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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|---|---|---|---|---|---|---|
P02591 | TNNC1_RABIT | Troponin C, slow skeletal and cardiac muscles | Oryctolagus | MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE | 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. | P02591 |
A6ZYC3 | TRM82_YEAS7 | Transfer RNA methyltransferase 82 | Saccharomyces | MSVIHPLQNLLTSRDGSLVFAIIKNCILSFKYQSPNHWEFAGKWSDDFDKIQESRNTTAKEQQGQSSENENENKKLKSNKGDSIKRTAAKVPSPGIGAPPIYSYIRNLRLTSDESRLIACADSDKSLLVFDVDKTSKNVLKLRKRFCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFTQEPILGHVSMLTDVHLIKDSDGHQFIITSDRDEHIKISHYPQCFIVDKWLFGHKHFVSSICCGKDYLLLSAGGDDKIFAWDWKTGKNLSTFDYSSLIKPYLNDQHLAPPRFQNENNDIIEFAVSKIIKSKNLPFVAFFVEATKCIIILEISEKQKGDLALKQIISFPYNVISLSAHNDEFQVTLDNKESSGVQKNFAKFIEYNLNENSFVVNNEKSNEFDSAIIQSVQGDSNLVTKKEEIYPLYNVSSLRKHGEHYS | Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. | A6ZYC3 |
Q3YW59 | ZNTA_SHISS | Zn(2+)/Cd(2+)/Pb(2+) export ATPase | Shigella | MSTPDNHGKKAPQFAAFKPLTTVQNANDCCCDGACSSSPTLSENVSGTRYSWKVSGMDCAACARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESAVQKAGYSLRDEQAADEPQASRLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARQALRLIKSGSYFAIETLMSVAAIGALFIGATAEAAMVLLLFLIGERLEGWAASRARQGVSALMALKPETATRLRNGEREEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGDKVPAGATSVDRLVTLEVLSEPGASAIDRILKLIEEAEERRAPIERFIDRFSRIYTPAIMAVALLVTLVPPLLFAASWQEWIYKGLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKGGAALEQLGRVTQVAFDKTGTLTVGKPRVTAIHPATGISESELLTLAAAVEQGATHPLAQAIVREAQVAELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHPADAFAGLINELESAGQTVVLVVRNDDVLGIIALQDTLRADAATAISELNALGVKGVILTGDNPRAAAAIAGELGLEFKAGLLPEDKVKAVTKLNQHAPLAMVGDGINDAPAMKAAAIGIAMGSGTDVALETADAALTHNHLRGLVQMIELARATHANIRQNITIALGLKGIFLVTTLLGMTGLWLAVLADTGATVLVTANALRLLRRR | Confers resistance to zinc, cadmium and lead. Couples the hydrolysis of ATP with the export of zinc, cadmium or lead. | Q3YW59 |
Q57NL6 | TREA_SALCH | Alpha,alpha-trehalose glucohydrolase | Salmonella | MIPPEIRRSVLLQKAIKLALAGTLLTFASFSATAADPSSDTETPQPPDILLGPLFNDVQNAKLLPDQKTFADAIPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKAGEKYVPPAGQSLREHIDGLWPVLTRSTKNVKKWDSLLPLPESYVVPGGRFREIYYWDSYFTMLGLAESGHWDKVADMVANFGYEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKEYLPQLQKEYAYWMEGVETLQPGQQNQRVVKLEDGSVLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLSTIRTTTIVPVDLNALLYQLEKTLARASAAAGDRAKASQYDALANARQKAIEMHLWNNKEGWYADYDLQNNKIRDQLTAAALFPLYVNAAAKDRAAKVAAAAQAHQLQPGGLATTSVKSGQQWDAPNGWAPLQWVAAEGLQNYGQDDVAMEVTWRFLTNVQHTYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPQEKPCDSVPSTRPASLSATPTKTPSAATQ | Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system. | Q57NL6 |
A0A343URW7 | TEX2_CATRO | Cytochrome P450 71D347 | Catharanthus | MEFVVSPFAFLIFFFILLKMIAKNFKNPKKNTKPLPPGPKKLPIIGNLHQLGGGLAHHILRDLSQNYGPLMHLKIGELSTIVISSTEMAKQVFKVHDIHFSNRPSHILVFKIVSYDYKDIVLSQYGNYWRELRKVCNLHLLSPNRVQSFRFIREDSVLNMMKSISSNEGKVVNLSEMILSLIYGITARAAFGVWSKRHEEFIRLESEIQRLATTFVLADMFPSIKILGALSGLRYKVEKVHKKVDEILEDILKEHRNNNISIEKEEEEEEENNGGKKDLVDVLLDIQKNGEMETPFTDQHIKAIIFDMFSAGTLTSTIAVDWAMAEMMKNPRVMKRAQEEVRNVYNGIGNVNESKLDELKYLQAIIKETLRIHPGTPIVHRETREECEINGYRIPAKARVMVNAWAISRDPNYWPDPDSFKPERFLGSEVDFKGTHFEYTPFGAGRRICPGISYAIANIQLPLAQLLYHFDWKLAGGMKPEELDMAEILGTAAQRKEDLLLIPNSHSCSSLKQQV | Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications . Cytochrome P450 catalyzing the conversion of tabersonine to lochnericine . | A0A343URW7 |
P83949 | UBX_DROME | Homeotic protein ultrabithorax | Sophophora | MNSYFEQASGFYGHPHQATGMAMGSGGHHDQTASAAAAAYRGFPLSLGMSPYANHHLQRTTQDSPYDASITAACNKIYGDGAGAYKQDCLNIKADAVNGYKDIWNTGGSNGGGGGGGGGGGGGAGGTGGAGNANGGNAANANGQNNPAGGMPVRPSACTPDSRVGGYLDTSGGSPVSHRGGSAGGNVSVSGGNGNAGGVQSGVGVAGAGTAWNANCTISGAAAQTAAASSLHQASNHTFYPWMAIAGECPEDPTKSKIRSDLTQYGGISTDMGKRYSESLAGSLLPDWLGTNGLRRRGRQTYTRYQTLELEKEFHTNHYLTRRRRIEMAHALCLTERQIKIWFQNRRMKLKKEIQAIKELNEQEKQAQAQKAAAAAAAAAAVQGGHLDQ | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds the consensus region 5'-TTAAT[GT][GA]-3'. This homeotic protein controls development of the cells in the posterior thoracic and first abdominal segments. It activates the synthesis of the decapentaplegic (DPP) growth factor. | P83949 |
Q555E8 | Y4669_DICDI | Very-long-chain 3-oxoacyl-CoA synthase DDB_G0274669 | Dictyostelium | METVQSIITEWTDPKSWEKLVQHSFKDSNWKELIDPVNYKFNFGVTPFSQFQIIPIVLVIYLVTIFSIKFLMKNRKPFSLKFISILHNAILCIWSLIMCVGVLYEIIKRVSNEGPLFTVCEDPNGGFDKGVTYYWSYIFYISKFYELLDTVIIVLKKKPLIFLHVYHHCKTVWWKKYITMIQILQFVCLGIAGVLHVYTINTIGCFTHYPAFAAAYSINFSFLFLFSKFFVKSYTPKNSNSNTNIKSKKID | Could be implicated in synthesis of very long chain fatty acids. | Q555E8 |
P23822 | YAML_STRVL | Uncharacterized HTH-type transcriptional regulator in aml 5'region | Streptomyces | GDVSVVGFDDSPLIAFTSPPLSTVRQPVQAMATAAVGALLEEIEGNPVQRTEFVFQPELVVRGSTAQPPGRVSQVLS | Putative sugar-binding regulatory protein for the alpha-amylase gene. | P23822 |
Q63SA4 | UVRC_BURPS | Excinuclease ABC subunit C | pseudomallei group | MTSPDAPESRFEPKPILAQLPHLPGVYRYYDAQDAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMITRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTGHRFPRMAYYRGAVDKKNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCSAPCVGAIGEEDYARDVDNASRFLLGRQGEVMGELERKMHAFAAELKFEQAAAVRNQMSSLAKVLHQQAIDVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPAHVETALALAGDIEALAGEGAGDGVQAAQAPLATDADATDAAATEAKTVTAAAAARAGARTAQAAGARAAASAEGDVERRAEGETHARADAREAAALPDGAAAAQEADADVDAAPLETEVLEAFIAQHYLGNRVPPVLVVSHAPANRELIDLLVEQAGHKVAVVRQPQGQKRAWLTMAEQNARLALARLLSEQGSQQARTRSLADVLGYESDDLAQLRIECFDISHTMGEATQASCVVYHHHRMQSSEYRRYNIAGITPGDDYAAMRQVLTRRYEKMVEEAAAEASADEAAGIDGNAVHAAASAGRLPNVVLIDGGRGQVEIARQVFSELGLDISMLVGVAKGEGRKVGLETLIFADGRAPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKTRQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVDELASVEGISRALAEQIYRQLH | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q63SA4 |
Q7VRC9 | TILS_BLOFL | tRNA(Ile)-lysidine synthetase | Candidatus Blochmannia | MNSTNFFSHDLYLYHQVIRCIVKYRNLLLAYSGGMDSTVLLDILTKLKKYFDFQVKGTSKILPFFLRAVYVHHGLNNKADYWADHCLQQCKMRNVPFHIIYINHSDLSKIKCNIEAMARDFRYKALFNALKPEEVLLTAHHMNDQVETVLLALKRGSGPAGLSGMTQDILYQHNEYQHRLLRPLLKCSHIQLQEYAYRKKLTWVEDDTNTDVRFDRNFLRVQVIPLFQKRWPAFNKVVSRTAQLCREQENLLHELLSESLDQLIDIDNALFFYPLIKYSDVRRRVVLRYWLSRFFINMPSYKLLDCIWKEVALSKVDSQSILHVGKKYICRRFRKKLYILPDNMKSSLDIFLLPWKNFNNTILLPNELGLLTSQSLTVNLFLFYKNLIPYTHLNMLSDIFLPRYHNNVGDEKILSVCFIRPPMNNEKVSIQFGYIQGLLHLANRDRGRKLKKIWQEYNVPPWLRNHIPLLFYNDTLISAIGIFITRNGSCIVNMNNLICNNKKSIILQKITWVQSDFYYRIFKNFVYNTLR | 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. | Q7VRC9 |
