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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|---|---|---|---|---|---|---|
P0C5Y7 | TEN1_SCHPO | Protein ten1 | Schizosaccharomyces | MDSAKLIFINQINDCKDGQKLRFLGCVQSYKNGILRLIDGSSSVTCDVTVVLPDVSIQKHEWLNIVGRKRQDGIVDVLLIRSAVGINLPRYRQMVSERQKCD | Required for telomere maintenance. | P0C5Y7 |
Q7M713 | TR116_MOUSE | TRB4 | Mus | MNGVLQVTFIVILSVEFIIGIFGNGFIAVVNIKDLVKGRKISSVDQILTALAISRIALLWLILVSWWIFVLYPGQWMTDRRVSIMHSIWTTFNQSSLWFATSLSIFYFFKIANFSNPIFLYLKVRLKKVMIGTLIMSLILFCLNIIIMNAPENILITEYNVSMSYSLILNNTQLSMLFPFANTMFGFIPFAVSLVTFVLLVFSLWKHQRKMQHSAHGCRDASTKAHIRALQTLIASLLLYSIFFLSHVMKVWSALLLERTLLLLITQVARTAFPSVHSWVLILGNAKMRKASLYVFLWLRCRHKE | Putative taste receptor which may play a role in the perception of bitterness. | Q7M713 |
Q9I7K5 | TMEDE_DROME | Protein eclair | Sophophora | MRDQFISLALILCVLHSACGLYFHISETERKCFIEEVPDETTVIVNYKVELYDPRSNGFMPSSPGIGMHVEVRDSDDKIVLSRVYSSQGRISFTSHTPGEHVICMFSNSTAWFSGAQLRVHLDIQVGEHAIDYAHVAQKEKLTELQLRIRQLLDQVEQITKEQNYQRYREERFRHTSESTNSRVLWWSLAQTVVLVCMGFWQMRHLKSFFEAKKLV | Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected. Involved in Golgi organization. | Q9I7K5 |
Q893R2 | THIG_CLOTE | Thiazole synthase | Clostridium | MDKLNIGGKQLESRLFIGTGKYGSNEILPKVIESSKSQVITVALRRVDLNSREENILNYIKDDCVLLPNTSGARNAEEAVRLARLSKAAGCGNWIKIEAISDNKYLLPDNYETIKATEILAKEGFYVFPYMNPDLMDAKRFVAAGAAAVMPLGAPIGTNKGLKTEEMIKILIEEIKEVPIIVDAGIGKPSDACKAMEMGADAVLLNTAIATAENPILMGEAFKNAVEAGRKAYLAGFGTEAKFANASSPLIGFLR | 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. | Q893R2 |
P55722 | Y4YN_SINFN | Probable translocation protein y4yN | Sinorhizobium | MYLSPAEIQILLHAAIELVAAAGLGAARALGIMLILPVFTRSQIGGLIRGCLAIAFGLPCLAHVSDGLQAPDPETSLIQIPLLGLKEVFVGVLLGTFLGIPLWGLQAAGEFIDNQRGITSPSTQADPATNSQASAMGVFLGITAITIFVAAGGVEAVLSALYGSYSIWPVYRFQPTLSTQGAVELFGLLDHIMRTTLLVSGPVVFFLGLIDISMMMLRRFAPQFKSGQLSPPIKNIVFPIIMVTYATYLLEGIKLEITQADGTLGWLDKLLK | Could be involved in the secretion of an unknown factor. | P55722 |
A4QK29 | YCF4_ARAHI | Photosystem I assembly protein Ycf4 | Arabis | MSWRSESIWIEFITGSRKTSNFCWAFILFLGSLGFLLVGTSSYLGRNFISVFASQQIIFFPQGIVMSFYGIAGLFISCYLWCTFLWNVGSGYDLFDRKEGIVRIFRWGFPGKSRRIFLRFLMKDIQSIRIEVKEGVSARRVLYMEIRGQGAIPLIRTDENFTTREIEQKAAELAYFLRVPIEVF | Seems to be required for the assembly of the photosystem I complex. | A4QK29 |
B5FB26 | YACG_ALIFM | DNA gyrase inhibitor YacG | Aliivibrio | MTKPTTEQPTIVKCPTCQSAVVWNAESPFRPFCSKKCQMIDFGEWADEEKSIPGAPDMSDSDGWSEDQY | Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase. | B5FB26 |
P73057 | Y1847_SYNY3 | Nucleoid-associated protein slr1847 | unclassified Synechocystis | MAQGKGFGFGLGKIKELQEAFQKAQQVQEGAKVLQEELERMEIPGKSADGLVTVLMSGNQEPLSIEIDPSALEKGAEGLSASVTEAMKAAYAESTETMRSKMEELTSGLNLPGM | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | P73057 |
Q493B5 | TILS_BLOPB | tRNA(Ile)-lysidine synthetase | Candidatus Blochmannia | MITTNTSSENWDLYRKVTHCLVGHTRLVLSYSGGLDSTVLLDILTRLKNNSDHFTSSPFMLRAIYVHHGISNYSDEWASHCFNQCKIRGIPFSVIHINCYNAENKQRNIEALARNLRYKKLYNRLNSKEILLTAHHMNDQVESLFLALKRGSGPSGLSGMSKNALYANKYRLLRPLLDCSREQLEMYAYKKKLVWIEDDTNTDTRFDRNFLRIKILPSIYQRWPCFNQVVARTAQLCRDQENLLNELLSESFQKLIDESDGSLLFIPLFQYSIPKRQALLRRWLLHFSMKMPSYQLINRIWKEVVLSRKDATPILQLDKYLCRRFREKLYILPVNMRCSLNRIELSWNIIHNVFILPYNLGKLIYQPLSINEHVPKNPFDLHLNINSSLNTSHDVFEKYKKVLTHCFVRSPKSDEKISIIFGNIDGLLYILGRNHGRHLKKIWQELGVPPWLRSRIPLLFYNKTLITAIGVFITHNGKIISKENTLWKISWLQDIISYKIFKNSVRYHLE | 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. | Q493B5 |
G2Q1N4 | XY30A_MYCTT | GH30 family xylanase | Thermothelomyces | MYSLLIALLCAGTAVDAQALQQRQAGTTLTVDLSTTYQRIDGFGTSEAFQRAVQMSRLPEEGQRRALDVLFSTTNGAGLSILRNGIGSSPDMSSDHMVSIAPKSPGSPNNPLIYSWDGSDNKQLWVSQEAVHTYGVKTIYADAWSAPGYMKTNGNDANGGTLCGLSGAQCASGDWRQAYADYLTKYVEFYQESNVTVTHLGFINEPELTTSYASMRFSASQAAEFIRILYPTIQKSNLTYKPTIACCDAEGWNSQAGMLGALSSVNSMFGLVTAHAYTSQPGFSMNTPHPVWMTEAADLQGAWTSAWYSYGGAGEGWTWANNVYNAIVNGNASAYLYWIGAQTGNTNSHMVHIDANAGTVEPSKRLWALGQWSRFVRPGARRVAVSGASGSLRTAAFRNEDGSVAVVVINSGGDAAVNVRLASSSSADQQPASAKAWATDNSRAIEEIQASFADGVATVNVPSRSMTTVVLYPAADA | Xylanase exhibiting endo- and exo-xylanase activity . Shows the highest activity toward beechwood glucuronoxylan, which consists of a beta-1,4-linked xylose backbone decorated with the methylated form of D-glucuronic acid (MeGlcA) attached directly to the main chain at xylose C2 . Acts also against wheat arabinoxylan, a xylan without MeGlcA substituents along the main chain, but the xylanase activity is about two orders of magnitude lower than that achieved in the case of beechwood xylan . Shows no activity against carob galactomannan, konjac glucomannan, or barley beta-glucan . The recombinant xylanase also exhibits an exo-activity by releasing processively disaccharide units from the non-reducing end of linear and decorated xylooligosaccharides (XOS) . | G2Q1N4 |
Q9SI37 | WRKY1_ARATH | Zinc-dependent activator protein 1 | Arabidopsis | MAEVGKVLASDMELDHSNETKAVDDVVATTDKAEVIPVAVTRTETVVESLESTDCKELEKLVPHTVASQSEVDVASPVSEKAPKVSESSGALSLQSGSEGNSPFIREKVMEDGYNWRKYGQKLVKGNEFVRSYYRCTHPNCKAKKQLERSAGGQVVDTVYFGEHDHPKPLAGAVPINQDKRSDVFTAVSKGEQRIDIVSLIYKLCIVSYDIMFVEKTSGSSVQTLRQTEPPKIHGGLHVSVIPPADDVKTDISQSSRITGDNTHKDYNSPTAKRRKKGGNIELSPVERSTNDSRIVVHTQTLFDIVNDGYRWRKYGQKSVKGSPYPRSYYRCSSPGCPVKKHVERSSHDTKLLITTYEGKHDHDMPPGRVVTHNNMLDSEVDDKEGDANKTPQSSTLQSITKDQHVEDHLRKKTKTNGFEKSLDQGPVLDEKLKEEIKERSDANKDHAANHAKPEAKSDDKTTVCQEKAVGTLESEEQKPKTEPAQS | Transcription factor. Binds to a 5'-CGTTGACCGAG-3' consensus core sequence which contains a W box, a frequently occurring elicitor-responsive cis-acting element. | Q9SI37 |
B7UK54 | TUSC_ECO27 | tRNA 2-thiouridine synthesizing protein C | Escherichia | MKRIAFVFSTAPHGTTAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWICAASLRERGLDPQTPFVVEATPLEADALRRELANCDVILRF | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. | B7UK54 |
Q85BP9 | YCF4_ANTAG | Photosystem I assembly protein Ycf4 | Anthoceros | MNWESEWFRIELIRGSRRISNFFWAFILLSGALGFLSVGLSSYFGKDLISFLSYEQIVFIPQGIVMCFYGIAGSAFSLYLWGTIFWNIGSGYNKFDKGKGIVCIYRWGFPGKNRRIRIEFSMKDIEAIGMEVQEGFYPRRTLRLKIKGQQDVPLTYIGENLTLREIEEEAAELARFLQISIEGF | Seems to be required for the assembly of the photosystem I complex. | Q85BP9 |
P0A3W1 | VIRB4_AGRT9 | Protein virB4 | Agrobacterium tumefaciens complex | MLGASGTTERSGEIYLPYIGHLSDHIVLLEDGSIMSIARIDGVAFELEEIEMRNARCRAFNTLLRNIADDHVSIYAHLVRHADVPSSAPRHFRSVFAASLNEAFEQRVLSGQLLRNDHFLTLIVYPQAALGKVKRRFTKLSGKRENDLAGQIRNMEDLWHVVAGSLKAYGLHRLGIREKQGVLFTEIGEALRLIMTGRFTPVPVVSGSLGASIYTDRVICGKRGLEIRTPKDSYVGSIYSFREYPAKTRPGMLNALLSLDFPLVLTQSFSFLTRPQAHAKLSLKSSQMLSSGDKAVTQIGKLSEAEDALASNEFVMGSHHLSLCVYADDLNSLGDRGARARTRMADAGAVVVQEGIGMEAAYWSQLPGNFKWRTRPGAITSRNFAGFVSFENFPEGASSGHWGTAIARFRTNGGTPFDYIPHEHDVGMTAIFGPIGRGKTTLMMFVLAMLEQSMVDRAGTVVFFDKDRGGELLVRATGGTYLALRRGTPSGLAPLRGLENTAASHDFLREWIVALIESDGRGGISPEENRRLVRGIHRQLSFDPQMRSIAGLREFLLHGPAEGAGARLQRWCRGHALGWAFDGEVDEVKLDPSITGFDMTHLLEYEEVCAPAAAYLLHRIGAMIDGRRFVMSCDEFRAYLLNPKFSAVVDKFLLTVRKNNGMLILATQQPEHVLESPLGASLVAQCMTKIFYPSPTADRSAYIDGLKCTEKEFQAIREDMTVGSRKFLLKRESGSVICEFDLRDMREYVAVLSGRANTVRFAARLREAQEGNSSGWLSEFMARHHEAED | A possible function of virB4 might be to provide the energy, via hydrolysis of ATP, for translocation of virulence proteins of the transfer of a T-DNA-protein complex across the agrobacterium membrane. | P0A3W1 |
