accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
P81176 | VSP1_GLOBL | Snake venom serine protease | Gloydius | IIGGDECNINEHRFLVALYTPRSRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGMHSKKVPNKDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSTHIEPFSLPSSPPSVGSVCRIMGWGRISPTEETFPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCRGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIKSIIAGNTDASCPP | Thrombin-like snake venom serine protease. Cleaves fibrinogen (beta chain of fibrinogen (FGB) and more slowly alpha chain (FGA)) without inducing fibrin clotting and cleaves kininogen to produce bradykinin (KNG), resulting in the reduction of blood pressure. | P81176 |
Q9BZM5 | ULBP2_HUMAN | Retinoic acid early transcript 1H | Homo | MAAAAATKILLCLPLLLLLSGWSRAGRADPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGNKTVTPVSPLGKKLNVTTAWKAQNPVLREVVDILTEQLRDIQLENYTPKEPLTLQARMSCEQKAEGHSSGSWQFSFDGQIFLLFDSEKRMWTTVHPGARKMKEKWENDKVVAMSFHYFSMGDCIGWLEDFLMGMDSTLEPSAGAPLAMSSGTTQLRATATTLILCCLLIILPCFILPGI | Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity. | Q9BZM5 |
Q4DPN8 | TRM52_TRYCC | tRNA methyltransferase 5 homolog 2 | Schizotrypanum | MSGEERHQGGGEKGPMDHDEPPSYRTRVEASVELMALRVKPVHLLGEVLKALRGCLYDMRGVRNVMDAPQPTSDPGEEHKLLLLNPQVIPPPSSAAKNDSMAPTQPLWVEANHASVPPVVRERLQSFLLGKRSVAQSLRVAVAQHTVRLSHRNFTMPELLQRILPPGTIPLSGFEQVGHIAHVNLSAAHLPYRADIGAVILDCNPTVRVVVNKVDNIASVFREFKMEVIARRTTHSDMKGTPVKENSGDEEELHGLLLATVRQHGCIFRVPYDRVYWNSRLSHEHARVVGMMQSGDMLYDAMAGVGPFAIPAAVAGVKTYANDLNPVAAEYLRINAELNHINKDTFHVFNMDGREFLNTVLYRDVVSGAAVCGRRHVTMNLPAIAVEFLDVFTKPPWSQPLVSLSSLEEKAKEGKEKGEHVKMHPDKRLLFHVYCFSKNMDDFLGDAVKQVERWLAFSLAGENLEAVHMVRDVAPLKRMVCVSFTLPEAFWLHREAKGMSPLKRARSD | Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. | Q4DPN8 |
A8NX72 | TVP38_COPC7 | Golgi apparatus membrane protein TVP38 | Coprinopsis | MAADSTPGSHHRNLFFQYGKAAIHRYHRLHLYGKAFIWLVILFYIAFGVFVIIVTPARIAQFLYDQAKLLAATRFGWVALLLSIICISFPPLIGHTTLVTLCGFAYGMKGFYIAFAGSILGSALVFVVLRFLFTEKIRSWSAQNEKWQALEAVVRSKGLPLIVLIRVSPFPPWVYANSLFASIEPVKLWQFVAATCFITPKLLLYVFMGSKMAALSDGDQRDRMDTHDKIINGLFLAGSLVIAVFTSWLVYNLVQNHIRHLHGVDPETDELAAEAIEDFDEDAPLLSPTASHRV | Golgi membrane protein involved in vesicular trafficking and spindle migration. | A8NX72 |
Q5L8Y2 | TRMB_BACFN | tRNA(m7G46)-methyltransferase | Bacteroides | MGKNKLEKFADMASYPHVFEYPYSAVDNVPFDMKGKWHKEFFKNDNPIVLELGCGRGEYTVGLGRMFPDKNFIAVDIKGARMWTGATESFQTGMKNVAFLRTNIEIIDRFFAEGEVSEIWLTFSDPQMKKATKRLTSTYFMERYRKFLVSNGIIHLKTDSNFMFTYTKYMIEENGLPVEFITEDLYHSDLVDDILGIKTYYEQQWLDRGLSIKYIKFLLPQEGELREPDIEIELDSYRSYNRSKRSGLQTSK | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q5L8Y2 |
Q08AM6 | VAC14_HUMAN | Tax1-binding protein 2 | Homo | MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVREFVAQNNTVQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESNKFDLVSFIPLLRERIYSNNQYARQFIISWILVLESVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDELDELRPGQRQAEPTPDDALPKQEGTASGGPDGSCDSSFSSGISVFTAASTERAPVTLHLDGIVQVLNCHLSDTAIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVILKDLEVLAEIASSPAGQTDDPGPLDGPDLQASHSELQVPTPGRAGLLNTSGTKGLECSPSTPTMNSYFYKFMINLLKRFSSERKLLEVRGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHALNTILLTSTELFQLRNQLKDLKTLESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLAEVDKLVQLIECPIFTYLRLQLLDVKNNPYLIKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDSLKAAPKSQKADSPSIDYAELLQHFEKVQNKHLEVRHQRSGRGDHLDRRVVL | 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. | Q08AM6 |
Q1LTT4 | TPIS_BAUCH | Triose-phosphate isomerase | Candidatus Baumannia | MRHPLVIGNWKLNGSKHMVSNFIISLRNQLSNMINCCNVAIAPPMIYLDRAKSYLTGSHIALGAQNVDLHVSGAFTGEISAKMLKDIGAKYIIIGHIERRLYHKESNEDIANKFACLKNEGLIPVLCIGETKEENEKDQTKAICVRQLDYILNIVGTQAFKNAVIAYEPIWAIATGKSANPLQIQKIHKFIRSYLFNHDQAIAEQVIIQYGGSVNASNAAELFNQPDVDGALVGGASLKADIFATIIKAAARAKKN | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q1LTT4 |
Q0SZ02 | XERC_SHIF8 | Tyrosine recombinase XerC | Shigella | MTDLHTDVERYLRYLSVERQLSPITLLNYQRQLEAIINFASENGLQSWQQCDAAMVRNFAVRSRHKGLGAASLALRLSALRSFFDWLVSQNELKANPAKGVSAPKAPRHLPKNIDVDDMNRLLDIDINDPLAVRDRAMLEVMYGAGLRLSELVGLDIKHLDLESGEVWVMGKGSKERRLPIGRNAVAWIEHWLDLRDLFGSEDDALFLSKLGKRISARNVQKRFAEWGIKQGLNNHVHPHKLRHSFATHMLESSGDLRGVQELLGHANLSTTQIYTHLDFQHLASVYDAAHPRAKRGK | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifically exchanges the top DNA strands. | Q0SZ02 |
Q836A6 | TAGU_ENTFA | Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU | Enterococcus | MSKGKKIFAIIFGIILVLFLAVVGMGAKLYWDVSKSMDKTYETVERSKKSQVNLNNKEPFSVLLLGIDTGDDGRVEQGRSDTTIVATVNPRDKQTTLVSLARDTYVDIPGQGKQDKLNHAYAFGGASLAMDTVENYLNIPINHYVSINMAGLKELVNAVGGIEVNNNLTFSQDGYDFTIGKISLDGEQALSYSRMRYEDPNGDYGRQERQRKVIEGIVQKVLSLNSVSNYQEILTAVSDNMKTDLSFDDMKKIALDYRSAFGKVKQDQLQGTGFMQDGVSYQRVDEQELTRVQQELKNQLNTK | May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG). | Q836A6 |
Q9UKN8 | TF3C4_HUMAN | Transcription factor IIIC subunit delta | Homo | MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKLQYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKVGSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRCLLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQRRHSMQTPVRMEWSGICTTQQVKHNNECRDVGSVLLAVLFENGNIAVWQFQLPFVGKESISSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPVILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWCLLLISKAGLNVHNSHVTGLHSLPIVSMTADKQNGTVYTCSSDGKVRQLIPIFTDVALKFEHQLIKLSDVFGSVRTHGIAVSPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLIDLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPTHEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAGGREPMEEKLLEIQGKIEAVEMHLTREHMKRVLGEVYLHTWITENTSIPTRGLCNFLMSDEEYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSCQSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF | Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box. | Q9UKN8 |
A5UZ98 | YBEY_ROSS1 | Endoribonuclease YbeY | Roseiflexus | MSDSERTVDIQVVPPYAAYVDSALIEQAVECTLQMEQVAGPVEVGILITDDAGLQRLNQAYRGVDAPTDVLSFAEADDDSAFVRPPDAPRYLGDIAISWERVVAQAAEYGHSRERELAFLVVHGMLHLLGYDHERSPADEADMRAREEEILRALGLSREE | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A5UZ98 |
Q8K9C3 | TYSY_BUCAP | Thymidylate synthase | Buchnera | MKQYLDLIKKIIKNGNSKKDRTGTGTLSIFGHHMKFDLKKGFPLITTKKCHIPSIIHELLWFLRGETNIKYLNENKISIWDNWADKFGDLGPIYGKQWRSWDTSNGKKIDQIKNVLKQIKEDPDSRRILVSSWNVGEIDKMSLAPCHILFQFYVLKKKLSCQLYQRSCDVFLGLPFNIASYAILIHMIAQQCNLQVGEFLWTGGDVHLYKNHVELAKKQILRIPKKLPELIILKKPQSLFQYSFEDFKIVGYKPYSLIKGKISV | 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. | Q8K9C3 |
