILGGAKVSDKIGVIENLLPKVDKLLIGGGMSYTFLKALGKTIGKSLLEEDKIDLAKHYLEIGKDKIVVPVDTACAKEFADVSPTIFEGNIPDEWDGLDAGPKTIELFKQEIKKAKTIVWNGPVGVFEFKNFENGTKSVCQAIAEQTQNGAFTLIGGGDSASAAINMGFKDKFSWISTGGGASLEFMEGKELLGISAIQDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MTRDLAPALQALSPLLGSWAGRGAGKYPTIRPFEYLEEVVFAHVGKPFLTYTQQTRAVADGKPLHSETGYLRVCRPGCVELVLAHPSGITEIEVGTYSVTGDVIELELSTRADGSIGLAPTAKEVTALDRSYRIDGDELSYSLQMRAVGQPLQDHLAAVLHRQR", "text": "FUNCTION: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). In M.tuberculosis, could be part of the pool of proteins required to scavenge RNS and ROS produced by the host during the immunity response. Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo. FUNCTION: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo. SIMILARITY: Belongs to the nitrobindin family. SIMILARITY: Belongs to the nitrobindin family."}
{"protein": "MVRGKIEIKKIENVTSRQVTFSKRRSGLFKKAHELSVLCDAQVAAMIFSQKGRLYEFASSDIRNTIKRYAEYKREYFVAETHPIEQYVQGLKKEMVTMVKKIEVLEVHNRKMMGQSLDSCSVKELSEIATQIEKSLHMVRLRKAKLYEDELQKLKAKERELKDERVRLSLKKTIYTHLCQVGERPMGMPSGSKEKEDVETDLFIGFLKNRP", "text": "FUNCTION: MADS-box transcription factor that acts with AGL42 and AGL71 in the control of flowering time. Promotes flowering at the shoot apical and axillary meristems. Seems to act through a gibberellin- dependent pathway. Interacts genetically with SOC1 and its expression is directly regulated by SOC1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGNIFHIPVLLEEIINLLEASNISDGFVFVDCTLGEGGHSSAVLKKYQNINVIGIDRDDVVLNRAKESLIEFKGRVSYFNTWFDDFFSEYPLSSKINFILADLGISMFHYKMSGRGFSFFEDERLDMRLYPGAGGLSAYDIINTFDKKRLENLIYELSGERYSRRIVKSILEYRKIKKIETPRELQDIVSKAYPRIKLKINPATKTFQALRIYVNDELFRLKRSLPLWVESLSNNGVLAIVTFHSLEDKIVKEFFKGLSKDQYCILTKKPIMPRCEEKRFNSASRSAKLRVIKKLYE", "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": "MAKEKFDRSKPHLNIGTIGHVDHGKTTLTAAITTTLAKLVGGKNKAIAYDQIDNAPEEKARGITIATSHQEYETPNRHYAHVDCPGHADYVKNMITGAAQMDAAILVVSATDGAMPQTKEHILLARQVGVPYIVVYLNKADMLAADERDDMVEMVKEEIKDLLNKYNFPGDKTPFISGSALKALEGEDSDLGMKSILKLMEAVDTYVPNPTRIVDKPFLMPVEDVFSITGRGTVATGRVEQGVLKINDEIEIVGIRDTTKSVVTGIEMFRKLLDQAEAGDNIGALLRGTKKEDIERGQVLAKPGTITPHRKFKAEVYVLTKDEGGRHTPFFNNYRPQFYFRTTDITGVCNLPGGMEMVMPGDNVTMSIELIHPIAMDQGLKFAIREGGRTIGSGVVAEIVE", "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": "MFAAIQPGLAEGAQYPGSLPPGVCQPDLQPDNNSNFVESAKDANKNWHGVPGKVDPILIRSSSESPSDNQVFQATRLPEAGVRSPPEGAEIPGAEPEKLSGASSVCSPLEDIGYASSSLSIDSFSSSPEPVCDTPRGPSPLDPLLPSVAQAVQQLQAQERYKEQEKEKHHAHLVMYRRLALLQWIRALQHQLVDQQARLQESFDTILDNRKELIRCLQQREAPCRHQDQG", "text": "SIMILARITY: Belongs to the UPF0500 family."}
{"protein": "MAVAIAAARVWRLNRGLSQAALLLLRRPGARGLARSHPRRQQQQFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPVSRLRHYLLSQGWWDEEQEKAWRKQSRKKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFDK", "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). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the BCKDHA family."}
{"protein": "MARYRHSRSRXRSRYRRRRRXRSRYRSXRRRYRGRRRRRSRRGRRRRGYSRXRYSRRRRRRY", "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": "MMICFVFLCVLTFVRGEIYPSTCPALGAGNGEAVRSGEMLLEISAYRNWRSGKMELWGSAAVNNQVFYGGMEDSQIEYDFGKFLVFRCFQVFHNVHKLLFNTVSSATMHLARKRVQKCGHGKMTFISIQVQCSVNKKSIRLSRMNETNLKKQVLRVAFFLDGSNNSWIADKNFQGEDRTMLRLWTELSTYRQYLISSCNNDVKVLSELYGEFRRMALSYDEELKLNFMPVIRSSSERLFRADDLKCSFSRWLGAEGEFAVCEYSGWGVSKLGKIEIFAEEPLTFDMVWKTVKMRSSGAYTSLFRDDVTWGLISLDKWVGDKYFCMCTNKESGDNVIVTLPEKNVEKSIQIYNEGSTMLAFAEITSIMVNLMFMGAVAVCVGILGISCFVGLKEIIYFIFVSVNSMWPFCNKLLTTAVNCFFKGRTFLRRELKI", "text": "FUNCTION: Binds to MHC class I molecules in the endoplasmic reticulum and targets them from the Golgi directly to the lysosomes. Once in the lysosomes both proteins are degraded. In consequence, surface class I molecules are down-regulated and infected cells are masked for immune recognition by cytotoxic T lymphocytes (By similarity). SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the herpesviridae U21 family."}
{"protein": "ADLGYGPATPAAPAAGYTPATPAAPAGADAAGKATTEEQKLIEKINAGFKAALAGAGVQPADKYRTFVATFGPASNKAFAEGLSGEPKGAAESSSKAALTSKLDAAYKLAYKTAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIEKVDAAFKVAATAANAAPANDKFTVFEAAFNDEIKASTGGAYESYKFIPALEAAVKQAYAATVATAPEVKYTVFETALKKAITAMSEAQKAAKPAAAATATATAAVGAATGAATAATGGYKV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Poa p IX/Phl p VI allergen family."}
{"protein": "MVPVLLSLPLLLGPAVLQETGSYSLIFLYTGLSRPSKGLPRFQATAFLNDQAFFHYNSNSGKAEPVEPWSHVEGMEDWEKESQLQRAREEIFLVTLKDIMDYYEDSTGSHTFQGMFGCEITNNRSSGAVWRYAYDGEDFIEFNKEIPAWIPLDPAAANTKLKWEAEKVYVQRAKAYLEEECPTMLKKYLTYSRSHLDRTDPPTVKITSRVAPGRNRIFRCLAYDFYPQRISLHWNQASKKLASEPERGVFPNGNGTYLSWMEVEVPPQNRDPFVCHIEHKGLSQSLSVQWDEKSKV", "text": "FUNCTION: Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MHC class I family."}
{"protein": "MTNSTKVEKPWTKWHERLHKSLKSKSNLLPYGSSLLISVSGGQDSMALLKLILDLQRIYEWKVHVWHGDHGWHNQSRQIAEELEEWCKCQKLSFFCNRTNKQKVSTEEDARNWRYKSLIQQAKTLSKESPSLPCERVLTGHTANDRTETFIMNLARGAHLKGLSSLREDRTLETKIQLIRPILRFSRQETIQICDEMDLPIWIDPSNSNIAYSRNKIRAEIIPVLESLHPQSTIRISNLAERLTSLQKDQHQLAHLALGALLTSTGLSRSKMTKLSKTVRAIILAQWLEDNKAPLLSSKQLEELSQKIGKNKGPGNMDISNHLKIRWNKNSIELIN", "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": "MSSINGIDNIKFDYEFSNSLYYRNSIFFSIIFFIIYKKSSYITENFFGELVKKAYTTLTEKKKLEWDQRVVSMIHAFLVLPFCIISAVESFKYGDIFYFQNDSLLMVLSISSGYFIWDLIICYKDPKLVGTPMIIHAIMGLSSNIYVALPHGRPCFVPIVAILLITEISTIPLNMKGFIQVVNSKSKYYNWSLGAFVITFLVSRCIIGLPFDIYLVYGCIQRWDVFPMDKSLVFITECGIQFFLNSYWSFLLIKKLYQTYLNPIPNHKKNED", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TLCD4 family."}
{"protein": "MTKQPEDWLDDVPGDDIEDDEIIWVSKSEIKRDTEELKRLGAEIVDLGKNALDKIPLDADLRAAIELAQRIKMEGRRRQLQLIGKMLRQRDVEPIRQALDKLKNRHNQQVVLFHKLENLRDRLIAQGDDAIAEVLNLWPDADRQQLRTLIRNAKKEKEGNKPPKSARQIFQYLRELAENEG", "text": "SIMILARITY: Belongs to the UPF0307 family."}
{"protein": "MAKPSQPTRDSHVAVLVFPFGTHAAPLLAVTCRLATAAPSTVFSFFSTARSNSSLLSSDIPTNIRVHNVDDGVPEGFVLTGNPQHAVELFLEAAPEIFRREIKAAETEVGRKFKCILTDAFLWLAAETAAAEMKASWVAYYGGGATSLTAHLYTDAIRENVGVKEVGERMEETIGFISGMEKIRVKDTQEGVVFGNLDSVFSKTLHQMGLALPRATAVFINSFEELDPTFTNDFRSEFKRYLNIGPLALLSSPSQTSTLVHDPHGCLAWIEKRSTASVAYIAFGRVATPPPVELVAIAQGLESSKVPFVWSLQEMKMTHLPEGFLDRTREQGMVVPWAPQVELLNHEAMGVFVSHGGWNSVLESVSAGVPMICRPIFGDHAINARSVEAVWEIGVTISSGVFTKDGFEESLDRVLVQDDGKKMKVNAKKLEELAQEAVSTKGSSFENFGGLLDEVVNFG", "text": "FUNCTION: Possesses low quercetin 3-O-glucosyltransferase activity in vitro. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MTKASVAIVGSGNISTDLLYKLQRSEWLEPRWMIGIDPESEGLARARTMGLETSAEGVGWLLNQPEKPDLVFEATSAHVHRDSAPRYEAAGIRAVDLTPAAVGPAVVPPANLREHLGAPNVNMITCGGQATIPIVYAVSRVVDVPYAEIVASVASVSAGPGTRANIDEFTKTTSRGIETIGGAQRGKAIIILNPADPPMIMRDTIFCAIPEDADRAAITDSIHRVVADIQQYVPGYRLLNEPQFDDPSVVSGGQATVTTFVEVEGAGDFLPPYAGNLDIMTAAATKVGEEIAQKLLSVEA", "text": "SIMILARITY: Belongs to the acetaldehyde dehydrogenase family."}
{"protein": "MPAYHSSFLSLTDVPTTGNIAMLPLKTKFRGPAYPADESQMDIIDECIGLFRANCFFRNFEIKGPADRTLIYGTLFISECLGRVNGLNYRDAERQLNSLALENFSIPGSAGFPLNALYAPPLSPQDAEIMRTYLTQFRQELAYRLLSHVYATEKDHPSKWWTCFSKRRFMNKAL", "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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch. SIMILARITY: Belongs to the ARPC3 family."}
{"protein": "MTKLTCFKAYDIRGRLGEELNEDIAWRIGRAYGEYLKPKTVVLGGDVRLTSEALKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEAGDFPPVNEAARGSYRQISLRDAYIDHLLGYISVNNLTPLKLVFNAGNGAAGPVIDAIEARLKALGAPVEFIKIHNTPDGTFPNGIPNPLLPECRDDTRKAVIEHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKHPGAKIIHDPRLTWNTEAVVTAAGGTPVMSKTGHAFIKERMRTEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKRQSLGELVRDRMAAFPASGEINSRLAEPAAAIARVEAHFAEEAQAVDRTDGLSMSFADWRFNLRSSNTEPVVRLNVESRGDIPLMEARTRTLLALLNQ", "text": "FUNCTION: Involved in the biosynthesis of the capsular polysaccharide colanic acid. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MQVSVQGNDVDKALRLLKRKLQTEGFFKEIKKRKHYEKPSVKKKRKQMEAERKRRKAQRFRKPDRD", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
{"protein": "MAERFKILVLNGPNLNLLGQREPELYGKQSLDDIADSLGAIAKQHATALDFRQSNAEHQLIDWIQQAAKDSVDYIVINPAAYAHTSVALRDALLAVKIPFIEVHLSNIYRRESFRHHSYLADVADGVICGLGARGYEYALQAALTTLNNTDN", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
{"protein": "MSNKYNNLLKEVAAKYASIILNDAKIKSLTSINSAEYLYDSFVEISKLPLEKKLPLKWKLITVKENICTKTNLTTAASNMLKDYNSPFDASIVESLKKAGGIILGKTNMDEFAMGVKSENNLFGRTVNPVVKDSNYDVGGSSGGAAAAIAADICYASVGSDTGGSIRLPAAYVGCVGFKPSFGRISRYGMLAFANSFDTVGIAANNVKGVTKVFNVLDHPDINDSTCLTKEARYFVKEQHKKLSRKPIKIGIPIDWNVSETHPNVLDKWNEFISLLKSNGYLVQEIQLPISLYANSVYSTMAYAEATSNLAKYNTIAFGNCLDEKFEEEIISSTARSFFLGDEVKKRLLLGAYSLARMNSSDLFSKARYVRRAIQLEFNKNFFLPSFSVDDPRGDIDFIVTPSFFNSSQPIETPSSYSHLSDTMLVPANMAGIPSVSIPFGTLNNGLPMGIQIMAQYLNDEDLLSFAGQFA", "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": "MSDTPFGDADHPRPAPIHPDAVLPPPMSSQSADNDPTEALNEAWTNILTKVSKPNRAWLSNTTPVTMHSSTAMVAVPNEFARDRLESKMRYELEELLSDHFHKAIHLAITIDPDLELALGAPDHEDEEEEVPPAQFVPKVTVGVTEPSARPTTTIDDDEGNRLNPKYTFDSFVIGASNRFAHAAAVAVAEAPGKSYNPLLIYGGSGLGKTHLLHAIGRYVMSYYDNVKVKYVSTEELTNDFINAIGTNRTTEFRRSYRDVDVLLVDDIQFLQSKIQTQEEFFHTFNTLHNAQKQIVMTSDRPPKLLEALEPRLRSRFEWGLLTDIQPPDLETRIAILRRKVAAEKITVEPDVLEFIASRIQTNIRELEGALIRVTAFASLNQQPVDISLAEVVLKDLIPEGRETPVTPERIIAETADYFDISADDLLGTSRAQTLVTARQIAMYLCRELTDLSLPKIGAEFGGKDHTTVMHADRKIRALMGEQRQIFNQVSEITNRIKQY", "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": "MDLPIQDSHDSSTSPKGKQPTTAEKSATKKEDKVPVKKQKTRTVFSSTQLCVLNDRFQRQKYLSLQQMQELSNILNLSYKQVKTWFQNQRMKSKRWQKNNWLKNSNGVTQGCLVNPTGNLPMWSNQTWNNSTWSNQTQNIQSWSNHSWNTQTWCTQSWNNQAWNSPFYNCGEESLQSCMQFQPNSPASDLQAALEAAGEGLNVIQQTTRYFNTPQTMDLFLNYSMNMQPEDV", "text": "FUNCTION: Probable transcriptional regulator. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Nanog homeobox family."}
{"protein": "MNPQELKSILSHGLLSFPVTDFNAQGDFNQAGYIKRLEWLAPYGASALFAAGGTGEFFSLAASEYSQVIKTAVDTCAKSVPILAGVGGSTRQAIEYAQEAERLGAKGLLLLPHYLTEASQDGVAAHVEAVCKSVNIGVVVYNRNVCRLNADLLEKLAERCPNLIGYKDGLGDIELMVSIRRRLGDRFSYLGGLPTAEVYAAAYKALGVPVYSSAVFNFIPKTAMDFYHAIARDDHATVGKLIDDFFLPYLDIRNRKAGYAVSIVKAGAKIAGYDAGPVRTPLTDLTAEEYEMLAALMDKMGPQ", "text": "SIMILARITY: Belongs to the DapA family."}
{"protein": "MAKEILFNIDARDQLKKGVDALANAVKVTLGPKGRNVIIEKKFGAPHITKDGVTVAKEIELADAYQNTGAQLVKEVASKTGDDAGDGTTTATVLAQAIVAEGLKNVTAGASPMDIKRGIDKAVAKVVESIKAQAETVGDNYDKIEQVATVSANNDPVIGKLIADAMRKVSKDGVITIEEAKGTDTTIGVVEGMQFDRGYLSAYFVTNTEKMECEMEKPYILIYDKKISNLKDFLPILEPAVQTGRPLLVIAEDVDSEALTTLVVNRLRSQLKICAVKAPGFGDRRKEMLEDIAILTGGVVISEEKGLKLEQATIEMLGTADKVTVSKDYTTIVNGAGVKENIKERCDQIKAQIVATKSDYDREKLQERLAKLSGGVAVLYVGAASEVEMKEKKDRVDDALRATRAAIEEGIIPGGGVAYIRAIDSLEGMKGDNADETTGIGIIKRAIEEPLREIVANAGKEGAVVVQKVREGKGDFGYNARTDVYENLHAAGVVDPAKVARVALENAASIAGMFLTTECVIVEKKEDKPEMPMGAPGMGGMGGMM", "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": "MATYKVTLVRPDGETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSDQSFLDDDQIEKGFVLTCVAYPRSDCKILTHQEEELY", "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": "MTILFLTMVISYFSCMKAAPMKEASVRGHGSLAYPGLRTHGTLESLTGPNAGSRGLTSLADTFEHVIEELLDEDQDIQPSEENKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCNPKGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDNKKRVGWRFIRIDTSCVCTLTIKRGR", "text": "FUNCTION: Important signaling molecule that activates signaling cascades downstream of NTRK2 (By similarity). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NGF-beta family."}
{"protein": "MSRVAKRPILIPEGIKIELNLQSISIKGKYGYLSRIIHDAVKVECLNNKITFSIRSGFSDAWAQAGTSRALVNSMIIGVSKKFSKKLQFSGVGYRVSLTKGNIVNMSLGYSHPIVYSLPPYIEAENPSPTEIVIKGVDKQLVGQIAANLRSYRRPEPYKGKGIRYSNEVVHMKEAKKK", "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": "NWKCNLSKADIAELVSAFNAAPPIDAAHVQVVVAPPAVYLDSTRQALRADFDTSAQNAWISKGGAFTGELDAAMVKDVGAEWVILGHSERRHIAQLKESDHTIAMKAAYALQHASLGVIYCIGELLEERESGQTIAVCERQLQALSDAISDWSDVVIAYEPVWAIGTGKVATPEQAEQVHEAVRAWLANNVSPQVAASTRILYGGSVSPANCESLAKQPNIDGFLVGGASMKPTFLEIVDSYKATLAEAV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVGRLNITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIHCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLRQGKVEDKWYSLSGRQGDDKEGMINLVMSYALLPAAMVMPPQPVVLMPTVYQQGVGYVPITGMPAVCSPGMVPVALPPAAVNAQPRCSEEDLKAIQDMFPNMDQEVIRSVLEAQRGNKDAAINSLLQMGEEP", "text": "FUNCTION: Component of the signaling pathway of IL-1 and Toll-like receptors (PubMed:10854325, PubMed:11751856). Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex (PubMed:10854325). Inhibits IRAK1 phosphorylation and kinase activity (PubMed:11751856). Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates (PubMed:25042851). The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (PubMed:25042851). In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes (PubMed:15047686). Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:26320582). SUBCELLULAR LOCATION: Cytoplasm Endosome Early endosome Note=Localized to endo/exosomal vesicles. SIMILARITY: Belongs to the tollip family."}
{"protein": "MTIYALSTGPGISGIAIVRVSGKDTKKVIKLLTNAALPETRVATLRKINKINTSELIDEGIILWFPGPESYTGEDMAEFHIHGSKAVIDALHHSISKIKNCRLADPGEFTKLAFQNGKINLLKAESIADLISAETEIQRQQAIKIMNGKSADKFNNLREKLLKILSHVEAKIDFPDEDLPEDILKNIKKISNEVILNIKKILDDQKVGERIREGFKIAIIGPTNAGKSSLLNHLSNRDVAIVSEIAGTTRDVIETHLNIDGYPVVVSDTAGIRDSKNEIEKKGIKLALDKADNADLKLIVIDAKSIDFKGVLKELMDENAILVINKSDLLNKDLNSEIKNYEHVLISVKNNLNLEDLISKIKNKLKNKFITSEDILITRARHRQHLEQSLNCLKNFEEKNEAEDFDKAAEDLRLATRHLGMIVGKVDVEEILGSIFNDFCIGK", "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": "MVYLEWAKADRNIQYRVINAIIKERIYPEQTFISQKGSLIEIQYHMHVLTIEVVRKSALERYEFTGDITYLNKGETSLIITLEGLLDVLNHDFDIPISERLREELIHSRDSLVETYKQMSHRQTLISQSFKFSRLPQDINFFSWLQHVKDSDKTDDLTYSESLVPEGHPTHPLTKTKLPLTMEEVRAYAPEFEKEIPLQIMMIEKDHVVCTAMDGNDQFIIDEIIPEYYNQIRVFLKSLGLKSEDYRAILVHPWQYDHTIGKYFEAWIAKKILIPTPFTILSKATLSFRTMSLIDKPYHVKLPVDAQATSAVRTVSTVTTVDGPKLSYALQNMLNQYPGFKVAMEPFGEYANVDKDRARQLACIIRQKPEIDGKGATVVSASLVNKNPIDQKVIVDSYLEWLNQGITKESITTFIERYAQALIPPLIAFIQNYGIALEAHMQNTVVNLGPHFDIQFLVRDLGGSRIDLETLQHRVSDIKITNDSLIADSIDAVIAKFQHAVIQNQMAELIHHFNQYDCVEETELFNIVQQVVAHAINPTLPHANELKDILFGPTITVKALLNMRMENKVKQYLNIELDNPIKKEV", "text": "FUNCTION: Involved in the biosynthesis of the siderophore staphyloferrin A. Catalyzes the ATP-dependent condensation of a citryl- D-ornithine intermediate, produced by SfnaD, and citrate to form staphyloferrin A. SIMILARITY: Belongs to the IucA/IucC family."}
{"protein": "MTKTFFSFSFFFTSSLLLLLAATSATASTGNVTSGLRYDGCAPGDTVGECITATVEEEDEEGVEAVVRRILQQRKYLSYKTLQKQPTCDGRIAGNCIGTVNPKGATCTYYQRCKRAA", "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": "MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFIAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLTFKAPSAVLA", "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": "MFSVLISLYNKEKPENLEQCLESLHQQTLNADEIVLVYDGPVSESLKAVATRWANLLPLVIVPLEKNLGLGKALNAGLERCTHNVVARMDTDDICLPERFEKQISYMESHPEVVLSGAAVIEFDEHGKERLKRLPLSNNDIHQFARMKNPFNHMCVVFRKDKVISAGSYQHHLYMEDYNLWLRIMSLGHPVANLPDVLMKVRAGSDMVNKRRGWNYIKSEVQLYRLKLALKQTGFIRGTLYFLIRTMTRLMPVKVMQFLYEKDRKG", "text": "FUNCTION: Involved in the biosynthesis of amylovoran which functions as a virulence factor. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MAKQEQAPGRANDVFALTSFLYGGNADYIEELYAKYEDDPNSVDPQWRDFFAKLGDNADDVKKNAEGPSWTRKNWPIAANGELVSALDGNWAEVEKHVTDKLKGKAAKGEAKGAAGTPLTAEEITQAARDSVRAIMMIRAYRMRGHLHANLDPLGLAEKPNDYNELEPENYGFTPADYNRKIFIDNVLGLEYATVPEMLDILKRTYCGAIGVEFMHISDPAEKAWIQERIEGPDKKVAFTPEGKMAILSKLIEAEGFEQFIDVKYKGTKRFGLDGGESLIPALEQIVKRGGQMGLKEVVLGMAHRGRLNVLSQVMGKPHRAIFHEFKGGSYTPDDVEGSGDVKYHLGASSDREFDGNKVHLSLTANPSHLEIVNPVVMGKARAKQDLLVGRTRDDMVPLSERAKVLPLLLHGDAAFAGQGVVAECLGLSGLKGHRVAGTLHFIINNQIGFTTNPAFSRSSPYPSDVAKMIEAPIFHVNGDDPEAVVFAAKVATEFRMTFHKPVVIDMFCYRRFGHNEGDEPSFTQPLMYKAIRAHKTTVQLYGEKLIAEGLVTQDDIDRMKADWRQKLEGEFEAGQSYKPNKADWLDGAWAGLRTADNADEQRCGKTAVPVKTLKEIGKKLVEVPKDFHVHRTIQRFLDNRAKMMETGEGIDWATAESLAFGSLAVEGHPIRLSGQDVERGTFSQRHTVLYDQENQNRYIPLNNLQKGQAIYEAINSMLSEEAVLGYEYGYSLSDPRALVLWEAQFGDFANGAQVVFDQFISSGERKWLRMSGLVCLLPHGFEGQGPEHSSARLERYLQLCAEDNMQVANVTTPANYFHILRRQMKRDFRKPLIMMTPKSLLRHKRAISTLAELSGESSFHRLLWDDAQYNKDEGIKLQKDAKIRRVVLCSGKVYYDLYEEREKRGIDDVYLLRVEQLYPFPAKALINELSRFRHAEMVWCQEEPKNMGAWSFIDPYLEWVLAHIDAKHQRVRYAGRPAAASPATGLMSKHLAQLAAFLEDALG", "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": "MKTPEDPGSPKQHEVVDSAGTSTRDRQAPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGRDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKSILALERWKCPSEEEIYGNWSMPLNTSHIWHPRIREVQGAIMVSSMVEVVIGLMGLPGALLSYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIVLFSQYLRNLTFLLPVYRWGKGLTLFRVQIFKMFPIVLAIMTVWLLCYVLTLTDVLPADPTVYGFQARTDARGDIMAISPWIRIPYPCQWGLPTVTVAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGIFTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAGIMLILGAIGKFTALFASLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLDSNPGAINTGIPEVDQILTVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSETSASLKSYDFPFGMGMVKRTTFFRYIPICPVFRGFSKKTQNQPPVLEDTPDNIETGSVCTKV", "text": "FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family."}
{"protein": "MLVLIPFKPVNPKTRLSKVMRKNERENFARCMLLDVLDALSSFDCDIKIISTHPFKIESYDVVVDSRELDDAINSRIEGETAVIMSDIPLINSRILRRFFESEGDVVIAPGRKGGTNMIIIRDRKFKVRYYYCSFLRHLEFAKSLDLKCTVFDSFYASVDIDTPDDLLELMIHGEGKKSYEFLYSIGFRIKYEKEPKLVRISNTFP", "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": "MSTVFKKTSSNGKFSIYLGKRDFVDDVDTVEPIDGVVLVDPEYLEGRKLFVRLTCAFRYGRDDLDVIGLTFRKDLYVQTKQVAPAEPTSIQGPLTALQERLLHKLGVNAYPFTLQMVANLPCSVTLQPGPEDSGKPCGVDFEVKSFCAENLEEKIPKSDSVQLVVRKVQFSALEPGPGPSAQTIRSFFLSSQPLQLQAWMDREVHYHGEAISVHVSINNYTNKVIRRIKIAVVQTTDVVLYSLDKYTKTVFVQEFTETVAANSSFSQTFAVTPLLAANCQKQGLALDGKLKHEDTNLASSTILRPGMNKELLGILVSYKVRVNLVVSYGGILGGLPASDVGVELPVILIHPKPSPGERAVATSSEDIVIEEFMQHNSQTQS", "text": "FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins. SUBCELLULAR LOCATION: Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the arrestin family."}
{"protein": "MSGLLTDPEQRAQEPRYPGFVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRATFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSSCRVLHFFTRSKRLFTASLFTFTTQQTSLRLVWILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAGDTGTAIKWAQQLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKLRQSEVVFKPQKKCQEYEMSLENWAKAVKRSMNWYNKT", "text": "SIMILARITY: Belongs to the FGGY kinase family."}
{"protein": "MIKSIKGFNDILQVETATSRPSSEWRQLEAMLKQALDQFGYEEIRLPIVEETQLFARAIGDATDIVEKEMFSFTDKSDPPTPITLRPEGTAGAVRAVIEHNLLRGDSPKLWYMGPMFRYEQPQKGRYRQFHQLGVEAFGSEHVDVEAELIAMTYLMWQRLGIDHELSLEINSLGELDERKAYRSALVEFLQTKKEQLDEDSQRRLTTNPLRILDSKDPNTQALLMEAPRLADFLGEDSQAHFEQLKTYLTALGIEYVVNPNLVRGLDYYNKTVFEWVTDKLGSQATVCAGGRYDGLIGQLKSIGKSEDKAKAVKSEPAVGFAMGLERLLLLVQAVNPIQAQPACDVFVVVHPDLYQQGLLYAQSLRQARSDLRVKMASASSLKAQMKKADKSGAQLTVILAQDEVESGTISVKTMHTGEQVSQDKLWLHSAENFRL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MFYSKNAYLSMKEMTVNAQYILNYLLPRGWTKNAICGMLGNMQTESTINPGIWQNLDEGNTSLGFGLVQWTPATKYLNWADRNGLKRDHMDSQLKRILWEVDNNEQWINLRNMTFKEFTKSTKSANELAMIFLASYERPANPNQPERGTQAEYWFKTLTGKGSTGIQLAQFPMDIINITQGENGSFSHKGTLCIDFVGKHEKYPYYAPCDCTCVWRGDESAYLAWTSDKEVMCADGTVRYITWVCVHDENLLYNVGKKLKKGELMGHSGKGGRATGDHLHLNVIEGNKYQGWVKKPDSALAGTELHIYDVFAVNGVEIVNGLGYDWKTSDWVDGSDENNGDDKDKDKDETKNIVNLLLCGALNGW", "text": "FUNCTION: Essential for tail assembly and the production of infectious particles (By similarity). Degrades the peptidoglycan layer of the host cell wall and thereby facilitates infection of host bacteria. Acts probably as multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall (By similarity). SUBCELLULAR LOCATION: Virion Note=Located at the end of the tail structure. SIMILARITY: In the N-terminal section; belongs to the glycosyl hydrolase 24 family. SIMILARITY: In the C-terminal section; belongs to the peptidase M23B family."}
{"protein": "MADTSKDIEELIGIMARLPGLGPRSARRAVLTLIKKRGALMRPLAETMARVAESARECVNCGNIGTGDLCEICMDVRRATGEICVVEDVADLWAMERGQAFKGRYHVLGGTLSALDDVGPEDLRIPKLRARMADEGITEVILALNATVDGQTTAHYIADELAPTGVTLSSLAQGVPIGGELDYLDDGTISAALRARKSL", "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": "MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVIQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGMTANESGRLIDFLKDVIESMDKEEMEITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLASIDLKYFNESTRKKIEKIRPLLIDGTVSLSPGMMMGMFNMLSTVLGVSILNLGQKKYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFESGRIKKEEFAEIMKICSTIEELRRQK", "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": "MSNVGTTGRIPLWFIGVIAGIAALSIVGLFFYGAYSGLGSSL", "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": "MARGPKKHLKRLAAPSHWMLDKLSGTYAPRSSAGPHKLRESLPLVIFLRNRLKYALNGREVNAILMQRLVKVDGKVRTDSTFPAGFMDVIQLEKTGENFRLVYDVKGRFAVHRITDEEAAYKLGKVKRVQVGKKGIPYLVTHDGRTIRYPDPLIKVNDTVKIDLATGKITSFVKFENGNIVMTTGGRNMGRVGTITHRERHEGGFDIVHIKDALDNQFVTRLTNVFVIGEGNKSLISLPKGKGIKLSIAEERDARRAKQE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
{"protein": "MEERNEQVVEEVKEAQVEEAVTPENSEETVEEKSEAALLQEKVDELQAKLTETEGRTLRLQADFENYKRRVQMDKQAAEKYRAQSLVSDILPALDNFERAMQVEATDEQTKSLLQGMEMVHRQLLEALTKEGVEVIEAVGKQFDPNEHQAIMQVEDSEFESNAVVEEFQKGYKLKDRVIRPSMVKVNQ", "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": "MSLNRSEKQAVIDEVTGLAAKAQTLVMAEYRGITVADMTKLRSQARDKGVNLSVLKNTLARRAVAGSAFEVVSDQMTGPLIYGFSTDAVAAAKVVADFAKTNDKLVIRGGAFAGKFLDVNGVKQLANIPSKEVLLAQVCGLLMSPMSRTAVVLGALAAKKGGGAAETPAPAEAVAA", "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": "MKRPALILICLLLQACSATTKELGNSLWDSLFGTPGVQLTDDDIQNMPYASQYMQLNGGPQLFVVLAFAEDGQQKWVTQDQATLVTQHGRLVKTLLGGDNLIEVNNLAADPLIKPAQIVDGASWTRTMGWTEYQQVRYATARSVFKWDGTDTVKVGSDETPVRVLDEEVSTDQARWHNRYWIDSEGQIRQSEQYLGADYFPVKTTLIKAAKQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: To E.coli YmcC."}
{"protein": "MQNPTQTMHIYDMPLRVIAGLSTLAKTTEEDDNTSTGIVVSEVGEPQVVNHPAWIDPFVAYQLRAPRKNITPDFIFGRADIGNAFSAFLPRRFSAPAVGTRLVVDPVFTYQQRTVLGLYNYFHADFYYIVHVPAPLGTGIYLKIYAPEFDTTTVTRGIRFKPSASPTIALSVPWSNDLSTVETSVGRVGQSGGSIVIETIEDNSNETVNTPLSITVWCCMANIKATGYRHADTSAYNEKGMNFISVPVPKPPVPPTKPITGEEQADNEVTAEGGKLVQELVYDHSAIPVAPVVETQAEQPEVPVSLVATRKNDTGHLATKWYDFAKISLSNPANMNWTTLTIDPYNNVTLSRDGESMVLPWRRNVWTTGSKSIGYIRTMVAQINIPRPPQISGVLEVKDSINNSSISLVEFGGKVEIPIIPKVMNGLATTASLPRHRLNPWMRTAESKVELQYRIIAFNRTSDIADLNVSVLLRPGDSQFQLPMKPDNNVDTRHFELVEALMYHYDSLRIRGEEQSLPENAPNAVSNPQQFITPATALSAEEYNVHEALGETEELELDEFPVLVFKGNVPVDSVTSIPLDLATIYDFAWDGEQNAISQKFQRFAHLIPKSAGGFGPVIGNYTITANLPTGVAGRILHNCLPGDCVDLAVSRIFGLKSLLGVAGTAVSAIGGPLLNGLVNTAAPILSGAAHAIGGNVVGGLADAVIDIGSNLLTPKEKEQPSANSSAISGDIPISRFVEMLKYVKENYQDNPVFPTLLVEPQNFISNAMTALKTIPIEVFANMRNVKVERNLFDRTVVPTVKEATLADIVIPNHMYGYILRDFLQNKRAFQSGTKQNVYFQQFLTVLSQRNIRTHITLNDITSCSIDSESIANKIERVKHYLSTNSSGETTEEFSRTDTGLLPTTTRKIVLGESKRRTERYVAETVFPSVRQ", "text": "FUNCTION: ORF4 polyprotein codes for VP4a, VP4b, and VP4c, three of the four proteins that self-assemble to form the icosahedral capsid. The capsid is made of VP3 (coded by ORF3), VP4a, VP4b and VP4c. SUBCELLULAR LOCATION: Virion."}
{"protein": "PPPPPPQQFPQFHVRSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFSKKTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPKAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH", "text": "FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (By similarity). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE- containing transcripts. Phosphorylates CEP131 in response to cellular stress following ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (By similarity). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
{"protein": "MNRSLYRTRIKFCGMTRAGDIRLAGELGVDAVGFIFAHGSPRRVAPAEARAMRQATAPMVDVVALFRNNSKEEVREVVRTVRPTLLQFHGEEDDAFCRSFNLPYLKAVPMGSSGVNGEDANARTLQLSYPNTAGFLFDSHAPGAGGGTGKTFDWSRLPTGLHRPFLLAGGINADNVFDAIVATLPWGVDVSSGVELAPGIKDGHKMRKFVEEVRRADCHDMS", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEIKDVEPDVFKEMMCFIYTGKASNLDKMADDLLAAADKYALERLKVMCEEALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVMETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS", "text": "FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the Tdpoz family."}
{"protein": "METGFPAIMYPGSFIGGWGEEYLSWEGPGLPDFVFQQQPVESEAMHCSNPKSGVVLATVARGPDACQILTRAPLGQDPPQRTVLGLLTANGQYRRTCGQGITRIRCYSGSENAFPPAGKKALPDCGVQEPPKQGFDIYMDELEQGDRDSCSVREGMAFEDVYEVDTGTLKSDLHFLLDFNTVSPMLVDSSLLSQSEDISSLGTDVINVTEYAEEIYQYLREAEIRHRPKAHYMKKQPDITEGMRTILVDWLVEVGEEYKLRAETLYLAVNFLDRFLSCMSVLRGKLQLVGTAAMLLASKYEEIYPPEVDEFVYITDDTYTKRQLLKMEHLLLKVLAFDLTVPTTNQFLLQYLRRQGVCVRTENLAKYVAELSLLEADPFLKYLPSLIAAAAFCLANYTVNKHFWPETLAAFTGYSLSEIVPCLSELHKAYLDIPHRPQQAIREKYKASKYLCVSLMEPPAVLLLQ", "text": "FUNCTION: May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily."}