Q21MR4 | TRPD_SACD2 | Anthranilate phosphoribosyltransferase | Saccharophagus | MNIKDALALVVNGKDLSVEQMTDVMREVMTGKATDAQRGAFLVALRIKSETLDEITGAAKVMRELATKVVVNADNLVDTCGTGGDGANLFNVSTASAFVVAAAGGHVAKHGNRSVSSSTGSADVLEAAGVNLQMPADQVARAIETIGVGFMFAPAHHSAMKHAIGPRKELGLRTIFNMLGPMTNPAGVKNQVIGVFTKALCRPMAEVLGRLGSEHVLVVHSEDGLDELSIAAPSHVAEYHKGNVTEYTLSPADVGIEMQSLEGLGVATAEESLALINGAFAGSDEPAAQKAAAIIALNAGAAIYVSGLATSFKDGVAMAEDALATGAAREKLKELVEFSAL | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q21MR4 |
O84315 | TAL_CHLTR | Transaldolase | Chlamydia | MSSQFDQLKLWSVLVGDTGDPALIKTLGVQDATTNPSLILKVAQEPKYQSMLTEAISWGIRQNGDDVQTLTFVLDKIQVNLGLEILKHVPGRVSLEIDARLSFNTEAMVQRAIFLSQLFEKMGGDKKRLLVKIPGTWEGICAAEVLESQGIACNVTLIFNLVQAIAAAKAKVTLVSPFVGRIYDWWIAAYGAEGYSIEADPGVASVANIYSYYKKFDIPTQIMAASFRTKEQVLALAGCDFLTISPKLLEELKKDQQPVERKLSVEEAKKLDIQPVELSESVFRFLMNEDAMATEKLAEGIRIFSGDTQILESAVTEFIRQIAAQEA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | O84315 |
Q2IM25 | THIE_ANADE | Thiamine-phosphate pyrophosphorylase | Anaeromyxobacter | MPVSEASVSAGRRARLGGLYVIVGGADPVAQARAAIGGGARAIQVRMKDAPAGAVLEATRRILALATGRALVLVNDRADLALLAGADGVHLGDDDLPVPEARRLLGPDLLVGRTTRTLEEARAALAEGADHVGYGPIFASRSKALPVPPRGLAALAEVARALPAPVVAIGGIGLDDVAAVARAGAACAAVIEAVLGAADPEAAAARMQAAFEAGRAARGATP | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | Q2IM25 |
Q48P32 | THIC_PSE14 | Thiamine biosynthesis protein ThiC | Pseudomonas | MSTTLKNAAHLSESAQVDSGSVQPFTRSQKIYVQGSRPDIRVPMREITLDVTPTDFGGEINAPVTVYDTSGPYTDPNVIIDVRKGLADVRSPWIDSRNDTERLAGLSSNFGQQRLSDAELTALRFAHVRNPRRANAGANVSQMHYARQGIITAEMEYVAIRENMKLQEARAAGLRTQQNAGHSFGASIPKEITAEFVREEIARGRAIIPANINHVELEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVGGAAEDLTWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHQENFLYTHFEDICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTKIAWKHDVQTMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARSYHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVREYAANQRIEAVDVDVAKGLAEQAERFKQEGSQLYKKV | 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. | Q48P32 |
P19813 | TREA_RABIT | Alpha,alpha-trehalose glucohydrolase | Oryctolagus | MPGSTWELHLLLLLGLGLGSEQALPPPCESQIYCHGELLHQVQMARLYPDDKQFVDMPLSTAPDQVLQSFAELAATYNNTVPREQLEKFVQEHFQAVGQELESWTPGDWKESPQFLQKISDPKLRAWAEQLHLLWKKLGKKIKPEVLSQPERFSLIYSQHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMAETVKGMLQNFLDLVTAYGHIPNGGRVYYLQRSQPPLLTLMMDRYVAHTGDLAFLRENIETLALELDFWAENRTISVSSGGNSHTLNRYHVPYGGPRPESYSKDTELAHTLPEGSWETLWAELKAGAESGWDFSSRWLVGSPNPDSLGSIRTSKLVPVDLNAFLCQAEELLSGFYSRLGNESQATKYRNLRAQRIAALTALLWDEDKGAWFDYDLENQKKNHEFYPSNLTPLWAGCFSDPAIADKALQYLQDSQILNHRHGIPTSLQNTGQQWDFPNAWAPLQDLVIRGLAKSPSARTQEVAFQLAQNWIRTNFDVYSQRSAMYEKYDISNAQPGGGGEYEVQEGFGWTNGVALMLLDRYGDRLSSGTQLALLEPHCLAAALLLSFLTR | Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose. | P19813 |
Q9P2D8 | UNC79_HUMAN | Protein unc-79 homolog | Homo | MSTKAEQFASKIRYLQEYHNRVLHNIYPVPSGTDIANTLKYFSQTLLSILSRTGKKENQDASNLTVPMTMCLFPVPFPLTPSLRPQVSSINPTVTRSLLYSVLRDAPSERGPQSRDAQLSDYPSLDYQGLYVTLVTLLDLVPLLQHGQHDLGQSIFYTTTCLLPFLNDDILSTLPYTMISTLATFPPFLHKDIIEYLSTSFLPMAILGSSRREGVPAHVNLSASSMLMIAMQYTSNPVYHCQLLECLMKYKQEVWKDLLYVIAYGPSQVKPPAVQMLFHYWPNLKPPGAISEYRGLQYTAWNPIHCQHIECHNAINKPAVKMCIDPSLSVALGDKPPPLYLCEECSERIAGDHSEWLIDVLLPQAEISAICQKKNCSSHVRRAVVTCFSAGCCGRHGNRPVRYCKRCHSNHHSNEVGAAAETHLYQTSPPPINTRECGAEELVCAVEAVISLLKEAEFHAEQREHELNRRRQLGLSSSHHSLDNADFDNKDDDKHDQRLLSQFGIWFLVSLCTPSENTPTESLARLVAMVFQWFHSTAYMMDDEVGSLVEKLKPQFVTKWLKTVCDVRFDVMVMCLLPKPMEFARVGGYWDKSCSTVTQLKEGLNRILCLIPYNVINQSVWECIMPEWLEAIRTEVPDNQLKEFREVLSKMFDIELCPLPFSMEEMFGFISCRFTGYPSSVQEQALLWLHVLSELDIMVPLQLLISMFSDGVNSVKELANQRKSRVSELAGNLASRRVSVASDPGRRVQHNMLSPFHSPFQSPFRSPLRSPFRSPFKNFGHPGGRTIDFDCEDDEMNLNCFILMFDLLLKQMELQDDGITMGLEHSLSKDIISIINNVFQAPWGGSHTCQKDEKAIECNLCQSSILCYQLACELLERLAPKEESRLVEPTDSLEDSLLSSRPEFIIGPEGEEEENPASKHGENPGNCTEPVEHAAVKNDTERKFCYQQLPVTLRLIYTIFQEMAKFEEPDILFNMLNCLKILCLHGECLYIARKDHPQFLAYIQDHMLIASLWRVVKSEFSQLSSLAVPLLLHALSLPHGADIFWTIINGNFNSKDWKMRFEAVEKVAVICRFLDIHSVTKNHLLKYSLAHAFCCFLTAVEDVNPAVATRAGLLLDTIKRPALQGLCLCLDFQFDTVVKDRPTILSKLLLLHFLKQDIPALSWEFFVNRFETLSLEAQLHLDCNKEFPFPTTITAVRTNVANLSDAALWKIKRARFARNRQKSVRSLRDSVKGPVESKRALSLPETLTSKIRQQSPENDNTIKDLLPEDAGIDHQTVHQLITVLMKFMAKDESSAESDISSAKAFNTVKRHLYVLLGYDQQEGCFMIAPQKMRLSTCFNAFIAGIAQVMDYNINLGKHLLPLVVQVLKYCSCPQLRHYFQQPPRCSLWSLKPHIRQMWLKALLVILYKYPYRDCDISKILLHLIHITVNTLNAQYHSCKPHATAGPLYSDNSNISRYSEKEKGEIELAEYRETGALQDSLLHCVREESIPKKKLRSFKQKSLDIGNADSLLFTLDEHRRKSCIDRCDIEKPPTQAAYIAQRPNDPGRSRQNSATRPDNSEIPENPAMEGFPDARRPVIPEVRLNCMETFEVKVDSPVKPAPKEDLDLIDLSSDSTSGPEKHSILSTSDSDSLVFEPLPPLRIVESDEEEETMNQGDDGPSGKNAASSPSVPSHPSVLSLSTAPLVQVSVEDCSKDFSSKDSGNNQSAGNTDSALITLEDPMDAEGSSKPEELPEFSCGSPLTLKQKRDLLQKSFALPEMSLDDHPDPGTEGEKPGELMPSSGAKTVLLKVPEDAENPTESEKPDTSAESDTEQNPERKVEEDGAEESEFKIQIVPRQRKQRKIAVSAIQREYLDISFNILDKLGEQKDPDPSTKGLSTLEMPRESSSAPTLDAGVPETSSHSSISTQYRQMKRGSLGVLTMSQLMKRQLEHQSSAPHNISNWDTEQIQPGKRQCNVPTCLNPDLEGQPLRMRGATKSSLLSAPSIVSMFVPAPEEFTDEQPTVMTDKCHDCGAILEEYDEETLGLAIVVLSTFIHLSPDLAAPLLLDIMQSVGRLASSTTFSNQAESMMVPGNAAGVAKQFLRCIFHQLAPNGIFPQLFQSTIKDGTFLRTLASSLMDFNELSSIAALSQLLEGLNNKKNLPAGGAMIRCLENIATFMEALPMDSPSSLWTTISNQFQTFFAKLPCVLPLKCSLDSSLRIMICLLKIPSTNATRSLLEPFSKLLSFVIQNAVFTLAYLVELCGLCYRAFTKERDKFYLSRSVVLELLQALKLKSPLPDTNLLLLVQFICADAGTKLAESTILSKQMIASVPGCGTAAMECVRQYINEVLDFMADMHTLTKLKSHMKTCSQPLHEDTFGGHLKVGLAQIAAMDISRGNHRDNKAVIRYLPWLYHPPSAMQQGPKEFIECVSHIRLLSWLLLGSLTHNAVCPNASSPCLPIPLDAGSHVADHLIVILIGFPEQSKTSVLHMCSLFHAFIFAQLWTVYCEQSAVATNLQNQNEFSFTAILTALEFWSRVTPSILQLMAHNKVMVEMVCLHVISLMEALQECNSTIFVKLIPMWLPMIQSNIKHLSAGLQLRLQAIQNHVNHHSLRTLPGSGQSSAGLAALRKWLQCTQFKMAQVEIQSSEAASQFYPL | Auxiliary subunit of the NALCN sodium channel complex, a voltage-gated ion channel responsible for the resting Na(+) permeability that controls neuronal excitability. Activated by neuropeptides substance P, neurotensin, and extracellular calcium that regulates neuronal excitability by controlling the sizes of NALCN-dependent sodium-leak current. | Q9P2D8 |
P34220 | YBF5_YEAST | Deoxyribonuclease Tat-D | Saccharomyces | MWGILLKSSNKSCSRLWKPILTQYYSMTSTATDSPLKYYDIGLNLTDPMFHGIYNGKQYHPADYVKLLERAAQRHVKNALVTGSSIAESQSAIELVSSVKDLSPLKLYHTIGVHPCCVNEFADASQGDKASASIDNPSMDEAYNESLYAKVISNPSFAQGKLKELYDLMNQQAKPHDTSFRSIGEIGLDYDRFHYSSKEMQKVFFEEQLKISCLNDKLSSYPLFLHMRSACDDFVQILERFIAGFTDERDTFQLQKLGASSSSGFYKFHPDRKLVVHSFTGSAIDLQKLLNLSPNIFIGVNGCSLRTEENLAVVKQIPTERLLLETDAPWCEIKRTHASFQYLAKYQEVRDFEYPAFKSVKKNKLADKLNAEELYMVKGRNEPCNMEQVAIVVSEVKDVDLATLIDTTWKTTCKIFGE | Has both endo- and exonuclease activities. Incises double-stranded DNA without obvious specificity via its endonuclease activity and excises the DNA from the 3'-to 5'-end by its exonuclease activity. May have a role in apoptosis. | P34220 |