Q62522 | ZPBP1_MOUSE | Sp38 | Mus | MEALAPGRAPRGRRRAGASGSVLSPLSLAAVLLCALLRAPPAVGHLARLPRSIHLTQDSLKIVGSTHFPVSVYVMLHQKSPHVLCVTQRLRNTELVDPSFQWHGPKGKLVSENTTAQVTSTGSLIFQSFEETMSGVYTCFLEYKPTVEESIKNLQLKYIVYAYREPRFYYQFTARYHAAPCNSIYNISFEKKLLQILSKLVLDLSCEISLIKSECHRVKMQRAGLQNELFFTFSVASIDTEKGSKPCTDHSCEASKRLSKAKNLIERFFIQQVEVLGKRAEPLPEIYYIEGTLQMVWVNRCFPGYGINVLKHPKCPECCVVCSPGSFNPRDGTHCLQCNNSLVYGAKTCM | Plays a role in acrosome compaction and sperm morphogenesis. Is implicated in sperm-oocyte interaction during fertilization. | Q62522 |
Q2PGY1 | XYNA_PENCI | 1,4-beta-D-xylan xylanohydrolase A | Penicillium | MPSLTSLFSFFALASGAFSATADLSKRESYTSSSTGTSNGYYYSFWTDGQGDITYSNGAAGEYSVTWSGDGNFVAGKGWNPGGSREVTFKGSYNPNGNSYLSVYGWTQNPLIEFYIVEDFGTYNPSSGATKKGTVTSDGSVYDIYTSERVNQPSIEGTATFTQYWSVRQNKRSEGTVTTGNHFNAWKNLGMDLGSFNYMIVATEGYYSSGSADITVS | 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. | Q2PGY1 |
Q2SIX0 | Y2614_HAHCH | Nucleoid-associated protein HCH_02614 | Hahella | MIKGNMGDLMKQAQKIQEQMQKAQEELANAEVSGESGGGLIKIVMNGRHDVKKVEIDASLMQEEKEILEDLLAAAVNDAVRKVEKNNQDKMSNMTAGLGIPPNFKMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q2SIX0 |
A0KY89 | TOLB_SHESA | Tol-Pal system protein TolB | Shewanella | MKILAKWLALAVLLCTMPAKAALDIVITEGVDAARPIAVMPFQWQGAGAPPQAIADVVMSDLIRSGTFKPLDELGLPQRGIGALAQFDASAWANVGAEAVVVGSVKPYGTDQFLVSFDLIDLVKAQNQALKGPTSATEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHTQKAAYSLMIADYDGYNEQMLLRSPEPLMSPSWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPTFSPDGKSLAVTLSKDGQPEIYVIDIATKAAKRITNHYSIDTEPSWYPDGKSLLFTSERGGRPQLYRVDLNSGKVTRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLSTRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPVGQGEVKSPSWSPFL | 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. | A0KY89 |
Q9HCK0 | ZBT26_HUMAN | Zinc finger protein Bioref | Homo | MSERSDLLHFKFENYGDSMLQKMNKLREENKFCDVTVLIDDIEVQGHKIVFAAGSPFLRDQFLLNDSREVKISILQSSEVGRQLLLSCYSGVLEFPEMELVNYLTAASFLQMSHIVERCTQALWKFIKPKQPMDSKEGCEPQSASPQSKEQQGDARGSPKQDSPCIHPSEDSMDMEDSDIQIVKVESIGDVSEVRSKKDQNQFISSEPTALHSSEPQHSLINSTVENRVSEIEQNHLHNYALSYTGSDNIIMASKDVFGPNIRGVDKGLQWHHQCPKCTRVFRHLENYANHLKMHKLFMCLLCGKTFTQKGNLHRHMRVHAGIKPFQCKICGKTFSQKCSLQDHLNLHSGDKPHKCNYCDMVFAHKPVLRKHLKQLHGKNSFDNANERNVQDLTVDFDSFACTTVTDSKGCQPQPDATQVLDAGKLAQAVLNLRNDSTCVN | May be involved in transcriptional regulation. | Q9HCK0 |
A7MHI5 | YEGS_CROS8 | Probable lipid kinase YegS-like | Cronobacter | MSRSAGSFLILNGKSADNEILRGSVKLLRDQGHPIEVRVTWEKGDAARYVSEAADQGAQTVIAAGGDGTINEVAAALAGVTQEKRPALGLLPLGTANDFATSAAVPDDIELALKLAIEGRAVPIDIAHVNDKTWFINMATGGFGTRITTETPERLKAALGGVSYLIHGLMRMDALKADRCEIRGENFHWQGDALVIGIGNGRQAGGGQELCPEALINDGLLHLRIFTGEELLPALFTTLTQPEESPNIIDGASPWFEITAPHEITFNLDGEPLSGQHFRIVVEPGALQCRLPPDCPLLK | Probably phosphorylates lipids; the in vivo substrate is unknown. | A7MHI5 |
B2A2P2 | TRMD_NATTJ | tRNA [GM37] methyltransferase | Natranaerobius | MHIDIMTLFPEMFHGVLESSIIGRALAREMITVNLIDIREFSTNKHRKVDDYPYGGGAGMVMKPEPIFYAMDELKKSPSFNVNQKTVFVTPQGNPYSQEKAKELSSLNRLTILCGHYEGVDERVRQHLVDEEISVGDYVLTGGELPAMVILDSVTRLVPGVLGDESSAKTDSFNNYLLEHPQYTRPAIFRGLEVPEILMSGDHKRIATWKTKESLKRTLSRRPDLLDKKSLTEEEYKLMREILKESPNKELDLDRL | Specifically methylates guanosine-37 in various tRNAs. | B2A2P2 |
C1EVE6 | THIE_BACC3 | Thiamine-phosphate pyrophosphorylase | Bacillus cereus group | MSRISKEEMSKLLSVYFIMGSNNCTKDPLQVLREALEGGITIFQFREKGEGALTGEERICFAKELQAICKEYGVPFIVNDDVELALELDADGVHVGQDDEGITSVREKMGDKIVGVSTHTIEEARWAIENGADYLGVGPIFPTSTKKDTKAVQGTKGLAHFREQGITIPIVGIGGISIENTASVIEAGADGVSVISAISLAESSYESTKKLVEEVSRSL | 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). | C1EVE6 |
P21980 | TGM2_HUMAN | Transglutaminase-2 | Homo | MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA | Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity. | P21980 |
Q484F1 | TORD_COLP3 | Chaperone protein TorD | Colwellia | MSHVSQETAQEISEEREARAIVYNFLSSLFAKEVTSDLVAQLTSAQGQSFLKSLALDPSLSASVNEINTKLVKLNSKESLLELAADFCGLFLVDGRTSVSPYAGQYLSVEQGGEPSEKLSNAAINESGSKSKKNKAQLFGELHQQMTEFLTDNKLQIHSDFPEPGDHIAVILAYIAHLCVTSGSEQQLNFINSYLMTWLSDFTQQVNKHDHGQFYCFVADLTFEWLKVDTEFLLSD | Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. | Q484F1 |
Q9RK00 | XYLB_STRCO | Xylulose kinase | Streptomyces albidoflavus group | MSAAEGPLVVGVDTSTQSTKALVVDAATGRVVASGQAPHTVSSGTGRESDPRQWWDALGEALSQCGEAAREAAAVSVGGQQHGLVTLDARGEPVRPALLWNDVRSAPQARRLIDELGGAKAWAERTGSVPSASFTVTKWAWLTEHEPEAARAVKAVRLPHDYLTERLTGEGTTDRGDVSGTGWWASGTEAYDEEILARVALDPALLPRVVRPGEVAGTVRDGHGLPFSKGTLVAAGTGDNAAAALGLGLRPGVPVMSLGTSGTAYAVSQRRPADPTGTVAGFADARGDWLPLACTLNCTLAVDRVASLLGLDREAVEPGTDVTLLPFLDGERTPNLPHSSGLLHGLRHDTTAGQLLQAAYDGAVHSLLGALDLVLDADADPSAPLLLIGGGARGTAWQQTVRRLSGRPVQIPEARELVALGAAAQAAGLLTGEDAAAVARRWNTAAGPVLDAVERDEATLNRITGVLSDAAPLLERDAASR | Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. | Q9RK00 |
Q255E4 | TAL_CHLFF | Transaldolase | Chlamydia | MSSQFEQLKLLSVLVCDTGDPELVKSSGSQDATTNPSLILKVAQEPKYQEMLTEAIAWGIRQNGDDVQTLTFVLDKIQVNFGLEILKCIPGRVSLEIDARLSFNTEAMVQRAIFLSELFVASGGDKKRLLVKIPGTWEGIQAVEILEKQGISCNVTLIFNLIQAIAAAKAKATLISPFVGRIYDWWIAAYGDEGYSIDTDPGVASVSNIYTYYKKFDIPTQIMAASFRSKEQVLALAGCDLLTVSPKLLDELKKDQSSVTKKLDVAEAKKLDVQPVELTESVFRFLMNEDAMATEKLAEGIRIFSGDTQILEAAVTEFIKQIAAQDA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q255E4 |
H9JD76 | TDRKH_BOMMO | Partner of PIWIs protein | Bombyx | MSLNTKLALPIALGLSLVTVTAFVAYYVLKRDEEENDNKTVKITKINTIEIHVPKSIVPALIGRNGSNIKDLQKKSGAQIHFKKFTDQDYDVCVVRGRADTTQLAETLIHDFIKQQPTIMSESITVPSWSCGRIIGSGGENVNDISHRSGARVKVESPKSTDKVAEHLVTFRGTKEQIEVAKKLVENCVSLERCRREIEQSKRPPRHSSSPPSPCPSPGDRDADADAQGDVDHTRVKYKRPETTGPSIEVYVSAVSSPSRFWVQFVGPQVAQLDDLVAHMTEYYSKKENREAHTLRHVSVGQVVAAVFRHDGRWYRARVHDIRPNEFDSSQQVADVFYLDYGDSEYVATHELCELRADLLRLRFQAMECFLAGVRPASGEEAVSPSGQTWDKWHPQAVERFEELTQVARWKALVSRTCTYKKTATAEGEKDKEIPGIKLFDVTDEGELDVGAVLVAEGWAVAGPAPSPRPSPPRGHTTPFGDLSKSKVLSMTGGGGRSSSVPKDHKDDGSNVLTVEGDDSKDKDGITASKSLASGLEKSDRHPLSISNFDLSYPDPSRNKQLNGSDDFLHGERQNIDNEITIDTLVPPSPLSNAPILSKTLQDEFKANMNRIDSHHSNLENLGKSAFEK | Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity . The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins (Siwi or Ago3) and govern the methylation and subsequent repression of transposons . Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs: acts by recruiting the exonuclease PNLDC1/trimmer to Siwi-bound pre-piRNAs . | H9JD76 |
Q65TC8 | TRUA_MANSM | tRNA-uridine isomerase I | Basfia | MKIALGIEYNGKNYFGWQRQEKVHSVQAELEKALSFVANEKIEVFCAGRTDSGVHGTGQVVHFETNAIRPEKAWAFGTNANLPDDIAVRWAKEVPDDFHARFSATARRYRYVLYCNKLRSAILPYGITHTHLDLDEHKMQEAGRFLLGENDFSSFRAAQCQSNTPWRNIHHLNVIRRGNFVIVDIKANAFVHHMVRNIVGSLMEVGCGNQPPEWIEWLLAQKNRKLAAPTAKAEGLYLVQVTYPEHFELPQMPLGPLFLADEL | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q65TC8 |
A4IRL4 | ZAPA_GEOTN | Z ring-associated protein ZapA | Geobacillus | MTDEPKTRVSVRIYGQDYTIVGTESPAHIRLVAAFVDDKMHEFSERNPVLDVPKLAVLTAVNIANEYLKLKEEYDRLAAKLRREKGGEDDD | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. | A4IRL4 |