{"protein": "MSEIKLNYHKTRFLTSAANIKQLPEDSGIEIAFAGRSNAGKSTALNALTNQKNLARTSKTPGRTQLINLFEVEPNCKLVDLPGYGYAAVPEQMKLQWQKSLGEYLQKRECLGGVVILMDIRHPLKALDQQMIEWAVSADLPLLLLLTKADKLSQSARSKTVKMVREAILPFQGDIQVETLSAQNKLGVDRLSAKLDAWFAPNFATE", "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": "MKKKLVSRLSYAAGAFGNDVFYATLSTYFIVFVTTHLFNAGDHKMIFIITNLITAIRIGEVLLDPLIGNAIDRTESRWGKFKPWVVGGGIISSLALLALFTDFGGINQSKPVVYLVIFGIVYLIMDIFYSFKDTGFWAMIPALSLDSREREKTSTFARVGSTIGANLVGVVITPIILFFSASKANPNGDKQGWFFFALIVAIVGILTSITVGLGTHEVKSALRESNEKTTLKQVFKVLGQNDQLLWLAFAYWFYGLGINTLNALQLYYFSYILGDARGYSLLYTINTFVGLISASFFPSLAKKFNRNRLFYACIAVMLLGIGVFSVASGSLALSLVGAEFFFIPQPLAFLVVLMIISDAVEYGQLKTGHRDEALTLSVRPLVDKLGGALSNWFVSLIALTAGMTTGATASTITAHGQMVFKLAMFALPAVMLLIAVSIFAKKVFLTEEKHAEIVDQLETQFGQSHAQKPAQAESFTLASPVSGQLMNLDMVDDPVFADKKLGDGFALVPADGKVYAPFAGTVRQLAKTRHSIVLENEHGVLVLIHLGLGTAKLNGTGFVSYVEEGSQVEAGQQILEFWDPAIKQAKLDDTVIVTVINSETFANSQMLLPIGHSVQALDDVFKLEGKN", "text": "FUNCTION: Responsible for transport of beta-galactosides into the cell, with the concomitant uptake of protons (symport system), and also for transport of homologous and heterologous exchange of beta-galactosides. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the sodium:galactoside symporter (TC 2.A.2) family."}
{"protein": "MSSSQDKANLPANNSRARAKKLVLELQDEICAGLETIDGEGKFLEESWERPEGGGGRSRVLKDGKIFEQGGVNFSEVHGNELPPSIISQRPEAKGHSWFATGTSMVLHPKNPYIPTVHLNYRYFEAGPVWWFGGGADLTPFYPYLSDTRHFHSCHKNACDTIDKDLHKVFKPWCDEYFFLKHRNETRGVGGIFYDYQDGSGLLYKGQNANGKASKIAKELGEYSLNWENLFSLAKACGQAFLPSYEPIIKKRKNQSFSTKERDFQLYRRGRYAEFNLVWDRGTIFGLQTNGRTESILMSLPPLARWEYGYKPEENSREALLTDLFTKPQDWFTDKSLEKRCLTHQALD", "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": "MKFAVFASLLASAAAFAPAQQSARTSVATNMAFESELGAQPPLGFFDPLGLVADGDQEKFDRLRYVELKHGRISMLAVVGYLVQENGIRLPGDIDYSGTSFASIPNGFAALSTISTAGIAQIVAFIGFLEIAVMKDITGGEFPGDFRNDYIDFGWDSFDEETQFKKRAIELNQGRAAQMGILALMVHEKLGVSLIPN", "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. In chromophytic algae, LHC is associated with photosystem II, energy being transferred from fucoxanthin and chlorophyll C 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": "MLSQSTLFLLLLMAIALIAKNQSLIIAISVLLLIKWTGLGDKVFPLMQAKGINLGVTIITIAVLVPIATGDIGFKQLGEATKSLYAWVALGSGIAVALVAASGIDLLKNDPHITAALVLGTIVAVSFLNGVAVGPLIGAGIAYLTMRAIQYIAQLWG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0756 family."}
{"protein": "MQIQPHPSGALLLLLLSNLLMWENVASVPRCIMENGGCQKVLNYLFNMTSTISESFNTLSSETLNDFYTEFDPHQTFQNRPAMTCHTSSRSIPNNKRKAERMEPAALLNVIIRMLASWKNLLYHVENNMANLDGTPYAIISKVKLIDRQIKKLTKNLQDIKTILSQVHPELKEKENYPVWSGEPYVQKSKRRTQLFGLHSLFFCLYSDAEKVSDYVNILRNKIVPNE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MQNDQDYGNKLNPAWDEKGLITAVLTDAKTGLLLMVAHMNKESFELSMATKEATFWSRSRKKIWRKGEESGHVMKIQEIRIDCDQDTLWLKVIPMGPACHTGAQSCFYRLVEDGHLVTIPKDKI", "text": "FUNCTION: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-CH family."}
{"protein": "MTADRWAGRTVLVTGALGFIGSHFVRQLEARGAEVLALYRTERPQLQAELAALDRVRLIRTELRDESDVRGAFKYLAPSIDTVVHCAAMDGNAQFKLERSAEILDSNQRTISHLLNCVRDFGVGEAVVMSSSELYCAPPTAAAHEDDDFRRSMRYTDNGYVLSKTYGEILARLHREQFGTNVFLVRPGNVYGPGDGYDPSRGRVIPSMLAKADAGEEIEIWGDGSQTRSFIHVTDLVRASLRLLETGKYPEMNVAGAEQVSILELARMVMAVLGRPERIRLDPGRPVGAPSRLLDLTRMSEVIDFEPQPLRTGLEETARWFRHHTR", "text": "FUNCTION: Catalyzes the stereospecific reduction of the C-4 keto group of dTDP-4-dehydro-6-deoxy-D-allose, leading to dTDP-6-deoxy-D-allose, an intermediate in the biosynthesis of the mycinose moiety of the chalcomycin antibiotic. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MVNQNKIIPYLFLVPALVFLLFVYIPIFENVFLSLFQWSSFSPEKTFIGLKNYVELFHDPVFYQALTNNVLYAVISIVCQVFGGLILAAVLEDKLVRKWSPFFRTVFFLPVVISMTVIALLFDFIYNPETGLLNQLLQAIGLDQLTRAWLGDDSTAMLSVIFVSQWQSVGYIAMLYIVSIQKIPDELYEAARLDGAGKIQQFFHITVPQTKEMSFVAVVMTLTGAFTVFNEPYILTGGGPGKASEVLSTFLYKSAFTKDMMGYASAIATVVLIITLALSLMQMKFFKTGKEE", "text": "FUNCTION: Probably part of the binding-protein-dependent transport system YurMNO. 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. MalFG subfamily."}
{"protein": "MRNYELMTVFPVEEDLYKPGIDALHSILADFGVQIKSEEPFGDRDLAYEIKKKTKGRYVLFNIEADPAKMIELDKRFKLITQMLTYLFVRLED", "text": "FUNCTION: Binds together with bS18 to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family."}
{"protein": "MSKVVHFDASKLTPFVHENELKEMQAMVTAADQELREGTGAGSDFRGWIDLPINYDKDEFDRIKKAAKKIQNDSEVLVGIGIGGSYLGAQASIEFLNSSFYGREKEKYPTVVFCGNSLSGSYLYDLLEWLGDKDFSINIISKSGTTTEPSIAFRVLKDKLIKKYGKEEAAKRIYATTDRAKGALKTEADAEGYEEFVVPDDIGGRFSVLSAVGLLPIAVAGGDIDAMMKGAADARAAYTDPDVLKDSPYQYAAMRNILYRKGYTTELLENYEPSLRMFGEWWKQLMGESEGKDQKGIYPSSANFTTDLHSLGQYIQEGRRNLMETVIRVEHPTHDVTIPDDKENLDQLNFLSGKTMNYVNDRAYEGVVLAHTDGGVPVMTVDIENQTAHTLGYLIYWFELAVGISGYLNGINPFNQPGVESYKRNMFGLLNKPGYEDLHDDLTKRLK", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MIDIAFSKLAIIGVAALVFIGPEKLPTVARMAGTLFGRAQRYINDVKSEVSREMELDELRKMHKDVQDAATDVERSIAQNISAADSSLHSAWDESDTDTNPLMEPPTLDQSSDKSKNFRKKKLAATSAVPSWYKRQSGQKSRVISGAARMAKFRPASARKSTPFFH", "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": "MNKMQGKKKKKEEEEEEERIIPPELWKLIIEQYKRQLAKTDVMKVSETVKLHEEKIKEKVPTDHIIHAQKPNAWVEETKKSGGCLLV", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. This major G-protein of the squid photoreceptor is involved in visual transduction. 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": "MVDEGILREVYRVLEDRRDRPIDSYTSRLMRDDDKMAEDKILEKIGEEAAEVIIASKNDENLVEEAADLIFHTLLLLVYKGVPLDSLLEEFAARRK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MQGTKNNIYTVSRLNGEVRQILEGQLGKIWLNGEISNFSSPSSGHWYLTLKDHSSQIRCAMFKGRNQTVSFKPINGQQVLVKGAISVYEPRGDYQLLIESMLPAGDGLLAQQFDALKMKLAAEGLFAADTKRPLPKNIQRIGVITSPTGAAIRDVLHVLARRDPSIEVIIYPTQVQGETAAQSICQAINIANQRLEVDVLLLTRGGGSLEDLWCFNSEALAHTIYNSALPVVSAVGHEVDTTISDYVADIRAPTPSAGAELLSQDSDNKAQKLATALSRLQQSAKHYQLKQERRLSLLEHRLQRQDPKRTLQQFEQRFDEMQLRLESALLNRLHILSRRQQLLASRLEQQSPKHKLTIEGNRLSYLASRLQDALQDKLSQSEQRIKYAAHQLETVSPLATLSRGYSITTDIHNQVVDSADKLTIGDSLQTRLRHGQVISTVTQIKPLE", "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": "MKTLDINQIKQYLPHRYPLLLVDRVLNWESGKSITAIKNVTVNEEFFNGHFPHKPVMPGVLMIEALAQTAALLSFLTMGQKPDDNSVVYFIGIDGARFKRPVEPGDQLKMEVEILRNARGIWKYKATGSVDGQLALEAELMCTMRTINDASPAAGQ", "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": "MRVEICIAKEKITKMPNGAVDALKEELTRRISKRYDDVEVIVKATSNDGLSVTRTADKDSAKTFVQETLKDTWESADEWFVR", "text": "SIMILARITY: Belongs to the DinI family."}
{"protein": "MARYTEANCRLCRREGLKLYLKGDRCYTDKCAFSRRGYAPGQHGQSRKKISNYGLQLREKQKAKRIYGVLEKQFRTYYKRADKARGITGENLLVLLEMRLDNVVYRLGYGDSRKESRQLVTHGHFLVNGKKVNIPSFNVSVNDVITVSEKSRATEKFKTFIENPRTLPNWLEGNLENFEGKVVSQPSREDIDVPVNETLIVELYSK", "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": "MKMDSAVSEEAFERLTAKLKARVGGEIYSSWFGRLKLDDISKSIVRLSVPTAFLRSWINNHYSELLTELWQEENPQILKVEVVVRGVSRVVRSAAPAETCDNAEAKPAVTPREKMVFPVGQSFGGQSLGEKRGSAVVAESAAATGAVLGSPLDPRYTFDTFVDGASNRVALAAARTIAEAGSSAVRFNPLFIHASVGLGKTHLLQAIAAAALQRQEKARVVYLTAEYFMWRFATAIRDNNALSFKEQLRDIDLLVIDDMQFLQGKSIQHEFCHLLNTLLDSAKQVVVAADRAPSELESLDVRVRSRLQGGVALEVAAPDYEMRLEMLRRRLASAQCEDASLDIGEEILAHVARTVTGSGRELEGAFNQLLFRQSFEPNISIDRVDELLGHLTRAGEPKRIRIEEIQRIVARHYNVSKQDLLSNRRTRTIVKPRQVAMYLAKMMTPRSLPEIGRRFGGRDHTTVLHAVRKIEDLVGADTKLAQELELLKRLINDQAA", "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": "MKVFYDKDCDLSLIKGKTVAIIGYGSQGHAHAQNLNDSGVKVVVGLRKGGASWDKVGKAGLTVKEVNDAVKEADVVMILLPDEQIAEVYKNNVEPHIKQGASLAFAHGFNVHYNQVVPRADLDVWMVAPKAPGHTVRNTYTQGGGVPHLVAVHQDKSGKARDLALSYAMANGGGKAGIIETNFKEETETDLFGEQAVLCGGAVELIKMGYETLVEAGYAPEMAYFECLHELKLIVDLIYEGGIANMNYSISNNAEFGEYVTGPEVINEQSRAAMRNALKRIQNGDYAKMFIQEGRLNYPSMTARRRNTADHSIEVVGAQLRAMMPWIAKNKLVDQTRN", "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": "MKLHELKPAAGSKKAPKRIGRGTGSGLGRNAGKGEKGQNARSGGGVRPGFEGGQMPLYRRLPKRGFTNIFAKKIVSINLDRLNIFENGTEVTPELLLERRVVSKVLDGVKILGNGTLEKSLTVKGCKFSKSAIEKIEAAGGKVEVM", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MTTRTIDNIRNFSIVAHIDHGKSTLADRLIQQTGTVALRDMSEQMLDSMDIERERGITIKANTVRLEYKAEDGQDYVLNLMDTPGHVDFAYEVSRSLAACEGSLLVVDASQGVEAQTLANVYQALDANHEIVPVLNKVDLPAAEPDRVKEQIEEVIGLDASEAVPISAKTGLNIEAVLEAIVKRLPPPKGDREAPLKALLVDSWYDVYLGVVVLVRIVDGVLKKGMTIRMMGADAAYGVDRIGVFRPKMADIGELGPGEVGFFTGSIKEVADTRVGDTITEDKRQTTQMLPGFKEVQAVVFCGLFPVDAADFENLRGAMGKLRLNDASFSYEMETSAALGFGFRCGFLGLLHLEIIQERLEREFNLDLISTAPSVVYRLMMRDGELKELHNPADMPDPMKIETVEEPWIRATILTPDDYLGGVLKLCQDRRGIQIDLNYVGKRAMVVYDLPLNEVVFDFYDRLKSISKGYASFDYHVSDYREGDLVKMSILVNAEPVDALSMLVHRTRAESRGRAMCEKLKDLIPRHLFQIPVQAAIGGKIIARETIRALSKDVTAKCYGGDISRKRKLLDKQKEGKKRMRQFGRVEIPQEAFIAALKMDD", "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": "MTTEITRPPAPPSRPSESRKPSLPGLLHLVAIAAVLATIVSAWAIDFVPTALIDGSDNIVALLQRMIPPRLDDPARIGMLAVETLLMAVLGTTLAAIASVPLAFLAARNTTPHPAVQAVARAVITFCRAMPDLLFAVLFVRALGIGVLPGVLALALHSIGMLGKVFADAIEQTDAGPREAVRSTGVGYFRELLNAVVPQVVPSWIAMFVYRIDINLRMSVVLGFVGAGGIGFALQDALRGLIYPRALGIVCVILVIIAGMELLAIAIRRILLDPSRSNPLRDRIARFGLSGVLVGSCVAAFVLLKINPLALFTWVFPSVGIFTRMVPPNFDALGVDLFTAAAQTVAIGVVATAIGIALSIPAGILAARNVSPHPALYWPARAWILVVRAVPELILAVVFVAALGLGPIAGTCALAIGSIGFLAKLVADAVEEIDPGPMEAVRSVGGGWWKTLFAAVLPQSMPALVGSSLYLFDVNVRTSTILGIVGAGGVGYLLFESIRTLNFDVAGAIVIVIFVIVYAIERLSGWIRSRLV", "text": "FUNCTION: Part of the ABC transporter complex PhnCDE involved in phosphate 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": "MIEKAGILIEALPYIRRFYGKTVVIKYGGNAMVAEELKESFAKDIVLMKYIGINPVVVHGGGPQIGRMLKRIGKESDFCAGMRVTDADTMDIVEMVLAGKINKEIVSLINRHGGHAVGLSGKDGNLIEARKLHVYRYKGDDQPPEIIDIGLVGEVNRVNVSILDTLAGGNLIPVIAPVGVGEQGETYNINADLVAGHIAGALQAAKLVLMTDVEGVLDGGGNLISSLTVAEAADALQDETLKGGMIPKVQCAIDALQSGVDKVHIVDGRVPHAILLEIFTDAGVGTEIVRYRRGQSVG", "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": "MKKSTLALVVMGVVASASVHAAEVYNKNGNKLDVYGKVKAMHYISDDDTKDGDQTYVRFGFKGETQINDQLTGYGRWEAEFAGNKAESDSSQKTRLAFAGLKLKDFGSLDYGRNLGALYDVEAWTDMFPEFGGDSSAQTDNFMTKRASGLATYRNTDFFGAIDGLDMTLQYQGKNENRDAKKQNGDGFGTSLTYDFGGTDFAVSGAYTNSDRTNAQNLLARAQGQKAEAWATGLKYDANDIYLAAMYSETRNMTPISGGFANKAQNFEVVAQYQFDFGLRPSLGYVQSKGKDNEGIGDEDLVKYIDVGATYYFNKNMSAFVDYKINQIDDDNKLGVSSDDIVAVGMTYQF", "text": "FUNCTION: Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Gram-negative porin family."}
{"protein": "MQRINREESFRAKEERLKDLFVRGLSGNNAAYQTFLGELSSYLRAFLRKRLIRLPDEVEDLVQEALLAVHNQRHTYDPSQPLSAWVQAIARYKLVDLFRRRAIYEQRNDTLDDGMDLFSSADAEAAEARRDLNKLLADLPDHFRLPIMHTKLEGLSVREAADVSGMSESAIKVGVHRGLKALAAKIRGAL", "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 (NrsF in this case) until they are released (Probable). Regulates expression of only a few genes (Dsui_0154 to Dsui_0159) in response to (hypo)chlorite, conferring resistance to reactive chlorine species (RCS) during oxic growth (PubMed:25968643). SUBCELLULAR LOCATION: Cytoplasm Note=Tightly associated with the inner cell membrane via NrsF which holds it in an inactive form until it is released (By similarity). SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily."}
{"protein": "MAEQLPEPVLLSELLHMDKVTIAGQLVEFRHVFYTWIAMLILFIVGLIVRRKLTLVPGRLQNFFEVLISSFENFTVINIGEEGRKFFPVLIGIFLLIAVENLLGLIPLCDAPTANINTNIGMAIFVFLYYNYEGIKKWGFHYIHHFMGPSIVLAPFMIILECISHLARPLSLTLRLFGNIKGEEIVLLLFFLMAPLVGTIPVYFLFLLAKLLQAFIFYILTLIYLKGALESAH", "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": "MTVAISAAVQQLPHGQGLALPAYQSAHAAGLDLLAAVAPDAPLVLAPGTYALVPTGLTLALPPGYEAQVRPRSGLAARHGVTVLNAPGTIDADYRGEIGVLLINHGSQPFTVRRGERIAQMVVARVARVDLTVAASLETTERGSGGFGSTGR", "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": "MDKKQLLRNLPKIDELLKEEIVNGYLQENSRTLVVDSLRQSIDHYRGEILKNNIDSFTKENVVNYFIDTLEENKSTKFKKVINATGVVIHTNLGRSLLAKEAIENVVKVSENYSNLEYDLKEGKRGSRYSHVEELIKKVTGAEAAMVVNNNAAAVMLALNTLCEEREAIVSRGQLVEIGGSFRVPDVMKFSRAHLVEVGTTNRTHLYDYENNINENTGVLLKVHTSNFKIMGFTEEVSSEEMVQLGGKYKLPVMEDIGSGTLVDFSKYGFTYEPTVQSSLEKGVDVVTFSGDKMLGGPQAGIIVGKKKYIDKMKKNQLTRALRIDKMTLAALEGTLKCYIDEKEAIENIPTLNMILSSEDIHKKRAQRLKRRLQNNVKDFNFKVSEDLSMVGGGSMPGERIPTYVVKVNSDKITAEKIEEKLRLSKNPIIVRVSKDEVILDVRTLFERDFNIIVEEFKKLLK", "text": "FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SelA family."}
{"protein": "MDSSTLSPAVTATDAPIQSYERIRNAADISVIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAAAGIAMGGFEWNALVFVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGKRIQIYLSVLSLLLYIFTKISADIFSGAIFINLALGLDIYLAIFILLAITALYTITGGLAAVIYTDTLQTAIMLVGSFILTGFAFREVGGYEAFMDKYMKAIPTLVSDGNITVKEECYTPRADSFHIFRDPITGDMPWPGLIFGLSILALWYWCTDQVIVQRCLSAKNMSHVKAGCTLCGYLKLLPMFLMVMPGMISRILYTDKIACVLPSECKKYCGTPVGCTNIAYPTLVVELMPNGLRGLMLSVMMASLMSSLTSIFNSASTLFTMDIYTKIRKGASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFCKRVNEPGAFWGLILGFLIGISRMITEFAYGTGSCMEPSNCPKIICGVHYLYFAIILFAISVVTVLVISLLTKPIPDVHLYRLCWSLRNSTEERIDLDAGEEEPVEEDPKDTIEIDAEAPQKEKGCFRKAYDLFCGLDQDKGPKMTKEEEEAMKLKMTDTSEKPLWRTVVNINGIILLAVAVFCHAYFA", "text": "FUNCTION: Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (By similarity). Has a primary role in the transport of dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception (By similarity). Acts as a water channel enabling passive water transport in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity comparable to aquaporins and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
{"protein": "MCGGCVQQEYPDRGSTCLETGSYLLNYVSCVQCNKRDFVLIVNKTAAEEDGEEIITYDHMCKNCHHVIAKHEYTFSVVDDYQEYTMLCMLCGRAEDSVSVLPDDPRQMAPLF", "text": "FUNCTION: Transcriptional activator that mediates FGF signaling during neural development (By similarity). Plays a role in the regulation of cell movement (By similarity). Does not bind DNA by itself (By similarity). SIMILARITY: Belongs to the Churchill family."}
{"protein": "MKFKSLITTTLALGVIASTGANLDTNEASAAAKQIDKSSSSLHHGYSKIQIPYTITVNGTSQNILSSLTFNKNQQISYKDIENKVKSVLYFNRGISDIDLRLSKQAKYTVHFKNGTKRVVDLKAGIHTADLINTSDIKAISVNVDTKKQVKDKEAKANVQVPYTITVNGTSQNILSNLTFKKNQQISYKDLENNVKSVLKSNRGITDVDLRLSKQAKFTVNFKNGTKKVIDLKAGIYTANLINTGGIKNININVETKKQAKDKEAKVNNQVPYSINLNGTTTNIQSNLAFSNKPWTNYKNLTTKVKSVLKSDRGVSERDLKHAKKAYYTVYFKNGGKRVIHLNSNIYTANLVHAKDVKRIEVTVKTVSKVKAERYVPYTIAVNGASNPTLSDLKFTGDSRVSYSDIKKKVKSVLKHDRGIGERELKYAEKATYTVHFKNGTKKVINLNSNISQLNLLYVKDIKNIDIDVKTGAKAKVYSYVPYTIAVNGTTTPIASKLKLSNKQLIGYQDLNKKVKSVLKHDRGINDIELKFAKQAKYTIHFKNGKTQVVDLKSDIFTRNLFSVKDIKKIDINVKQQSKSNKALNKVTNKATKVKFPVTINGFSNLVSNEFAFLHPHKITTNDLNAKLRLALRSDQGITKHDIGLSERTVYKVYFKDGSSKLEDLKAAKQDSKVFKATDIKKVDIEIKF", "text": "FUNCTION: Both native and recombinant protein bound to labeled vitronectin, fibrinogen, recombinant osteopontin and fibronectin. It was also shown to be able to bind to a 15-amino acid synthetic peptide of vitronectin. Map could affect the severity of arthritis and osteomyelitis in mice through a T-cell-mediated mechanism and could play a role in abscess formation through a T-cell-independent mechanisms. It could potentiate the survival of the bacterium by modulating host immunity."}
{"protein": "MARKNAQAEDLSNVEFETSEDVEVIPTFNAMNLKEELLRGIYAYGFEKPSAIQQRSITPIVKGRDVIAQAQSGTGKTATFSISILQSLDTTLRETQVLCLSPTRELAVQIQKVILALGDMMNVQCHVCIGGTNLGEDIRKLDYGQHIVSGTPGRVFDMIKRRVLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERDEIMKEFRAGQSRVLITTDVWARGIDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKSDDIRILRDIEQYYSTQIDEMPMNVADLI", "text": "FUNCTION: ATP-dependent RNA helicase (PubMed:22961380). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:14973490, PubMed:22961380). Involved in exon definition of genes containing long introns, including the rolled/MAPK gene (PubMed:20946982, PubMed:20946983). Has a role in oskar mRNA localization at the posterior pole of the developing oocyte (PubMed:14973490). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family."}
{"protein": "MDPAAFVQALADHGIVLNDHQQDQFAAYYQYLISENEKMNLTGITAEGDVYLKHFYDSLTLALVLPELQTQVMSVCDVGAGAGFPSIPLKIAFPQLKITIVDSLQKRIGFLERLTARLELTDVQLFHDRAEAFGAKKSPHRASFDLVTARAVAALDVLAELCLPLVKPQGRFVAMKAAATPAELIAAKSAIGLLGGKLAQDAALTLPETGDPRHLLVIDKVKPTPNKYPRKPGIPNKQPLGGA", "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": "MADKRKLQGEIDRCLKKVSEGVEQFEDIWQKLHNAANANQKEKYEADLKKEIKKLQRLRDQIKTWVASNEIKDKRQLIDNRKLIETQMERFKVVERETKTKAYSKEGLGLAQKVDPAQKEKEEVGQWLTNTIDTLNMQVDQFESEVESLSVQTRKKKGDKDKQDRIEGLKRHIEKHRYHVRMLETILRMLDNDSILVDAIRKIKDDVEYYVDSSQDPDFEENEFLYDDLDLEDIPQALVATSPPSHSHMEDEIFNQSSSTPTSTTSSSPIPPSPANCTTENSEDDKKRGRSTDSEVSQSPAKNGSKPVHSNQHPQSPAVPPTYPSGPPPAASALSTTPGNNGVPAPAAPPSALGPKASPAPSHNSGTPAPYAQAVAPPAPSGPSTTQPRPPSVQPSGGGGGGSGGGGSSSSSNSSAGGGAGKQNGATSYSSVVADSPAEVALSSSGGNNASSQALGPPSGPHNPPPSTSKEPSAAAPTGAGGVAPGSGNNSGGPSLLVPLPVNPPSSPTPSFSDAKAAGALLNGPPQFSTAPEIKAPEPLSSLKSMAERAAISSGIEDPVPTLHLTERDIILSSTSAPPASAQPPLQLSEVNIPLSLGVCPLGPVPLTKEQLYQQAMEEAAWHHMPHPSDSERIRQYLPRNPCPTPPYHHQMPPPHSDTVEFYQRLSTETLFFIFYYLEGTKAQYLAAKALKKQSWRFHTKYMMWFQRHEEPKTITDEFEQGTYIYFDYEKWGQRKKEGFTFEYRYLEDRDLQ", "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. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of embryonic stem (ES) cell identity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, P-body Note=NANOS2 promotes its localization to P-body. SIMILARITY: Belongs to the CNOT2/3/5 family."}
{"protein": "MKLLALLSLLILMLQEARTASLSEEREGDPYAILHLGDYVLSLDNYDEVIDPSNYDELIDYGDQLPQVKGTSLASLTRTRFTQSTEAARTLPSNPTTARPPTLGLLAAPANHGLPTCLICVCLGSSVYCDDADLENIPPLPQTTAYLYARFNRISHIRAGDFKGLTKLKRIDLSGNSISSIDDKALRLLPALRDLILPENKLVALPTLPTSIEVLDVRMNRLQSSGIQPEAFRALEKLQFLYLADNLLDAIPPSLPLSLRSLHLQNNMIETMQRDAFCDAEEHRHTRRPLEDIRLDGNPINLSLFPSAYFCLPRLPTGRFV", "text": "FUNCTION: Inhibits angiogenesis in the vitreous humor of the eye, and therefore represses neovascularization (By similarity). Binds collagen fibrils (PubMed:12951322, PubMed:10636917). May be involved in collagen fiber organization via regulation of other members of the small leucine-rich repeat proteoglycan superfamily (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class III subfamily."}
{"protein": "MSESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSPVKVLAEEKGLPVFQPVSLRPQENQQLVADLQADVMVVVAYGLILPKAVLEMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAETGVTIMQMDVGLDTGDMLYKLSCPITAEDTSGTLYDKLAELGPQGLITTLKQLADGTAKPEVQDETLVTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLEIEGQPVKVWKASVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDLLNSRREWFVPGNRLV", "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": "MNHSETITIECTINGMPFQLHAVPGTPLSELLREQGLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKPLTITEIRRGLAGNLCRCTGYQMIVNTVLDCEKTK", "text": "FUNCTION: Iron-sulfur subunit of the xanthine dehydrogenase complex."}
{"protein": "MNVKTTYRRVFLIVMDSVGIGEAPDAEKYNDKGADTLGHIAEYRGGLYMPNMAKLGLSHIREIKGVPKVERPLAYYTKMKEASAGKDTMTGHWELMGLRIDKPFRVFPNGFPDELIAELERRTGRNVIGNKPASGTAIIEELGEEHMKTGAIIVYTSADSVLQIAAHEQVVPLDELYRICEIARELTRDEPYMVGRVIARPFIGKPGHFERTANRHDYALKPFGKTVMNELKDAGYEVIAIGKIADIYDNEGVTQSLRTTSNMDGMDKLVDTLGMDFTGLSFVNLVDFDAKYGHRRDPKGYGDALEEFDARLADVLPRLKEDDLLIITADHGNDPVHHGTDHTREYVPLLVYSPRFRGGKPLPVRETFADVGATIADNFQVNRPPYGTSFLADLA", "text": "FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of pentose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphopentomutase family."}
{"protein": "MTKPVVAIVGRPNVGKSTIFNRIVGERVSIVEDTPGVTRDRIYSSGEWLTHDFNVIDTGGIELTDAPFQTQIRAQAEIAIDEADVIIFMVNQREGLTQTDEMIAQMLYKTNKPVVLAVNKVDNPEMRTDIYDFYALGFGEPFPISGSHGLGLGDLLDEVANNFKDEEDDDYDEDTIKLSLIGRPNVGKSSLVNAILGEDRVIVSNIAGTTRDAIDTEYSYEDQDYVLIDTAGMRKKGKVYESTEKYSVLRALKAIERSNVVLVVLDAEEGIIEQDKRVAGYAHEEGKAVVIVVNKWDTLDKDSKTMKKFEDKIRQEFQFLDYAPIAFVSAKEKQRLRTLFPLIKEASENHKKRVQSSTLNEVITDAISMNPTPTDKGRRLKVFYATQVAVEPPTFVVFVNDAELMHFSYKRYLENQIRDAFGFEGTPIRIIPRKRN", "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": "MIQISALPAFTDNYIWLLQDHRSQRCAVVDPGDAAPVLAWLEQHPGWVLSDILITHHHHDHVGGVERLKQHSAATVHGPAREKIPARDIGLEDNQRVSILGWEFEVFAVPGHTLGHIAYYHHGLLFCGDTLFAAGCGRLFEGTPEQMHHSLGRLAALPDDTLIYCTHEYTLSNLRFAQAVEPANPDIAERLAKVTQMREQGRMTLPSTLALEKLTNPFLRTGETSVKQKADERNGQDNQSQSAVFAALRAWKDKF", "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": "MSKINKLEHIRNIGICAHIDAGKTTTTERILYYTGKSHKIGEVHEGGATMDWMEQEQERGITITSAATTCRWQDKIINIIDTPGHVDFTIEVERSLRVLDGAVAVFDGVAGVEPQSETVWRQADKYNVPRMCFVNKMDRMGADFYRCVEMLKDRLGAKPLVIQLPVGIEENFKGIIDLIKMKAVIWKDEALGAEYFEEDIPADMKDKAEEYRAKLLDMVVELDDHVMEKYLSGEEVTAEEIKRLIRKGTISAAFYPVLCGSAFKNKGVQPLLDAVVDFLPSPIDIGIVKGMEVSTGEEKDFPISVTEPFAALAFKIMNDPFVGSLTFIRIYSGKITSGTTVINTVKNKREKIGRMLLMHANNREDVKEASAGDIVALAGLKDTTTGDTLSDIDQQVILERMEFPEPVIELAVEPKSTADQEKMGLALSRLAAEDPSFRVSTDYETGQTVIKGMGELHLEIIIDRMRREFKVEANIGAPQVAYRETITKVCEIDYTHKKQSGGAGQFARVKIIFEPLKEVKDLKDEDKNKIFVFESKIIGGAVPKEYIPGVEKGLNNIRETGVIAGYPMIDFKATLVDGAFHDVDSSVLAFEIAAKAAFREGMPKGNPKLLEPIMQVEVITPDEYMGDIIGDLNSRRGQIQSMDPRGNAQVVTANVPLAEMFGYVNTLRSLSQGRAQFSMIFSHYDQVPSQVADIIKAKK", "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": "MGSNLPAQPNLRVTIIAADGLYKRDVFRLPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNPNQANGLHRTQLGASTSSGLVPQVAPTPSVPQAGPSSVDQSAAASSASLNPQRVPSATRPTSQIAPPNGAPPIANGQGVPRPNLSSFEDNQGRLPAGWERREDNLGRTYYVDHNTRTTTWNRPSANYNEQTQRTQREANMQLERRAHQNRMLPEDRTGASSPNLSETQPQAQTPPAGGSGASNSNVVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNASGGNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLENDIEGIIDLTFTVDDEKFGERRTIELKPGGEDIPVTNENKHEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQEQDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPIALPKSHTCFNRLDLPPYKSHEVLEHKLSIAVEETLGFGQE", "text": "FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. Ubiquitinates 'Lys-528' of the uric acid/xanthine transporter uapA at the cell membrane, leading to its internalization, sorting into the endosomal pathway to the vacuolar lumen where it is eventually degraded. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RSP5/NEDD4 family."}
{"protein": "MDIQTFDHTKEENPKNLELITDILEFAGNYLHLDEETEISVTLMHNDEIHQINKEYRNVDRPTDVISFAINDADEDIIMDPEMAEEIPANIGDLMISVDKVAEQAEFLGHSYERELGFLCVHGFLHLNGYDHMEKEDQEKMFPLQKEIMNAYGLKR", "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": "MNIFRDKKTHINIATIGHFNHGKTTLSAAIAMTLANKKYRLDKKSIKVTLEEKNQGIGIYTHHFQYETTLRHYSHTDCPGHTDYINNMIAGISQVDSTILVVSAVDGSMSQTKEHLLIAKLLGISSFIVFINKEDQLDDDKFVYLVQKEISQFLMSHGFQTNKIPIVSGSALLALETLIQQPNVLRGENYWVDKIYTLIELLDSYIPKPKRKKDKHFLMWIDSVKFLPNIGPIAMGRIEQGTIKVGEFIDIVGFRETRTAKIISLEFFNQSCMQVLAGDDIGVSIEGTKNHNDIKKGMIISTPGTIKSWLEFEAQVYILKREEGGRTSPFFKGYCPQFFFKTTCVTGRIEAIEYTTGSKTWMIMPGDKLKIQVNLVYPIGIKKRMRFLIREGGVLVGVGIISNLIK", "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": "MKGLIYYMAMNDNNKTPQDPQANNWMKTLLIGGGIIAAMTLAVTFFDGNGGRDHNTTSVAYSEFLNRVDNNGVKDVTIGHDELSGHFTDNSAFKTVAPSDPLLVQRLQSKNVTFRALPEDTVSFWQILLSQFLLPFILFVGLGFLFVRQMQKNGGGGAMGFGKSRARLLTEKQGRVTFKDIAGIEEAREELEEIVDFLKDPTRFSRLGGKIPKGALLVGPPGTGKTLLARAIAGEAGVPFFSISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGNGNDEREQTLNQLLVEMDGFEANEGIIILAATNRPDVLDPALLRPGRFDRQVIVPRPDIEGRLKILQVHMKKTPLAPDVDVRTIARGTPGFSGADLANIVNEAALLAARKGKRLVAMSEFEEAKDKVMMGAERRSVIMTEEEKRSTAYHEAGHALVSLHIPGCDPLHKVTVIPRGRALGVTWNLPERDQLSINIKQMKARLALCFGGRIAEQLVYGEDSLNTGASNDIQQATDMARAMVTEYGMSPKLGWLRYRENQDEVFLGHSVSRSQNISEDTAKIIDQEVRVLVEEGESRARQVLTEHIDELHRLANALIEYETLSGEEAKRAIAGEKITTIEVKPQVTIPLSGGASGVPKSPPFNGWGNAAPQGA", "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": "MKKILIMAGGTGGHVFPGLALAEALADKQVKTVWLGTCNGMEKQWVDAAKIPFYTIAISGLRGNGLLGWLKAPFNVFKAWRQARYIIQQEAPDLVLGMGGFVCGPGGLAALSLNKPLVLHEQNATPGLTNKLLAPFAKKVICAFPQSTIKGKQVTVIGNPVRSGLESLPVVKAHSPRHLLVLGGSRGALALNEMVPEALSLLPEEQRPQVIHQTGQKTLQQAMSSYEAANVAADVVPFIDDMVSAYQQADLVVCRSGALTVSELMAAARPAILVPFPYAVDDHQTANAQALVDLNGGEVLQQADMTSELLAERLQFWMADKRCETASRSIRESAPHSAKEKIVDELLTLCDSSVH", "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": "MNKDLAAMRVGYAHQGADGRYVDSDLDADQLIGGWLPLMRLWLEDAVEAGVPEPNAMTLGTVDEHGHPCTRTVLCKGLSTDGVLFFTNYDSDKGRQLEAVPYASVTFTWVPVARQITVRGPVERVSAEVTDEYWHSRPRGSRLGAWASEQSKPIGSRAELDAALLHAAERFPVDVDIPVRPDWGGILIRPAVVEFWQGRANRMHNRIRTSLVDGSWTVERLQP", "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": "MNPLEQLVTQAQTDFAAAIDAAALENAKAKYLGKTGQITEQMKSLGKLAPEERKAQGAVINSAKEKIEAALTARRDALSNAQMEARLNAEAIDITLPGRGRGTGGIHPVMRSWQRVEEIFGSIGFDVADGPEIENDWTNFTALNSPENHPARSMQDTFYIEGKDTQGKPLLLRTHTSPMQVRYARMNKPPIKVIAPGRTYRVDSDATHSPMFHQVEGLWIDENISFADLKGVYLNFVKAFFETDDLQVRFRPSYFPFTEPSAEIDIAFGSGPLKGRWLEVSGAGQVHPTVLRNMGFDPEQFIGFAFGSGLERLTMLRYGINDLRLFYEGDLRFLKQFN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD", "text": "FUNCTION: [Isoform 2]: Induces ICE-like proteases and apoptosis. FUNCTION: [Isoform 3]: Does not induce apoptosis. FUNCTION: [Isoform 1]: Induces ICE-like proteases and apoptosis. FUNCTION: Induces caspases and apoptosis (PubMed:14583606). Counters the protective effect of BCL2 (By similarity). FUNCTION: [BH3-interacting domain death agonist p15]: Induces caspase activation and apoptosis (PubMed:15661737, PubMed:32029622). Allows the release of cytochrome c (PubMed:32029622). FUNCTION: [Isoform 4]: Induces ICE-like proteases and apoptosis. SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane Note=A significant proportion of isoform 2 localizes to mitochondria, it may be cleaved constitutively. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion membrane Mitochondrion outer membrane Note=When uncleaved, it is predominantly cytoplasmic. SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p13]: Mitochondrion membrane Note=Associated with the mitochondrial membrane. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p15]: Mitochondrion membrane Note=Translocates to mitochondria as an integral membrane protein. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm."}
