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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|---|---|---|---|---|---|---|
Q5UXH1 | TRUB_HALMA | tRNA-uridine isomerase | Haloarcula | MATRGRHRSRTSGTSSEPMTLRAPPDERDLDSLRSFGVVNLDKPPGPSAHQVAAWIRDATGQDRVAHGGTLDPKVTGCLPVLLGDAARMAQVFDNAVKEYVTVLELHDQAPADIADIVAEFETDIYQKPPRKSAVKRQLRSRRIHSLDILEQGDRRLLLRVRCASGTYIRKLCHDIGLAAGTGAHMGDLRRTATGTFDDGSLSTMHDLVDALAFAADGDEAQLREIIQPAERALSHLPRVTIAPSAAREVAEGAPVYAPGVIETGPAEVGDATPEIDSQVVSVTPDGAAVCLGTLVSDPDADSGLVVELDRMLV | Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q5UXH1 |
Q8JIS6 | TBX6_DANRE | T-box transcription factor TBX24 | Danio | MLGVEMYPGLALGPQRLSDCYYRDRDVPLYPSTCEMAARALPPALLKPHANTDSPATPQDSVRMELENAGLWKQFSTVGTEMIVTKKGRRMFPQLRVKLSGLNPSLRYILLLDIVPVDSSRYRFQDNSWQVVGGAEARLPDRVFIHPDSPATGEHWQNRTISFHRAKLTNNTLDAQGYIILHSLHRYQPRVHVIEARDVLMWGRTQHSFTFPETQFITVTAYQNNKITELKINSNPFAKGFRENGMNCKKQREARLKRKITSSQEECLDIESCDPCDSTELLPQSVDLPSSALTIMNTALPITDSGFHTEVSSHPDQTDSDQTLVLEQAFLTSEMPSSMESQQQTTSETNVNNALMDETGQMMDLSGYTSSFPTPQLSSHTSVPQSSSMYSVVSSTQSSDLELPQASSISSPHSMPAYSSIPSAEYPGVNSSTAMPASTTSLSDSYPSISHSTSSHLLQSSSYHSLLPTDQSQDNLSPHTPTNPPFQSIPACQGTRLTIDSGQNQVDDGGLSSANATTPAVPNPTQTAFPFPPVQPNNDPDPTSPSCQSLPQSALPYQQVSQCNQIPTPSDPNTTPTAFPFPPSEQSTPNSIMVSSNPNTTAFPFPPVQQQLNLSTSGPSSFPVSQSSGLNAIPNPVHPTTGSFSFPSTSAIHQGPMQSVPNTLHPSTAYTFPSSLPKHTGPLPNPAPTSYPFPTPIPPGPHPLQSLTLPSSCSIPNTSQIQSTFPQSYHNPSFSHIPPQMANHSQITSQSFPPLQTSSAPQLLSQSSTHPQCPPPSNAYPAVAPTEIGTFPQLNSAAPYLPDVVLHPSILPSLDPSLSSSAPPSLYNPFPSYSLRLCQDPRSSLHLPLRHIYRQPQHAHGQGSYFDLGGRTVF | T-box transcription factor involved in the development of paraxial mesoderm. | Q8JIS6 |
Q6LVS3 | UBIA_PHOPR | 4-HB polyprenyltransferase | Photobacterium | MLAMTKAKAFCQLARFDRPIGSLLLLWPTLWALFLAADGLPNMHVLVVFVLGVVFMRAAGCVINDFADRNFDGHVKRTAKRPMPSGKISEREALGLFGLLVLVSFVLVLTMNTLTIMLSVVGLVLAAAYPFMKRYTHLPQLVLGMAFGWSIPMAYAAQAGELPVVAWLLFTANILWTIAYDTQYAMVDRDDDLKVGIKSAAILFGRFDKIIIGVLQLSTLVTMILIGHSLDLHQIYYWFLLMASGLFVYQQRLIGSREREPCFKAFLNNNYVGMLIFLGIAISVMMQ | 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. | Q6LVS3 |