Q9SF16 | TCPH_ARATH | Chaperonin CCT7 | Arabidopsis | MASMMQPQIILLKEGTDTSQGKAQLVSNINACTAVGDVVRTTLGPRGMDKLIHDDKGSVTISNDGATIMKLLDIVHPAAKILVDIAKSQDSEVGDGTTTVVLLAAEFLKEAKPFIEDGVHAQNLIRSYRTASTLAIAKVKELAVSIEGKSVEEKKGLLAKCAATTLSSKLIGGEKEFFATMVVDAVMAIGNDDRLNLIGIKKVPGGNMRDSFLVDGVAFKKTFSYAGFEQQPKKFLNPKILLLNIELELKSEKENAEIRLSDPSQYQSIVDAEWNIIYDKLDKCVESGAKVVLSRLAIGDLATQYFADRDIFCAGRVAEEDLNRVAAAAGGTVQTSVNNIIDEVLGTCEIFEEKQVGGERFNIFSGCPSGRTATIVLRGGADQFIEEAERSLHDAIMIVRRAVKNSTVVPGGGAIDMEISKYLRQHSRTIAGKSQLFINSYAKALEVIPRQLCDNAGFDATDVLNKLRQKHAMQSGEGASYGVDINTGGIADSFANFVWEPAVVKINAINAATEAACLILSVDETVKNPKSESAQGDAAGAMGRGRGGGRGRGMRRR | Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Q9SF16 |
P84788 | VSP1_PROEL | Snake venom serine protease | Protobothrops | VIGGDECNINEHPFLVLVYYDDYQCGGTLINEEWVLTAAHCNGKNMEIYLGVHSKKVPNKDVQRRVPKEKFFCDSSKTYTKWNKDIMLIRLDRPVRKSAHIAPLSLPSSPPSVGSVCRVMGWGTITSPQETYPDVPHCAKINLLDYSECRAAYPGLPPKSRTLCAGVLEGGKDTCGGDSGGPLICNGQFQGIVSWGGDPCAQPHEPGSYTNVFDHLDWIKGIIAGNTDATCPL | Thrombin-like snake venom serine protease that clots rabbit fibrinogen. Only the beta chain of fibrinogen (FGB) is cleaved, releasing fibrinopeptide B. Incubation with human fibrinogen alpha and beta resulted in cleavage of both fibrinogen chains but generated neither fibrinopeptide A nor fibrinopeptide B. Promotes clotting of rabbit fibrinogen, but not bovine or human fibrinogen. | P84788 |
Q3AE33 | THIC_CARHZ | Thiamine biosynthesis protein ThiC | Carboxydothermus | MTQLLKAKEGVITREMEVVAAEERKSPEEIRQKVALGEVVIPANVNHQNLHPKGIGAGLKVKVNANLGTSENRCFYEDELKKVKVAIKAGADAIMDLSTGGNLDEIRRAIIKESSVPVGTVPLYQAAAETLNKYGDISRLDPELLFDVIEKQAADGVDFMTVHVGVTREILKVLDRFPRVTEVVSRGGSLTIAWMEKNGRENPLYEQFDRLLAICRKYDVTLSLGDGLRPGSIADATDQLQIMELMKLGELVKYAQNQGVQVMVEGPGHVPINQIEMNVKLMKRLCANAPFYVLGPLVTDIAPGYDHITAAIGGAWAAYFGADFLCYVTPAEHLGLPTVEDVEEGVIALKIAAHAADLARGNREAWNRDYEMSVARKELNWERQFELAINPERARKMRIERGSQDIKSCSMCGELCAMKIMNERGGKNA | 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. | Q3AE33 |
A9KZW9 | TRUB_SHEB9 | tRNA-uridine isomerase | Shewanella | MARRPKGRFIDGIVLLDKSTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPVCLGEGTKFSQHLLDADKRYLVTAKLGERTDTSDSDGEVVQTRAIDFTEAQLLTALDFFRGETQQVPSMYSALKYQGQPLYKYAREGIEVPRESRPITVFELNFIGLEGDELTLDIHCSKGTYIRTIIDDLGEMLGCGAHVIMLRRTQVAQYPYARMVSLEQLEALVAQAHEQQIDPSVLLDPLLLPMDTAVADFPEVNVPDAIAPYLMQGQAVRVPVNADLKTDELVRITLGDIRRFVGIGTMNEDGLLAPKRLIVIHDEPAETD | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A9KZW9 |
Q9D6J3 | YJU2_MOUSE | Coiled-coil domain-containing protein 94 | Mus | MSERKVLNKYYPPDFDPSKIPKLKLPKDRQYVVRLMAPFNMRCKTCGEYIYKGKKFNARKETVQNEAYLGLPIFRFYIKCTRCLAEITFKTDPENTDYTMEHGATRNFQAEKLLEEEEKRVQKEREDEELNNPMKVLENRTKDSKLEMEVLENLQELKDLNQRQAHVDFEAMLRQHRMSQEQWQQQQEEEDERETAALLEEARHRRLLEDSESEDEAPPSRPRAAARPNPTAILNEVPQTKRKAEALCSKAQLAGLVVPKKVKTEANGASEQVGVPTAAGAPKSRKADNPTPQTPGTSSLSQLGAYGDSEDSDS | Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates. May protect cells from TP53-dependent apoptosis upon dsDNA break damage through association with PRP19-CD5L complex. | Q9D6J3 |
A4XCT1 | TILS_SALTO | tRNA(Ile)-lysidine synthetase | Salinispora | MAALAPPVAAIRRAIRHALIELPDPGPVLVACSGGADSLALAAATAFVAPRLGRSAGLVTVDHGLQEGSAQRAAAVADWARATGLAPVEVVRVDVSGRPGGPEAAARQARYRALTEVAGGLGAAALLTGHTRDDQAETVLLALARGAGPRGLAGMPARRWLGAALLLRPLLEVSREQTRAACTALGLDPWVDPHNADPAYARARVRAEVLPALVRALGPAVVDNLARTARLVAVDTAALDEQASTALDGVRHPDGGLSVGGLAALVPAVRGRVLHAWARELGARPAALSHRHVGALEALVTGWRGQGAAHLPGGLRVLRRAGRLTAIDPGAQV | 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. | A4XCT1 |
Q0W5V8 | TATC_METAR | Sec-independent protein translocase protein TatC | Methanocella | MAAESSLPPGDMEMSLSEHLRELRNRLIIVIAVTLLLMLAIFPFSAGLVDAVLAHAVPSYVKITTYAPMEMFKARLTMCFIGAITVGFPLLVYEAFRFAAPGLYPHEKRFLYLVFPFSLLLFVAGGLVAYFVTLPLFFSIVIGHGLEVAAPALSVGETFSIVTNFVAGLGLVFQVPLIIVLAIKMGLVKRETLVKGRLGVYGLLFGVAMFFSPDPTLFSQLIVLAVLAILFEVSMVLTRFL | 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. | Q0W5V8 |
A4T7D6 | URED_MYCGI | Urease accessory protein UreD | Mycolicibacterium | MTAPTIQPGELGIEVVADSAGRTRTASLRQRYPQRVTMPLHCDPDRPGAVTLCVQSPSGGTFSDDELRTTVACRAGSHLHLTTQSATQVFAGDGAGARHHLDFTVDRGAALEYYPGTVIPHTDSTFTQTIEVNVETGGLYLGWEAVAAGRLAHGERYGYHTYDSAILARVDGRAVARDRQVIRPGTDAMSLLEGDYLATLLVVAPGADIEALLRRLRATLDDGSGVSGGAGRLPAHAGVFLRLIAQRAPDLHRARTDLFAAARRELLPGKDES | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A4T7D6 |
A6VMS2 | TORD_ACTSZ | Chaperone protein TorD | Actinobacillus | MIALEKDEKLLILNWLRNLLARELSDEQLQTLQAVEFSQFFAFLAEIGFEKQSSALQQEIQKIALFQHPRLELAADFTQCFLLEGKVSALPYASAYLDGQSLKQNLAKMDRYLEHFQLQINRQTNEPSDHLVVYLEVLIKLLEQNKTTEAKEFIQQQLLTWFPQFAAKTEKTNIRTNFYPILVKLLFAVLQNF | Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. | A6VMS2 |
Q5XGW0 | VATG3_XENLA | V-type proton ATPase subunit G 3 | Xenopus | MASQSQGIQQLLQAEKRAKDKLEEAKKRKNKRLRQAKEEATADIDQYRLKREADFRRIQTSVMGSQGNLAVKIEEQTVEKIQFYSSSYNKYKEGVLKELLDLAYNIKPELHTNYKYKI | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. | Q5XGW0 |
Q6BTZ4 | VAC8_DEBHA | Vacuolar protein 8 | Debaryomyces | MGACCSCLCSRNRDSKYPPLLLAENEREAISALLQYLENRSDVDFFSNGPLRALSTLVYSENIDLQRSAALAFAEITEKDVREVNRDVLEPILILLQSADSEVQRAACGALGNLAVNNENKILIVEMGGLEPLIRQMMSTNIEVQCNAVGCITNLATQDDNKTKIAKSGALIPLAKLAKSKDIRVQRNATGALLNMTHSGENRQELVNAGAVPVLVSLLSNEDADVQYYCTTALSNIAVDEMNRKKLSTTEPKLVSQLVNLMDSPSPRVQCQATLALRNLASDSGYQVEIVRAGGLPHLVQLLTCNHQPLVLAAVACIRNISIHPLNEALIIDAGFLKPLVGLLDFNDSEEIQCHAVSTLRNLAASSERNRLALLAAGAVDKCKELVLKVPLSVQSEISACFAILALADDLKPKLYESHIIDVLIPLTFSENGEVCGNSAAALANLCSRVSSEHKQYIFKNWSEPNEGIYGFLLRFLQSGSATFEHIALWTILQLLESNNTEINSLIKENESILSGIKNLSASQQQTQQSQVNNPDSSDQFDDPKVELFNLTQQILQILG | Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. | Q6BTZ4 |
B0RCR5 | YBEY_CLAMS | Endoribonuclease YbeY | Clavibacter | MSIEINNESAVEVDEPLIQRLATYALDTLHVHPDAELAIVMVDEGAMEQLHVQWMDEPGPTDVLSFPMDELRPGTEDRPTPAGLLGDIVVCPQVAAEQAVTAGHSTMEEILLLTAHGILHLLGFDHAEPDEEREMFGLQRDILIGFAMSERGR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B0RCR5 |
Q941V3 | YSL18_ORYSJ | Protein YELLOW STRIPE LIKE 18 | Oryza sativa | MESVGDPRDGPSTERAFEGQPVPPWTEQVTLRAVVASVALGVALSSVMMNLVFTSGIIPSLNISAGLLGFFLLKAWTRLLDQLGSPGRPFTRQENAVVQTCVVACASMTYSGGFGSYLLAMDRKTAEKTSTGDDSSASVSEPEFGRMMAFFFLVSFVGLLAIVPMRKTMIIRHRLTFPSGSATAHLINSFHTPHGARQAKRQVSLVLRSSLASLFWSIFQWFYTGGPNCGFTSFPTFGLSAFNRGFYISLNGTYVGIGMISPHLINVSMLFGSIISWGIMRPYIRSKRGIWYDADLQETNLKSFSGYKVFCAIAMILGDGIFQLVAISLRTIHTVRHHQVAAETLRSFSDVDAMPRPVMSFDDRRRTQVFLREHIPSTFAISGYVVLATVSTVVIPLMYGQVRYYHVAAAYAFAPVLAFCNAYGTGVAETNFSAQYNKLVILMFASWIGIKNGGIVGSLVICGIVSSIVSTASDFMSDFKTSYLTLTSPRATLVSQVIGTAMGCVVNPAVFTVFHHFYEMNPNKTYQAPLAKIYRGIAVLGAGGLELPKYCLAISATFFVLALAVCAMREVAAHGKWRAEPYIPSVTGMAVSFLLVPAVSIDMCIGSLIVFLWNRNDKLGSQVFGPVLASGLICGDGLFSIPYALLARYDVTPPICIRFLGRVQNDKLDAFLASKAKAG | May be involved in the transport of nicotianamine-chelated metals. | Q941V3 |