Q40286 | UFOG4_MANES | UDP-glucose flavonoid 3-O-glucosyltransferase 4 | Manihot | CNKLKLDKAERGDKASVDNTELLKWLDLWEPGSVIYACLGSISGLTSWQLAELGLGLESTNQPFIWVIREGEKSEGLEKWILEEGYEERKRKREDFWIRGWSPQVLILSHPAIGAFFTHCGWNSTLEGISAGVPIVACPLFAEQFYNEKLVVEVLGIGVSVGVEAAVTWGLEDKCGAVMKKEQVKKAIEIVMDKGKEGEERRRRAREIGEMAKRTIEEGGSSYLDMEMLIQYVSERSPSRA | In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. | Q40286 |
Q07271 | TFS_SULAC | Transcription elongation factor IIS/RNA polymerase subunit homolog | Sulfolobus | MKFCPKCGSMMMPRKENGKTVYKCSKCGYIDTENQKEAKITTVIKHSAKEKTLVLESDMPKTGVQLTRGISCPSCGNDEAYFWILQTRSADEPATRFYKCTKCGKVWREYE | Induces RNA cleavage activity in the RNA polymerase. In its presence, the cleavage activity of the RNA polymerase truncates the RNA back to position +15 in a stepwise manner by releasing mainly dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs are able to continue elongation. Involved in transcriptional proofreading and fidelity. Misincorporation of nucleotides during elongation of transcription leads to arrested elongation complexes which are rescued by TFS-promoted removal of a dinucleotide from the 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled elongation complexes (resulting from the next missing nucleotide or a reduced incorporation rate of a wrong nucleotide) preventing misincorporation and enabling proofreading in a post-incorporation manner. Pausing of elongation complexes is the main determinant of TFS-induced RNA cleavage. | Q07271 |
O59819 | UGPA2_SCHPO | UDP-glucose pyrophosphorylase | Schizosaccharomyces | MLHRRIHFKSQSTLDFDSVAVSISASTMKNELDKLVLNSRVSDKKTFGIQMDNFFALYRRYLLHTVKGYECDWDSIRPLGPEDMIDYGDLPLCKNAGKYLNRLAVVKLNGGMGNALGVNYPKAMIEVRDNQSFLDLSIRQIEYLNRRYDVSVPFILMNSYDTNDETCKVLRKYAGCKIDISTFEQSRYPRVFVDSQLPVPKAAPSPIEEWYPPGHGDIFDALVHSGTIERLLAQGKDYLFVSNIDNLGASVDLNILSHVIDNQIEYSMEITDKTKADIKVGILVNQDGLLRLLETNQVPEQHREEFMSDKVFKYINTNNVWLYLPAVKRVVENRELNLDIMPNIETVYYNNEPARIIEFTTAIGSAISQFKKTEGIRVSRPRFISVKNSSDLFLVRCDLYNVDHGSLKIEESRLGFPPPVVRMSNEFKDIAELFCRIPYMPSMKDLVSLSISGNVYFGRNVILKGNIVIVASENTILCIPSNAVLENCVVTGNCKIMEC | Plays a central role as a glucosyl donor in cellular metabolic pathways. | O59819 |
Q9LVW6 | THA8_ARATH | Protein EMBRYO DEFECTIVE 3123 | Arabidopsis | MALSLSQTRPPSLSHSHTLSVIVPKRTFVSIRCGPRDNRGPLLKGRILSTEAIQSIQSLKRAHRTGVSLSLTLRPLRRLIKSDLISVLRELLRQDYCTLAVHVLSTLRTEYPPLDLVLYADIVNALTRNKEFDEIDRLIGEIDGIDQRSDDKALAKLIRAVVGAERRESVVRVYTLMRESGWGSESWEADEYVAEVLSKGLLRLGEPDLASQVSLKSSILKP | Essential protein required during embryogenesis . Mediates group II organellar RNA introns splicing (e.g. ycf3-2 and trnA) . Binds weakly to specific RNA . Promotes the biogenesis of chloroplast thylakoid membranes . | Q9LVW6 |
A4JMC2 | TRUA_BURVG | tRNA-uridine isomerase I | Burkholderia cepacia complex | MRIALGVQYDGAAFCGWQAQPHGKTVQDALERALGEFACVPLHTTVAGRTDTGVHGLGQVVHFDTALDRAEFSWVRGTNAFLPPTVSVQWAKAMPDTFHARFSAFERTYYYALYVHPVRSPMLAGRAGWIHTPLDDDAMRAAAVHLIGEHDFSSFRSSECQSKTPVKHLYQIDVRRSGHFIHFRFRANAFLHHMVRNLMGCLVAVGRGRYPADWLADVLAGRDRNLAAPTFMADGLYLAHVGYPAEFAVPPAQLGSVPWSSVWADLDPQP | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | A4JMC2 |
Q8TB69 | ZN519_HUMAN | Zinc finger protein 519 | Homo | MELLTFRDVAIEFSPEEWKCLDPAQQNLYRDVMLENYRNLVSLAVYSYYNQGILPEQGIQDSFKKATLGRYGSCGLENICLWKNWESIGEGEGQKECYNLCSQYLTTSHNKHLTVKGDKEYRIFQKKPQFLSAAPTEPCIPMNKYQHKFLKSVFCNKNQINFNHDSNISKHHSTHFLENYYNCNECEKVFYQSSKLIFPENIHIQKKPYNSNECGETSDPFSKLTQHQRIYIGESSQRCNKKCIIVFSQSHLKGHKIINTGEKSVKYKERGKAFTRGLHLGHQKIHTGEKPYKCKKCDKAFNKSSHLAQHQRIHTGEKPFKCKECGKAFNRGSYLTQHQRIHTGERAFKCEECGKAFNRGSYLTQHQRIHTGEKPFRCKECGKAFNRSSYVTQHQRMHTGEKPFKCKECGKAFNRASHLTQHQRIHTGEKHFKCKECGKAFNRGSHLTRHQRIHTGEKSFKCEECGKAFIWGSHLTQHQRVHTGEKFFKCKECGKAFTRSSHLTQHQRIHTGEKPFKCKECGKAFNRRSTLTQHQIIHTR | May be involved in transcriptional regulation. | Q8TB69 |
Q8IWB7 | WDFY1_HUMAN | Zinc finger FYVE domain-containing protein 17 | Homo | MAAEIHSRPQSSRPVLLSKIEGHQDAVTAALLIPKEDGVITASEDRTIRVWLKRDSGQYWPSIYHTMASPCSAMAYHHDSRRIFVGQDNGAVMEFHVSEDFNKMNFIKTYPAHQNRVSAIIFSLATEWVISTGHDKCVSWMCTRSGNMLGRHFFTSWASCLQYDFDTQYAFVGDYSGQITLLKLEQNTCSVITTLKGHEGSVACLWWDPIQRLLFSGASDNSIIMWDIGGRKGRTLLLQGHHDKVQSLCYLQLTRQLVSCSSDGGIAVWNMDVSREEAPQWLESDSCQKCEQPFFWNIKQMWDTKTLGLRQHHCRKCGQAVCGKCSSKRSSYPVMGFEFQVRVCDSCYDSIKDEDRTSLATFHEGKHNISHMSMDIARGLMVTCGTDRIVKIWDMTPVVGCSLATGFSPH | Positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines . | Q8IWB7 |
A0KNH6 | TORD_AERHH | Chaperone protein TorD | Aeromonas | MQEFLATSERRAELYWWFATLFTAQLSDEQIAEYDSYDVRSFLKSLSTLDPMRPAVAELNDAIARLLVRPERANALAGDFHELFLANDAVSPHESAHQDAAALERMKARLSRLNIDVSAKYQQPVDHLGVELDLMGNLIIRAAEAASADLRERWLGEQEALLHGHLLAWFPHFERACRAADPFGFYGASARLLGVFLTMDANYLSLVKPAPAAD | Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. | A0KNH6 |
Q9L9J1 | THIG_SALTY | Thiazole synthase | Salmonella | MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETKAMLEIIIQQSTVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVMMATAFRLAVEAGVLARQAVPGNRSTYANATSPLTGFLEALA | 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. | Q9L9J1 |
Q9GDV1 | YCF4_CARCL | Photosystem I assembly protein Ycf4 | Carpobrotus | MNWRSKRIWIELITGSRKISNFCWAFILFLGSLGFLLVGISSYLGRNLISLFPPQQILFFPQGIVMSFYGIAGLFISSYLWCTISWNVGSGYDRFDRKEGIVCIFRWGFPGKNRRIFLRFLIKDIQSIRIELKEGIYTRRVLYLEIRGQGAIPLTRTDDNLTPREIEQKAAELAYFLRIPIEVF | Seems to be required for the assembly of the photosystem I complex. | Q9GDV1 |
A6NCJ1 | TKTI1_HUMAN | Tektin bundle interacting protein 1 | Homo | MQTLRQEAARPCIPSGTLEASFPAPLYSDDYLSLEGSRWPPAIRQATRWKYTPMGRDAAGQLWYTGLTNSDAWEAWYNLPRAPASPFREAYNRWHSCYQHRECSMPSAYTQHLRETAWHDPIVPAQYQAPSTRWGSALWKDRPIRGKEYVLNRNRYGVEPLWRASDYVPSLSAPQRPPGTTQNYREWVLEPYCPSTCQRSPPSLTPTPR | Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Located at the center of the tektin bundle where may function to recruit tektins or stabilize the bundle. | A6NCJ1 |
Q2Y5S3 | UBIA_NITMU | 4-HB polyprenyltransferase | Nitrosospira | MTLTQRLVHYEKLMRLDKPIGILLLLWPTLWGLWLAAEGVPRLDILLIFVLGTVLMRSAGCVVNDYADRNFDGHVERTRTRPLALGAVSTREALLLAAGLSLVAFLLIQPLNRLTIELSFVALFLAASYPFTKRFFAMPQAYLGIAFSFGIPMAFAAQTGEVPFPAWFLMGANLLWVIAYDTEYAMVDKVDDLRIGIKTSAITFGRFDVVGVVLCHMAFLAGMVAIGLLQNLGVIYYIGLATALGLILYQYRLIHDRDRARCFKAFLHNNWVGATIFAGIVLDYLVRAAS | 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. | Q2Y5S3 |
Q9BTA9 | WAC_HUMAN | WW domain-containing adapter protein with coiled-coil | Homo | MVMYARKQQRLSDGCHDRRGDSQPYQALKYSSKSHPSSGDHRHEKMRDAGDPSPPNKMLRRSDSPENKYSDSTGHSKAKNVHTHRVRERDGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPYDSADDWSEHISSSGKKYYYNCRTEVSQWEKPKEWLEREQRQKEANKMAVNSFPKDRDYRREVMQATATSGFASGMEDKHSSDASSLLPQNILSQTSRHNDRDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTSSVPAQKTERKESTSGDKPVSHSCTTPSTSSASGLNPTSAPPTSASAVPVSPVPQSPIPPLLQDPNLLRQLLPALQATLQLNNSNVDISKINEVLTAAVTQASLQSIIHKFLTAGPSAFNITSLISQAAQLSTQAQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPIKPLISTPPVSSQPKVSTPVVKQGPVSQSATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNASNATVVPQNSSARSTCSLTPALAAHFSENLIKHVQGWPADHAEKQASRLREEAHNMGTIHMSEICTELKNLRSLVRVCEIQATLREQRILFLRQQIKELEKLKNQNSFMV | Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1) . Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription . Regulates the cell-cycle checkpoint activation in response to DNA damage . Positive regulator of amino acid starvation-induced autophagy . Also acts as a negative regulator of basal autophagy . Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation . May negatively regulate the ubiquitin proteasome pathway . | Q9BTA9 |