A7NH01 | TMUUS_ROSCS | Type I terpene cyclase | Roseiflexus | MDQDYRARLVYPFSGAISPHADIVDQATLAWAAMFGLLTDSLRHKSRRLQYGLLAARAYPRADREMLQIAADWIAWLFFMDDQCDETGIGRDLQRMIALHERFLAILDGATPEAHDCALTYALADLRRRLALRAPDNWLRRFSEHVRLYFTANRWETVNRQRGATPNVATYCAARLFSGAVYACFDLIELAEQIELPFYARHHSIVQQLEQAANNIICWCNDVLSYPKEMQHGDRHNLVLVIQGEHQCSLPEAIDRALDLHAREVATFVRKRTCVPYFDAAVNTALEKYVTGLQFWICANRDWSLTATRYAPTHKSQEMVMAVAQQ | Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (+)-T-muurolol via a 1,10-cyclization, which requires isomerization of FPP to nerolidyl diphosphate (NPP) and then abstraction of the pyrophosphate from intermediate NPP leading to a (E,Z)-germacradienyl (helminthogermacradienyl) cation. | A7NH01 |
Q9TSL6 | UDB23_MACFA | UDP-glucuronosyltransferase 2B23 | Macaca | MSVKWTSVILLIQLSFYFSSGSCGKVLVWAAEYSHWMNMKTILEELVQRGHEVTALASSASILFDPNNSSALKIEVFPTSLPKPEFENIVTQEIKRWIELPKDTFWLYFSQMQEIMWKFGDIFRNFCKDVVSNKKLMKKLQESRFDVVFADPIFPCSELLAELFNIPLVYSLRFTPGYVFEKHCGGFLFPPSYVPVVMSELSDQMTFMERVKNMIYMLYFDFCFQIYDMKKWDQFYTEVLGRHTTLSEIMGKADIWLIRNSWNFQFPHPLLPNVDFIGGLLCKPAKPLPKEMEEFVQSSGENGVVVFTLGSMITNMKEERANVIASALAQIPQKVLWRFDGNKPDTLGVNTRLYKWIPQNDLLGHPKTKAFITHGGANGIYEAIYHGVPMVGIPLFADQPDNIAHMKTRGAAVQLDFDTMSSTDLVNALKTVINDPLYKENVMKLSRIQRDQPVKPLDRAVFWIEFVMRHKGAKHLRPAAHDLTWFQYHSFDVIGFLLACVATVIFIIMKCCLFCFWKFARKGKKGKSD | UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity on 6 steroids and the bile acid, hyodeoxycholic acid. May potentially play an important role in estrogen and androgen catabolism in peripheral steroid target tissues. | Q9TSL6 |
B1VNP0 | UREG3_STRGG | Urease accessory protein UreG 3 | Streptomyces | MPDNASAQQPGQPAQGPNEHYHQPLNQPRALRIGVAGPVGTGKSSILATLCRELAGELSMAVVTNDIYTDEDARFLRSAGVLPTERIRAVETGACPHTAIRDDVSANLDAVEDLEEAYGPLDLVLIESGGDNLTATFSPALADAQLFSIDVAGGGDVARKGGPGITGADLLVINKTDLAPHVEVDVTAMVADAERARDGLPVLALSKHDPESIARLADWVRAVLVRHRSGTHVPTDPGPMAPHSHSHDGS | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | B1VNP0 |
A8HVC4 | UBIG_AZOC5 | 3-demethylubiquinone 3-O-methyltransferase | Azorhizobium | MRMTANATIDPSEVARFDALGAQWWDPKGKMAPLHAINPVRLGFVRDVLVRHFGHDARSLRPLKGLRILDIGCGGGLLSEPLARMGADMVGVDPAPGNIVVAQSHADEAGVRVDYRQGTAEELADAGERFDVVLALEVVEHVADVGLFLRRAGEMVNPNGIMIVSTLNRTVKSFALAIVGAEYVLRWLPRGTHRWDKFITPAELEAEMGAAGFEMSELAGMVFDPLRGEWKIAADTDVNYFLVGKPAFHTSEG | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | A8HVC4 |