Q6H3Z6 | YSL2_ORYSJ | Protein YELLOW STRIPE LIKE 2 | Oryza sativa | MEAAAPEIERCDAGDVESDHDGAAAAAERVPPWREQVTARGMVAALLIGFVYTVIIMKLALTTGIIPTLNVSAALLAFLALRGWTRAPALLLPGGGAASSSSRRRPFTRQENTVVQTCAVACYTMGFGGGFGSSLLALNRKTYELAGVSTPGNSPGSYKEPGVGWMTGFLFAISFVGLLNLLPLRKALIIDYKLTYPSGTATAVLINGFHTPQGENSAKKQVRGFLNCFGISLLWSFFQWFYTGGESCGFLQFPTFGLKAWKQTFYFDFSLTYVGAGMICSHLVNLSALFGAILSWGIMWPLISIQKGKWYPGNVPESSMTSLFGYKSFMCVALIMGDGLYHFIKVTGITAKSLHERSNRRHAKKATDEDTFVIADMQRDEFFNKDYIPNWLAYAGYALLSIVAVIAIPIMFQQVKWYYVVVAFVLAPVLGFSNAYGTGLTDMNMSYNYGKIALFIFAAWGGRDNGVIAGLVGCGIVKQLVQVSADLMHDFKTGHLTLTSPRSMLVGQAIGTAMGCIIAPLTFLLFYKAFDIGNPDGYWKAPYALIFRNMAILGVEGFSALPKHCLELSAGFFAFSVLINLMRDFLPRKYRDYVPLPTAMAVPFLVGANFAIDMCVGSLIVFAWHKINSKESALLVPAVASGFICGDGIWMFPSSLLSLAKVKPPICMKFTPGS | Involved in the phloem transport of iron and manganese and their translocation into the grain. Transports iron- and manganese-nicotianamine chelates, but not iron-phytosiderophore. | Q6H3Z6 |
Q086H0 | TRUB_SHEFN | tRNA-uridine isomerase | Shewanella | MARRPKGRFIDGIVLLDKDTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDSDKRYLVTAKLGQRTDTSDSDGEVVQTRPVNVTQALLDEKLAFFRGTTQQIPSMYSALKYQGQPLYKYAREGIEVPRESRPITVFELNFIKLEGDELTLDIHCSKGTYIRTIIDDLGEMLGCGAHVVMLRRTQVAEYPYEKMVTLAQLEALLEQAHRQDVAPQTLMDPLLLPMDTAVAKFAEINLPEAMLYYVMQGQAIQAAGLKPDELVRITIGDERRFVGMGIMNDDGLLAPKRLIVIHDNDAAE | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q086H0 |
Q9Z0R7 | TS1R2_RAT | Sweet taste receptor T1R2 | Rattus | MGPQARTLCLLSLLLHVLPKPGKLVENSDFHLAGDYLLGGLFTLHANVKSISHLSYLQVPKCNEFTMKVLGYNLMQAMRFAVEEINNCSSLLPGVLLGYEMVDVCYLSNNIHPGLYFLAQDDDLLPILKDYSQYMPHVVAVIGPDNSESAITVSNILSHFLIPQITYSAISDKLRDKRHFPSMLRTVPSATHHIEAMVQLMVHFQWNWIVVLVSDDDYGRENSHLLSQRLTKTSDICIAFQEVLPIPESSQVMRSEEQRQLDNILDKLRRTSARVVVVFSPELSLYSFFHEVLRWNFTGFVWIASESWAIDPVLHNLTELRHTGTFLGVTIQRVSIPGFSQFRVRRDKPGYPVPNTTNLRTTCNQDCDACLNTTKSFNNILILSGERVVYSVYSAVYAVAHALHRLLGCNRVRCTKQKVYPWQLLREIWHVNFTLLGNRLFFDQQGDMPMLLDIIQWQWDLSQNPFQSIASYSPTSKRLTYINNVSWYTPNNTVPVSMCSKSCQPGQMKKSVGLHPCCFECLDCMPGTYLNRSADEFNCLSCPGSMWSYKNDITCFQRRPTFLEWHEVPTIVVAILAALGFFSTLAILFIFWRHFQTPMVRSAGGPMCFLMLVPLLLAFGMVPVYVGPPTVFSCFCRQAFFTVCFSICLSCITVRSFQIVCVFKMARRLPSAYSFWMRYHGPYVFVAFITAIKVALVVGNMLATTINPIGRTDPDDPNIMILSCHPNYRNGLLFNTSMDLLLSVLGFSFAYMGKELPTNYNEAKFITLSMTFSFTSSISLCTFMSVHDGVLVTIMDLLVTVLNFLAIGLGYFGPKCYMILFYPERNTSAYFNSMIQGYTMRKS | Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. | Q9Z0R7 |
Q0I5H8 | TRUD_HAES1 | tRNA-uridine isomerase D | Histophilus | MNELTYLQTMPKQTALLKTHCADFVVKEQLGYEMSGDGEFVAVKVRKTDCNTLFVAEKLAHFAGIPAKNMGYAGLKDRKAITEQWFCLQMPGQPTPDFNQFQLDGVEILEVTRHNRKIRTGSLDGNHFEILLREAQENADLKVRLENIKKNGFPNYFTEQRFGRDGHNLTQALRWAKGEINVKDRKKRSFYLSAARSEIFNLIVSARIRQGLHHKILVNDILQLSGSHSWFHADQKEDFNLLQQRLAQQDIQITAPLIGENVQIASDVENEIIAKHQELLYLMHQEKMKSARRPILMQAQHLSWSFIPEGLKLTFYLPAGSYATALVRELVNINE | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q0I5H8 |
B4JIY0 | UBA5_DROGR | Ubiquitin-like modifier-activating enzyme 5 | Hawaiian Drosophila | MSAAIDELQAIIAELKSELEEQKTTTRNARERIERMSAEVVDSNPYSRLMALQRMNIVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVCIETHNYNITTVDNFDQFLSTISASGIAVGQPVDLVLSCVDNFEARMAINAACNEKNMNWFESGVSENAVSGHIQFVRPGDTACFACAPPLVVAENIDERTLKREGVCAASLPTTMGITASLLVQNALKYLLNFGEVSDYLGYNALSDFFPKMTLRPNTQCDDRNCLVRQKEFHLRPKPVEKLVEVEVSDEPLHACNDWGIELVADNVPTTTTKSPENTNVAFGLRLAYEAPDKSEKSETTATAGDGVSEASLEELMAQMKSM | E1-like enzyme which activates UFM1. | B4JIY0 |
P55471 | Y4HA_SINFN | Putative ionic transporter y4hA | Sinorhizobium | MKSRLQVRSAHVPLWSWIIPLFGCVIAAMTLAHVLPERSVVLLLMSAGLLTGAVFASVHHAEILAARVGQPSGAILLAVCVTIIEVAIIGSLMLSGAEGNEEVARDTVFAAVMIVLNGVIGLCLVLGGRRHREQSFQLNAASAALAVLGTLATLSLVLPNFVTAGKPQQFAAIQLVVIGLVSVVLYGVFLFVQTVRHRDYFIDDEDAASPPATHETPRNPLAAGALLVLALIAVILLAMLLSYPLDSAVEALGLPQAVVGVTIAGVVLLPEGITSVKAALMNRLQNSINLVLGSALASIGVTIPVVAAISVALGRDLALGLAPQNLIMLILTLFVGTITLGTGRTTVLQGAVHLAIFTVFLLLSAIP | Possible cation transporter. | P55471 |
Q09064 | UREE_HELPY | Urease accessory protein UreE | Helicobacter | MIIERLVGNLRDLNPLDFSVDHVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAVNILDSEVIHIQAKSVAEVAKICYEIGNRHAALYYGESQFEFKTPFEKPTLALLEKLGVQNRVLSSKLDSKERLTVSMPHSEPNFKVSLASDFKVVVK | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q09064 |
Q6ZN06 | ZN813_HUMAN | Zinc finger protein 813 | Homo | MALPQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMMKEFSSTAQGNREVIHTGTLQRHESHHTGDFRFQEIDKDIHNLEFQWQEDERNSHEAPMTEIKKLTGSADRYDQRHAGNKPIKDQLGSSFHSHLPELHMFQTQGKIGNQVEKSINDASSISTSQRISCRPKTHISNNYGNNFRNSSLLTQKQEVHMREKSFQCNESGKAFNYSSLLRKHQIIHLGEKQYKCDVCGKVFNRKRNLVCHRRCHTGEKPYRCNECGKTFSQTYSLTCHRRLHTGEKPYKCEECDKAFSFKSNLKRHRRIHAGEKPYKCNECGKTFSQTSSLTCHRRLHTGEKPFKCNECGKTFSRKSSLTCHHRLHTGEKPYKCNECGKTFSQELTLKCHRRLHTGEKPYKCNECGKVFNKKANLARHHRLHSGEKPYKCTECVKTFSRNSALVIHKAIHIGEKRYKCNECGKTFSRISALVIHTAIHTGEKPYKCNECGKGFNRKTHLACHHRLHTGEKPYKCNECGKVFNRKTHLAHHHRLHTGDKPYKCNECGKVFNQKAHLARHHRLHTGEKPYKCNECGKVFNQKANLARHHRLHTGEKPYKFNECGKAFN | May be involved in transcriptional regulation. | Q6ZN06 |
P05470 | YKP4_KLULA | Plasmid pGKL-2 protein 4 | Kluyveromyces | MVLKRVRCYYLIITIRLKMKVFTNKNLSIEQYGFINTFPNQNYILSYLHPYNPYSSLIVCYDVGLGKTYAAACLAHMYLDSGFKVLYLSNSLNSIDNFSNEYEKVVLDSRLNSLKKNITIKSFSKFYNCEKRGESDNVDYGLIILDEVHNLRESAYRYKLIKNKLDTMNNSKILVITATPMIDSKDELDSILSLTKETSRIIFSENKIDIKISYVGQEINGETLFLSEMKGQQLKEYLKVVNEENDTVYSSSRQASISLSNKFNPSIPLDEQSSKINAFINSIKEGELTVLFSFYVKRGIDFTSSVLESIGYKKWNSNKKQKRTYAVIDGRTNKKNVEEILTSFNSIANIKGDNIHILLGSSVLSESITLYRVKHLHIISPFWNYGQIKQSIGRAIRIGSHEGLEDKSMKVYLHAAHYDKEGKDIDIWKIAYDKNKDIIKRLEELKIDNEFSNDSLLDIPKIDNEMVIKINEWVWDFRNCFDTNKFKISWCKIYEDKAIGYNLENNTKIMGNIPSYIRINRPIPGGYTIWRSCIDKKLRISFIDGEVNKFSKRGKLISNVNTSEIAKDLNCENNIESIINTLKEQNRYFDKQIEYDL | The presence of the two linear plasmids, termed pGKL1 and pGKL2, in strains of Kluyveromyces lactis confers the killer phenotype to the host cell, by promoting the secretion of a toxin able to inhibit the growth of sensitive strains. | P05470 |
B7MU99 | TRPA_ECO81 | Tryptophan synthase alpha chain | Escherichia | MERYESLFTQLKERKEGAFIPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEVLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAECEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKAFVQPMKAATRS | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B7MU99 |
A8YUE4 | TPIS_LACH4 | Triose-phosphate isomerase | Lactobacillus | MSRTPIIAGNWKLHMNPEQTAEFVDAVKDKLPDPSKVESLICAPAVDLDALRKAAKGSNLHIGAENCYFEDEGAYTGETSPKVLKEMGIDYVIIGHSERRGYFHETDEDINKKAKAIFANGLKPIICCGESLETREANKQEDWVVGQIKAALDGLTAEQVSNLVIAYEPIWAIGTGKTASSDQAEEMCKTIRETVKDLYNEETAENVRIQYGGSVKPANVKELMSKPDIDGGLVGGASLKPESYLELVNYQD | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A8YUE4 |