A8AGD8 | ZNTB_CITK8 | Zinc transport protein ZntB | Citrobacter | MEAIKGSEVNVPDAVFAWLLDGRGGIKPLENDDIIDSQHPCWLHLNYTHPDSAQWLASTPLLPNSVRDALAGESSRPRVSRMGEGTLITLRCINGSTDERPDQLVAMRVYMDERFIVSTRQRKVLALDEVVSDLQEGTGPSDCGGWLVDVCDALTDHASEFIEQLHDKIIDLEDNLLDQQIPPRGFLALLRKQLIVMRRYMAPQRDVYARLASERLAWMNDDQRRRMQDIADRLGRGLDEIDACIARTGVMADEIAQVMQESLARRTYTMSLMAMVFLPSTFLTGLFGVNLGGIPGGAWHFGFSMFCILLVVLIGGVTLWLHRSKWL | Zinc transporter. Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake. | A8AGD8 |
F4IG60 | ZPR1_ARATH | Protein LITTLE ZIPPER 1 | Arabidopsis | MQREHKTHNKLSFIYITPLYISPINQTRLTYLSSSFLLSSSSKMCLSSSETFSDTPTRLVLYLKTQSHVRIPRLSRRRRMWREEKKMEMINLKLYVENQNIIRENEKLKKKALLLHQENKTLFSLLQTKKLSSVHK | Competitive inhibitor of the HD-ZIPIII transcription factors in shoot apical meristem (SAM) development. Acts by forming non-functional heterodimers. Part of a negative feedback loop. Essential for proper functioning of stem cells in the SAM. | F4IG60 |
Q2GW27 | VAC8_CHAGB | Vacuolar protein 8 | Chaetomium | MGICSSSCCGGKSRDALYENVLAENEREAVADLLQYLENRAETDFFSGEPLRALSTLVYSDNIDLQRSASLTFAEITERDVRAVDRDTLGPILFLLENSDIEVQRAASAALGNLAVNTDNKVLIVQLGGLQPLIKQMMSPNVEVQCNAVGCITNLATHEENKAKIARSGALGPLTRLAKSKDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSSDVDVQYYCTTALSNIAVDANNRRKLAETEQRLVQYLVNLTESSSPKVQCQAALALRNLASDEKYQLEIVQAHGLGPLLRLLRSSYLPLILSAVACIRNISIHPQNESPIIEAGFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKSLVLEAGAVQKCKQLVLEVPVTVQSEMTAAIAVLALSDELKTHLLELGVFDVLIPLTMSPSVEVQGNSAAALGNLSSKVGDYSIFVQNWMEPRDGIHGYLNRFLASGDATFQHIAIWTLLQLLESEDKKLIGLIGKSDGVVDMIKQIANRQMMESDNEAEDDDEGEVVNLAQRCLELLGQGGSKSHIEG | Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. | Q2GW27 |
A5WCC7 | TSAD_PSYWF | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Psychrobacter | MKVLGLETSCDETGLAIFDSELLAEGKNGLLGQVLYSQIELHATYGGVVPELASRDHIRKLVPLLDELLAQCDISKDEIDAIAYTKGPGLIGALMTGALFGRSLAYGLDVPAIGIHHMEGHLLSPLLGPNPPKFPFVSLLVSGGHTLLVAAHGIGEYEILGESIDDAAGECFDKAAKMLGLPYPGGPNVARLAEQGDPLKYELPRPMLHRGLDFSFSGMKTAVHNLIKDTPGSDNDEQVRADIAASFQHAVVDTLVKKCVKALKQTGMKQLVIAGGVSANLHLRQTLEQQLAKIGATVHYAPLELCTDNGAMIAYAGYQRLQAGQQDALSVSCVPRWNISDLPALAQ | 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. | A5WCC7 |
A8H2X4 | TRPB_SHEPA | Tryptophan synthase beta chain | Shewanella | MSKLNPYFGEYGGMYVPQILMPALKQLETAFIEAQEDESFQQEFTELLKNYAGRPTALTLTRNLSPNPLTKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLGLKCKVYMGAKDVERQSPNVFRMKLMGAEVIPVTSGSATLKDACNEAMRDWSGSYDKAHYLLGTAAGPHPFPTIVREFQRMIGEETKSQILEREGRLPDAVIACVGGGSNAIGMFADFIDEEEVALIGVEPAGKGIDTPMHGAPLKHGKTGIFFGMKAPLMQDSEGQIEESYSVSAGLDFPSVGPQHAHLAATGRATYESATDDEALEAFQLLARSEGIIPALESAHALAYAVKLAKEATKETILVVNLSGRGDKDIFTVADILEQQKVEQQEAEQQQTNNQNN | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | A8H2X4 |
Q8BTV1 | TUSC3_MOUSE | Protein N33 | Mus | MSARAAPSRRRQAGRRLRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFVKAPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYSSAFCNKLFFGMVDYDEGTDVFQQLNMNSAPTFMHFPSKGRPKRADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQAQFVAESHIILVLNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSFLIK | Magnesium transporter. | Q8BTV1 |
Q12KS4 | YQGF_SHEDO | Putative pre-16S rRNA nuclease | Shewanella | MTMNQTVLGFDYGTKSIGVAVGQSITASASPLLALKAQDGIPNWDEIEKLIKEWQPDLVVVGLPLNMDGTEQDITQRAKKFANRISGRFGVKVLTQDERLTTADAKARLFELGGYKALTKGQVDAVSAVLIIESYFENQYD | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q12KS4 |
Q3ILA5 | UBIG_PSET1 | 3-demethylubiquinone 3-O-methyltransferase | Pseudoalteromonas | MTEHQNVDHAEIAKFEAIAERWWDLDGEFKPLHEINPLRLDFIANKTGGLFDKETLDVGCGGGILSQSMARMGAKVTGIDMGQEPLTVAKLHSLETGVNVEYIKVPAEQYASEHPARFDVVTCMEMLEHVPDPASIIHAVAELAKPGADVFFSTLNKTPKAYLYAIIGAEKLLKMVPEGTHDHKKFIKPAQLIAWAEQAGLKVRASAGLSYNPLSKQYSLNTDVSVNYILHFEKLA | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q3ILA5 |
Q60WL8 | TM258_CAEBR | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258 | Caenorhabditis | MDISKMDRYAAPVHFSSLPLLATVLCGVGLLLLAAFTMLQVTSTKYNRNVFKELFIAATSSIFLGFGSVFLLLWVGIYV | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. | Q60WL8 |
P58305 | TXGRX_BUNCN | Granulitoxin | Bunodosoma | AKTGILDSDGPTVAGNSLSGT | Injection into mice produces severe neurotoxic effects such as circular movements, aggressive behavior, dyspnea, tonic-clonic convulsion and death. | P58305 |
B8XA40 | ZFPS_SOLHA | Z,Z-farnesyl pyrophosphate synthase | Solanum subgen. Lycopersicon | MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLSLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLDVSEGHKHLFPKLKEICDISSKLGIQVITAFAFSTENWKRAKGEVDFLMQMFEELYDEFSRSGVRVSIIGCKTDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGDQRVSNFLLWQLAYTEFYFTKTLFPDFGEEDLKEAIINFQQRHRRFGGHTY | Specifically forms (2Z,6Z)-farnesyl diphosphate (Z,Z-FPP) from dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP). Also able to use nerylpyrophosphate (NPP) as substrate. Involved in the biosynthesis of several sesquiterpenes. | B8XA40 |
Q5NFN4 | UVRB_FRATT | Excinuclease ABC subunit B | Francisella | MNKFNLVTKYAPAGDQPQAIQSLVNGINTGLQHQVLLGVTGSGKTYTMANVIQQTQKPCLILAHNKTLAAQLYSEFKQYFPDNAVEYFVSYYDYYQPEAYIAASDTYIEKDSSVNEHIEQMRLSATKAILERNDVIIVATVSAIYGLGDPEQYMQMLLHLKVGEELGLKKAQTKLVEMQYSRNDMDFSRGSFRVRGEVLDIFPADSEKDAIRVEFFDDEIEAISVIDSLTSKKLKSLHRATIFPSTHYVASKERKEIVIEDIKKELKERVKYFEKEGKLLEAQRIEQRTKYDIEMIQELGYCTGIENYSRLLSGRAPGYPPPTLIDYLPENALVIVDESHVTLPQFGGMYKGDLSRKSNLVNYGFRLPSALDNRPLKFNEFESLLPQTIYVSATPANYELEKSQNTVQQVIRPTGLLDPEVFVRPVAIQVEDALSEINKAIAKEERVLITTLTKKMVENLTEYLSEHGVNVRYLHSDIDTVERVQIIHDLRHGVFDVLVGINLLREGLDMPEVGVLLIFDADKEGFLRSEKSLIQTIGRVARNQNGRAILYADVVTKSMQKAMDETLRRRKLQDEYNQKHNIVPKTIIKNIDDMLDSSPEMQKRAYKNNLRLKVDDVDVSAILGMTEATKVIKALEKRMRAYAKELEFEKATTIRDKITEVKQKFINL | 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. | Q5NFN4 |
B7KC96 | UVRB_GLOC7 | Excinuclease ABC subunit B | Gloeothece citriformis | MNLFHLQAPFQATGDQPQAIAQLVNSIEKGNRFQTLLGATGTGKTFTIAATIEKIGKPTLVLAHNKTLAAQLCNELRQFFPENAVEYFISYYDYYQPEAYIPVSDTYIEKSASINDEIDMLRHSATRSLFERRDVVVVASISCIYGLGMPSEYLKASIGLEVGKEINQRQLLRDLVSVQYSRNDLDLQRGRFRLRGDVLELVPAYEDRVIRVEFFGDEIDAIRYLDPVTGNSLQSLERVNIYPARHFVTPDDQLEAACQGIELELEDRLEELEKQGKLLEAQRLGQRTRYDLELLREVGYCNGVENYSRYLAGREPGQPPECLIDYFPKDWLLVIDESHVTIPQLRGMYNGDQARKKVLIEHGFRLPSAADNRPLKAEEFWEKVNQCVFVSATPGNWEIEQSQGQVIEQIIRPTGVLDPEIFVRPTEGQVDDLLGEIKQRIKRKERVLITTLTKRMAEDLTEYFQERGVKVQYLHSEISSIERIEILQNLREGEFDVLIGVNLLREGLDLPEVSLVAILDADKEGFLRAERSLIQTIGRAARHIQGQAILYADNLTDSMIKAMEETERRRNIQMAHNKRHGITPQPIVTRSSNAILSFLDISRRLNAQQLEKVYDQADELPLEKVPELIGQLEEQMKEAAKKLEFEEAAKYRDRIQHLRDKLLGH | 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. | B7KC96 |
A8FFL2 | Y2363_BACP2 | Uncharacterized methyltransferase BPUM_2363 | Bacillus | MGREFLSLFDHWADSYDDTVSGHDEQYEEVFRRYSVILKEIVHRAGQHVLEFGSGTGNLTAALLAADKNVFGVEPSDAMKKAALQKGIPDVFHDGDFLSFPAPPFEPDTIVSSYAFHHLTDEEKKQAIHTYSNILHSDGKIVFADTMFQNQSAHQAEIDKAKAAGFDQLAEDLETEYYPSIDVLKQIFEEEGFSTSFHQMNDFVWIVEAKKRE | Could be a S-adenosyl-L-methionine-dependent methyltransferase. | A8FFL2 |