Q90WA0 | VKT2_PSETT | Kunitz-type serine protease inhibitor textilinin-2 | Pseudonaja | MSSGGLLLLLGLLTLWEVLTPVSSKDRPELCELPPDTGPCRVRFPSFYYNPDEQKCLEFIYGGCEGNANNFITKEECESTCAA | Serine protease inhibitor that inhibits plasmin (Ki=2.2 nM), and reduces blood loss in the mouse tail vein blood loss model. | Q90WA0 |
Q9I745 | TSSE1_PSEAE | Type VI secretion system component TssE1 | Pseudomonas | MAELTLQERLQPSLLDRLTDDEPGNLKEAAERRVLTLNQLKASVLRDLAWLFNTTSLFDHGPAARMPAGNSVLNYGLPALAGHTASSVDVHAIEALLTETIATFEPRIIRSSLRVRAQLLPGEMDHNALSFEIEGDLWAEPAPLRLLLTTNLDLETGHVRVAQGERRRT | 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. Plays a role in correct elongation and stability of TssB1-sheath . Functions downstream of TssK1 and prevents detachment of TssB1-sheath and its premature disassembly. Once bound onto the sheath via an interaction with TssB1, provides an ideal docking point for ClpV1 to be recruited to the sheath . | Q9I745 |
Q9FG77 | WRKY2_ARATH | WRKY DNA-binding protein 2 | Arabidopsis | MAGFDENVAVMGEWVPRSPSPGTLFSSAIGEEKSSKRVLERELSLNHGQVIGLEEDTSSNHNKDSSQSNVFRGGLSERIAARAGFNAPRLNTENIRTNTDFSIDSNLRSPCLTISSPGLSPATLLESPVFLSNPLAQPSPTTGKFPFLPGVNGNALSSEKAKDEFFDDIGASFSFHPVSRSSSSFFQGTTEMMSVDYGNYNNRSSSHQSAEEVKPGSENIESSNLYGIETDNQNGQNKTSDVTTNTSLETVDHQEEEEEQRRGDSMAGGAPAEDGYNWRKYGQKLVKGSEYPRSYYKCTNPNCQVKKKVERSREGHITEIIYKGAHNHLKPPPNRRSGMQVDGTEQVEQQQQQRDSAATWVSCNNTQQQGGSNENNVEEGSTRFEYGNQSGSIQAQTGGQYESGDPVVVVDASSTFSNDEDEDDRGTHGSVSLGYDGGGGGGGGEGDESESKRRKLEAFAAEMSGSTRAIREPRVVVQTTSDVDILDDGYRWRKYGQKVVKGNPNPRSYYKCTAPGCTVRKHVERASHDLKSVITTYEGKHNHDVPAARNSSHGGGGDSGNGNSGGSAAVSHHYHNGHHSEPPRGRFDRQVTTNNQSPFSRPFSFQPHLGPPSGFSFGLGQTGLVNLSMPGLAYGQGKMPGLPHPYMTQPVGMSEAMMQRGMEPKVEPVSDSGQSVYNQIMSRLPQI | Transcription factor. Regulates WOX8 and WOX9 expression and basal cell division patterns during early embryogenesis. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Required to repolarize the zygote from a transient symmetric state. | Q9FG77 |
A0KNW8 | YCIB_AERHH | Inner membrane-spanning protein YciB | Aeromonas | MKQFIEFIPLIVFFAVYKFYDIYMATGALVVVTGLQLAYSWIRYRKVEKMQLFTFLLVGFFGGLTVFFHDDTFIKWKVTVINVLFALGLLISRYGFGKNLIKQMLGKELQAPDPVWDRVNLGWAGFFTVCGLLNLYVAFNLPQEMWVNFKVFGLLGMTLVFTLLSGVYLYRHLPAEQKNEMKK | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A0KNW8 |