Q9YAD3 | TRM56_AERPE | tRNA ribose 2'-O-methyltransferase aTrm56 | Aeropyrum | MKPGGPYGDVYVLRLGHRPERDKRVTTHVALVARAFGANGFVLEGVCDEGVVESVRRVVARWGGPFTVECGVSGRRYVRMWREGGGEVVHLTMYGVNVDDVAPVIAASPRRKLVVVGAEKVERFYYEEADWNVSVGTQPHSEVAALALFLDRLFRGEWRFIDYSGGFLRVMESQRGKRVERKG | Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs. | Q9YAD3 |
Q5RBK9 | TPC2L_PONAB | Trafficking protein particle complex subunit 2-like protein | Pongo | MAVCIAVIAKENYPLYIRSTPTENKLKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDNMVTSMMIQVC | May play a role in vesicular transport from endoplasmic reticulum to Golgi. | Q5RBK9 |
Q642B2 | ZN672_RAT | Zinc finger protein 672 | Rattus | MFTAPGVAATRERPYSCSVCGKSFQYSAVLLRHERAHGGDKRFRCLECGERCARASDLRVHRWTHAGQTLYICSECGQSFSHSSLLDLHLGTHRRRSSTCPCRLCGRRFPHVSALLLHRVRQHPPEKPHRCPLCARSFRQSALPFHLARAHPPETTIATAPAPSTLYHCTQCPRAFHSSAGLRNHSRIHVVPSLSDPGAEAHRCGVCGKSFSKSSTLTRHLQRHSGEKPFKCPECGKGFLESATLVRHQRTHTGEKPYACNDCGRCFSESSTLLRHQRSHQGERPHICATCGKGFGQRYDLVVHQRSHTGERPFPCPECGRGFTDRSDLTKHLRTHTGEKPYHCELCGKRFTCISNLNVHLRNHAGHKPHKCPECGKSFSVASKLALHRKTHLGERTAECTECGKFFSHGRSLSQHQRSHRRARAAAMAATTTTTVVTEMTIGPSLTLTGPTEQEKSGLLVSTFQETC | May be involved in transcriptional regulation. | Q642B2 |
Q7NJH7 | UVRB_GLOVI | Excinuclease ABC subunit B | Gloeobacter | MTDDRFVVSAPYRPTGDQPRAIAQLSAGALGGVTFQTLLGATGTGKTFTIANVIEKVGKPTLVLAHNKTLAAQLCNELREFFPDNAVEYFVSYYDYYQPEAYIPQTDTYIEKSASINDEIDMLRHSATRSLFERRDVIVVASVSCIYGLGMPEEYLRAAIPLKVGSNIDQRELLRQLVTVQYERNDIDLGRGRFRVRGDVVEIGPAYEDRIIRVEFFGDEVEAVRWLDPVTGEVVRSVNSLNIYPAKHFVTPEEQLEQACIAIEQELEARVAELEGENKLLEAQRIKQRTRYDLEMLREVGYCNGVENYSRHLAARRPGEAPSCLIDYFPQDWLLVVDESHVTIPQIRGMYNGDAQRKKVLIDHGFRLPSAADNRPLKAPEFWDKVRQAIFVSATPGDWEVELSGGGRDPETGRMAGEHVAEQIIRPTGVLDPEVFVRPVAGQVDDLLHEIHDRVARRERVLVTTLTKRMAEDLTEYFQERGVKVRYLHSEIQAIERIEILQALRQGDFDVLIGVNLLREGLDLPEVSLVAILDADKEGFLRAERSLIQTIGRAARHVRGQVIMYADRLTASMDKAISETERRRQIQRAYNAAHGLTPQPIVKRLDANSILDYLAVSRRLNQQELEAAAAAPAEVALADIPELVSQLEIQMRDAAKKLEFEKAAEYRDKIHKLRERLLGK | 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. | Q7NJH7 |
B2KA63 | UNG_YERPB | Uracil-DNA glycosylase | Yersinia | MSPSLTWHDVIGQEKEQPYFKDTLAYVAAERRAGKTIYPPQKDIFNAFRLTELDQVKVVILGQDPYHGPNQAHGLSFSVLPGVPAPPSLGNIYKELVTDIPGFQRPNHGFLQSWAEQGVLLLNTVLTVEAGKAHSHANLGWETFTDRVIAALNEHREGVIFMLWGSHAQKKGRIINTERHYILKAPHPSPLSAHRGFLGCKHFSQANQLLQQQNQQPIDWQPKLPAVE | 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. | B2KA63 |
Q9JKT2 | TR119_MOUSE | Taste receptor type 2 member 19 | Mus | MMEGHMLFFLLVVVVQFLTGVLANGLIVVVNAIDLIMWKKMAPLDLLLFCLATSRIILQLCILFAQLGLSCLVRHTLFADNVTFVYIINELSLWFATWLGVFYCAKIATIPHPLFLWLKMRISRLVPWLILASVVYVTVTTFIHSRETSELPKQIFISFFSKNTTRVRPAHATLLSVFVFGLTLPFLIFTVAVLLLLSSLWNHSRQMRTMVGTREPSRHALVSAMLSILSFLILYLSHDMVAVLICTQGLHFGSRTFAFCLLVIGMYPSLHSIVLILGNPKLKRNAKTFIVHCKCCHCARAWVTSRNPRLSDLPVPATHHSANKTSCSEACIMPS | Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. | Q9JKT2 |
B8DB42 | TRUA_LISMH | tRNA-uridine isomerase I | Listeria | MTRYKAIISYDGSGFYGYQVQPNTRTVQAEIEKALTKMHKGKTVRITASGRTDTGVHAKGQVIHFDSELDITAEKFQKALQVMTPFDISFLTVEEVPDDFHARFGTVGKEYRYVVKRTKIFDPFSRDFALHYPYELDISKMKLASKRLIGEHDFTSFCSARTERDSKVRTLYSIDFYEEDDETLVIAFQGNGFLYNMVRILTGTLLDAGQGRISPDDISKALLARDRQKLISKTAPPQGLYLWRVDYE | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | B8DB42 |
Q7XT97 | UGT79_ORYSJ | Deoxynivalenol-UDP-glucosyltransferase | Oryza sativa | MGSMSTPAASANGGQVLLLPFPAAQGHTNPMLQFGRRLAYHGLRPTLVTTRYVLSTTPPPGDPFRVAAISDGFDDASGMAALPDPGEYLRTLEAHGARTLAELLLSEARAGRPARVLVYDPHLPWARRVARAAGVATAAFLSQPCAVDLIYGEVCARRLALPVTPTDARGLYARGVLGVELGPDDVPPFVAAPELTPAFCEQSIEQFAGLEDDDDVLVNSFSDLEPKEAAYMESTWRAKTIGPSLPSFYLDDGRLRSNTAYGFNLFRSTVPCMEWLDKQPPRSVVLVSYGTVSTFDVAKLEELGNGLCNSGKPFLWVVRSNEEHKLSVQLRKKCEKRGLIVPFCPQLEVLAHKATGCFLSHCGWNSTLEAIVNGVPLVAMPHWADQPTISKYVESLWGMGVRVQLDKSGILQREEVERCIREVMDGDRKEDYRRNATRLMKKAKESMQEGGSSDKNIAEFAAKYSN | Involved in the detoxification of the Fusarium mycotoxin deoxynivalenol by the transfer of glucose from UDP-D-glucose to the hydroxyl group at C-3, forming deoxynivalenol-3-O-beta-D-glucoside. | Q7XT97 |
A9M657 | TYSY_BRUC2 | Thymidylate synthase | Brucella | MRTYLDLLQHVLDHGVDRDDRTGTGTRSVFGYQMRFDLEEGFPVLTTKKLHLRSIIHELLWFLKGDTNIAYLKENGVTIWDEWADENGDLGPVYGYQWRSWPAPDGRHIDQIANLLKMLHTNPQSRSLIVSAWNPALVDEMALPPCHCLFQFYVANGRLSCQLYQRSADIFLGVPFNIASYALLTMMIAQVTGLKPGEFIHTLGDAHIYSNHFEQARLQLTRTPKKLPVMHINPDVKDLFAFRFEDFRLDGYEADPTIKAPIAV | 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. | A9M657 |
A0A6G9KIT6 | TX13A_MANRB | U13-myrmicitoxin-Mri1a | Manica | MKIIHVLLLVAVVAITMSPSIMAESVAEADKPGQAKKIGLFDQIDKAAAAFMKLFEG | Induces paralysis 1 hour after injection into blowflies (L.caesar) but does not appear to be lethal. | A0A6G9KIT6 |
Q84JE8 | ZDP_ARATH | DNA nick sensor protein | Arabidopsis | MITVAPFVSLRFQFPLYIINRSTLFFRERTQYLVYNTCHILRTTAKTMPVVAEYAKSNRSSCRSCSNKIAVKSLRLGLISKGRGGVDMTRWHHFDCFPTDSESIASVDDIQGLSALEKEDQDALTKLVEQCGKVPAKKPDEKKGKAKKHIMGPKGLTKAATSSKVIADNAKSSRSSCNRCSQTIVSKDLRVGLVTEDSRGFDITRWHHLGCFPIDFHPIDSVEDIGGYSSLEKGDQMELKYLAEVNKKDKTLIDDVQKMDEGDDEAIADNELTEETKKGKHSPVAKLVEQPGEPAKEDEDEESKKPASDEISEQKTKDVKNSPDSSKVISEYAKSSRSTCKKCSQTIAAKELRLGLVTRNFRGFDMKQWHHLGCFPVDSDPIVSVEDIGGFSELQSGDQDALKELVQQCGKQTLVDKMDEDNDDTEAKIKLTEETNKRKHSEVGEMVEEDESLTKAKQQMAKTHKVNMSESTSQVEVEAEITLSASDVKDKYRDANLLPKWKAFETVIFLERDDGLNDSEKIAAFDFDGCLAKTSVKIVGADAWSLMYPSIPEKLQSLHDQGYKLVIFTNESNIDRWKNKRQAAVDSKIGRLNSFIERVKVPIQVFIACGVSSSGGKGGKDDLYRKPKAGMWQLMKKHFNSGIAIDMDKSFYVGDAAGRKMDHSDADIKFAQASGLKFFTPEEYFIPSSTSPGT | Nick-sensing 3'-phosphoesterase involved in a base excision repair pathway required for active DNA demethylation. The N-terminal DNA-binding domain binds specifically to gap sites and sharply bends the target DNA. Lacks 5'-kinase activity but is capable of 3'-phosphoglycolate end processing. Inactive on 3'-alpha,beta-unsaturated aldehyde (3'-dRP). Protects partially genes from transcriptional silencing by preventing promoter DNA hypermethylation. | Q84JE8 |
O61379 | TPM_PANST | Allergen Pan s I | Panulirus | MKLEKDNAMDRADTLEQQNKEANIRAEKAEEEVHNLQKRMQQLENDLDQVQESLLKANTQLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKFVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | O61379 |
A0LIM7 | TATA_SYNFM | Sec-independent protein translocase protein TatA | Syntrophobacter | MIGGIGMPELIVILVIVLIIFGAGRLPELGAGLGKGIKNFRKATSELESAATGEKKPEELEEKK | 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. | A0LIM7 |
P42729 | TFXG_RHILT | Trifolitoxin immunity protein | Rhizobium | MNDEICLTGGGRTTVTRRGGVVYREGGPWSSTVISLLRHLEASGFAEAPSVVGTGFDERGRETLSFIEGEFVHPGPWSEEAFPQFGMMLRRLHDATASFKPPENSMWRDWFGRNLGEGQHVIGHCDTGPWNIVCRSGLPVGLIDWEVAGPVRADIELAQACWLNAQLYDDDIAERVGLGSVTMRAHQVRLLLDGYGLSRKQRGGFVDKLITFAVHDAAEQAKEAAVTPESNDAEPLWAIAWRTRSASWMLHHRQTLEAALA | Required for TFX resistance. | P42729 |
P38952 | XEN3_XENLA | Xenoxin-3 | Xenopus | LKCVNLQANGVKMTQECAKEDTKCLTLRSLKKTLKFCASDRICKTMKIASLPGEQITCCEGNMCNA | Lacks alpha-neurotoxic activity, has apparently no antibacterial activity, nor anti-coagulant potency. | P38952 |
