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
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|---|---|---|---|---|---|---|
Q837R9 | UVRB_ENTFA | Excinuclease ABC subunit B | Enterococcus | MIERETSNTFHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVSLRVGMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAIFPATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPYTLLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQTETVVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEIHERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRAMDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSYKDLSRQEKADLLMKLEREMKDAAKALDFETAATLRDTILELKAAK | 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. | Q837R9 |
Q925I4 | TS1R2_MOUSE | Sweet taste receptor T1R2 | Mus | MGPQARTLHLLFLLLHALPKPVMLVGNSDFHLAGDYLLGGLFTLHANVKSVSHLSYLQVPKCNEYNMKVLGYNLMQAMRFAVEEINNCSSLLPGVLLGYEMVDVCYLSNNIQPGLYFLSQIDDFLPILKDYSQYRPQVVAVIGPDNSESAITVSNILSYFLVPQVTYSAITDKLRDKRRFPAMLRTVPSATHHIEAMVQLMVHFQWNWIVVLVSDDDYGRENSHLLSQRLTNTGDICIAFQEVLPVPEPNQAVRPEEQDQLDNILDKLRRTSARVVVIFSPELSLHNFFREVLRWNFTGFVWIASESWAIDPVLHNLTELRHTGTFLGVTIQRVSIPGFSQFRVRHDKPEYPMPNETSLRTTCNQDCDACMNITESFNNVLMLSGERVVYSVYSAVYAVAHTLHRLLHCNQVRCTKQIVYPWQLLREIWHVNFTLLGNQLFFDEQGDMPMLLDIIQWQWGLSQNPFQSIASYSPTETRLTYISNVSWYTPNNTVPISMCSKSCQPGQMKKPIGLHPCCFECVDCPPGTYLNRSVDEFNCLSCPGSMWSYKNNIACFKRRLAFLEWHEVPTIVVTILAALGFISTLAILLIFWRHFQTPMVRSAGGPMCFLMLVPLLLAFGMVPVYVGPPTVFSCFCRQAFFTVCFSVCLSCITVRSFQIVCVFKMARRLPSAYGFWMRYHGPYVFVAFITAVKVALVAGNMLATTINPIGRTDPDDPNIIILSCHPNYRNGLLFNTSMDLLLSVLGFSFAYVGKELPTNYNEAKFITLSMTFSFTSSISLCTFMSVHDGVLVTIMDLLVTVLNFLAIGLGYFGPKCYMILFYPERNTSAYFNSMIQGYTMRKS | Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. | Q925I4 |
Q0SSM0 | THIG_CLOPS | Thiazole synthase | Clostridium | MDKLIIGGVEIKNRLFVGSGKYPSNEIIKDVLEGSGSQVITLALRRVDLDNKEEDILQNIPKDVILLPNTSGATNAEEAIRIARIARAMGCGNWIKIEVISDSKYLLPDNEETIKATKVLADEGFIVLPYMCPDLYAGRRLIEAGAAAVMPLGAPIGSNRGLKTKELIQIMIDELDIPIIVDAGIGKPSQAMEAMEMGAAACLVNTAIASSEDPINMARAFKMAVEGGRLAYEAKMGRESKFGNASSPLTGFLD | 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. | Q0SSM0 |
P56158 | TBXT_HALRO | Protein T | Halocynthia | MSITNNMESPSDSEVRLTLNDRALWTKFCSLTNEMIVTKSGRRMFPVLKLTASGLEPNSMYSFLLDFAPADSNRWKYVNGEWVPGGKPEPHAASCVYVHPDSPNFGSHWMKQPVSFNKVKLTNKGNGGGQQIMLNSLHKYEPRIHVVKVGGEAASERTIATFSFPESQFIAVTAYQNEEVTSLKIKHNPFAKAFLDAKERPDQTDFHSLAGIPVSSPQVPSWYGRNGSTSSARHFTHCNSYGGESELTSVQDTAIPSYTSRNCMRNSYRGNARATPYTIPHKELTCQATSFPEPVPNDGFYPMFPNSELLPRTTLNNYSPAMGAYTNSSIVTSSDIQSGNNNNFFYSNNNNINTTDEVPTTYMTNDFNSFYNQSSNSGMPGTTYLPYQSSPVNQFYSYQPPYSTEIADISPTQQDIINAQNPYQTAWTPPLSYDGCSTMYNSITPYSSSGESTTSEMTLLATARYLQNLRL | Involved in the transcriptional regulation of genes required for mesoderm differentiation. | P56158 |
Q5ZLD7 | VPS53_CHICK | Vacuolar protein sorting-associated protein 53 homolog | Gallus | MEEDELELAAGLEAALELAPAVQAAIEQVFPSQDPLDRADFNAVEYINTLFPTEQSLANIDEVVNKIRLKIRKLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVVNVLEHFNKYMGIPQIRQLSERVKAAQNELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANVLDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWIKRQLVDYEEKYGRMFPQEWCMTERIAVEFCHVTRTELAKIMRTRAKEIEVKLLLFAIQRTTNFEGLLAKRFSGCTLADGTVKKPEAPPPSTNPFLEDETGTETDEIVIEKSDADKPKKPKVPDNPFHGIVSKCFEPHLYVYIESQDKNLSELIDRFVADFKAQGPPKPNVDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTTSSSGGLTITSLLKEKEGSEVAKFTLEELCLICSILSTAEYCLATTQQLEEKLKEKVDASLVERINLTGETDTFSIVISNSIQLLVQDLDAACDPALTAMSKMQWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCIKFANSFIPKFINHLFKCKPISMVGAEQLLLDTHSLKMVLLDLPSIGSQVVRKAPASYTRIVVKGMTRAEMILKVVMAPHEPPVVFVDNYIKLLADCSTDTFQKILDMKGLKRSEQSSMLELFRQRLPAPPSGVENSGSLSLSAPTPEQESSRIRKLEKLIKKRL | Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). Acts as component of the EARP complex that is involved in endocytic recycling. | Q5ZLD7 |
Q6GFZ4 | TPX_STAAR | Thioredoxin-dependent peroxiredoxin | Staphylococcus | MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEGIVLTISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEELRLLARAVFVLDADNKVVYKEIVSEGTDFPDFDAALAAYKNI | 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. | Q6GFZ4 |
P28109 | WNT5A_ANSCE | Protein Wnt-5a | Anser | SGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMKLNSRGKLVQVNSRFNAPTIHDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQRERCHCKF | Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Required during embryogenesis for extension of the primary anterior-posterior axis. | P28109 |
Q5XIS7 | UBAP1_RAT | Ubiquitin-associated protein 1 | Rattus | MASKKLGTDFHGTFSYLDDVPFKIGDKFKTPAKVGLPIGFSLPDCLQVVREMQYDFSLEKKAIEWAEDIRLIQEAQQEAERKSEEAEAKVNSKSGPEGDSKVSFSKTHSPATMPPPINPILASLQHNNILTPTRVSSSATKQKVLSPPHTKADFNPADFECEEDPFDNLELKTIDEKEELRNILVGTTGPIMAQLLDSNTPRGNSGSVLQDEEVLASLEQATLDFKPLHKPNGFITLPQLGNCEKMSLSSKVSLPPIPTVSNIKSLSFPKLDSDDSSQKTVRLASTFHSTSCLRSGASRNFLKPSTQSSASELNGDHALGLSALNLNSGTEVPALTSSQMPSLSILSVCTEESSPPSTCPTVTPLNFSVSQVPTMPSCPQAYLELQALSPSERQCVETVVNMGYSYDCVLRAMKKKGENIEQILDYLFAHGQLCEKGFDPLLVEEALEMHQCSEEKMMEFLQLMSKFKEMGFELKDIKEVLLLHNNDQDNALEDLMARAEAS | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2. | Q5XIS7 |
Q5LGZ6 | TRUA_BACFN | tRNA-uridine isomerase I | Bacteroides | MSVQRYFIYLAYDGTHYHGWQIQPNGISIQECLMKALATFLRKDTEVIGAGRTDAGVHASLMVAHFDYEGEPLDVDKVAEKLNRLLPQDISVYKVCRVKPDAHARFDATARTYKYYITTVKFPFNRQYRYRIHNPLDFQKMNEAALTLFHYSDFTSFSKLHTDVKTNICKIMHAEWTQEDEYTWVFTIQADRFLRNMVRAIVGTLLEVGRGKLSVDDFRKIIEQQNRCKAGTSAPGNALFLVNVEYPQEIFE | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q5LGZ6 |
Q5HRJ7 | TARI_STAEQ | Ribitol-5-phosphate cytidylyltransferase | Staphylococcus | MIYAGILAGGIGSRMGNVPLPKQFLLLQGKPIIIHTVEKFLMYKDFDEIIIATPQKWINYMHDLLNNYRLDDKKIKVIQGGDDRNHTIMNIIESIEQHKKLNDEDIIVTHDAVRPFLTNRIIRENVEYASQYGAVDTVVNAVDTIISSNDAQFISEIPIRSEMYQGQTPQTFKIKELKDSYLSLTQSQKEILTDACKILVELGKPVKLVKGELFNIKITTPYDLKVANSIITGAVDND | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q5HRJ7 |
Q1MPX3 | YBEY_LAWIP | Endoribonuclease YbeY | Lawsonia | MAVILLGNEHIWKLPFCRLEFVAILEKMLSFAKLQTIEVYLVSDTTIAFFNLHYMNCLGITNVLSFPMDDEDLAGSIILSVDAVCRESLLYRQPILDYCLSLLSHGIAHIAGYTHGVEMDKFCSNLLLPFKLA | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q1MPX3 |
F1QX91 | ZD23B_DANRE | Zinc finger DHHC domain-containing protein 23-B | Danio | MSIMKKRSSRAADPDELLCCCEYIDRHGSRSHMVACCCDCEDLDEACDRWMNKEPQNPDSVSRALATINDRLRVPWISGARQIDVSLIPPLILLPVFLHIAALHYLLGIIMLTAMPITVLWYYFFTHRKKGRTLFFLGLALFSLFYMFYLFLTQVVPRGEVTELQLAVVTAGVALTVIFLMLTKRGPGLVRPRPSETHSTVTYHSTPPDVDGVYLNGARHQVVIGSRVASSEHTGEPGTEEEEEGVQKRNWCAVCKVVRPQRAGHCRICGVCVLRLDHHCVWINSCVGLANHRTFLLTLLFFLLTSIYGISLVLASVCPDQRVLTALFYCPDVYSQYSSALCFTCAWYSSIVTGGLLHLLLLQILNISLNVTEREARLALREKSAQRRLWGLIVHTGHYSRGFWSNWTEFLTMTEDTQPAGHKTEDLV | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes. | F1QX91 |
Q99595 | TI17A_HUMAN | Inner membrane preprotein translocase Tim17a | Homo | MEEYAREPCPWRIVDDCGGAFTMGTIGGGIFQAIKGFRNSPVGVNHRLRGSLTAIKTRAPQLGGSFAVWGGLFSMIDCSMVQVRGKEDPWNSITSGALTGAILAARNGPVAMVGSAAMGGILLALIEGAGILLTRFASAQFPNGPQFAEDPSQLPSTQLPSSPFGDYRQYQ | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. | Q99595 |