Q6GBX9 | TILS_STAAS | tRNA(Ile)-lysidine synthetase | Staphylococcus | MQLNSNGWHVDDHIVVAVSTGIDSMCLLYQLLNDYKDSYRKLTCLHVNHGVRSASIEEARFLEVYCERHHIDLHIKKLDLSHSLDRNNSIQNEARIKRYEWFDEMMNVLEADVLLTAHHLDDQLETIMYRIFNGKSTRNKLGFDELSKRKGYQIYRPLLAVSKKEIKQFQERYHIPYFEDESNKDNKYVRNDIRNRIIPAIDENNQLKASHLLKLKQWHDEQYDILQYSAKQFIQEFVKFDEQSKYLEVSRQAFNNLPNSLKMVVLDCLLSKYYELFNISAKTYEEWFKQFSSKKAQFSINLTDKWIIQIAYGKLIIMAKNNGDTYFRVQTIEKPGNYIFNKYRLEIHSNLPKCLFPLTVRTRQSGDTFKLNGRDGYKKVNRLFIDCKVQQWVRDQMPIVLDKQQRIIAVGDLYQQQTIKQWIIISKNGDE | 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. | Q6GBX9 |
Q17CQ8 | ZGPAT_AEDAE | Zinc finger CCCH-type with G patch domain-containing protein | Stegomyia | MSGSQDLNDSIRIYNEQLAQVEQALEGTSSGPERESLINLKSDLEELVKLTLETVQHENGDDLNAAASGSNEDDEFALFMREINALDDPGSVDAKPPKPDEVSVDEQEPFKDLVGSKCSAPHIHKWGSKSYHNALICSLDASDLDDVAAKVLFINPTHQEMVPCAYFLEGDCKFNDEMCRFSHGELISINELKEYREPRFELLRKKGCKVLAKNRNRIWSKGTIQTADFETKTCKIQMDEGRHEVELQFENVLPLEGDDVPSSDSESNSDSDEENEDDVVSLQQAQIIERSLLNPAPDQRLGDWEKHTKGIGSKIMLKMGYVVGAGLGSKGEGIVVPVSAQVLPQGRSLDYCMQLREQANGDKNLFSVEKKLQREKRIQEKRDAKNYAANKSKKDVFNFLNSEIFGSSNGSSSSSGSKKPAAKDNQMDLPSCSSKNLNIASLKLSEQMRRLELDIDRLSHSLTRHQPGSKMHSNLQKQIAEKRREISEIKKTEYSISREQQLRNDKRKMTVF | Transcription repressor. | Q17CQ8 |
P48733 | UROM_BOVIN | Uromodulin, secreted form | Bos | MKCLFSPNFMWMAAVVTSWVIIPAATDTSSAKSCSECHSNATCTVDGAATTCACQEGFTGDGLECVDLDECAVLGAHNCSATKSCVNTLGSYTCVCPEGFLLSSELGCEDVDECAEPGLSRCHALATCINGEGNYSCVCPAGYLGDGRHCECSPGSCGPGLDCVREGDALVCVDPCQVHRILDEYWRSTEYGSGYICDVSLGGWYRFVGQAGVRLPETCVPVLHCNTAAPMWLNGTHPSSDEGIVNRVACAHWSGDCCLWDAPIQVKACAGGYYVYNLTAPPECHLAYCTDPSSVEGTCEECRVDEDCKSDNGEWHCQCKQDFNVTDLSLLERRLECGVDDIKLSLSKCQLKSLGFEKVFMYLHDSQCSGFTERGDRDWMSVVTPARDGPCGTVMTRNETHATYSNTLYLADEIIIRDLNIRINFACSYPLDMKVSLKTSLQPMVSALNISMGGTGTFTVRMALFQSPAYTQPYQGSSVTLSTEAFLYVGTMLDGGDLSRFVLLMTNCYATPSSNATDPLKYFIIQDRCPRAADSTIQVEENGESPQGRFSVQMFRFAGNYDLVYLHCEVYLCDTVNEKCRPTCPETRFRSGSIIDQTRVLNLGPITRKGGQAAMSRAAPSSLGLLQVWLPLLLSATLTLMSP | In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals. | P48733 |