{"protein": "MSIFIGQLIGFAVIAFIIVKWVVPPVRTLMRNQQEAVRAALAESAEAAKKLADADAMHAKALADAKAESEKVTEEAKQDSERIAAQLSEQAGSEAERIKAQGAQQIQLMRQQLIRQLRTGLGAEAVNKAAEIVRAHVADPQAQSATVDRFLSELEQMAPSSVVIDTAATSRLRAASRQSLAALVEKFDSVAGGLDADGLTNLADELASVAKLLLSETALNKHLAEPTDDSAPKVRLLERLLSDKVSATTLDLLRTAVSNRWSTESNLIDAVEHTARLALLKRAEIAGEVDEVEEQLFRFGRVLDAEPRLSALLSDYTTPAEGRVALLDKALTGRPGVNQTAAALLSQTVGLLRGERADEAVIDLAELAVSRRGEVVAHVSAAAELSDAQRTRLTEVLSRIYGRPVSVQLHVDPELLGGLSITVGDEVIDGSIASRLAAAQTGLPD", "text": "FUNCTION: This fusion protein includes a component of the F(0) channel (subunit b) and of the F(1) subunit (subunit delta). Two copies of subunit b and one of delta together form the peripheral 'stator' stalk which links F(1) to F(0) (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 membrane; Single-pass membrane protein. SIMILARITY: In the C-terminal section; belongs to the ATPase delta chain family. SIMILARITY: In the N-terminal section; belongs to the ATPase B chain family."}
{"protein": "MTTDMDLEQLEYEKEVEEIEKWWATPKQSQIKRPYTASTVAVLSEVTKAYYPSSQQALKLYDLLREHRNKGTATLTYGVVDPVLASQASKAGLETIFVSGCLCGLSSVDEPGMDHADYPWDTVPKAVDRIFRSQNWHARRQKQFHLMKPAEERKQLPKYDYLLPIIADGDMGFGSVTSTMKMTKRFVESGVAMIHLDDLAIGLKRFTVGQGRTVVPTSEYLRRLTAVRLQFDIMKAETMLLCRCDTDHAEFITSVVDPRDHAYVLGATTKIESLIKALKDAESTGVSMKKARENWIERAKLMTFDEAVKSTATPKEYENYISAISKKPFHSISERQELAEKYLSNEVFFDWELPRSSDGQYFFKPTVQTVIERAIAAAPLGEMTWARMDYPKWQDIKAFHEGVRAVYPDRMFAFGFTGNYDFKAAGFSEEQLRNLTSDMAKLGVCWQVQPYFTCQVLNKASVDYSNIWKKDGIFGYVKTVQEPALKEDVDGFENEWCGTYFADKLLSAAGSSDKTIPY", "text": "FUNCTION: Catalyzes the formation of pyruvate and succinate from 2- methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix Cytoplasm. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family."}
{"protein": "MTFINRWLFSTNHKDIGTLYLIFGTWAGMAGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTIINMKPPALSQYQTPLFVWSVLITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAILAGFTHWFPLFTGFTLHPTWTKAHFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTLSSIGSLISMTAVIMLMFIVWEAFSAKRKVLQPELTATNIEWIHGCPPPYHTFEEPAFVQVQE", "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": "MDENESNQSLMTSSQYPKEAVRKRQNSARNSGGSDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNHSIPHVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVRETGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRRFMKYQHVDPEEAVRIHIDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNTDDENF", "text": "FUNCTION: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (By similarity). 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 (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). 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. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity). 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": "MVKQLKFSEDARQAMLRGVDQLANAVKVTIGPKGRNVVLDKEFTAPLITNDGVTIAKEIELEDPYENMGAKLVQEVANKTNEIAGDGTTTATVLAQAMIQEGLKNVTSGANPVGLRQGIDKAVKVAVEALHENSQKVENKNEIAQVGAISAADEEIGRYISEAMEKVGNDGVITIEESNGLNTELEVVEGMQFDRGYQSPYMVTDSDKMVAELERPYILVTDKKISSFQDILPLLEQVVQSNRPILIVADEVEGDALTNIVLNRMRGTFTAVAVKAPGFGDRRKAMLEDLAILTGAQVITDDLGLDLKDASIDMLGTASKVEVTKDNTTVVDGDGDENSIDARVSQLKSQIEETESDFDREKLQERLAKLAGGVAVIKVGAASETELKERKLRIEDALNSTRAAVEEGIVAGGGTALVNVYQKVSEIEAEGDIETGVNIVLKALTAPVRQIAENAGLEGSVIVERLKNAEPGVGFNAATDEWVNMLEAGIVDPTKVTRSALQHAASVAAMFLTTEAVVASIPEKNNDQPNMGGMPGMM", "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": "MTEHMRIPLAGVIGSPIAHSRSPALHGYWLKRYGLKGHYIPMDVAQADLREVLAAMPRMGFVGCNVTIPHKETVIALADIVTDRAALIGAANTLIFRKDGKIHADNTDGAGFTANLRQNAPDWQPQAAPAVVWGAGGAARAVIAALIEVGVPEIRLSNRSRARADALRSDFGAKVQVFDWVQAGNILEDATTVVNTTSLGMIGKPDFRVPLDALSPKAVVTDLVYTPLRTRLLAEAEAAGCRTVDGLGMLLHQAAPGFERWFGVRPEVDEDTRAAVLAT", "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": "MFGTPSSSPSFGTPSSTPAFGTSSPAFGTPSATPAFGTPSNPSFSSGGFGSSLFSSPFSSQQPQQQQQQQQQQQPSSLFQQQPSSNFGFQSPFNNTAQQQQQTPFPNAQLTTQMAPVAPIPYSLADRDVQAIIEAYKEDPTNPKYAFQHLLFSVTEPQYRVKPAAVSDIMWAEAMSKLEGMDSTERERLWPQLVQGFKDLSQRLKLQDEVLVSDRDRIKTTQSNVKMLQRHLQASTFPSIERLRQKEQSLQRRMLRVMRIIEGLEGKGFRLPLTKGEAELSEKLTAITRQVKGPGAELSRRVQSLQTISRAQANSIAAGSSLYLPGSTKIDEQSLIDMQEVLQQETEAIGRLGNVLKRDMRDMEIMVAEDTEMALDS", "text": "SUBCELLULAR LOCATION: Nucleus envelope Nucleus, nuclear pore complex. SIMILARITY: Belongs to the NUP54 family."}
{"protein": "MPSVESFELDHTIVKAPYVRHCGVHNVGSDGIVNKFDIRFCQPNKQAMKPDVIHTLEHLLAFNLRKYIDRYPHFDIIDISPMGCQTGYYLVVSGTPTVREIIDLLELTLKDAVQITEIPAANETQCGQAKLHDLEGAKRLMNFWLSQDKDELEKVFE", "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": "MAKELADKAKEAFVDDDFDVAVDLYSKAIDLDPNCAEFFADRAQAYIKLESFTEAVADANKAIELDPSLTKAYLRKGTACMKLEEYRTAKTALEKGASITPSESKFKKLIDECNFLITEEEKDLVQPVPSTLPSSVTAPPVSELDVTPTAKYRHEYYQKPEEVVVTVFAKGIPKQNVNIDFGEQILSVVIEVPGEDAYYLQPRLFGKIIPDKCKYEVLSTKIEICLAKADIITWASLEHGKGPAVLPKPNVSSEVSQRPAYPSSKKVKDWDKLEAEVKKQEKDEKLEGDAALNKFFREIYQNADEDMRRAMSKSFVESNGTVLSTNWQEVGTKTIESTPPDGMELKKWEI", "text": "FUNCTION: Functions in R gene-mediated resistance, but participates in a lower extent than SGT1B to RPP5-mediated resistance. Not required for RPM1, RPS2, RPS4 and RPS5-mediated resistance. Probably required for SCF-mediated ubiquitination, by coupling HSP90 to SCF complex for ubiquitination of HSP90 client proteins. SIMILARITY: Belongs to the SGT1 family."}
{"protein": "MFSESDLKRLVEEVLVEMTTKEGANIKDTPVSQPTPTVVDEDGIIPDITEVDIRTNLLVDNPENAEEYLKMKKHTPARIGVGKAGTRYKTETILRFRADHAAAQDAVFTDVDEKILEEMNLETIQTMCSSKDEFITRPDLGRKISKEELSKLSSYKKNAQVQIYVSDGLSSKAVEANVKNILPALIQGLEGYGISVGKPFFVKLGRVGAMDVISEEFGADVTCVLIGERPGLVTAESMSAYIAYKGTVGMPESRRTVVSNIHKGGTPAVEAGAYIADIIKLMLEKKASGLDLKL", "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": "MSKLVLTTDFPDLKLAARGKVRDIYDLGETLLIVTTDRISAFDVIMNEGIPDKGYVLTQISAFWFRQMEDIIPNHIISTEVKDFPAECQKYADVLEGRSMLVKKAKPLPAECIVRGYISGSGWKDYQATGSVCGITLPAGLKESDRLPEPIFTPSTKAELGTHDENISFEKMVDMCGKDIAEKVRDITLKIYKKARDIADGKGIIIADTKFEYGIYEGELIIIDECMTPDSSRFWPKDSYQPGGPQPSFDKQFLRDYLETLDWDKTAPAPPLPEEIVRKTGEKYMEALVKLTGKGK", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MSEATTTLDGWYCLHDLRSIDWAAWKTLSSDERGQAVSEFLNVVEKWNEVATAKKGSHAMYTVVGQKADIMLMILRPTMEELNEIETELNKTTLAEYMVPAYSYVSVVELSNYLPADEDPYQNPQILARLYPELPKANHICFYPMDKRRQGDDNWYMLPMEERKKMMYSHSKIGRQYAGKVRQVISGSVGFDDFEWGVTLFADDVLQFKKLIYEMRFDEVSARYGEFGTFFVGNILPDEKVEKFLHI", "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": "MRVVTRFAPSPTGSLHLGGARTALFNWLFARHHKGKFLLRMEDTDKKRSSDVVVQSIIDDMSWLGLQHDGDIVVQSSRAARHVAVARELVELGRAYRCYCSEDEVNEQKLQSEGTGKYFRHVCPWKHLNSTGDLPNKPYVVRLKSPENTTIEFLDGVYGKISVKSDQIDDMVILRSDGTPTYLLAVVVDDHDMEITHIIRGSDHITNTVKQIVLAEAMSWVSPKFFHIPLIHDENGAKLSKRNRAPGIHEYKEQGFLPEALCNYLLRMGWSYQNKEIVSMQEAIALFSMEDVGVSCSCLDYKKLVFLNHHYMGSKSESEILDLLLPILEEKLGGRISEEKLSRLSLGIKQLVERAKTLTDLAEDSLFYVQDVEININPEAVETIQNSKKFLAELLESMSGIHPDMWKKTHLSSQIKEFSKTRNLAMSDVYHFLRASITGRLQSPNISEVMEILGQEMCINRMLSAQEI", "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": "MAVVTLAEMMEAGAHFGHQTRRWNPKMSRYIYCARNGVHIIDLVQTAVCMNNAYKWTRSAARSGKRFLFVGTKKQASEVVALEAARCGAAYVNQRWLGGMLTNWTTMKARIDRLKDLERMESSGAIAMRPKKEGAVLRRELERLQKYLGGLKTMRRLPDVVVLVDQRRESNAVLEARKLDIPLVSMLDTNCDPDLCEVPIPCNDDAVRSVQLVLGRLADAINEGRHGNNEQRGGGDAEG", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MAAPRHHHLALAVALALLVVTAAAADEGGPRGRRVLVLVDDLAVRSSHSAFFASLQGRGFDLDFRLADDPKLSLHRYGQYLYDGLVLFAPSTPRFGGSVDQNSILEFIDAGHDMILAADSSASDLIRGIATECGVDFDEDPEAMVIDHINYAATDAEGDHTLIAGDDLIQSDVILGSKKIEAPVLFRGIGHAVNPSNSLVLKVLSASPSAYSANPKSKLASPPSLTGSAISLVSVMQARNNARVLISGSLDLFSNRFLKSGVQKAGSKIRHEKAGNEQFVTETSKWVFHERGHLKAVNVKHNKVGETNEPGMYRINDDLEYSVEIYEWSGTSWKPYVADDVQVQFYMMSPYVLKTLSTDKKGVFSTSFKVPDVYGVFQFKVEYQRLGYTGLSLSKQIPVRPYRHNEYERFITSAYPYYAASFSTMGAFFIFSFVYLYHK", "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": "MAEAAPETPPENESPQREPWEEWVEDVMEEIKQEALRHFDPRLLTALGNFIYSRHGDTLAGAGELIKILQRALFLHFRAGCQHSRIGQPGGGNPLSAIPPS", "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": "MVNMKASMFLTFAGLVLLFVVCYASESEEKEFPKEMLSSIFAVDNDFKQEERDCAGYMRECNEKLCCSGYVCSSRWKWCVLPAPWRR", "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": "MGQNQSRDKQKAIQNQPKDTGNRADIIPDATGMGPEFCKSCWFERRSLVACNNHYLCMNCLTLLLSVSERCPICKLPLPQKLKLTSSPSAPPSPSPPPYSP", "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": "MPAGGGLWRGPRGHRPGHHGGAGLGRLWPAPHHAAAARGAVALALLLLALAAAPPCGAAAVTRAASASPTPGTGATPNDVSAEASLEEIEAFSPGPSEAPDGEYGDLDARTAVRAAATERDRFYVCPPPSGSTVVRLEPEQACPEYSQGRNFTEGIAVLFKENIAPHKFKAHIYYKNVIVTTVWSGSTYAAITNRFTDRVPVPVQEITDVIDRRGKCVSKAEYVRNNHKVTAFDRDENPVEVDLRPSRLNALGTRGWHTTNDTYTKIGAAGFYHTGTSVNCIVEEVEARSVYPYDSFALSTGDIVYMSPFYGLREGAHGEHIGYAPGRFQQVEHYYPIDLDSRLRASESVTRNFLRTPHFTVAWDWAPKTRRVCSLAKWREAEEMTRDETRDGSFRFTSRALGASFVSDVTQLDLQRVHLGDCVLREASEAIDAIYRRRYNSTHVLAGDRPEVYLARGGFVVAFRPLISNELAQLYARELERLGLAGVVGPAAPAAARRARRSPGPAGTPEPPAVNGTGHLRITTGSAEFARLQFTYDHIQAHVNDMLGRIAAAWCELQNKDRTLWSEMSRLNPSAVATAALGQRVSARMLGDVMAISRCVEVRGGVYVQNSMRVPGERGTCYSRPLVTFEHNGTGVIEGQLGDDNELLISRDLIEPCTGNHRRYFKLGSGYVYYEDYNYVRMVEVPETISTRVTLNLTLLEDREFLPLEVYTREELADTGLLDYSEIQRRNQLHALKFYDIDRVVKVDHNVVLLRGIANFFQGLGDVGAAVGKVVLGATGAVISAVGGMVSFLSNPFGALAIGLLVLAGLVAAFLAYRHISRLRRNPMKALYPVTTKTLKEDGVDEGDVDEAKLDQARDMIRYMSIVSALEQQEHKARKKNSGPALLASRVGAMATRRRHYQRLESEDPDAL", "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": "MLEQIRGPADLQHLSQAQLEDLAHEIRDFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPILFDTGHQAYVHKMLTGRCRDFDSLRKKDGLSGYPSSAESEHDWIESSHASSALSYADGLAKAFELSGHRNRHVVAVVGDGALTGGMCWEALNNIAASRRPVVIVVNDNGRSYAPTIGGFAEHLAGLRLQPGYERVLEEGRKAVRGVPMIGEFCYQCMHSIKVGIKDALSPQVMFTDLGLKYVGPIDGHDEHAVESALRHARAFNAPVVVHVVTRKGMGYAPAENDADDQMHACGVIDPETGLATSVPGPGWTSTFSEALIRLAGKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGMHPVVAIYSTFLNRAFDQMLMDVALHKLPVTVVLDRSGVTGPDGASHNGMWDLSILGIVPGMRVAAPRDGARLREELGEALDVSDGPTAIRFPKGDVGEDIPAIERRGDVDVLAVPADGMSEDVLLVAVGPFAAMALAVADRLRNQGIGVTVVDPRWVLPVPEEIATLATRHKLVVTLEDNGGHGGVGSAVSGALRHKEIDVPCRDAALPQEFFAHASRGEVLESVGLTERNIARQITGWVAALGASTGDREVSEHVD", "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": "MIISTTHSIEGRQITAYLDIVSAESVQGVNVIRDMFAGMRDFFGGRSQTLERALKEARVQATDEIKERARALQADAVVGVDFEISMPAGKGGMVVVFATGTAVKLR", "text": "SIMILARITY: Belongs to the UPF0145 family."}
{"protein": "MKFDVVIIGGGLAGLTCGIMLQQKGKCCAIINNGQSAMNFSSGSMDLLSQLPNGEKINSFEQGYDSLEEQLPNHPYCLFGKQHVLQKAKQFEQLIEKINLNVTGSYKQNHFRVTPLGGLHRTWLSADCIPTMDLHDEHFGYQKITVLGIEGYHDFQPHLLAENLIQHPQFTHCSITTALLHLPELDQLRLTSREFRSVNISQLLEHRLAFRELVQEIKQASGDGEAIFLPACFGLDNQDFFNKLTLETGLNLYELPTLPPSLVGLRQHKKLKTYFEKLGGFILNGDKALRAVIEDQQVKQIYTQLHQEHGIFAEHFVLASGSFFSNGLVSVFDRLLEPIFDVDMIGNSMIDIQNRLTWTARRFSSPQPYQSAGVAINSCCQLKKSGQIIKNLYAAGNVIGGYNALELGCGSGVAVVTALTVADNIIEAQNRV", "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": "MSEKTIAVKAQKVDEVADMFSNSVSAVVADVRGLTVAQADDLRAQLRDEGVSLKVIKNKILTRAAEKAGYQELNDLFKGPSAIAFSKEDVVAPARILKKFSGTADALELKGGVIDRKVADLDTINRYAALPSKETLLQQLLAEFQSPLRSFMYAVKAVAEKREADGETAETPAQETASDDSKSTKAEASDASTTENK", "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": "MIDQNKLITKWKKAFAKAKNLTTLVNLKNTLHNSDLKPLLQKIKTATKLSEKSSLGKLYQSLDIQLTDLLTSYKKTFEINNQVSQKPSLDVMLPATEFTNGSNNALYQVIDNLVEYFKSFLFTINFDSELTSISDCFDLLNIPKDHSSRNESDSFYIDKTSLLRTHCTATTLKAVRTSKKTNNPDIRVVSLGAVFRNDSDDATHSHQFTQLDFMWIKKGLSLANLKWFINNMITHFFGENTFTRFRLSHFPFTEPSFEIDIRCWLCQNGCSICKQTKWIEILGAGIIHPQVMNNMGIGDTENITGIAAGIGIERLAMLKYGIDDIRDFYDNNFKFLTQFTD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MARIGDSGDLLKCSFCGKSQTQVKKLIAGPGVYICDECIDLCNEIIEEELADADDVQLDELPKPVEIREFLEGYVIGQDTAKRTLAVAVYNHYKRIQAGEKGRDSKREPVELAKSNILMLGPTGCGKTYLAQTLAKMLNVPFAIADATALTEAGYVGEDVENILLKLIQAADYDVKRAETGIIYIDEVDKIARKSENPSITRDVSGEGVQQALLKILEGTQASVPPQGGRKHPHQEFIQIDTTNVLFIVAGAFAGLDKIIYERIGKRGLGFGAEVRSKAEIDTTDHFADVMPEDLIKFGLIPEFIGRLPVIASVINLDMESLVKILSEPKNALVKQYTWLFEMDGVELEFTNDALEAVADQAIHRGTGARGLRAIMEEVLLPVMYDIPSRDDVAKVVVTKETVQDNVLPTIVPRKPSRTERRDKSA", "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": "MTEYLLLLVSTVLINNFVLVKFLGLCPFMGVSGKLETAVGMGLATTFVMTLASASSYLMEHYILIPLNIAYLRTLAFILVIAVVVQFTEMVIRKSSPTLYRLLGIFLPLITTNCAVLGVALLSINERHNFIQSIIYGFGAAAGFSLVLILFAAMRERLVAADVPTPFRGVSIAMVTAGLMSLAFMGFTGLIKI", "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": "MDNYTDVLYQYRLAPSASPEMEMELADPRQMVRGFHLPTNESQLEIPDYGNESLDYPNYQQMVGGPCRMEDNNISYWNLTCDSPLEYAMPLYGYCMPFLLIITIISNSLIVLVLSKKSMATPTNFVLMGMAICDMLTVIFPAPGLWYMYTFGNHYKPLHPVSMCLAYSIFNEIMPAMCHTISVWLTLALAVQRYIYVCHAPMARTWCTMPRVRRCTAYIALLAFLHQLPRFFDRTYMPLVIEWNGSPTEVCHLETSMWVHDYIGVDLYYTSYYLFRVLFVHLLPCIILVTLNILLFAAMRQAQERRKLLFRENRKKECKKLRETNCTTLMLIVVVSVFLLAEIPIAVVTAMHIVSSLIIEFLDYGLANICIMLTNFFLVFSYPINFGIYCGMSRQFRETFKEIFLGRLMAKKDSSTKYSIVNGARTCTNTNETVL", "text": "FUNCTION: Receptor for two functionally unrelated ligands; SP (A70A) for controlling reproductive behaviors and MIP for controlling sleep behavior (PubMed:18066048, PubMed:20458515, PubMed:20308537, PubMed:24089336, PubMed:25333796). MIP-SPR pathway functions as a sleep homeostat which perceives the need for sleep and stabilizes it by providing a slow-acting inhibitory input to the fly arousal system that involve the pigment dispersing factor (pdf) neurons (PubMed:25333796). SP-SPR is one of the multiple SP pathways that induce female post- mating behavioral responses (PMR) such as the suppression of mating receptivity and initiation of egg laying (PubMed:18066048, PubMed:24089336). The PMR switch is achieved by mediating the synaptic output of neurons such as those expressing fruitless (fru), double sex (dsx) and pickpocket (ppk) (PubMed:18066048, PubMed:24089336). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSFSRPSGRTADQLRPVRIERAFTRHAEGSVLVSFGDTRVLCTASVENRVPNFLRGKGEGWVTAEYGMLPRSTHTRSDREAARGKQGGRTLEIQRLIGRALRACVDRNALGERTITLDCDVLQADGGTRTAAITGAYVALADAVNLLLKRGDIKKHPLIGAVAAVSVGIYRGEPVLDLDYPEDSDCDTDMNVVMNDGGGFIELQGTAEGHAFRRDELNALLALAEKGVGELFELQRAALAG", "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": "MEEKRSTNSPGFDKPKLNRSGSITSATSHPPRSNSNPKLVAKHQQQLYEESKNKRNQEQQNQQPQQQQQKQTSNQSEDPATQLSSLKFESDKEKEQALLWAFLASYLPEDKGSLQKEFVKHVEYTLAQTKSECTDFSSFQALSYCTRDRLIERWKDTKLFFKQKNVKQVNYMSLEFLLGRSLQNSLSALGLVGKYSDALMDLGFKLEDLYDEERDAGLGNGGLGRLAACFMDSLATCNFPGYGYGLRYKFGMFYQTLVDGEQVELPDYWLNYGSPWEIERLDVSYPINFYGKVSEVEDENGKKVMKWDQGEQMLAVAYDYPIPGFKTYNTVAIRLWSSKPSDEFNLDSFNRGDYLGAIEEKEKSENITNVLYPNDNTMQGKELRLKQQYLFVSATIQDIISQFKETGKPFSEFHNFHAIQLNDTHPTLGIPELMRILIDEEKKSWDEAWDITTKTFSYTNHTVLPEALEKWSVSMVENVLPRHIMIIYEINERFLKLVDQKWPGDMSKRRALSIIDESDGKFIRMAFLAIVGSHTINGVAYLHSELVKHDVFPLFYEIWPNKFQNKTNGVTPRRWIQQSNPQLAELITRSLNSDRWLVNLDIIKDLVHLADNSSFQKEWMEIKRNNKIRLAKYIEKRCDIQVNVDVLFDVQVKRFHEYKRQLLNVLSVINRYLDIKEGKKVAPRVVIFGGKAAPGYYMAKLIIKLINSVADVVNNDPKVGDLLKVVFIPNYCVSNAEIIIPASDISQHISTAGTEASGTSNMKFSMNGGLIIGTLDGANIEIRDAIGHENMYIFGARSEEVNKVKKIIHDGKFTPDTRWARVLTAIKEDTFGPHEQFQDIINSVSGGNDHYILSYDFGSYLDIQNSIDQDFKDRAKWAKKSIMASVCCGKFSSDRTIKEYAQQIWGIEEWKRPGPVPVSNEEARSLLVPPPSGSPNDINAISIERLSPLTFVKQTSASPLSVISGGDKTNNTLKPKQTTKGFNIGGQPGNPTN", "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. SIMILARITY: Belongs to the glycogen phosphorylase family."}
{"protein": "MRIILLGAPGAGKGTQAQFISSTFSIPQISTGDMLRAAINEGTPLGLEAKKVMDAGKLVSDEIILGLVKERLSKSDCKNGCLFDGFPRTIAQADALKNDCIQIDHVIDIEVDDEEIIKRMSGRRVHPASGRTYHVLFNPPAKEGVDDITGDPLVQREDDCEETVRKRLDIYHKETAPLIEYYREYKKNGGPNALKFSTIKGTGSVESIKEKILNIFHN", "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": "MAKSSMKAREAKRAKLVAKYAEKRLALKAIISNPTTSDEDRWDAVLKLQGLPRDSSAARQRNRCSQTGRPHGFLRKFGLSRIKLREATMRGEVPGLRKASW", "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": "MAPKFPDSVEELRAAGNESFRNGQYAEASALYGRALRVLQAQGSSDPEEESVLYSNRAACHLKDGNCRDCIKDCTSALALVPFSIKPLLRRASAYEALEKYPMAYVDYKTVLQIDDNVTSAVEGINRMTRALMDSLGPEWRLKLPSIPLVPVSAQKRWNSLPSENHKEMAKSKSKETTATKNRVPSAGDVEKARVLKEEGNELVKKGNHKKAIEKYSESLLCSNLESATYSNRALCYLVLKQYTEAVKDCTEALKLDGKNVKAFYRRAQAHKALKDYKSSFADISNLLQIEPRNGPAQKLRQEVKQNLH", "text": "FUNCTION: Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the Tom34 family."}
{"protein": "MSDVEERINQIIQVLREQVVQDTAVPRNIRRAAEQAIEALMNKEKEPAVRAADAIAILEEISEDPNMPLHTRTIIWEVLGALEQIK", "text": "SIMILARITY: Belongs to the UPF0147 family."}
{"protein": "MSKFVFVTGGVVSSIGKGIVAASLGRLLKSRGYSVSILKLDPYLNVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFTDTAMTRLNSVTTGSIYQAVINKERRGSYNGGTVQVIPHITREIRERIHRVASNSNADIIITEIGGTVGDIESLPFLEAIREFKNDVNRNDVAYIHVTLLPYIKTSGEIKTKPTQHSVKELRSIGIQPDLLVCRSDKSINEGLKKKLSGFCGVNINSVIEALDADSIYSVPLSLKKEGLCKETLKYLELEDKECDLKNWEKLVHNLRNPGTPIKVALVGKYIELGDAYLSVVEALRHACIEQKALLDLHWVSAEMIEKDSAETYLNEVDAIVVPGGFGNRGVNGKISAIKFARENKIPFLGLCLGMQCAVIEWARNVANLPDASSSELDPKTPNPVIHLLPEQEDVVDLGGTMRLGVYPCRLTNNTIGKKLYDEDVIYERHRHRYEFNNYYKQSFLNSGYKISGTSPDGRLVELIELDNHPYFLACQYHPEFLSRPGKPHPLFKGLIKSSQENLTQSN", "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": "MLGKALLLLLSSPICAWAQSAADYYVKSIPGQPDGPLLKMHAGHVEVDAETNGHLFFWHFQNRHIANRQRTILWLNGGPGCSSMDGALMEIGPYRVKDDHTLIYNNGSWDEFANLLFVDQPVGTGFSYVNTNSYLHDLDHVAAHMITFLEKWFAMFPEYESDDLYIAGESYAGQYIPHIARAIVERNKNIQRNQQHWPIKGLLIGNGWISPRDQYPANLQYAYAEGIVKEGTAIANELDGIEKSCDEQLNAPGAGDLVDIRQCESILNKLLDLTRTSDDQCINVYDIRLKDATCGNAWPPDLDQMTDYLRRADVGAALNLDNGKANGWTECNNQVTANFRMGHNGVPSIQLLPGLIESGVKVLLFSGDRDLICNHLGTESLIHNMKWSGGTGFETKPGVWAPRRGWTFEGEAAGYYQQARNLTYVLFYNASHMVPYDFPRRTRDMVDRFINVDIANIGGPPADSRLDGEKLPQTSVGNTTSSTSGTDQVDEAKLKDAEWKAYTKSGEAALIVVIIGVSVWGFFIWRARQRAARDGTSPTKKGYRAVYQDGVDNNSSTDGAGLLSRFRNQSNSNSSRDLEARDFDEAELDSLTPNLQNGHERDHYVIGEEDEDEDNDIGNGAKSSLH", "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": "MNNKINNIKITQVHSAIGRKYDQRLILVGLGLNKINKSVILANTNSIKGMVNKVKHLLKIENM", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MTEKLLEIKHLKQHFVTPRGTVKAVDDLSFDIYKGETLGLVGESGCGKSTTGRSIIRLYEATDGEVLFNGENVHGRKSRKKLLEFNRKMQMIFQDPYASLNPRMTVADIIAEGLDIHKLAKTKKERMQRVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVDPEFIIADEPISALDVSIQAQVVNLMKELQKEKGLTYLFIAHDLSMVKYISDRIGVMYFGKLVELAPADELYENPLHPYTKSLLSAIPLPDPDYERNRVRQKYDPSVHQLKDGETMEFREVKPGHFVMCTEAEFKAFS", "text": "FUNCTION: Component of the oligopeptide permease, a binding protein- dependent transport system. Necessary for genetic competence but not sporulation. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MSEWKESLNVPKKDTRHKTEDVTATKGTGFEDFFLKRELLMGIFEAGFENPSPIQEEAIPIALAGRDILARAKNGTGKTAAFVIPALQQVNPKVNKIQALIMVPTRELALQTSQVCKTLGKHLGIKVMVTTGGTNLRDDIMRLEDTVHVLVGTPGRVLDLAGKGVADLSESPMFIMDEADKLLSPDFTPIIEQVLHFFPEDRQILLFSATFPLTVKAFMDRNLHKPYEINLMDELTLRGITQYYAFVDEKQKLHCLNTLFSKLDINQSIIFCNSTVRVELLARKITELGYSCYYSHAKMIQSHRNRVFHEFRNGTCRNLVCSDLLTRGIDIQAVNVVINFDFPKNAETYLHRIGRSGRFGHLGIAINLINWNDRYNLYKIEQELGTEIKPIPAQIDKNLYVAESSENIPRPFPIADMPRGKESKRNEQFQPQQNQNQQQQQDGQNQHSLGPVPPQGPPQGIPGPGYGYPPPQGFPQGMPPQGMPPQGAGGYMPPTPYGYQQQGFPPQPPQGFNNGQPQQPSQ", "text": "FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily."}
{"protein": "MLAKRIVPCLDVKDGKVVKGVQFRNHEIVGDIVPLAARYAQEGADELVFYDISASAKGAIVDKSWVSRIAERIDIPFCVAGGIKTAEQAREILAFGADKISINSPALSDPSLIRRLHDEFGRQCVVVGIDSFYDAGSGNYTVKQFTGDEAATKDTRWHTLDWVEEVQRQGCGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGTMAHFAEVFTDARVDAALAASVFHKGIINIGELKQFLVSQGIAIRLTE", "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": "MSSNNGDVRLWGGRFADGPADALARLSASVHFDWRLAPYDIAGSRAHARVLNRAGLLTEDELTRMLAGLDRWPPMWRTLLHRTIADEDVHTALERGLLERLGAELGGKLRAGRSRNDQVATLFRMYLRTTPGSSGLIAELQDALVGLAEAHPEVAMPGRTHLQHAQPVLFAHHVLAHVQALSRDAERLRQWDARTAVSPYGSGALAGSSLGLDPEAVAADLGFEGGSAGNSIDGTASRDFVAEFAFITAMAGINLSRLAEEIIIWNTKEFSFVTLHDAFSTGSSIMPQKKNPDIAELARGKSGRLIGNLTGLLATLKALPLAYNRDLQEDKEPVFDSCDQLEVLLPAFTGMVATLTVHRERMEELAPAGFSLATDIAEWLVRQGVPFRVAHDVAGACVKECESAGIELHQLTDEQFAAISEHLTPEVRSVLTVRGALASRDGRGGTAPSAVAVQLAEVKADLAVQHAWAARES", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MGSSSSSSVVLLLLLLSSLSIALACNKALCASDVSKCLIQELCQCRPADGNCSCCKECMLCLGSLWEECCDCVGMCNPRSMSESPATGRSTVEDLFQPIPSLFRALTEGDAPTHTLVLTLPLAEELQYQHNLHNYLETLHNTQHNNTTSVPENSIHSSYHTQDKQCTVVYFDECVSIRQCKQYCESMGGSKYRWFHNACCQCIGPECVDYGSKSVRCLNCLY", "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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the twisted gastrulation protein family."}
{"protein": "MDKFWWHAAWGLCLLPLSLAQQQIDLNITCRYAGVFHVEKNGRYSISRTEAADLCQAFNSTLPTMDQMVMALSKGFETCRYGFIEGHVVIPRIQPNAICAANHTGVYILTSNTSHYDTYCFNASAPLEEDCTSVTDLPNSFEGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNTTDDDVSSGSSSEKSTSGGYVFHTYLPTIHSTADQDDPYFIGSTMATTRSGGKDGRRGGGLPKDATTSLEGYTTHYPETMENGTLTPVTPAKTGVFGETEVTVAEDSNFNVDGSLPGDQDSSMDPRGNSLTVTDGSKLTGHSSGNQDSGANTTSRPGRKPQIPEWLIVLASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGKVEDRKPSELNGEASKSQEMVHLVNKEPSETPDQFMTADETRNLQNVDMKIGV", "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": "MLRGWGGPSVGVCVRTALGVLCLCLTGAVEVQVSEDPVVALVDTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQGSAYSNRTALFPDLLVQGNASLRLQRVRVTDEGSYTCFVSIQDFDSAAVSLQVAAPYSKPSMTLEPNKDLRPGNMVTITCSSYQGYPEAEVFWKDGQGVPLTGNVTTSQMANERGLFDVHSVLRVVLGANGTYSCLVRNPVLQQDAHGSVTITGQPLTFPPEALWVTVGLSVCLVVLLVALAFVCWRKIKQSCEEENAGAEDQDGDGEGSKTALRPLKPSENKEDDGQEIA", "text": "FUNCTION: Modulates T-cell-mediated immune responses and the development of acute and chronic transplant rejection. Plays a positive regulatory role in bone formation and has a dual role in the bone- immune interface. Induces antitumor immunity as it activates both acquired and innate immunity leading to natural killer cell and CD8 T- cell dependent killing of tumor cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family."}
{"protein": "MPEQSNDYRVAVFGAGGVGKSSLVLRFVKGTFRESYIPTVEDTYRQVISCDKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVYSITSRQSLEELKPIYEQICEIKGDVESIPIMLVGNKCDESPNREVQSSEAEALARTWKCAFMETSAKLNHNVKELFQELLNLEKRRTVSLQIDGKKSKQQKRKEKLKGKCVVM", "text": "FUNCTION: Displays low GTPase activity and exists predominantly in the GTP-bound form. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras family."}
{"protein": "MDDNKKRALAAALGQIERQFGKGAVMRMGDHERTGIPAISTGSLGLDIALGIGGLPKGRIVEIYGPESSGKTTLTLSVIAEAQKSGATCAFVDAEHALDPEYAGKLGVNVDDLLVSQPDTGEQALEITDMLVRSNAVDVIIVDSVAALVPKAEIEGEMGDMHVGLQARLMSQALRKITGNIKNANCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRTGAVKEGDEVVGSETRVKIVKNKVSPPFRQAEFQILYGKGIYRNGEIIDLGVSQGLVEKSGAWYAYQGNKIGQGKANAAKYLQENPAIGAEIEKQIREKLLKAGVVAEAGKAAAADAKADDVADADAGY", "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": "MNSTQPLGMHTSLHSWNRSAHGMPTNVSESLAKGYSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDAQSFTVDIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVKRVAITISAIWAACTVSGVLFIIYSDSSAVIICLITVFFTMLALMASLYVHMFLMARLHIKRIAVLPGSGTIRQGANMKGAITLTILIGVFVVCWAPFFLHLIFYISCPQNPYCVCFMSHFNLYLILIMCNSIIDPLIYALRSQELRKTFKEIICCSPLGGLCDLSSRY", "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": "MFNSNVKLGIAPIAWTNDDMPDLGKENTFEQCISEMALAGFKGSEVGNKYPRDVEVLKKALELRDMEIASAWFSAFLTTKPYEETEKAFIEHRDFLNAMGAKVIVVSEQGHSIQGQMETPIFDGKYVLNEEEWKTLAEGLNKLGALAKEKGMKLVYHHHMGTVVQTTEEIDKLMDLTDENLVYLLFDSGHLVYSGEDALEVLKKYVNRVKHVHLKDIRKKKVEEVKRDKLSFLQGVRKGAFTVPGDGDIDFEPIFKVLDDNNYEGYLLVEAEQDPAIANPLEYAIKARKYIKEKTNL", "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": "METLHRLRQFDAYPKTLEDFRVKTCGGAVVTVISGLIMLILFFSELQYYLTKEVYPELFVDKSRGDKLKINIDVIFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDLDKKPVTSEADRHELGKSEEQVVFDPKTLDPNRCESCYGAETDDFSCCNSCDDVREAYRRKGWAFKTPDSIEQCKREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHAVEIHDLQSFGLDNINMTHEIKHLSFGKDYPGLVNPLDGTSIVAMQSSMMFQYFVKIVPTVYVKVDGEVLRTNQFSVTRHEKMTNGLIGDQGLPGVFVLYELSPMMVKFTEKHRSFTHFLTGVCAIIGGVFTVAGLIDSLIYYSTRAIQKKIELGKAT", "text": "FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERGIC family."}
{"protein": "MQDPNEDTEWNEILRNFGILPPKEEPKDEIEEMVLRLQQEAMVKPYEKMTLAQLKEAEDEFDEEDIKAIEIYREKRLQEWKALKKKQKFGELREISGNQYVNEVTNAEKDLWVVIHLYRSSVPMCLVVNQHLSVLARKFPETKFVKAIVNSCIEHYHDNCLPTIFVYKNGQIEGKFIGIIECGGINLKLEELEWKLSEVGAIQSDLEENPKKGIADMMVSSIRNISIYDSDSSGSDTEAK", "text": "SIMILARITY: Belongs to the phosducin family."}