B0TY94 | Y120_FRAP2 | Nucleoid-associated protein Fphi_0115 | Francisella | MNFDMSKLMQQAQKMQEQMKKAQQERENMEVIGESGAGLVSVTMTGKYDVKKVTIDDSLMSEDKEMLEDLIAAAVNSAVKKVEDSSSSADIGKMAKEAGIDLPNGFNFPFK | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | B0TY94 |
P70906 | VLP18_BORHE | Variable large protein 18 | Borrelia | MRKRISAIINKLNISIMMMIVVLMIGCGQQAVEAGKDGARAATGGRSLSEVLMEVGKSAENAFYSFMALVSDTLGLRVTKDTKKNEVGGYFNSLGGKLGKASDELEEVAKKSEVEGAKDGPIAVAIRAAVDTAKTTLSTLKGHLESLKGIGDDKVVGWAENDQQGIKPADDGLNKFLNALQSIVKAATDAGVLAPKAGNTTLTVNGVDNKDGAKVLAIDKPGAAVGEKASLIVSAVSGEEILASIVASKEGDQALGAAADGTTTAMSFAKGGTKDNLSNANTPKAAAVAGGIALRSLVKDGKLASHNDNSEKAVQAAGVIAANKLLVSVEDLIKKTVKNVLEKAKEKIDKARAPKATGQQ | The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. | P70906 |
Q8N4W9 | ZN808_HUMAN | Zinc finger protein 808 | Homo | MLREEAAQKRKGKESGMALPQGRLTFRDVAIEFSLAEWKFLNPAQRALYREVMLENYRNLEAVDISSKHMMKEVLSTGQGNREVIHTGTLQRHQSYHIGDFCFQEIEKEIHNIEFQCQEDERNGHEAPTTKIKKLTGSTDQHDHRHAGNKPIKDQLGSSFYSHLPELHIFQIKGEIANQLEKSTSDASSVSTSQRISCRPQIHISNNYGNNPLNSSLLPQKQEVHMREKSFPCNESGKAFNCSSLLRKHQIPHLGDKQYKCDVCGKLFNHKQYLACHRRCHTGEKPYKCKECGKSFSYKSSLTCHHRLHTGVKPYKCNECGKVFRQNSALVIHKAIHTGEKPYKCNECGKAFNQQSHLSRHQRLHTGVKPYKCKICEKAFACHSYLANHTRIHSGEKTYKCNECGKAFNHQSSLARHHILHTGEKPYKCEECDKVFSQKSTLERHKRIHTGEKPYKCKVCDTAFTCNSQLARHRRIHTGEKTYKCNECRKTFSRRSSLLCHRRLHSGEKPYKCNQCGNTFRHRASLVYHRRLHTLEKSYKCTVCNKVFMRNSVLAVHTRIHTAKKPYKCNECGKAFNQQSHLSRHRRLHTGEKPYKCEACDKVFGQKSALESHKRIHTGEKPYRCQVCDTAFTWNSQLARHTRIHTGEKTYKCNECGKTFSYKSSLVWHRRLHGGEKSYKCKVCDKAFVCRSYVAKHTRIHSGMKPYKCNECSKTFSNRSSLVCHRRIHSGEKPYKCSECSKTFSQKATLLCHRRLHSGEKPYKCNDCGNTFRHWSSLVYHRRLHTGEKSYKCTVCDKAFVRNSYLARHIRIHTAEKPYKCNECGKAFNEQSHLSRHHRIHTGEKPYKCEACDKVFSRKSHLKRHRIIHTGEKPYKCNECGKAFSDRSTLIHHQAIHGIGKFD | May be involved in transcriptional regulation. | Q8N4W9 |
B5XXK0 | TRHO_KLEP3 | tRNA hydroxylation protein O | Klebsiella | MPVLHNRISNETLKAQMLAETEPRTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPESNVEALREFLYGFDPALAGLRFNIALEDDGKSFWVLRLKVRDRIVADGIDDPSFDASNVGDYLKAADVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGLPVRFIGKNFVFDERMGERISDDVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAGCCSEACVEEHKLPEEEQRKLRAGRENGNKIFNKSRGRLNTKLGIPEPESSEKP | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | B5XXK0 |
Q9D516 | YJU2B_MOUSE | Coiled-coil domain-containing protein 130 | Mus | MGERKGQNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILVIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGASRKEERWDMEDNEQVLTTEHEKKEKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQNAWKDDFALNSMLRRHFREKKKAMQEEEEKDQALQAKASLAIPLVPESEDDRRLAALLRLHTLDSYEDKQRMKRTEIIHRSWFPSAQGPSASSSKASSVLKKLCQGRRPPPSSTGTVGDLGIVRRKSRDVPESPQCAADNSLSEEQRRPPGTTQGSKTLEEAAEASRTSKTSESKRNCSDQAFPLGSSQEDLLNPNTPNASLVADYSDSESE | May be involved in mRNA splicing. | Q9D516 |
P0C184 | ULAA_SHISS | Ascorbate-specific permease IIC component UlaA | Shigella | MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWTAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSSLIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. | P0C184 |
B5ZTC5 | TSAD_RHILW | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Rhizobium | MVPFLRILGIETSCDETAAAVVERDAEGNARVLSDVVLSQLDEHSAYGGVVPEIAARAHVEALDELIEEALNRANVSLDEVDAIAATSGPGLIGGLLVGLMTGKAIARAAGKPLYAVNHLEGHALTARLTDGLAFPYLMLLVSGGHTQLILVRGVGEYQRWGTTIDDALGEAFDKTAKLLGLPYPGGPAVERMARDGNPDRFAFPRPLVGEARLDFSFSGLKTAVRQAAQDIAPISDQDVADICASFQKAISRTLKDRIGRGLQRFKTEFAATDEKPALVVAGGVAANLELRGTLQALCDKNGFRFIAPPLHLCTDNAVMIAWAGLERMATGAAPDPLDVQPRSRWPLDSNAETLIGFGKRGAKA | 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. | B5ZTC5 |
A8GA20 | TRMD_SERP5 | tRNA [GM37] methyltransferase | Serratia | MFIGIVSLFPEMFRAITDYGVTGRAVKNGLLSVQCWSPRDFTYDRHRTVDDRPYGGGPGMLMMVQPLREAIHAAKAAAGEGAKVIYLSPQGRKLDQTGVCELAANPKMILVCGRYEGVDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVARFIPGVLGHQASAEEDSFADGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLESLALTDEQAVLLAEFQREHQTKQQDYEGNV | Specifically methylates guanosine-37 in various tRNAs. | A8GA20 |
A5F888 | TTCA_VIBC3 | tRNA 2-thiocytidine biosynthesis protein TtcA | Vibrio | MTAQTQELTKAQQYNFNKLQKRIRRNTGQAIADFNMIEDGDRIMVCLSGGKDSFTMLDILMSLQKSAPISFELVAVNLDQKQPGFPEHVLPEYLDSLGVEYKIVEEDTYSIVQDKVPEGKTTCALCSRLRRGILYRTAKELGATKIALGHHRDDILETLFLNMFYGGKMKGMPPKLVSDNGEHVVIRPLAYCREKDIIKYSDMRGYPIIPCNLCGSQPNLQRQAVKQMLNDWDKRFPGRIETMFRAMQNVVPSHLADFSLFDFKSIDKNSGVINGGDIGFDKEEIAPQVVEDEDLVMEFDPSLQLNVTNI | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | A5F888 |
Q0E3I9 | URED_ORYSJ | Urease accessory protein D | Oryza sativa | MEAEAAMEAEAAPAAATGAVRVEKVRGRSAVTRCFAKYPLKLIAPSKAGRASSGAAWLYAITYGGGIVSGDIISCTVAVGDGCAAAMTTQASTKVYKAVDSKCSEQVLEARVGEDALFALIPDPVTCFSMARYHQKQVFHVFPNSNLVVVDWFTSGRYESGEKWNFSFYKSINHILLEDQPLFIDSVLLEQSSNFSIADRMQEYNVVAMVILLGPKLKHIQDQMQDEVKKMMSVQLRPPTSAGGRYSTRSQPLHPQRPPIIASCSPFGRMGTGMVARITAVSTESVYSFLRHHLAALEPFLGACPYPAS | Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter. | Q0E3I9 |
Q6GK63 | TARI2_STAAR | Ribitol-5-phosphate cytidylyltransferase 2 | Staphylococcus | MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNITDQRVKVVAGGTDRNETIMNIIDHIRNTQGINDDDVIVTHDAVRPFLTQRIIKENIEVAAKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDSYRALSSAQKEILSDACKIIVESGHAVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q6GK63 |
A9BXA7 | TATA_DELAS | Sec-independent protein translocase protein TatA | Delftia | MGSFSIWHWLIVLAIVVLVFGTKKLKNIGSDLGGAVKGFKDGVKDGSTSTDTPAAAPGQVAGQTAADKTTIDVEAKQKG | 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. | A9BXA7 |
O97162 | TPM_RHIMP | Tropomyosin | Boophilus | MEAIKKKMQAMKLEKDNAVDRAETAEQQSREAALRAEKAEEEVRSLQKKIQQIENELDQVQEQLSQANSKLEEKDKALQAAEAEVAAHNRRIQLLEEDLERSEERLKIATQKLEEASQAADESERMRKMLEHRSITDEERMDGLEGQLKEARTMAEDADRKYDEVARKLAMVEADLERAEERAETGETKIVELEEELRVVGNNLKSLEVSEEKALQKEETYEMQIRQMTNRLQEAEARAEFAERSVQKLQKEVDRLEDELVQEKEKYKAISDELDQTFSELTGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | O97162 |
P18115 | THAB_XENLA | Nuclear receptor subfamily 1 group A member 1-B | Xenopus | MDQNLSGLDCLSEPDEKRWPDGKRKRKNSQCMGKSGMSGDSLVSLPPAGYIPSYLDKDEPCVVCSDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYDGCCIIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEENRVRRRKEEMIKTLQQRPEPSSEEWELIRIVTEAHRSTNAQGSHWKQRRKFLPEDIGQSPMASMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELTCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLSGEMAVKREQLKNGGLGVVSDAIFDLGRSLAAFNLDDTEVALLQAVLLMSSDRTGLICTDKIEKCQETYLLAFEHYINHRKHNIPHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFEDQEV | High affinity receptor for triiodothyronine (T3). | P18115 |