Q9LTH9 | ZIP2_ARATH | ZRT/IRT-like protein 2 | Arabidopsis | MALSSKTLKSTLFFLSIIFLCFSLILAHGGIDDGDEEEETNQPPPATGTTTVVNLRSKSLVLVKIYCIIILFFSTFLAGVSPYFYRWNESFLLLGTQFSGGIFLATALIHFLSDANETFRGLKHKEYPYAFMLAAAGYCLTMLADVAVAFVAAGSNNNHVGASVGESREDDDVAVKEEGRREIKSGVDVSQALIRTSGFGDTALLIFALCFHSIFEGIAIGLSDTKSDAWRNLWTISLHKVFAAVAMGIALLKLIPKRPFFLTVVYSFAFGISSPIGVGIGIGINATSQGAGGDWTYAISMGLACGVFVYVAVNHLISKGYKPREECYFDKPIYKFIAVFLGVALLSVVMIWD | Mediates zinc uptake. May also transport copper and cadmium ions. | Q9LTH9 |
Q6FTI0 | TVP38_CANGA | Golgi apparatus membrane protein TVP38 | Nakaseomyces/Candida clade | MPTDNADLGQEDIDVFDNGRESFDRLNKPVLDGIGIEGNDDDDDDYLTLYNMTPRERLMYTFRRSMYKALDHFNSLPKWQRLLIILFGALVIVLGILMLIFHNKILDKVLETSKDLNERSSTNFILLVLLFFVGFPPMIGYSFLSTSTGLIYGVSFHGWFVLALGSVTGSVASFYVFKNLLHSRAEKLVHMNKRFEAFASILQEDNSYLMLALLRLCPFPYSLTNGAIAGIYGISVKNFTIANIITTPKLLIYLFIGARIKNMAEDHSTSSRIFDLVSILITLIIFTLTAWLLYFKTKQRYAQLKNQAVAQNSSANREVDFEI | Golgi membrane protein involved in vesicular trafficking and spindle migration. | Q6FTI0 |
B2VKT1 | TRPA_ERWT9 | Tryptophan synthase alpha chain | Erwinia | MERYDLCFKRLAEKQEGAFVPFVTLGDPTPELSLQIIDALVAGGADALELGIPFSDPLADGPTIQNANLRAFAAGVTPEHCFDMLAAIRQKYPDMPIGLLMYANLVFSNGIDSFYARCQQVGVDSVLVADVPVEESAPFRQAAMRHNVAPIFICPPNAGDDLLREISSHGRGYTYLLSRAGVTGSETRASLPLKHLVDKLREYHAAPALQGFGISEASQVQQAISAGAAGAISGSAVVRIIEKHLNDPALMLSELTAFAASLKAATRS | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B2VKT1 |
U3U992 | UGT8_CATRO | UDP-glycosyltransferase 709C2 | Catharanthus | MGSQETNLAPHVLIFPLPIQGHVNSMLRLAELLCLAELDITFIVSEFSHSRLIKHTNVASRFARYPGFQFQPISDGLPDDHPRAGERVMDILPSTKNVTGPLFKQMMVENKCFSSATRRPITCIIADGVLSFAGDFAQEKGIPLIYFRTVSACSFWACFCMPELIESGDIPIKGNGMDLIVKSVPGMETFLRRRDLPGFCRVNDINEPKLQILKTETRQTTRAQAAILNTFEDLEGPILSQIRKHMPRLFTIGPSHSHLTSRLETKNIKTLISSGSFWEEDRSCVDWLDAQPPRSVLYVSFGSITVVTRDQLLEFWYGLVNSGQRFLWVMRPDSIMGKDGQSQIPADLEEGTKARGYMVGWAPQEEVLNHPAIGGFLTHSGWNSTLESIVAGVPMICWPYFADQMINSRFVSEIWKIGLDMKDTCDRETIVKMVRELMEIRKDEFLQRADHMAKLAKEAVSEGGSSYSNLDGLVDYIKSLII | Iridoid glucosyltransferase acting exclusively on 7-deoxyloganetic acid. No activity with 7-deoxyloganetin. Catalyzes the fourth to last step in secologanin biosynthesis. | U3U992 |