{"protein": "MSSNKLPTSKYDLSTYWGRVRHAMDITDPRTLLSTSQDLNSAVKTLEDYGAGKIAQLDETVWHAKKIVDSTLHPDTKEPVFLPFRMSCFVLTNLVVTAGMLQPNLGTAGTVFWQWMNQSVNVAFNSANANKSTQLTLPQMTKSYIYAVSASCGVAIGLNKIVPRMNFLSSSSKAVLGRLTPFAAVASAGVLNVFLMRGEELRQGIDVFDKEGESLGKSKKAAFYAVGETALSRVINASPIMVIPPLVLMRLQKQNWLRTRPKLTIPVNLGLITLTSLIALPLAIGVFPAREKISPFKLEPQFHHLKDKSDQPIVEVEFNRGL", "text": "FUNCTION: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sideroflexin family."}
{"protein": "MESTSSPELLQMARWLAGDFSNQEQAWENPPFFASIRVAYRPLPTAVLGGIGFYVEQAYSGHLEEPYRQAVVELTQVGDGIVIRNYRPLQPQRWRGCARGRAEQLSQLSAADLAYLPGCDVQVKRQGSLFVGVTEPGCRCCVVRNGQTTYLQTTLHLSENEFCSHDRGMDPVTHRQVWGAVAGPFRFRKVVDWQAELLQ", "text": "FUNCTION: Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins. SIMILARITY: Belongs to the CpcT/CpeT biliprotein lyase family."}
{"protein": "MSVLEQEKKSGKVYIETYGCQMNEYDSGIVSSLMRDAEYSTSSDPENSDIIFLNTCAIRENAHAKIYNRLQSLGYLKKRNPNLVIGVLGCMAQNLGDDLFHQELPLDLVVGPDNYRSLPELIQRIRKGENSISLTRLSKIETYDEIEPRVVNGIQAFVTIMRGCNNFCTFCVVPYTRGRERSRDPKSIVREVQDLVQKGIRQITLLGQNVNSYKEQDTDFAGLIQMLLDETSIERIRFTSPHPKDFPTHLLQLMSENPRFCPNIHLPLQAGNTRVLEEMKRSYSKEEFLDVVKEIRNIVPDVGITTDIIVGFPNETEEEFEDTLAVVREVQFDMAFMFKYSEREGTMAQRKLPDNVPEEVKSARLTKLVDLQTSISHEQNRARIGRVYSILIENISRKSEKQLCGRTPCGRMTVFPLPQETNVSGMIGSTVSVQIESATSATLKGRILA", "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": "MKKYLHILPACFLFYAAAHAQQKDTVYVTDFGAVPYSYENCVTQIQAAIDECKRTGAKVLSLPEGRYDIWPEGAIRKEYYISNTSTEQECPSKVKTVGLMLHEIDDLTIEGNGATLMYHGKMTTIALEHCNGVRINNLHIDFERPAGSEIQYRKVTGGETEVTLHRDTRYEIVNGKIRLYGEGWRSNRNHCIEYDPDTESFTYSQGWNTLSASDAREIAPGIVRFNTPAEFMPKAGNTLTVRDIIRDQVGLFILESKNITLSRLQMHYMHGLGIVSQYTENITMDRVKCAPRPDSGRLLAASADMMHFSGCKGKVIIDSCYFAGAQDDPVNVHGTNLRALEKIDAQTLKLRFMHGQSYGFNAYFKGDTVAFVRAATMERFASATVRDVRRISDRIVEVRFDRDIPTSLELNHDCVENMTCTPEVEIRNCYFTRTSTRGTLVTTPRKVVIENNTYYKTGMSAILIEADAEGWYESGPVKDVLIKGNTFIDCAYNGGPGHAVIAIHPSNKIIDAERPVHQNIRIEDNTFRTFDYPVLYAKSTAGLLFRNNTIVRTETFPAVSGNPYVFYLNGCKKAVIEGTVFEGETPRQSIKTENMKRKDLKTTIK", "text": "FUNCTION: Alpha-galactosidase that specifically removes branched alpha- 1,3-linked galactose residues present in blood group B antigens. Has no activity toward linear alpha-1,3-linked galactose residues. SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily."}
{"protein": "MEDKIQSDDFTSHKNPTLPQVIEELKELWAMVLPITAMNCLVYVRAVVSVLFLGRLGSLELAGGALSIGFTNITGYSVMVGLASGLEPVCSQAYGSKNWDLLTLSLHRMVVILLMASLPISLLWINLGPIMLFMGQNPEITATAAEYCLYALPDLLTNTLLQPLRVYLRSQRVTKPMMWCTLAAVAFHVPLNYWLVMVKHWGVPGVAIASVVTNLIMVVLLVGYVWVSGMLQKRVSGDGDGGSTTMVAVVAQSSSVMELVGGLGPLMRVAVPSCLGICLEWWWYEIVIVMGGYLENPKLAVAATGILIQTTSLMYTVPMALAGCVSARVGNELGAGRPYKARLAANVALACAFVVGALNVAWTVILKERWAGLFTGYEPLKVLVASVMPIVGLCELGNCPQTTGCGILRGTGRPAVGAHVNLGSFYFVGTPVAVGLAFWLKIGFSGLWFGLLSAQAACVVSILYAVLARTDWEGEAVKAMRLTSLEMRKVGQDEESSLLLLDDEKLGDVL", "text": "FUNCTION: May function as a multidrug and toxin extrusion transporter in the export of IAA-conjugates from the cytoplasm into peroxisomes. SUBCELLULAR LOCATION: Peroxisome membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MSAYIIETLIKILILVAVFSALGGFATYIERKVLAYFQRRLGPCYVGPFGLLQVAADGIKLFTKEDIIPQGANKFIFTLAPIIAMVSAFVSMAPIPFFPNFTLFGYEIKPLISDINIGFLFFLAVGSAGIYAPILAGLASNNKYSLIGSARATIQLLSFEVVSTLTILAPLMVVGSLSLVEINHYQSGGFLDWLVFKQPLAFVLFLIASYAELNRTPFDLLEHEAEIVAGYCTEYSGLKWGMFFLAEYAHLFAFSFVISIVFFGGFNAWGFIPGGIAILIKAGFFVFLSMWVRATYPHVRPDQLMNMCWKIMLPLALLNIVLTGIVILI", "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": "MDRFIIHGGHRLRGDIVIGGAKNAALKLLVAGLLTSERLVLRNVPRIADITTMRRLLEQHGVTVEDLEGDGGTLAVGGTITNTEAPYDIVSQMRASILVLGPLLARCGEARVSLPGGCAIGTRPVDMHLKGLEALGAEISLENGYINARAPRGLVGERIILPFASVGATENLLMASCLARGRTEIINAAREPEIADLVACLNGMGARITGTGTGSLAIEGVEALHGTTHRVMPDRIECGTYACAAGITGGELRLIGGRADHLGAVVRALEEAGVEVFQEDDALRVRRTGALRGVDIMTEPYPGFPTDMQAQFMALLSVAEGASMVTETIFENRFMHVPELNRMGARINVHGSSAIIRGVHSLSGAPVMATDLRASFSLILAGLAAHGETILSRVYHLDRGYEAVEQKLARCGAQIERVRE", "text": "FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily."}
{"protein": "MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP", "text": "FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade. Phosphorylates PFKFB2 (PubMed:36402789). FUNCTION: [Isoform 2]: Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily."}
{"protein": "MNILTLILSYLIGSISFALIVGKMFYKKDIRDYGSGNLGATNAYRVLGIKAGVIVAIADILKGTFACLLPLILSSTINPIVCGLLAILGHIFSVFASFKGGKAVATATGVFLFLSPLGVLVGFVVFVLTLLFTKYVSLSSMLAGIALFIYSLIFEDKVIIALSLLIIVSIIILHRQNIKRILNGTENKIV", "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": "MKVAADPDPSLVSQRDMEPEAAKDKDSFRNYTSGPLLDRVFATYKLMHTWQTVDFVRRKHAQFGGFSYKRMTVMEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLALAGEPQWAVVGDTFPVGCRPQASVVFRDCTFQDNPDLQDPLYSTELGMYQPHCGLENVLMSWGHDEYMYRMMKFNKFALPPEAFYIIRFHSFYPWHKFGDYQQLCNEQDLAMLPWVQEFNKFDLYTKSSSLPDVAALRPYYQGLVDKYCPGILCW", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the myo-inositol oxygenase family."}
{"protein": "MSTRVRYAPSPTGLQHIGGIRTALFNYFFAKSCGGKFLLRIEDTDQSRYSPEAENDLYSSLKWLGISFDEGPVVGGDYAPYVQSQRSAIYKQYAKYLIESGHAYYCYCSPERLERIKKIQNINKMPPGYDRHCRNLSNEEVENALIKKIKPVVRFKIPLEGDTSFDDILLGRITWANKDISPDPVILKSDGLPTYHLANVVDDYLMKITHVLRAQEWVSSGPLHVLLYKAFKWKPPIYCHLPMVMGNDGQKLSKRHGSTALRQFIEDGYLPEAIINYVTLLGWSYDDKREFFSKNDLEQFFSIEKINKSPAIFDYHKLDFFNSYYIREKKDEDLFNLLLPFFQKKGYVSKPSTLEENQKLKLLIPLIKSRIKKLSDALNMTKFFYEDIKSWNLDEFLSRKKTAKEVCSILELIKPILEGFEKRSSEENDKIFYDFAESNGFKLGEILLPIRIAALGSKVSPPLFDSLKLIGKSKVFERIKLAQEFLRINE", "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": "MNKKILDVLEYDKIKQSIRQFIATENGTKELRELVPSSDETEVRNALKQTLDAVNIYRLKNGIPVPRLEDVTEALQRLKIDAALNGQELAQIGRILRATRTVINFFDDLENEEIEIIALDQVIEQLVTIPEVEERLSNSIEGNGHLLNSASSELRRIRASITRIESDVRSRMEKFTRGNNVKYLSEPIVTIRNERYVIPARVEYRSKFGGVVHDQSSSGQTLYVEPESVVDLNNELRQNQVAEVHEEQRILQELSALVAPYTDTLKDNSRILGHLDLLNAKAQYAHQLKATEPQISASNEINLREARHPLIDQKKVVSNDIRLGGEYETLVITGPNTGGKTITLKTVGLLQLMAQSGMFIPANENSTVRIFEEIFADIGDEQSIEQNLSTFSSHMDNTIRILGNLNERSLALFDELGAGTDPKEGAALAIAILDKVRSTGAVSMTTTHYPELKTYGYERMGTINASMEFDVDTLQPTYKLLLGIPGQSNAFEISKRLGLDSDIISQARGLVDQDSQDLNNMIKDLTTRQKRAQKINQQAVELLKQAEEYHQTLVKGVDSLNSQRSNLIESAKEDANRIVNDSQAEADRIIKRLRKLEHSTGSFKENDLIDAKSKINALHQDTNLKRNKVLRRAKEAQKFHENDEVVVLTYGQRGELLRQVDKKHWEVQMGIMKMKVAVDELEKVKPDKTVKRRVHNSVQRTASAGVKTTLDLRGKRYEEALTETDRYIDAALLAGYDEVTIVHGKGTGALRSGITKYLKNNRRIKAFEYAPANAGGNGATIVHFK", "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": "MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYLTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAPSGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsA family."}
{"protein": "MSTVIATYLLHDEKDIRKKAEGIALGLTVGTWTDLPALEQEQLRKHKGEVVGIEELGESGPANEYFDKRLKRAIVKIAYPTVNFSADLPALLATTFGKLSLDGEVRLLDLELSDEWKRHFPGPRFGIAGIREKVGVYDRPLLMSIFKGIIGRDLAYLTSELKKQALGGVDLVKDDEILFDNELLPFEKRITAGKAALQEVYEQTGKRTLYAVNLTGKTFELKEKAKRAAELGADVLLFNVFTYGLDVLQGLREDENINVPIMAHPAFSGAMTPSEFYGVAPSLLLGKFLRLAGADFVLFPSPYGSVALEREQALGIARALTDEQEPFARAFPVPSAGIHPGLVPLLVRDFGLDCIVNAGGGIHGHPDGAIGGGQAFRAAIDAALAGRLLREAVKENEALQKAIDRWGAIEVEA", "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": "MNMPGKTPIEKIVSLSAKPFKVSRGSPRDDKERSYENTFRTPIPYNCPDVSTHLSDCPVCSNLYGKEKLLYIFLGAMIVIIFLVIKNQLN", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the IIV-6 466R family."}
{"protein": "MRFLIRLVPEDKDRAFKVPYNHQYYLQGLIYNAIKSSNPKLATYLHEVKGPKLFTYSLFMAEKREHPKGLPYFLGYKKGFFYFSTCVPEIAEALVNGLLMNPEVRLWDERFYLHEIKVLREPKKFNGSTFVTLSPIAVTVVRKGKSYDVPPMEKEFYSIIKDDLQDKYVMAYGDKPPSEFEMEVLIAKPKRFRIKPGIYQTAWHLVFRAYGNDDLLKVGYEVGFGEKNSLGFGMVKVEGNKTTKEAEEQEKITFNSREELKTGV", "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), also called psiRNA (prokaryotic silencing) in this organism. This protein processes pre-crRNA into individual crRNA units, with an 8-nt 5'-repeat DNA tag that may help other proteins recognize the crRNA. Further processing occurs at their 3' termini in this organism. Generates a 5'- hydroxy and 2',3'-cyclic phosphodiester. SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family."}
{"protein": "MKLIKQGAEAKIYLAEFSELYFDYPIKVIVKERIKKRYRIPEIDLKLRKERTIREARILRRAKEFGVNVPYVFEVDTKNMIIVMEYIEGERLKELLEKLPMEERLKVCREVGRQIGKLHEAGIVHGDLTTSNMILREGKVYFIDFGLAEFDDTIEAQGVDLHLLKRAMESTHYKWFERGFEEVLKGYIEIRGEDKGREIREKIREIELRGRYRERSWITQ", "text": "FUNCTION: Component of the 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 KEOPS complex and likely plays a supporting role to the catalytic subunit Kae1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family."}
{"protein": "MGQVFLLMPVLLVSCFLSQGAAIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVDKHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLLVGNANQISEKLSDLKVGINLLIMGSQDGLLSLDDNDSQQLPRYGNYYQNPGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL", "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": "MAAKRTHERDPIYKIKGLAKDMLDGVFDDLMDKNVLNGDELLKIGEGASLILSKAENLVESFFEKTEMAGKIFAGHIANSDKQLSLQFPSDDEEDELQKMFTPSSASESRGKVEDEEMEVNVGVAHASHLMLTVPQGIQSTEVQDSLKLCSRDWFCTMKTERAEEIYPVMEKEGRTRLALIICNKKFDYLFDRDDAETDILNMKELLQNLGYSVVIKENLTAQEMETELMKFAGRPEHQSSDSTFLVFMSHGILEGICGVKHRNKKPDVLHDDTIFTIFNNSNCPSLRNKPKILIMQACRGRHTGTIWVSTSKGIATADTDEECVLSHRWNNSITKAHVETDFIAFKSSTPHNISWKVGKSGSLFISKLIDCFKKYCWCYHLEEIFRKVQYSFEVPGELTQMPTIERVSMTRYFYLFPGN", "text": "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. SIMILARITY: Belongs to the peptidase C14A family."}
{"protein": "MNKAKFLEVISGGLIVSCQALPGEPFYTEEGGLMPYFALAAKNAGAVGIRANSVRDIKEIKEKVSLPIIGIIKRDYPPEEPFITATMREVDELVAIGVEVIALDCTLRKRHDGLSINTFIEKVKKKYPQQLLMADISTFEEGKNAYQAGVDFVGTTLSGYTKESKKQNGPDMKLIKQLVQENICVIAEGKIHTPEQARQIKKLGVAGIVVGGAITRPQEIAKRFVDALNKEEKDV", "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": "MKKNIHPDYHPVVFKDASTGHQFLTRSTATSDRTVEWEDGNEYPLIVVDVTSESHPFWTGAQRVMDTAGRVEKFQRRYGNRLRRAKK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily."}
{"protein": "MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL", "text": "FUNCTION: Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11175748, PubMed:11779464, PubMed:12637535, PubMed:21317875, PubMed:28128204, PubMed:9637683, PubMed:30118681). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP (PubMed:21317875). Accumulation of misfolded proteins in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:21317875). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:24508390, PubMed:21317875). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11779464, PubMed:24508390, PubMed:21317875). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (PubMed:21884936, PubMed:28067262). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MKINSPLEAYKYLPQTNCGECGQPTCMAFASTLIDRSGKTTDCPPLIKEKKFAKKLAELDRLLAPEIRQVTIGVGERAANIGGDDVLYRHKLTFFNKTKMFFDVADNMDEAAIVERVKKISDYKKFYVGRNLLLDGVAIRAASNDPAKFATAVKKVIENTELPVILCSFNPAVLKAGLEVAKGKNPLLYAANKDNWKEVGELALEYNVPVVVSAFNDLDGLKTLAKTFAEAGIKDIVLDPGTYPTGKGLKDTFTNFLKIRRAGIMGDTEIAYPIMAMPLTAWMAGIADPVSASYWETVLSSIFTIRYGDIMLLHSMEPYATMPEVHLAETIYTDPRSPVAVDSKMYKVGNPTADSPVLFTTNFALTYYTVESDLASNGIDCWLLAVNTDGIGVEAAAAGGQLTADKVKDAFEKSGFDLKSDVTHNSVVIPGLAARLQGDIEDKLNVKVMVGPMDSGRLPGWMEKNWPPKK", "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."}
{"protein": "MEAVLRHPSLSRLKPPNPNAQRTPALSITVPFRLRLPNRRLTAAAVFQDQTNPRNPASKGGDDDEAYGEVDRIVSSRTIKNPVFAEDGSATTVTATEYLVEWKDGHEPSWIPAEAIAADVVAEYETPWWTAAKKADAAEITALLADETLRRDPDAEDAQGRTAMHFAAGLGSEECVRALAEAGADVGRPERAGGGLTPLHIAVGYGRPAAVRALLELGAEPEAPDGQGRTPLELVQDVLAKTPKGNPATFERRLALEAAAKELEKAVYEWGEVEKVVDGRGEGKWREYLVEWRDGGDREWVRAAWVAEDLVKDFDAGLEYAVAEAVVNKREAAEGEGKWEYLVKWVDIEEATWEPAENVDAELLQEFEQRQSGVAAGGDAPPPPPVAG", "text": "FUNCTION: Component of the chloroplast signal recognition particle pathway. Targets proteins into the thylakoid membrane (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MARDKTRIKRKERKNIATGVAHVNSSFNNTKILISDVQGNAISWSSAGTMGFKGSRKSTPYAAQMAAEDAGKKAQEHGVRTLEVEVQGPGSGRESALRALAAVGFNITAIRDVTPIAHNGCRPPKRRRV", "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": "MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGSALTHKWITTDFAEALLEFITPVDGDIQHMLTFMRDLHRYTARKLGDERMWPLSMPCYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVHYNFSLPMAFWQAKCGVTEGEAAKEKISAGYFRLIRNYYRFGWVIPYLFGASPAICSSFLQGKPTTLPFEKTDCGMYYLPYATSLRLSDLGYTNKSQSNLGITFNDLHEYVAGLKRAIKTPSEEYARIGVEKDGKRLQINSNVLQIENELYAPIRPKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFMVWCVLADAPEMSSDELLCTRTNWNRVILEGRKPGLTLGIGCETAQFPLPKVGKDLFRDLKRVAQTLDSIHGGEEYQKVCDELVACFDNPELTFSARILRSMIDEGIGGTGKAFGEAYRNLLREEPLEILQEEEFIAERDASVRRQQEIEAADTEPFAAWLAKHA", "text": "SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily."}
{"protein": "MSIFSSISSLGLEACYRHHVRTSPNATAVVDGDQSMTYRELETRVNDLASILGRENIEEEEPIGILVPMGIAHVVAQAAVLRLGGSCVPMDLSFPDQRINDLLRALKTRIVLTVESEKARFAEFQTILVDSKYANLHQNGYHEDTIPAVETGRNHRTHILHTSGTTGLPKPVEIMSKGITRMAFNTQCVEFKSTDRVAQISAPSFDAALFEIWTTLARGAAIVLLPKNVVIDPVALHDSLRKYRITSILVTTALLNHVVSAIPNAFEDLDYVLTGGEAANPSVMQVILENGPPKKLVHAYGPTECTIITTYHLTTLEEVRRGQTPIGRPLDNTTVYILDDNLQPVKEGIVGELYIGGDAVARGYLGRPEANAKSFLEVSHLSKDGSPVRIYRSGDLVRMLDTGAIEFVARADNMVKIRGFRIEPAEIEGALLKSEMVQGTVVLPVHRPGKETYIVAFVIPKHDGAFSLEQLDEYLRRRLPAYMMPRLEAVASLPLTVHGKIDRVAVMKKHMEETKRAEQQVLISSNVKDAGDSVTWLRTLWTSVLGISNIDNEASFFHLGGSSLQAAALLVHIRRRFGLTLTMQQIYDSPTLLGLASVIDAGHAKSKVDHSRLGIFIADSQLAKDIPVLSKEAPDWRSPSEGKVFLTGATGFLGTYFLRELIDRPDVRSVKCLVRASDAHSARKRLLGALDKYGLGWADNLDKVTAIAGDLGKDLFGLSETEFHELALWTSVIFHVGAHVNYVQPYEKHRNTNVYGTLNCIKLATTGRTKALHYTSTAAVTGPVSHFTGADKIPEDVDLGEFQGWLPYDIGYTQSKWVSEQLIHSMIAKGLPAIVFRPGFIMGDSLRGKGNCDDFMCRVFIGSIKLGYRPILPNQSKIMIPVDFITTALLHITSNPYNFGRTFHLVPQTPEEDTDIETSWNMLKELGYDLKAVEYKDWLEILSKDKDLLTNPLLPMLPVLQEPVRKHLTRWELYEDMATYDVTNTRRSLADRGKLKSGIGLEDLRRHVEDWVARGLVPSRN", "text": "FUNCTION: Nonribosomal peptide synthetase; 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 NRP synthetase family."}
{"protein": "MIFSTLEHILTHISLSIILILMTIHLIIFLVDEIRKLYDSSEKGMLVTFFCITGLLATHWISSEHFPLSDLYESFIFLSWSFALIHIIPYFTKNTKFLSKIISPSAIFTQGFATSGLLTEIHQSSILVPALKSEWLIMHVSMMILGYAALLCGSLLSVALLVITFRKNGKLFSGGNDFLTESFLFGENLFQKTSFFSAKNYYRTQFIQQLDFWSYRVISLGFLFLTIGILSGAVWANEAWGSYWSWDPKETWAFITWIVFAIFLHTRTNLNLQSVNSAIVASIVASIGFLIIWICYFGVNLVGIGLHSYGSFPSTSS", "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": "MQEIQKNTKKEQYNLNKLQKRLRRNVGEAIADFNMIEEGDRIMVCLSGGKDSYTMLEILRNLQQSAPINFSLVAVNLDQKQPGFPEHILPAYLEQLGVEYKIVEENTYGIVKEKIPEGKTTCSLCSRLRRGILYRTATELGATKIALGHHRDDILQTLFLNMFYGGKMKGMPPKLMSDDGKHIVIRPLAYCREKDIVRFAEAKAFPIIPCNLCGSQPNLQRQVIADMLRDWDKRYPGRIETMFSAMQNVVPSHLCDTNLFDFKGITHGSEVVDGGDLAFDREEIPLQPAGWQPEEDDTALEALRLDVIEVK", "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": "MSLIKIDQKAYEYNLRHIAKKIGSFQRLICVFKDNAYGHGAKLLAPLAKNLGVSFVAVKSEEEAREIEEFFENILILSHRPHGNENSRFIYALNDISQVKNYKQDIKIHLKIDTGMHRNGICVENLEHAIDLIRSSNLKLTGMFTHFASADEMDGSFFVQKENFQKAKKMVKKYFSNLLFHSHNSAALFRGKIPEDEYCRIGLVQFGYGDSNLKRILSLYAHRLSQRILQKGQSIGYGGIFTAVKDMEVATYDLGYADGLFRYNGKGELVLGNGKAMLGKMSMDSFSCENSGEEICVFKDADIWADFFHTINYEILVKLNPNIQRVLV", "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": "MSPSTSIEALDQPVKPVVFRPLTLRRRIKNSVATTFFFTSFVVALIPLVWLLWVVIARGWFAVTRSGWWTHSLRGVLPEQFAGGVYHALYGTLVQAGVAAVLAVPLGLMTAVYLVEYGTGRMSRVTTFTVDVLAGVPSIVAALFVFSLWIATLGFQQSAFAVALALVLLMLPVVVRAGEEMLRLVPDELREASYALGVPKWKTIVRIVAPIAMPGIVSGILLSIARVVGETAPVLVLVGYSHSINLDVFHGNMASLPLLIYTELTNPEHAGFLRVWGAALTLIIVVATINLAAAMIRFVATRRR", "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": "MKLDQAARALFLTELVSGFFLAMRYFFKPKATINYPFEKNPISPRFRGEHALRRYPNGEERCIACKLCEAICPAQAITIEAGPRRNDGTRRTTRYDIDMVKCIYCGFCQEACPVDAIVEGPNFEFATETREELYYDKEKLLANGDRWEREIARAIAADAPYR", "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": "MSRVCQVTGKRPVTGNNRSHARNATKRRFLPNLQTHRFWVESEKRFVKLRLTAKGMRIIDKKGIDIVLAEMRVRGESV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MAAQGATAAVAATTSGTVGEGEPGPGENAAVEGPARSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK", "text": "FUNCTION: Histone acetyltransferase which may be involved in transcriptional activation (PubMed:31794431). May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac (Probable). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120' (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the MYST (SAS/MOZ) family."}
{"protein": "MTEKIVVIVGPTEVGKTKLGIALAKKLGGEIISGDSMQIYKGMDIGTAKVKPDEMEGVPHHLLDIKEPCEPFSVVEFQRLARALITDISARGRLPIIVGGTGLYIQAAIYDYRFSDAPSDEAYRRALRQLAAEQGAEALHEQLKAVDPESAARIHPNNVRRVIRALEVYHCTGKPFSEWQRGQQRQLLYETALIGLTAERSVLYRRINERVDEMIAEGLIEEVRSLYDRGLRDCQAVQAIGYKELYDYFDGRVSLDEAIEQLKQNSRRYAKRQLTWFRNQMPVEWFDMTDPEKFAVKVEEIFRYIAGKLRLEANI", "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": "MRTPLVVGNWKMNGSRAANRALLESMRKEMEAGVTAEVAVCPPFVYLADMESLLQGSVINWGAQNLSHHEVGAYTGEIAPSMLADLGCRFVIVGHSERRTLYGETDSLVAEKAIVAQKVNIIPIICVGETLQEREQNITEQVVKRQLNAVLELAGVNALEKAVIAYEPIWAIGTGRTATPEQAQEVHALIRSHVAIQNSGIAEELLILYGGSVKGNNAAELLAMPDIDGGLIGGASLDAKEFLTICQAAG", "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": "MAASTMALSSPAFAGKAVNLSPAASEVLGSGRVTMRKTVAKPKGPSGSPWYGSDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGNGPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLADHLADPVNNNAWAFATNFVPGK", "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": "MQDMRLQGLYGISESGWYKRPHEAIELLLEAIEGGMKIFQLREKEGSDEEILPLARALWNHCRQKGVLFILNDRLDLALSLGVDGVHLGIDDAEASRARILLPHGIIGISCYGDLDRAHKAKEEGASYVAFGSCFPSPTKPASSVIDLTLFKKAQEELAIPLCAIGGIEAQNVGELIHCDMIAVISSLWSGGVAQVRKNAKGLIQSWRENRERV", "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": "MSKVVHFDASKLTPFVHENELKEMQAMVTAADQELREGTGAGSDFRGWIDLPINYDKDEFDRIKKAAKKIQNDSEVLVGIGIGGSYLGAQASIEFLNSSFYGREKEKYPTVVFCGNSLSGSYLYDLLEWLGDKDFSINIISKSGTTTEPSIAFRVLKDKLIKKYGKEEAAKRIYATTDRAKGALKTEADAEGYEEFVVPDDIGGRFSVLSAVGLLPIAVAGGDIDAMMKGAADARAAYTDPDVSKDNPYQYAALRNILYRKGYTTELLENYEPSLRMFGEWWKQLMGESEGKDQKGIYPSSANFTTDLHSLGQYIQEGRRNLMETVIRVESPEHDVTIPDDKENLDQLNFLSGKTMNYVNDRAYEGVVLAHTDGGVPVMTVDIENQSAHTLGYLIYWFELAVGISGYLNGINPFNQPGVESYKRNMFGLLNKPGYEDLHDDLTKRLK", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MANPTHSQVVAAPDSSGRLLRLVSASSVMMQLLGKSTNIRMSQILEHHEDEDFSAHRTKIVCTMGPSCWDVDKMVQLIDAGMNVCRLNFSHGDHEAHGRVVKNLQEALKQRPGKRVALLLDTKGPEIRTGMLEGDKPIELHAGDMLKIVTDYSFVGNKSCIACSYEKLPSSVKPGNTILIADGSLSVEVVECGKDYVMTRVMNPAIIGNKKNMNLPGVKVDLPVIGEKDKNDILNFGIPMGCNFIAASFVQSADDVRYIRSILGTKGRNIKIIPKIENVEGLLNFDEILQEADGIMIARGDLGMEIPPEKVFLAQKMMISKCNVAGKPVITATQMLESMTKNPRPTRAEAADVANAVLDGTDCVMLSGETANGSFPVQAVTVMSRVCFEAEGCIDYQQVFRATCQATMTPIDTQEAVARAAVETAQSINASLILALTETGRTARLIAKYRPMQPILALSASEETIKQLQVIRGVTTFLVPTFQGTDQLIRNALSAAKELQLVSEGDSIVAVHGIKEEVAGWSNLLKVLVVE", "text": "SIMILARITY: Belongs to the pyruvate kinase family."}
{"protein": "MKYELQTTDGRARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMNWHGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDSIFLSPEKSMEIQNDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRQRFDELENKNALFGIIQGSVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDVSSLDEHCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLELFVVDFYQRIGKPIPPLAEKDVAASN", "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": "MQILKENASNQRFVTRESEVNRICCGFNGFQLGERLRRDMKTSSITTLVVNTTTYFFKDTTELIDFKEKRIDLYEYARYGNPTTMALEEKISVLEGAESTLVMASGMYASNVMLLALVPTNGHIVATKDCYKETRIFMENFLTKLGITVTFIDSDDIAGLQTLVNNHEVSLFFTESPTNPFLRCVDIKLVSKICHRRGTLVCIDATIATPINQKTLALGADLVHHSATKYIGGHNDFLAGSISGSMELVSKIRNLHKLLGGTLNPNAAYLLIRGMKTMHLRVRQQNSTGMKMAQVLEAHPKVSRVYYLGLPSHPEHLIAKRQMTGIGGLISFEIDGDLKTTIKFIDALKIPYLAASFGGCESLVDQLATGIWDIPREERLKDGFQDNLVRFSFGIEDFEDIKADVLQALETI", "text": "FUNCTION: Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
{"protein": "MAGVTDVQRLQARLEELERWVYGPGGSRGSRKVADGLVKVQVALGNIASKRERVKILYKKIEDLIKYLDPEYMDRIAIPDASKLQFILAEEQFILSQVALLEQVEALVPMLDSAHIKAVPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAAKQVKPAEE", "text": "FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (PubMed:33734450, PubMed:36071160). Together with dynein is involved in spindle assembly and cytokinesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle Cleavage furrow Midbody Cytoplasm, cytoskeleton Note=Localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis. Colocalizes with dynein to the cleavage furrow and to midbody of dividing cells. SIMILARITY: Belongs to the dynactin subunit 3 family."}
{"protein": "MKIIAVIPARYASTRFPAKLMQDLGGKTVILRTYQAAVETNLFDDVFVVTDSELIYNEIITNAGKAIMSIKEHESGSDRIAEAIQNLEVDIVVNVQGDEPFINKEPLEEVIQVFRNDTHKKVDLASLMRNITHKNDIQNPNNVKVIVDQKGFALYFSRSVIPYPREENVGVRYMQHIGIYAFRKQALLDFYHLPMLSLEASEKLEQLRYLEYGKRIKMIETTHVGIGIDTLEDLEKARSML", "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": "MTFSVAVAGASGYAGGELLRILADHPDFDIRTVTAHQNAGQPLAAHQPHLRSLAGLTLSESTAENLAGHDVVFLALPHGKSGEIATQLPADTLVVDCGADHRLEDPDAWAAFYGGEHFGSWAYGVPELPVGAGRQRERLAGAKRIAAPGCNASAVSLALAPGIHAGLIEDADIVSVLAVGPSGAGKALKTMYLASEILGSANPYAVGGTHRHIPEIQQSLRKAGALSPTISFIPVLVPMSRGILATSTARVKPGVSAAQVQAAWEETYAGEPFVQVLPAGSVPRTSDVLGANTALIGVALDAAAGRVVAVLAIDNLYKGTAGAAIQSANIALGLAETAGLSVNGVAP", "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": "MANLRDIRKKIGSVKNTQRITHAMKLVSTSKLRKAEEVARNSRAYALKLDAVFDDVLSKMKNQGIEDIQSKYFRELERLEIKKVDIIFITADKGLCGGFNTNTIKKVLACTNEYKEKDIKVRLRGIGKKGNEYFSFNGIEVLDKINNLSSMPNYERAQEFMKKVVEDYLSGKTDKVIIIHNGFKNMITQEIRVKTILPIGYKIIHQNPQPSETQETITSEPSGSEDEILDSLAEKYVEYSLYYALIDSLAAEHSARMQAMDTATNNAKDLVKTLTISYNKARQEAITTELVEINAGVEALK", "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": "MTDNNTALKKAGLKVTLPRLKILEVLQEPDNHHVSAEDLYKRLIDMGEEIGLATVYRVLNQFDDAGIVTRHNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSDDSIEARQREIAAKHGIRLTNHSLYLYGHCAEGDCREDEHAHEGK", "text": "FUNCTION: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon. FUNCTION: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family."}
{"protein": "MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY", "text": "FUNCTION: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MVSAMRSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYKPHTITLLTFTTVSLMYFAFTRENTSQEDNIWKGILSVIFFFLIISVLAFPNGPFTRPHPAIWRMVFGLSVLYFLFLVFLLFLNVEQVKAVMYWLDPNLRYATRESDVMEYAVNCHVITWERILSHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWEMTELFFMHLLPNFAECWWDQVILDILLCNGGGILLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWIYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWCRILFIGIITAPTVRQYYAYLTDTQCKRVGTQCWVFGAIAFLEATVCIKFGQDLFSKTHLLYVFLWLFSVAVITFLCLYGMVWYADYCGQREKTFSECEDSTYNTDIPWHHIDKPVEAPVKQNEGTSRRKNRHKGKVTNGVGKK", "text": "FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (By similarity). Catalyzes mainly the conversion of phosphatidylcholine but also converts, in vitro and to a lesser extent, phosphatidylethanolamine (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Highly enriched in the mitochondria-associated membrane (MAM). SIMILARITY: Belongs to the phosphatidyl serine synthase family."}
{"protein": "MIFEHALVLSAFLFSIGIYGLITSRNMVRALMCLELILNAVNINLVTFSDFFDRRQLKGNIFSIFVIAVAAAEAAIGPAIVSSIYRNRKSTRINQSNLLNK", "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": "MLSDFYKYATSTQLDLICTQLINLSTHVFNTNNGNIPKWEQAIKQIKTQNTGSLDFITPYLNISAHHINNFTLEKSLKQLIPWRKGPYQIGDLQLDSEWRGDMKWHRLIPHIKPLKDKVVLDVGSGNGYFTYLMAISGAKIALGIEPFLLFNYQFQAIRTLINNLPNVFVLPLSLDKIPKKPLFDTVFSMGVLYHQKDYELHLNQLKDVMKPSGELILETLIIDLEKVKKIIPKGRYAKMRNVYCLPSKNTLRTWLEDAEFKNIKLLDVTKTTSKEQRATHWIGNNTQSLKNFLDPNNRDLTIEGFPAPKRAIFICQK", "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": "MSEDKYCLVTGGAGYIGSHTVVELCEAGYKCIVVDNLSNSSYESVARMELLTGQEIKFAKIDLCELEPLNKLFDDYKIDSVLHFAGLKAVGESTQIPLTYYFNNIVGTINLLECMKSHDVKKLVFSSSATVYGDATRFENMIPIPETCPTGPTNPYGKTKLTIEDMMRDLHFSDKSFSFAILRYFNPIGAHPSGVIGEDPLGIPNNLLPFMAQVAIGRRPKLYVFGDDYDSVDGTPIRDYIHVVDLAKGHLAALKYLEKYAGTCREWNLGTGHGTTVLQMYRAFCDAIGFNFEYVVTARRDGDVLNLTAKCDRATNELEWKTELDVNKACVDLWKWTQDNPFGYQIKGVDSKFFGDKGDFSSRVVSLGKGTSFEVKLANLGATIVDIVVNGCSVVASLDNETEYKDQSNPFFGATVGPYANRIANGTFEINGKRIQLTVSKEDGNVVHSGINSYHSKKFLGPIVKNPEAHIWTADFKYVDEETEFPARLSTLVRYKVDSEKKTLTVEYESKVAGQGSTGANITNHTYFNLNKFNEATIKGSKVQLIDNTGLEVNNKLLPTGNLKKYTQVATFNDSPTEITEKEPVLDFCFVSGLPAKLDTRSSPLTPVFKLSNEDAKLEVEVATTEPTFQVYTGDYVDVKDKYENRAGICCEPGRYIDAVNNPEWKSSVVLPAGETYGHKLSYTFRTL", "text": "FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity). SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. SIMILARITY: In the C-terminal section; belongs to the aldose epimerase family."}