Q3YUF6 | ULAR_SHISS | HTH-type transcriptional regulator UlaR | Shigella | MTEAQRHQILLEMLAQLGFVTVEKVVERLGISPATARRDINKLDERGKLKKVRNGAEAITQQRPRWTPMNLHQAQNHDEKVRIAKAASQLVNPGESVVINCGSTAFLLGREMCGKPVQIITNYLPLANYLIDQEHDSVIIMGGQYNKSQSITLSPQGSENSLYAGHWMFTSGKGLTAEGLYKTDMLTAMAEQKMLSVVGKLVVLVDSSKIGERAGMLFSRADQIDMLITGKNANPEILQQLEAQGVSILRV | Represses ulaG and the ulaABCDEF operon. | Q3YUF6 |
P28128 | WNT5A_MELGA | Protein Wnt-5a | Meleagris | SGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMKLNSRGKLVQMNSRFNAPTIHDLIYIDPSPDYCMRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVERERCNCKF | 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. | P28128 |
B6ENU2 | UBIA_ALISL | 4-HB polyprenyltransferase | Aliivibrio | MTLSKAKAFWQLTRMNRPIGSLLLLWPTLWALFLAADGIPDWHVLIVFILGVVFMRSAGCVINDFADRKVDGHVKRTANRPLPSGLVSSKEALILFSVLVTCSFILVLTMNTLTIMLSSIGVLLAIAYPFMKRITYLPQFVLGLAFSWAIPMAYAAESNQVPPEAWLLFVINAVWTIAYDTQYAMVDRDDDLNIGIKSTAILFGRFDKLMIGLLQLTVLTLLIALGIQLSLPSLYNWGVLAAAGCFVYQQWLIKGREREACFEAFLNNNYVGGFIFVAISASVLI | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. | B6ENU2 |
Q5QUY5 | UPPP_IDILO | Undecaprenyl pyrophosphate phosphatase | Idiomarina | MDFLQSIILGIIQGITEFLPISSSAHLILMPILTGWDDQGVGFDLAVHVGTLLAVILYFRKDVSELFIDGLRSIAARQHVGQSRLGWAVVVGTIPACIAGILLLDYIDTALRAVGVIITTTVVFAVLLAAGDRFARGSRTLQDIGFKDAIIVGLAQAVALIPGTSRSGATITAGLFLGLNRESASKFSFFMAIPITAAAALVKLLTIASESIAVDWLGFLVGGIVSFLTAITAIHFFLKWLNAFGMWPYVIYRLVLAVVLYLLFF | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q5QUY5 |
D3UAG1 | U7A16_PYRCO | UDP-glucose:flavonol 2'-O-glucosyltransferase | Pyrus | MKRSAQLVFVPAPGIGHIVSTVEMAKQLVARDDQLFITVLVMKLPYDQPFTNTDSSISHRINFVNLPEAQLDKQDTVPNPGSFFRMFVENHKTHVRDAVINLLPESDQSESTSKPRLAGFVLDMFSASLIDVANEFEVPSYVFFTSNSSTLALLSHFQSLRDEGGIDITELTSSTAELAVPSFINPYPVAVLPGSFLDKESTKSTLNNVGRYKQTKGILVNTFLELESHALHYLDSGVKIPPVYPVGPLLNLKSSHEDKGSDILRWLDDQPPLSVVFLCFGSMGSFGDAQVKEIACTLEHSGHRFLWSLRQPPSKGKRALPSDYADLKTVLPEGFLDRTATVGRVIGWAPQAAILGHPAIGGFVSHCGWNSTLESIWNGVPIAAWPMYAEQNMNAFQLVVELGLAVEIKMDYRKDSDVVVSAEDIERGIRQVMELDSDVRKRVKEMSEKSKKALVDGGSSYSSLGRFIDQI | Glycosyltransferase that possesses chalcone and flavonol 2'-O-glycosyltransferase activity. Converts phloretin to phlorizin (phloretin 2'-O-glucoside), a potent antioxidant. Possesses glycosyltransferase activity toward eriodictyol, apigenin, luteolin, kaempferol, quercetin, isoliquiritigenin, butein and caffeic acid. | D3UAG1 |
Q5RJW4 | UFM1_XENLA | Ubiquitin-fold modifier 1 | Xenopus | MSKVTFKITLTSDPRLPYKVLCVPENTPFTAVLKFAAEEFKVPAATSAIITNDGIGLNPAQTAGNVFLKHGSELRLIPRDRVGSC | Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the ufm1-activating E1 enzyme uba5, the ufm1-conjugating E2 enzyme ufc1, and the ufm1-ligase E3 enzyme ufl1. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. | Q5RJW4 |
Q92SX1 | Y231_RHIME | Nucleoid-associated protein R00231 | Sinorhizobium | MRDIMGMMGKVKEMQAKMEKMQAEIAALEIDGTSGGGLVTVRLDGKGHMKSLKVDPSLFKEDDVEILEDLIVAAHKDAKDKAEAVQAEKTRELTAGLPIPPGMKLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q92SX1 |
P75859 | YCBU_ECOLI | Uncharacterized fimbrial-like protein YcbU | Escherichia | MKKKTIFQCVILFFSILNIHVGMAGPEQVSMHIYGNVVDQGCDVATKSALQNIHIGDFNISDFQAANTVSTAADLNIDITGCAAGITGADVLFSGEADTLAPTLLKLTDTGGSGGMATGIAVQILDAQSQQEIPLNQVQPLTPLKAGDNTLKYQLRYKSTKAGATGGNATAVLYFDLVYQ | Part of the elfADCG-ycbUVF fimbrial operon, which promotes adhesion of bacteria to different abiotic surfaces. | P75859 |
A0QRF3 | URED_MYCS2 | Urease accessory protein UreD | Mycolicibacterium | MKLAERTAADLRFARAGAHTVLTRRRHRWPFVIGRVFADPQDPGLGTLTLQNAAGTVIPGDVIRQRIEVVDGGRAAVNGQGATLISGVPGGDASAEETELYVDAHSWLRFDPAPRILTAHARHRQRTEVCVAHRGCAVVVDAVVLHPDLDAATFGSIESTVTVRSPGGALLAMDAQVLDAPPVTGRFTAFGTVYFVGAGFTGGHHEGPTDPPGVYTAVTELPNGAGCAVRIAAADGGTLRTYLRLLSAETAFQRASTRTFTDGMPFRRSQV | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A0QRF3 |
P68420 | TXH6_CYRSC | Huwentoxin-VI | Cyriopagopus | NCIGEQVPCDENDPRCCSGLVVLKKTLHGIWIKSSYCYKCK | Intracerebroventricular injection paralyzes mice. Has no effect on voltage-gated sodium currents. | P68420 |
F8WKW8 | UGT9_GARJA | UDP-glycosyltransferase 94E5 | Gardenia | MFPWLAYGHISPYLELAKRLTDRGFAIYICSTPINLGFIKKRITGKYSVTIKLVELHLPDTPELPPHYHTTNGLPPHLMATLKRALNGAKPELSNILKTLKPDFVIYDATQTWTAALTVAHNIPAVKFLTSSVSMLAYFCHLFMKPGIEFPFPAIYLSDFEQAKARTAAQDARADAEENDPAAERPNRDCDSIFLVKSSRAIEGKYIDYLFDLMKLKMLPVGMLVEEPVKDDQGDNSNELIQWLGTKSQRSTVLVSFGTEYFLTKEEMEEIAHGLELSEVNFIWVVRFAMGQKIRPDEALPEGFLERVGDRGRIVEGWAPQSEVLAHPSTGGFICHCGWNSVVESIEFGVPVIAMPMHLDQPLNARLVVEIGAGMEVVRDETGKFDRKEIARAIKDAMVEKTGENTRAKMLDVKGRVELKEKQELDEVAELLTQLVTETTQSSN | Glucosyltransferase catalyzing the beta 1-6 glucosylation of the sugar moiety of crocetin glucosyl esters to produce crocetin gentiobiosyl esters. Weak activity toward curcumin glucosides, but no activity with flavonoid glucosides, coumarin glucosides, 4-nitrophenyl glucoside or crocetin. Involved with UGT75L6 in sequential glycosylation of crocetin to crocin (bis(beta-D-gentiobiosyl) crocetin). | F8WKW8 |
P69424 | TATC_ECO57 | Sec-independent protein translocase protein TatC | Escherichia | MSVEDTQPLITHLIELRKRLLNCIIAVIVIFLCLVYFANDIYHLVSAPLIKQLPQGSTMIATDVASPFFTPIKLTFMVSLILSAPVILYQVWAFIAPALYKHERRLVVPLLVSSSLLFYIGMAFAYFVVFPLAFGFLANTAPEGVQVSTDIASYLSFVMALFMAFGVSFEVPVAIVLLCWMGITSPEDLRKKRPYVLVGAFVVGMLLTPPDVFSQTLLAIPMYCLFEIGVFFSRFYVGKGRNREEENDAEAESEKTEE | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. | P69424 |
Q9LKG7 | UGPA_ASTPN | UDP-glucose pyrophosphorylase | Astragalus | MATATATDRLSNLKSSVAGLNQISENEKSGFINLVARYLSGEAQHVEWSKIQTPTDEVVVPYDTLAPTPDGSLEIKNLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNSKYGSNVPLLLMNSFNTHDDTQTIVEKYQNSNIEIHTFNQSQYPRLVVDDFLPLPSKGRTDKDGWYPPGHGSMFPSLSNSGKLDALISQGKEYVFVANSDNLGAIVDLKILNHLVAHKNEYCMEVTPKTLADVKGGTLISYEGRVQLLEIAQVPDEHVGEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDKAIGINVPRSRFLPVKATSDLLLVQSDLYTVENGSVIRNKARTNPENPSIELGPEFKKVSNFLGRFKSIPSIVELDSLKVVGDVWFGTGVILKGKVSIVAKSGVKVEIPDGAVIANKEINGPKDL | Plays a central role as a glucosyl donor in cellular metabolic pathways. | Q9LKG7 |