P50143 | TCPG_XENLA | CCT-gamma | Xenopus | MMGRPVLVLSQNMKRESGRKVQSGNINAAKTIADIIRTCLGPRAMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEQFLEQQMHPTVIISAYRKALDDMVNTLKEISTPVDTNDRELMLKIINSAINTKAIKLWADMACGIALDAVKTVELEENGRKEIDIKKYAKVEKIPGGIIEDSCVLRGVMVNKDVTHPKMRRLIKNPRIILLDCSLEYKKGESQTEIEITREEDFARILQMEEEYIQQVCEDIIRLKPDVVITEKGISDLAQHYLVKANITAVRRVRKTDNNRIARACGARIASRTDELREEDVGTGAGLFEIKKIGDEYFTFITDCKDPKACTIVLRGASKEILAEVERNLQDAMQVCRNVVIDPYLVPGGGASEMSVAHILTEKSKTMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRILTSLRAKHTQEGCQTWGVDGEAGVLADMKELGIWEPLAVKLQTYKTAVETAILLLRIDDIVSGHKKKGEDHGRQPAAAPEAPQQAE | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. | P50143 |
A7MRY6 | YCIB_VIBC1 | Inner membrane-spanning protein YciB | Vibrio | MKQILDFIPLIVFFALYKMYDIYVATGALIVATAIQIVLTFALYKKVEKMQLITFAMVAIFGGMTIFLHDENFIKWKVTIVYAIFAIGLAVSHAMGKSAIKGMLGKEITLPDAIWTKINWAWVAFFSFCAGLNVYVAFELPLDVWVNFKVFGLLIATFAYMIATGFYIYKHMPKEQKEQKEKSSDVSLDD | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A7MRY6 |
A8IC06 | YACG_AZOC5 | DNA gyrase inhibitor YacG | Azorhizobium | MSDETAKPFEPKPCPICGKPSIERYKPFCSKRCADVDLNRWLTGAYAIPVVEEEDEDGEPLSPPLRPE | Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase. | A8IC06 |
F1QMV3 | TPC6B_DANRE | Trafficking protein particle complex subunit 6b | Danio | MADEALFQFLHSEIIQYVNSAETGESENGRCVSKLENMGFRVGQGLIERFTKDTPRFKDELDVMKFICKDFWTSVFKKQIDNLRTNHQGIYVLQDNKFRLLTQLSAGKQYLEHAPKFLAFTCGLVRGALSNIGVKSIVTAEVSVMPACKFQVMIQKM | Component of a transport protein particle (TRAPP) complex that may function in specific stages of inter-organelle traffic. Specifically involved in the early development of neural circuitry, likely by controlling the frequency and amplitude of intracellular calcium transients implicated in the regulation of neuron differentiation and survival. | F1QMV3 |
Q1A7B3 | TNNC1_BLAGE | Troponin C, isoallergen Bla g 6.0101 | Blattella | MDELPPEQIQLLKKAFDAFDREKKGCISTEMVGTILEMLGHRLDDDMLQEIIAEVDADGSGELEFEEFVSLASRFLVEEDAEAMQQELREAFRLYDKEGNGYITTNVLREILKELDDKITAEDLDMMIEEIDSDGSGTVDFDEFMEVMTGE | Troponin is the central regulatory protein of striated muscle contraction. It consists of three components: Troponin-I (Tn-I) which is the inhibitor of actomyosin ATPase, Troponin-T (Tn-T) which contains the binding site for tropomyosin and Troponin-C (Tn-C). The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. | Q1A7B3 |
Q6D7Z8 | Y1177_PECAS | Nucleoid-associated protein ECA1177 | Pectobacterium | MFGKGGIGNLMKQAQQMQEKMQQMQEEVANLEVTGESGAGLVKITINGAHNCRRVEIDPSLMEDDKEMLEDLIAAAFNDAARRIAETQKEKMATVSSGMQLPPGFKMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q6D7Z8 |
Q0VGE8 | ZN816_HUMAN | Zinc finger protein 816 | Homo | MLREEATKKSKEKEPGMALPQGRLTFRDVAIEFSLEEWKCLNPAQRALYRAVMLENYRNLEFVDSSLKSMMEFSSTRHSITGEVIHTGTLQRHKSHHIGDFCFPEMKKDIHHFEFQWQEVERNGHEAPMTKIKKLTGSTDRSDHRHAGNKPIKDQLGLSFHSHLPELHMFQTKGKISNQLDKSIGASSASESQRISCRLKTHISNKYGKNFLHSSFTQIQEICMREKPCQSNECGKAFNYSSLLRRHHITHSREREYKCDVCGKIFNQKQYIVYHHRCHTGEKTYKCNECGKTFTQMSSLVCHRRLHTGEKPYKCNECGKTFSEKSSLRCHRRLHTGEKPYKCNECGKTFGRNSALVIHKAIHTGEKPYKCNECGKTFSQKSSLQCHHILHTGEKPYKCEECDNVYIRRSHLERHRKIHTGEGSYKCKVCDKVFRSDSYLAEHQRVHTGEKPYKCNKCGRSFSRKSSLQYHHTLHTGEKPYTCNECGKVFSRRENLARHHRLHAGEKPYKCEECDKVFSRRSHLERHRRIHTGEKPYKCKVCDKAFRSDSCLANHTRVHTGEKPYKCNKCAKVFNQKGILAQHQRVHTGEKPYKCNECGKVFNQKASLAKHQRVHTAEKPYKCNECGKAFTGQSTLIHHQAIHGCRETLQM | May be involved in transcriptional regulation. | Q0VGE8 |
Q3AB71 | TRMFO_CARHZ | Folate-dependent tRNA(M-5-U54)-methyltransferase | Carboxydothermus | MKEVDVVGAGLAGAEAAWQLAKRGIKVRLFEMRPKKFTPAHQTPLFAELVCSNSLGGINLDNAAGLLKEELRFLDSLVIKVADRNRIPAGNALAVDRNLFAEEVTLRLSHHPLIEVIREEVVDINPERVTVIASGPLTSKALAENLKKYLESDYLYFFDAVAPIVAGESLDMEKLFFAGRYQQDKDYLNAPMNEEEYLRFYEALITAERHPLKPFEKDIYYEGCLPIEVIASRGKDTLRFGPLKPKGIIDPRTGKEPYAVVQLRRENLAGDYYNLVGFQTNLTWKEQNRVFRLIPGLENAEFIRFGVMHKNTFINSPALLTPYLNLKKYPRLFFAGQITGGEGYVAAIATGAWAGIAASGMFGKMPEPLPETTMLGGLIRYLNTAPVENFQPMGVNFGLVKPLDRKIKNKKERYKLLAERSLKDLKRWLAVNG | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q3AB71 |
P49338 | WNT4_XENLA | Protein Wnt-4 | Xenopus | MTPEYFLRSLLMMILAVFSANASNWLYLAKLSSVGSISEEETCEKLKGPIQRQVQMCKRNLEVMDSVRRGAQLAIEECQYQFRNRRWNCSTLDTLPVFGKVVTQGTREAAFVYAISSAGVAFAVTRACSSGDLEKCGCDRTVHGVSPQGFQWSGCSDNILYGVAFSQSFVDVRERSKGGSSSRALMNLHNNEAGRKAILNNMRVECKCHGVSGSCEVKTCWKAMPTFRKVGNVLKEKFDGATEVEQKKIGSTKVLVPKNSQFKPHTDEDLVYLDSSPDFCDHDLKNGVLGTTGRQCNKTSKAIDGCELMCCGRGFHTEEVEIVERCSCKFHWCCFVKCKQCHKVVEMHTCR | Ligand for members of the frizzled family of seven transmembrane receptors. Plays an important role in embryonic kidney development. Acts downstream of Notch signaling during pronephric kidney development. During early pronephros development, patterns the proximal pronephric anlagen to promote glomus and nephrostome formation. Also required later in pronephros development for tubulogenesis. | P49338 |
Q8F5J7 | YBEY_LEPIN | Endoribonuclease YbeY | Leptospira | MNCKILFRKELNDSECELSLLLVGDSDMKEINRLRRGKDKTTDVLSFPLEFDFSPLQKILPKNTSSDQKMFPPIALGEIVISIDTLQKQAKEIGHSEKDEFYRLLVHGFLHLLGYDHERGDKEEHIMKLKEDECLEILQGL | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q8F5J7 |
Q7UDQ6 | TILS_SHIFL | tRNA(Ile)-lysidine synthetase | Shigella | MTLTLNRQLLTSRQILVAFSGGLDSTVLLHQLVQWRTENPGVTLRAIHVHHGLSANADAWVTHCENVCQQWQVPLVVERVQLAQEGLGIEAQARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSEFAGTRLIRPLLARTRGELEQWALAHGLRWIEDESNQDDSYDRNFLRLRVVPLLQQRWPHFAEATARSATLCAEQESLLDELLADDLAHCQTSQGTLQIAPMLAMSDARRAAIIRRWLAGQNAPMPSRDALVRIWQEVALAREDASPCLRLGAFEIRRYQSQLWWIKSITGQSETIVLWQTWLQPLELPAGLGTVQLTAGGDIRPPRADEAVSVRFKAPGLLHIVGRNGGRKLKKIWQELGVPPWLRDTTPLLFYGETLIAAAGVFVTQEGVAEGENGVSFVWQKTLS | 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. | Q7UDQ6 |
Q5FSH9 | TRHO_GLUOX | tRNA hydroxylation protein O | Gluconobacter | MSDTFEPIRIVALYHFTPFEDPAALRGPLLELCEKEGIKGILLLAREGINGTIAGTDEGMERVMAHIRALPGCADLESKDSRAPELPFRRMKVRLKKEIVTMGEPDIDPRQGVGRYVAPEDWNALISDPDTILIDTRNDYEVAIGTFKGAEDPKTKSFREFPEWFRRRRQELEAKGRLPKIAMFCTGGIRCEKSTSFARAEGVDEVYHLKGGILKYLETVPEEESLWEGECFVFDQRVSVKHGLEIGTHDVCHACRRPLNEKDKASPLFVQGVSCPHCHNERTEEQRHRYAERERQEALAQARRAGHLGVRQK | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q5FSH9 |
Q5RAW8 | WDR48_PONAB | USP1-associated factor 1 | Pongo | MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWILKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVNPMDEEENEVNHVNGEQENRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETESMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST | Regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46. Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. Also activates deubiquitinating activity of complexes containing USP12. Docks at the distal end of the USP12 fingers domain and induces a cascade of structural changes leading to the activation of the enzyme. Together with RAD51AP1, promotes DNA repair by stimulating RAD51-mediated homologous recombination. Binds single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). DNA-binding is required both for USP1-mediated deubiquitination of FANCD2 and stimulation of RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during these processes.Together with ATAD5 and by regulating USP1 activity, has a role in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Together with ATAD5, has a role in recruiting RAD51 to stalled forks during replication stress. | Q5RAW8 |