P29444 | XYLB_KLEPN | Xylulose kinase | Klebsiella | MYIGIDLGTSGVKAILLNEQGEVVASHTEKLTVSRPHPLWSEQDPEQWWLATDTAMKALGAHDSLRHVKGLGIAGQMHGATLLDKSLQVLRPAILWNDGRCAEECQLLEDKVSASRQITGNLMMPGFTAPKLLWVQRHEAAVFSQVDKVLLPKDYLRLRMTGELASDMSDAAGTMWLDVARRDWSDEMLAACDLSRDAMPALFEGSDVTGQLRPEVAQAWNMPPALVVGGGGDNAAGAVGIGMADAGQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHACRGRWHLMSVMLSAASCLDWAAKLTGLASVPALIAAAQTADESAGPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPAELARAVLEGVGYALADGMDVVHACAIKPEAITLIGGGRARYWRQMLADISGLQLDYRTGGDVGPALGAARLAHVAVHDEADRPGLLKPLPLEQAHRPDDRRVAHYAPQREIFARIFSKLKPLMS | Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. | P29444 |
G3Y416 | YANC_ASPNA | Yanuthone D biosynthesis cluster protein C | Aspergillus subgen. Circumdati | MALVHLTALAACGLLLVILRAAFNSWRLQRKLPPGPPGAPLIGNILQLPKVRAHQKFTEWARTYGGLYSFRIGPATAAVVTDRALVKELFDKRSALYSSRPTSYVGQNIITRGDHLLVMDYSDNWRLFRKAINQHFMASMCEKTHVRLLEAEHTQMMRDFLLHPEKHMLHTKRTTNSIIMSLLFGIRTPSWDTPHMQELYEIMEIWSQIMETGATPPVDIFPWLHWVPQQWLGHWVDRSQTVARGMKRLYSSFHRRAIEARRKAESTSQSRARTFLDDVLDLQEKLGLTDNQVDFLGGVMMEGGSDTGSTMLLVMIQALALHPEIQQRARAELDAVCGEHRSPTWEDFPRLPYINMIVKETMRWRPVTPLAFPHALNKDDWVNGYFLPKGTTVFLNVWGLHHDENIFPNPDQFDPSRFEGRHKLAFDYAASPDYMQRDHYIYGAGRRLCPGIHLSERSMFLGAAKLLWAFNFEPARDEDGNPIRIDTDPVTGYTEGFLVCPRPYQCNVTPRSPAHAETILREFSRAESEVLSQYAMP | Cytochrome P450 monooxygenase; 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 . YanC is also involved in the synthesis of yanuthone X1 which does not have 6-methylsalicylic acid (6-MSA) as precursor . | G3Y416 |
B5YI18 | Y235_THEYD | Nucleotide-binding protein THEYE_A0235 | Thermodesulfovibrio | MNFDKFIVIVTGLSGGGKTVTLRTLEDIGFFCVDNLPPPIVLEFLGMLNEYSSFKNIAIGIDIRVQQFLEKATELIKRIKDIYKIEVLFLEADDDTILLRYKETRRPHPLSTHYNDLHKAIKQERELLYPLRCLSDRIIDTSNLNPHELKFLIRSMYGAEKISPSITIISFGYKKGIPANADLIFDARFLPNPYFIPSLTDLNGKDKPVKDFVLKQNETIEFLTYIKNFLSFAVSGYKREGRAYVTIAIGCTGGRHRSVVLVEEIADYLRSLSLNPVVIHRDL | Displays ATPase and GTPase activities. | B5YI18 |
P29598 | UROK_RAT | Urokinase-type plasminogen activator chain B | Rattus | MRVWLASLFLCALVANSEGGSELEASDESNCGCQNGGVCVSYKYFSSIRRCSCPKKFKGEHCEIDTSKTCYHGNGQSYRGKANTDTKGRPCLAWNSPAVLQQTYNAHRSDALSLGLGKHNYCRNPDNQRRPWCYVQIGLKQFVQECMVQDCSLSKKPSSTVDQQGFQCGQKALRPRFKIVGGEFTVVENQPWFAAIYLKNKGGSPPSFKCGGSLISPCWVASATHCFVNQPKKEEYVVYLGQSKRNSYNPGEMKFEVEQLILHEDFSDETLAFHNDIALLKIRTSTGQCAQPSRTIQTICLPPRFGDAPFGSDCEITGFGQESATDYFYPKDLKMSVVKIISHEQCKQPHYYGSEINYKMLCAADPEWKTDSCSGDSGGPLICNIDGRPTLSGIVSWGSGCAEKNKPGVYTRVSYFLNWIQSHIGEENGLAF | Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. | P29598 |
B1HPX1 | TMCAL_LYSSC | tRNA(Met) cytidine acetate ligase | Lysinibacillus | MKAVGIVVEYNPFHNGHAYHLTQAKKVAKADIVIAVMSGTFLQRGEPAMVDKWTRTKMALAGGVDIVIELPYVYSTAPATDFAKGAISILTAVGCDSFAFGSEDGSIQPFLNTYDLIDNNRTEYDALIKDSLKTGASYPKSLYYAYEQLTQKFPAPYIDLAQPNNILGFHYLEAARTLDSNIKPLTIPRIAAGYHDALKQDSSIASATGIRKALASTSSLQSVQKVVPETSFDYLTDWHRHYKKFASWESFWPLLQFTIMRHTPSELTRYAEVTEGIENAIMKAAKNSSSFNSFMEKIKSKRYTWTRIQRMITHIYTGFTKEQLQSFEAPSFIRLLGMSAKGQAYLGKRKKDIELPLISRVAAANDAMLAIDIHAAELYNLSIEQGVTAQSLPKDYQTPPIRN | 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. | B1HPX1 |
Q8TE23 | TS1R2_HUMAN | Sweet taste receptor T1R2 | Homo | MGPRAKTISSLFFLLWVLAEPAENSDFYLPGDYLLGGLFSLHANMKGIVHLNFLQVPMCKEYEVKVIGYNLMQAMRFAVEEINNDSSLLPGVLLGYEIVDVCYISNNVQPVLYFLAHEDNLLPIQEDYSNYISRVVAVIGPDNSESVMTVANFLSLFLLPQITYSAISDELRDKVRFPALLRTTPSADHHIEAMVQLMLHFRWNWIIVLVSSDTYGRDNGQLLGERVARRDICIAFQETLPTLQPNQNMTSEERQRLVTIVDKLQQSTARVVVVFSPDLTLYHFFNEVLRQNFTGAVWIASESWAIDPVLHNLTELRHLGTFLGITIQSVPIPGFSEFREWGPQAGPPPLSRTSQSYTCNQECDNCLNATLSFNTILRLSGERVVYSVYSAVYAVAHALHSLLGCDKSTCTKRVVYPWQLLEEIWKVNFTLLDHQIFFDPQGDVALHLEIVQWQWDRSQNPFQSVASYYPLQRQLKNIQDISWHTINNTIPMSMCSKRCQSGQKKKPVGIHVCCFECIDCLPGTFLNHTEDEYECQACPNNEWSYQSETSCFKRQLVFLEWHEAPTIAVALLAALGFLSTLAILVIFWRHFQTPIVRSAGGPMCFLMLTLLLVAYMVVPVYVGPPKVSTCLCRQALFPLCFTICISCIAVRSFQIVCAFKMASRFPRAYSYWVRYQGPYVSMAFITVLKMVIVVIGMLATGLSPTTRTDPDDPKITIVSCNPNYRNSLLFNTSLDLLLSVVGFSFAYMGKELPTNYNEAKFITLSMTFYFTSSVSLCTFMSAYSGVLVTIVDLLVTVLNLLAISLGYFGPKCYMILFYPERNTPAYFNSMIQGYTMRRD | Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. | Q8TE23 |
Q8Y5L0 | TMCAL_LISMO | tRNA(Met) cytidine acetate ligase | Listeria | MKATGIVVEYNPFHNGHKLHLNKARELTQADVVIAVMSGSFVQRGEPAIIPKWERAKMALSAGVDMVVELPVSFATQHATIFAEEAVRILDAIHIDTLFFGSEHGVAEDFTFAAKKVVENEARFDEAIQLALVDKKTSYARAYTEAFKKLFGQNLLDITKPNNILGFHYALAVQKQNPSISLQTIPREHAGYHDEEASHDQIASATAIRKLILAGKLEEASHYLPASSIDILRNYEGPFLSWTDYWSFLQYRLIQASTEELEGIRGVSEGIQNRMQQAATKAQNFSDFIELTKTKRYSNARLQRTALQILLNAKSKASSPYIRILGMNKTGQKYLSLHKKNISLPIVTTVSKAPPGLLEEELRATNIYTLVKKLENYQAGDFHIPPILTL | 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. | Q8Y5L0 |
Q6FWS5 | YBT1_CANGA | Pleiotropic ABC efflux transporter of multiple drugs YBT1 | Nakaseomyces/Candida clade | MVVEAMSSCQFWYFDDITKYGRIEVLNNYVPTTLVTISILILLHNFFIRFYKYDIKKETPTPSLSLKLSSLNLSESDEEMPLTMHAQHNYGSHPSPSELNTDSSALYDRHFSINNIDSGEVNDPTKYHLIKRNMFEKFRVVIEFVIVAFQLLLHCYLSIEKSNLNGDLQKFHFKPHVLLWTILFTLATLRVLNLNQNNKFVNKYSGNIWLVSFANYTVIFLAHILPFRSALIGHVNDYGSSQYYKSQFWLNLVLMALLLTSPIGNNLPVLYQPQQDRAPSPEPYVSLLTFFSFHWVQPFINKAYKNNSLSHSDLWSLKLEDYSINVMKSFLEFRNRPSMRSSRFGISLLRYFLNLFMFQWCFTTISAFSIFVPTILLKKLLDFIEHKDKGSMNLAWFYVFGMFISRFIVAICDHCNLFLGRRVCVRMKSIIISEIYSKALKRKITKQSKPADENNENDMIKHDEVSPQEVNDTTHVNADEESYSSNLGSIINLMSVDAFKISELCAYLHYFLETAIMLTVSLILLYKVIGTAAFVGILITIIIIPINSKLYAVVGTLQAGNLACTDKRVEKLNESFQAIRIIKYFSWEDKFKEGIMLVREKELALLLKRCMVWCVLAFSWFITPTLITGCTFAYSILIEKKQLTTPVAFTALSLFTLLRDPLDRISDMLSYLIQSKISLDRVQRFLETEETDKYDQLTVDKNGKRLAFENVTLRWDSDKDSFVLRNLDIEFMTGKLNVIVGATGSGKTSILMGLLGEMQLSEGKIIVPSLSPRHEYQSQAGVINDSIAYCSQAAWLLNDTVRNNILFNAPFDQARYDAVVEACSLKRDFQILKAGDSTEIGEKGITLSGGQKQRVSLARALYSSAGHLLLDDCLSAVDSHTALWIYDKCISGPLMEGRTCILVTHNIALTMKNADFVVMIEDGKVKEKGTPIELLAKGLLGEDENMKKSIISRSASSASLKGKSERSLGTTPAPVEIVQDSTPVNDDGKLIEEEGKAMGFVGKEIYKWYIKMYGGWYTIVALASVFTAILCLQITQAWWIRNWTVKRFSDVDESNYNLPASTFIVESRNRVLLTNEAGKKESENQNAGIAKFLVVYCLIGVMSSIIGSIKTFVNSLFGIRASKLIFDSLLDRVLHARVRFFDSTPIGRIMNRFSKDIESIDQEIPPNIQSVFYSAIEVFATLLLISYITPAFFPVAIIIVLGYSIVGFFYLTTSRELKRLDSISKSPIFQHFSETLVGVTTIRAFGDEQRFIKENLSMIDQNSMPFFYLWVVNRWLSFRIDLIGALVIFSSGVFILLNINNIDAGLAGISLTYAISFTEAALWLVRQYSELEMNMNSVERVLEYMNIEQEPLIADPANAVTPPPQWPDSGKVEVNNLSLKYAPHLPYVIKDVTFTIEPLEKVGIVGRTGAGKSTIITALFRFLEADTGSIKLDGVNIANIDLKRLRRSITIIPQDPTLFAGSIRSNLDPYDEYSDEEIFTALKRVNLVSTEEMEASTSEIQSNSSKNVNKFLNLESEIAEGGSNFSQGQRQLMCLARSLLRMPKVILLDEATASIDYNSDAKIQETIRQEFNNSTVLTIAHRLRSIVDYDKILVMDAGEVKEFDHPYSLLLEKKSIFYNMCEDSGELDVLIDLAKKSFISRLNSDSKK | Pleiotropic ABC efflux transporter that might be involved in the resistance to azoles such as fluconazole. | Q6FWS5 |
B1W317 | TATA_STRGG | Sec-independent protein translocase protein TatA | Streptomyces | MIGNLKPLEIVLIIAVILLLFGAKKLPDMARSLGKSARILKSEAKAMKKDDAATAAPTTETVADDTVPPQSTTARTIQAAPGDVTSSRPVSEAKPTTQS | 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. | B1W317 |