Q5VIR6 | VPS53_HUMAN | Vacuolar protein sorting-associated protein 53 homolog | Homo | MMEEEELEFVEELEAVLQLTPEVQLAIEQVFPSQDPLDRADFNAVEYINTLFPTEQSLANIDEVVNKIRLKIRRLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVMNVLEHFHKYMGIPQIRQLSERVKAAQTELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANILDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWIKRQLVDYEEKYGRMFPREWCMAERIAVEFCHVTRAELAKIMRTRAKEIEVKLLLFAIQRTTNFEGFLAKRFSGCTLTDGTLKKLESPPPSTNPFLEDEPTPEMEELATEKGDLDQPKKPKAPDNPFHGIVSKCFEPHLYVYIESQDKNLGELIDRFVADFKAQGPPKPNTDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTTTSSGGLTISSLLKEKEGSEVAKFTLEELCLICNILSTAEYCLATTQQLEEKLKEKVDVSLIERINLTGEMDTFSTVISSSIQLLVQDLDAACDPALTAMSKMQWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCVKFANSFIPKFITHLFKCKPISMVGAEQLLLDTHSLKMVLLDLPSISSQVVRKAPASYTKIVVKGMTRAEMILKVVMAPHEPLVVFVDNYIKLLTDCNTETFQKILDMKGLKRSEQSSMLELLRQRLPAPPSGAESSGSLSLTAPTPEQESSRIRKLEKLIKKRL | Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD . Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane . | Q5VIR6 |
A4XIW8 | TRMFO_CALS8 | Folate-dependent tRNA(M-5-U54)-methyltransferase | Caldicellulosiruptor | MRITVIGAGLAGVEAANAITKFGIKVRLYEMKPKKFSPAHKQEGFAELVCSNSLKSKLLTNASGLLKEEMKLFGSIVMEAAYNTQVEAGQALAVDRYLFSEYITKKIKQNPLIEVIHEEVTEVPRDEVVVVSTGPLTTESLLEDISKLCNSKNLYFFDAAAPIVLKDSIDFSKAFFASRYNKGTDDYINCPMTKEEYERFYYELVNAEVIEVKDFERDLLFEGCMPIEEMAKRGIDTIRFGPLKPVGIIDPKTGKMPYAVVQLRKDTQDGRLYNMVGFQTRLKWGEQKRVFRLIPGLENAEFVRYGVMHKNSYINSPQVLTKFLSLKKYPNIFFAGQITGVEGYLESAATGIVAGINAARYVLGRAQITLPPSTCIGALIEYITTPKKDFQPMNANYGIISIDEEIARIKDKEKRKLLIAEKSLSVCREIANQIF | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | A4XIW8 |
Q630Y6 | TAGU_BACCZ | Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU | Bacillus cereus group | MKKKILFWVLGILGVLIIGGGIYAYNVYSSVSNTLKEVHQPLKRDQNNSNVGEKVSKSEPVSILLLGADERGEDKGRSDSLMVITLNPKNNSMKTVSIPRDTYTEIVGKGKSDKINHAYAFGGVDMSVATVENFLNVPINYYIEVNMEGFKDIVDAVGGVDVKNDLEFTQDGHHFAKGNIHLTGDQALAFTRMRKQDPRGDFGRQMRQRQVMQGVIKKGASFSSLTGYGDVLAAIQKNVKTNLTQDQMFDMQKNYKDCLKNSEDIQIPGDGHKAADGIWYYYVPDAAKQDLTNKLRTHLEVTK | 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). | Q630Y6 |
Q9H0E7 | UBP44_HUMAN | Ubiquitin-specific-processing protease 44 | Homo | MLAMDTCKHVGQLQLAQDHSSLNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNTTGDLKLLRRTLSAIKSQNYHCTTRSGRFLRSMGTGDDSYFLHDGAQSLLQSEDQLYTALWHRRRILMGKIFRTWFEQSPIGRKKQEEPFQEKIVVKREVKKRRQELEYQVKAELESMPPRKSLRLQGLAQSTIIEIVSVQVPAQTPASPAKDKVLSTSENEISQKVSDSSVKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEKTRSCKHPPVTDTVVYQMNECQEKDTGFVCSRQSSLSSGLSGGASKGRKMELIQPKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIASQPCLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLLGSQHPNEDADTSSNEILS | Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination. | Q9H0E7 |
O33380 | TYSY_NEIGO | Thymidylate synthase | Neisseria | MKAYLDLMRHVLDNGTDKSDRTGTGTLSVFGYQMRFDLGKGFPLLTTKKLHLRSIIHELLWFLKGDTNIKYLKDNNVSIWDDEWADENGDLGPVYGYQWRSWPAPDGRHIDQIANVVEQIKKNPDSRRLIVSAWNPALVDEMALPPCHALFQFYVADGNLSCQLYQRSADIFLGVPFNIASYALLTMMMAQVCGLEAGEFVHTFGDAHLYRNHFEQAALQLEREPRALPVMKINPEVKDLFAFKFEDFELEGYDPHPHIKAVVSV | 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. | O33380 |
Q8TAF3 | WDR48_HUMAN | p80 | Homo | MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWTLKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVNPMDEEENEVNHVNGEQENRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETESMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST | (Microbial infection) In case of infection by Herpesvirus saimiri, may play a role in vesicular transport or membrane fusion events necessary for transport to lysosomes. Induces lysosomal vesicle formation via interaction with Herpesvirus saimiri tyrosine kinase-interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK, resulting in down-regulation of T-cell antigen receptor TCR. May play a role in generation of enlarged endosomal vesicles via interaction with TIP . In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1 . | Q8TAF3 |
P75806 | YBJG_ECOLI | Undecaprenyl pyrophosphate phosphatase | Escherichia | MLENLNLSLFSLINATPDSAPWMISLAIFIAKDLITVVPLLAVVLWLWGLTAQRQLVIKIAIALAVSLFVSWTMGHLFPHDRPFVENIGYNFLHHAADDSFPSDHGTVIFTFALAFLCWHRLWSGSLLMVLAVVIAWSRVYLGVHWPLDMLGGLLAGMIGCLSAQIIWQAMGHKLYQRLQSWYRVCFALPIRKGWVRD | Overexpression leads to increased undecaprenyl diphosphatase activity and to increased resistance to bacitracin. May have a preferred substrate other than undecaprenyl diphosphate in vivo. | P75806 |
B0TZW0 | XEEP_FRAP2 | L-Xxx-D/L-Glu epimerase | Francisella | MSKIIDIKTSIIKIPLKRTFITAVRSTNHIDSLAVELTLDNGVKGYGVAPATTAITGDTLQGMQYIIREIFAPVILGSDLSDYKQTLELAFKKVMFNSAAKMAIDLAYHDLLAKEQDISVAKLLGAKANSIVTDVSISCGNVAETIQNIQNGVEANFTAIKVKTGADFNRDIQLLKALDNEFSKNIKFRFDANQGWNLAQTKQFIEEINKYSLNVEIIEQPVKYYDIKAMAEITKFSNIPVVADESVFDAKDAERVIDEQACNMINIKLAKTGGILEAQKIKKLADSAGISCMVGCMMESPAGILATASFALAEDITVADLDPLDWVAKDLYSDYITFNEPNIILKDNLKGFGFNL | Catalyzes the epimerization of dipeptides with L-Glu in the second position. Has epimerase activity with L-Ala-L-Glu, L-Pro-L-Glu, L-Val-L-Glu, L-Thr-L-Glu and L-Met-L-Glu (in vitro). | B0TZW0 |
A6VMQ5 | YCIB_ACTSZ | Inner membrane-spanning protein YciB | Actinobacillus | MKQLLEFIPLILFFTVYKLSGIRDAAITLVIATIVQMLILRVKYGKIEKQQVIMGVAVVFFGLLTAYFNEVKYLQWKVTIVYALFAAILLIGQFVFKTPLIRKLLGKEIELPDTAWQKLNLGWAGFFVLCMLVNIYISQYYSEDIWVDFKSFGIIGMTLLATLITGVYIYRYLPKDKD | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A6VMQ5 |
Q8UA66 | UBIG_AGRFC | 3-demethylubiquinone 3-O-methyltransferase | Agrobacterium tumefaciens complex | MSETAQTTVDQSEVDRFSAMAAEWWSPTGKFRPLHKFNPVRLEYIRNRVCENFGRNPKAHRPLEGLRVLDIGCGGGLLSEPVARMGATVVGADPSEKNIGIASTHARESGVSVDYRAVTAEQLQEAGESFDVILNMEVVEHVANVDLFVTTCAKMVRPGGLMFAATINRTLKARALAIFAAENVLRWLPRGTHQYEKLVRPEELERPIVASGMDIIHRTGVFYNVLQDRWNLSPDMEVNYMMMAKRPAAA | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q8UA66 |
Q47YA8 | XNI_COLP3 | Flap endonuclease Xni | Colwellia | MSAHLILIDALNLIRRVYAVQERPFIQIKQDHDDELSASTLKQVLFNTQNTCVNALIKIIDQHQPTHALTVFDSQEPCWRYQLFEGYKKGRKKMPDHLANKLIDIQDAFMEQGVDSLTSDEDEADDLIATLAVKMALHGQKVTIISTDKGFLPLLSPNIHIYDYFNRRYLDEEHVQSKFSVKTSQLIDFWTLTGDNTNKIEGVSGIGQVTAAKLLNQYGSLKAILEATDLKDSLAEKLTQSLEQMDLARKLLTLKQDIPLGFNLKDIRLTTSSSAHEINANINLTTDDKS | Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. | Q47YA8 |
C5CNT0 | YCIB_VARPS | Inner membrane-spanning protein YciB | Variovorax | MKLILDFFPILLFFGAYKLADIYTATGVLMAATVLQMGIIYAMERKLQAMQKATLVLILLFGTLTLVLHDDRFIKWKPTVLYGAMAIALAVALWALKKNFLKMLLGSQLQLPDRIWGRLNVAWIGYCLFMAAINGYVAAYFTTEAWVNFKLWGYVFPIVFLVAQGLYISPHLKNDEPSV | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | C5CNT0 |
Q2WAT0 | TRUA_MAGSA | tRNA-uridine isomerase I | Magnetospirillum | MPRYRLLVEYDGTPFNGWQRQDKGLSVQGILEKAVEKLCGVPCTLHAAGRTDAGVHATGQVAHVDLPRDYPADTVRDALNYHMKPKPVAVVAAELVDEDFHARFSAVGRAYLYRIVNRRAPLALDQHRAWWVPVALDAEAMAEGARRLLGHHDFSTFRASECQAKSPMKTLDVLDVTRVGEEIRIVAEARSFLHHQVRNMVGTLKLVGEGKWSPDDMAKVLEARDRTKGGPTAPAAGLVLTGVSYSASGGKSGPTG | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q2WAT0 |