{"protein": "MAQNTLRLVEENGVDKSKALDAALSQIERAFGKGSIMRLGANDKVVEIETISTGSLGLDIALGVGGLPRGRIIEIYGPESSGKTTLALHTVAEAQKKGGICGFIDAEHALDPVYARKLGVDLENLLISQPDTGEQALEICDTLVRSGAVDVIVVDSVAALTPRAEIEGEMGESLPGMQARLMSQALRKLTASISRSNTMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSVKDREETVGNQTRVKVVKNKMAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGVVEKAGAWFSYNSQRLGQGRENAKLFLRDNPEVAREIELALRQNAGLIAERFLEADKDGSLDDAAES", "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": "MRVLGIETSCDDCCAAIVEDGVKILSNIKLSQKEHKKYYGVVPEIASRLHTEFIMSVCQQAITNAQIHASEIDLIAVTSKPGLIGSLIVGVNFAKGLSIALKKPLICIDHILGHLYAPLMIKKIEYPFLSLILSGGHTILAKQNNFDDIEILGRTLDDACGEAFDKVAKYYKMGFPGGPNIEKLAKNGNQYAFNFPITIFDKKENRYDFSYSGLKTACIHQLEKFKDKNENITKNNIAASFQRVAFENLIIPIKRAIKDTNIKKLIISGGVASNLYLREKIKNLEIETYYPPIDLCTDNGAMIAGIGYLMYLKYGASPIEIDANSRIENYKHTKGKTV", "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": "MVIKAKSPAGFAEKYIIESIWNGRFPPGSILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTKVNQFMETSGLHILDTLMTLDVDNATNIVEDLLAARTNISPIFMRYAFKVNKENSERTIKTVIDSCEQLVAAESWDAFLSSSPYADKIQQNVKEDNEKDEAKRQEILIAKTFNFYDYMLFQRLAFHSGNQIYGLIFNGLKKLYDRVGSFYFSNPASRELALKFYRQLLLTCESGQREQLPALIRQYGIESAMIWNEMKKQLPTNFTEDDC", "text": "FUNCTION: Multifunctional regulator of fatty acid metabolism. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MPDAVKVGFVPFATPARGTLIVFCDDGLKFGATATKALGAAVATVKRAAATAQFKGKSGSAMDLLAPEGLKVGRLIVVGAGKVASINDYDLLKLGGAVAGKIGAGDTAVTVVADLPTGAMKPEQAAAIASGIRLRAYKFDRYKTKKKDDENGAANASVTLAVADPAAAKKAFTPDSHVVDGVILARELVNEPPNVLYPEEFAKRAAQLKKLGVEVQILDVKAMTQLKMGALLGVSQGSAHPGRTVIMRWNGGKKGEQPLAFVGKGVCFDTGGISIKPSASMEDMKGDMGGAACVVGLMHALAARKAKVNAVGAIGLVENMPDGNAQRPGDIVTSMSGQTIEIINTDAEGRLVLADVLWYVAQKHKPKFMVDLATLTGAIMVALGTEYAGLFSNNDQLAERLAAVGQSTGEKVWRMPLGPEYDKQIDSQFADMKNTGSRNGGSITAAQFLQRFVDGTPWAHLDIAGTAMASPKNEINQSWGSGYGVRLLNQLVAEYYEAKK", "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": "GANDFMRF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
{"protein": "MPIIKVRDNEPFDVALRRFKRSCEKAGILADVRAREFYEKPTTARKRAKAAAVKRLAKKLSRENARRVRLY", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
{"protein": "MSTSSSDPFYNFAKTSFKSAAAQKASATSLPPLPGPDQKVPGMDIKYDVVIVGSGPIGCTYARELVEAGYKVAMFDIGEIDSGLKIGAHKKNTVEYQKNIDKFVNVIQGQLMSVSVPVNKLVVDTLSPTSWQASTFFVRNGSNPEQDPLRNLSGQAVTRVVGGMSTHWTCATPRFDREQRPLLVKDDPDADDAIWDQLYTKAESYFKTGTDQFNESIRHNLVLNKLAEEYKGQRTFQQIPLAATRRNPTFVEWSSANTVFDLQNRPNIDAPEERFNLFPAVACERVMRNASNTAIESLHIRDLISGDRFAIQADVYVLTAGAVHNTQLLVNSGFGKLGRPDPANPPELLPFLGSYITEQSLVFCQTVMSTELIDSVKSDMTIIGNPGELGYSVSYMPGASTNKHPDWWNEKVQNHMMQHQEDPLPIPFEDPEPQVTTLFQPSHPWHTQIHRDAFSYGAVQQSIDSRLIVDWRFFGRTEPKEENKLWFSDKITDAYNMPQPTFDFRFPAGRTSQEAEDMMTDMCVMSAKIGGFLPGSLPQFMEPGLVLHLGGTHRMGFDEQEDNCCVDTDSRVFGFNNLFLGGCGNIPTAYGANPTLTAMSLAIKSCEYIKKNFTPSPFTPAQ", "text": "FUNCTION: Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase (By similarity). SUBCELLULAR LOCATION: Periplasm Note=Hyphal periplasmic space. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MHEGVQVSSKLEELQALLAPVVVALGYECWGIEFSAQGRHSMLRVYIDKEGGVLVDDCAIVSRQISGVLDVEDPISVEYTLEVSSPGMERPLFTIDQFAKFAGEQVKIKLRSPFEGRRNFQGLLRGVEEQDVVVQVEDHEFLLPIDMIDKANIIPSFD", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MSEFWLISAPGDKENLQALERMNNVTSKSNLSHNTKFAIPDFKVGTLDSLVGLSDELGKLDTFAESLIKRMAQSVVEVMEDSKGKAHETLLANGVDLTSFVTHFEWDMAKYPAKQPLVSVVDTLAKQLAQIETDLKSRTAAYSVLKANLENLEKRSTGNLFTRTLSDIVSKEDFVLDSEYLITLLVIVPKSSFAQWQKTYESLSDMVVPRSTKLIAEDNEGGLFTVTLFRKVIEDFKVKAKENKFIVREFYYDEKEIKREREEMTRLLSDKKQQYPTSCVALKKGSATYRDHKVKVAPLGNPARPAAGQTDRDRESEGEGEGPLLRWLKVNFSEAFIAWIHIKALRVFVESVLRYGLPVNFQAVLLQPHKKSATKRLREVLNSVFRHLDEVAAASILDASVEIPGLQLSNQDYFPYVYFHIDLSLLD", "text": "FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit 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). SIMILARITY: Belongs to the V-ATPase C subunit family."}
{"protein": "MENSEKLANSKEVIAYIAERFPKCFILEGEAKPLKIGIFQDLAERLSDDSKVSKTQLRAGLRQYTSSWRYLHGVKPGASRVDLDGNPCGELEEEHVEHAKASLEESKAKVAARRKEQAKKAREEAKAKKPARATTPPKRRPQPAAVAKKQEKPVETRALNSDEITVGNNVSVNMGKGNMPATIVEINKDDVRIRLSNGLQMVVKAENLRS", "text": "FUNCTION: RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ProQ family."}
{"protein": "MKFSKLSITLAVILTQAVFVLCGMKNEDFMEKGLESNELHDAIKKPVNSGKPDTERLLDCVLSRVCSSDANCCGLTPTCKMGLCVPKVGGLLGGLLGGIL", "text": "FUNCTION: Potent inhibitor of insect, but not mammalian, voltage-gated calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 15 family. 02 (omega-actx) subfamily."}
{"protein": "MIDFTNFYSSIAKNRLSHWLRTLPMQLHEWENTHVHGQLASWIRVLNKFPDIKTSHIELKDRVEIGSATELSPGETKKLENLLQKFHPWRKGPFVIHGIHIDTEWRSDWKWDRLLPHISPLKYRYVLDVGCGSGYHMWRMRGEGAEFVVGIDPSELFLCQFEAVRHFANKEQNVHLLPLGIQELPKLGAFDTVFSMGVLYHRKSPMDHITQLQDQLVEGGELVLETLVIGGDENAVLVPQDRYAKMRNIWFLPSAQALKLWVEKCGFENVRIADINDTLTGEQRSTAWMTNESLEDYLDPNDPSRTVEGYPAPKRALLIAKKAIKALS", "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": "MARIAGVDIPRDKRVVISLTYIYGIGKPTAQKILKEAGVSEDTRVRDLTEEELGRIREIVGRLKVEGDLRREVSLNIKRLMEIGCYRGLRHRRGLPVRGQNTKNNARTRKGPRRTVANKKK", "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": "MAFLTHLLVCVFGMGSWVAINGLWVELPLLVTELPEAWYLPSYLTVVIQLANIGPLLVTLMHRFRPGCLSEVPVIFLILCVGTAACILLAFLWNVTSWIQGGQHSVAFIVLTFFLALVDCTSSVTFLPFMSQLPTYYLTTFFIGEGLSGLLPALVALVQGSGITTCVNVTETPGTTLNTMETPITQGNLSPSLPSPSWHQESRYLAPRFSPLLFFLLLSFLTGCCLVAFFLLQRQPWGRQGSIEDLLHSQVTLHSIRPRDTEDTSSLGAPVSSPGKGSVEASVASLRPAQLAFIYSVVAFVNALTNGVLPSVQTYSCLPYGPVAYHLSATLSSVASPLACFLPIFLPNRSLLFLGVLTVLGTGFGAYNMAMAAMSPCPVLQGHWGGEVLIVLSWVLFAACLSYVKVMLGVILRDRSRSALLWCGAAVQLGSLIGALLMFPLVNVLKLFSSADYCSLDCSV", "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": "MEDLTEKQSLVFEFIMEYTADHGYPPTVRELCDELGFKSPNTAHFHLKGLKDKGYIQSAKGKNRGITVLKTPPGAGGKIPLVGRIAAGAPILAVENVMDTLDVDRAFFGSSDAFSVRVEGDSMIEAHIEDGDYVVIKPTATPRNGDIVAALVNDEVTLKYFHRDGSRIELRPANVRYKPFCYTEEDFIDVRVLGVMAGLIRKV", "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": "MAQLALLLLSLFLTLISLAPPGASISSCNGPCRDLNDCDGQLICIKGKCNDDPQVGTHICRGTTPSPQPGGCKPSGTLTCRGKSYPTYDCSPPVTSSTPAKLTNNDFSEGGDDGGPSECDESYHNNNERIVALSTGWYNGGSRCGKMIRITASNGKSVSAKVVDECDSRHGCDKEHAGQPPCRNNIVDGSNAVWSALGLDKNVGVVDITWSMA", "text": "FUNCTION: [Kissper]: pH-dependent, voltage-gated and anion-selective pore-forming peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kiwellin family."}
{"protein": "MKTLLVRISGKVQGVWYRGWTVETAKGLGLAGWVRNRADGTVEALFHGPEAAVEAMLIACRGGPPSARVDDLRVTPVAAPDQPGFSQKPSL", "text": "SIMILARITY: Belongs to the acylphosphatase family."}
{"protein": "MHVGVLGGTFDPPHNGHLALALFARELLCVDRLILSVSDNPLKQRRSASDSQRKAMTELLCHEINRTGTFCDACGWELEQKRPSYTVNLLRFVRSLYPSARLSLLVGEDSWRNFGSWKSPEEIEELADVVVFARGAEHMTERPDAVSGIRFVEFSCPLSSTMLRGRIAEGQSVSSLLPSSIDRYIRREGLYGE", "text": "FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). SIMILARITY: Belongs to the NadD family."}
{"protein": "MVEEVQKHSVHTLVFRSLKRTHDMFVADNGKPVPLDEESHKRKMAIKLRNEYGPVLHMPTSKENLKEKGPQNATDSYPHKQYPANQGQDVEYLVTGTHPYPAGPGVALTADTKIQRMPSESAAQSLAVALPSQTRVDANRTGPAGSEYRHPGASDRSQPTAMNSIMETGNTKNSALMAKKAPTMPKPQWHPPWKLYRVISGHLGWVRCIAVEPGNQWFVTGSADRTIKIWDLASGKLKLSLTGHISTVRGVIVSTRSPYLFSCGEDKQVKCWDLEYNKVIRHYHGHLSAVYGLDLHPTLDVLVTCSRDSTARIWDVRTKASVHTLSGHTNAVATVRCQAAEPQIITGSHDTTIRLWDLVAGKTRVTLTNHKKSVRAVVLHPLLYTFASGSPDNIKQWKFPDGGFIQNLSGHNAIINTLAVNADGVLVSGADNGTMHLWDWRTGYNFQRVHAAVQPGSLDSESGIFACAFDRSESRLLTAEADKTIKVYREDETATEETHPVSWKPEIIKRKRF", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre- mRNA splicing. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the WD repeat PRL1/PRL2 family."}
{"protein": "MRSPLVLLDGASMWFRSFFGVPSSITAPDGRPVNAVRGFIDSMAVVITQQRPNRLAVCLDLDWRPQFRVDLIPSYKAHRVAEPEPNGQPDVEEVPDELTPQVDMIMELLDAFGIAMAGAPGFEADDVLGTLATRERRDPVIVVSGDRDLLQVVADDPVPVRVLYLGRGLAKATLFGPAEVAERYGLPAHRAGAAYAELALLRGDPSDGLPGVPGVGEKTAATLLARHGSLDQIMAAADDRKTTMAKGLRTKLLAASAYIKAADRVVRVATDAPVTLSTPTDRFPLVAADPERTAELATRFGVESSIARLQKALDTLPG", "text": "FUNCTION: 5'-3' exonuclease acting preferentially on double-stranded DNA."}
{"protein": "MTSIFGYPKEELQLDLVAHGFKKYLAEQIFDWIYVKNIYSFDEMTNISKTDRNKLQEYYTIEPLKIVVQQQSKDWTVKFLFQLADGYKIETVLMPQSYGNSVCVTTQVGCNMACTFCASGLLKKTRNLSTAEIVQQVMMVNRYLATTNERVSHIVVMGIGEPFDNFDNTLKFVNIINDPKGYQIGARHITISTCGLVPKIKQFAELKTQVNLAISLHAPNNTIRNQLMPINKAYPVEKLMDAVRYYIELTNRRVTFEYILIENVNDSRETALELAKLIRGLNAYVNLIPYNTVAENGHQRSTKINKFFETLQQQKINCIVRREFGHDIDAACGQLRAKNEGVIRK", "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": "MAKKLKIKLVKSPIGYNRRQRATLKALGLRKISDEVVHDDSPQIRGMINAVIHMLEVKEIEN", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MARPGLTIALLLTTPNLVDACQQWLPDTRYHSIVLSGPHQGQEQLDLVSTLEAQQEEIDAVVVEQQLLDASSRDQLLGRGLLFPAVVVGEMKGHVDYHAEELHLAEDQLAQLGYTVDAAISRFLRQGRADGRSDDDGLASVDKLSRRLQERLGYLGVFYKRDPSRFLGSLPTEERRELLESLQRTYRDLLISYFSDPAASNQALESFVNTAFFSDLPITRTVDIHVDQIDEFWKQLRLEGNKSEFLQDYRLALLDVMAHLCEMYRRSIPPDIPLSGLASGRHRREADLPDAPEVSS", "text": "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. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator. FUNCTION: Binds oxidized quinones via the N-terminal PsR domain, allowing it to sense redox changes and possibly mediate clock input."}
{"protein": "MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPHAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGGLGKQSEGLSDKLGFGLEDEPLETATKDN", "text": "FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5- trisphosphate receptors (IP3Rs) such as ITPR1. Promotes sterol- accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex. Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane. SIMILARITY: Belongs to the band 7/mec-2 family."}
{"protein": "MLKRDMNIADYDADLFAAIQEETVRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACELFGAEYANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNFSGKLYNIIPYGIDENGQIDYEEMEALAVEHKPKMIIGGFSAYSQVCDWARMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILSNEGEDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARGYNIVSGSTENHLFLVDLIDKDITGKEADAALGSANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFTEEDAKNLAGWMCDILDNMGDESVIEATKAKVLEICKRLPVYA", "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": "MPVFLSSRFLFFCIIVPLLISITLYQLDTFDPAHHPADSLISSTASIPPLINERFLTGAEFIGVGLLNSPEDIAYHEDSGFIYTGCVDGWVKRVKVAESVNDSLVEDLVNTGGRPLGIAFGIHGEVIVADAYKGLLNISGDGKKTELLTEEADGVRFKLPDAVTVADNGVLYFTDGSYKYNLHQFSFDILEGKPHGRLMSFDPTTKVTRVLLRDLYFANGVSLSPDQTHLVFCETPIRRCSKYYINGGRVELFIQGLPGYPDNIRYDGDGHYWIAMPSGVTTLWKLSMKYPFLRKITAMAAKYGYEPMFMENAGVLQVDLDGNPIAYYHDQALSHITTGVKIGNYLYCGSLWHSHILRLDLLKYPAQNKKL", "text": "SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the strictosidine synthase family."}
{"protein": "MSVQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSNTCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAELLREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFREDLIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGKLSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKVDSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLGINSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQPFLKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVLGGGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDSSELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSASEAAEVLLRVDNIIRARPRTANRQHM", "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. In yeast may play a role in mitotic spindle formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MKSIEELYKRALELKNKGMSDKEISTELHLSVNTVTWLLSKEFLKEGAVQDVKIGWRSLGVFGSRIISIAEVMSDIIREEMQRNSFEVDSILGIAINGIPYATMVSYLMDKELIVYRPHPARKEGFFSSNFAGVEGKRIVIIDDVASTGETLKRTITDVTKEGGKAVLCVILASKMGVDDLNGVPVRSLLRTRIIGGT", "text": "SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MEAAAGERAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDQEQSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALRPYRPLGALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVVHRMSALCS", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure (PubMed:23807208). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, microtubule organizing center Note=Enriched at the centrosomes during mitosis (By similarity). Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis (PubMed:23807208). Localized at centrioles and in the nucleus at interphase (PubMed:23807208). Colocalizes with nubp-1 at prometaphase (PubMed:23807208). SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily."}
{"protein": "MTIMRKKHPLLKMINHSFIDLPTPSNISSWWNFGSLLGMCLMIQILTGLFLAMHYTSDTTTAFSSVAHICRDVNYGWLIRYLHANGASMFFICLFIHVGRGIYYGSYMLLETWNIGIVLLLTTMATAFVGYVLPWGQMSFWGATVITNLLSAIPYXGNTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPSGLDSNSDKIPFHPYYTIKDLLGALILLMVLMILVLFFPDVLGDPDNYTPANPLNTPAHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILATLPLLNSSKQHGLIYRPITQALYWIFVANLLTXTWIGGQPVEXPFTLIGXIASXLXFXIIIIFMPIASTIXNNIPXLH", "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": "MSITFGELVGNFILVTGSVIVLLLLIKKFAWGAIESILQTRSQQISRDIDQAEQSRLSAQQLEAKSQANLDASRSQASKIISDAKEIGQLQGDKLVAEATDEAKRLKEKALTDIEQSKSDAISAVKTEMSDLTVLLAEKIMGANLDKTAQSQLIDSYLDDLGEA", "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": "MQRSDPPRPLLEMRGISKTFPAVRALAGVSLTVHPGEVHSLMGENGAGKSTLMKILSGAYQADPGGEILIDGRPISIDGPLAARDAGVAVIYQELCLAPNLSVAENIHVGRELRRGNGRRGTIDRAAMARGCQDVLERLGADFGPNTLVGTLSIAEQQLVEIARAVHTRARILVMDEPTTPLSSRETDNLFRLIRQLRAEGLAIIYISHRMAEIYELSDRVSVLRDGAYVGTLERDALSAERLVGMMVGRDISGFYKKAHAPYDPGNLLLSVRDIADGARVRGCSLDLHAGEVLGIAGLVGAGRTELARLIFGAEPRVRGEVTLAGKAFAAHSPREAIDAGLVYLTEDRKRQGLFLDMSVRENINISVCGRDARLGALDLARGAQRARDAIAALSIRVPHANVNVGALSGGNQQKVLLSRLLETKPRVLILDEPTRGVDIGAKSEIYRIINELARAGVGVIVISSELPEIIGVADRVLVMREGRIAGELGGRTDAPITQEAIIALATGSRTEASAAH", "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": "MTSKSPKFRIGNGYDIHRLEIGRKLIIGGVKLNHPDNLGLDGHSDADVLSHSIMDALLGALSLGDIGKYFPPSDEKWKDVDSLILLSKVIDLVRKQGWEINNIDSVIVAERPKIKPYVEIMKRNLSKTLKIDDSFIGIKATTNEKLGPEGREEGISCHSVVLLEKK", "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": "MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQVESFDQFVILLKNTVSQMVYKHAISTVVPSRPFNVSNHQATNAQAGFNAQHDDGDDK", "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": "MEKPSREAFEGNNKLLIGIVLSVITFWLFAQSLVNVVPILEDSFNTDIGTVNIAVSITALFSGMFVVGAGGLADKYGRIKLTNIGIILNILGSLLIIISNIPLLLIIGRLIQGLSAACIMPATLSIIKSYYIGKDRQRALSYWSIGSWGGSGVCSFFGGAVATLLGWRWIFILSIIISLIALFLIKGTPETKSKSISLNKFDIKGLVLLVIMLLTLNILITKGSELGVTSLLFITLLAIAIGSFSLFIVLEKRATNPLIDFKLFKNKAYTGATASNFLLNGVAGTLIVANTFVQRGLGYSSLQAGSLSITYLVMVLIMIRVGEKLLQTLGCKKPMLIGTGVLIVGECLISLTFLPEILYVICCIIGYLFFGLGLGIYATPSTDTAIANAPLEKVGVAAGIYKMASALGGAFGVALSGAVYAIVSNMTNIYTGAMIALWLNAGMGILSFVIILLLVPKQNDTQL", "text": "FUNCTION: Multidrug efflux pump that acts independently of NorA and is one of the factors that confers resistance against diverse quinolones and chemical compounds. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MDSNTVSSFQVDCFLWHVRKRFADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILKEESDEALKMTIASVPASRYLTDMTLEEMSRDWFMLMPKQKVAGSLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTDEDVKNAVGVLIGGLEWNDNTVRVSETLQRFAWRSSNENGRPPLPPKQKRKMARTIKSEV", "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": "MAKISRAAYADMFGPTVGDRVRLGDTELWIEVEKDYATYGHEVKFGGGKVIRDGMGQSQRPNTEAVDTVITNALILDHWGVVKADIGLKQGRIAAIGKAGNPDIQDNIDIIIGPGTEVIAGEGMIATAGGIDAHIHFICPQQIEEALMSGVTTMLGGGAGPATGTNATTCTPGPWHMGKMLQAADAFPMNLGFLGKGNASLPAALEEQMLAGAMGLKLHEDWGTTPASIDNCLNIAEKYDVQVAIHTDTLNESGFVEDTLAAFKGRTIHTYHTEGAGGGHAPDIIKACGELNVLPSSTNPTRPYTINTVDEHLDMLMVCHHLDPDIPEDVAFADSRIRKETIAAEDILHDLGAFSMISSDSQAMGRVGEVVCRTWQTAHKMKVQRGPLAQDSERADNFRAKRYIAKYTINPAIAHGIAHEVGSLEPGKLADIILWRPAFFGAKPSLIIKGGMIAAAPMGDANASIPTPQPVHYRPMFGAFGRAMQQTRLTFVCQAALDNGVKEQFGLQSPLSACRNTRTVTKKSMVLNDLTPQMEVDSQTYEVRANGELLVCEPAKVLPLAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "ILGKLLSTAAGLLSNL", "text": "FUNCTION: Shows more potent growth inhibitory activity against the Gram-positive bacteria S.aureus (MIC=50 uM) than against the Gram- negative bacteria E.coli (MIC=150 uM). Has a weak hemolytic activity against human erythrocytes (LC(50)=135 uM). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Alyteserin-2 subfamily."}
{"protein": "MTELNKLTLADSIKGLKNKDFTSTELVNAHIQQIEKHKNLNAYVTKTFDLALKGAQIADQNYAQNKARTLEGIPFAAKDLFCTKGIRTTACSNILKNFIPNYESSVTQNIFNNGGVMLGKTNMDEFAMGAANITSCFGNVINPWKANNDNSDLVPGGSSGGSAASVSGFMASAALGSDTGGSVRQPASFTGLVGFKPTYGRCSRYGMVSFASSLDQAGIFTRSVLDSAIMLEAMMGFDEKDSTSLKAEVPQLQSAIGSSVKNMKIGVPLSLGEGSIIEPDVMKMWQDTIELLKNAGTEIVDITLPYAKYGVAVYYVIAPAEASSNLSRYDGVRYGLRVERENMTLDEMYEMTRSAGFGEEVKRRIMIGTYVLSSSCMDAYYLKAQKVRSLVANDFNNAFTKVDTILLPAAPSEAFKIGEKQNDPTIMYLNDLFTIPASLAGLPCVSVPAGLSARGLPLGMQIIGKQLDEYNVLKVASTIESGVKHIKFEPKGF", "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": "MLTITSYFGFLLAALTITSALFIGLSKIRLI", "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 (By similarity). Seems not to be required for photosynthesis. 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": "MAWENVRVRVAPSPTGDPHVGTAYMALFNEIFAKRFNGKMILRIEDTDQTRSRDDYEKNIFSALQWCGIQWDEGPDIGGPHGPYRQSERTEIYREYAELLLKTDYAYKCFATPKELEEMRAVATTLGYRGGYDRRYRYLSPEEIEARTQEGQPYTIRLKVPLTGECVLEDYCKGRVVFPWADVDDQVLMKSDGFPTYHFANVVDDHLMGITHVLRGEEWLSSTPKHLLLYEAFGWEPPIFLHMPLLLNPDGTKLSKRKNPTSIFYYRDAGYIKEAFMNFLTLMGYSMEGDEEVYSLEKLIANFDPKRIGKSGAVFDVRKLDWMNKHYLNHEGSPENLLARLKDWLVNDEFLLKILPLCQSRMATLAEFVGLSEFFFSVLPEYSKEELLPAAISQEKAAILFYSYVKYLEKTDLWVKDQFYLGSKWLSEAFQVHHKKVVIPLLYVAITGKKQGLPLFDSMELLGKPRTRMRMVHAQNLLGGVPKKIQTAIDKVLKEENFENKILEF", "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": "MSEEAWARSAGGRAILAESPRPVPSRQRSNGVVRLRVARAGIAADGPTRIVDLAEGGPLRLRFPRQGAERMLEGVLVNTGGGVACGDVFEVSVMVEAGAACLLTTTAAEKIYRSDGANATILNRIEVGPAGRLDWLPQETILFDRARLVRRFEADLAPDASLLVAEIAVLGRAARGERLEQALFEDRWRIRRGGRLVYADSLRLDGAVSDLMARAATGGGARALATLLDLAPGAEARLDEARTLLDALPAGVEAGASAWNGHLAVRMLAPAIAPLREAAARFLAVWRDRPMPRVWQS", "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": "MIVLGVDPGLTRCGVGVIEAGAYRRLSFIHVDVVRSDPHESQDLRLLKIYDGLCAKMDEFIPDTVSIERVFAQENRNTVLGTAQAAGMAMLAAAQRGIPVALHTPTESKMAITGNGKAEKIQMERMVARILNLNALPTPADAADALAIAICHALRPSGALEGGEREQHLTPAQRQWAQATQHATRRRGVRRGM", "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": "MRNQSSLSDRLTVEVDCSSLGSNECPSMTSSFSPLESPTPTPTSIYSQGSLESPGWHGAGSLPNNTYERTPGSASMRSAFRLAGMASTESLGLPYGSMEGQERMPMPDFLSGYDENIEQLWMPSEAPKSYDHVAQGLAYHQGMHQYPTMARNTNNNYRHQAAAYLPESTTNPCLSRSIFHQPERVPSSMSSSMSMNNMLPWMNLGDSIAPQTIAPSQVGPVTPPPSYTDFPTSLSAFKQHSPTTPIRSCSLGTGSGADTPLSRLSGGPCEYMDDFQPSPVYRDGFQRPHRVASRKMLRRQTSKQNLMLENLPQVIKQVQFKCKEPGCNGRFKRQEHLKRHMKSHSKEKPHVCWVPGCHRAFSRSDNLNAHYTKTHSKRGGRNRYVATLDENSPDYDPEFRGQLTPDGRPIYGSKLDDPIPGAGDMSLDGWDE", "text": "FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:8508769, PubMed:5366214, PubMed:2823119, PubMed:2655931, PubMed:2196567, PubMed:7704830). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (PubMed:2823119, PubMed:2655931, PubMed:2108321). Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'- (C/A)(A/G)AGGG(G/A)-3' (PubMed:8417986). Controls the expression of the conidiophore-specific phenol oxidase ivoB (PubMed:1901560). Controls the expression of the hydrophobin rodA (PubMed:2065971). Mediates the developmental switch from the indeterminate, apical growth pattern of vegetative cells to the budding growth pattern of conidiophores (PubMed:3293800). Expression of brlA leads to activation of abaA, wetA and stuA, cessation of vegetative growth, cellular vacuolization and spore formation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNKLLCCALVFLDISIKWTTQETFPPKYLHYDPESSRQLMCDKCPPGTFLKQPCTARRKTVCAPCPDHYYTDTWHTSDECLYCSPVCKELQYVKQECSRTHNRVCECEEGRYLELEFCLKHRSCPPGFGVLHPGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSAFGLLLTQKGNATHDNICSGSSESSTHKCGIDMTLCEEAFFRFAVPTKLTPNWLSVLVDNLPGTKVNAESIERIKQRHNSREQTFQLLKLWKHQNKDQDMVKKIIQDIDLCENSVRRHIGHLNLTFEQLLKLMESLPGKKVTTEDVEKTVKTCKSSEQLLKLLSLWRIKNGDQDTRKGLLHALKHLKTYHFPKTVIQSLKKTIRFLHSFTMYRLYRKLFLEMIGNQVQSLKISCL", "text": "FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTISKFNPQKPFECFIVQSEAMKSAVENAKRFAMFDAPLLIQGETGSGKDLLAKACHYQSLRRDKKFIAVNCAGLPDEDAESEMFGRKVGDSETIGFFEYANKGTVLLDGIAELSLSLQAKLLRFLTDGSFRRVGEEKEHYANVRVICTSQVPLHLLVEQGKVRADLFHRLNVLTINVPALRDRMADIEPLAQGFLQEISEELKIAKPTFDKDFLLYLQKYDWKGNVRELYNTLYRACSLVQDNHLTIESLNLALPQSAVISLDEFENKTLDEIIGFYEAQVLKLFYAEYPSTRKLAQRLGVSHTAIANKLKQYGIGK", "text": "FUNCTION: 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 (By similarity). Acts by binding specifically to TyrR boxes in the promoter region of the target genes (PubMed:9226720). Can efficiently repress the transcription of the aroF promoter, but lacks the ability to function as a transcriptional activator (PubMed:9226720). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MVGGDEVIANSFLEAGELVSFKRGEDIVSQGDVEDDSVYFLLSGAADVFVNGKRRDDIQRTAPITVGEMSALNPAQKRSATVRAASRQLVALKVEGETFRKVVGENREFLRRVHEDFSGRGRQAILATGISRRTSGWNWTVISLTAGVLSAAAIWYTLRVDGNPVFVRVLLPLVVGLTIFLLTLLADPVYRFFRLGTLCVGAILVDEALQWQVRGSFMGAEFQYQISSSGDPQQATALLAPIVLGALAAYLFWIDTTKR", "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 B Pycsar system. FUNCTION: The effector gene of a two-gene Pycsar system. Expression of this and adjacent uridylate cyclase RsmPycC (AC A0A1V0HUX5) probably confers resistance to bacteriophage. The genes are probably only expressed in response to bacteriophage infection. Probably only responds to cUMP (produced by its cognate NTP cyclase), it may act by degrading NAD(+) and/or by impairing membrane integrity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MKVALIGITGYGGMVLYQMLKTHPGIDQVDLYARHLAGPTPLNQLVPNLFDDQPVYPYDSQKILANDGAVFFATPAGVTKTAARPYLTAHFPVIDLSGDYRLKNGATYEKWYHQSPAATADLKVAHYGLTDFCDATDENLIANPGCYATATLLGLAPLIIDQLIDLDTIVVDAKSGTSGAGKKPTSSTHFTQVNENAQLYNVNHHKHIPEIVQQLQAWDPAVDAIQFSTTLLPITRGILATIYAKPKPGVNKDQVVAAFKQTYATDPFVRYTGENLPTIKQVVGTNYCDLGVLFNERANTIMVASVIDNLIKGAGGQAIQNFNQRFNFAPTAGLPTAPLLP", "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": "MPLILLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVELSGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQIIDGEHRLRGRGWETDGGDLWDVLERLDSEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTHRGVEGAIVGKALYARRFTLPQALAAVRD", "text": "FUNCTION: Involved in both the histidine and tryptophan biosynthetic pathways. FUNCTION: Involved in both the histidine and tryptophan biosynthetic pathways. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MPHGTLEVVLVSAKGLEDADFLNNMDPYVQLTCRTQDQKSNVAEGMGTTPEWNETFIFTVSEGTTELKAKIFDKDVGTEDDAVGEATIPLEPVFVEGSIPPTAYNVVKDEEYKGEIWVALSFKPSENRSRGMDEESYGGWKNSEASY", "text": "FUNCTION: Binds to both sense and antisense RNA (By similarity). Can also bind sheared DNA and dodecamer DNA with a low affinity (By similarity). Interacts with mesophyll plasmodesmata to mediate its own cell-to-cell transport and potentiate RNA trafficking (By similarity). May play a role in plant defense signaling (By similarity)."}
{"protein": "MNIRYLLLLSLMPHLVWAAEEPTPEIPFSQCLIEPPVSRSFDDRAQLTDIDPNDIVIISDRTDASFNKQAHFDGDVSFSQGQRHIAADKATLDQRQQQLSATGNLIFKDENITVTADTLEAQMSSNSATLDNTQYWLHGQQVHGKASKMQITSENNLLLSNANFTTCPPGDESWLLEAELIKIDSKEEWGEIWNAKLRIADVPVLYIPYMTVPVSDKRKTGFLFPNFSTSTTNGVQVSTPYYWNIAPEYDLTFTPDMMSSRGLFTKTQVNYLAGEAQQGQVNFEYLDNDNKLAGSPNRYLYNMSHQGAINDNWRVQANFTDVSDNNYFNDLNSDVNRSTDNQLSRIGETSYFERNWDMSVRVQDIKVLGESEKPYQVMPQLNFNYRVADIWQAIDFNFNSELTNFEHQDDNRNTATRIHLVPSLVWPIQGPAGSFTSELKLLQTQFFQQTQDSNNPYNQDVSRTIPQLRLHGKVNFERPANIWGEAYRQTIEPQVQYLYVGYEDQSNIGFYDTAQLQDDYFGLFRDRRFSGHDRIADANQATVGLTSRLLDASNREQFKFSIGQTLYIEDSKVLLNQGLRDAQQSASVLAAELDARLYQDWFISGAVQHDTEHGKNKKSEVTLDYRPSNDKLLQFSYRFVPDLLNTNTNGRVNISQMGVRTSWPLTDSLYFVGNWYHDLKEERDVETYTGIQYESCCWAVRLSYHYRIKTNYDDELMASIDNREEFEKGVYLNFVIKGLGGSGPLGVSDMLDEGLFNYRKPLYLRN", "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": "MATRSPSIVIGDDEPGYDLDLFCIPKHYAEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKSLNRNTDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSALTGKNVLIVEDIIDTGKTMQTLLSLVQKYSPKMVKVASLLVKRTPRSVGYRPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISESGKAKYKA", "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": "MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF", "text": "FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility. 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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family. SIMILARITY: Belongs to the actin family."}
{"protein": "MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP", "text": "FUNCTION: Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily."}