Q7MXZ3 | YIDD_PHOLL | Putative membrane protein insertion efficiency factor | Photorhabdus | MASSLSFGSRFLIALIRGYQLVISPLLGPRCRFNPTCSQYGIEALRRFGVIKGCWLTVKRVLKCHPLHEGGDDPVPPVKNNDNREH | Could be involved in insertion of integral membrane proteins into the membrane. | Q7MXZ3 |
Q5R885 | UXS1_PONAB | UDP-glucuronate decarboxylase 1 | Pongo | MVSKALLRLVSAVNRRRMKLLLGIALLAYVASVWGNFVNMRSIQENGELKIESKIEEMVEPLREKIRDLEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARIKKGRTRHN | Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis. | Q5R885 |
Q9YFG3 | Y010_AERPE | Putative antitoxin APE_0279a.1 | Aeropyrum | MSKVIRVRYEKGVLKPLEPVNLEDGEEVDIIIRENLAELARRIRRRLSQEREEPSEILSRERSRLA | Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. | Q9YFG3 |
P0C5H6 | TUTLA_RAT | Immunoglobulin superfamily member 9A | Rattus | MIWCLRLTILSLILSQGADGRRKPEVVSVVGRAGESAVLGCDLLPPAGRPPLHVIEWLRFGFLLPIFIQFGLYSPRIDPDYVGRVRLQTGASLQIEGLRVEDQGWYECRVLFLDQHSPEQDFANGSWVHLTVNSPPQFQETPPLVLEVKELEAVTLRCVALGSPQPYVTWKFRGQDLGKGQGQVQVRNGTLWIRRVERGSAGDYTCQASSTEGSVTHTTQLLVLGPPVIVVPPNNNTVNASQDVSLACRAEAYPANLTYSWFQDRINVFHISRLQSRVRILVDGSLWLQATQPDDAGHYTCVPSNGFPHPPSASAYLTVLYPAQVTVMPPETPLPIGMRGVIRCPVRANPPLLFVTWTKDGQALQLDKFPGWSLGPEGSLVIALGNEDALGEYSCTPYNSLGTAGSSPVTRVLLKAPPAFIDQPKEEYFQEVGRDLLIPCSARGDPPPIVSWAKVGRGLQGQAQVDSNNSLILRPLTKEAHGRWECSARNAVAHVTISTNVYVLGTSPHVVTNVSVVPLPKGANVSWEPGFDGGYLQRFSVWYTPLAKRPDRAHHDWVSLAVPMGATHLLVPGLQAYTQYQFSVLAQNKLGSGPFSEIVLSIPEGLPTTPAVPRLPPTEMPPPLSPPRGLVAVRTPRGVLLHWDPPELIPERLDGYILEGRQGSQGWEILDQGVAGTEIQLLVPGLIKDVLYEFRLVAFADSYVSDPSNIANISTSGLEVYPSRTQLPGLLPQPVLAGVVGGVCFLGVAVLVSILAACLMNRRRAARRHRKRLRQDPPLIFSPRGRSGPHSAPGSDSPDSVTKFKLQGSPVPSLRQSLLWGEPARPPSPHPDSPLGRGPLPLEPICRGPDGRFVMGPTVAPPQEKLCLERSEPRTSAKRLAQSLDCSSSSPSGVPQPLCITDISPVGQPPAAMPSPLPGPGPLLQYLSLPFFREMNVDGDWPPLEEPTPASPPDFMGSHPCPTSSFLPPPDSPPTNLRAVLPGTLMGVGVSSEPPYTALADWTLRERVLPGLLSAAPRGSLTSQSSGRGSASFLRPPSTAPSAGGSYLSPAPGDTSSWASGPERWPRREHVVTVSKRRNTSVDENYEWDSEFPGDMELLETWHPGLASSRAHPELEPELGVKTPEKSCLLNTTHAPGPEARCAALREEFLAFRRRRDATRARLPVCQQSISYPEQATLL | Functions in dendrite outgrowth and synapse maturation. | P0C5H6 |
Q96GE5 | ZN799_HUMAN | Zinc finger protein 842 | Homo | MASVALEDVAVNFTREEWALLGPCQKNLYKDVMQETIRNLDCVGMKWKDQNIEDQYRYPRKNLRCRMLERFVESKDGTQCGETSSQIQDSIVTKNTLPGVGPYESRMSGEVIMGHSSLNCYIRVGAGHKPYEYHECGEKPDTHKQRGKAFSYHNSLQTHERLHTGKKPYNCKECGKSFSSLGNLQRHMAVQRGDGPYKCKLCGKAFFWPSLLHMHERTHTGEKPYECKQCSKAFSFYSSYLRHERTHTGEKLYECKQCSKAFPDYSSCLRHERTHTGKKPYTCKQCGKAFSASTSLRRHETTHTDEKPYACQQCGKAFHHLGSFQRHMVMHTRDGPHKCKICGKGFDCPSSLKSHERTHTGEKLYECKQCGKALSHSSSFRRHMTMHTGDGPHKCKICGKAFVYPSVFQRHEKTHTAEKPYKCKQCGKAYRISSSLRRHETTHTGEKPYKCKCGKAFIDFYSFQNHKTTHAGEKPYECKECGKAFSCFQYLSQHRRTHTGEKPYECNTCKKAFSHFGNLKVHERIHSGEKPYECKECGKAFSWLTCFLRHERIHMREKPYECQQCGKAFTHSRFLQGHEKTHTGENPYECKECGKAFASLSSLHRHKKTHWKKTHTGENPYGCKECGKAFASLSSLHRHKKTH | May be involved in transcriptional regulation. | Q96GE5 |
Q042F3 | TPIS_LACGA | Triose-phosphate isomerase | Lactobacillus | MRTPIIAGNWKLHMNPEQTVEFVNAVKGKLPDPSKVESVIAAPAVDLYVLKKAAEGSDLHTGAENAYFEVEGAFTGETSPKVLNEMGIDYCIIGHSERRGYFHETDEDINKKAKALFANGVTPIICCGESLETREANKQEDWVVAQIKAALDGLTAEQVSKLVIAYEPIWAIGTGKTASADQAEEMCKTIRETVKDLYNEETAENVRIQYGGSVKPANVKELMSKPDIDGGLVGGASLDPESFLALVNYQD | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q042F3 |
P0CS27 | VPS27_CRYNB | Vacuolar protein sorting-associated protein 27 | Cryptococcus neoformans species complex | MSWLWGSTTNPQFEELAEKACSPLNLPYPQSEDIATALEVADMIRSKAIQPKMAMQSLKKRIASKNGRVQMYAIGLTDTCIKNGGDHFLLEVASKEFVDELSNLIKATTTSPEVKQMLIKYFQQWALAFKSKSELSFFVEVYNELRASGITFPPPPAPVPSHLLTTTTAPAWVDSDACMRCRSAFTFTNRKHHCRNCGLVFDQACSSHSMPLPKYGITEEVRVCDGCWAKAGRNKADAPAPAVPGRTPRSRADLDADLQRAIELSLAESQHSQNRHHSHFTPSEPPLAHGTVEDEDEQMRLAIEASLRDMEARPSAPAGLGEAPEPEYRPLPTFDLSPRENETILTFSNTMDQMAAYGERDLRRFPHAHVLAEQANTVGGRLRRNVEEKSTKQQMLMEMQDKLSQAVNLYGQILDGQQAYAAKRAHEEQARRYQQQQSYYTQQYQPQPQLYGQYPPNGYQAFVPPQQAYQPPQPQPEAQAQHAPSLYPTMPYTTPNFTSPPQERVYPQQSHSSPYSQWSPAPSHVQPGLARQASVVVPPVSSPVPAGVQRQASMTYGAPIPVAEQSQRQQQQYASAPPFASGAAPVDIPSAPPPVNLSTHPNSPQRHSYIPSHPQTQTQTQYESQPQEIPSQQDMQYGASAPPPDSLGSYVSEGTVGSAKSGLEQEHAASQIQPQPQPQASAQTQTQSQSQLQAQPQQNQYAAQTQLPAGMYNAASFPQPLPPTIFPDAPVEAPKGLEKEEKEEALLIEL | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. | P0CS27 |
Q5LSP9 | UREG_RUEPO | Urease accessory protein UreG | Ruegeria | MSKMNGPLRVGIGGPVGAGKTTLTAALSEALRDSHSIGVITNDIYTREDAEALMRLQILPQDRIIGVETGGCPHTAIREDASINLAAVAEMERRHPGIEIILIESGGDNLSATFSPELADVTLYVIDVAAGEEIPRKGGPAITKSDILIINKTDLAPHVGASLEVMERDAGRMRCGRPFVFSSLRNRDGVAEIVKLLAEIAGLEIRSDLQVANLA | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | Q5LSP9 |
Q8EGH1 | UPPS_SHEON | Undecaprenyl pyrophosphate synthase | Shewanella | MSSTVEFDPQSRPTEADAYAQTSLPEVLPELVKQSLPKHVAIIMDGNGRWAQTQGKPRVMGHKAGVKAVRRAVSAASQLGIQSLTLFAFSSENWRRPDKEVSLLMELFFTVLQREIKLLDKNQVKLNIIGDISRFSARLQKQIRAAEEKTAGNSGLILNVAANYGGRWDILQAAQKLAEKVETGEMTSSQFTEEALSEHLCMQNQSEVDLIIRTGGDYRISNFVLWQAAYAELVFLDTLWPDFDEQAFHEAIATFANRQRRFGLTGSQIDEMRAL | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. | Q8EGH1 |
C4XT96 | UPPP_SOLM1 | Undecaprenyl pyrophosphate phosphatase | Solidesulfovibrio | MTESLAAVVLGIVEGATEFLPVSSTGHLILVGHLIGFTGEKADSFDVIIQLGAILAVVCLYWRRFWWLVSPKPHHAFSGIRGLWMLFLTSLPAGLIGLVARKSIKAYLFNPWSVALALSVGAVMIFLVEQRKTRDRYYSLDEMTPGLALGIGCFQCLSLWPGFSRSAATIMGGMLLGAKRSLAAEYSFIGAVPLMFAATLYDFYKSAHLFSADDLGVLGIGFVVSFVSALIAVKAFIVLVQRITLRPFAWYRLALAAAVFFFWPK | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | C4XT96 |
Q2S371 | THIG_SALRD | Thiazole synthase | Salinibacter | MSDVTHANGAVANEADDALVIGDHSFSSRILVGTSRYPNPQVMLDALEATGTELVTVAIRRVNIENPAPESHLDLLRRGGYEVLPNTAGCYTAREAVLTARLAREALGTDLLKLEVIGDDETLMPDVEQLLDAAKTLVDDGFTVLAYANDDPITCRKLADLGCAAVMPLGSPIGSGMGIVNPYNLRIIREMIEDTPLIVDAGIGTASDAVTAMELGYDGILVNTAIAQAQHPVDMGRAMRKAVEAGRSAHRAGRIPRRLYAEASSSMEGRIGT | 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. | Q2S371 |
P09860 | TNNC1_CHICK | Troponin C, slow skeletal and cardiac muscles | Gallus | MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKTEEELSDLFRMFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE | Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. | P09860 |
Q9XUK2 | ZIP3_CAEEL | BZIP transcription factor family zip-3 | Caenorhabditis | MQPSYDADDFMRRGFFGSFIGFRKRSSSKPEPPVPPKFAPPAAPSVAPNFRASDSAAPHLLSVPSNRTEYDIYREIVSEAEYIERSSPASPDFSCPTTPQPSNYYTPLPLPQQPPTFDPSTLMPQQQMMFHPGQYHMVMSPIAPHPIPVDTNGVPLGTQCPMAPPPYSSFAPQSSSSGMLQQQPQDLVIPQDIPFDVKREIQEHLVLQNGKKQMSIEEIVKLVVVALKDSQIEEGREEEESPEEILRRKRIQNNLAAARYRKRQREARESAESELGDLTRRNDELRDQVSRMEREIDRLKQAVLGRQ | Transcription factor which negatively modulates activation of the mitochondrial unfolded protein response (mtUPR) . Plays a role in response to infection by the Gram-negative bacterium P.aeruginosa . | Q9XUK2 |