Q484P6 | TOLB_COLP3 | Tol-Pal system protein TolB | Colwellia | MKLLSNIVFGALIAFTSVKAMAALEIVITGGVDSARPIAIIPFNWTGTGERPELLSKVISDDLLRSGKFSPIAIDRFPQTISDAKAIDYSAWANLGAEAVLLGNINEVAPGRYQVSYQLVDVIRGQITGGETSMLSNGELVNPKDHILAQSSANIQLNQARRYAHSISNVIYEKLTGSKGAFLSKIAYVIVRDQGKYPYQLAFADYDGFNEHVLLSSKEPLMSPSWHPNGDQLAYVSFENRQAQIHSIDIYTGVRKSISSFNGINSAPRFSPDGKSMAMVLSKDGNPDLYVMELATMKLRRITRNRAIDTEPSWTPDGNSLIFSSERGGKPQLYRVDLAGGKVRRLTFDGEVNLGGSVTPDGKQLIMVNRTRGKYRLAKQELSSGLFQVLTETRLDESPSVSPNGGMIIYSTLHNNRQVLGLVSVDGRFKARLPALDGQVKAPAWSPFL | 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. | Q484P6 |
A1TNT7 | UPPP_ACIAC | Undecaprenyl pyrophosphate phosphatase | Acidovorax | MDFILLAKAAVMGVVEGLTEFLPVSSTGHLILAGALLGFDDDKAKVFDIAIQTGAIFAVVLVYWQKIRETLVALPTQPRARRFALNVLIGFLPAVVLALIFGKAIKAHLFTPVVVASTFILGGFVILWAERRAPGAVRVDSVDDMTPLDALKVGLVQCLAMVPGTSRSGATIIGGMLLGLSRKAATDFSFFLAIPTLIGAGVYSLYKERHLLSMADLPLFAVGLLFSFVSAWLCVRWLLRYISTHSFVPFAYYRIAFGIVVLATAWTGWVHWGE | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A1TNT7 |
Q9S7Y7 | XYL1_ARATH | Alpha-xylosidase 1 | Arabidopsis | MASSSSSLAFSLSLLLALILCFSPTQSYKTIGKGYRLVSIEESPDGGFIGYLQVKQKNKIYGSDITTLRLFVKHETDSRLRVHITDAKQQRWEVPYNLLPREQPPQVGKVIGKSRKSPITVQEISGSELIFSYTTDPFTFAVKRRSNHETLFNTTSSLVFKDQYLEISTSLPKEASLYGLGENSQANGIKLVPNEPYTLYTEDVSAINLNTDLYGSHPMYMDLRNVGGKAYAHAVLLLNSNGMDVFYRGDSLTYKVIGGVFDFYFIAGPSPLNVVDQYTQLIGRPAPMPYWSLGFHQCRWGYHNLSVVEDVVDNYKKAKIPLDVIWNDDDHMDGHKDFTLNPVAYPRAKLLAFLDKIHKIGMKYIVINDPGIGVNASYGTFQRAMAADVFIKYEGKPFLAQVWPGPVYFPDFLNPKTVSWWGDEIKRFHDLVPIDGLWIDMNEVSNFCSGLCTIPEGKQCPSGEGPGWVCCLDCKNITKTRWDDPPYKINATGVVAPVGFKTIATSATHYNGVREYDAHSIYGFSETIATHKGLLNVQGKRPFILSRSTFVGSGQYAAHWTGDNQGTWQSLQVSISTMLNFGIFGVPMVGSDICGFYPQPTEELCNRWIEVGAFYPFSRDHANYYSPRQELYQWDTVADSARNALGMRYKILPFLYTLNYEAHMTGAPIARPLFFSFPEYTECYGNSRQFLLGSSFMISPVLEQGKTEVEALFPPGSWYHMFDMTQAVVSKNGKRVTLPAPLNFVNVHLYQNTILPTQQGGLISKDARTTPFSLVIAFPAGASEGYATGKLYLDEDELPEMKLGNGQSTYVDFYASVGNGTMKMWSQVKEGKFALSKGWVIEKVSVLGLRGAGQVSEIQINGSPMTKKIEVSSKEHTYVIGLEDEEENKSVMVEVRGLEMLVGKDFNMSWKMGIN | Glycoside hydrolase releasing xylosyl residues from xyloglucan oligosaccharides at the non-reducing end. Has alpha-xylosidase activity against xylan oligosaccharides. Also has alpha-glucosidase activity against p-nitrophenyl-alpha-D-glucopyranoside. No activity against p-nitrophenyl-D-xyloside. | Q9S7Y7 |
Q6AQG4 | XGPT_DESPS | Xanthine phosphoribosyltransferase | Desulfotalea | MSDQYKRTYPISWDQLHRDSKALAWRLLDKDFFKGIIAITRGGMVPAAIIARELDIHLIDTICISSYDWKEKKGEADILKGFDGDGEGWLLIDDLVDTGRTAEVVKNLIPKAHFATVYAKPSGRPLVDTFVTEVSQDTWILFPWDTESQFAAPLIGREQR | Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine. | Q6AQG4 |
Q9I8X2 | VSP1_DEIAC | Snake venom serine protease | Deinagkistrodon | MVLIRVLANLLILQLSYAQKSSELVIGGVECDINEHRFLVALYELTSMTFLCGGTLINQEWVVTAAHCDRLQLYLYIGMHDKYVKFDDEQGREPIEKYFYNCSNNLTTRDKDIMLIRLDRPVDNSTHIAPLSLPSRPPSVGSVCRVMGWGAISPSRDVLPDVPHCVNINLVNNAECRRAYPRLPATSRTLCAGVMQGGIDSCNRDSGGPLICDGQFQGVVNWGGNPCAQPNMPALYTKVYDYNDWIRSITAGNTTAACPP | Thrombin-like snake venom serine protease that coagulates human fibrinogen by hydrolysis of the alpha chains (FGA). | Q9I8X2 |
Q8C5P7 | TDRP_MOUSE | Testis development-related protein | Mus | MWKLSRSRVLLDEPPEEEDVLRGAPPASAAAPASGASLRGWKEATSLFNKDDEEHLLETSRSPKSKGTNQRLREELKAEKKSGFWDALVLKQNAQPKKPDQIEGWEPPKLTAEDVVADHTEDDRSGCPPWSAWEDDTKGSTKYTSLANSASSSRWSLRSAGKLVSIRRQSKGHLTETCEEGE | Contributes to normal sperm motility, but not essential for male fertility. | Q8C5P7 |
B4X640 | VCL_PISVE | Vicilin Pis v 3 | Pistacia | MGSRTKFCLTLFLVSVLILCAGLALAKTDPELKQCKHQCKVQRQYDEEQKEQCAKGCEKYYKEKKGREQEEEEEEEWGSGRGRGDEFSTHEPGEKRLSQCMKQCERQDGGQQKQLCRFRCQEKYKKERREHSYSRDEEEEEEGDEEQEEEDENPYVFEDEHFTTRVKTEQGKVVVLPKFTKRSKLLRGLEKYRLAFLVANPQAFVVPNHMDADSIFFVSWGRGTITKIRENKRESMNVKQGDIIRIRAGTPFYIVNTDENEKLYIVKLLQPVNLPGHYEVFHGPGGENPESFYRAFSREVLEAALKTPRDKLEKLFEKQDEGAIVKASKEQIRAMSRRGEGPSIWPFTGKSTGTFNLFKKDPSQSNNYGQLFESEFKDYPPLQELDIMVSYVNITKGGMSGPFYNSRATKIAIVVSGEGRLEIACPHLSSSKNSGQEKSGPSYKKLSSSIRTDSVFVVPAGHPFVTVASGNQNLEILCFEVNAEGNIRYTLAGKKNIIEVMEKEAKELAFKTKGEEVDKVFGKQDEEFFFQGPKWRQHQQGRADE | Seed storage protein. | B4X640 |
B8IN25 | TIG_METNO | PPIase | Methylobacterium | MQVTETKSEGLMREFQVVLAAAELEDRLATELAGLKDKVQLKGFRPGKVPVAHLRRVYGRSIMADVVQNAVNEANQKILEENKLKLALEPRIEMPEDKAEIEKALDAKADLSFKVALEVMPTFDLVDHSDITLTKPVAAVADEEVDAALTRMAEQNRSYSDRPEGAAAETGDRVVIDFVGRIDGEVFQGGSAEDANLDLGSNTFIPGFEDQLLGAKAGEQRTVTVTFPQDYPAEQLAGKEAVFDVTVKAVQAPGEATIDDELAKTFGLESLDKLKEAVRTSLSAELDAQSRRRVKKALLDALDSRYAFDLPPTLVHQEFAAVWAQVENDLKSRGKSFEDEGTTEEKAQSEYRRIAERRVRLGLVLAQVGESADIKVPDEEVNQALIARLRQFPGREREVYDFYRKNPQAMAELRAPLFEEKVVDHVLGQVKLVEEPVSKEALFADDEDEAAPAAETASEAGASPETKTETSAA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | B8IN25 |
P22028 | VM3B_BOTJA | Disintegrin-like botrocetin | Bothrops | IISPPVCGNELLEEGEECDCGTPEN | Metalloproteinase that binds to von Willebrand factor (VWF) and induces its interaction with GPIb (GP1BA), resulting in platelet aggregation. | P22028 |
P9WLT0 | Y1708_MYCTO | Uncharacterized protein MT1749 | Mycobacterium tuberculosis complex | MPAGLPGQASVAVRLSCDVPPDARHHEPRPGMTDHPDTGNGIGLTGRPPRAIPDPAPRSSHGPAKVIAMCNQKGGVGKTTSTINLGAALGEYGRRVLLVDMDPQGALSAGLGVPHYELDKTIHNVLVEPRVSIDDVLIHSRVKNMDLVPSNIDLSAAEIQLVNEVGREQTLARALYPVLDRYDYVLIDCQPSLGLLTVNGLACTDGVIIPTECEFFSLRGLALLTDTVDKVRDRLNPKLDISGILITRYDPRTVNSREVMARVVERFGDLVFDTVITRTVRFPETSVAGEPITTWAPKSAGALAYRALARELIDRFGM | May play a role in septum formation. | P9WLT0 |
B0T866 | TRMFO_CAUSK | Folate-dependent tRNA(M-5-U54)-methyltransferase | unclassified Caulobacter | MSTSPKPVAPIHVIGGGLAGSEAAWQIAQAGVPVVLHEMRRDLPSSSGAVGPTKVRTDAHQTDGLAEMVCSNSFRSDDWQFNAVGLLHAEMRKLDSLILSAADQHQVPAGGALAVDRDGFSAEVTRRIEAHPLITIEREEVAGLPPEDWDSVVVATGPLTSPALADAILELSGEGQLSFFDAIAPIIHVESIDMDIAWRQSRYDKEGPGGDAAAYINCPMNKAQYEAFIDALLEGPKAEFKDWEHVPYFDGCLPIEVMAERGRETLRHGPMKPVGLTNPRDPTVKAYAIVQLRQDNALGTLWNMVGFQTKLKHGAQAEVFRMIPGLQNAQFARLGGLHRNTFINSPRLLDRSLRMKVAPRLRFAGQMTGVEGYVESAATGLLAGRFAAAERLGKTLDAPPPTTALGALVDHVTGGHIEGEALGKTSFQPMNINYGLLPPTETPKVGDDGVKIPMKERGRAKKRLMSLRALADLDQWMAGA | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | B0T866 |
Q9I753 | TSSK1_PSEAE | Type VI secretion system baseplate component TssK1 | Pseudomonas | MSWNNRVVWSEGMFLRPQHFQQHDRYLETLVDGRCRSLLAGGWGFSELKLDDALLTQGKLAIVSARGVLPDGTPFNIPADDPAPAPLNVEESLRDGIVYLGLPLKRVGTRDTVEEGEALGGARYVSQVQEVRDDNAAFESRAPVALGSQAFRLLTERDGLGEYAAVGVARVREKRADQALSLDEDYLPPVLDIAAAPPLASFAKELLGLLHQRGEALAGRVVASSAGGASEIADFLLLQLVNRAEALTGHLSRVRPLHPQELYRELVALAGEFCTFTASQRRPEEYPVYNHDDLAASFAPVMLALRQALATVIDAKAIAIPIVEKAYGVHVAMLSDRSLIDNASFVLVVRADVPGESLRGHFPQQAKVGSVEHIRDLVNLQLPGIGLLPMPVAPRQIPYHAGSTYFELDRGSAHWKQLTHSGGFAFHIAGQFPGLNLAFWAIRG | Core component of the H1 type VI (H1-T6SS) secretion system that plays a role in the release of toxins targeting both eukaryotic and prokaryotic species. Functions as a spatio-temporal marker for assembly of contractile apparatus made of TssB1 and TssC1. This role in assembly depends on TssM1. | Q9I753 |