Q54C02 | UBA5_DICDI | Ubiquitin-like modifier-activating enzyme 5 | Dictyostelium | MATPYREKIEKMSSEVIDSNPYSRLMALKKMGIVNNYENIRNLSVIIVGLGGIGSVAAEMLTRCGIGKLLLFDYDTVEIANMNRLFFRPEQSGKSKTMAAQETLSSINPDVQFESHNYNITTIDNFEHFKGRIEKGGLVEGEPVDLVLGCVDNFEARTAINQACLELGKSWMESGVSENAISGHIQLIIPGESACFQCVPPLIVASGIDERTLKREGVCAASLPTTMGIVAGMLVQNTLKYLLKFGEVSSLLGYNALLDYFPKDNMKPNPECSNSFCIIHQQKYKEFLKNNPKENLIQNNNNNNINNNEKKSTYENEWGIELIETSEDFNNNNNNNNKPSNNSFEFSYDKKPTVELNEQSTVKVNSSSNLEDLMNQLKNMK | E1-like enzyme which activates ufm1. | Q54C02 |
B6YV16 | VATD_THEON | V-ATPase subunit D | Thermococcus | MAELLNVKPTRMELLNLKRRIKLAKKGHKLLKDKQDALIMEFFTIYDEALSLREELGRKMEEAFKALQMAEIDVGMLRLKEISLSVEPNKEVDIKKRNVMGVSVPLIEAESFRRSTSERGYAFVSSSPRVDLAAEKFEEVLDLAVRLAEVEETLKRLAREIEVTKRRVNALEYIIIPRMEATVKFIKQRLDEMERENFFRLKRVKALIEARS | Produces ATP from ADP in the presence of a proton gradient across the membrane. | B6YV16 |
O35305 | TNR11_MOUSE | Receptor activator of NF-KB | Mus | MAPRARRRRQLPAPLLALCVLLVPLQVTLQVTPPCTQERHYEHLGRCCSRCEPGKYLSSKCTPTSDSVCLPCGPDEYLDTWNEEDKCLLHKVCDAGKALVAVDPGNHTAPRRCACTAGYHWNSDCECCRRNTECAPGFGAQHPLQLNKDTVCTPCLLGFFSDVFSSTDKCKPWTNCTLLGKLEAHQGTTESDVVCSSSMTLRRPPKEAQAYLPSLIVLLLFISVVVVAAIIFGVYYRKGGKALTANLWNWVNDACSSLSGNKESSGDRCAGSHSATSSQQEVCEGILLMTREEKMVPEDGAGVCGPVCAAGGPWAEVRDSRTFTLVSEVETQGDLSRKIPTEDEYTDRPSQPSTGSLLLIQQGSKSIPPFQEPLEVGENDSLSQCFTGTESTVDSEGCDFTEPPSRTDSMPVSPEKHLTKEIEGDSCLPWVVSSNSTDGYTGSGNTPGEDHEPFPGSLKCGPLPQCAYSMGFPSEAAASMAEAGVRPQDRADERGASGSGSSPSDQPPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGPGSAEPESEPVGRPVQEETLAHRDSFAGTAPRFPDVCATGAGLQEQGAPRQKDGTSRPVQEQGGAQTSLHTQGSGQCAE | Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells. | O35305 |
Q8N8E2 | ZN513_HUMAN | Zinc finger protein 513 | Homo | MPRRKQSHPQPVKCEGVKVDTEDSLDEGPGALVLESDLLLGQDLEFEEEEEEEEGDGNSDQLMGFERDSEGDSLGARPGLPYGLSDDESGGGRALSAESEVEEPARGPGEARGERPGPACQLCGGPTGEGPCCGAGGPGGGPLLPPRLLYSCRLCTFVSHYSSHLKRHMQTHSGEKPFRCGRCPYASAQLVNLTRHTRTHTGEKPYRCPHCPFACSSLGNLRRHQRTHAGPPTPPCPTCGFRCCTPRPARPPSPTEQEGAVPRRPEDALLLPDLSLHVPPGGASFLPDCGQLRGEGEGLCGTGSEPLPELLFPWTCRGCGQELEEGEGSRLGAAMCGRCMRGEAGGGASGGPQGPSDKGFACSLCPFATHYPNHLARHMKTHSGEKPFRCARCPYASAHLDNLKRHQRVHTGEKPYKCPLCPYACGNLANLKRHGRIHSGDKPFRCSLCNYSCNQSMNLKRHMLRHTGEKPFRCATCAYTTGHWDNYKRHQKVHGHGGAGGPGLSASEGWAPPHSPPSVLSSRGPPALGTAGSRAVHTDSS | Transcriptional regulator that plays a role in retinal development and maintenance. | Q8N8E2 |
P32386 | YBT1_YEAST | ATP-dependent bile acid permease | Saccharomyces | MHHVLNSTRPDHRFWFYDDVTQYGRTKYLNYYTPLVLLIFTVLFITYNIWKHYYYYDVLHLKQKNPIDELLYSSTDEDEQSPLINNNTITTNYVDNNCTKDALKNRHFSLEKLKSVKVNGEPHGTPEIVRRGFIEKSRIILEFFLVLSQVIIHSFILLHYVNKNPEFTQQGTITGLVEWCALFIIVSLRLANVNQNFKFINKYPGNLWSVSFINYLALFISMILPFRSIFIHHINSPISRKYYISQISINLALFLLLFFARIRNNFAIIYKTDSWITPSPEPVTSIAGFICWAWLDSFVWKAHKVSIKVKDIWGLMMQDYSFFVVKKFRYFVDHKVKRKRIFSLNLFFFFSNYLVLQCFWAFLGSVLSFIPTVLLKRILEYVEDQSSAPSNLAWFYVTVMFVGRILVAICQAQALFFGRRVCIRMKSIIISEIYTKALRRKISTNKTKPSNEDPQEINDQKSINGDEESTSSANLGAIINLMAIDAFKVSEICGYLHSFLEAFVMTVVALALLYRLLGFAAIVGVLIIVAMLPLNYKLAKYIGDLQKKNLAVTDNRIQKLNEAFQAIRIIKYFSWEENFEKDINTIRENELSLLLMRSIVWSISSFLWFVTPTIVTAASFAYYIYVQGEVLTTPVAFTALSLFTLLRDPLDRLSDMLSFVVQSKVSLDRVQDFLNENDTKKYDQLTIDPNGNRFAFENSTISWDKDNQDFKLKDLNIEFKTGKLNVVIGPTGSGKTSLLMALLGEMYLLNGKVVVPALEPRQELIVDANGTTNSIAYCSQAAWLLNDTVKNNILFNSPFNEARYKAVVEACGLKRDFEILKAGDLTEIGEKGITLSGGQKQRVSLARALYSNARHVLLDDCLSAVDSHTASWIYDNCITGPLMEDRTCILVSHNIALTLRNAELVVLLEDGRVKDQGDPIDMLQKGLFGEDELVKSSILSRANSSANLAAKSSTSLSNLPAVKEQQVSVNNNSSHFEAKKLQKSLRTEAERTEDGKLIKEETKEEGVVGLDVYKWYLKIFGGWKIVSFLASLFLIAQLLYIGQSWWVRAWASHNVIAKIIPRAQRAIAFISKKASHLIDWRGSSQISMASAENQPSSGHSTMYYLVLYLIIGFAQALLGAGKTILNFVAGINASRKIFNMILNKVLHSKIRFFDATPTGRIMNRFSKDIEAIDQELTPYIQGAFYSLIECLSTVILITFITPQFLSVAIVVSILYYFVGYFYMAGSRELKRFESISRSPIYQHFSETLVGVTTIRAFGDEGRFMQENLHKIDENNKPFFYLWVANRWLAFRIDMIGSLVIFGAGLFILFNINNLDSGMAGISLTYAISFTEGALWLVRLYSEVEMNMNSVERVKEYMEIEQEPYNEHKEIPPPQWPQDGKIEVNDLSLRYAPNLPRVIKNVSFSVDAQSKIGIVGRTGAGKSTIITALFRFLEPETGHIKIDNIDISGVDLQRLRRSITIIPQDPTLFSGTIKTNLDPYDEFSDRQIFEALKRVNLISEEQLQQGATRETSNEASSTNSENVNKFLDLSSEISEGGSNLSQGQRQLMCLARSLLRSPKIILLDEATASIDYSSDAKIQETIRKEFQGSTILTIAHRLRSVIDYDKILVMDAGEVKEYDHPYSLLLNKQSAFYSMCEHSGELDILIELAKKAFVEKLNSKKD | Vacuolar class C ABC transporter which regulates the translocation of phosphatidylcholine to the vacuole lumen, the release of lumenal calcium stores, and acts as a negative regulator of vacuole fusion. Exhibits ATP-dependent bile acid transport. | P32386 |
A4Y5I1 | TIG_SHEPC | PPIase | Shewanella | MQVSVEATQGLERRLTISVPAEQIEKLVKDSLQREAKRARIPGFRPGKVPVTVINKRYGAAIRQDITGEVMQRNFIEAIIAEKLNPAGAPTFIPGSTDSEKFEFVATFEIYPEVELKGLDAIEVEQPKASVTDADVDSMIETLRKQHATYAAVEREAADGDKVKMNFVGSVDGEEFEGGKAEDFELQLGSGRMIPGFEAGILGHKAGEEFVIDVNFPEEYHAENLKGKAAKFAITLTEVQAANLPEVNDEFAALFGINEGGLEALKTEIRKNMNRELEQALKANVKEQVIAGLLANNDIELPKALIDGEVNVLRQQAMQRFGGQTANMPELPAELFTEQAARRVKIGLLLGEVIKTNELKAEDERVQGLIASMASAYEDPSEVIAYYNSNKELMQNMRNVALEEQAVEALLKSAKVTEKEVAFEEFMNKATGRA | 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. | A4Y5I1 |
Q9GL27 | TBXT_CANLF | Protein T | Canis | MSSPGAESAGKSLQYRVDHLLSAVESELQAGSEKGDPTERELRVGLEDSELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGAQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDHKDMMEEPGDSQQSGYSQWGWLIPGTSTLCPPATPHPQFGGPLSLPSTHGCERYPALRNHRPSPYPSPYAHRNNSPTYSDNPSACLSMLQSHDSWPSLGTPAHTSMLPMSHSAGPPTGSSQYPSLWSVSNGTITPGAQPAGMSNGLGAQFFRGSSAHGAPLGHAVPAPSASGSPLYEGAPTATDVPDSQYDASAQARLIASWTPVSPPSM | Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic site (called T site) and activates gene transcription when bound to such a site. | Q9GL27 |
B1KK11 | YCIB_SHEWM | Inner membrane-spanning protein YciB | Shewanella | MKQLLDFLPLVIFFAVYKMYDIYIASGALIAATALQLIVTYALYKKIEKMHLITFVMVTFFGTLTLIFHDDAFIKWKVTVVYALFAIALAVSQLLNKPILKSMLGKELVVADKIWAHVTWYWVSFFVACGLVNIYVAFSLSQETWVNFKVFGLTALTLINTVITVVYLFKNMPEEHKKELNK | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B1KK11 |
B8GT83 | YCIB_THISH | Inner membrane-spanning protein YciB | Thioalkalivibrio | MKLLYDLLPVILFFLAYKFYGALPPEWILAVGVWLPVALEPDNPGHAIYLATAVAMVVMAVQLALGLAIKRRLETMPLLTAAVILVLGGATLWLHDPVFILWKPTLVNWLFALVFMAPPLFGRRTLVETLMGHALSVPRAIWSRVNLAWVVFFLVSGLANLFVAYTFSEAVWVDFKLFGMLGMTFVFVIGQAVYLGLHHREDDPHTTKGDPS | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B8GT83 |
Q0HWI3 | TRPB_SHESR | Tryptophan synthase beta chain | Shewanella | MSQLKLNPYFGEYGGMYVPQILVPALKQLENAFVEAQADESFQAEFTDLLKNYAGRPTALTLTRNLSPNPMVKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLGLKCKVYMGAKDVARQSPNVFRMRLMGAEVIPVTSGSATLKDACNEAMRDWSGSYEKAHYLLGTAAGPHPFPTIVREFQRMIGEETKKQMLEREGRLPDAVIACVGGGSNAIGMFADFIDETSVELIGVEPAGKGIDTHMHGAPLKHGKTGIFFGMKAPLMQDSEGQIEESYSISAGLDFPSVGPQHAHLNAIGRARYESATDDEALEAFQLLARSEGIIPALESAHALAYALRLARECTKETILVVNLSGRGDKDIFTVSDILNGKEE | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Q0HWI3 |