Q2S6M5 | YIDC_HAHCH | Membrane protein YidC | Hahella | MDFLRTSLIVGLLVVSYLLVLEWNEDMSPQQQPVAQTPSVTIDSNGADSSALLNSPNTGELDTPETASKPATAEDSNISSTASSGKIITVITDVLRVEIDLNGGNVVEASLLQYPISLKNPTPLDLMQKNNGVYYVAASSLIGANGFDDSKNGGNPIYIAEKNSYSLQEGQDKLSVDLRTERDGVTIVKRYEFEKSSYSINVNFQINNQSDAPWKANFSAKLVRDKSPDPTFSGGFGAASFLGAVVSTPEKPYEKIDFSDMEESGPSGVKVNSSNGWIAFIQHYFVSAWIPLSNDTHTYQTRLRNGLYLMGFVDPEFTVEPGQTHNVGAKLYAGPKIMETLKEVAPNLDLTVDFGWLWLIAKPLYLVLEFIHDYVGNWGIAIILLTVLIKALFFHLSATSYRSMANMRRVTPEMQRIREQYGDDRQRMSQAMMELYKKEKINPLGGCLPMLVQMPVFISLYWVLLESVQLRQAPFFFWIQDLSIKDPYFVLPLLMGAAMFLQTSLNPTPPDPIQARVMKMMPIIFTVFFLWFPAGLVLYWLVNNILSIAQQWYITKKIENGGLAAKKIAS | 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. | Q2S6M5 |
Q13EZ9 | UBIG_RHOPS | 3-demethylubiquinone 3-O-methyltransferase | Rhodopseudomonas | MALQSESTGPVSPSVDPAEIAKFSRLSAEWWDPTGKMAPLHRINPLRISFIRDAACRKFERNAKSLSCLSGLRMLDIGCGAGLLCEPFTRLGAQVIGIDPSATNIAAAKLHADKSHLAIDYRCTTVEEIDPRERFDIVMAMEVIEHVNDVPAFLGRCAALMKPTGIMLVATLNRNWKSFALAIVGAEYVMRWLPRGTHQWDKFVTPDELEQHLQGLGLVVTEQSGLVFNPLADRWRLSPDMDVNYMVVAETAP | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q13EZ9 |
Q2K3S8 | UBIG_RHIEC | 3-demethylubiquinone 3-O-methyltransferase | Rhizobium | MTEGARSTIDQGEVNRFSAMAAEWWSPTGKFKPLHKFNPVRLGYIRDKACENFGRDPKSARPLEGLRVLDIGCGGGLLSEPVARMGASVVGADPSEKNIGIASTHAKASGVSVDYRAVTAEELAEAGETFDIVLNMEVVEHVADVELFMTTCAKMVRPGGLIFVATINRTMKAAALAIFAAENILRWLPRGTHQYEKLVRPEELEKPLAASGLEITDRTGVFFNPLSNQWKLSRDMDVNYMLLAKRPA | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q2K3S8 |
Q640J6 | WD82A_XENLA | WD repeat-containing protein 82-A | Xenopus | MKLTDGVLRSFRVAKVFRENSDKINCFDFSPTGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISASLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTSLKFSQDGKLILMSTNGGFLRLVDAFKGAVMHTFGGYNNSKAVTLEASFTPDSQFIMIGSEDGKIHVWNCESGMKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD | Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs). | Q640J6 |
B1ZNZ6 | URED_OPITP | Urease accessory protein UreD | Opitutus | MDFAGHLHLRAAPRAFGHTALTLQSFRAPFHLSKPYWDYDSRVLLVQVVNPTAGILAGDRIESEITVDAGAALLITTPSASRVFRMDAGVATCRQHFTVAAGAWLEVMPGPLVPHRGSDYRQSTIVELTRGAGGFFVDQLMPGRAAHGEAWAWRRLCLEFECRLDGRLLVRERVDQSGEELRALAELAGSGAAACFANAILIPGAEADEDWRAAVEGLHRDGAWVGVSALREAGWSIKVIAPDGAYLRETLRAIRAVLAEAFPRMRCDPRRL | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B1ZNZ6 |
Q2GGH9 | TSAD_EHRCR | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Ehrlichia | MDKLKIVLGIETSCDETAVAIVNSNKEVLSHKILSQQEHAAYGGVVPEIASRAHINYLYELVGSCIEESQLCFNDIDAIAVTAGPGLIGGLIVGIMMAKAISSVTGKPIIEINHLEAHALIIRMFYEIDFPFLLLIMSGGHCQFLVAYDVRCYYKLGSSLDDSLGEVFDKVARMLNLGYPGGPIIEEKSLLGDSGSFTLPRALTNRPGCDFSFSGLKTAVRNIIAGQKCINHELVCNISASFQDCVGDILVNRINNAIVMSKDIDHRINKLVVTGGVAANKLLRNRMSVCANDNGFEILYPPSKLCTDNGVMIGWAGIENLAKGYVSNLNFFPRARWPLENLRFDILRK | 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. | Q2GGH9 |
Q1QDK2 | TRPA_PSYCK | Tryptophan synthase alpha chain | Psychrobacter | MTRIESTFETLKAQNKKALIPYVMAGDPNPSNFVGLLHDLVKHGADMIEVGLPFSDPMADGPTVALAGERALAAGTSTRDALKMVKEFRQQDTQTPIILMGYLNPVEIIGYDNFVSLCEQSGVDGILMVDLPPAEAGSFTQHLTEHAMNEIFLLSPTTLAERRQQVLTHCGGYIYYVSLKGVTGSATLDTDDVAKQVQAIKAETDLPVCVGFGIRDATSAKAIGAHADGIIVGSALVQNFADIDANDITAVANAQQKIMAKMDELRGALDSL | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q1QDK2 |
Q8F9Q1 | TRMB_LEPIN | tRNA(m7G46)-methyltransferase | Leptospira | MVQDLEQKLWSIASGIPFSSDYFLQASPIRKLKKENLFSKVFETYFLELGSGWGEVAISMALQRPNTGFILMEKKFDRIRHTIREIEKHSLDNVKILCVNFNWFLEEVFEENLFSEILLNFPDPWPKKRHHKKRTVNSKFLESLKILLPEKGKFYFATDYGPYARKVIRLFRDSKAFSPEKVELKSERNEIPVSHFERKKREEGKRIYYIDRVLVQK | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q8F9Q1 |
P49381 | TREA_KLULA | KlNTH1 | Kluyveromyces | MDGKVNNNPPRSRHRRTSSLEEVVDPFSTPDVYYGPKSDPSKLLSKNRFTRTRTFSVAEPGGGKGHSSSYTSPYFDTTVPLRRRGSEDDSYSASQGQRRFYIEDVDKTLKELLASEDTDGNYQITIEDTGPKVIRVGTVNSNGYKHVHIRGTYMLSNLLQELTLAKLFNRKQVILDEARLNENPVNRMTRLISGQFWKSLTRRIDSNNIAKIAYDTKIDTPKAKNPRIYVPYNCQDEYQQLVQWSEMDPSLQLEVNYLPKDITPEFVKSLNDKPGLLCLAMESHMDPVTGEETWVGFPYAVPGGRFNELYGWDSYFMALGLLESNKLDVARGMVEHFIFEIDHYGKILNANRSYYLCRSQPPFLTDMALQVCRKMGGDKNPVAVDLLRRAFKAAIKEYLTVWTASPRLDEKTGLSCYHPDGIGIPPETEPGHFDSILRKYAEKYNVSIPEFRDLYNSQKVHEPDLDVFFLHDRGVRESGHDTTYRFENVCAYLATIDLNSLLYKYEVDIAYVIKKYFGDNFEGLPEGHRTSNDWEKLAEVRKERIDKYLWDEETGFYYDYNVKTEKRTSYESVTTFWALWAGMSSQEQAQRMVENALPKLEEFGGLVACTARSRGELSLDRPTRQWDYPFGWAPHQILVWDGLVRYGYENHTRRLAYRWLFLMTKAFVDYNGIVVEKYDVTRGTDPHRVDAEYGNQGADFKGVATEGFGWVNSSYLLGMKYMNNFARRALGTCVTPKVFFGRLPPKEKKKYGLE | Hydrolyzes intracellular trehalose to glucose (Probable). The disaccharide trehalose serves as a storage molecule for energy and carbohydrates that is mobilized during nutrient stress . | P49381 |
A6TCF3 | TRMJ_KLEP7 | tRNA Cm32/Um32 methyltransferase | Klebsiella | MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAQIVDTLDEALAGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEGQHAPVALVFGRERVGLTNDELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLAAQEQAQPAVEHEEAPYPLVDDLERFYDHLEQTLLATGFIRPNHPGQVMNKLRRLFTRARPESQELNILRGMLASIEQQNKGK | Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. | A6TCF3 |
P0DSJ6 | TX13A_MYRGU | U-myrmeciitoxin(01)-Mg3a | Myrmecia | MKTTVILLLAIAIIFAIMTTLTSAKNEETMEEALKGLNELKERLKKQGIDTAALNLDEKLLT | May have antimicrobial properties, like most ant linear peptides. | P0DSJ6 |
A6VD86 | THIC_PSEA7 | Thiamine biosynthesis protein ThiC | Pseudomonas | MSATQKNNITRLEQLDRQSTQPFPNSRKVYLTGSRPDIRVPVREISLADTPTAFGGEKNPPVFVYDTSGPYTDPEVRIDLRKGLPDVRSRWIDERGDTEILPGLTSEFGQARLADASLDALRFAHVRTPRRAKPGANVSQMHYAKKGIITPEMEYIAIRENMKLQEARAAGLLDQQHPGHSFGANIPKEITPEFVREEVARGRAIIPANINHTELEPMIIGRNFLVKINGNIGNSALGSSIEEEVEKLTWGIRWGADTVMDLSTGKHIHETREWILRNSPVPIGTVPIYQALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFEEICEIMKAYDVSFSLGDGLRPGSVADANDAAQFGELETLGELTKIAWKHDVQVMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARAFHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVRDYAKENGLSDESKAIEAGFQEQAARFKDEGSVIYKQV | 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. | A6VD86 |
B5EHR5 | TRMFO_CITBB | Folate-dependent tRNA(M-5-U54)-methyltransferase | Citrifermentans | MTQEITVIGGGLAGCEAAWQAAKRGVKVRLFEMKPNCYSEAHHLPGLSELVCSNSLRGDSLENAVGLLKEELRRLQSLFMEGAEATKVPAGGALAVDRDLFSQYITSRIESHPLIEVVREEVTRIPEEGIVVLASGPLTSGLLAEEIGRLAGSYLYFYDAIAPIVAADSIDYDKAFRASRYGKGDGDDYLNCPMDEEQYQAFVREIVAAEKVEPKSFEKVVHFEGCMPIEEMASRGPETLRFGPMKPVGLVDPRVGVEPHAVIQLRQENREATMYNLVGFQTKLTWPEQKRIFRMIPGLENAQFLRLGSMHRNTFINAPELLMATCQLKSDQRIFFAGQITGVEGYVESASSGFVAGVNAARLAQGEGLVVPPAETAIGALARHITNTEAGHFQPMNVNYGLFPSLPGRVKKKEKRGLLAQRGLETLEKWLPELS | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | B5EHR5 |