Q6ITB2 | VKT2_NOTSC | Kunitz-type serine protease inhibitor tigerin-2 | Notechis | MSSGGLLLLLGLLTLWAELTPVSSKDHPEFCELPADSGPCRGILHAFYYHPVHRTCLEFIYGGCYGNANNFKTIDECEPPCAA | Serine protease inhibitor. | Q6ITB2 |
Q32LJ4 | TPRGL_BOVIN | Protein FAM79A | Bos | MLQLRDSVDSAGTSPTALLAAGEEVGPGSGGGGGGGGRPGVGTPLRQTLWPLSVHDPTRRARVKEYFVFRPGTIEQAVEEIRVVVRPVEDGDIQGVWLLTEVDHWNNEKERLVLITDQALLICKYDFISLQCQQVVRVALNAVDTISYGEFQFPPKSLNKREGFGIRIQWDKQSRPSFISRWNPWSTSVPYTTFIEHPMAGVDEKTASLCQLDGFKALLIQAVKKAQKESPLPGQEGGVLVLECPLLIETYVGLMSFINNEAKLGYSMTRGKIGF | Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release. | Q32LJ4 |
Q9Y7K8 | UPPS_SCHPO | Dehydrodolichyl diphosphate synthase complex subunit nus1 | Schizosaccharomyces | MYDDIFFYLALWVIQSVYGAWDWAKNWVFWTCSYLLNFLYHHHCSRDLIRRDTKKLKKKPKHIAVIIECVEDGGIEGLIHDACELSAWCVCSNIRELTIYERKGFLKQSPEAVEKAIYSHLPFYLGGDKCTVHVTNPCSPDEKNQNDCVDLKVHLIAKEDGRDAIIDLTRGLADLCTKKVISSTQVTLELIDKELKESVIPEPDLLIIFAPLLKLQGFPPWQLRLCEIFHDPILYTTNYLTFFKALVHYSNAEMRLGH | With SPAC4D7.04c, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). | Q9Y7K8 |
P13359 | VIRG_AGRRH | Regulatory protein VirG | Agrobacterium | MKHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSKQFNRVLSSETVDVAVVDLNLGREDGLEIVRTLATKSDVPMIIISGDRLEEADKVVALELGATDFIAKPFGTREFLARIRVALRERPSVARTKDRRSFYFADWTLNIRQRRLISEEGGEIKLTAGEFNLLVAFLEKPRDVLSREQLLIASRVREEEVYDRSIDVLIFRLRRKLEGDPTSPQLIKTARGAGYFFDADVNVSYGGMMAA | VirG is required for the positive regulation of at least two vir loci encoded by the Ri plasmid of A.rhizogenes. | P13359 |
D7PHY7 | VRTR2_PENAE | Viridicatumtoxin synthesis protein R2 | Penicillium | MPSLSSKTSTMQRSCRPQMSACPNQQQKDRPVPQLSCVLCRDRKLKCDKLDPCSNCTSSGVACTPIYRPRLPRGRHARTVQTKASTPPDTRRRGSSNESTTAPAPDDGGLGTHIDQLDNLVQDREVSKLGLSGEGNGLQELISLVSDETMPATAWSTHCFGTISRILSSRIRRLESLVQETARIQTPKRARKPMTPVVVQWYSAPLAGCNWNRMVVQTPQGLEVQQFPAPPTSYSARRSPELSGNDIWADLMDHDMHDPPQYNALELPPDLTNEGGVDNMGSSGRDDPINNGFNALRLLGINNSLSPSFISLPRDRLSASKLCQVYLQNVDPIIKILHRPSLSRWMVDGAPTYLGSSEDDYAVKALESAVCYTAANTMTEHQCQAAFQKTKSSIMAVRRKMCEDALENAGLLTTRDMTVLQAFILYLVTPTDLSKIGRRSEDKDTAVWALVALAIRLIKAMGLNQEPSEGARKGESFFQQQLRLRLWLTACLIDLQASFAQATDPLITHRDAACAVPYVANINDSDFDVDTAHPVASHEELTDTTFALVTYRVQVAGRLFNFGPGCSTAAERHKLAQEVQQQVFTLLHYCDPESSSYAWFTWHSTQSIIFAVRLSELLPFRCGQPGGHVPPPSPRAEGDTTLLWRALQNLEKAQLIRADPRGDGFRWYITTPWLALSTAISECNSCTDVALVCRAWPVIEISYRQHEELQISDECQLPQGPLVHLMNKTREKLAPLLQEGGARLSDSQTVDRASADSLQPPVPVGSIPIDPLLTNGSLGADTAMSEASSIGSLPPFEQQCWKQMTMPTDGAPVRDGVVFTSELYNPLQSDFLNSHG | Probable transcription factor that regulates expression of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system . | D7PHY7 |
A7ZHJ3 | ZAPD_ECO24 | Z ring-associated protein D | Escherichia | MQTQVLFEHPLNEKMRTWLRIEFLIQQLTVNLPIVDHAGALHFFRNVSELLDVFERGEVRTELLKELDRQQRKLQTWIGVPGVDQSRIEALIQQLKAAGSVLISAPRIGQFLREDRLIALVRQRLSIPGGCCSFDLPTLHIWLHLPQAQRDSQVETWIASLNPLTQALTMVLDLIRQSAPFRKQTSLNGFYQDNGGDADLLRLNLLLDSQLYPQISGHKSRFAIRFMPLDTENGQVPERLDFELACC | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | A7ZHJ3 |
Q9P7C5 | YJU2_SCHPO | Pre-mRNA-splicing factor cwf16 | Schizosaccharomyces | MSERKVLNKYIPPDYDPSIRPPKKKKKFQGPNGGKLTVRLMTPFSMRCHTCGEYIYKGKKFNARKEKTGEKYFSIDILRFYIRCTRCAAEITFITDPKHADYAAESGASRNYEPWHEKRLQEYEENELAERNDIPEEDEMEKLEQKTLDTKRQMQISDALDELREKSARRSRVNIDDAIALLKEDAYGSIEEEESKKRKFEEEEIDREAKSLFSSQDGEIIRRLNAETTVEKELPKPIDLVSEKLATSNIPNFQPPKYAKRKMEKKKVLV | 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. | Q9P7C5 |
Q8EG20 | TIG_SHEON | PPIase | Shewanella | MQVSVEATQGLERRLTISVPAEQIEKLVKDSLQREAKRARIPGFRPGKVPVTVINKRYGAAIRQDITGEVMQRNFIEAIIAEKLNPAGAPTFVPGATDGEKFEFVATFEIYPEVELKGLDAIVVEQPKASVTDADVDSMIETLRKQHATFAAVEREAVDGDKVKMNFVGSVDGVEFEGGKAEDFELQLGSGRMIPGFEAGILGHKAGEEFVIDVTFPEEYHAENLKGKAAKFAITLTEVLAANLPEVNDEFAALFGITEGGLEALKTEIRKNMNRELEQALKANVKEQVIAGLLANNDIELPKALIDGEVNVLRQQAMQRFGGQTANMPELPAELFTEQAARRVKIGLLLGEVIKTNELKAEDERVQGLIASMASAYEDPSEVIAYYNSNKELMQNMRNVALEEQAVEALLKTAKVTEKTVAFEEFMNKATGRA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | Q8EG20 |
B3EQ72 | TAL_CHLPB | Probable transaldolase | Chlorobium | MKFFIDTADLEEISAANDLGVLDGVTTNPSLVAKIVSDPEKFTYQDFKDHIAKVCEIVDGPVSAEVTTLSPEEMISQGEELAAIHDNVVVKCPLTRDGLKAMRHLSGNGIRINATLVFSPSQAILAAKAGASYVSPFVGRLDDISTEGMALVDQIVRIYDNYRFPTEVLVASIRHPQHVVEAALMGADIATIPFDVIGQLLKHPLTDSGLKRFMDDASVIQQG | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B3EQ72 |
Q5BPG5 | VUP4_ARATH | Vascular-related unknown protein 4 | Arabidopsis | MESSMNNAFIMSKHETAMFTDDQNPEESSWTMYFEDFFEASSSIVDVGDFSSSSVSDAASFVATKKTLNVSKQEGSNLDIKRTRNREIPFGRHHDLEDTASSPSGSPNVYSMMNLQDNNTRHGGGIVGDDEKRVSAVPNQGGLPIDLKKKGLCLVPLSMVTNFLG | Involved in the regulation of plant growth. | Q5BPG5 |
A5UT95 | TRPD_ROSS1 | Anthranilate phosphoribosyltransferase | Roseiflexus | MPIRDQIIQIVRGHDLSEDQAAEAMEEIMTGMATPAQVAALLTALHLKGETDAEIAGMARVMRAKAIPVHFDAPLLDTCGTGGDGAGTFNISTTAAFIAAGAGAIVAKHGNRAMSSVCGSADVLEGLGVNIELDAASVARCLDQAGIGFMFAQKFHPAMRFVGPVRREIGIRTVFNILGPLSNPAHARHQVLGVADPALAEKMARALHLLGTQHALVIHGHGGLDELTLSGPNLVIDVRAGHTPRRYEVTAADLGLAPAPREALRGGDVSVNVAIVRGILSGEDQSARRDVALLNAAAALVAADRAADLRDGLHQARHSLESGAALARLERLITVSRGGEG | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A5UT95 |
P16227 | UROK_PAPCY | Urokinase-type plasminogen activator chain B | Papio | MRALLAHLLLCVLVVSASKGSRELQVPSDCGCLNGGTCMSNKYFSSIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRSCLAWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKQRVQECMVHNCADGKKPSSPPEELQFQCGQRTLRPRFKIVGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFINYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHEDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPNDPPFGTSCEITGFGKENSTDYLYPEQLKMTVVKLVSHQKCQQPHYYGSEVTTKMLCAADPQWETDSCQGDSGGPLVCSIQGHMTLTGIVSWGRGCALKDKPGVYTRVSRFLPWIHSHTREQNGLAL | Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. | P16227 |
Q9RXU7 | TRMFO_DEIRA | Folate-dependent tRNA(M-5-U54)-methyltransferase | Deinococcus | MSSPTITVVGAGLAGSEAALAAAKLGVRVRLFEMRPQKMTPAHRTANFAELVCSTSLGGEGEMQSKGLLQAEMRSVGAAIVTSADASRVPAGNALAVDRDAFSAHVTEQVKNHPLIEVVEGEVETVPDGICVIASGPLTADALASDLRRLTGSERLSFYDAAAPVIDVDSIDMDIAWRAGRYDQSADYINCPFTKEEYLAFFEALETARSHTPHDWEKLEFFEGCMPIEEIARRGVDTPRFGPMSPKGLDDPKTGRWPYAVAQLRQEDAEGRMWSLVGFQTGLKWGDQKAVVQLIPGLHNADIVRYGVMHRNTYLNAPEVLDSTLQLRADPQKLVAGVLAGTEGYLESSATGWLAGTNAARLALGLEPLTPPAESMLGGLVRYLASANPKGFQPMNVNWALVPELPTEINEKTGKPKKLGKREKRPPLFRRGLGAFMAWAGQDAGVPVTPPAVPEHPQDELPAIR | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q9RXU7 |