Q5D7I3 | TRIM5_ERYPA | TRIM5alpha | Erythrocebus | MASGILLNVKEEVTCPICLELLTEPLSLPCGHSFCQACITANHKKSMLYKEEERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDRKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVLADFEQLREILDWEESNELQYLEKEEEDILKSLTKSETKMVRQTQYVRELISDLEHRLQGSMMELLQGVDGIIKRIENMTLKKPETFHKNQRRVFRAPALKGMLDMFRELTDVRRYWVDVTLAPNNISHVVIAEDKRQVSSRNPQIMYWAQGKLFQSLKNFNYCTGILGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDAMYDVEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIAPLSVIFCPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q5D7I3 |
Q42676 | TKTC_CRAPL | Transketolase, chloroplastic | Craterostigma | VDHYTYCILGDGCQMEGVSNEACSIAAHWGLGKLIALYDDNHISIDGDTDIAFTEDVDKRFEALGWHVIWVKNGNNGYDKIRAAIKEAQAVKDKPTMIKITTTIGFGSPNKSNSYSVHGSALGAKEVEATRQNLGWPYEPFHVPDDVKKHWSRHTPQGASLESEWNAKFAEYEKKYPEEAAELKSIITGELPLGWEKALPTYTPENPGDATRNLSQQNLNALAKVLPGLLGGSADLASSNMTLLKSSGDFQKNTPEERNVRFGVREHGMGAICNGIALHSPGLIPYCATFFVFTDYMRAAMRISALCEARVIYVMTHDSIGLGEDGPTHQPIEHLASFRAMPNILMLRPADGNETAGAYKVAVQNLKRPSVLALSRQKLPQLPGTSIEGVEKGGYVISDNSSGNKPDVILIGTGSELEIAAKAGEVLRKEGKGVRVVSFVSWELFDEQSKEYKESVLPSSVTARVSIEAGSTFGWGKIVGSKGKAIGIDRFGASAPAGKIYEEFGITVEAVVAAAKELI | Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. | Q42676 |
P18738 | ZG9_XENLA | Gastrula zinc finger protein XlCGF9.1 | Xenopus | TGEKPFICSDCGKCFNDSSILIRHMKIHTGEKPFCCPQCGRKFRRRAHLIVHERTHTGEKPFTCPECGKSFARRSHLMDHRIIHNGEKKYSCPECGKCFGLQGYLNKHFKIH | May be involved in transcriptional regulation. | P18738 |
O08781 | ZMAT3_RAT | p53-activated gene 608 protein | Rattus | MILLQQVWLPLPNRPSTSPPMSVAARSTGTLQLPPQKAFGQEASLPLAGEEDLAKRGEPDSALEELCKPLFCKLCNVTLNSAQQAQAHYQGKNHGKKLRNYYAANSCPPPARMSSVAEPVATPLVPVPPQVGSCKPGGRVILATENDYCKLCDASFSSPAVAQAHYQGKNHAKRLRLAEAQSHSFSDSAEAGQRRTRKEGSEFKMVTTRRNMYTVQSNSGPYFNARSRQRIPRDLAMCVTPSGQFYCSMCNVGAGEEVEFRQHLESKQHKSKVSEQRYRSEMENLGYVQ | Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus. | O08781 |
B2AH07 | UBIE_CUPTR | Demethylmenaquinone methyltransferase | Cupriavidus | MSETHFGFEKVDETEKAGKVAGVFHSVASKYDVMNDLMSGGMHRLWKMFTIAQAGVRPGHKVLDIAGGTGDLAKAFAKQAGPTGQVWLTDINESMLRVGRDRLLNKGIVTPVALCDAEKIPFPDNYFDLVTVAFGLRNMTHKEAALAEMRRVVKPGGKVMVLEFSKVWKPLEKAYDVYSFKVLPWLGQRVAGDAPSYRYLAESIRMHPDQVSLVRLMEHAGLENVEYFNLTAGVVALHVGRKY | 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). | B2AH07 |
A2WXU2 | ZIP4L_ORYSI | Protein ZIP4 homolog | Oryza sativa | MKISELSPEYRQPPPHAGLIADLSKAVSDVESFAASATAPEKLAADLRRILTSLASAASSSSFTESLSVQIWRLGTRLWNAVVDRANSAALAGGPAALAVEAEIRQAAPELLLLAGIPNGVPSAAAKVASFFHRSGLAWLDLGRVDLASACFEKATPLVSAAATEDRGVLLELNLARARAASDAGDQALAVALLSRSKPLAAASPEGAKSLAQGYLSIGEATLAAKHSNPAVEASTLFTEALDLCEKAASPSSSSPRTPPYGGATPKTPNLEGLKRRCLRFLALERLQAQDYEGVLRCIRVSRASMGLEEEHPSIGVMAMRAWIGSGNMAEADKELERLMANALATENLCVSAAEAYLAAAGPEAARKVLIALAARCRAGGAAAAVRVVKQVIDGGGGGIGRARAIAELVSDERVVALFDGPGNTHERGTMHALLWNCGTEHFRAKNYDTSADLIERSMLYVSRDEESRSRRADCFRVLSICHIALQHLDRALEFVNEAYKVEPNIKCAFLKVKINLQKGEEDEAFKQMKTMVGCVDFNPEFLTLTAHEAMSCKSFGVAVASLSYLLGLYSAERPMPMPEVAVLRNLIELLSREPGTEAEILKYSRRAKQRMADLGVESFFGSGIVGGRELNWFADLSWNMGLRASKEKKYNFGSEFFELAAEFFSSRNAECDENRSKVCKALIMAVTIMLNAEELNNSPLSDSDIKKGVEMLSRAGKLLPLISPSVPVASDQLEANNFLYLHTFNSYQLMGRMGTPAHPQQLQLIKNFASSKACTPANLLTLGVTASKGALPNMLAAEFSLKACITTALASQSPNYRVISCALRKLACLAGLQDLNGSKSDAAYDVFQQAYQIVVGLKEGEYPVEEGQWLVATAWNMSCLPLRLHQAKVARKWMKMGLDLARHLEGMKERIASMQTTFENLERVSGDEPDECSQEEAPKASISGSMSQPVLV | Required for crossover formation, complete synapsis of homologous chromosomes and bivalent formation during meiosis. Is specific to recombination events resulting in interference-sensitive crossovers (class I meiotic crossover) and works cooperatively with MER3 to promote crossovers. | A2WXU2 |
Q2EET0 | YPDJ_ECOLI | Protein YpdJ | Escherichia | MGYDSRLDHLAATSWYPFFNNVTTRGEIIEPYSLTLDEACQFLKIS | May be involved in H(2) production during fermentative growth. | Q2EET0 |
P37045 | TX23B_AGEAP | Omega-agatoxin-4B | Agelenopsis | MKLCMTLLITAIAVVTFVVATQEESAEFNEVEESREDNCIAEDYGKCTWGGTKCCRGRPCRCSMIGTNCECTPRLIMEGLSFA | Antagonist of voltage-gated Cav2.1/CACNA1A (P-type) calcium channels. Paralyzes insect by blocking neuromuscular transmission. | P37045 |
Q04210 | YET2_YEAST | Endoplasmic reticulum transmembrane protein 2 | Saccharomyces | MGVYLAVLFSLLVIEMAILFILVLPLPQRMRRWLYIRYSIISTNKKFRTYMVGIMIFVGLLFIDSWKRSQIRVSTYRNQKNPYIINSVTPVDALASRAYNQRNVYISGFIIYFYICILTVMSILRRIVEWNDKMKAGDDILKEKLRRKQKYLEELQKKKF | May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. | Q04210 |
A2CBJ0 | YIDD_PROM3 | Putative membrane protein insertion efficiency factor | Prochlorococcus | MRESNTLSGGIFALLNRAIGSVLLALIGFYRTWLSPLLGPHCRFIPSCSAYGLEAIQRHGPWRGGWLTLRRLSRCHPFTPCGCDPVPD | Could be involved in insertion of integral membrane proteins into the membrane. | A2CBJ0 |
Q9NSD4 | ZN275_HUMAN | Zinc finger protein 275 | Homo | MMSHPCVSLLGVPVLNPALVPHLAQGQVLLVSDPSPNTDPAKYSESTSATRHQMKGEDAQPQEMASTSFPRASGPSPEFRQHGDSDGKRGSPQNLPIEHHFACKECGDTFRLKVLLVQHQRVHSEEKGWECGDCGKVFRGVAEFNEHRKSHVAAEPQPGPSRALENAAEKREQMEREAKPFECEECGKRFKKNAGLSQHLRVHSREKPFDCEECGRSFKVNTHLFRHQKLHTSEKPFACKACSRDFLDRQELLKHQRMHTGHLPFDCDDCGKSFRGVNGLAEHQRIHSGAKPYGCPHCGKLFRRSSELTKHRRIHTGEKPYACGQCGKAFRQSSSLLEHARIHSGERPYACGECGKAFRGPSDLIKHRRIHSGLKPYECDKCGKAFRRSSGLSRHRRIHSGARRCECSQCGRVFKRRSALQKHQPTHHE | May be involved in transcriptional regulation. | Q9NSD4 |
O34753 | TAGO_BACSU | Undecaprenyl-Phosphate GlcNAc-1-phosphate transferase | Bacillus | MLDERMIRIVVAFIVSLLTVLIITPIVKRIAIKIGAVDQPSNRKVHDKIMPRMGGLAIFIGVVAGVLASGIYTETRMTAITVGAFIIIVLGILDDKYQLSAKVKFLIQLGVAIMIVSTGLKMDFFSVPFLTERFELGWMAYPLTVLWIVGITNAINLIDGLDGLAAGLSVIGLSTIAVMALSGGKVLILSLSLVVIASTLGFLFYNFHPAKIFMGDTGSLFLGYSISILSLLGLYKSVTLFSIVIPIIILGVPIFDTTFAIIRRILNKQPISAPDKSHIHHRLMAFGLSHRMSVLVIYLIGFIFSISAIVLKSATIWLSLFIIFILIIFMQIIAEVTGLVNEKFKPFTKFYKRLVKRN | Catalyzes the formation of undecaprenyl-PP-N-acetylglucosamine. Involved in the synthesis of anionic cell-wall polymers as it mediates the initiation of the linkage unit formation that appears to be common to the two types of teichoic acids attached to the peptidoglycan of B.subtilis; may also be involved in teichuronic acid biosynthesis (Probable). | O34753 |
Q09022 | XEN1_XENLA | Xenoxin-1 | Xenopus | MRYAIVFFLVCVITLGEALKCVNLQANGIKMTQECAKEDTKCLTLRSLKKTLKFCASGRTCTTMKIMSLPGEQITCCEGNMCNA | Lacks alpha-neurotoxic activity, has apparently no antibacterial activity, nor anti-coagulant potency. | Q09022 |
Q2L875 | TCTP_TRIPS | Translationally-controlled tumor protein homolog | Trichinella | MIIYRDLFSGDELCSDTFPMKLVNDVVFEFTGKHVVRKLGEVTLEGANPSAEEFDEGTEEQMESGIDIVLNHQLMEMPMYQDIKIFKDWIKEYMKKLVEKMKSDGESEESISKFKKNMQEYVTSLLKKDRFKELQFFSGPGENAAEGQLAIVEYRQVSDTEQPIVMLIKQGLVVEKC | Involved in calcium binding and microtubule stabilization. | Q2L875 |