{"protein": "MGAPDEVLNIAPDEGDKLRAKALAADAEELPAGYYTSPRVVCTFMSISLTLLSTYFAFEASAAAISFIIEDIGPSENVSLFSTVWTVSQSISILLMGRLTDRFGRRGFILGTNCVGIIGGIGCLYSFQRFNTMIGAQVLLGLAAGQPGACILFIGELMSNKTKFLGNVIVAFPNVIATGFGPYIGQSLGINGNWRWIFYIYIIITAVSTVLAFIFYHPPSFAQLHGKKISRRDELLKVDWIGAFFLTAGMTLFLLGVSWGGSPDPWDSPKILGLLISGIVSCVIFVLYECYAKIDRPIIPMEFFPGTFAGFGCMLLISGVMGSMNTALFIMYPQQVQHIFSSTLSSWQEVAWMSSTAGFGIWAGIVTLGSLFHIFRHIRWQLIFGSAWVTAFLGAMASVNRHKKSEAIAFSICTGFVIGWAEDVTMLLVQFISSDENLGVTFSVVSATRAICGSIFTAAFISLYTIKFPGQLQSKLVPAVPRRWGFPGVLLVAGFAYWRALTGQCPSYWLLFPGMTSNLIQVTNDAVADSYAAAYSYVYYFAMALGVIAIIASACTKDFDHYLTSHVPHQIYAAKDADVDLLDSDRSTENVSSAAVTVSEKE", "text": "FUNCTION: Efflux pump that provides the dual role of trichothecene export and self-protection by allowing the fungus to evade the harmful effect of its own trichothecene production. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MSTAELAVSYAALILADDGIEVSADKIQTILGAAKVQEVEPIWATIFAKALEGKDIKEILTNVGSAGPATAGAPAAAGAAAPAEEKKEEKEEEKEESDEDMGFGLFD", "text": "FUNCTION: Plays an important role in the elongation step of protein synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family."}
{"protein": "MATIPVNPKPFLNNLTGKTVIVKLKWGMEYKGFLASVDSYMNLQLGNTEEYIDGQLTGNLGEILIRCNNVLYVRGVPEDEELEDADQD", "text": "FUNCTION: Probable common Sm protein, is found in U1 and U2 snRNPs and may be part of the spliceosome. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily."}
{"protein": "MIIMVTEVDVLVIGAGPAGSTAAKHAALGGADVLLIDKKSEIGAPKRCAEGVSIGGLESLGIEPNPRWITKKLDGVRMVSPNGTDVWLTSDKVELPEAGYILERKVFDKFMAMDAARAGSRIMVKTIATGMERTDDGYLVSAECMGEKFEIKARIVIAADGPESRVARWAGLNTATRPKDMESAAQFEMVGVEMEDNNCIEFYFGSVAPGGYALDIPEGDDIANVGLGVLSTETDKSAYEHLLEFVESCPATRNAQPVELNIGGDPVGGMPKKLVADSLMVVGDAAGQVNPLTGGGIISGMKGGMLAGQVAAAAVSEGDVTARRLGEYERLCREEIGDEISKYLKVKEYLLTLSDSELDSIAEAFQDVEFEKVSTTELVKKLIKVSPKALLKLGKLF", "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": "MAQHTVYFPDAFLTQMREAMPSTPSFDDFLAACQRPLRRSIRVNTLKISVADFLRLTAPYGWTLTPIPWCEEGFWIERDNEDALPLGSTAEHLSGLFYIQEASSMLPVAALFADGNAPQRVMDIAAAPGSKTTQIAARMNNEGTILANEFSASRVKVLHANISRCGISNVALTHFDGRVFGAAVPEMFDAILLDAPCSGEGVVRKDPDALKNWSPESNQEIAATQRELIDSAFHALRLGGTLVYSTCTLNREENEAVCLWLKETYPDAVEFLPLGDLFPGTNKALTEEGFLHVFPQIYDCEGFFVARLRKTQAIPALPTPKYKVGNFPFSPVKDREAGQIRQAAASVGLNWDENLRPWQRDKELWLFPVGIEALIGKVRFSRLGIKLAETHNKGYRWQHEAVIALASPDNENAFELTPQEAEEWYRGRDVYPQAAPVADDVLVTFQHQPIGLAKRIGSRLKNSYPRELVRDGKLFTSNA", "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": "MAKISAVERNKKRERLTKRDAGKRAELKALIKDRALEPEDRFQAVLKLAQLPRNGSKTRVHNRCELTGRPHSVYRKFKLGRIMLRDLASQGQIPGMVKSSW", "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": "MGDPGSLVTEGRAGERSWCLRRVGMNTEWLLLEDGNEVTVGRGFGVTYQLVSKICPLMISRNHCILKQNAEGQWTIKDNKSLNGVWLNRERLEPLKVYSIHKGDHIQLGVPLENKENAEYEYEVTEEDWERIYPCLSPKSDQMMEKNKGLRTKRKFSLDELEGSGAEGPSNLKSKISKLSCEPGQQVKSHGKGKVASQPSEYLDPKLTSFEPSVKTTGAHVNPGPAKVIELLRKKKKASNPSASQSSLELFKVTMSRILMLKTQMQEKQVAVLNVKKQTKKGSSKKIVKMEQELQDLQSQLCAEQAQQQARVEQLEKTIQEEQQHLEGLEKEEGEEDLKQQLAQALQEYRSLVEELNRSKKNFEAIIQAKDKELEQTKEEKEKVQAQKEEVLSHMNDVLENELQCIICSEYFVEAVTLNCAHSFCSYCINEWMKRKVECPICRKDIKSKTRSLVLDNCISKMVDNLNSEVKERRIVLIRERKGKRLF", "text": "FUNCTION: E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non- histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'- linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'- linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites (By similarity). Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity (By similarity). In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA- mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2 (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Midbody Chromosome, telomere Note=Recruited at uncapped telomeres. Following DNA double-strand breaks, recruited to the sites of damage. During prophase, concomitant with nuclear envelope breakdown, localizes throughout the cell, with a dotted pattern. In telophase, again in the nucleus and also with a discrete dotted pattern in the cytoplasm. In late telophase and during cytokinesis, localizes in the midbody of the tubulin bridge joining the daughter cells. Does not seem to be associated with condensed chromosomes at any time during the cell cycle. During spermatogenesis, sequestered in the cytoplasm by PIWIL1: RNF8 is released following ubiquitination and degradation of PIWIL1. SIMILARITY: Belongs to the RNF8 family."}
{"protein": "MAAVTSVSFSAITQSAERKSSVSSSRSIDTFRFRSNFSFDSVNVRSSNSTSRFVVHCTSSSAADLPTVADTKLKFLTAYKRPIPTVYNTVLQELIVQQHLTRYKKSYQYDPVFALGFVTVYDQLMEGYPSEEDRNAIFKAYIEALKEDPEQYRADAQKLEEWARTQNANTLVDFSSKEGEIENIFKDIAQRAGTKDGFCYSRLFAVGLFRLLELANVTDPTILEKLCAALNVNKKSVDRDLDVYRNLLSKLVQAKELLKEYVEREKKKRGERETQKANETVTKCLGDYQYAGR", "text": "FUNCTION: Involved in a dynamic process of vesicle-mediated thylakoid membrane biogenesis. Required for the normal organization of vesicles into mature thylakoid stacks and ultimately for leaf development (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Single-pass membrane protein. Plastid, chloroplast stroma. SIMILARITY: Belongs to the THF1 family."}
{"protein": "MEESKVSMMNCNNEGRWSLKGTTALVTGGSKGIGYAIVEELAGLGARVYTCSRNEKELDECLEIWREKGLNVEGSVCDLLSRTERDKLMQTVAHVFDGKLNILVNNAGVVIHKEAKDFTEKDYNIIMGTNFEAAYHLSQIAYPLLKASQNGNVIFLSSIAGFSALPSVSLYSASKGAINQMTKSLACEWAKDNIRVNSVAPGVILTPLVETAIKKNPHQKEEIDNFIVKTPMGRAGKPQEVSALIAFLCFPAASYITGQIIWADGGFTANGGF", "text": "FUNCTION: Catalyzes the stereospecific reduction of tropinone to tropine. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. SDR65C subfamily."}
{"protein": "MDTQKDVQPPKQQPMIYICGECHTENEIKSRDPIRCRECGYRIMYKKRTKRLVVFDAR", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity). FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family."}
{"protein": "MENIMTLPKIKQVRAWFTGGATAEKGAGGGDYHDQGANHWIDDHIATPMSKYREYEQSRQSFGINVLGTLIVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLNATLYYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYAIKLAHACAPYNLKWIEECLPPQQYEGYRELKHNAPAGMMVTSGEHHGTLQSFRTLSETGIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMRPQFDPILLNEPVPVNGRIHKSVLDKPGFGVELNRDCNLNPPYSH", "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": "MALTKAEVAEHLFEKVGLSKRDAKDMVEIFFEEIRETLESGDQVKLSGFGNFDLRLKSERPGRNPKTGEDIPISARKVVTFRPGQKLKSRVEDGNSD", "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": "MSMQDPIADMLTRIRNGQAANKVAVTMPSSKLKVAIANVLKEEGFIEDFKIEGDAKPVLELVLKYFQGKPVVESIQRISRPGLRIYKKKDELPKVMAGLGIAVVSTSKGVMTDRAARQAGLGGEIICYVA", "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": "MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIDAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPVETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADDPVMMAQAFRLAVEAGVMARRAVPGTRSSYAQATSPLTGFLEASA", "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": "MFLLHEYDIFWTFLIISSVIPILAFLISGVLAPINEGPEKLSSYESGIEPMGDAWVQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFIEAFIFVLIPIVGSVYAWRKGALEWS", "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": "MHSSSPFYISNGNKIFFYINLGGVMNMTISFLSEHIFIKLVILTISFDTLLGCLSAIKSRKFNSSFGIDGGIRKVAMIACIFFLSVVDILTKFNFLFMLPQDCINFLRLKHLGISEFFSILFILYESVSILKNMCLCGLPVPKRLKEKIAILLDAMTDEMNAKDEK", "text": "FUNCTION: [Isoform 1]: Holin-like protein required for secretion of toxins A and B (TcdA and TcdB) (PubMed:22685398). Facilitates the release of toxins to the extracellular environment without causing the bacterial cell lysis (PubMed:22685398). FUNCTION: [Isoform 3]: Has weak activity, suggesting that it may act as a antiholin when multiple forms are produced. FUNCTION: [Isoform 2]: Has weak activity, suggesting that it may act as a antiholin when multiple forms are produced. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bacteriophage holin family."}
{"protein": "MDVAALVSGGVDSSVVVHRLCEEGYKPAIFYIRIGMEDKDGYIDCPAEEDIELTTLIARRYGCPFEVVDLHKEYWERVVSYTVETVRRGLTPNPDMMCNKLIKFGCFEERWGYQFDRIATGHYATTDLLNGKTYLSTAKDPVKDQTDFLAQINFAQISKLMFPIGHLLKSEVRAIANAAGLPSAKRKDSQGICFLGKIDYNDFIERYLGKKEGRIIELETGKVIGRHQGYWFHTIGQRKGLGLSGGPWFVVKKDIKRNIILVSRGYDPDAQYGKTIEMETFDFITEDAYEAGYWNREDATPVTFKIRHTPEFTRGLLYKGEKGYRLESEERIQGIAPGQYCVIYDEDHHLCYGSGMITKGR", "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": "MAKKVVTDLDLKDKKVLVRVDFNVPMKDGKITNDNRIVAALPTIEYILEQNGKAILFSHLGKVKTEEDKEGKSLRPVAARLSELLGKEVKFVPTTRGPELEKAIDELKDGEVLLFENTRFEDIDGKKESKNDPELGKYWASLGDVFVNDAFGTAHRAHASNVGIASNLESAAGFLMEKEIKFIGGVVDNPARPLVAILGGAKVSDKIGVIENLLTKADKVLVGGGMTFTFMAAKGQEIGKSLLEADKVELAKGLLEKAGDKLVLPVDAVVSKEFSNDAPFHTVSADSIPADEMGLDIGQATIDLFTKELQGAKTVVWNGPMGVFELSNFAKGTIGVCEAIANLTDATTIIGGGDSAAAAMDLGFADKFTHISTGGGASLEYLEGKELPGVASISDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MTLALALYEPDIAQNAGTLARAVACLGLELHIVEPAGFPVGDAGFRRAGMDYLDRAVIRRHASFKAFEEWRRAEGRRLVLATTRGAVAHVDFAFTETDVVLLGRESAGVPEAVHESADARIVIPLNEGARSLNVALAGAMILGEALRQTGGFARTGTG", "text": "FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily."}
{"protein": "MFIEHPLIKPKTLEARLYQQIIAANALKKKTLCVLSTGLGKTAIAILVIAGILTKKDGKVLILAPSRPLVEQHYNRLKQVLNIDEDKIIALTGKIQPKKRAELYKKGKIFIATPQVIENDIIAGRINVDEFILLIADEAHHTTGDHAYAFVAKKFKDKCHILGLTASPGSDIDKVMEICENLGIEHVEVRTEDDEDVKPYIAKVKLIPIRIDLPNEFKRALKLINEALKERLKILKDAGVINSIADVTKTELIELNNKLFSYDEEVKYELIKVCSEALKLMHAKELLESQGKSVFLNYINKLSMQRTKSAKSIVNDEKVREAVNLLMKSDVEHPKLGKVVDMVKNILEKNKDERIIIFAQYRDTVEKIVNLLTQNGIKAIRFIGQANKEGKGMSQKEQIEAIERFKKEGSVLVSTSVSEEGIDIPSVNYIIFYEPVPSEIRFIQRRGRAMRGEGGKVYVLIAKGTADEAYYRSALYKEREMKRLLKNMCYLLNKRLQKKFEEKSKEEIKEETEEIKEKEIESKTAVKEETKEEEEKTKKPVTILDFIKQIEVKERSKSEEDKIKQEIKIPKKPIKIIVDVREKNMAKLLHNYANIELKTLEVGDYVLSDRVVVERKTAEDFVNSIIDKRLFSQLKNLKKVEKPLLIVEGENFSRLHENALKGAILSIILDFGIPIIFTKNAEETADLLIKIAEKEQIKEKRTVMVRYGKTAMSLKEQQKFIVESLPDVGGALAERLLKHFKTVENVFTAKEEELMKVEGVGKERAKKIREVLTAEYEG", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
{"protein": "MMASLSCVEDKMKTSCLVNGGGTITTTTSQSTLLEEMKLLKDQSGTRKPVINSELWHACAGPLVCLPQVGSLVYYFSQGHSEQVAVSTRRSATTQVPNYPNLPSQLMCQVHNVTLHADKDSDEIYAQMSLQPVHSERDVFPVPDFGMLRGSKHPTEFFCKTLTASDTSTHGGFSVPRRAAEKLFPPLDYSAQPPTQELVVRDLHENTWTFRHIYRGQPKRHLLTTGWSLFVGSKRLRAGDSVLFIRDEKSQLMVGVRRANRQQTALPSSVLSADSMHIGVLAAAAHATANRTPFLIFYNPRACPAEFVIPLAKYRKAICGSQLSVGMRFGMMFETEDSGKRRYMGTIVGISDLDPLRWPGSKWRNLQVEWDEPGCNDKPTRVSPWDIETPESLFIFPSLTSGLKRQLHPSYFAGETEWGSLIKRPLIRVPDSANGIMPYASFPSMASEQLMKMMMRPHNNQNVPSFMSEMQQNIVMGNGGLLGDMKMQQPLMMNQKSEMVQPQNKLTVNPSASNTSGQEQNLSQSMSAPAKPENSTLSGCSSGRVQHGLEQSMEQASQVTTSTVCNEEKVNQLLQKPGASSPVQADQCLDITHQIYQPQSDPINGFSFLETDELTSQVSSFQSLAGSYKQPFILSSQDSSAVVLPDSTNSPLFHDVWDTQLNGLKFDQFSPLMQQDLYASQNICMSNSTTSNILDPPLSNTVLDDFCAIKDTDFQNHPSGCLVGNNNTSFAQDVQSQITSASFADSQAFSRQDFPDNSGGTGTSSSNVDFDDCSLRQNSKGSSWQKIATPRVRTYTKVQKTGSVGRSIDVTSFKDYEELKSAIECMFGLEGLLTHPQSSGWKLVYVDYESDVLLVGDDPWEEFVGCVRCIRILSPTEVQQMSEEGMKLLNSAGINDLKTSVS", "text": "FUNCTION: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Seems to act as transcriptional activator. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Mediates embryo axis formation and vascular tissues differentiation. Functionally redundant with ARF7. May be necessary to counteract AMP1 activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARF family."}
{"protein": "MPAYRSRTSTHGRNMAGARGLWRATGMKNEDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEKAGGVAKEFNTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMVNAHCADAMVCISNCDKITPGMLMAALRLNVPAVFVSGGPMESGKVNVNGKIRSVDLIDAMVAAADDSVSDADVEAIERSACPTCGSCSGMFTANSMNCLTEALGLALPGNGSVLATHADRKGLFVEAGHLIVDLARRYYEQDDARVLPRAIASFKAFENAMTLDISMGGSTNTVLHLLAAAYEGEVPFTMKDIDRLSRRVPVLCKVAPSVVDVHLEDVHRAGGIMGILGELDRAGLIDSSLPTVHSTSLKDGLERWDIKRTKSDSVRSFYLAAPGGVRTQVAFSQDKRFEELDADRSSGCIRDAEHAFSKDGGLAVLYGNIARDGCIVKTAGVDDSILTFSGPARIFESQDAAVDAILTNRIQPGDVVLIRYEGPRGGPGMQEMLYPTSYLKSKGLGKQCALITDGRFSGGSSGLSIGHVSPEAAEGGAIGLVEEGDRIVFDIPNRKVHLDVSDAELERRRAAMEAKGDKAWKPAPRKRRVTMALKAYAAHATSAALGAVRVVKD", "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": "MKISVAVSGASGYAGGEVLRLLANHPQVQIGAITAHSNAGSRLGELQPHLYSLADRLLEENSVANLAGHDVVFLALPHGASGEIAAQLPAETLVIDAGADHRLVYAGAWQEFYHSEHAGTWPYGLPELPIAHGRRQREELRTTKRIAVPGCYPTSALLALAPGFAAGALLADDVVIVSASGTSGAGKAAKTNLLGSEVIGSMAPYGVGGVHRHTPEIEQGLSSVAGEQVTVSFTPTLAPMSRGILTTATAKVAPQLLKETSAAQLRQIWVDAYEDEEFIHVLPEGQWPATQSVLGSNHVGIQVALDERTGRVIVCSVIDNLTKGTAGAAVQSMNIALGLEENLGLKQLGVAP", "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": "MADGGASPAQQEGEMSAAGPGLRRERQHRGSGRPPSARDLQLALAELYEDEAKRQSLRSDKPTTTKMSNSKGLKIDSFRSLRKPERSMSDDKENQRFYSGDSEYRGLQIWGASNNPSKIVAELFKEAKEHGAVPLDEASRTSGDFSKAKSFSGGGYRLGDSSQKHSEYIYGENQDVQILLKLWRNGFSLDDGELRSYSDPINAQFLESVKRGEIPVDLQRLVHGGQVNLDMEDHQEQEYVKPRLRFKAFSGEGQKLGSLTPEIVSTPSSPEEEDKSILNAPVLIDDSVPATKIQIRLADGSRLIQRFNQTHRIKDIRDFIIQSRPAFATTDFVLVTTFPNKELTDESLTLREADILNTVILQQLK", "text": "FUNCTION: Adapter protein required for Golgi and endoplasmic reticulum biogenesis. Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis. Regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Endoplasmic reticulum Golgi apparatus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to centrosome during mitotic prophase and metaphase. SIMILARITY: Belongs to the NSFL1C family."}
{"protein": "MDTIAAISTPMGEGAIAIVRMSGPEALAIADKVYKGPRGKRLSSVDSHTINYGHIVDPETEKVVEEVMVSVLKAPKTFTREDIVEINCHGGLVTVNQVLQLVLREGARLAEPGEFTKRAFLNGRIDLSQAEAVMDLIRAKTDRAMNVAMNQMEGRLSSLIKRLRAEILETLAHVEVNIDYPEYDDVEEMTHKMLIEKATKVKKEIEALLTTSEQGKILREGISTVIIGRPNVGKSSLLNSLVHETKAIVTDIPGTTRDVIEEYVNVRGVPLRLVDTAGIRETEDIVERIGVERSRQVLKEADLILLVLNYSESLSDEDIKLFEATKGMDIIVIVNKTDLEQKLDLDRVRELAGNQPVVTTSLLKEEGIDELEEAIQSLFFTGAIESGDLTYVSNTRHISLLHEAKRAITDALEGIENDVPIDMVQIDLTRCWEVLGEIIGDAVHESLIDQLFSQFCLGK", "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": "MNKEALVNRLNASAKRQKADIVIKNGKIMDVYNQEWIYEDIAITDGVIVGLGEYEGENIIDAEGQMIVPGFIDGHVHIESSMVTPIEFAKAVLPHGVTTVVTDPHEIANVSGEKGIEFMLEQARHTPLNIHFMLPSSVPAASFERSGAILKAADLKPFYEEEEVLGLAEVMDYVSVQQAEKDMVQKLLDARVAGKRIDGHLAGLSTDLINIYRTAFVLNDHEVTSKEEALDRIRRGMYVMMREGSVAKNTLNVLPAVNEKNARRFFFCTDDKHVDDLLSEGSVNHQVKMAIQAGLNPFLAYQLGSLNAAECYGLDTKGAIAPGFDADLLFVSDLENVTVTMTMVKGQTVAEDSKAVYQDHASTAAPDQALLDSVKLAAPLNKQDFHMPIDSEQQINVIQIIPNQLETRLVQVPAPVAREFEPDTELDLLKIAVVERHKGLKETGLGVVKGFGFKSGAIATTISHDSHNIIAVGTNDEDIAAAVNKLQEIGGGLTIIKNGEELHSVPLPIAGLLSDQSAEQVNQSLLTLHDKLSLIGFTGGFNPFLTLSFLALPVIPDIKMTTTGLFDVKSFQHISLQ", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family."}
{"protein": "MTDKSKESGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKDVLPKKESEALPTPKQIREHLDDYVIGQDYAKKVLAVAVYNHYKRLRNGDTTSEGVELGKSNILLIGPTGSGKTLLAETLARFLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVAKAERGIVYIDEIDKISRKAENPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVIEQRVATGTGIGFGAEVRSKNETKTVGELFTQVEPEDLVKYGLIPEFIGRLPVTTTLTELDEEALIQILCEPKNALTKQYAALFELEDAELEFREDALRAIAKKAMERKTGARGLRSILESVLLETMYELPSATDVSKVVIDESVINGESEPLLIYSNADNQAAGAE", "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": "MIKEAGAIISTRHCNPQNGDRCVAALARVECTHFLWPMCIGEVAHVSAEITYTSKHSVEVQVNMMSENILTGAKKLTNKATLWYAPLSLTNVDKVLEEPPVVYFRQEQEEEGQKRYKTQKLERMETNWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHSFVHEGVTMKVMDEVAGILAARHCKTNLVTASMEAINFDNKIRKGCIKTISGRMTFTSNKSVEIEVLVDADCVVDSSQKRYRAASVFT", "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. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSPKTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEESQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLASQGNEIIREASKWSPELAAACEVWKEIKFEFKAVDTL", "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": "MSSGIILLIVAIVLLVIIAYLVGVIIRKRNDTLITSLEERKQALFGLPVNDEIEEVKSLHLIGQSQTSFREWNQKWVDLTLNTFTDIEKHIFEAEHLNDTFNFIRAKHEINSVESQLNLVEEDITAIREALGILKEQEEKNSARVTHALDLYEKLQASVAENEDNFGSTMAEIEKQMKNIEAEFSQFVALNSSGDPVEAAEVLDKAEEHTIALGQITEQIPAIVAKLEDDFPDQLDDLETGYRRLLEENYHFPEKNIEARFQEIRESIRANSSELVTLDLDRARDENTHIQERIDSLYELFEREIAAYKVVAKNSKILPRYLAHAKHNNEQLKHEIARLSRKYILSENEGLNIKAFDKDLKDIEDNVLEIAEAFDQQEKPFSELQLILDRSIKTLASVESGQMDVFAAVKDIEKIESQARQHLEIYVTQLHMIKRYMEKRNLPGIPQDFLSTFFTTSSQLEALMDELSRGRINIEAVSRLSEVATAAIANLEELTYQVVQHATLTEQLLQYSNRYRSFEAGVQNSFEHALKLFEVDNDYQASFDEISYALETVEPGVTERFVNSYEKTRERIRF", "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": "MKIKNSLKALKERHRNNRLVRRKGRVYILNKTNPRFRARQG", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MDNCVNSFEDQKDDLVHKKKSQNFGYVCGSINLGTNVIAQSPTKPLNFFHSSRWSPDGSTILSLTEDQCLNCWNVPFSDLSKKADGPLNFSKHLSYKYQSPETVYSYSWYSRMKLDDPSSNLFAVSSRDQPIKLINFTTGKNKASYHMIDHQERYQGSHCLQFTNDGEYLIAGDKNCLHHFNIRTGCKEPVMTTVTHGYKVPLWEFSLKGIQSCFSLNPMDSKTLAVGTYSNRVGIYNDCGRRPCQLEFSIERGNGVTHLQWCEDGEKLYVGSRCSDKIEVWDIRYVRDMVYALEGHRGDTNQRILFDTDKKDEILAGGTDGSIRRWRNKDLVEETHVTGNYDLTVNTVQANPINMQIKCVCYGNRIYKYEKDESEEEDESKEKDLWTGTVSALQVWMD", "text": "FUNCTION: Negatively regulates the pheromone-response pathway. Acts as a structural mimic of the G protein beta subunit thereby interacting with gpa1 which then inhibits gpa1 signaling. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MRSGVIAQKVGMTRVFTDAGEHVPVTVLKVDQCQVVAHRTVEKNGYVALQVGVGKAKVKNVSKAERGRFAIAKVEPKRKLAEFRVTEDALIPVGAEITADHFIPGQFVDVTGTTTGKGFAGGMKRWNFGGLRATHGVSISHRSIGSTGGRQDPGKTFKNKKMPGHLGVERVTTQNLRVVRTDPERGLILVEGAVPGVAGGWIQIRDAVKRKLPAEAPMPGKFRELADGAAPAVDAAPEAPAVEENA", "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": "MHSPSSTSFTWILITLGCLAFYASLSDAQLTPTFYDTSCPNVSNIVRDIIINELRSDPRITASILRLHFHDCFVNGCDASILLDNTTSFLTEKDALGNANSARGFPTVDRIKAAVERACPRTVSCADVLTIAAQQSVNLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDAFAKVGLDRPSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRQQCPLNGNQSVLVDFDLRTPTVFDNKYYVNLKEQKGLIQSDQELFSSPNATDTIPLVRSFADGTQKFFNAFVEAMNRMGNITPLTGTQGEIRLNCRVVNSNSLLHDIVEVVDFVSSM", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SUBCELLULAR LOCATION: Secreted Vacuole Note=Carboxy-terminal extension appears to target the protein to vacuoles. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MADKENSTPASAARLTRSSAAAGAQAKRSAAAGVADGGAPPAKRKRVALSDLPTLSNAVVVAPRQPHHPVVIKPSSKQPEPAAEAAAPSGGGGGSPVSSASTSTASPSSGWDPQYASDIYTYLRSMEVEARRQSAADYIEAVQVDVTANMRAILVDWLVEVADEYKLVADTLYLAVSYLDRYLSAHPLRRNRLQLLGVGAMLIAAKYEEISPPHVEDFCYITDNTYTRQEVVKMESDILKLLEFEMGNPTIKTFLRRFTRSCQEDKKRSSLLLEFMGSYLAELSLLDYGCLRFLPSVVAASVVFVAKLNIDPYTNPWSKKMQKLTGYKVSELKDCILAIHDLQLRKKCSNLTAIRDKYKQHKFKCVSTLLPPVDIPASYLQDLTE", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily."}
{"protein": "MENFFNQFFESIGEDKNREGLKETPKRVQELWKFLYKGYKEDPRVALKSAYFQGVCDEMIVAQNIEFYSTCEHHLLPFLGNISVGYIPKEKIVGISAIAKLIEIYSRRLQIQERLTIQIAETFDEIIEPRGVIVVCEAKHLCMSMQGVQKQNAIIKTSVLRGLFKKDSKTRAEFMQLLKS", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I family."}
{"protein": "MATTASLHLHLHLLLSSSRRRCRLLVPRAHTDSISTGRRRFIADTATASAAAAVGPLVLPRTPLARADQPPSLSEWERVLLPIDPGVVLLDIAFVPDDPSHGFLLGTRQTILETKNGGNTWFPRSIPSAEDEDFNYRFNSVSFMGKEGWIIGKPAILLHTSDAGDSWERIPLSAQLPGNMVYIKATGEQSAEMVTDEGAIYVTSNRGYNWKAAVQETVSATLNRTVSSGISGASYYTGTFNTVNRSPDGRYVAVSSRGNFYLTWEPGQPFWQPHNRAVARRIQNMGWRADGGLWLLVRGGGLFLSKGSGFQFFYRGLNDAHAISYLHPPNQITEDFEEASVQSRGFGILDVGYRSKDEAWAAGGSGVLLKTTNGGKTWVRDKAADNIAANLYSVKFLGDNKGYVLGNDGVLLRYVG", "text": "FUNCTION: Essential for photosystem II (PSII) biogenesis; required for assembly of an early intermediate in PSII assembly that includes D2 (psbD) and cytochrome b559. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen Note=Restricted to the stromal lamelae. Translocation into the thylakoid lumen occurs via the Tat pathway (By similarity). The position of the signal peptide cleavage has not been experimentally proven (By similarity). SIMILARITY: Belongs to the Ycf48 family."}
{"protein": "MLDLKFIRDNLDLVKRSIKARGLVLDIDKLIYLDDKRKKIITKIGELNAKRNENSSKMRENLDKVLKISLIETGKILKKQLIDLEEELERVSFDFDLENKRVPNILSPDVPIGNSEEDNFEIKKVGIIPRFDFKPKDHLELGRDLDLLDFDRAREVSGSKFYYLKNEAVFLEIALINFSLNKLREKGFNVFITPDVAREFIVDGIGFNPRGNESNIYKIEDTDKYLVGTSEITLGGYYYNKIIDLTLPIKMAGFSHCFRKEAGAYGQLSKGLYRVHQFSKVEMFCFCKAEESSIIHDEFLSIQEQIFTELEIPYRVLNICSFDLGSPAYKKYDIEAWMPGRDGKGGYGEITSTSNCTDYQSRRLKIRYKDQDGQNKFAHMVNGTAIATTRVIISILENFQDEKGGVKIPKSLVKYTGFDYIPFKN", "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": "MSAILSADDLNDFISPGVACIKPVESLPQKESQSENPYEVTKEDKVQPENLPPAQISLTDCLACSGCVTSAEAVLISLQSHTEVLNTLDLYPELPLDFASDQRGTQNVGSADSDSRIFVASVSPQVRASLAATYGITEREAKYMIDQFLMGPHGLRAGGKHGNGFTWVVDTNVMREAVLALTADEVTNSLLSTGSGSLPKSPILSSACPGWICYAEKTHPFILPHLSRLKSPQALSGTFLKSVLSKALGVSPSQIWHLAIMPCFDKKLEASREELTDIAWASTSAESQTTPVRDVDCVITTRELLTLASARGLSLPNLPLKALPASCSTPFPDQALDSFLFSKSSSDQTVESGTSGGYLHHVLKIFQARNPGSKIVTQRGRNADVVEYVLMSSGDEPLLKAARYYGFRNIQNLVRKLKPARVSRLPGAKPQAVTSSANRRQPMSRNAAPAGTGADYAYVEVMACPGGCTNGGGQIRIEDAREAVPNALKETSTETPVAASKPTPHEQRARLARVDEAYYSADSDSEGSVTTEPVSVLSRDTKIHEFLKYWSEKIDIPLSQLAYTSYREVESDVGKTQNAPNETARVVELAGKIGGGW", "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": "MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKASQDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPGDTNSLFPGTWYLERVDEQHRRKYARRPV", "text": "FUNCTION: Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family."}
{"protein": "MMQDVSSSPVSPADDSLSNSEEEPDRQQPASGKRGARKRRSSRRSAGGSAGPGGATGGGIGGGDEPGSPAQGKRGKKSAGGGGGGGAGGGGGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH", "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. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYNATRAQAGNFIALCKNAELACEVTLQPLRRFPLDAAILFSDILTVPDAMGLGLYFETGEGPRFTHSVTCHADIQRLPIPDPEQELGYVMDAVRTIRRSLRGDVPLIGFSGSPWTLATYMVEGGSSKAFTKIKKVMFSDPAALHLLLDKLAQSVILYLNAQIRAGAQAVMIFDTWGGVLTGRDYREFSLRYMHQIVDGLQRESEGRRVPVTLFTKGGGQWLEAMADTGCDALGLDWTCDIADARRRVGGRVALQGNMDPSLLYAPPARIEQEVETILAGFGQGEGHICNLGHGIHPDVPPKHAGVFVDAVHRLSVPYHR", "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": "MACVLLFRLFLLLVLAAFSQGKRLGPTSPLRYSRFLDPSRAVFLRWDFDYEAEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLPNGNVYFSDQHLLDEDTLEQDGSQDAELLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMRVLAAYGPDDIPKMSREHTFVKSIFLLQMLQYDDQDAPEDTIIHDLKISNFIIPEDDTTYACTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSVLPTGIGECYGSDPAFSLCSHVIAGWAVGGLSYQFPDDVGISIGTPFDPQWIRLEIHYSNFQNLPGIRDTSGMRLFYTSHLRKYDMGVLQLGISVFPIHFIPPGAEAFLSYGLCKTDKFEELNGAPVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCKDFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSCMGYPDIIYVTNELGEEASENPMENLMVLDNVEWTPENIKKAEKACKESQQTVLIKTIDEEVENTTGWIPDIIPTPRGPCLESTGGKVEPQDNTPAGFRAVPLALSGSNTATLRPLPMIAVLFLQGSLSCLLAMLQTGV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the copper type II ascorbate-dependent monooxygenase family."}
{"protein": "MNQMNPAFVMPDVQSTVDTRQIPIQRVGVKAVRHPLTVLTESGDVQPTVGVWNLDVRLPAEQKGTHMSRFVALLEENRAPLTIERFRAMIASMLEKLEAEAGRIEVTFPYFVNKTAPVSGVQSLLDYEVTLAGESRNGDTRLFLKVLVPVTSLCPCSKKISQYGAHNQRSHVTIDAELAADVPVEALIRIAEEEASCELWGLLKRPDEKFVTERAYENPKFVEDLVRDVAARLDADARIVAYVLEAENFESIHNHSAYALIERDKRHAA", "text": "FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. SIMILARITY: Belongs to the GTP cyclohydrolase IV family."}
{"protein": "MGFKNICKQGSQLYLNGIFPERILARKLKNCAKSYPRTALTIEVLVSSVLGALKVILIPCASTYAALTLPLRALFNAIKTKSCQHLASYAMAWLLNILTIAVIIGLVFSLVFIPPPVVFISLGLLMSVTTSVTLFQVHKNLFPPYEPPPSRPHTPPPFADEYVPLISESYFD", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chlamydial CPn_0442/CT_006/TC_0274 family."}
{"protein": "MGNCESRELVAQAKQNKIINTELDKAKKTDENIIKLLLLGAGESGKSTVLKQMKIIHNSGFSQEEISNKRNVVCANTVQAMGALLDGMKQLQFDFSTRVCNAHEKLIRETLNDKAEYGPFSDAMFNALTELWADKGVQCAYDKREFFYLHDSAKYFFDAIARVHTPNYVPTENDILHTRVPTMGVIEVNFTIKGKFFRVFDVGGQRSQRKKWIHCFDDAKAMIYVASLSEYDQVLLEDNTTNRMHESIQLFKQVINNKYFVNTSVILFLNKIDLFEEKIVTKKRSLGIAFESFSGPSQDLNAAVAFVEKKYRSMAENKEKNIYCHHTCATDTQQVQYVLDAVLDTILSTKLKGCGLY", "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": "MRIWIDADACPKAAKDLIVKFALKRKLEVVMVAGQAVAKPAFAVVRLIVVPSGMDAADDYLVEHAVPGELVICSDVPLADRLIKKGVAALDPRGREFDERNMGDRLAVRNLFTELREQGQAGGGQGPYGEREKQAFANALDRILARLAKG", "text": "SIMILARITY: Belongs to the UPF0178 family."}
{"protein": "MSDSPTSSPPAPSADSAPPPDTSSDGSAAPPPTDSAPPPSPPADSSPPPALPSLPPAVFSPPPTVSSPPPPPLDSSPPPPPDLTPPPSSPPPPDAPPPIPIVFPPPIDSPPPESTNSPPPPEVFEPPPPPADEDESPPAPPPPEQLPPPASSPQGGPKKPKKHHPGPATSPPAPSAPATSPPAPPNAPPRNSSHALPPKSTAAGGPLTSPSRGVPSSGNSVPPPANSGGGYQGKTMAGFAIAGFAVIALMAVVFLVRRKKKRNIDAYSDSQYLPPSNFSIKSDGFLYGQNPTKGYSGPGGYNSQQQSNSGNSFGSQRGGGGYTRSGSAPDSAVMGSGQTHFTYEELTDITEGFSKHNILGEGGFGCVYKGKLNDGKLVAVKQLKVGSGQGDREFKAEVEIISRVHHRHLVSLVGYCIADSERLLIYEYVPNQTLEHHLHGKGRPVLEWARRVRIAIGSAKGLAYLHEDCHPKIIHRDIKSANILLDDEFEAQVADFGLAKLNDSTQTHVSTRVMGTFGYLAPEYAQSGKLTDRSDVFSFGVVLLELITGRKPVDQYQPLGEESLVEWARPLLHKAIETGDFSELVDRRLEKHYVENEVFRMIETAAACVRHSGPKRPRMVQVVRALDSEGDMGDISNGNKVGQSSAYDSGQYNNDTMKFRKMAFGFDDSSDSGMYSGDYSVQDSRKGSNGASSEFTRNETENRNFNNRRY", "text": "FUNCTION: Regulates negatively root hairs elongation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MTKSELVEKLAARFPQLLLRDADISVKTILDAMSDALADGHRIEIRGFGSFGLNRRPPRVGRNPKSGERVLVPEKRVPHFKAGKELRERVDRNLTPSSGGSGNGHLTGTPSGKGPQGAAPGSPAVLHEGGGLNLARS", "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": "MSETITVNCPTCGKTVVWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEEPKQ", "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. 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": "MSIKSDKWIRYMAQAHGIIEPFEPRQIREANNARIISYGTSSYGYDIRCSNEFKIFTNINSAVVDPKNFDASSFVDVQSDVCIIPPNSFALARTVEYFRIPRSVLTICLGKSTYARCGIIVNITPLEPEWEGHVTLEFSNTTPLPAKVYANEGVAQVVFFESDELCETSYRDRSGKYQGQTGVTLPKA", "text": "FUNCTION: Catalyzes the deamination of dCTP to dUTP. SIMILARITY: Belongs to the dCTP deaminase family."}