G3Y419 | YANA_ASPNA | Yanuthone D biosynthesis cluster protein A | Aspergillus subgen. Circumdati | MSASRSSTKFSTPAEGSDNGKEFTTPATSTEGHEVPDRPGDALADVAIIGMACRTPGDVRSPDSLWQYLLKKGDASGSLPDWRWEPYRQRHPRNAALLAQTTAKGYFLDDIDHFDAAFFSISPREAEQMDPQQRLALEVAWEALENAGISPPQLAGSNTSVYMGVNSDDYAKLLLEDLPNVDAHMGVGTAYCGIPSRISYILDLMGPSVALDAACASSLVAVHHARQAIRAGETDLAIAGGVNALLGPGLTRVLDEAGAISTDGKCRSFDETASGYGRGEGAGVVILKRLDKALADGDHVLAVLKGSAVASDGKTLGIMAPNARAQLLVAQKALAEAKVSADSINYVEAHATSTSLGDPTETNALAEVYGAGSGRSPSDPCYIGSIKPNIGHLEAGAGVMGLIKAVLVLRHGQVPPQANLKTLNSKIAWNENLLCPPRELVTLPCPGPIHPLRAAVASYGYSGTVSHAVLEAFAGHSEFAERLSQIPTGDDPSPVLLLISAPQARRVSAAAGALKQWLSENEASISLKTVSSTLAQRRAHHRYRHAIVADSVPDAIAALDDVSKEAPNRWVIKDKIDSKAAKGPVWIFSGHGAQWADMGRELFESSPAFEEVVRNLEPIIQDEVGFSAIETLQKGCPDRSDVVQVMTFLMHLGIAAVLEIESGPPSAVVGHSLGEAAAAVVSGALTWREGALVVCRRARLYRELMGQGAMALVRVSAEEARTRIGRQTGVWVAIETSPSACVLSGEVDAIKQLSDRWREEGIEVRMVASDVPFHTPMLERLAKPLYESLRGELHPRVPNRALFSTSQPDPRSEVLRDAQYWVTNMIQPVRLQSAIAAIAQDGFRALVEVSSHPIVTHSVVETMGECTEDPVLVTPTMVRRQPALKSILAATGRLHCFGCAIKFIELDPNAPWNSSVPSTVWHHQPFYRAVSQTSASSQLETTHDPAANNLLGKRIALWGTEEVLYQTRLEEENRPFPGHHPLHGSEIVPAAVLLRTFLQALTPRCVEQVSLQVPVVVSPARKVQIRHNTRNITITSCLEESSSQEDGSWLVNTTAAVGAANVVPSQSRMDLSELRKRLPQKLADSFSIDYLASVGVSAMGFPWQVTHHVASDDEMLARVDANPDNMGGMNDFLTSLMDAATSISSTLWHRQPLLRMPTSVRRVVAVHEIPIPRVVYIHCTKVASTSECTADVTLTGEDGTVLMEIQGMSFAGLEGESFSRKSTAGLVHQIQWPPAALVEDPSEFSHIAFVTPDITDPRLEQYQSQLDALAITSSVHQAASDLPLTSHTSLAVVYLPQTMTDVFDTATRSCNDLVSIIQTITAAASSTTRVFVLTAGTELGHSALLGLSRIIQAEHPDIWGSLIEVEDTFSLPLMAMRYVRDADVIRIKDGVPRIARLRPLPSASSSLTPLTFSPASTYLITGGLGALGLSVAHWMVTQGARRLLLLSRRALPPRSTWSSTHMNNPTIQSILALERLGATVHCLPIDISLPMAASGLRSTLETLNLPSVAGVIHAAGIVSDQLVEQVTPDVLESVLAPKIKGALNLHDVFPPASLDFFVLFSSCGQLLGFPGQASYASGNAFLDGLARSRRAQGDNAISLLWTTWRGMGMGQSANGAMEAELYARGITDITPDEAFRAWSAVASTGGGGTDHAVIVRARVLEGGEPLPHPILTDIATRKAEVVNAGEHPAGSQEVKLSGRELEQHLRDVINGCVSKTLSVKEDEIDDAVALAEMGMDSVMTVNFRMTLQQTLKVPVGPTLIWKCPTVQHLVKHFTKELDA | Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria . The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA . 6-MSA is then converted to m-cresol by the decarboxylase yanB . The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol . Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A . The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A . O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E . Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D . Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E . | G3Y419 |
Q5JQD7 | YSL12_ORYSJ | Protein YELLOW STRIPE LIKE 12 | Oryza sativa | MASHANASGGGGDEEMVEASTLRHRHGAGKDANGVGTERQLAAAAAEGEEEGPSSVERAFVDRAVPSWREQLTVRAFVVSFFLSIMFSIIVMKLNLTTGIIPSLNVSAGLLGFFFVRLWTAAIERVGLLRQPFTRQENTVIQTCVVAAYGIAFSGGFGTYLFGMSETIAKQATEANNAQNVKNPHIGWMIGFLFLVSFIGLLALVPLRKIMIVDYKLTYPSGTATAYLINGFHTPEGAKLAKKQVKELGKFFLFSFVWGFFQWFYTAGDGCGFQSFPTLGLQAYKNRFYFDFSPTYVGVGMICPHIVNVSVLLGGILSWGIMWPLIRNKKGSWYAASLSETSLHGLQGYRVFISIALILGDGLYNFVKVLIRTTAGFVVMMKKNSTLPVSNNGSPMVATEAISFDDERRTELFLKDQIPKTVAFGGYVAVAAVSIGTLPQIFPQLKWYYILVAYVFAPVLAFCNAYGAGLTDWSLASTYGKLAIFIFGAWAGASNGGVLVGLAACGVMMSIVSTASDLMQDFKTGYLTLASPRSMFVSQVIGTAMGCVIAPCVFWLFYKAFADIGVSGTEYPAPYAIVYRNMAILGVDGFSSLPKHCLTLCYIFFAAAIAINLARDLAPSKVARFIPLPMAMAIPFYIGSYFAIDMFIGTVILFVWEMVNKAKAEAFAPAVASGLICGDGIWTLPQSILALAKVKPPICMKFLSRSVNAQVDGFLGN | May be involved in the transport of nicotianamine-chelated metals. | Q5JQD7 |
G0LES5 | TRI5_TRIAR | Trichothecene biosynthesis protein 5 | Trichoderma | MVELNDVPGEEEFPRATYLETMVRLLDTVSYNDENFTDEERVECLKYAYGKAAEHFAQPHVQETLKVPPKRMAAALKTIVGMCVYSWCRVSKEVMADLSIHYTYTLLLDDSREEPAGTMATWYEDLLNARPQAHGWWRLVNDFIPNVLRHYGGYCQMNMVRSTIDFFQGCWIEQHNFKGFRGSSDYPGFLRRINGLGHCVGSSIWPIELVDEEEHFLEITTAIAQMENWMVWTNDLFSFYKEYFAERDQTSLVNNYVECEGITLDQALDKLCKDTIRSSEEIIQVFHDKDPKMYEILTRFIQGYITWHLCDDRYRLVEVYEAAGDDPVAQKFKKYAESARRVGAIDPARYCVPSVTELCEREMAKQSAGRSWDFGLGKIANKISSVAQ | Trichodiene synthase; part of the gene cluster that mediates the production of the antimicrobial trichothecene harzianum A (HA) that plays a role in Botrytis cinerea antagonistic activity and plant defense priming . The biosynthesis of harzianum A begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 . Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichodiol . Isotrichodiol then undergoes a non-enzymatic isomerization and cyclization to form 12,13-epoxytrichothec-9-ene (EPT) which is further converted to trichodermol by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation . The last step of HA synthesis is esterification of an octatriendioyl moiety to the C-4 oxygen of trichodermol. The octatriendioyl moiety is probably produced by the polyketide synthase TRI17 and the esterification performed by the trichothecene O-acetyltransferase TRI3 (Probable). | G0LES5 |
A4WAG4 | TAM_ENT38 | Trans-aconitate 2-methyltransferase | Enterobacter | MADWNPSLYLQYGAERTRPAAELLARIALDDVSDLLDLGCGPGNSTALLLKRWPLARITGVDNSPAMLEQARVAVPECRFIEADVRQFKPEHAVDLIYANASLQWVPDHYALLPHLISLLKLNGVLAVQMPDNVDEPSHVLMREVAYEQGYPNRAREPLPGIHAYYDILTETGCDVDIWRTTYYHKMSSHQAIIDWVSATGLRPWMQELSEHEQLKFLERYHELLVQQYPIQENGQILLAFPRLFFVARREP | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | A4WAG4 |
Q8KE85 | Y805_CHLTE | Nucleoid-associated protein CT0805 | Chlorobaculum | MAMPNFGDMMKQLQEAGAKMQDLQKQLEKLVSEGEAGGGMVRAKVNGRQKLLELTIDPEIMDDVDMVQDLVVAAVNKALEASAQLAQSEIQKAAGGMINPADLMKQFGGQG | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q8KE85 |
Q9CZR3 | TM40L_MOUSE | Protein TOMM40-like | Mus | MGNTLGLAPMGTLPRRSHRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTVHMSALGLPGYHLHTAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSITHRLVLGGELVYHRRPGEEGAILTLAGKYSAVHWVATLNVGSGGAHASYYHKANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQADMVFRGLVDSNWCVGAVLEKKMRPLPVTLALGAFLNHWRNRFHCGFSITVG | Potential channel-forming protein implicated in import of protein precursors into mitochondria. | Q9CZR3 |
A5CXC5 | TATA_VESOH | Sec-independent protein translocase protein TatA | Candidatus Vesicomyosocius | MMPGPFELIIILVIVLLLFGGKRLKDIGGDLGNAIKGFKKAMKESTDSINNKDDIVEAKIIKKEIKQEK | 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. | A5CXC5 |
B3NZ68 | WRNXO_DROER | Werner Syndrome-like exonuclease | Sophophora | MEKYLIKMPIKSKASEVPKDKAVVKQGTPKIRSKVTKNDTPKELKNKENAGEDNTPKQTNGRLGRPAGKRKNLDTPETKAEKIATEEENPPKRRSSRLTRSTRSMAEDGSPSPEKEKPEKLPFIKYKGAIKYYTESQDIAASADDVLQWVEKQKDEVVPMAFDMEWPFSFQTGPGKSAVIQICVDEKCCYIYQLTNLKKLPAVLVALINHSKVRLHGVNIKNDFRKLARDFPEVSAEPLIEKCVDLGVWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELERREKAKIINEEEFKEKNGEAAFKAMKTLGETFLSKINEVTL | Has exonuclease activity on both single-stranded and duplex templates bearing overhangs, but not blunt ended duplex DNA, and cleaves in a 3'-5' direction. Essential for the formation of DNA replication focal centers. Has an important role in maintaining genome stability. | B3NZ68 |