Q04545 | TDA9_YEAST | Topoisomerase I damage affected protein 9 | Saccharomyces | MSSEEFKGLPIKRDISSTIYADRPPALSAPPCVGATGNDKIQVLPIPKKSRTIKTDKPRPFLCHICTRGFVRQEHLKRHQRAHTNEKPFLCVFCGRCFARRDLVLRHQHKLHSALVSKESINSKDKTEIDAINDKNIIQIQGNKQTILPTPSNPLAKTAVQLKKAAKEKKNGKQGKLDLSPSYGANNHSTDVSPSVGNSSTPAVIEETDSSSHFPLPDTNIPTKSKRHASFSASSAFTYSSDNFQKLHQQAKSDFDELQESIPHQVGFSTPQLTAQQLIENAIESGVVDLETLDLPPFLSLDGLPPASSSAAVAASEQIDICPSSATDTISGANSTPNQAATAPPFQLPIARESSSLFLANTPYLSDFLTMGSSYGGSGGFAKSITADPSLDYFNYKNHSHPDSRHNNSSSGINYSNNKNNNESIEKSQNNSNVINETIDHTDIHAHHADAHDDSFIESEEWLSKFIMDSQIDNDLKLNINHFNDIGFNNLHPQNPTTHSEPRNMHNENRDMHRSASKFQSVSENISPREQMSLFKTKQNKAISKFLSDEKIPSTASPSSSASPVQFDKKNVDINEFLLDESVSNLFTTRQIDLFKKNVNLYSPLFQNQKDAVSSTSLTPSLTTQTATTQSGPGWTDSSQKLTFFTEQLRNLIIKENNLKSNLFPTVDELNHYVDLYQVEFHKYFPFIHLYSIIPSSENYPLVISISMIGALYGFHSTHALLLSKIARTRVRMFLENTRSNHDKTPIWLMQSLVLLTFTSIFSNDMNAFRTVNTQIMILVQLIKISKLNYPLENFIKPPIESDHVLEYQDNPAVLNQFKAQYNTREQINRNFKYFILAQSRIRICHIVLLISNLFKSLVDFDCCFHSIDLKCGVPCYNEVLFFCENSRTWNENLTRFNIVLDSKFSLIEVSNGESNYEKCLMYLSNGNPYLYKNAKISFKTLLSLLISIHEKINIERDALKDSYESDFHAKNVQWRMHSRPLVATMLKHWELLYIKNGGILALSDENLPIINTNPSFRLIIPLYFFAKLRKCLDIAPTLRCIWNQDWNSMNSSLEKVCYERESLREATEYAVSVITFWIDTVSVMKGKSTQTPIFTITCIFVSILVIAGYMRRLEDFAQNKNSDCMIGSLKSTDRILWLKAFKTLKRIESHLSEREYKLQTFAEFLRVPDNGSLDIESLDSSLIENTLNSHDVTNQALDIITRTRLSSRTLYCGARILGDTPVWPVSLLFAHALQSRAIYNINHRKSVNSV | DNA-binding protein that acts probably as a transcription factor. | Q04545 |
Q8RGR2 | UVRB_FUSNN | Excinuclease ABC subunit B | Fusobacterium | MENNLFKIHSDYKPTGDQPTAIDSIVKNIENGVKDQVLLGVTGSGKTFTIANVIERVQRPSLIIAPNKTLAAQLYSEYKKFFPENAVEYFVSYYDYYQPEAYIKTTDTYIEKDSSVNDEIDKLRNAATAALIHRRDVIIVASVSSIYGLGSPDTYRRMTIPIDKQTGISRKELMKRLIALRYDRNDVAFERGQFRIKGDVIDIYPSYMNNGYRLEYWGDDLEEISEINTLTGQKVKKNLERIVIYPATQYLTADDDKDRIIQEIKDDLKVEVKKFEDDKKLLEAQRLRQRTEYDLEMITEIGYCKGIENYSRYLAGKNPGDTPDTLFEYFPKDFLLFIDESHITVPQVRGMYNGDRARKESLVENGFRLKAALDNRPLRFEEFREKSNQTVFISATPGDFEVEVSDNHIAEQLIRPTGIVDPEIEIRPTKNQVDDLLDEIRKRAAKKERVLVTTLTKKIAEELTEYYIELGVKVKYMHSDIDTLERIEIIRALRKGEIDVIIGINLLREGLDIPEVSLVAIMEADKEGFLRSRRSLVQTIGRAARNVEGRVILYADIMTDSMKEAITETERRRKIQKEYNAYNHIDPKSIIKEIAEDLINLDYGIEEKKFENDKKVFRNKTDIEKEITKLEKKIKKLVEELDFEQAIILRDEMLKLKELLLEF | 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. | Q8RGR2 |
A6WC54 | TPIS_KINRD | Triose-phosphate isomerase | Kineococcus | MSRTPLIAGNWKMVLDHQQGTLLVQKLDWTLKDAKHDYSAVEVAVLPSHTSLRTVQTLIEGDKLSIALGAQDVSEHDSGAYTGEVSAAMLAKLGVTYVAVGHSERRQYHGETDATVRAKAAKALAAGLTPIVCVGEALEIRKAEQHVEFTVGQVTQALTGLTAEQAAGLVLAYEPVWAIGTGEVATPEDAQEVCAALREAVAELFDRATADAVRVLYGGSVKPASIAAIMRQPDVDGALVGGASTDAGDFAAIVRFRDHPA | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A6WC54 |
Q6CXJ8 | TVP38_KLULA | Golgi apparatus membrane protein TVP38 | Kluyveromyces | MADLYEARVSSGGLSRPSDTDFLDSNDNFDDLDDDFLDIYNLSWRQRIVQHGKRHLRNGKDKFNALSRRKKALVVFLGVLEIILIFITVVKREAIMKGLVDASNDLRQKWYTPLVLMLLILAVSFPPLIGYSFLSLSTGLIYGLSFKGWFILAMSTVIGSVLSFTVFQRLLHSHAERLIRMNPKLEAVSSVLQGNDSYWMIALIRLCPFPYSFINGAIAGIYGISIKNFAIANIITTPKAVIYLFVGERLKNMGETDSGSTRLINFISILLANGFLILTTWFLYYRFKKRYLELQSEQQNSFDIF | Golgi membrane protein involved in vesicular trafficking and spindle migration. | Q6CXJ8 |
Q492F0 | UREF_BLOPB | Urease accessory protein UreF | Candidatus Blochmannia | MCADHGISSVLSLMQLVSSNFPVGSFAYSRGLEWAVENNWVNSVETFYSWQQQWIDGPLIYLEWPMLKRCYYYAQIRDEMNFFQCALRILSYRDTHELRLEERQRGKALSRIILQWYPFTDGGTWLSALEHSGLASIAWLGYTWSISLENLALGYAYNMLESATMAGLKLVPFGQITAQRLLRSLMERLPNDWKKSDMIADHELGNGFLLQSIASSCHETQYSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q492F0 |
A4G3Y9 | Y1046_HERAR | Nucleoid-associated protein HEAR1046 | Herminiimonas | MMKNQLAGLMKQAQAMQDNMKKMQEQLALIEVEGQSGAGLVKIVMSCKNDVKRVSIDPSLLADDKDMLEDLVAAAFNDAVRKAEATSQEKMAGATAGMPMPPGFKMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | A4G3Y9 |
Q9BS34 | ZN670_HUMAN | Zinc finger protein 670 | Homo | MDSVSFEDVAVAFTQEEWALLDPSQKNLYRDVMQEIFRNLASVGNKSEDQNIQDDFKNPGRNLSSHVVERLFEIKEGSQYGETFSQDSNLNLNKKVSTGVKPCECSVCGKVFICHSALHRHILSHIGNKLFECEECPEKLYHCKQCGKAFISLTSVDRHMVTHTSNGPYKGPVYEKPFDFPSVFQMPQSTYTGEKTYKCKHCDKAFNYSSYLREHERTHTGEKPYACKKCGKSFTFSSSLRQHERSHTGEKPYECKECGKAFSRSTYLGIHERTHTGEKPYECIKCGKAFRCSRVLRVHERTHSGEKPYECKQCGKAFKYSSNLCEHERTHTGVKPYGCKECGKSFTSSSALRSHERTHTGEKPYECKKCGKAFSCSSSLRKHERAYMW | May be involved in transcriptional regulation. | Q9BS34 |
B0U1W3 | TPIS_XYLFM | Triose-phosphate isomerase | Xylella | MRPKIVVGNWKLHGSHAFAQALVAQVAAGLPLPGVSVIILPPLLYLSDLTQRFKGEGLAFGAQNVSHHDKGAYTGEVSAAMVADVGAHYTLVGHSERREYHHEDSELVARKFAAALSAGLRPILCVGESLPQREAGQAEVAIAMQLAPVLALVGPQGVARGLIAYEPVWAIGTGRHADPSQVQAMHAFIRGEIARQDARIGDSLLILYGGGIKPCNAAELFSQQDVDGGLIGGASLVADDFLAIARATV | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | B0U1W3 |
P13994 | YJU2B_HUMAN | Coiled-coil domain-containing protein 130 | Homo | MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMADNEQVLTTEHEKKQKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRRRFREKKKAIQEEEERDQALQAKASLTIPLVPETEDDRKLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSAPGSASSSKVSGVLKKLAQSRRTALATSPITVGDLGIVRRRSRDVPESPQHAADTPKSGEPRVPEEAAQDRPMSPGDCPPETTETPKCSSPRGQEGSRQDKPLSPAGSSQEAADTPDTRHPCSLGSSLVADYSDSESE | May be involved in mRNA splicing. | P13994 |
B1HZE5 | UREE_LYSSC | Urease accessory protein UreE | Lysinibacillus | MLIEKIMGNIAHEEEHHEKKTEWIELEWEELSKRILRTETDQGTDIALRLEGDEPLKYGDLLWEDEHRRIAIRTKLEPVIVITPNDMHEMGKSAFELGNRHTPCLIENNEIIVRADHTINPLLDEIGVHYETTERRFKQPFKYRGHSH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | B1HZE5 |
Q9VQ91 | TDRKH_DROME | Partner of PIWIs protein | Sophophora | MLRNTPFGATPTYKLLLGFGLCSLGGAMLYAYFKTRNDEEEADSGGQRPASGIRGQTEEQKPQKEVCLKIVVDNEHVPLIMGRGGSNIKLIEEKTLAKIRLRDKDSGHKFCDISGVPDAVKAARALLIKEIERAPVVKVELQVPQRLASKINGRGGELLQEIRSSSLAKLNIDLNGRNGKAKITIIGNQKQVNIARKMLDDQIEEDEELVRSMEEVEQRREPRRSPTNSIASSMYSSQTSLSSHTQPRDKLMASKGEGKPMEVYVSAVASPTKFWVQLIGPQSKKLDSMVQEMTSYYSSAENRAKHVLTAPYVGQIVAAVFKFDEKWYRAEIVDIMPNQYNPKEQVIDLYFVDYGDSEYISPADICELRTDFLTLRFQAVECFLANVKSTIQTEPITWPKSSIAKFEELTEVAHWRKLIARVVTYKERPRATTAVSAAAKEGTPLPGVELFDPADNSELNIADLMITQGFALPLDDSYPVRSRSSTPSSNSDSTIEELCVSNPVTPLTPHSPMSMSIDVDSITQAENEHLAQQLQHLQHKLNGNDIKNINPAKLTATDLENGNNNNASTTNGASAH | Involved in the piwi-interacting RNA (piRNA) metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons which is essential for germline integrity . Likely to act by recruiting Piwi proteins such as AGO3 and piwi to the piRNA biogenesis machinery in the nuage . Required for the final steps of primary piRNA biogenesis by participating in the 3' end-trimming of piwi-bound intermediates into mature piRNAs . | Q9VQ91 |
B7NES3 | TDH_ECOLU | L-threonine 3-dehydrogenase | Escherichia | MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLASIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVAKHVGARNVVITDVNEYRLELARKMGVTRAVNVAKENLNDVMAELGMTEGFDVGLEMSGAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFSIDDFQKGFDAMRSGQSGKVILSWD | Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. | B7NES3 |
P59892 | TRUD_HELHP | tRNA-uridine isomerase D | Helicobacter | MSPHLPQFTNISRIYPFTHTPIECYFNTSPRDFVIKEIPLYEPSGSGEHLLLYVRKKGLSTFELLNILSSSLGCRVRDIGYAGLKDKAATSYQYLSIHRSLQNRLESALPHLHSQHIKILTITPHNHKLKIGHLKGNSFFMRLKKVSSNNATKLHSTLELLAHSGFPNYFGNQRFGKEGDNFQSGKAISEHKLTLKNKKISNFLISSYQSHLFNAWLSSRIQLAQILRSFKPNEVLRALQSPNFPTLHTFAKSCTPQLIKTLQSQKQPFVILQGDIMCHYPFGKNFVCDDTLIESTRFLQKDIAPTGALCGTKFTHSKCLAYDIEEQFLDSQIKANGTRRYAWVWAENIEGRYIPQEAHFELHFHLPKGSYATIFLESLLSTHNC | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | P59892 |