{"protein": "MAYQEPNKDGFYGKFGGRFVPETLMTAVLELEKAYRESQADPSFQEELNQLLRQYVGRETPLYYAKNLTQHIGGAKIYLKREDLNHTGAHKINNALGQVWLAKRMGKKKIIAETGAGQHGVATATAAALFNMECTIYMGEEDVKRQALNVFRMELLGAKVEAVTDGSRVLKDAVNAALRSWVANIDDTHYILGSALGPHPFPEIVRDFQSVIGREAKQQYRDLTGQNLPDALVACVGGGSNAIGLFHPFVEDESVAMYGAEAAGLGVDTEHHAATLTKGRPGVLHGSLMDVLQDAHGQILEAFSISAGLDYPGIGPEHSHYHDIKRASYVPVTDEEALEGFQLLSRVEGIIPALESSHAIAFAVKLAKELGPEKSMIVCLSGRGDKDVVQVKDRLEADAAKKGEAHA", "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": "MFSRDLTIAKYDAELFEAMQQEALRQEEHIELIASENYTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGADYANVQPHAGSQANAAVYLALLSAGDTILGMSLAHGGHLTHGASVSSSGKLYNAIQYGIDGNGLIDYDEVERLAVEHKPKMIVAGFSAYSQVLDFARFRAIADKVGAYLFVDMAHVAGLVAAGVYPNPVPFADVVTTTTHKTLRGPRGGLILARANADIEKKLNSAVFPGAQGGPLEHVIAAKAICFKEALQPEFKAYQQQVVKNAQAMASVFIERGFDVVSGGTQNHLFLLSLIKQEISGKDADAALGKAFITVNKNSVPNDPRSPFVTSGLRFGTPAVTTRGFKEAECKELAGWICDILADLNNEAVIDAVREKVKAICKKLPVYGN", "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": "MIKLNVNLQDRSYPIYISTDYSQIGKCIQSAKLTGKMVLITDTNVDKYQAEECVKAFSDAGYEVSKFVIPAGEENKNLDTTRDIYKYLLGLKLDRSATLMALGGGVVGDITGFAAATFLRGINFVQIPTTLLAQSDSSVGGKVGVDFEGTKNIIGAFYQPKFVYINVNTLKTLPERELKAGLAEVVKHGVIMDEEFYEYIDYNVHKILNHDEAVLQYIAKRNCSIKASVVEKDEKEGGLRAILNFGHTIGHAIETVMNFELLHGECVSLGMVGAMRMALYLEMIDEQSVNRVKNTLDKIGLPTRLEGIDVDKVYNQMFYDKKIKGSKLTFVLPRKRIGEVIQCTIDDEDLIKRVIASLGE", "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": "MSEIIAYKLNGELIDTQSINGREAVAQPVYFDNSPDALHVIRHSCAHLMAQAIKSLYPNAKFFVGPNVEDGFYYDFRVDEAGTKLGESDLEAIEKKMKELAEAKFEITKICSTKAAMSEKFKNDDLKQEVLKRIPEGEVSSYAQGDFEDLCRGPHVPNTKFLRFFKLTRVAGAYLGGDETREMLNRIYGTAYADKASLAEHIRIIEEAKKRDHRKLGVEMKLFGFDEEVGGGLPIWLPNGGRLRSKLEQILYKAHRDRGYEPVRGPELLKADVWKRSGHYANYKENMYFTTIDDAEYGIKPMNCVGHIKVYQTEIRSYRDLPLKFFEYGVVHRHEKSGVLHGLFRVREFAQDDSHIFCMPSQIKQNILEILSFAGKIMQNFGFEYEMEISTKPAKAIGSDEIWDIATNALKEALDENGFKYGIDEGGGAFYGPKIDIKITDALKRKWQCGTIQVDFNLPERFDLGYIDANNERQRPVMLHRALLGSFERFIGILIEHTAGELPFFIAPTQVVIVPISDAHLDYAKEIARELRKFNIDSEVASKNESLNKRIRTAEKQRVPMIIVLGDNEVANRSVALRDRQARTQSDMSLAEFLNLTKEKLSEVHF", "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": "MDLRKSPLYSKYIESNAKLVDFAGWEMPISFSGLIKEHESVRSSAGLFDISHMGVISVKGINPKDYIQKFFPTNLYSFSEGQGLYTVMLNDKGGIIDDLIIYDLGIQENDITELLLIVNASRYEEDFQWIKNNLNKDEISITNFKKAKVLLALQGKKSFDLFEEWIDSSISHIPNFGCEYKIFEHISPKEKIFFSKTGYTGENGLEILLSKKAAINLWDFSISKNVAPCGLGARDTLRLEAGMHLYGQDINEETSPYEAGLGWLVHLENNHEFFGRRFLEEQSRLGIQKKLVGLFIEGKAIGRKGCTVLKGEENIGTITSGSWSPTKQQAIAFAYINTSHALINNEVQVLIRGKKFKGVITKRAFYKKNY", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. SIMILARITY: Belongs to the GcvT family."}
{"protein": "MNREEATLLGFEIVAYAGDARSKLLEALNAAQAGEYDRAEELVAAADDCIVDAHKAQTSLLAKEAQGDDIELSVTLMHGQDHLMTTILLKDLMKHLIELYKRGS", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "NLGKQWAVGHFM", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombesin/neuromedin-B/ranatensin family."}
{"protein": "MALKSYKPTTPGQRGLVLIDRSELWKGRPVKTLVEGLIKTGGRNNTGRVTMWHKGGGAKRLYRIVDFKRRKFDVPAVVERIEYDPNRTAFIALVRYEDGELAYILAPQRLAVGDSVVAGVKTDVKPGNAMPFSGMPIGTIVHNVELKPGKGGQLARAAGTYAQFVGRDGGYAQIRLSSGELRMVRQECMATVGAVSNPDNSNQNFGKAGRMRHKGVRPTVRGVAMNPIDHPHGGGEGRTSGGRHPVTPWGKGTKGNRTRKSKASDKLIVRSRHAKKKGR", "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": "MKNQDQALIFEVSKEGRIGYSLPKLDVEEVKLEDVFESDYIRVEDAELPEVSELDIMRHYTALSNRNHGVDSGFYPLGSCTMKYNPKINESVARFAGFANIHPLQDEKTVQGAMELMYDLQEHLIEITGMDTVTLQPAAGAHGEWTGLMLIRAYHEANGDFNRTKVIVPDSAHGTNPASATVAGFETITVKSNEHGLVDLEDLKRVVNEETAALMLTNPNTLGLFEENILEMAEIVHNAGGKLYYDGANLNAVLSQARPGDMGFDVVHLNLHKTFTGPHGGGGPGSGPVGVKADLIPYLPKPILEKTEDGYRFNYDRPEAIGRVKPFYGNFGINVRAYTYIRSMGPDGLRAVTEYAVLNANYMMRRLAPFYDLPFDRHCKHEFVLSGRRQKKLGVRTLDIAKRLLDFGYHPPTIYFPLNVEECIMIEPTETESKETLDGFIDKMIQIAKEVEENPEVVQEAPHTTVIKRLDETMAARKPVLRYEKPAPVQV", "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": "MRCGSREVFVKIQEATNPEWGKPPSRRSAEEHIKYSLVLLDKPRGPSSHEVAAWVKKILGVERAGHAGTLDPKVSGVLPIAVAEGTKVLLALSRSDKVYVAVAKFHGDVDEGKLRAVLGEFQGIIYQRPPLRSAVKRQLRTRQVYSIELLELDGRYAVIKMHVEAGTYARKLIHDIGEVLGVGANMRELRRVAVSCYTEEETVTLQDVADAYYIWRKYGDDTYLRRVLLPIEEIARHLPKIWVRDSAVDALCNGAPLAAPGVAKFEAPFSRGELVAYFTLKGELIGVGRALVDSEEVKKMEKGLVARTDRVVMKRGTYPPLWKRRGEGAKA", "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": "MEGLQPVRSLFTRFFQLEAASGLLLIAAAVLALIINNSPLSYLYGGLLDVPVAVQVGALNIAKPLLLWINDGLMALFFLLIGLEVKREVVDGHLSKPSQVILPATAAVGGMVVPALIYWFINRDNPAAVAGWAIPTATDIAFALGVLALLGKRVPVSLKLFLMTLAIIDDLGAIIVIALFYSGTLSSVSLLLAAACLLVLVAMNRLGVIKLGPYMIVGLILWVCVLKSGVHATLAGVALAFCIPLRTRNAESSPLLALEHALHPWVAYAILPIFAFANAGVSLAGMTVDSFTHPVPMGITVGLLLGKTVGVFGLTWVAVKLRLAALPAGAGWGQILGVAILCGIGFTMSLFVGSLAFAPGSSEYAGMDRMGILTGSFFAAVIGYAVTAMASRKTNVA", "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": "MNQPAIKHALNVKRADDFAQWYQAVIAEAELAEESGVRGCMVIKPWGYGIWERIQKLMDAEIKEAGVENCYFPLFIPLSYFTKEAEHVEGFAKEMAVVTHHRLISDGKGGLTPDPEAKLEEPLVVRPTSETVIGAAMSRWIQSWRDLPLLTNQWANVVRWEMRTRMFLRTSEFLWQEGHTAHVDEADAMKETLRALEMYRAFAEGPLAMPVIAGPKPENERFPGAVETFSIEAMMQDGKALQAGTSHYLGTTFAKAAGIQYQNKEGQQALAHTTSWGVSTRLIGGVIMTHGDDDGLRVPPQVAPQQIVILPMLRDNEGDDALLAYCEEIRASLVKLSVFGERIRVLLDKRPGKATQKRWAWVKKGMPLILEIGGRDAEGGLVSVLRRDRLWRQDAKPNFVGQAKDDFLASAATELESIQAALYDEARARRDAQIVRDVTDLEGLKGYFAEGNKYPGWVEMGWAKPTGEALDKVVEQLKALKLTIRNTPMDAEKPVGACPFTGEPAVEKILIARSY", "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": "MATDTGSGRGKGGKGVTLGKGSKGAKASKGGKRIRTKTQQDALKGITKPAIRRLARRGGVKRINGAVYDETRNVLKQFLEQVIRDSVTYTEHAKRRTVTAMDVVYALKRQGRTLYGYS", "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": "MKLPIYLDYSATTPVDPRVAQKMIDCLTVEGNFGNPASRSHVFGWKAEEAVENARRQVADLVNADPREIVWTSGATESNNLAIKGVAHFYASKGKHLITSKVEHKAVLDTTRQLEREGFEVTYIEPGEDGLITPAMIEAALRDDTILVSIMHVNNEIGTINDIAAIGELTRSRGVLFHVDGAQSTGKVEIDLASLKVDLMSFSAHKTYGPKGIGALYVSRKPRVRLEATMHGGGHERGMRSGTLATHQIVGMGEAFRIAKEEMAAENVRIKALSDRFFKQVENLEELYVNGSLTARVPHNLNLSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFSTEEEIDYAAQKVCEAVTRLRTLSPLWDMFKDGVDISKIEWAAH", "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": "MRTTSVGVFKIVTKGPGDVSGLMAMIGSGAIDPKSILAVLGKTEGNGGVNDFTREYAVAALCTALAPQLGLSPEEVEQRIAFVMSGGTEGVLSPHITVFTRREVERRPAGLSGKRLSIGMAHTRDFLPEELGRAAQIAETAAAVKAAMADAGIADPADVHFVQIKCPLLTSDRVEAASARGNKTATTSAYGSMAYSRGASALGVAVALGETGSDISDGDVLRRYDLFSKVASTSAGIELMHNVVIVLGNSAASASEFEIGHAVMNDAIDAAAVTSALKCVGLGVAPQAEAGRELVNIFAKAEASPDGSVRGFRHTMLEDTDISSTRHARAAVGGLIAGLAGTGAVYVSGGAEHQGPAGGGPVAVIARLSD", "text": "FUNCTION: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6- trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family."}
{"protein": "MAAVTYELIKTCKQSGARLGKLHTPHGTIETPIFMPVGTLATVKTMSPEELKQLGAQIILSNTYHLWLRPGHDIVKEAGGLHEFMNWDRPILTDSGGFQVFSLSDLRTIEEEGVHFRNHLSGEKLFLSPEGAMEIQNALGSDIMMAFDECPPYPAERDYMRPSVERTSRWAERCLKAHKRPEDQALFGIIQGGEYEDLRRQSAQDITSLDFPGYAIGGVSVGEPKDVMNRVLEFTTPLLPANKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSNGRLVVRNAKYARDFRSLDENCDCHVCQTYTRAYIRHLVKCDETFGFRLTTYHNLYFLLKLMKDVRQAILDDRLLDFREEFFEQYGFNQPNAKNF", "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": "MRVLVLGSGVIGTTSAWYLRQAGFEVTVIDRQPGPALETSFANAGQLSFGYTSPWAAPGVPKKAIGWLFEKHAPLAIKPGMDLAQYRWLWQMLRNCTHERYAINKARMVRMSEYSRDCLNELRAQIGIEFEGRDLGTTQLFRTQQQLDASAQDIEILAQYGVPYEVLDRAGIIQAEPALAHVDGLVGALRLPRDQTGDCQLFTRRLAQMCVDAGVEFRFDQDITGLEFDGDRITGVRIDGKLETADRFVVALGSYSPALVAPLGMRLPVYPLKGYSLTLPITDPAMAPTSTILDESYKVAVTRFDDRIRVGGMAEVAGFDLSLSQRRRETLELVVSDLYPKGGDLSRAQFWTGLRPATPDGTPVIGATPFRNLYLNTGHGTLGWTMACGSGRYLADLMSARQPQISTEGLDIFRYGQYGHAPQQENRTCVLPAR", "text": "FUNCTION: Oxidative deamination of D-amino acids. SIMILARITY: Belongs to the DadA oxidoreductase family."}
{"protein": "AGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRGLTDYLMKILTERGYMFTTSAEREIVRDVKEKLAYVALDFEQELETAKSSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSFIGMEAAGIHETTYNSIMKSDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQ", "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": "MPSSGPGDTSSSSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPMAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEENQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGGDAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDSGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV", "text": "FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:9662389, PubMed:11399089, PubMed:10555141, PubMed:11919202, PubMed:16567415, PubMed:17713477). DNA methylation is coordinated with methylation of histones (PubMed:9662389, PubMed:11399089, PubMed:10555141, PubMed:11919202, PubMed:16567415, PubMed:17713477). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:9662389, PubMed:11399089, PubMed:10555141, PubMed:11919202, PubMed:16567415, PubMed:17713477). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (PubMed:18823905). Plays a role in paternal and maternal imprinting (PubMed:15215868). Required for methylation of most imprinted loci in germ cells (PubMed:15215868). Acts as a transcriptional corepressor for ZBTB18 (PubMed:11350943). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (PubMed:20547484). Can actively repress transcription through the recruitment of HDAC activity (PubMed:11350943). Also has weak auto- methylation activity on Cys-706 in absence of DNA (PubMed:21481189). 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": "MSERDRNGGRSADNNRNDRNERGGRNDRGGRNDRRNNQQDERNQYIERVVTINRVSKVVKGGRRFSFTALVIVGDGQGMVGVGYGKAKEVPAAIQKGAEEARKNFFRVPMINGTITHPVQGEAAAGVVMLRPAAPGTGVIAGGAARPVLECAGVQDILCKSLGSPNAINVVHATVAGLKELVRPEEVAARRGKSLEEVAPAAMLRARAAGQGA", "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": "MIKEYYGAETFILNKDFAYILVIGTTDVSLIPGLTIAGATPELTHFTPAADAEYVLLGKCKSINTIPVSPTGIPTPALLTRASLSFINPLKIVVNAGSRIVPKIPYIDLQGEPGKDIRKQALSMEKVNNIIENSIKLGEELSNEYELIMIGESIPAGTTTAMATLLALGYDAMDKVSSASPDNPKELKRKVVEEALRNLPTDPLQRLAKVSDPVLLGVAGTSLGFKGKILLAGGTQMTAAAAIINEFDKNKLKDITIGTTKWIVEDKFADMLSLAKQVGVKVLASMLDLSISAYEGIRAYEKGYVKEGVGAGGSAIMALVRGVSNNTLVRKIDELYGELVGSNNLHI", "text": "SIMILARITY: Belongs to the UPF0284 family."}
{"protein": "MATNGHFASIGNSASDTTAYEHGVQVIDENKEFKNPNLSQYLSLENVTPSGFNYHLISVFGSQSTGKSTLLNHLFGTHFSVMSELERRQTTKGIWMSKNKNESSSMASNILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNLQLFLKDKNTTHRSLLFFVIRDYSGMTPLQNLQKTLMEDMARLWDSISKPGGLENSNVHDYFDFQFYGLPHKGYQPEKFVEETQKLSLRFCDGQRDPNLDARKGEFSDGGVFLPEYHRRIPADGFSRYAEGIWDQIVNNKDLDLPTQQELLAQFRCDEILREVMVAFDETIVPFEDKQSQAARLGEPEILGGLGAAMRSSRTKAVKAFESEASRYHKGVYQRKRAELESKADTRLKTLFQGQLNAAHKSGISEFSEAVTAAVKSGQKKGTGYDFAEIVNEEAKKAVDKFEEVARATVVDGTSWSDYKQELALYEKELAEVSARLRRDEMRRLASRVERWVQSRLGESVGLEFNALGSGRAGGGAPEKGDQPTEKKFWDRVWNVFVETVLDAERRFTDRASSFDASLEEVDVGLWRLRRKSWGVLRAKIDEEMIEGNLLLKLRENFEDKFRYDDAGVPRIWRPTDDIEGIYTRARESTLTLIPLLSKFRLDETSAPPPLDRWIGHTPSSATSADEEDLAPIGGVDEEEGKSLEEEMTIVSDAKRQELTVRFKKAADGVYVEAKRSAIGGMTQVPLYFYGLLLALGWNEIIAVLRNPAYFFLLFVCAVGAYITYQLNLWGPIIKMTEAASNQAVTEGKKRLREFLESSDTGRQAIAMSTPGGSGRGGEEHEMSRLNQQGKSAAADEDVDDL", "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": "MMDWFMSTVYFYGPEINVSNRVVRNFSSDIENFLRISFVDEDCEKLRATDLSPRSASGHDANRTALYKRVLSVLSDGITIGGKNFEFLAFSSSQLRDNSAWMFASRQGLAASDIRTWMGDFRNIRNVAKYAARLGQSFSSSTETLKVQKYEVEEISDIKNGTQHVFSDGIGKISSAFANEVAMKCNLKRFAPSAFQIRYGGYKGVVAVDPTSRWKLSLRKSMLKFQSDNITVDVLAYSKYQPGFLNRQLITLLSTLGVRDSVFEQKQEEAVNQLNKMVTDPQAAIEAIELMPMGEITNAVKELLLCGYQPDDEPYLSMLLQTFRASKLLELKTKSRILIPKGRAMMGCLDETRTLKYGQVFIRATSGVNDNDRFTVTGKVVIAKNPCLHPGDIRILHAVDVPVLHHMFNCVVFPQQGPRPHPNECSGSDLDGDIYFVSWDPSLIPPRMVTPMDYTPAPTETLDHDVTIEEVEEYFTNYIVNESLGMIANAHVVFADKEDLKAESSPCIELAKLFSIAVDFPKTGVPALIPPELHVKEYPDFMEKLDKVTYESKGVIGKLYREIKKHTPHIKHFTREVARRSYDTDMIVDGYEDYITEAMALKDEYDFKLGNLMDHYGIKSEAEIISGCILKMAKNFTKKSDADAIRLAVRSLRKEARSRFSEMSLDDNGHGHDASEAKASAWYHVTYHPEFWGCYNEGYERPHFISFPWCIYEKLLRIKQRRKFVRKMQPELFSLHNLRI", "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": "MTISKERKEEVISEHGAAAGDTGSPEVQIAILTERINGLTEHMRTHRKDYASRRGLLGLVSRRRRLLDYVRGQDPQRYLDIIGKLGIRK", "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": "PVPDSSFLRDP", "text": "FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRF amide related peptide) family."}
{"protein": "MQFIDLAEIHVKAGKGGDGIIAFRREKYVPAGGPSGGNGGNGGSVILKAVSNLQTLLDFRYAHVFKAENGQRGGPNNRTGACGADLVIEVPCGTMVWDAETGELLGDLTTPGQTLLVAKGGKGGLGNKHFLSNHQRAPDYALPGLEGEERHLRLELKLLAEVGIIGLPNAGKSTLISVLSAARPKIADYPFTTLVPNLGVVRQPNGDGTVFADIPGLIAGAHTGLGLGHEFLRHIERTRLLLHLIDATAEDVVAAYQTIRDELVAYGHGLGDRPQIVALNKIDALDASQITTLQETLAAYVGQRVFAISAVARQGLEPLLEAVWQELGVSVSH", "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": "MEPQVTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQMQVHEGCHVVDEVLPQTVVEKQATARTGKKPLAHYSSLVRVLGSDMKTTEEPTAEARSPVPCDTDKPQDKPPDWFTSYLEMFREQVVKETVEKLEQRLQEKLVLQKPPFSSSPSEVSMPISEEETLFLPENQFSWHIACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPYSHDTNHILLKFRRPVVISSEPFFYSKYPTPRLPAALEQVRLQKQVDKNFVKAEKQRLRAEKKQRKAEVKELKKQLKLHRKIHLWNSIHGLQSPKSPLGRPESLLQSNTLMLPLQPCAPVMPTLSAAFVDENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTEKKDVLVPCLKAGHIGVVSVEFIAPTLEGTYTLHWRLSHKGQQFGPRVWCSIIVDPFPSSESPVNLERDGISSSKADDFTCEQEEAFLLAEEEIPLGEVTKQTEGTGSSAPQKTQHAASERELYIPSVDLLTAQDLLSFELLDINIVQELERVPHNTPVDVTPRMSPLPHDSPLIEKPGLGRIQEESEGAGLKASPDSTVLTKRKAETPASVEETEEDLSGTQFVCETVIRSLTLDAAPDHNPPCRQRSPQRELQLYSTEEQQPLMLPGFCRKDSSLKFALPEEGPHGDEREEIVHIAEEEAIEEEDVQDEEVQSQSSASSEDYIIILPECFDTSRPLGDSMYSSALSQPGLERGAEGEPGIESGQEPAEARERLPERESQPKEQSISDILTTSQHLDTVPLVPEVAGLPAALSRSAPCGQYEAPRVDSPVTIQEVLPVPDHVRGEPRGSTGLANSRQKSCDHSRHHNGSSIAGGLVKGALSVAASAYKALFSGPPVTAQPVISEDQTAALMAHLFEMGFCDRQLNLRLLRKHNHNILQVVTELLQVNNNDWYSHRY", "text": "FUNCTION: Ubiquitin-binding autophagy adapter that participates in different processes including host defense or intracellular homeostasis. Possesses a double function during the selective autophagy by acting as a shuttle bringing ubiquitinated proteins to autophagosomes and also by participating in the formation of protein aggregates. Plays a role in the regulation of the innate immune response by modulating type I interferon production and targeting ubiquitinated IRF3 for autophagic degradation (By similarity). In response to oxidative stress, promotes an increase in SQSTM1 levels, phosphorylation, and body formation by preventing its autophagic degradation (By similarity). In turn, activates the KEAP1-NRF2/NFE2L2 antioxidant pathway (By similarity). Plays also non-autophagy role by mediating the shuttle of IL-12 to late endosome for subsequent secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, autophagosome Lysosome Cytoplasm, myofibril, sarcomere, M line Note=In cardiac muscles localizes to the sarcomeric M line (PubMed:15802564). Is targeted to lysosomes for degradation (By similarity)."}
{"protein": "MNINVADLLNGNYILLLFVVLALGLCLGKLRLGSVQLGNSIGVLVVSLLLGQQHFSINTDALNLGFMLFIFCVGVEAGPNFFSIFFRDGKNYLMLALVMVGSALIIALGLGKLFGWDIGLTAGMLAGSMTSTPVLVGAGDTLRHSGMEGSQLSVALDHLSLGYALTYLIGLVSLIVAARYLPKLQHQDLQTSAQQIARERGLDTDTKRKVYLPVIRAYRVGPELVAWADGKNLRELGIYRQTGCYIERIRRNGILANPDGDAVLQMGDDIALVGYPDAHARLDPSFRNGKEVFDRDLLDMRIVTEEIVVKNHNAVGRRLAQLKLTDHGCFLNRVIRSQIEMPIDDNVVLNKGDVLQVSGDARRVKTVADRIGFISIHSQVTDLLAFCAFFIVGLMIGMITFQFSNFSFGVGNAAGLLFAGIMLGFLRANHPTFGYIPQGALNMVKEFGLMVFMAGVGLSAGSGIGHSLGAVGWQMLVAGLIVSLLPVVICFLFGAYVLRMNRAMLFGAMMGARTCAPAMEIISDTARSNIPALGYAGTYAIANVLLTLAGTLIIIIWPGLG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family. YbjL subfamily."}
{"protein": "MENGFVNFYDHVKGYGFIRRERGRDVFFRYDDFLFLGHDVDICKGILVRFKLEKTDKGFKAVAIQKV", "text": "FUNCTION: Probable cold shock-like component of antiviral defense system retron Se72, composed of a non-coding RNA (ncRNA), a reverse transcriptase (RT) and this protein. Expression of retron Se72 confers protection against bacteriophage lambda. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with lambda but do not collapse, at MOI 2 cultures enter growth stasis."}
{"protein": "MRAVVLISGGMDSLVVAAQARALGYELAAMHVNYGQRTWQKELTAFRRICSHYAIERKLEVDAAYLEHIGGSSLTDSSIPVEQADLQTVAIPSSYVPFRNASFLSMAVSWSEVIGAERIFIGAVEEDSSGYPDCRKIFYDAFNKVIELGTKPETTIEIRTPLIDLQKSEIVRKGVELDVPFFHSWSCYKSEGKACGLCDSCARRLRAFQLVGLDDPIDYEVRPDYI", "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": "MTNIRKSHPLLKIMNDAFIDLPAPSNISSWWNFGSLLGVCLIMQILTGLFLAMHYTSDTTTAFSSVAHICRDVNYGWIIRYLHANGASMFFICLYIHVGRGLYYGSYTFSETWNVGMVLLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVAVHLLFLHETGSNNPTGISSDMDKIPFHPYYTIKDILGALLLMLALLILVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILAFIPALHTSKQRSMTFRPISQCLFWVLVADLLTLTWIGGQPVEPPFIMIGQVASILYFSLILILMPVAGIIENRILKW", "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": "MAQPALKVVDMPPVDKDKSKAIDAALSQIERAFGKGSIMRLGKSDKVQEVETVSTGSLGLDIALGVGGLPRGRVIEIYGPESSGKTTLALHTIAEAQKKGGVCAFVDAEHALDPVYARKLGVNLDDLLISQPDTGEQALEITDTLVRSGAIDVLVVDSVAALTPRAEIEGEMGESQPGLQARLMSQALRKLTGSISRSNCMVIFINQIRMKIGVMYGSPETTTGGNALKFYASVRLDIRRISTLKDRDEAIGNQVRVKVVKNKVAPPFKQVEFDIMFGEGVSKVGELIDLGVKAGIVEKSGAWFSYNSQRLGQGRENSKGFLRDNPKIAAEIEGSIRQNSGLVAEKILENAAPTADDLDEGEA", "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": "MNSKIFAVLFLLAFLSCVLSDQYCPKSSITACKKMNIRNDCCKDDDCTGGSWYCATPCGNFCKYPTDRPGGKRAAGGKSCKTGYVY", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom protein 11 family. 01 (wap-1) subfamily."}
{"protein": "MSGGDGRGHNTGAHSTSGNINGGPTGLGVGGGASDGSGWSSENNPWGGGSGSGIHWGGGSGHGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMAALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSSAMESRKKKEDKKRSAENNLNDEKNKPRKGFKDYGHDYHPAPKTENIKGLGDLKPGIPKTPKQNGGGKRKRWTGDKGRKIYEWDSQHGELEGYRASDGQHLGSFDPKTGNQLKGPDPKRNIKKYL", "text": "FUNCTION: Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. FUNCTION: Inactivates ribosomes by hydrolyzing 16S RNA in 30S ribosomes at a specific site. SIMILARITY: Belongs to the cloacin colicin family."}
{"protein": "MDEVLEMIADAVSSLVVAITDSEEKNTLFGDMVPGVELIQQAVNGMAEAAEETVSLIDEEFIGQLESTSKQLKNSAGQLYVHAVRAREDPWNRVPQKDAIKAAKQILQNVVLLVLIEEQSNIKVLVNIAKKAAEGVRRIDEIENIKQLDVMIGDVNQLQNELVKRSQRRSEGSHNPELRSKLEDIATMVNILSEQHQASARDVCRNPREETLRSKRSELSSKLLSAIDDLIYTIKLIFENNTKFVDLAFKWKPVRTMAEDEVTRASAVLIDNLRTLPKSIEAGNGPAAAREIVNAANLQISNAIIVANRCQDPVKKKMLLKQIEELKKLTPMLISAMKPVLENPNDQEAQKHLESVIYSTQKASEALATAVVSSPAEIVAASGVSLARDLDSLEEAIASGDKKRAQVILSHIPSAIDKHIELANALLETITDPGQRHQIKQSIERLQTLKPRIIENANRAIANPNDHEARKNLSSDIKEAKKAIGQISQPYEVVSALNTKIHNDLDSLIKCIDEGGPDMQVKGVQYAKDIANSIKKQIEAAEAYAQTITDPDRKKQVLDSIEQLKKLTPQLLEAIRACLANPDDKEARKRLDDVVRRVKEASSNLSQVIQPTADELKEEKRKRNEEIARIEAEEKAKARALLKAAELARIEAEEEKKRLAIIEEEKKRLAAEEEERKRAPKLVVPEGPVNKAVFGAAADVAQALESKVRDGTPLGILVQLSDEIAQQMALIASFAMNGDVKGMITAARKIADTIKQVQTQAKHIADNCTDPRLKQNVLTYCDCGGNFSTQLKILCAVKSNDFNDPTAEEQLVTCAKGLSGAVINLVKSSEAASIKQRKVPQQ", "text": "FUNCTION: Involved in cell adhesion. Thought to play an important role in cytokinesis B, probably by providing substrate adhesion and traction forces. Required to organize and polarize the tip epithelium during cytokinesis. Required for the normal distribution of myosin in the tip epithelium. Involved in the localization of ctxA, ctxB, dcsA, exoc6 and rgaA. Thought to form a complex with ctxA, ctxB, and rgaA which regulates myosin accumulation to the apical plasma membrane. SUBCELLULAR LOCATION: Cytoplasm, cell cortex Cell junction Note=Localized during interphase over the cell basal surface with levels decreasing at the basal surface when cells enter the mitotic phase. At this time, there is intense localization along the polar edges (PubMed:19065153). Also found at cell-cell contacts in the slug and fruiting body and in columnar cells of the tip epithelium (PubMed:21393547). SIMILARITY: Belongs to the vinculin/alpha-catenin family."}
{"protein": "MGCCTGRCTLVFICTLQMLVALERQIFDFLGYQWAPILGNFLHIIVVILGLFGTIQYRPRYIVAYTIWTAFWVAWNVFIICFYLEVGGLSKDTDLMTFNISIHRSWWREHGPGCVWRLVPAPPSKNLGDHSFISVTGCIIEYQYLEVIHSAVQILLSLIGFVYACYVISVITDEEDSST", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NKAIN family."}
{"protein": "MNLILLGPPGAGKGTQAKLLIKKYRIPQISTGDILRAAVKDMTPMGGKAKSFMDAGALVPDEVVVGIIQERLNLADCSNGFILDGFPRTVAQADALAKVLSGLGRSIDHVISIVVDNEELLERVTGRRTCRNCGKGFHVSFDPPKSSGICDECSGELYQRDDDREDTMRKRLEVYWQQTSPLVEYYKNKSLLRSVEGVGSMEEIQQKIVSILQG", "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": "MSLLKIYWRAMQYLAVERTATITMCVASVLVALVTLAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFAQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAGGLKLEDKQPKQPVVEGSNVMPFPVKGAVA", "text": "FUNCTION: Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Beta- (1-->2)glucan exporter (TC 3.A.1.108.1) family."}
{"protein": "MLDFKGKNAVITGGSRGIGRAIALGLAKQGANILISYASHDSEADEVLETASKYGVKAHKVKVDQSDPYESIRFAEKAIETFGKVHILVDNAGICPFEDFFRISVDLFEKVWKVNVESHYFITQRIAKNMIENKINGRILLISSISAHVGGEFQTHYTTTKSALNGFMHSIAIVLGKYGILVNSLEPGTILTDINKEDLSNQEKRAYMERRTVVGRLGLPEDMVAPALFLLSDDNTYVTGTELLADGGMLINLQ", "text": "FUNCTION: Involved in the non-phosphorylated metabolic pathway of L- rhamnose catabolism. Catalyzes the oxidation of L-rhamnose to yield L- rhamnono-1,4-lactone. It can also oxidize L-lyxose and L-mannose, and uses only NADP. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MNIKDIGVIIAKKTLKENTFIITVFTKNHGLYSGVVKEFSKKSKFIYQEGNIIDFLWQARLHEHIGMAKCELIKSYTGYFITNKAKLYAFNSVISLIKELFHEREEHSKFFSFLINYLDNLSKNFCFRDYINFELALLAETGYKLDLTKCGVSHVTTDLIYVSPKSARALSYAVGKPYKDKLLMLPRFLLSDNSEITLEEKRQALALTNYFFNRYLFHNNRQVEARQTFIEYTLNNF", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family."}
{"protein": "MADNEILQMHDLKPAPGAKKDRTRVGRGEGSKGKTSGRGAKGQTKRNHVRPGFEGGQLPLYMRLPKLRGFKNPFKVEFQVINIARLVELFPEGGEVAVADLIAKGAVRDNAPVKVLGDGETTVAFTLKGVKASASAKSKIEAAGGSVSED", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MMPTVTAVSAILPLAILFVFSRALWKLWYLSDIPGPFWCKLTNIPRLCWVRTGRAHDIHYELHKEYGKLVRIGPSMISISDPAALSTVYPTRMGVPKSDFYKTQRPYVPGTGALPVVFNTQNEELHKELRGPVSSLYAMSNVMKLEPLMDETLQVLFDQIDARFVSGTKAFDLSNWLQFFAFEVMGTISFSKKYGFLEAGRDFNGLLSGIWGFMKSAAPMGQMPWLDDVLYKNALAAKLRGTTGMPVLRIVNKYITERITGHAKASSDHADMLSQFLDIQASNEKVPTWAPKAWTFSNVIAGSDSSANSMTTVMYNLMTHPETMARLYQELSEAKQQAGNVTAHILPWTSIRDLPYLDACVMEAFRIHPAFCLHLERLVPETGMEICGKQIPPGAIVGMSPWVINRHKPTFGEDVHQWRPERWLGHSETRLQELKNTILTFGYGRRVCLGKNIAIMEIKKLISSLVLNYEWTVIDPSEYRVENKWFFKQSGFDVTVKHRSSVRHTPRATNMTKVPPTLAIPASSSTVEVRVINTRTIMRTDHSLLWKSPVEGFKGLDLPIYAFLISNGNRHIIFDLGLRQDYENLPPRIAGLLKNAPYIVTEANVSEILDSDDTGLDIKGRDIEAVIWSHHHYDHTGDPSTFPPSTKLVVGPGVLSLTGGGYPKNPNTTVLETDLSGRKIQEISFDAQADSSVKVGPFDGVDYFGDGSFYLLNAPGHSVGHMCGLARVTTAPDTFIFMAADGCHHPGAIRPSEYMALPRDIPKSLVRKLRTAEADSGGKAQDGDTKPLLPFLPALFPDYTQAMETVEKIKQLDACDNVFVILPHDGSLLGAIDFFPRPINDWKKKGLKESTRWKFCQEMEEALSG", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of anditomin, a fungal meroterpenoid (PubMed:25216349). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM (PubMed:25216349). DMOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450 monooxygenase andK, which is further prenylated by the prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349). Further epoxidation by the FAD-dependent monooxygenase andE leads to epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid A through opening of the epoxide ring followed by the cyclization of the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn oxidized at the C-3 hydroxyl group to yield preandiloid B by the dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely responsible for the dehydrogenation of preandiloid B leading to the enone preandiloid C, as well as for the intriguing structural rearrangement to generate the bicyclo[2.2.2]octane core, transforming preandiloid C into andiconin (PubMed:25216349). FAD-binding monooxygenase andJ then produces andilesin D which is reduced by dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of acetyltransferase andG followed by a spontaneous acetate elimination leads then to andilesin B, which is in turn substrate of the short chain dehydrogenase andH to yield andilesin C (PubMed:25216349). Finally, the dioxygenase andF catalyzes the transformation of andilesin C to anditomin (PubMed:25216349). SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MAKFDAHLKCSFCGKSQDQVRKLIAGPGVYICDECIDLCNEILDEELLDNQANTNNSPQVKKKLPTDNPKKSVPLELTSIPKPLEIKSFLDNQVVGQESAKKILSVAVYNHYKRLAWKFKEENKNSNSKDSQATKLQKSNILLIGPTGSGKTLLAQTLAEFLDVPFAVADATTLTEAGYVGEDVENILLRLLQKSEMNVELAQKGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKMLEGTIANVPPQGGRKHPYHDCIQIDTSQILFICGGAFIGLEDIVQKRMGKHSIGFTTNSDQNKVDTKKIVDPRDALKNLELDDLVKYGLIPEFIGRIPVCAVLDRLTKETLESILTQPRDALVKQFKTLLSMDNVELSFEPDSVEAIANEAYKRKTGARALRSIIEELMLDIMYTLPSEENVKEFTITKKMVDNLFSSKIVKLPSGSKRVIKESA", "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": "MKLLFFIWFAIFSKVFGISEEVAEAADVVSEDLKEDFDVEESPVQQYVNLNVTYSIVERPGLNLTDLFEFVPEETLTLNYNLYNGENSSVSVVGVSGNVYTFPDGYYAANITESSIEPLEVMFNRSAIFQQEVRLVLPEGRYYLEPVLIVEKDEKLMRVAVQPVTVEIAPLPLSIFNPQFLSIIVTLGALVGGAFYYLVYLKASTKETKGKSKTVKVDETWLPDTYKK", "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": "MRQRLLFLTTLVPFVLAPRPPEEPGSGSHLRLEKLDSLLSDYDILSLSNIQQHSIRKRDLQSATHLETLLTFSALKRHFKLYLTSSTERFSQNLRVVVVDGKEESEYSVKWQDFFSGHVVGEPDSRVLAHIGDDDVTVRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKDFSRLQSPKVCGYLNADSEELLPKGLIDREPSEEFVRRVKRRAEPNPLKNTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEQIRILKSPQEVKPGERHFNMAKSFPNEEKDAWDVKMLLEQFSLDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYNPGVKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKPGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGDAEDDTVCLDLGKCKAGKCIPFCKREQELESCACADTDNSCKVCCRNLSGPCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHHSNIEMLSSMDSASVRIIKPFPAPQTPGRLQALQPAAMMPPVSAAPKLDHQRMDTIQEDPSTDSHVDDDGFEKDPFPNSSAAAKSFEDLTDHPVTRSEKAASFKLQRQSRVDSKETEC", "text": "FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane- associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2 (By similarity). Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (By similarity). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPSDSPYSGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNVNSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRAKYESTARSWTQKYAMG", "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": "MRGVVGVLALQGDFREHKEALKRLGIEAKEVRKVKDLEGLKALIVPGGESTTIGKLAREYGLEEAVRRRVEEGTLALFGTCAGAIWLAREILGYPEQPRLGVLDAAVERNAFGRQVESFEEDLEVEGLGPFHGVFIRAPVFRRLGEGVEVLARLGDLPVLVRQGKVLASSFHPELTEDPRLHRYFLELAGV", "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": "MAIELNVGRKVTVTVPGSSANLGPGFDTLGLALSVYDTVEVEIIPSGLEVEVFGEGQGEVPLDGSHLVVKAIRAGLKAADAEVPGLRVVCHNNIPQSRGLGSSAAAAVAGVAAANGLADFPLTQEQIVQLSSAFEGHPDNAAASVLGGAVVSWTNLSIDGKSQPQYAAVPLEVQDNIRATALVPNFHASTEAVRRVLPTEVTHIDARFNVSRVAVMIVALQQRPDLLWEGTRDRLHQPYRAEVLPVTSEWVNRLRNRGYAAYLSGAGPTAMVLSTEPIPDKVLEDARESGIKVLELEVAGPVKVEVNQP", "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": "MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHNSSHNKKDKVVICQRVSQEEVKKWAESLENLISHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLVNPSSCGAEKQKGAKSSADCASLVPQCA", "text": "FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)- alpha-1 is inhibited by palmitoylation of the G-protein (By similarity). FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)- alpha-1 is inhibited by palmitoylation of the G-protein."}