Q5FWU5 | ZN513_RAT | Zinc finger protein 513 | Rattus | MPRRKQSHPQPVKCEGVKVDTEDSFDEGPGALVLESDLLLGQDLEFEEEEEEEEGDGHNDQLMGFERDSEGDSQGARPGLPYGLSDDESGGGRALSAESEVEEPARGPGEARGERPGPACQLCGGPTGEGPCCGAGGPGGGPPLPPRLLYSCRLCAFVSHYSSHLKRHMQTHSGEKPFRCGRCPYASAQLVNLTRHTRTHTGEKPYRCPHCPFACSSLGNLRRHQRTHTGPPTPPCPTCGFRCCAPRPTRPPSPTEQEGTMPRRSEDALILPDLSLHVPPGGTSFLPDCGQLRGEGEGLCGTGSEPLPELLFPWTCRGCGQELEEGEGSRLGTAMCGRCMRGESGGGGSGGPQGPSDKGFACSLCPFATHYPNHLARHMKTHSGEKPFRCARCPYASAHLDNLKRHQRVHTGEKPYKCPLCPYACGNLANLKRHGRIHSGDKPFRCSLCNYSCNQSMNLKRHMLRHTGEKPFRCATCAYTTGHWDNYKRHQKVHGHGGAGGPGLSAPEGWAPPHSPPSVLSTRGSAALGATGSRALHTDSP | Transcriptional regulator that plays a role in retinal development and maintenance. | Q5FWU5 |
A2T344 | YCF4_ANGEV | Photosystem I assembly protein Ycf4 | Angiopteris | MNYQSEWLRIDPIKGSRRFSNLCWAFILVLGAIGFSLVGFSSYLGRDLIPILSSQQIIFLPQGIVMCFYGIAGIFLGFYLWCTILWNVGSGYNQFNKREGIVYLFRWGFPGENRRICIRFMIKDIQAIRMEIQEGFSPRRVLYLRIKGQQDVPLTRLDEELTLREMEEKAAELARFLRVSIEGF | Seems to be required for the assembly of the photosystem I complex. | A2T344 |
Q44444 | VIRG_RHIRD | Regulatory protein VirG | Agrobacterium tumefaciens complex | MIVHPSRENFSSAVNKGSDFRLKGEPLKHVLLVDDDVAMRHLIIEYLTIHAFKVTAVADSTQFTRVLSSATVDVVVVDLNLVREDGLEIVRNLAAKSDIPIIIISGDRLEETDKVVALELGASDFIAKPFSIREFLARIRVALRVRPNVVRSKDRRSFCFTDWTLNLRQRRLMSEAGGEVKLTAGEFNLLLAFLEKPRDVLSREQLLIASRVRDEEVYDRSIDVLILRLRRKLEADPSSPQLIKTARGAGYFFDADVQVSHGGTMAA | VirG is required for the positive regulation of at least two vir loci encoded by the Ti plasmid of A.tumefaciens. | Q44444 |
Q9P7B3 | YI14_SCHPO | Putative cation exchanger C521.04c | Schizosaccharomyces | MSQPADINQSESSAETITQGRRADRPEETPSSSVYEQNLRFGDFLMPTVGDADATDSLSQSTNDRDIYSPREIDQYTRKVSSRTDPSTSTISNARQHPRNSVSRLSRSSSNVRQQRDIPKQNFKVRPLSPLRGQSPASLRSEESFTLKERQNAINKTRAFGMRLWKPALYKKFRSINRDADIDIHDEPLKRPNTSISNVIWLICFGAPLFLVIFICYIFFTVLSFFNVPDAIVYSKLCRGLMFYLLYPFGQHVRHKVKRLSVRSPAHPIYQTQHSHYDETPTSHHPDPARLNFLSFSFCVNPMNQSLDCNTTPHRRNASSIIYTLMYYLIIAPTLLITSAICMFTIFFVPCARTLWAICRHLRTCPLSLSFRPNLALPLSMDSSDVVLLCVKKAASWKYYKYTIDGIYIIYFDMLALIIPTIFFGFFGSQGHWFTSSVFLFTASLVSIIPLAYFIGMAVASISAQSSMGMGAFINAFFGSVIEVFLYSVALRKGNAGLVEGSVIGSILAGLLLMPGLSMCAGAIRKKFQFFNIKSAGATSTMLLFAVLGAFAPTMLFRIYGPFRLDCEPCGANCQKCTKHYVLENDSLYKNRVLPFTYCCSIMLVLAYAIGLWFTLRTHASHIWQNFTADDISFLKAEEEVGEPVNQDTAGNMSDSSEGGEAVVNGNSQHHHNRDDASSGLSSNGSENESLEHEPTNELPQRPLVNQSQNSHGDDAPNWSRSKSAIILLSATFLYSLIAEILVEHVDTVLDKFAISEKFLGLTLFALVPNTTEFMNAISFALNENIALSMEIGSAYALQVCLLQIPCLMGYSLFQYYRSGDSISFKHLFTMVFPTWDMICVMICVFLLTYVHSEGKSNYFKGSILVLAYLVSMLGFTFFNY | Putative cation exchanger. | Q9P7B3 |
O02789 | TDT_MONDO | Terminal deoxynucleotidyltransferase | Monodelphis | MHRIRTIDSDFGKKRQKKMDNHISSMIYEIKFHEFVLFILEKKMGATRRTFLTDLARKKGFRVENELSNSVTHIVAENNSGSDVLAWLKTHKMEKTTQFELLDISWLIECMKVGKPVDTKGKYQLMESRVDSANPDPTAGTLNILPPTTKTISQYACQRRTTINNHNQRFTDAFEILAKNYEFKENDDTCLTFMRAISVLKCLPFEVVSLKDTEGLPWIGDEVKGIMEEIIEDGESLEVQAVLNDERYQSFKLFTSVFGVGLKTADKWYRMGFRTLNKIRSDKTLKLTKMQKAGLCYYEDLIDCVSKAEADAVSLLVQDAVWTFLPDALVTITGGFRRGKEFGHDVDFLITSPGAEKEQEDQLLQKVTNLWKKQGLLLYCDLIESTFEDLKLPSRKIDALDHFQKCFLILKLYHHKEDKRKWEMPTGSNESEAKSWKAIRVDLVVCPYDRYAFALLGWSGSRQFERDLRRYATHEKKMMLDNHALYDKTKKIFLKAKSEEEIFAHLGLEYIQPSERNA | Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. | O02789 |
Q9H8X9 | ZDH11_HUMAN | Zinc finger protein 399 | Homo | MDTRSGSQCSVTPEAILNNEKLVLPPRISRVNGWSLPLHYFQVVTWAVFVGLSSATFGIFIPFLPHAWKYIAYVVTGGIFSFHLVVHLIASCIDPADSNVRLMKNYSQPMPLFDRSKHAHVIQNQFCHLCKVTVNKKTKHCISCNKCVSGFDHHCKWINNCVGSRNYWFFFSTVASATAGMLCLIAILLYVLVQYLVNPGVLRTDPRYEDVKNMNTWLLFLPLFPVQVQTLIVVIIGMLVLLLDFLGLVHLGQLLIFHIYLKAKKMTTFEYLINNRKEESSKHQAVRKDPYVQMDKGVLQQGAGALGSSAQGVKAKSSLLIHKHLCHFCTSVNQDGDSTAREGDEDPCPSALGAKARNSRLICRRLCQFSTRVHPDGGSMAQEADDAPSISTLGLQQETTEPMKTDSAESED | Has also a palmitoyltransferase activity-independent function in DNA virus-triggered and CGAS-mediated innate immune response . Functions as an adapter that recruits IRF3 to STING1 to promote the activation of that key transcriptional regulator of type I interferon (IFN)-dependent immune response . | Q9H8X9 |
P0DP82 | XPTB_EMENI | Xanthone prenyltransferase B | Aspergillus subgen. Nidulantes | MATDGMVLHKRSLSEGGTSTQAWKVLSQTLPSRGPDVDAWWQLTGRHLAVLLDAAAYPIEKQYECLLYHYHYAAPYLGPAPREGASPPTWKSMLQLDGTPFEFSWKWNNPGGEPDVRFGLEPIGPMAGTSLDPLNHLAMREILYKLSSAVPGSDLTWTHHFLATLFDHDYAKYTQKAATMGSSIGTSLVYSLEFQRKSTGLKTYFHPRKLDQQAFLDIPSWEASFRGLHPNSPSRTAVHEFLSTNPEGKLLKPFCLSVDNCSPAKARIKWYFNSPHTNFRAIREIMTLGGRIADTETRTKQFSELFNLLKTVTEEHADFPETSEFPYVPNNGDSIIPNFADAPDMLKGCVYFFDIAPGRNLPAIKVYFPVRNHCRNDLAVTQNLNRWLESRGRGQYGAAFGRALETIADYRRLEDSGGLLSFLSCQFMEDGELDLTSYFNPQAFHSGRLTHRRATRRRGDDRW | Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB . XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring . Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC . | P0DP82 |
C3MGH8 | UREG_SINFN | Urease accessory protein UreG | Sinorhizobium | MPSKNGPLRVGIGGPVGSGKTALTDKLCKAMREKYSVAVVTNDIYTKEDAEALVRMQALPSERIVGVETGGCPHTAIREDASINLQAIADLNRRIPDLDVVFIESGGDNLAATFSPDLADLTIYVISVCQGEEIPRKGGPGITKSDLLVINKKDLAPYVGADLEVMEHDATRMRAEKPFVFSDMKRGEGIERIVEFLTVQGGL | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | C3MGH8 |
Q0SM64 | TILS_BORAP | tRNA(Ile)-lysidine synthetase | Borreliella | MHFLDDNIQIKIDKFYKKNSLNKNRVIVAFSGGADSTTLLLNLKYYLSNNIIAFYFAHFIRPDNEQNKEIEHVKGFCDLYNIALQIKKCDIDIKSESVRLGVSIEELARKCRYNALENALKENDANYIALAHNENDQIETIIMRFFQGSFLDGLAGIPSVNKNIIRPLLEVSRPEIENFLSLNNIRVFIDSTNSQNLYLRNKVRNNLLPSIEKIFKGYEKCLKRISEFSKEFVNYFEKDEFFPVEKGKYYYSFDLKAFLDFPKYLVFRLIFKILNSEGIVAKISYKALNELFKIEIDRKKNNVLLKTNDFFLEKRHNKINLIFKRDEKFYKPFDFILEVGKWHSLSLGKILLKCLECNAASVSRLKCCSYEFRYKFFKDKLKAKKFFSKFIRCNPIYLMLLALDNRLIGIIDLNTLNLVWSEKSILKKISISLIGGLLKE | 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. | Q0SM64 |
O23034 | UBA5_ARATH | null | Arabidopsis | MEVGFKALLDDLDVLEKSLSDPALINKLRSHVENLATLSKCNPHRRSKVKELSSEVVDSNPYSRLMALQRMGIVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRPDQVGMTKTDAAVQTLAEINPDVVLESFTMNITTVQGFETFTSSLTNKSFCPSKEGGSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGVSEDAVSGHIQLLVPGETACFACAPPLVVASGIDERTLKREGVCAASLPTTMGVVAGLLVQNSLKFLLNFGEVSPYLGYNSLKDFFPTMKMRPNPQCSNVACLERQKEYMLAKPERDAAAKAKMEADASTTIDEGPLHDDNEWNISVVDDENEKDTTKAASSSDTLPEGLTRELPVADEYEKAIAIASGSGETEEEDDLEDLKKQLEALNAA | E1-like enzyme which activates UFM1. | O23034 |
Q91XL3 | UXS1_MOUSE | UDP-glucuronate decarboxylase 1 | Mus | MVSKGLLRLVSSVNRRRMKLLLGIALFAYAASVWGNFVNMRSIQENGELKIESKIEEIVEPLREKIRDLEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARVKKGRTRHS | Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis. | Q91XL3 |