Q97DU2 | Y3379_CLOAB | Sugar phosphatase | Clostridium | MEQLNICIDIDGTITDAYYWIDLCNSYFKTSITEKDATQYYIHKILNVPLEEYNEFYEKYKYKLHSEQKLRKDVKSVITKLSQNNNIFFVTARERDLTILTYSYLRKKEIPYDSLFILGTHHKVPTARQLNCDLFIEDNYDNALELSKAGFKVLLIDTYYNRKPLNQNIIRFYNWDEVYGIVDRLFEKSEAI | Catalyzes the dephosphorylation of nucleotide monophosphates and of different sugar phosphates in vitro. | Q97DU2 |
Q603G8 | TSAC_METCA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Methylococcus | MGWISGFRLRLAANALRNGRIVAYPTEAVYGLGCDPFNEDAVRKLLALKRRSQIKGLILIAADVEAVESLVDLARVPLGAEVRAGWPGPTTWLIPPRPGIPDWLRGAHDSLAVRVTAHPVAAALCRVFGGAIVSTSANLSGHRPARTPVRLWRQFPRRAIHFLPGRLGGAVRPTAIFDAMSGRRIR | 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. | Q603G8 |
Q2SXS5 | UVRC_BURTA | Excinuclease ABC subunit C | pseudomallei group | MTSPDASESRFEPKPILAQLPHLPGVYRYYDAQEAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMVTRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTGHRFPRMAYYRGAVDKKNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFSNRTRPCLLHQIGRCSAPCVGAIGEEDYARDVDNASRFLLGRQGEVMGELERKMHAFAAELKFEQAAAVRNQMSSLAKVLHQQAIDVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPTHVETALALAGGVDAHAGEGAGDDARDAAESPAQARLAGDAAANGVANAAAAARADDRSAQPTRARAEGDVERSADASAGARGEADAREAAAPSEPDSVTAASQDADADAAPLETEVLEAFIAQHYLGNRVPPILVVSHAIANRELIDLLVEQAGHKVALVRQPQGQKRAWLAMAEQNARLALARLLSEQGSQQARARSLADVLGYESDDLAQLRIECFDISHTMGEATQASCVVYHHHKMQSSEYRRYNIAGITPGDDYAAMRQVLTRRYEKMVEEAAAEASADEAAGIDGNAVHAAASAGRLPNIVLIDGGRGQVEIARQVFSELGLDISMLVGVAKGEGRKVGLETLIFADGRAPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKTRQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVDELASVEGISRALAEQIYRQLH | 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. | Q2SXS5 |
A8SEB4 | YCF4_CERDE | Photosystem I assembly protein Ycf4 | Ceratophyllum | MNWRSERIWIEVITGSRKTSNFFWACILFLGSLGFLLVGTSSYLGRNLISLFPSQQIPFFPQGIVMSFYGIAGLFISSYLWCTISWNVGSGYDRFDRKEGIVYIFRWGFPGKNRRIFLRFLMKDIQSIRMEVKEGVYPRPALYMEIRGQGTIPLTRTDENFTSREMEQKAAELAYFLNVPIEVF | Seems to be required for the assembly of the photosystem I complex. | A8SEB4 |
Q325G5 | TIG_SHIBS | PPIase | Shigella | MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDSAVEAEDRVTIDFTGSVDSEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKETTFNELMNQQA | 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. | Q325G5 |
Q7YJW2 | YCF4_CALFG | Photosystem I assembly protein Ycf4 | Calycanthus | MNWRSERIWIELITGSRKTSNFCWACILFLGSLGFLLVGTSSYLGRNLISLFPSQQIIFFPQGIVMSFYGIAGLFISSYLWCTISWNVGSGYDRFDRKEGIVCIFRWGFPGINRRIFLRFLMRDIQSIRMEVKGGLYSRRVLYMEIRGQGAIPLTRTDENFTPREIEQKAAELAYFLRVPIELK | Seems to be required for the assembly of the photosystem I complex. | Q7YJW2 |
Q9XHZ3 | UREF_ARATH | Urease accessory protein F | Arabidopsis | MEEDERRDIVMSRASSCMQWSQWQLLDSILPTGGFAHSFGLEAAIQTRLVSSPEDLETHIIHVLDNTASLLLPFVYSALKSPDIETWHKLDGILNATLTNQVSSKASMSQGSALFRIAASVFTEVPNLKMIRDASLGSKNVCFHHAPIFGLVCGLLGMDSETSQRAYLFVTLRDVLSAATRLNIVGPMGASVMQHRIAIVTETVLEKWMNREAGEACQTSPLLDVVQGCHGYLFSRLFCS | Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter. | Q9XHZ3 |
Q9PPV5 | Y535_UREPA | DegV domain-containing protein UU535 | Ureaplasma | MKKSFLIMTDSSTTLDREWAKNNDVMILPLSILRSDHTLIVDDGIESKPERIYEDIDNGYTFQTSCTPYGVLIEAIEQKLQEYEKIIFIGISSGFSSQFNNAKNLEKEYQDKLFVVDTEDFGYSLEHLVYKIKAMLSNNISFGDILKMINKHHDYTSSFLACENITGLVRSGRIPKIIGTMLKLSKVTPIIKAEWKNHRAGMALNIRSAPHKILENINHVFDNQLNNHTIEKVCILQAGLSSERIDELKNDVINHFHVDKEKIVIRSGPPIFLVYVWKGALGIQVIANIPKKHVEKKH | May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | Q9PPV5 |
Q11JM2 | YIDD_CHESB | Putative membrane protein insertion efficiency factor | unclassified Chelativorans | MALPAGYSRNWSGPWPKTPGRVLGTAFVRLYQLTLSGFIGNSCRHFPTCSEYAYEAIARHGLWAGGWMGLFRVMHCGPGGTHGIDPVPEILQPRHAWWAPWRLWKLKP | Could be involved in insertion of integral membrane proteins into the membrane. | Q11JM2 |
Q89T99 | Y2140_BRADU | Putative cysteine protease YopT-like blr2140 | Bradyrhizobium | MYDRIGGSSTRTSQTDEPSQSVDSGSFTETLADLAPQWSSRSGELPDKMGACCSKPDTLDANVQTSSASEPSTSSPESPATSLFEYRTADLRDANVDGICVGLTAEWFRNLSNSPSTRMSALTPGSQTHASAAERQQQYQRLKDQLRSRGAGSSQADLQAQNTILEEAGLEPAGEEKRFAFGKSSNVKSMVNEINEDGSNHLLSLYFAEGGAHTVATSASNGTTTLFDPNYGEFTVRSDPDQMASLLQSLANRYRNPNGQHLSTITTQRMQ | Potential cysteine protease, which may play a central role after invasion of host cell. | Q89T99 |
Q0K6N8 | ZAPD_CUPNH | Z ring-associated protein D | Cupriavidus | MILYEYPFNERIRTLLRLEDLFDRLEYFLGQDHAHQHHVALTTLFEIIDVAGRADLKTDLIKELERQRQALAPLRANPQIDQEALDAVIGEIEQGIAMLNQTVGKAGQLLADNEWLTSIRSRAIIPGGTCEFDLPAYYAWQHRPAEDRRADILKWVRPLLSLRMGTTIVLRLLREAGQSGKVIATGGSYQQMLSGRSYQLMQVYLDDSLLAFIPEMSANKYMLWVRFTQQDGDLRPRSVDADIPFLLKLCNF | 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. | Q0K6N8 |
A9ADC9 | UVRC_BURM1 | Excinuclease ABC subunit C | Burkholderia cepacia complex | MTSAEAPDTPFEPKKILAQLPHMPGVYRYYDAAGAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMVTRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTSHRFPRMAYYRGAVDKQNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCTAPCVGAISAEDYAVDVSNAARFLLGRQSEVMKELEQKMHAFAAELKFEQAAAVRNQMSSLATVLHQQAIEVGSDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPTHVESALTLAEGGLGDDTDADAVEAPDVPAEAPVGEPGSARDTTASIEAEVLDAFIAQHYLGNRVPPVLVVSHAPASRDLLELLSEQAGHKVSLVRQPQGQRRAWLSMAEQNAQIALARLLSEQGSQQARTRALAETLGLECDDLATLRIECFDISHTMGEATQASCVVYHHHKMQSGEYRRYNITGITPGDDYAAMRQVLTRRYEKMVEQAAQAAAADDAAGIDGESTRQAEASSLLPNIVLIDGGKGQVEIARQVFTELGLDTSMLVGVAKGEGRKVGLETLVFADGRAPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKARQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVEELASVDGISHALAEQIYKQLH | 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. | A9ADC9 |
A6TET6 | TSAC_KLEP7 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Klebsiella | MNNNLPSEAVAHAVAVLKNEHVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVEKGLILIAASFEQLKPYIDDSRLSDSQREAIFSCWPGPVTFVFPARPETPRWLTGRFDSLAVRVTNHPLVIELCEAYGKPLVSTSANLTGQPPCRTTAEVHAQFGDSFPVVDGATGGRQNPSEIRDALTGELFRQG | 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. | A6TET6 |
Q5E7A7 | XNI_ALIF1 | Flap endonuclease Xni | Aliivibrio | MAIHLVIIDALNLIRRVHSAQPNQDDIQAVITTTTRTINKILKETEPTHIIAVFDHHLQDRGWRAEILPQYKEDRKPMPEALQKGMDDIQEAWWKLGIDSLLSDGDEADDLVATLANKVAMHNEQVTIISTDKGYCQLLSPTLRIRDYFQHRWLDAPFVEKEFGLKPEQLADYWGLAGISSSKITGIPGVGPKAALEILTQFPTIEAANESEDLPKKYRKKFDEHYETAILCRQVAGLRTDIELGFNLQDIRYEKGTRD | 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. | Q5E7A7 |