A7ZKL0 | THIK_ECO24 | Thiamine kinase | Escherichia | MPFRSNNPIMRDELLSRFFPQFHPVTTFNSGLSGGSFLIEHQGQRFVVRQPHDPDAPQSAFLRQYRALSQLPASIAPKPHLYLRDWMVVDYLPGAVKTYLPDTNELAGLLYYLHQQPRFGWRITLLPLLELYWQQSDPARRTVGWLRMLKRLRKAREPRPLRLSPLHMDVHAGNLVHSASGLKLIDWEYAGDGDIALELAAVWVENTEQHRQLVNDYATRAKIYPAQLWRQVRRWFPWLLMLKAGWFEYRWRQTGDQQFIRLADDTWRQLLIKQ | Catalyzes the phosphorylation of thiamine to thiamine phosphate. | A7ZKL0 |
A0RHI1 | TRUB_BACAH | tRNA-uridine isomerase | Bacillus cereus group | MEGVVLLHKPKGMTSHDCVFKLRKILREKRIGHTGTLDPDVTGVLPICVGRATKIAQFLTSETKTYEGEVTLGFSTTTEDASGEVVETKHVDRVITRKEVEGALAALTGTIEQMPPMFSAVKVNGKKLYEYARAGQEVERPVRTITIHEFVLLDDREVFEGETISFRFRVTCSKGTYVRTLAVMIGEKLGFPSHMSHLVRTASGEFLLEDCISFEEIEENVQNGTVESIFISIDEALSKFPKMVVDEKQAEKIKNGMFLKNELQITAPFITVFDKNDRCLAIYEHHPKHPGMLKPMKVLVNNQELKL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A0RHI1 |
Q9CK03 | YIHI_PASMU | Der GTPase-activating protein YihI | Pasteurella | MARKKKTRRVSDIMPARKVDKKVELPKGKQGKKLTRYELDAKAREDKKKKKRKGLASGSRHSATENNNNHQALAKKDPRLGSRKKVPLIVEFVNKPEKGMTIPPMKVEEKVAKLDPMLELEQLENNECLNQLLDALDAGKTLSAEDQQFVDDCLDRIAQLMDELGISEDDDPEEDLLRTFEKIDINQFR | A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis. | Q9CK03 |
B3EK52 | THIG_CHLPB | Thiazole synthase | Chlorobium | MDLVQIGSYTFSSRLILGTGKFGNTASMVDAVRASGTELVTVALRRFNREETDHDLFTTLADLDGITLMPNTSGASNAKEAVRAAHISRELSGSPFIKVEIHPNPQHLMPDPIETYEACKILAGEGFLVMPYIPADPVLAKRLEDVGCASVMPLGSSIGSGQGLATAGMIRLIIRESTIPVIVDAGLRSPSEACAAMEMGCTAVLVNSAIAVAQNPPEMAAAFAEAVQAGYRAKAAGIMPKSGSAIATSPLTSFLDTTS | 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. | B3EK52 |
Q6P0X2 | ZN511_MOUSE | Zinc finger protein 511 | Mus | MLLPPALYSRLAGEPGAAEPLPVERNPAAGEAPFRFAPRAVRFPRDHEFFEDGDVQRHLYLQDMLTQVSETPEKSMVPEFTCQVAGCCQVFAAIEDYQHHYHMMHGNTCSFCNRAFPSGHLLDVHILEWHDSLFQILAQRQDMYQCLVESCPEKFKTSQDRKDHMVRLHLYPADFRFDKPKTNRGPAMPAAADAATRAPTDDSDAMEICSEPAAPPPCRRTYSHRSV | May be involved in transcriptional regulation. | Q6P0X2 |
Q1LRG9 | UBIE_CUPMC | Demethylmenaquinone methyltransferase | Cupriavidus | MSETHFGFEKVDESEKAGKVAGVFHSVASKYDVMNDLMSGGMHRLWKVFTIAQANVRPGQKVLDIAGGTGDLAKAFAKQAGPTGEVWLTDINESMLRVGRDRLLNKGVVTPVALCDAERIPFPDNYFDLVTVAFGLRNMTHKDAALAEMRRVIKPGGKVMVLEFSKVWKPLEKFYDVYSFKVLPWLGERVAGDAPSYRYLAESIRMHPDQGSLVRMMEQVGLEQVEYFNLTAGVVALHVGRKY | 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). | Q1LRG9 |
A1W6J1 | YCIB_ACISJ | Inner membrane-spanning protein YciB | unclassified Acidovorax | MKLLIDFFPIILFFAAFKVWGIYVATAVAIAATVVQIGYIRLKHGKVEPLQWLSLGVIVLFGGATLLAHSETFIKWKPTVLYWLMGGTLLVGQLVFRKNFIQSLMGAQIDLPAPVWRNLNWGWTGFFATMGVLNLWVAYNFDTDTWVNFKLFGGIGLMFAFVIAQALYLSRHVKDEGDAAPKDLQP | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A1W6J1 |
A2RKR4 | TRHO_LACLM | tRNA hydroxylation protein O | Lactococcus cremoris subsp. cremoris | MTQDYRVLLYYQYVPIEDGESFAQKHLSDCKALGLKGRILVADEGINGTVSGTVEQTNAYMSLMKNDSRFTSTIFKIDEAKQNAFKKMHVRYRPELVNLSLEDDVNPLELTGAYLDPKEFREAMLDENTVVIDARNDYEFDLGHFRGAIRPEIRSFRELPQWIRDNKEQFMEKRVLTYCTGGIRCEKFSGWLVREGFKDVGQLHGGIATYGKDPEVQGDLWDGQMYVFDSRIAVPINQKEHVIVGRDWFDGSPCERYINCGNPECNRQMLASKENEAKYLGACSHECRVHPDNRYIKAHQLSNQEVQERLALLEKDLAS | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | A2RKR4 |
A0A291PQF1 | UGT5_DACCO | UDP-glucosyltransferase 5 | Dactylopius | MIFFYFLTLTSFISVAFSYNILGVFPFQAKSHFGFIDPLLVRLAELGHNVTIYDPYPKSEKLPNYNEIDVSECFVFNTLYEEIDTFIKTAASPFSSLWYSFEETLAVFQKENFDKCAPLRELLNSTVKYDLLITETFLTDITLLFVNKFKIPFITSTPNVPFPWLADRMGNPLNPSYIPNLFSDYPFDKMTFFNRLWNTLFYVMALGGHNAIILKNEEKINKYYFGSSVPSLYNIARETSIMLINAHETLNPVIPLVPGMIPVSGIHIKQPAALPQNIEKFINESTHGVVYFCMGSLLRGETFPAEKRDAFLYAFSKIPQRVLWKWEGEVLPGKSENIMTSKWMPQRDILAHPNVKLFISHGGLLGTSEAVYEGVPVIGIPIFGDQRTNIKALEANGAGELLDYNDISGEVVLEKIQRLINDPKYKESARQLSIRYKDRPMSPLDTAVYWTEYVIRHKGAPHLKTAAVDMPWYQYLLLDVIAFLIFILVSVILIIYYGVKISLRYLCALIFGNSSSLKPTKKVKDN | Catalyzes the transfer of a glycosyl group from a UDP-sugar to an acceptor molecule. | A0A291PQF1 |
B8G9R8 | TRMD_CHLAD | tRNA [GM37] methyltransferase | Chloroflexus | MRFDILTLFPAMFQGPLTESILKRAQQAGKITIHLHDIRDWATDRHRTVDDAPYGGGAGMVMKAEPLAAAIRAVQAADEPGGPVVLLTPDGELFNQSIARELATLPRLILVCGHYEGIDERVRERLVDREISIGDYVLTGGELAAMVVVDAVARLVPGVIDSESIVEESHSDFLLEYPHYTRPAVWEGLAVPSILLSGHHGEIARWRRSERLRRTLARRPDLLARAAAAGVLTKADLALLAEWGWDGMSEGGWMS | Specifically methylates guanosine-37 in various tRNAs. | B8G9R8 |
Q5E7J6 | TYPH_ALIF1 | TdRPase | Aliivibrio | MYLPQEIIRKKRDNKELTAEEINFFIQGVAKETVSEGQIAAFAMAVYFNEMTMPERIALTCAMRDSGMVIDWSHMNFDGPIVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLESIAGYNITPSNDVFGKVTKEAGVAIIGQTGDLAPADKRVYATRDVTATVDNISLITASILSKKLAAGLDSLVMDVKVGSGAFMPTYEASEELAKSIVAVANGAGTKTTALLTDMNQVLASTAGNALEVREAIRFLTGEYRNPRLYEVTMALCAEMLVIANLAKDEQDARAKLQTVLDNGKAAECFGKMVFGLGGPSDIIENYDNHLESAQIIKPVFADTTGFVQAMDTRDLGMAVVGMGGGRRVASDTIDYAVGLSDMIRLGQTADNQQPLAMIHARNEEQWQQAANAVKAAIVISEKQPEATPEVYRKIRPEDV | 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. | Q5E7J6 |
P96190 | TPIS_XANFL | Triose-phosphate isomerase | Xanthobacter | MTAERRPLIAGNWKMNGLRAAKSELRTVAAGLAGLSAETMICPPFTLIGAFAADVAGTQLMIGGQDCHPAESGAHTGDISAEMLRDAGAVAVILGHSERRIDHQEGDAIVKAKVKAAWRAGLLPVVCVGETLVERDAGEAAAVVTRQVRQSVPEGATAVSLVIAYEPIWAIGTGRTPTTDDVAEVHGAIRHILAERFGAEANGIRILYGGSVKPDNAAALLATANVDGALVGGASLKAADFLAIARAVG | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | P96190 |
O60347 | TBC12_HUMAN | TBC1 domain family member 12 | Homo | MVGPEDAGACSGRNPKLLPVPAPDPVGQDRKVIRATGGFGGGVGAVEPPEEADEEEEADEEEETPPRQLLQRYLAAAGEQLEPGLCYCPLPAGQAGAPPPSAAPRSDACLLGSGSKHRGAEVADGRAPRHEGMTNGDSGFLPGRDCRDLEEARGLARAGGRESRRRRPYGRLRLEGPGDEDADGAGSPSDWASPLEDPLRSCCLVAADAQEPEGAGSDSGDSPASSCSSSEDSEQRGVGAGGPEEGAPPATSAERTNGGAEPRLGFSDIHFNSRNTFQVSRGQSARDHLPPAGPPVPLPAAEQGPAGASARARRSGGFADFFTRNLFPKRTKELKSVVHSAPGWKLFGKVPPRENLQKTSKIIQQEYEARTGRTCKPPPQSSRRKNFEFEPLSTTALILEDRPSNLPAKSVEEALRHRQEYDEMVAEAKKREIKEAHKRKRIMKERFKQEENIASAMVIWINEILPNWEVMRSTRRVRELWWQGLPPSVRGKVWSLAVGNELNITPELYEIFLSRAKERWKSFSETSSENDTEGVSVADREASLELIKLDISRTFPSLYIFQKGGPYHDVLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLEEADAFIAFANLLNKPCQLAFFRVDHSMMLKYFATFEVFFEENLSKLFLHFKSYSLTPDIYLIDWIFTLYSKSLPLDLACRVWDVFCRDGEEFLFRTGLGILRLYEDILLQMDFIHIAQFLTKLPEDITSEKLFSCIAAIQMQNSTKKWTQVFASVMKDIKEGDKNSSPALKS | RAB11A-binding protein that plays a role in neurite outgrowth. | O60347 |
Q8E7Y2 | TILS_STRA3 | tRNA(Ile)-lysidine synthetase | Streptococcus | MYNTILKDTLSKGLFTAHQKVLIAVSGGIDSINLLQFLYQYQKELSISIGIAHINHGQRKESEKEEEYIRQWGQIHDVPVFISYFQGIFSEDRARNHRYNFFSKVMREEGYTALVTAHHADDQAETVFMRILRGSRLRYLSGIKQVSAFANGQLIRPFLPYKKELLPNIFHFEDASNASSDYLRNRIRNVYFPALERENNQLKDSLITLSEETECLFTALTDLTRSIEVTNCYDFLRQTHSVQEFLLQDYISKFPDLQVSKEQFRVILKLIRTKANIDYTIKSGYFLHKDYESFHITKIHPKTDSFKVEKRLELHNIQIFSQYLFSYGKFISQADITIPIYDTSPIILRRRKEGDRIFLGNHTKKIRRLFIDEKITLKEREEAVIGEQNKELIFVIVAGRTYLRKPSEHDIMKGKLYIENLEKR | 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. | Q8E7Y2 |