O57896 | WTPC_PYRHO | Molybdate/tungstate import ATP-binding protein WtpC | Pyrococcus | MLKVESISKDYREFKLREISFDVREGEHFIILGPSGSGKTVLLEIIAGIISPDRGRILLRGEDITGLPPEKRNFSYIPQNYALFPHMTVFDNIAFGLKLRKIPRKEVARKVREVAESLGIDHLLHRKPRTLSGGEQQRVAIARALVVKPELLLMDEPFANLDVQTKSKLIREMKRWRKEFGFTAIHVTHSFEEALSLGDRVGIMLRGRLVQVGDVRDVFSKPKSEEVARFLGFENIIEGVANGRILKVGDLRIELPREVWGKVRVGIRPEDITIFMEGVKTSARNVFKARVEGIEDLGALVKLTLNLGGIILRAFITRSSLIELGIREGEEVYASFKASAIHVFP | Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system. | O57896 |
O35092 | TI17A_RAT | Inner membrane preprotein translocase Tim17a | Rattus | MEEYAREPCPWRIVDDCGGAFTMGTIGGGIFQAFKGFRNSPVGVNHRLRGSLTAIKTRAPQLGGSFAVWGGLFSTIDCGMVQIRGKEDPWNSITSGALTGAILAARNGPVAMVGSAAMGGILLALIEGAGILLTRFASAQFPNGPQFAEDHSQLPSSQLPSSPFGDYRQYQ | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. | O35092 |
Q72CB6 | TATA_DESVH | Sec-independent protein translocase protein TatA | Desulfovibrio | MFGIGFQELLVVLVLVLLVFGANKLPEIGGGLGRAIRNFKRAASEPDEIDVTPTDKKDKNDDKQA | 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. | Q72CB6 |
Q5E626 | YCIB_ALIF1 | Inner membrane-spanning protein YciB | Aliivibrio | MKQILDFIPLIIFFALYKMYDIYTATGALIIATAIQLVVTYALYKKVEKMQLITFIMVTVFGGMTIFLHDDNFIKWKVTIVYCVFAAGLIIAHILGKPVIKGMLGKEVTLPDDKWTKINHAWVLFFTVCAIANLYVAFEMPLDVWVNFKVFGLLGLTFLYTLFTGMYVYKHMPKEKKEEQE | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q5E626 |
Q96GC6 | ZN274_HUMAN | Zinc finger protein zfp2 | Homo | MASRLPTAWSCEPVTFEDVTLGFTPEEWGLLDLKQKSLYREVMLENYRNLVSVEHQLSKPDVVSQLEEAEDFWPVERGIPQDTIPEYPELQLDPKLDPLPAESPLMNIEVVEVLTLNQEVAGPRNAQIQALYAEDGSLSADAPSEQVQQQGKHPGDPEAARQRFRQFRYKDMTGPREALDQLRELCHQWLQPKARSKEQILELLVLEQFLGALPVKLRTWVESQHPENCQEVVALVEGVTWMSEEEVLPAGQPAEGTTCCLEVTAQQEEKQEDAAICPVTVLPEEPVTFQDVAVDFSREEWGLLGPTQRTEYRDVMLETFGHLVSVGWETTLENKELAPNSDIPEEEPAPSLKVQESSRDCALSSTLEDTLQGGVQEVQDTVLKQMESAQEKDLPQKKHFDNRESQANSGALDTNQVSLQKIDNPESQANSGALDTNQVLLHKIPPRKRLRKRDSQVKSMKHNSRVKIHQKSCERQKAKEGNGCRKTFSRSTKQITFIRIHKGSQVCRCSECGKIFRNPRYFSVHKKIHTGERPYVCQDCGKGFVQSSSLTQHQRVHSGERPFECQECGRTFNDRSAISQHLRTHTGAKPYKCQDCGKAFRQSSHLIRHQRTHTGERPYACNKCGKAFTQSSHLIGHQRTHNRTKRKKKQPTS | Probable transcription repressor. Specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions . | Q96GC6 |
B2GDC8 | TRMB_LIMF3 | tRNA(m7G46)-methyltransferase | Limosilactobacillus | MRVKHKKWAVPLMEAHPEMMTMDPASFKGRWQERFAKPQPLQVEVGMGKGQFIIGMAKAHPEINFIGLEIESTVAAIALKNALPEQLPNLTLVRGDGAGLDTYFEDGSIDRLYLNFSDPWPKTRHEKRRLTYKTFLANYQQVVKPGGGLEFKTDNQGLFEYSLTSLNNFGMIFDGVWLNLHESPENEGNVETEYEQRFASLGQPIYKLKAHFPVN | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | B2GDC8 |
Q0HPE6 | YIDC_SHESR | Membrane protein YidC | Shewanella | MESQRNILLIGLLFVSFLLWQQWQADKAPKPVATESSVVANATTNHSADVPEADTGVPAAMTATQNLITVKTDQLDVQINPVGGDIVFAALVSHKLEQGKDQPFVLLEQTKDFTYIAQSGLIGRDGIDSSAKGRAAFAASKTEFTLADGQDTLEVPLTYVADNGVTYTKVFVFHRGKFNVDIDYKINNTSAAPLQVQMYGQIKQTIKPSESSMMMPTYRGAAFSTQDVRYEKYKFEDMSKSNLNQPTLGGWAAMLQHYFVSAWIPPATDSNTIFSSVSAGGLANIGFRGAVYDIAPGATQEISSQFYVGPKDQKALSALSDTLNLVVDYGFLWWLAVPIHWLLMFYQSFVGNWGVAIILITLTVRGLLFPLTKAQYTSMAKMRNLQPKLQDLKERFGDDRQKMGQAMMELYKKEKVNPMGGCLPILLQMPIFIALYWVLLESFELRHAPFMLWIHDLSVQDPYYILPLLMGVSMFVMQKMQPIAPTMDPMQVKMMQWMPVIFTVFFLWFPSGLVLYWLVGNIVAIIQQKIIYAGLEKKGLK | 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. | Q0HPE6 |
C0RG97 | Y033_BRUMB | Nucleoid-associated protein BMEA_A0033 | Brucella | MRDMMGMMKQAKELQAKMKAMQDEIATMEASASSGGGLVTVTLSGKGTLSALKIDPSLMKEDEVEILEDLIIAAHNDGKAKLEAAMAEKTQSLTAGLPIPPGFKLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | C0RG97 |
A3MFQ3 | TRPD_BURM7 | Anthranilate phosphoribosyltransferase | pseudomallei group | MTITPQEALQRTIEHREIFHDEMLHLMRLIMRGDMSPVMAAAIITGLRVKKETIGEIAAAATVMREFARRVEVEDNANFVDIVGTGGDGSHTFNISTATMFVAAAAGAKVAKHGNRGVSSKSGSADVLEALGVNIDLQPEQVAASIAETGMGFMFAPNHHPAMRNIAPVRRELGVRTIFNILGPLTNPADAPNQLMGVFHPDLVGIQVRVMQRLGAQHVLVVYGKDGMDEVSLGAATLVGELRDGEVREYEIHPEDFGMQMVSNRTLKVESADESRVMLLEALGNKPGVAREIVTLNAGTALYSADVAGSIADGIQLARDAIASGRAREKVDELVRFTQQFKR | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A3MFQ3 |
Q3J349 | TRMFO_CERS4 | Folate-dependent tRNA(M-5-U54)-methyltransferase | Cereibacter | MAESLHIVGAGMAGSEAAWQAAEMGVPVVLHEMRPKVGTFAHRTGQFAEMVCSNSFRSDDDERNAVGLLHWEMRAARGLIMEMAAAHRLPAGGALAVDRDPFAESVTGRLRAHPLISVVEEEVADLPSSGNWIVATGPLTSSALAESLRALTGAEALAFFDAIAPIVYAETIDMEVAWRQSRYDKGETEDERTAYINCPMNREQYEAFIDALLAAEKTEFHEGETAGYFDGCLPIEVMAERGRETLRHGPMKPVGLTNSHRPEEKAHAVVQLRRDNKLGTLYNIVGFQTKMKYGAQTAVFKMIPGLENASFARLGGIHRNTFLNSPTLLDDRMRLKLRPNIRFAGQVTGVEGYVESAAMGLLAGRMAAAEILGRDLPPPPPETAMGALVTHITGGAEAKSFQPMNVNFGLFPPIDARGGRRGRKDRYKAYTDRAKAAFTEWLGA | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q3J349 |
Q30XF7 | TGT_OLEA2 | tRNA-guanine transglycosylase | Oleidesulfovibrio | MATIGEFTLHATDGKARTGVLQTAHGPVRTPIFMPVGTVGSVKGVAPDDLDAIGAEIILGNTYHLYLRPGDELVARRGGLHEFNAWRKPILTDSGGFQVFSLSGLRRISEEGVEFRSHLDGSKHLFTPEKVVSIQRNLNSDIMMVLDECVPYGADKDYTARSLKMTTRWAQRCRDAYPAGSGGNLMFGITQGGFFKDLREESIGELTRIDFDGFALGGLSVGESKTEMMDILYHTAPMLPAHKPRYLMGVGTPLDIINGINAGIDMFDCVLPTRNARNGTLYTSAGKINIKRREFAEDDGPLDPNCSCYTCRTFSRAYLRHLFHAQEILSYRLNSIHNLTYFLDLVRGAREAIAQGTFAEYKSRYDAIYPQEAALCP | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). | Q30XF7 |
B3A0S5 | XYNA_FUSO4 | Xylanase III | Fusarium oxysporum species complex | AASGLEAAMKAAGKQYFGTALTVRNDQGEIDIINNKNEIGSITPENAMKWEAIQPNRGQFNWGPADQHAAAATSRGYELRCHTLVWHSQLPSWVANGNWNNQTLQAVMRDHINAVMGRYRGKCTHWDVVNEALNEDGTYRDSVFLRVIGEAYIPIAFRMALAADPTTKLYYNDYNLEYGNAKTEGAKRIARLVKSYGLRIDGIGLQAHMTSESTPTQNTPTPSRAKLASVLQGLADLGVDVAYTELDIRMNTPATQQKLQTNADAYARIVGSCMDVKRCVGITVWGISDKYSWVPGTFPGEGSALLWNDNFQKKPSYTSTLNTINRR | Catalyzes the hydrolysis of the internal glycosidic bonds in heteroxylans, releasing mainly xylobiose and xylotriose. Most active on oat-spelt xylan. | B3A0S5 |
Q8NIG9 | TRI5_FUSCU | Sesquiterpene cyclase | Fusarium | MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMLNYFDDLQAGREQSHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKDLFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYEKVKDQDTEDAKKFCKFFEQAANVGAVAPSEWAYPQVAQLANVRAKDDMKEAQKPILSSIELVE | TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. | Q8NIG9 |
Q2NXR3 | TTCA_XANOM | tRNA 2-thiocytidine biosynthesis protein TtcA | Xanthomonas | MTAVLPLPHPLADPAPRDPRQRLQREQLRLGKRLQRQVGQAIADFGMISPGDKIMVCLSGGKDSYTMLDMLLQLQRKAPVPFTLVAVNLDQKQPDFPAHVLPAYLDALGVPFDIVEQDTYSVVSRVVPAGKTMCSLCSRLRRGALYAYAQTHGVTKIALGHHRDDIVATFFMNLFHHARLAAMAPKLRSDDGAHVVIRPLAYVREAHIAAYAQARQFPIIPCNLCGSQENLQRQQVGKMLQHWDHEQPGRVEQIARALGDVRPEQLADRTLFDFLALGRSGDAPPDLAPDPGAWLTASDATHDSD | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q2NXR3 |