{"protein": "MDVRIKCNSEEPESPEQKILASSQRLLQFTNCRLVRDHRIIHDDLWVRDGRIVNPEPVFFDERTKAHCRIDCGGAIIAPGYIDLQINGGYGVDFSYDTETIEEGVATVARGLVKSGVTSFCPTLVTSPSDSYHTILPRIPAEVPKGAGILGIHAEGPFINPQKKGAHPEHCIQTIDKGLSTLKETYGSLERIKIITLAPEKVTDPEVIGQLVERGITVALGHSMASLSDGERAVQQGATLITHLFNAMLPFHHRDPGLVGLLASDAVPHGRTVYFGIISDGVHTHPAALRIAYRTHPQGLILVTDAISALGLEEGVHHIGQLPLQVKQGKAFIAGTETLCGSIAPMDECVRIFQKATDCSVVYAIEAATLHPAQCLKIEKQKGTLDFGSDADFVLLDDQLRVLSTWIAGVCVHRTVK", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. NagA family."}
{"protein": "MSDSNLDGVLVLIPARMASTRLPGKPLADICGLPMIVQVAMRAQEAAIGRVVVAVDDIRVFDAVSAAGFEVVMTSSDHQSGSDRIFEALQKVDPAGKAEFIVNVQGDLPTIDPETVRAALRPLENEAVDIGTLTTEIDNEEDKTAPHIVKVVGSPVSDTRLRGLYFTRATAPYGKGPLYHHIGLYAYRRAALERFVSLGPSTLERREALEQLRALEAGMRIDAEIVDTVPLGVDTPADLEKARRILSARTG", "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": "MGKKQVALPRALPPMPSTSIDEIPHSRPKKKKTKSNNNTPDDVLQNAGFTTSENNDPLSPERRKRKKKRFSIDAETSLTQNNPSIPVVLNGKDTDNQTTEEGATRKPRRRTKKTRLAEEEFPNELGVEDEDIIPDGHTKIPTQNPAFLASSLTSQPVGKLFVEKNRRFQAADRSEIIKTTEQMDVFLDVKPTWSSMDVSLTAHHIFRMVGLFCCGFLAGYAVWNIVVIYVLAGSQLTNLPNLLQTYKILAYPSQCFLYFLLVLSTVTAFDRIDLERAADALRGLLKLDPAAVASFFYFVALFLVLSQQMTSDRMNFYTPPTQNGSLWQTDTEGQILQPWIVINLVVAILVGLAWLFLSCRPDIDHSEEAMFIPEEEDYPDMEKGMKIQG", "text": "FUNCTION: Component of the transition zone in primary cilia. Required for ciliogenesis (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cell projection, cilium Note=Localizes to the transition zone. SIMILARITY: Belongs to the TMEM237 family."}
{"protein": "MKVIFNADDFGLTQGVNNGIIKAHQQGVVLSTTMMMGMDAEQHAVELANQNPNLKIGVHLRFTAGNPLTGHPNLTGGGEQFVRFNELWKKRDFQEEAVYQEAVAQVERFLSLGLPLSHIDSHHHAHTHPQLLPVIRRVAEQYRVPLRGSGLCHIDCDTTYHFTDEFYDQGVSLDGVMAHLKSLKSQYDVVEVMCHPADVDQHLLSISGYALLRELELQVLTSPILKQELAEHGMSITDYSTLISTRKFASV", "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": "MNFEGKLLGQDLKIGIVVSRFNDFITGRLLDGAKDVLVRHEVESEKIDVAFVPGAFEIPLAAKKLAETGKYDAVITLGCVIRGATSHYDYVCNEVAKGVSKVSDTTGLPVIFGVLTTETIEQAVERAGTKAGNKGAEAAMAAIEMANLLKSI", "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": "MGKVWKQQMYPQYATYYYPQYLQAKQSLVPAHPMAPPSPSTTSSNNNSSSSSNSGWDQLSKTNLYIRGLPPHTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPAAAQKAVSALKASGVQAQMAKQQEQDPTNLYISNLPLSMDEQELENMLKPFGQVISTRILRDSSGTSRGVGFARMESTEKCEAVIGHFNGKFIKTPPGVSAPTEPLLCKFADGGQKKRQNPNKYIPNGRPWHREGEVRLAGMTLTYDPTTAAIQNGFYPSPYSIATNRMITQTSITPYIASPVSAYQVQSPSWMQPQPYILQHPGAVLTPSMEHTMSLQPASMISPLAQQMSHLSLGSTGTYMPATSAMQGAYLPQYAHMQTTAVPVEEASGQQQVAVETSNDHSPYTFQPNK", "text": "FUNCTION: Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKPSPRTPDFSPYLDFDRAQWRELRNSMPQVLTQKEVIELRGIGENIDLAEVAEVYLPLSRLIHLQVAARQQLTAATETFLGTSPSISVPFVIGVAGSVAVGKSTTARLLQVLLQRWNSHPRVDLVTTDGFLYPGAELIRRGLMSRKGFPESYDQRALLRFVTDVKSGKLEVNAPVYSHTAYDRVPGEFTTVRQPDILIVEGLNVLQTGPTLMVSDLFDFSVYVDARTEDIEKWYIDRFLKLRDTAFRRPGAHFSHYADMADPESIAVARELWQSINLPNLVENILPTRVRASLVLKKGSDHLVERVRMRKI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic pantothenate kinase family."}
{"protein": "MIHSNISIQINGEPFNCSKPISLQFLLNYLDFNSERVAVELNDILLPETLFHSTYLNDQDKLEVITIVGGG", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf40 family."}
{"protein": "MRPKSWGWISMSERLEGKRVRIKAKGKIFEGIVMPSFTGNFVLKLDNGYNVGFKEYELLEVLEVEPFEPHLPELVKREGLPDVKIISTGGTIASKVDYRTGAVTSQFTAEEIASEVPELTEICNVDAELLYNILSENMKPENWIELARHVYKALKDHEGVIITHGTDTMHFSAAALSFMLSTPKPVVFVGAQRSSDRPSSDAAMNLLCAAKAATEDIGEVVVCMHGSTSDDYCLVHRGVKVRKNHTSRRDAFQSVNAKPIGRIDYPSLSVEWLSWRYRRGERELKLTDRLERKVVLIKFFPGLSSDILEYYHSKGYRGFVIEGTGLGHVSTDWIDTLRRVCEDSVVVMTSQCLWGRVCDRVYDTGRDILRAGVIEGEDMLPEVALIKLMWLLGNYSIEEAKEMVKKSVAGEIEPTTQY", "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": "MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATSRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGPCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS", "text": "FUNCTION: Thrombin-like snake venom serine protease. Displays a specificity similar to trypsin. Releases only fibrinopeptide A in the conversion of fibrinogen to fibrin. Reversibly increases the permeability of the blood brain barrier (BBB) in mice (PubMed:11137545, PubMed:20637222). Induces the barrel rotation syndrome in mice, which is manifested by gyroxin-like, rapid rolling motions (PubMed:11137545, PubMed:20637222). This syndrome may be due to its effect on BBB permeability, and certainly also to other actions affecting endogenous substrates present in the endothelium, nervous tissues or blood (PubMed:11137545, PubMed:20637222). Also shows a moderate inhibitory activity on the human voltage-gated potassium channel Kv10.1/KCNH1/EAG1 (58% current inhibition at 5 uM) (PubMed:32161292). It blocks Kv10.1/KCNH1/EAG1 in a time and dose-dependent manner and with a mechanism independent of its enzymatic activity (By similarity). It may have a preference in interacting with Kv10.1/KCNH1/EAG1 in its closed state, since the inhibitory effect of the toxin is decreased at more depolarized potentials (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MPQLNTAVWPTTITPMLLTLFLITQLKMLNSNYHLPPSPKPMKMKNYNKPWEPKWTKICSLHSLPPQS", "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": "MSYQEQQCKQPCQPPPVCPPPKCPEPCSPSVCPEPCPPPKCPEPCPEPCPPPSFQQKCPPVQPPPPCQQKCPPKSK", "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 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cornifin (SPRR) family."}
{"protein": "MASMGTLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPRMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAETSCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE", "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 Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MRAKWRKKRMRRLKRKRRKMRQRSK", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (By similarity). Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII (By similarity). FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. 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). Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII (By similarity). FUNCTION: Component of the large ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII (PubMed:9299532). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL41 family."}
{"protein": "MSKLKSSESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTSHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEDGDDKDDYWREQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYTSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKNKIMNRSFFDDEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSMMIRPEPRYRAENIMLLELDMPSRTTRDYEGPAISPKVQAALDAALQDEDEIQVDASSFESTASRKPKARPKSGRKSGSSSSSSGNPASQFYPQSRGLVPK", "text": "FUNCTION: Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (PubMed:7559760). Plays a role in cilia formation (PubMed:9865700). Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors (By similarity). Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (PubMed:31746486). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, cilium Cell projection, dendritic spine Note=Colocalized with GRIN2A in dendritic shafts and in DLG4-positive spines. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily."}
{"protein": "MTDYLLLFVGTVLVNNFVLVKFLGLCPFMGVSKKLETAIGMGFATTFVMTIASISSWLMDTFILVPLDLLYLRTLSFILVIAVVVQFTEMVVRKTSPTLYRLLGIFLPLITTNCAVLGVALLNINQSHTFMQSAVYGFGAAVGFSLVMVLFAAIRERLAVANIPAPFKGSSIGLITAGLMSLAFMGFSGLVKL", "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": "MDLKNLTQEERSELSLIDVAHFILEQRKETILFPELVKEIQAFLGLKDAEIRERLVQFYTDMNIDGNFISLGNNTWGLRAWYPMDAIDEEVQTQTTPKKKRKSDDDDDEDEEILDDDVDYDDEEIVEELGEEEISLADVLLDEDEDDDDHLPDGIEGDLATVEDDYTDGDYTEDPEDK", "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": "MIGKLTGRLDYRSTDHVLIDVRGVGYIVYCSDRTLAALPGVGEVVALYTDMVVREDLMQLFGFMSLAEKEWHRLLCSVQGVGAKVSLAILGALGPDGVSRAIALGDWASVKSAKGVGPKTAQRIVLDLKDKAPGVMAMGGTVAQAMEGAVEVVEVIEPAAPAPRKAAPPGGAGAATAGALSALSNLGYGPSDAAAAVAQAAAEAPEAGETDLIRAALRLLAPKT", "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": "MAELEFEKPVVELRNKIRELKEYTKHSQMDFSEEIRILEDKLENLEEEIYGNMKVWDRVQIARHAERPTTLDYIEHLFTDFFECHGDRFFGDDAAIVGGIAKYNGMPVTVIGHQRGKDTKENIRRNFGMPHPEGYRKALRLMKQAEKFNRPIICFIDTKGAYPGKAAEERGQSEAIARNLFEMAGLTVPVICIVIGEGGSGGALGLGVGDYIYMLENSTYSVISPEGAATILWKDATKARDAAEALKITAADLKELGVIDEIIPESRGGAHRNILKQSENINVVLQKTFEQLSGISKDELIEKRYEKYMKIGQVSFSNASIWVK", "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": "MQKLAVYVYIYLFMQILVHPVALDGSSQPTENAEKDGLCNACTWRQNTKSSRIEAIKIQILSKLRLEQAPNISRDVIKQLLPKAPPLQELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLVQMEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRQVQKPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKAFDENGRDLAVTFPGPGEDGLNPFLEVRVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS", "text": "FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MAKKSLNETSPVARFEQSLEELEQLVQKMEVGDLSLEQSLTAYERGIGLYRDCQQALEQAELRVRLLTDPARPELAQAFEPPSLDG", "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": "MTAVQAARRARIERRTKESDIVIELDLDGTGRVDVETGVPFYDHMLTALGSHASFDLTVRTTGDVEIEAHHTIEDTAIALGAALGQALGDKRGIRRFGDAFIPMDETLAHAAVDVSGRPYCVHSGEPDHLQHSTIAGSSVPYHTVINRHVFESLAMNARIALHVRVLYGRDPHHITEAQYKAVARALRQAVEPDPRVSDVPSTKGVL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MGKRVVYPGTFDPPHYGHLDIVKRSARIFDEVVVAVAKKPRKFLLFDAEERVKMFEKMVEDIPNVEVKMFDCLLVDFMKREGINVIVRGVRLFTDFEYELQIALTNYKLAGVETVFMMPSQEYIHISSTIVRDVASYCGDLDNMVHPYVKQKLREKFNCGS", "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": "MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWSFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLRKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANTQQFEHIVQLRRVLTTATITLLPDAERFSFPRVINSADGATTWYFNPVILRPNNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHHATVGLTLRIESAVCESVLADASETMLANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLVK", "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": "MVVLMLREILKKVAHFSEQKPFLMLLIILIITVFAGISATNVKSQTAFEKMLPQDNPIIKTLYEVRDEFGGTDVITICIKLKPSDSSDKVVDIRDPRVLKAIKELEDNLRYVDGITSVSSPVDIIIQKNNGIVPNDIDTVKDILNKLPEDKRKRIFNSDYSMTVVNAYTDAGGDQKKLMRVMDDVNERIEETPFPPGVEVIATGTPPMRKLMDELMKESQSFTTTVGLIGILIILIIYFRKPLSSIMPLLPVLIAVIWTGGAMGLLDIPLDMATAGIGSLILGLGIDYGIHLMHRYDEERRKGMPIDKAIETAVVETGTAVMATTATTVVGFLALVLAPLPMMANLGKVCALGISFCMVVVLTLLPALIVIEERHIMPLIKRLKGDTQ", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily."}
{"protein": "MVATSKQTTQGYVVEAYGNLLRVHVDGHVRQGEVAYVSVDNTWLKAEIIEVVGDEVKIQVFEETQGISRGALVTFSGHLLEAELGPGLLQGIFDGLQNRLEILADTSLFLRRGEYVNAICRETVWAYTQKASVGSVLSRGDVLGTVKEGRFDHKIMVPFSCFEEVTITWVISSGNYTVDTVVAKGRTSTGEELEFTMVQKWPIKQAFLEGEKVPSHEIMDVGLRVLDTQIPVLKGGTFCTPGPFGAGKTVLQHHLSKYAAVDIVVLCACGERAGEVVEILQEFPHLKDPHTGQSLMHRTCIICNTSSMPVAARESSIYLGITIAEYYRQMGLHILLLADSTSRWAQALREISGRLEEIPGEEAFPAYLASRIAAFYERGGAVKMKDGSEGSLTICGAVSPAGGNFEEPVTQATLSVVGAFCGLSKARADARRYPSIDPMISWSKYLDSVAEILEKKVPGWGESVKQASRFLEEGAEIGKRIEVVGEEGISMEDMEIFLKSELYDFCYLQQNAFDAEDCYCPFDRQIELFSLMNHIFNSRFCFDCPDNARSFFLELQSKIKTLNGQKFLSEEYQKGLEVIYKLLESKMVQTA", "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": "MSALTRLASFARVGGRLFRSGRARTAGDGGVRHAGGGVHIEPRYRQFPQLTRSQVFQSEFFSGLMWFWILWRFWHDSEEVLGHFPYPDPSQWTDEELGIPPDDED", "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 NDUFB2 subunit family."}
{"protein": "MAARRDGWLGPAFGLRLLLATVLQTVSALGAEFSSESCRELGFSSNLLCSSCDLLGQFNLLQLDPDCRGCCQEEAQFETKKLYAGAILEVCGUKLGRFPQVQAFVRSDKPKLFKGLQIKYVRGSDPVLKLLDDSGNIAEELSILKWNTDSVEEFLSEKLERI", "text": "FUNCTION: May be involved in redox reactions associated with the formation of disulfide bonds (By similarity). May contribute to the quality control of protein folding in the endoplasmic reticulum. May regulate protein folding by enhancing the catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Note=The association with UGGT1/UGCGL1 is essential for its retention in the endoplasmic reticulum. SIMILARITY: Belongs to the selenoprotein M/F family."}
{"protein": "MKTLLLTLVVLTIACLDLGYTKTCFNDDLANPKTTELCRHSMYFCFKNSWIAGGVERIERGCSLTCPDIKYNGKYIYCCTRDNCNA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Orphan group IX sub-subfamily."}
{"protein": "MRSTYILIIVPLIIIGGGVVADNTNETPVLAHSSDEQPHQRLTYYNWDHKDLGTSAFEDLPPLQDQPTPLPIDQSDRCPDGWLRYSDSCYFIETESLGFAKAERKCHDKQATLFVANSMEEWDAVRDHAEKSVLSWIGLVRFSHYERLEQLPRWQTTGSINPSKINWLIKPFKPVVNGWSSYANCAASFQSPTEVESASYTFFYPCTMAFKSICERNSTILNARN", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "EDESTVLVDNKCQCVRITSRIIRDPDNPSEDIVERNIRIIVPLNTRENISDPTSPLRTEFKYNLANLCKKCDPTEIELDNQVFTASQSNICPDDDYSETCYTYDRNKCYTTLVPITHRGGTRMVKATLTPDSCYPD", "text": "FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MVLLDPLANALSTIKNAEAIGKSSCIVRPASKNIGNVLKVMQDLGYIGDFEFIDDGKAGIYSVTLVGRINKCGAIKPRYSVGTGSFERWEKQFLPAKNFGALILTTSSGVMSQYEARDKKIGGQLLAYVY", "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": "MKFVDEAPIFVHAGKGGNGCMSFRREKFIEKGGPDGGDGGDGGSVYLEADENLNTLVDYRYQRSFRAQSGEGGRGRNCTGAKGEDLILPVPVGTSVIDMETEEVIGDLTKAGDRLLVAQGGFHGLGNARFKSSVNRAPRQTKPGSEGEDRQIKLELKVLADVGMLGLPNAGKSTFIRSVSSAEPKVADYPFTTLVPSLGVVKVQTHRSFVVADIPGLIEGASDGAGLGIRFLKHLTRCRILIHLVDVNPIDESSPVESARAIVDEINKFSPTLAQRERWLVLNKCDTLSEDEVAEVERQIREALNWVGPIYKIAAISNTGTAQLCEKLLGHLEVLWQKERDNEELAEQEHEVQLQMQQEARERIALLQQRHRAAKAAAKGRALDNDDDDEDDDHEMEIHYVP", "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": "MHALQAKILDPRIGNEFPLPAYATPGSAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYVGDPGLAALILPRSGLGHKHGIVLGNLVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEEFDETQRGAGGFGHSGSH", "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": "MATFSQKPAEVEKKWVIIDAEGLVVGRLASIIAMRLRGKHKATFTPHVDDGDNVIVINADKVVFTGKKYSDKVYYWHTGYAGGIKERTARQIIEGRFPERVLEKAVERMVPRGPLGRRQMKNLRVYAGSNHPHEAQQPVALDVAALNKKNVRSA", "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": "MAIVRAHLKIYGRVQGVGFRWSMQREARKLGVNGWVRNLPDGSVEAVLEGDEERVEALIGWAHQGPPLARVTRVEVKWEQPKGEKGFRIVG", "text": "SIMILARITY: Belongs to the acylphosphatase family."}
{"protein": "MNIYAVGGAIRDELLGVPVQDRDYVVVGATPEQMTAQGFRPVGKDFPVFLHPQTQEEYALARTERKTAAGYHGFQFHYAPDVTLDEDLARRDLTINAMAREVSPEGTLVGPVIDPFDGQADLRARVFRHVSDAFVEDPVRILRIARFAARFADFTVADETLALMRRMVDAGEVDALVPERVWQEIARGLMEAKPSRMFAVLRDCGALARILPEVDALWGVPQRADYHPEVDTGVHVMMVVDYAAKQGYSLAVRFAALTHDLGKGTTPADVLPRHVGHESRSVELLKPLCERLRVPNECRDLALVVAREHGNLHRVMEMGAAALVRLFERSDALRKPARFAELLQACESDARGRLGLDAQPYPQAERLRVALAAARSVDAGAIARGIGSDTEKIKEAVHRARIQAVAQALAIGE", "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": "MAKIHELSEILANQIAAGEVVERPASVVKELVENSIDAGAKQIDIIIEDAGLKSIQIIDDGNGIEAEDVETAFKRHATSKIIDRKDLFKVHTLGFRGEALPSIASVSDVVMETAVSGRAGTKIHIKGGEVLEKTLSASREGTTITVSDLFYNTPARLKYLKSVQTELSYISDIVNRLALSHTDVALSLTNNGRQLLQSAGNGNLQQTIGAIYGVQNARQMIKFEDANLDFKISGYTSLPKLTRASRNYISLLVNGRYVKNFQLTKAVIEGYGSKLMTGRYPITVLSIELDPTLVDVNVHPTKQEIKISKEDELVTFIQKTIFERIGQENLIPDGLQNIKSKTKEKLDFEQLKVGLNEASKQYQTKQHRTGITSEVTAALFGEKLTKDESQTQTNEKIKEETKVELSPIIIKDKQDLKSDRVKEWDEKYQSRNKETEVTSIAEKNGSVDDKRKDTPRFPTLRYIGQMHGTFLFAEGEEGLYIVDQHAAQERVKYEYYREEIGKVSPTQQNLLVPIVLTYPTTDALIIDENIDKLKELGIYLEDFGQNTYIIRQHPTWFKEGQEESIIREMIDYFLKDRKLSIAKFREKTAIMMSCKRSIKANHHLDDKQAKSILEQLKTCENPFNCPHGRPVLVKLSNKDLEHMFKRIQDPHHTGILEED", "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": "MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLTMAMRDSGTVLDWKSLNLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGFDIFPDDNRFREIIQDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITGSILAKKLAEGLDALVMDVKVGSGAFMPTYELSKALAEAIVGVANGAGVRTTALLTDMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGQLAKDDAEARAKLQAVLDNGKAAEVFGRMVAAQKGPSDFVENYDKYLPTAMLSKAVYADTEGFISAMDTRALGMAVVSMGGGRRQASDTIDYSVGFTDMARLGDSIDGQRPLAVIHAKDEASWQEAAKAVKAAIILDDKAPASTPSVYRRITE", "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": "MKKINIIKIVFIITVILISTISPIIKSDSKKDISNVKSDLLYAYTITPYDYKDCRVNFSTTHTLNIDTQKYRGKDYYISSEMSYEASQKFKRDDHVDVFGLFYILNSHTGEYIYGGITPAQNNKVNHKLLGNLFISGESQQNLNNKIILEKDIVTFQEIDFKIRKYLMDNYKIYDATSPYVSGRIEIGTKDGKHEQIDLFDSPNEGTRSDIFAKYKDNRIINMKNFSHFDIYLEK", "text": "FUNCTION: Superantigen that acts as a causative agent of the symptoms associated with scarlet fever. Has been associated with streptococcal toxic shock-like disease and may play a role in the early events of rheumatic fever. Superantigens cross-link major histocompatibility complex (MHC) class II and T-cell receptor (TCR) molecules, resulting in an overstimulation of T-cells associated with a massive release of pyrogenic and inflammatory cytokines. FUNCTION: Superantigen that acts as a causative agent of the symptoms associated with scarlet fever (PubMed:1500157, PubMed:1987034, PubMed:9253413, PubMed:11163233). Has been associated with streptococcal toxic shock-like disease and may play a role in the early events of rheumatic fever (PubMed:1500157, PubMed:9253413, PubMed:11163233). Superantigens cross-link major histocompatibility complex (MHC) class II and T-cell receptor (TCR) molecules, resulting in an overstimulation of T-cells associated with a massive release of pyrogenic and inflammatory cytokines (PubMed:9253413, PubMed:11163233). SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family."}
{"protein": "MSQSVSERTRIKSDRYESGVIPYAKMGYWDASYAVKTTDVLALFRITPQPGVDPVEAAAAVAGESSTATWTVVWTDLLTACDRYRAKAYRVDPVPNAADQYFAFIAYECDLFEEGSLANLTASIIGNVFGFKAVAALRLEDMRIPHSYLKTFQGPATGIVVERERLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVMGYTAIQSMALWARENDMLLHLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYHTLRLTTLDVNLPYGLFFEMSWASLRRCMPVASGGIHCGQMHQLIHYLGDDVVLQFGGGTIGHPDGIQAGATANRVALESMVLARNEGADYFNQEVGPQILRNAAKTCGPLQSALDLWKDISFNYTSTDTADFAATSTANV", "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": "MLKSRIIPCLDVKDGRVVKGVNFVDLTDAGDPVEAAIRYDAAGADELCFLDITASSDDRPILLDVVRRTAEACFMPLTVGGGVRTLDDIRALLLAGADKASIMTAAVANRDFVREAAEKFGSQCVVVAIDAKQVRPGRWEIFTHGGRKPTGLDAVDYAREVVALGAGEILLTSMDRDGAKTGFDIPLTKAVTDAVNVPVIASGGVGTLDHLVEGVRDGGASAVLAASIFHFGEFTIAEAKLHMANCGLRMRLDGIV", "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": "MTINALLLSSSRVGDTPYLAHAIPFIKPLTTNARKWIFIPYAGVSMSYDTYLASVVTGLSGLELDISGIHQHPDPQQAIKDADGILIGGGNTFHLLHQLYRYDLVTLIGEQVALGKPYIGWSAGSNVSGLSIRTTNDMPIIEPPSFNALNLVPFQLNPHYSNYQAPGHNGETRAQRLLEFTKVDPLTPVVGIVEGSALWRQGDKLSLLGNQPAYLFCGEQQEIPIPVGSDLSNLLKPSL", "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": "MQKTWSDRFEEGLNPFIESFNASINFDFLLIEEDLDGSIAHARMLAKTGIITSEEADQLEAALQKIRLEASQGLFKPDISDEDVHMSVERRLISILGPLGKKLHTARSRNDQVGTDLRLWLRRRIDDIDIELKKLQVALFKKAEKNLLTLIPGYTHLQRAQPLSLAHHLLAYIEMLQRDRNRLADVRERVNICPLGAAALAGTSLPIDRAFTANQLGFTSIYSNSLDAVSDRDFTVEFTAAASLIMTHISRLADEIILWASEEFSFVRLTDRCSTGSSLMPQKKNPDVPELVRGKTGRVFGHLQSLLTMMKGLPLAYNKDFQEDKEAVFDTVKTVRDSLKAMTILLEEGLEFSLERLKETVEADFSNATDVADYLVSKNIPFREAYQIVGRVVRLCIQKKILLKDLTLKEWQEINTLIDHDIYEKITPEKVVAARISDGGTGFDRVREELEKWRNDLISLNQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MGAALKMTIFLLIVACAMIATTEAAVRIGPCDQVCPRIVPERHECCRAHGRSGYAYCSGGGMYCN", "text": "FUNCTION: Has antifungal activity against T.rubrum. Blocks voltage- dependent N-type calcium channels (Cav2.2 / CACNA1B). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the diapausin family."}
{"protein": "MNFNHVPVLLEETIDSLNIKEDGIYVDCTLGGAGHSSEILKKLSKKGRLIGIDQDINAIKAAKERLKDYENVTYVHNNFYNLASILDELNVDKVDGILMDLGVSSYQLDTPERGFSYMKDAMLDMRMNTENGISAYDVVNGYSEDDLFRIIKDYGEERFSRKIAKAIVKERNEKPVETTLELVKIIKDVIPMKFQQGGHPAKKTFQAIRIEVNHELEILNKTVEDGVNYLNPNGRISVITFHSLEDRIIKTKFKELENPCTCPKEFPICVCGKKPVVKVVTRKPIEPNEFERENNSRSRSSKLRVAQKI", "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": "MKNQKTVVVGMSGGVDSSVSALLMKEQGYNVIGLFMKNWEEKDENGVCSSAQDYDDVRRVCDHINIPYYAVNFVENYRKQVFTQFIADFQKGWTPNPDILCNREIKFKVFLEKALELGADFLATGHYCQNLILDKGSPSLVKGIDHNKDQTYFLYTLNQQILQQVLFPVGGLEKSQVRDIARKHQLVTAEKKDSTGICFIGERDFRSFLSQYVAIQPGAFQTLQGKNVGKHMGTAYYTLGQRKGLGIGGAGEAWFVVGKDHERGIVFVEQGANHPALYCDELIATDLSWVAEAPLLPYTCQSKVRYRQNDQFCTIHRIENGKAFVTFDRPQRAVTPGQSIVFYVGNICLGGGVIQQPGPTYYDQKKSLPHQSPRND", "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": "MARMIHCAKLGKEAEGLDFPPLPGELGKRLYESVSKQAWQDWLKQQTMLINENRLNMADPRARQYLMKQTEKYFFGEGADQASGYVPPAQG", "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": "MKLLHLDASILGTGSVSRELSALIVRRLAGDAPDAVTYRDLVAENPPHLTVATLPGAHPVSAMAGPLDAAGQAVRDASDRMLSEFVAADTVVIGVPMYNFTIPSQLKAWIDRLLVPGTTFRYGAAGPEGLMGGKRVILALARGGFYGPGTASVPAEHAEHYLRTVFGFMGIVPELVLAEGLAAGEHNKAQALASARDAVGQLAA", "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": "MAVVWMQQNFQQLIEQLKGTLGKLGARKLIALGLVGAALMGAILYTSIYLGRPSYETLYVGLSRDDVNRMGLALGEAGIPFDVKSDGSSILVPIGKAENARMYLAEKGLPTSNNAGYELFDNMGSLGLTSFMQEITRVRALEGEIARTIQAIRGVKAARVHIVLAEKGSFRRGDQKPSASVVIRAEGGFSAESAQSIRQLVAAAVPSLDASSVTVLDTNGHLLASAGEGANGAALMTASLEQQVASHVDDSIRKALAPYLGLGHFQTSVQAALDTDRRQTKETTYDPESRVERSVRVVRESGDSRNNRNDNATGVEQNIPQEQIQNRNGESSTEKTDRREELTNYEVNSMTVSTVSDGYSIKRLSIAVVIDQARLLQTAGTTPPPANFVDQQITKIRDLVATAAGLNTNRGDVINVTAVNFLDSAGADMEPVSAPWTDTLLRQSGSYANALAILAAVGLLIWFGLRPLLRDQNVKPAGTEVAIREAGEVATPNFIGGAESVGEGVQAVIGGPAAYADQMKTSLSDLRQRMRMPAKLRLEQMIEMDEERVAAVLKQWIHETASGREADPAKASAMPELKAA", "text": "FUNCTION: The M ring may be actively involved in energy transduction (By similarity). The flagellum is required to cause a persistent disease in a murine model of infection. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Bacterial flagellum basal body. SIMILARITY: Belongs to the FliF family."}
{"protein": "MAFRWAIQMALRRGGGGGQRLLLTQHQHQNYQFFKTSSSTQFSTRNSQILDLDTPQKSPNFSENSKNKKSKKIEWSTGSILMLGLPAFAFSLGVWQIYRLIWKLELIEHLKSRLSQEAIELPDDLSSSSLEPLEYCRVRVTGEFLHQKEFVISPRGRFDPAKKTSASVGSMLSENEMSSHGGHLITPFRLKNTGKVILINRGWLPTFYFDPESHAKTNPQGTVILEAIVRKTEQRPQFVGQNVPEQGVWYYRDLEQMAKWHGTEPVWLDAAYETTVPGGPIGGQTNINVRNEHMNYLTTWFTLTLVTMLMWIHKFRK", "text": "FUNCTION: Probably involved in the biogenesis of the COX complex. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SURF1 family."}