B1KK02 | TRPB_SHEWM | Tryptophan synthase beta chain | Shewanella | MTKLDPYFGEYGGMYVPQILMPALKQLETAFVEAQEDEAFKTEFNDLLKNYAGRPTALTLTRNLSPNPLVKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLDLKCKVYMGAKDVERQSPNVFRMKLMGAEVIPVTSGSSTLKDACNEAMRDWSGSYDKAHYLLGTAAGPHPFPTIVREFQRMIGAETKKQILEREGRLPDAVIACVGGGSNAIGMFADFIDEESVKLIGVEPAGLGIDTPMHGAPLKHGKTGIFFGMKAPLMQDREGQIEESYSISAGLDFPSVGPQHAHLAATGRATYESATDDEALEAFQLLARSEGIIPALESAHALAYAVKMAKAATQETILVVNLSGRGDKDIFTVADILEERERSQTGQQKEESGND | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | B1KK02 |
B5FUW0 | YQGF_SALDC | Putative pre-16S rRNA nuclease | Salmonella | MSDTLLAFDFGTKSIGVAIGQRITGTARPLPAIKAQDGTPDWMLIERLLKEWQPDEIIVGLPLNMDGTEQPLTARARKFANRIHGRFGVTVTLHDERLSTVEARSGLFERGGYRALNKGKVDSASAVIILESYFEQGY | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B5FUW0 |
Q9FIK1 | Y5780_ARATH | BTB/POZ domain-containing protein At5g47800 | Arabidopsis | MKFMKIGTKPDTFYTQEASRILITDTPNDLVIRINNTTYHLHRSCLVPKCGLLRRLCTDLEESDTVTIELNDIPGGADAFELCAKFCYDITINLSAHNLVNALCASKFLRMSDSVDKGNLLPKLEAFFHSCILQGWKDSIVTLQSTTKLPEWCENLGIVRKCIDSIVEKILTPTSEVSWSHTYTRPGYAKRQHHSVPRDWWTEDISDLDLDLFRCVITAARSTFTLPPQLIGEALHVYTCRWLPYFKSNSHSGFSVKENEAALERHRRLVNTVVNMIPADKGSVSEGFLLRLVSIASYVRASLTTKTELIRKSSLQLEEATLEDLLLPSHSSSHLHRYDTDLVATVLESFLMLWRRQSSAHLSSNNTQLLHSIRKVAKLIDSYLQAVAQDVHMPVSKFVSLSEAVPDIARQSHDRLYKAINIFLKVHPEISKEEKKRLCRSLDCQKLSAQVRAHAVKNERMPLRTVVQALFFDQESGSKGASSRSESQELFTRGKETPTDEHSMMHKLHLGPASTGKAKNVLEEGCKRGEEKTRSSTDPKKIVWKGTGSEHKHHISRDR | May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. | Q9FIK1 |
B7G5J1 | TRM52_PHATC | tRNA methyltransferase 5 homolog 2 | Phaeodactylum | MTTRVTGNERRGRQLLLRFSGFLSAALTVMALITATRALAPVVAYIAPQRVRSHFMRRAFASGNCRSRRFSVLRSTVGTETRNENNITTPYHSPLPTSRYVYQSSRTLSSRNPALPLESTLMHSNANELTDVELKNLVAHWRDHPVLNPMVTFRSWVVPIKGKMIQAILNSKSLQPYLASRHELLQEMHVRLKIVRDYTDSTDGTEKLILLHPDTPPLSELPADVQQLLRNCQIHENGPVMPTKFTYKDFTASYILSQLLPIAVHPPPTAFETIGHVAHLNLKERHWPYRFLIGQVLLETLPLIESVINKVGEVSGPYRTYDFGLLAGRNDTRVKLTESGVQLQFDLADVYWCSRLSEERQRLLRTFQPGQIIADPFCGVGALCLLAASLPQRNCTIWANDWNPKAVEYLRENARRNHVSDRIERLQCGDAYDFLMDMGLQQHQKASTRSRKEDVTNKDGNHVTPTEPMRLPDHVVMNYPVEAPKFLGALRWWPVPPSSRRGSTTRDGGIGSVIVPRVHVYTFARADPTTDRDAEEVAVDLVAANLLPLGNTIHCRTEMNEDYDCDIQVHPVRDVAPGKVVLCGDFR | 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. | B7G5J1 |
Q1GRG3 | Y2050_SPHAL | Nucleotide-binding protein Sala_2050 | Sphingopyxis | MSGQASPGAESRLLLVTGLSGAGKSTVLKVLEDLGWEVVDNLPLALLEALIDAPVKRGEAERPLAVGIDSRSRGFRPALLVRRIKELREGGGRDIQTLFLDCAGAELERRFSETRRRHPLAEDRPAADGIAREREMMEPLRRWAEHVVDTTNYSSNDLQQEVRQRFGEADDGEPVLNILSFGFARGLPRNADLVFDMRYLRNPHWDPALKPGTGLDPDVAAYVIADPAYEETVSQIERLILTLLPRYRAEGKSYVTIAFGCTGGRHRSVHVAARVAQTLRGSGYEPTLTHRNLDSAPQDGLEGKPPSAARASGGAR | Displays ATPase and GTPase activities. | Q1GRG3 |
Q8Y556 | YHAM_LISMO | 3'-5' exoribonuclease YhaM | Listeria | MEKRLLDFEVGETVDLFLLIKSSVKGTASNGKPFLSLVLQDKSGELEAKLWDVKESDEANYGVQQIVHLMGDIQNYRGRKQLKIRQIRQATALDGVSASEFMETAPINKEEMADEITQYIFEMKNANLQRITRALLKKYQDDFYDYPAAMRHHHEFVSGLSFHVVSMLRLAKSVADLYPSVNRDLLYAGVILHDLGKVIELSGPVSTTYTLEGNLIGHISIVVEEVSKIADELSIDGEEVVVLKHVLLSHHGKGEWGSPKPPLVREAEILHQIDLMDASLNMMDKVLKHTKPGEFSERVFGLDNRSFYNPTFE | Shows a 3'-5' exoribonuclease activity. | Q8Y556 |
O34311 | YKOW_BACSU | Signaling protein YkoW | Bacillus | MEIHVTYNTTLICLSILIACTASYISLELSRKVTINTGLKSKIWLIGGSLIMGFGIWSMHFVGMMAVHMEMPMEYEFMPLMAAIGASVSGSFVSLYFVSRHILTYYRLLTGSVVLGASIASMHYIGMSAISRVMIIYEPILFTVSIIIAIAASFVSLKIFFDLAVKKHSEHLIFYKGVSSIVMGIGISGMHYTGMLAATFHKDMAPPGSHMEVQTFHWSIFVTLIIFCIQTLLLFSSHADRKFIKQSERIKDNEQRFQSLIVHNIDAIFILSLEGDIISSNHAGEEMISKFGFSMHDWRNYTSLKVKRLFEQVKKDKQAMNSDSDLITEKGQFHLNITLIPVEVNQELDSIYVICKDMTKQYKAEKEIHRMAHYDSLTDLPNRRHAISHLTKVLNREHSLHYNTVVFFLDLNRFKVINDALGHNVGDQLLQFAAKRLSSVVPDNGFIARLGGDEFIIILTDANTGTGEADVLARKIIQKFKKPFKIQDHTLVTSVSIGIAISPKDGTDGLELMKKADMAMYAAKERNKSKYRYYSFSIGNKETVKLNQEMVLREAIENDRFVLHYQPQFSVKKQKMTGAEALIRLVTPDGQLRPPGEFIGVAEETGLIIDIGKWIIDEACKQARIWHDKGYDLSVAINISARQFQSKDLIPLIKDTLNKYQLPPQLLEVEVTESMTMDNLNHSKKVLSSLTELGIRISIDDFGTGHSSLSYLKDFPIHRLKIDKSFIDDIQTHPKSEQITGAIIAMGHQLSLQVIAEGVENAAQKQLLFEKGCDHLQGFFFSRPIPPEQFEQFIIEQPSQ | Probable signaling protein whose physiological role is not yet known. | O34311 |
Q9KRE2 | YCIB_VIBCH | Inner membrane-spanning protein YciB | Vibrio | MKQLLDFIPLIIFFALYKFYDIYVATGALIAATTVQVIVTYAMYKKVEKMQLITFVMVALFGGMTLALHDDNFIKWKVTIVYVVFALGLTISQIMGKPAIKGMLGKELTLPDAVWSTINWAWVMFFSGCAALNLYVAYHLPLDVWVNFKVFGLLAATLVFTLLTGGYIYKHLPHEPKQKNQ | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q9KRE2 |
Q65PF4 | TILS_BACLD | tRNA(Ile)-lysidine synthetase | Bacillus | MKSIEDFMKKYELSFDGVTLIAGVSGGPDSMALLHALHHTVPASATLIAAHVDHMFRGEESERDMRFVQDYCEAEGIQCEAVQIDVLAFAAENNLNKQAAARECRYAFFQELMKRHRAEYLVLGHHGDDQVETMLMKMAKGTVGIGLAGIQPKRRFDSGWLLRPFLKLSKDDLLAYCKENRIPFRTDPSNSEDDYTRNRFRHHVLPFLKKESEDVHKRFQSVSEFLTEDELYLQALTKDKMNTVITSKSSSGVEISIERLLALPMPLQRRGVHLILNYLYENVPSAFSAHHIQVFLDWISQDGPSGSLDFPNGLKVAKSYHTCLFTFQRLQCENVSYHYEISGAGEEELILPGGSSLHVSGPGSTRKLQGNDVFATSPKQVQFPLYVRTRQNGDRVKLKGMNGSKKVKDIFIDEKVPLSKRDSWPIVTDAVGNIIWIPGLKKTIFEELDVTNNDRIVLQYRQHEKCRGLAKNETGY | 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. | Q65PF4 |
B6JUP5 | VASA2_DROME | Sisters on the loose | Sophophora | MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDAKELPPIPSSCDKDEVGAFIDQLDLSKYTTSLALIRKLRDYLLTAFKALVNQAWASLEKLAQEKRAQKAHQIRETTDMMNRLMEDMGRLIREGEHEEANGIGMGFQSIDADCRADLSQWRNLQQVVMPQSSEIRDGQTNRTSGTEGGRSGGLTDGDDLTEIQSAAYAVYHQVLDRGYQTGRRLYDDNQGALREDSIPTEDREHPENNQVDGSTYGVTRFLHWLSENFVTRHEIRAVRFGSPHMVFQSYDWPESPKQHISTVHQKGIFYSQPLIRTRIIATVASEPNNSSSGQLSSMVNLARHQRSQNQETPDGIYVSRYNATGDEETPCSATGVPGRVVALRASSTPNEHRSDPGLSFIPNLTYEDGTIPSLAAGGAASTPLAPSLPAEHSLGLEMDSNTLVVPADADETRLVGHPGSTVVRSRLGGPPASTPLLSFRPRLPVIDEEHHLRFTRVSRELQMSVAFPPEETTLSEQREWGSIFRPRDEMVNYAEGPPPRQTQRARRRSRTRRRRNRIASAASPQLTPERIVRREEAFQSSRHIAATFMSSLLQNAAGEVTTSSGLAVTRSVKEITTSVHITRNVLQEEVPPTTEATTTSLEVAQATGYSDSGACMQSAAFSQDLPVVAPLEISGNASSDQASFDQALALLPPINSTPIGQHPIAVFGPKTEIEIKPQKMDISNMMNTSVPPMPMEVDEVPLEVSNTLANMSDHAYVTDIQILPSLQLNSLNLVSTNITDNAVNIAPSTSTNDLQTPSDRRTSMQNQLYRVSMNDLAYISQHANVVRLMVDRQEELGAQVSSLGPFKENSQGALNFSTMPAVKVYDPRIIQNIQKDKMRVVHGLFGALIRQSQVDMHNAPFIRNRKDALMAYRFLLELKTANIISLSSDGRFFGLL | Isoform solo and SMC1 function as partners in mediating sister chromatid and centromere cohesion in meiosis. Not required for sister chromatid arm cohesion or for mitotic chromatid segregation. | B6JUP5 |
Q5HLZ4 | TOP3_STAEQ | DNA topoisomerase III | Staphylococcus | MKSLILAEKPSVGRDIANALNLQQKSNGYIEGKQYIVTWALGHLVTNATPEQYNPSYKEWNLEDLPIIPKKMKTVVISKTNRQFKIVKSLILDKNVKEIIIATDAGREGELVARLILDKVGNKKPIKRLWISSVTKKAIQEGFKQLKNGNAYQNLYEAALARSEADWIVGINATRALTTKYDAQLSLGRVQTPTIQIVKSRQDEINYFKPEKYYTLSINVDGYDLNLKQQKRYKDKKELELIEHKIKHQEGKILEVKGKNKKSYAQPLFNLTDLQQEAYKHYKMGPKETLNTLQHLYERHKLVTYPRTDSNYLTDDMVDTIQERLRAILATDYKSHVRDLISESFSSKMHIFNNQKVSDHHAIIPTEVRPSIEQLSQREFKIYMLIAERFLENLMNPYLYEVLTIHAQLKDYNFVLKEIIPKQLGYKALKDQTSSHTLTHSFKEGQLFKVHRIEIHEHETKAPEYFNEGSLLKAMENPQNHIDLNDKKYAKTLKHSGGIGTVATRADIIEKLFNMNALESRDGKIKVTSKGKQILELSPSELTSPILTAQWEEKLMLIEKGKYNSQKFIQEMKNFTFKVVNKIKSSEQKYKHDNLTTTECPTCGKFMIKVKTKNGQMLVCQDPKCKTKKNIQRKTNARCPYCKKKMTLFGKGKEAVYRCVCGHTETQSQMDKRMRDKTNGKVSRKEMKKYINKKEEIDNNPFKDALKNLKL | 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. | Q5HLZ4 |