G5E8Z2 | TAF4B_MOUSE | Transcription initiation factor TFIID 105 kDa subunit | Mus | MPAGLTEPAGAAAPVVSSASGAVTMAPVAALPVRVEGTPVALGPVTKAPVSVCVESVAPQPLPAPVGTLVTKVVPVTALPKLGSPRLPAPQIVTVKTPGTTTIQLPANLQLPPGTVLIKSNSGQLMLVSPQQAVTGAKTTSNITPRPAVPANTQTVKICTVPNSSSQLMKKVTVAPVKNLTQIGTTVATTASSTSSGQPVALPSSVITVTPAKLVNTVSTLKSSSLGVLSTPSNDARLKAETSVAAQTALPPTVLENVKKCKNFLSMLIKLACSGSQSPEMGQNVKRLVEQLLDAEIEAEEFTRKLYIELKSAPQPHLVPFLKKSVVALRQLLPNSQSFIENCVKEVSGDVVISSCTMTTATSPVVTSTVSPVLVSGATAPRTLSVQQTLNPLAGPGVANTGVVTLHSVAPAAATGGTTAATVLLQTSKPLTTSVPNTVAAVSLQPENPVVSGAAVTLAIPSATFGEASATPLCLPSAKPAITSAGTKADKPAIGTPVQIVTQPSTLLPQAAGIPQTAKVKQLVVQQPSGSSVNHVTSISHSSPLSTQNCGQKTPVNAVMPTSSIIKQITLPGNKLLSLQAQRSSIQSNKIKENGPTCFRGEDDINDVTFMAEVNLDEENACILAAHSDFVGTLIQSCKEEPFLVIGALQKRILDIGKKHDITELNSDAVNLISHATQERLRGLLEKLTTIAQHRMTIYKGSENYILSTDTRSQLKFLEKLDQLEKQRKDLEEREMLLKAAKSRSNKEDPEQLRLKQKAKELQQLELAQIQYRDANLTALAAIGPRKKRPLESGNESFKDNPSTSGTSSLTATKPFRPRITRICLRDLIFCMEQEREMKYSRALYLALLK | Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators asond repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis. | G5E8Z2 |
B1XN07 | TRHO_SYNP2 | tRNA hydroxylation protein O | unclassified Synechococcus | MKDFVVITFYKFFDFPDYKERQQPIFNFADEQKIIGTILLAHEGINATIAGTQTALDAMVNFLHQDPRLADLTYKVSTAPKQPFKRLKVKLKQEIVTLGQPNVDPNNTVGTYIDPKDWNDLIQNPDVTLVDTRNDYEVGIGTFKGAINPNTKSFREFPDYVAENLDPQKNAKVAMFCTGGIRCEKATSYLLNQGFQEVYHLKGGILKYLEEIPVAESLWEGECFVFDERVTVKHGLETGHYELCYACGHPIDAEDKTSAAYEIGVSCPYCIEALTPERRSRFEAKWQQRQQMKACQAS | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | B1XN07 |
B1GZV6 | TSAD_ENDTX | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Endomicrobium | MNIFAIETSCDETSASVVLNGLKVKSVVIYSQIKIHAGFFGVVPELASRSHIENINLVIWRALSDAGINFTDFSQKIDALAFTSGPGLAGALLVGAIAAKSLACVYKKPLIPVNHLDGHLYSSLIENRSVKLPFLSLIISGGHTELVVVEDFGKYKVLGSTRDDAAGEAFDKAAKMLGLSYPGGPIIDKIAESGNPEAVRFTRPYLKGSWDFSFSGIKTALLNYLKTNPVRNEKQLNDICASFRQAVAETLCFKSFEAAKKFNLKRIVLGGGVSANSLIRKIFLETGQKNNTKVFIPSLIYSTDNAAMIGCAAYFKQKKCGLKYDNIQLKPNPSLPLENWRL | 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. | B1GZV6 |
B1KIF6 | TOLB_SHEWM | Tol-Pal system protein TolB | Shewanella | MKTLGKWLLLGLVVMSMPARAALDIVITEGVDAARPIAVIPFVWQGQGPAPQQISDVVMSDLARSGTFNPIDELGLPQRNIAKVSQFVAKEWSNVAAEAVVMGSVKPMGPDQFLVNFELVDLVKAQMQAGNGPQSSSEYLIDSSEVVISAEQFRQYGHRISDIVYEKLTGIRGAFLTRIAYVVVKHGEKSPYHLMISDYDGHNEKMLLRSPEPLMSPSWSPDGSKLAYVSFENKKAEVFVQNIYTQARAKITSYDGINGAPVFSPDGKKLALTLSRDGQPEIYVVDIDTKALKRVTNHYAIDTEASWFPDGKSLIFTSERGGRPQIYKVTLASGKVQRMTFEGEWNLGGSISPDGRSMIFVNRTNGKFNIARMDLETRFVQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPAGQGEVKSPSWSPFL | 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. | B1KIF6 |
Q5LLL4 | YBEY_RUEPO | Endoribonuclease YbeY | Ruegeria | MTLDLTLEDPRWTILPPLADRAISATLAQMGLDPELCEISLLGCDDARITALNAEFREKPSPTNVLSWPAEDLAAETPGGTPLAPEPDFTGAVPLGDIAIAFDTCQREADAAGKPIADHVTHLIVHGLLHLLGYDHIRDEDATLMEGLETRILGNLGIDDPYTME | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q5LLL4 |
P64232 | TRMFO_BRUME | Folate-dependent tRNA(M-5-U54)-methyltransferase | Brucella | MSNNTDLSPVHVIGGGLAGSEAAWQIAQAGVPVVLHEMRPVRGTDAHKTEQLAELVCSNSFRSDDAETNAVGVLHAEMRLAGSLIMACADAHQVPAGGALAVDREGFSQAVTARLEAHPLITIEREEITGLPPTEWGTTIIATGPLTAPSLAEAIAAETDADALAFFDAIAPIIHFDSINMDVCWFQSRYDKVGPGGTGKDYINCPMDKEQYEAFVAALIEGDKTDFKEWEGTPYFDGCLPIEVMAERGPETLRHGPMKPMGLTNAHNPTVKPYAVVQLRQDNALGTLYNMVGFQTKLKYGSQTGIFKMIPGLENAEFARLGGLHRNTYLNSPVLLDNVLRLKSRQTLRFAGQVTGCEGYVESSAIGLLAGRFTAAEKLSQAAVPPPPTTAFGALLGHITGGHIVTDDEPGKRSFQPMNVNFGLFPPVDVPKPEGKRLRGKEKTIAKKRALSARALADCRNWLSLY | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | P64232 |
P0CH13 | U7B_CONDE | Conotoxin de7b | Kohniconus | DCIPGGENCDVFRPYRCCSGYCILLLCA | May inhibit sodium (Nav) or calcium channels (Cav). | P0CH13 |
A6UET3 | TYPH_SINMW | TdRPase | Sinorhizobium | MAMLPQEVIRKKRDGGRLVPAEIAGFIEGLADGSISEGQAAAFAMAVWFSGMSRDECVALTLAMRDSGETLDWGEFGRPVVDKHSTGGVGDNVSLMLAPIVAACGPVVPMISGRGLGHTGGTLDKLESIPGYNIQPSPELFRRVVDEVGCAIIGQTANLAPADKRLYAIRDVTATVDSVPLITASILSKKLAAGLQSLVLDVKLGNGSFMTDPAETEILARSLVEVANGAGVRTSALITDMNEPLADAAGNALEVENCLAYLSGKKAGTRLDRVVMAFAAEMLAAAGVSAHKAEGEAMARRALESGEALERFGLMVHRLGGPADFVERPEAYLERAPAIVPVAAARDGYLAACETRELGMAVIALGGGRRRPDDRIDHRVGLAGLRPLRTKVEKGEPIAFVHGADRDQAEAVAKRVATLYAIAEEAPAQRPVIASRLV | 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. | A6UET3 |
Q60FS1 | TCTP_PLUXY | Translationally-controlled tumor protein homolog | Plutella | MRIYKDIITGDEMFSDTYKMKLVDEVIYEVTGKLVTRTHGDVQIEGFNPSAEEADEGTDAATESGVDIVLNHRLMETYAFGDKKSYTLYLKDYMKKLVAKLEETAPDQVDVFKTNMNKVMKDILGRFKELQFFTGESMDCDGMVAMCEYRDINGVSTPVMMFFKHGLLEEKF | Involved in calcium binding and microtubule stabilization. | Q60FS1 |
Q04FE3 | TMCAL_OENOB | tRNA(Met) cytidine acetate ligase | Oenococcus | MEATGLITEYNPFHNGHLYHLKKAQELTKADVTIVLMSGNWVQRGLPAITDKWKRAQAAIDAGADLVFELPFYYAVQAGEIFAQGAVRLLSDLQVSSIICGSEHADIDFINLAAHEPDISGNSNFDKKNRTFASNYAAALEEKTGFYLENANDILAFSYAKAILNQNLTEKIKLRTISRVSADYHDQFLNDGEIASATAIRKALSEGQNVDSYTPMSDLQYTDYEARLFQLLKYRLSTDGLGQIRSIYQVNEGMEYLIKQAIEKNPSDFGELLALIKSKRYTFARLHRVLVYILLNIKVDQMNLAMQNPYHRLLGFTEKGRQYLHEKKGRFNFPTISHVDQKTANKSLAIDYKAGLVYNQIMDYKSTQDIKRTPIQS | 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. | Q04FE3 |
A6UFC2 | UPPP_SINMW | Undecaprenyl pyrophosphate phosphatase | Sinorhizobium | MADQSIISALVLGLIEGLTEFIPVSSTAHVLLAGHFLGFRSPGNTFAVLIQLGAILAILLVYFQKLLSIALALPTSVRARRFVLSVLLAFLPAALIGAAAHGFIKSVLFETPMLICVVLIVGGIILYVIDRLPLTPRYTDVFDYPPSLALKIGLFQCLAMIPGTSRSGATIAGALLMGTDKRSAAEFSFFLAMPTMVGAFALDLYKNREALSIDDIGLIAAGFIAAFIAGIFVVRSLLDFVSHRGFTPFAIWRILVGTAGLVGLWLLG | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A6UFC2 |
Q30PM2 | XEEP_SULDN | L-Xxx-D/L-Glu epimerase | Sulfurimonas | MKIVNITTQVESIELKTPFKTALRQTSHVEFVRVEVECDNGFVGIGEASATKVITGEDIYIILTSIASVEELFLNLTCEEALGALHTKCAIGSSAKASLDIAFVHLLSQEAKKPLYEYFGATDKSALKSDITISLNEADVMLNDAKKAFSNGMDILKIKVGSDILHAIDIVRKIAKELPECDILVDANQAWSFENTVLFIENMLNTPIKLIEQPVEAPNLDGLKKITELSHIPILADEAVFTLKDAKKVIEEKCADMINIKLMKCGGVSKAIEILEFARNREFKCMLGSMLEGPYSINMALHLAFAYRDVIEFVDLDSPLLYKEMPKELDFVFDGCEIKPL | Catalyzes the epimerization of dipeptides with L-Glu in the second position. Has epimerase activity with L-Gly-L-Glu, L-Ala-L-Glu, L-Ser-L-Glu, L-Pro-L-Glu, L-Val-L-Glu, L-Met-L-Glu, L-Thr-L-Glu and L-Phe-L-Glu (in vitro). | Q30PM2 |
B0REK3 | YQGF_CLAMS | Putative pre-16S rRNA nuclease | Clavibacter | MRVGSRLAVDVGKARIGLARSDPHGLIATPVETVPRDAAGSADVRRILEVAAEIDCTELVVGLPLALSGRATASTDDAEGFARRLADATEIRVRLVDERLSTVSAQGALRASGRGSRKQKPVIDQVAAVIILQHALETERAAGSPPGALVPRNRVDPDRHA | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B0REK3 |
B5ZV71 | TRPA_RHILW | Tryptophan synthase alpha chain | Rhizobium | MTARMDKRFAELKAEGRPALVTYFMGGDPDYDTSLGIMKALPEAGSDIIELGMPFSDPMADGPAIQLAGQRALKGGQTLKKTLQLAADFRKTDDATPIVMMGYYNPIYIYGVEKFLDDAIAAGIDGLIVVDLPPEMDDELCIPAIRKGINFIRLATPTTDEKRLPKVLKNTSGFVYYVSMNGITGSALPDPSLVSGAVERIKQHTQLPVCVGFGVKTAEHAKVIGGSADGVVVGTAIVNQVATSLTSDGKATADTVQAVATLVRGLSTGTRSARLVAAE | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B5ZV71 |
B1KC83 | TYPH_BURCC | TdRPase | Burkholderia cepacia complex | MFLPQEFIRRKRDGQPLDRDGMAAFVRGVTDGSVTEGQVAAFAMAVYFNDLSTDERVALTLAQRDSGDVLDWRALGLGGPVIDKHSTGGVGDVVSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLSAIPGYDVMPDTDAFRRTVREVGVAIIGQTARLAPADKRIYAIRDVTATVESVAMITASILSKKLAAGLDGLVMDVKVGSGAFMPTAEKSAELARSIVDVGNGAGMKTTAILTDMNQSLAPCAGNALEVACAIDYLTGKSRPARLHDVTMALSAELLVTGGLARDAAHAREKLQQALDSGAAAERFARMVVALGGPADLLDAPARHLARAAVIVPVPAPASGVVQRVDCRALGLAVVALGGGRTRAEDAIDVSVGLSALAEIGQRIESGEPLGFVHARDEAAAAHAADAIRRGYVLGDTGEAPPTLYRQIG | 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. | B1KC83 |