Q73VN9 | TRMD_MYCPA | tRNA [GM37] methyltransferase | Mycobacterium avium complex (MAC) | MRIDVVTIFPAYLDPLRQSLPGKAIQSGLVDLRVHDLRRWTHDAHRSVDDAPYGGGPGMVMKAPVWGEALDEIASAETLLVVPTPAGVLFDQATAARWSAERHLVFACGRYEGIDQRVVEDAARRMRVEEVSIGDYVLPGGESAAVVMIEAVLRLLDGVLGNPASRHDDSHSPALDRRLEGPSYTRPPSWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPELLADPVGPQDDPGR | Specifically methylates guanosine-37 in various tRNAs. | Q73VN9 |
B5G6G6 | VKT2_PSEPO | Kunitz-type serine protease inhibitor blackelin-2 | Pseudechis | MSSGGLLLLLGLLTLWEGLTPVSSKDRPDFCELPDDRGPCRGIFHAFYYNPDQRQCLEFIYGGCYGNANNFKTIDECKRTCAA | Serine protease inhibitor. | B5G6G6 |
Q5KW56 | THII_GEOKA | tRNA 4-thiouridine synthase | Geobacillus thermoleovorans group | MNYDRILIRYGEMTTKGKNRNIFVRRLKNNIARKLQAFERIQIEYMRDRMYILLNGEPHEPIIEKLKTVFGIHSFSLAMKCENDLDAIKETALAAVRQLPYKGKTFKVSARRVDKQFPYRSDELNYEVGAHILRQTDGLRVNVREPDIDVRIEVRQDGTYVTCRDIFGAGGLPVGTSGKAMLMLSGGIDSPVAGYLAMKRGLEIEAVHFFSPPFTSERAKQKVIDLVRKLTTYGGRIKLHIVPFTEVQQAIYQGVPNEYSLISTRRAMLRITDALRRRQRALAIVTGESLGQVASQTLESMYVINEVTNTPILRPLVSMDKLEIIELAKQIGTHDISILPYEDCCTIFTPRAPKTKPKKEKVFHYESQLDLAPLLEKAVNDTETLVIDEETGQGDEFAELF | 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. | Q5KW56 |
B1LEK0 | TRPR_ECOSM | Trp operon repressor | Escherichia | MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEDVLLKDH | This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. | B1LEK0 |
P60975 | TXHA5_CYRHA | Hainantoxin-V | Haplopelma | ECLGFGKGCNPSNDQCCKSANLVCSRKHRWCKYEI | Inhibits selectively tetrodotoxin-sensitive voltage-gated sodium channels (Nav). Does not act by binding to receptor site 3 to slow the inactivation kinetics of sodium currents. | P60975 |
Q6MLS8 | TILS_BDEBA | tRNA(Ile)-lysidine synthetase | Bdellovibrio | MKLSKAKQDLDHHVWKLIKLHSLQDKKILVALSGGTDSVALLRSLTKVHKKNLLGACYFHHGEDSNQEYRKEAQEFCEKLCKKLEIEFYPLRASQLAKSEAEYRELRYEALDRLKKEQGFELVATGHHRDDLLETRLIRLIRGTGAQGFAAMHVLRDGLFRPLLEISKKELKKYLREERLRSFEDPTNKALDPLRNWLREEWLKSLERRARGSTAALARSLETIAQEIENRPWGDLLGQNEAYKTQGLRRSFYLTLSPFEQKRLLAQYLFSLGKRDFSQSHLEEIQKRLDKSQKVITFKVAGCQWEVNAEQIKVQS | 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. | Q6MLS8 |
O23402 | U84A4_ARATH | Hydroxycinnamate glucosyltransferase 1 | Arabidopsis | MEMESSLPHVMLVSFPGQGHISPLLRLGKIIASKGLIVTFVTTEEPLGKKMRQANNIQDGVLKPVGLGFLRFEFFEDGFVYKEDFDLLQKSLEVSGKREIKNLVKKYEKQPVRCLINNAFVPWVCDIAEELQIPSAVLWVQSCACLAAYYYYHHQLVKFPTETEPEITVDVPFKPLTLKHDEIPSFLHPSSPLSSIGGTILEQIKRLHKPFSVLIETFQELEKDTIDHMSQLCPQVNFNPIGPLFTMAKTIRSDIKGDISKPDSDCIEWLDSREPSSVVYISFGTLAFLKQNQIDEIAHGILNSGLSCLWVLRPPLEGLAIEPHVLPLELEEKGKIVEWCQQEKVLAHPAVACFLSHCGWNSTMEALTSGVPVICFPQWGDQVTNAVYMIDVFKTGLRLSRGASDERIVPREEVAERLLEATVGEKAVELRENARRWKEEAESAVAYGGTSERNFQEFVDKLVDVKTMTNINNVV | UDP-glucosyltransferase that forms glucose esters with phenylpropanoids . Glucosylates 4-coumarate, ferulate, caffeate, sinapate and cinnamate . | O23402 |
Q12071 | VPS54_YEAST | Temperature-sensitive clathrin synthetic mutation protein 3 | Saccharomyces | MSISETPHNKSQGLQKAAGRPKIVVPEGSPSRNSDSGSFTIEGDTSLNDDLLSISGSVTPRARRSSRLSLDSITPRRSFDSRTLSVANSRSFGFENETHSGSMDFSPLGNNSIYEIVMNTRRKNWLNYPTVADIPQVSLSKNDLDDHWKTHVIEYVKNIKSDYQIFQSTNNIRNMNQMEQLKELREGENMHEESFEANLRQGDAELINSIPDFYFSDKFQLDNPRTFHKVLDAIDLFLTKLDMKRQAERDEAFSELRDRLNDFLDIVETLLVTEISKSSHKFFHALSEVDNIQKRALDTMSELKELAQNIKTIDAENIRKKISHLEMIFKRKNVEKLEQGLLQAKLVLNKTDECKSMYEENKLDNCLELIKSIDYLIKGDDSINEDVQSWTRCWPYKLSNLRTIPALSATREFLTNMKIEIGGKFSLQLSILLIDDLRSFCKSIKPKETLHRIQTGSNDKKQTIFTDNFSSKITELIVRLNRCEELTSAFDLYREKSITELKSIIKIYLPTENAHADNNHDEKHLNNGSTSGSKLSRLIKEQTPAEFQSMLVNIFTHALEALRRLYGHQKLLLDISLNELASVKSPNENQHNMITQLDIRTGINEIIRIIQLRTGKIIAVRRELNLSLRYDYFLKFYAICVIFIQECEVLSGEFLTKYLSNVLASQIKHYANAQSSKNYRNIKKKIDAEEWIPYIVDSSIQSDVNDIVSSIDIDPLSWTTILDMVGGSHDCENGRSEDKEKDEGNETYQGHRKSVVVGDKTFVASSSLLATIEVIKELMVLSINLPSIYLSNFEKLCYDALQYYNSSAMASVTQPGNSLLKTGRNLSIMGESLDCLAEFVIIVQRFYQRLSNSNRDFEPFDASHYTTLLGQFQASSNKIYMANAPPPPV | Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. Seems also to be involved in protein transport from Golgi to the plasma membrane and is required for the integrity of the actin cytoskeleton. | Q12071 |
Q8MHY7 | UROK_RABIT | Urokinase-type plasminogen activator chain B | Oryctolagus | MRVLLVCLLLCALVVSDSEGSHELHGVSDASNCGCLNGGTCVTYKYFSNIWRCNCPKKFQGEHCEIDTLKTCYHGDGHSYRGKANTDIMDRPCLAWNSANVLTKTYHAHRPDALQLGLGKHNYCRNPDHQRRPWCYVQVGLKQLIQECKVHDCSSGKKPALPPGKLEFQCGQKALRPRFKIIGGEFTIIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFINHQKKEDYIVYLGRSRLNSMTPGEMKFEVEQLILHEGYRADTLAHHNDIALLKILSNNGQCAQPSRSIQTICLPPWNADPNFGTSCEITGFGKENSTDYLYPEQLKMTVVKLVSYQECQQPHYYGSEVTTKMLCAADPQWETDSCQGDSGGPLVCSVQGRMTLTGIVSWGRGCALKNKPGVYTRVSRFLPWIRSHIGEENGLAL | Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. | Q8MHY7 |
Q9SR34 | TA1_ARATH | Protein TELOMERASE ACTIVATOR1 | Arabidopsis | MENIKNPKNADDCSDSISKNSHQGVDDSLNQSRSYVCSFCIRGFSNAQALGGHMNIHRRDRAKLRQKLMEDNKDDVVAESDASEVVSLDLNEQQQQQGEALTCDDHDQYVDNDISPKQKLEFWVQESKLDTNDHGKVTEASIDGSSSSHHRDIEVLDLELRLGQSVVKKKTT | Activation factor which mediates telomerase activity and potentiates responses to auxin through the regulation of BT2. Binds in vitro to the DNA sequence 5'-GACAGTGTTAC-3' of the BT2 promoter. | Q9SR34 |
Q9QXQ5 | WNT4_RAT | Protein Wnt-4 | Rattus | MSPRSCLRSLRLLVFAVFSAAASNWLYLAKLSSVGSISEEETCEKLKGLIQRQVQMCKRNLEVMDSVRHGAQLAIEECQYQFRNRRWNCSTLDSLPVFGKVVTQGTREAAFVYAISSAGVAFAVTRACSSGDLEKCGCDRTVHGVSPQGFQWSGCSDNIAYGVAFSQSFVDVRERSKGASSSRALMNLHNNEAGRKAILTHMRVECKCHGVSGSCEVKTCWRAVPPFRQVGHALKEKFDGATEVEPRRVGSSRALVPRNAQFKPHTDEDLVYLEPSPDFCEQDMRSGVLGTRGRTCNKTSKAIDGCELLCCGRGFHTAHVELAERCGCRFHWCCFVKCRQCQRLVEMHTCR | Ligand for members of the frizzled family of seven transmembrane receptors. Plays an important role in the embryonic development of the urogenital tract and the lung. Required for normal mesenchyme to epithelium transition during embryonic kidney development. Required for the formation of early epithelial renal vesicles during kidney development. Required for normal formation of the Mullerian duct in females, and normal levels of oocytes in the ovaries. Required for normal down-regulation of 3 beta-hydroxysteroid dehydrogenase in the ovary. Required for normal lung development and for normal patterning of trachael cartilage rings. | Q9QXQ5 |
Q5R8X1 | ZN665_PONAB | Zinc finger protein 665 | Pongo | MGEAFYTVKLERLESHDTEGLSFQEVQKNTYDFECPWKDDEGNSKRVLTLQKENLPGRRDQRDRRAAGNRLIENQLGVSFQSHLPELQQFQGEGKIYEYNQVEKSLSNRGKHYKCDECGKVFNQNSRLTSHKRIHTGEKPYRCNECGKAFTVRSNLTIHQVIHTGEKPYKCNECGKVFSQPSNLAGHQRIHTGEKPYKCNECGKAFRAHSKLTTHQVIHTGEKPYKCNECGKCFTQNSHLASHRRIHTGEKPYKCNECGKAFSVRSSLTTHQTIHTGEKPYKCNECGKVFRHNSYLTKHRRVHTGEKPYKCNECGKAFSMHSNLTKHQIIHTGEKPFKCNECVKVFTQYSHLANHRRIHTGEKPYRCDECGKAFSVRSSLTTHQAIHTGEKPYKCNDCGKVFTQNSHLASHRGIHSGEKPYKCDECGKAFSQTSQLARHWRVHTGEKPYKCNECGKAFSVHSSLTTHQTIHTGQKPYKCNDCGKVFRHNSYLAVHQRIHTGEKPYKCNECGKAFSVHSNLATHQVIHTGEKPYKCNECGKVFTQNSHLANHRRIHTGEKPYRCNECGKAFSVRSTLTTHMAIHTGDKPYKCNECGKVFTQNSNLAKHRRIHSG | May be involved in transcriptional regulation. | Q5R8X1 |
Q2YVL8 | XPT_STAAB | Xanthine phosphoribosyltransferase | Staphylococcus | MELLGQKVKEDGVVIDEKILKVDGFLNHQIDAKLMNEVGRTFYEQFKDKGITKILTIEASGIAPAIMAALHFDVPCLFAKKAKPSTLTDGYYETSIHSFTKNKTSTVIVSKEFLSEEDTVLIIDDFLANGDASLGLYDITQQANAKTAGIGIVVEKSFQNGHQRLEEAGLTVSSLCKVASLEGNKVTLVGEE | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q2YVL8 |
P24335 | WAG13_TROWA | Wtx-1 | Tropidolaemus | SLGGKPDLRPCHPPCHYIPRPKPR | Waglerin-3 selectively blocks the epsilon subunit of muscle nicotinic acetylcholine receptor (nAChR). It elicits tachypnea, ocular proptosis, rapid collapse and spasms in mice. It causes death by respiratory failure. | P24335 |
Q89ZY4 | TRUA_BACTN | tRNA-uridine isomerase I | Bacteroides | MQRYFIYLAYDGTNYHGWQIQPNGSSVQECLMKALSTFLRRDVEVIGAGRTDAGVHASLMVAHFDHEDVLDTVTVADKLNRLLPPDISVYRVRQVKPDAHARFDATARTYKYYVTTAKYPFNRQYRYRVYGSLDYERMNEAARTLFEYIDFTSFSKLHTDVKTNICHISHAEWTKMEGEDTTWVFTIRADRFLRNMVRAIVGTLLEVGRGKLTVEGFRKVIEQQDRCKAGTSAPGNALFLVNVEYPEDIFSEETKKSVLSTLLPEGGEC | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q89ZY4 |
Q186R1 | THIG_CLOD6 | Thiazole synthase | Clostridioides | MDKLVLGGHEFNSRLLVGTGKYGSNNILPEVIKESGSEIITMALRRVDLDNKQENILTYIPKEMTILPNTSGATNAEEAVRIARISRKMGCGDFIKIEVISDTRYLLPDNEETIKATKILADEGFIVLPYMTPDLYAGRRLIEANAAAVMPLGAPIGSNRGLQMKEMIRIMIDELDIPIIVDAGIGKPSQAMEAMEMGADAVLVNTAIASAGDPVQMARAFKLAVEGGREAYIAKTGNVSEFANASSPLTGFLGNL | 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. | Q186R1 |
Q4CNL4 | TRM51_TRYCC | tRNA methyltransferase 5 homolog 1 | Schizotrypanum | MSGEERHQGKGEKGPMDHDEPPSYRTRVEASVELMALRVKPVHLLGEVLKALRGCLYDMRGVRNVMDAPQPTSDPGEAHKLLLLDPQVIPPPSPAAKNASTAPTQPLWVEANHASVPPVVRERLQSFLLGKRSVAQSLRVAVAQHIVRLSHRNFTMPELLQRILPPGTIPLSGFEQVGHIAHVNLSAAHLPYRADIGAVILDCNPTVRVVVNKVDNIASVFREFKMEVIARRTTHSDMKGSPAEENSGDEEKLHRLLLATVRQHGCIFRVPYDRVYWNSRLSHEHARVVGMMQSGDMLYDAMAGVGPFAIPAAVAGVKTYANDLNPVAAEYLRINAELNHINKDTFHVFNMDGREFLNTVLYRDVVSGAAVCGRRHVTMNLPAMAVEFLDVFTKPPWSQPLVSLSLLEEKEKAKEGKEKEEHVEMHPDKRVLFHVYCFSKNMDDFLGDAVKQVERWLAFSLAGENLEAVHMVRDVAPLKRMVCVSFTLPEAFWLHREAKGMSPLKRARSD | 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. | Q4CNL4 |
Q1W5S8 | TPRA3_MAIZE | Protein RAMOSA 3 | Zea | MTKHAAYSSEDVVAAVAAPAPAGRHFTSFQALKGAPLDCKKHAAVDLSASGAAVVGGGPWFESMKASSPRRAADAEHGDWMEKHPSALAQFEPLLAAAKGKQIVMFLDYDGTLSPIVEDPDRAVMSEEMREAVRRVAEHFPTAIVSGRCRDKVLNFVKLTELYYAGSHGMDIQGPAACRQPNHVQQAEAAAVHYQAASEFLPVIEEVFRTLTAKMESIAGARVEHNKYCLSVHFRCVREEEWNAVNEEVRSVLREYPNLKLTHGRKVLEIRPSIKWDKGKALEFLLKSLGYAGRNDVFPIYIGDDRTDEDAFKVLRNMGQGIGILVSKLPKETAASYSLSDPAEVKEFLRKLANKKGARQP | Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Is specific for trehalose 6-phosphate. Does not possess activity toward glucose, sucrose or fructose 6-phosphates. Regulates inflorescence branching. Required to establish the correct identity and determinacy of axillary meristems in both male and female inflorescences. May act through a sugar signal that moves into axillary meristems. Acts upstream of RA1. May have a transcriptional regulatory function. | Q1W5S8 |
P0CH17 | U6A_CONPI | Conotoxin pr6a | Phasmoconus | TCLARDELCGASFLSNFLCCDGLCLLICV | Intraperitoneal injection into fish (1 nmol) provokes hyperactivity and erratic swimming in various directions after 14 min. | P0CH17 |
P50260 | TBB2_OOMCK | Beta-2-tubulin | Stramenopiles | DEHGVDPTGTYHGDSDLQLERINVYYNEATGGRYVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKIREEYPDRVMLTFSVCPSPKVSDTVVEPYNATLSVHQLVENADEVMVLDNEALYDICFRTLKLTTPTYGDLNHLVCACMSGVTSCLRFPGQLNSDLRKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQQFDAKNMMCAADPRHGRYLTASCMFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLKMSACFIGNSTAIQEMFKRIGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEYDEDEDDEGGDYA | 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. | P50260 |
B3PCK0 | THIC_CELJU | Thiamine biosynthesis protein ThiC | Cellvibrio | MNTSVDKILSQTAEVDQASVQPFTGSQKIYVQGSRNDIRVPMREISLDDTPTDFGGEKNPPVRVYDTSGPYTDPEVAIDLRAGLPDIRSAWIEERGDTEILSDSQSIFTRERLDDPKLAHLRFNLTRKARRAKPGMNVSQMHYAKKGIITPEMEYIAIRENMALAQVRELGVLNQQHPGMSFGANIPGEITPEFVRSEVARGRAIIPANINHVELEPMIIGRNFLVKINGNIGNSALGSSIEEEVEKLTWGARWGADTVMDLSTGKNIHETREWIIRNSHVPIGTVPIYQALEKVNGIAENLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHRENFLYTHFEEICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTEIAWKHDVQTMIEGPGHVPMHMIKENMDKQLEVCKEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWYGCAMLCYVTPKEHLGLPNKKDVKEGIITYKIAAHAADLAKGHPGAQLRDNALSKARFEFRWEDQFNLGLDPDTARAYHDETLPKESAKVAHFCSMCGPKFCSMKITQEVRDYAAQQGVNVEGISEDQLVKMIDVEAEMQEKAREFIEQGAELYHKV | 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. | B3PCK0 |
Q9SSP5 | THRC2_ARATH | Threonine synthase 2, chloroplastic | Arabidopsis | MASFSLPHSATYFPSHSETSLKPHSAASFTVRCTSASPAVPPQTPQKPRRSPDENIRDEARRRPHQLQNLSARYVPFNAPPSSTESYSLDEIVYRSQSGALLDVQHDFAALKRYDGEFWRNLFDSRVGKTNWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQYLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRKMNKPVIGVGCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPLYLHYKSGFKEDFNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATALADSTGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLKFTQSKIDYHSKNIKEMACRLANPPVKVKAKFGSVMDVLKEYLKSNDK | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. | Q9SSP5 |
P05467 | YKP1_KLULA | Uncharacterized killer plasmid pGKl-2 protein 1 | Kluyveromyces | MSYIDYLAYTGNTTFYDRFDGDLTSEHRIKCIINGCLINIMFSIRTIKEFPEEIKICQAAVSKFLTCGYVNDYLIEKYPPFYLWHKRFCDYDIYKMLMEKHPKLNYTVAKAAIMQRYNDLYFSFDFQPEEELIMTAALTENTEIYEDQINKAKKLGYCYSYLDYDNYCIKEEPGIEEIPDIEPKFNPFYVYVESGSKMEDVEYAVVNLVEEFKYLQMVYDMSKI | 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. | P05467 |
A1TWN4 | TSAC_MARN8 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Marinobacter | MADTSSPSFLQLALARQTVLAGGVIAYPTEAVWGLGCDPWNREAVEYILELKQRPMEKGVILVAASVEQVRFLLDPLPDAVQSEALRHWPGPVTCLLPDVNQQVPEWVRGKHSSIAVRVSDHPVVRALCEATGMPLVSTSCNPAGRQPARAIWQVRRYFGDRIDRIVPGALGGNRKPSRIIDIVTGQQFR | 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. | A1TWN4 |
Q1C2S1 | TAUB_YERPA | Taurine import ATP-binding protein TauB | Yersinia | MLNVSGLWAEYQGKPALQDVSLQIASGQLVVVLGPSGCGKTTLLNLIAGFMTPSAGVITLDNIPVSGPSAERGVVFQNEGLLPWRDVVSNVEFGLQLAGMSKEQRRVTALKMLNRVGLAGFEHHFIWQLSGGMRQRVGIARALAVDPRLLLLDEPFGALDAFTREQMQELLLTIWRDTGKQILLITHDIEEAVFLASELLLLSPGPGQVVERLSLNFGQRYAEGEPCRAIKSDPEFIARREDVLGKVFQQREVLI | Part of the ABC transporter complex TauABC involved in taurine import. Responsible for energy coupling to the transport system. | Q1C2S1 |
Q6GCM3 | TARI2_STAAS | Ribitol-5-phosphate cytidylyltransferase 2 | Staphylococcus | MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNITDQRVKVVAGGTDRNETIMNIIDYIRNVNGINNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDSYRALSSAQKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q6GCM3 |