B3DFP2 | UQCC3_DANRE | null | Danio | MSGMRILTGSVALGGLTYAIWIIFSPGEERKKEILKSLPEANPVRMEETRKRNAIMLQVLKDAAETNDNIARGFGSQK | Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology. | B3DFP2 |
Q145H3 | UBIA_PARXL | 4-HB polyprenyltransferase | Paraburkholderia | MFARLPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGRPSLPLLVIFTVGTVLMRSAGCAINDYADRDFDRYVRRTENRPITSGKIRAWEAVALAAALSLLAFLLILPLNALTKELSVAALFVAGSYPFTKRFFAIPQAYLGIAFGFGIPMAFAAIQNHVPMLAWVMLLANVFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAIMLCYAVTLGIYVGIGVLLGFGALYWLGWAAAAGCAIYHYTLIRNRERMACFAAFRHNNWLGGALFAGIAAHYAATWF | 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. | Q145H3 |
O32127 | YUTD_BACSU | Putative antitoxin YutD | Bacillus | MILIQNAEFELVHNFKDGFNEEAFKARYSDILNKYDYIVGDWGYGQLRLKGFFDDQNQKATFETKISTLDEYIYEYCNFGCAYFVLKRIRK | Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Probably neutralizes cognate toxin YutE. | O32127 |
B1KZM6 | YBEY_CLOBM | Endoribonuclease YbeY | Clostridium | MIYIDNRQNKIKVDEEFENKIKEIIDYALKEEKVNIDYEISVIFIDNNSIKEINKDYRNIDKATDVLSFPMLDYEEGEVFKDVYLNYEFDESDLDEGNLVLGDIALSLEKAEEQSKEFGHSFLRETCYLTIHSVLHLLGYDHMEEDEKAIMRQREEEILKSFNLHR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B1KZM6 |
B5YCC8 | Y1981_DICT6 | Nucleoid-associated protein DICTH_1981 | Dictyoglomus | MKNPFEAMKQLKKLQEKMAKIEEELEQTLVEGTAGGGVVKIIMNAKEEIKEVKIDPEVVNKDEVDILEDLIAAALRDALTKAKEKSAEKMGSLADGLPLPPGLF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | B5YCC8 |
Q5UBX3 | TBB_TRIRU | Beta-tubulin | Trichophyton | MREIVHLQTGQCGNQIGAAFWQTIAGEHGLDGSGHYTGSSDLQLERMNVYFNEASSKKYVPRAVLVDLEPAALDAVRAGPFGQLFRPDNVVFGQSGAGNNWAKGHYTEGANLVDQVIDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPAGMMATFSVVPSPMVSDTVVEPYNATLSIHQLVEHSDETFCIDNEALYNICMRTLKLTNPSYGDLNHLVSAVMSGVSTSLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRNAYSFRAVSVPELTQQMFDPKNMMAATDFRSGRYLTCSAIFRGKVSMKEVEDQMRNIQNKNSAYFVEWIPNNVQTALCSIPPRGLQMSSTFVGNSTSIQELFKRVGDQFTAMFRKKAFLFWYTGEGMDEMEFTEAENNMNDLVSEYQQYQDASVSDGEEEYLEDEQLEGEE | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Q5UBX3 |
Q09818 | YAC4_SCHPO | Putative general negative regulator of transcription C16C9.04c | Schizosaccharomyces | MLKTQEIYSSEDEDDMCCPLCMEEIDISDKNFKPCQCGYRVCRFCWHHIKEDLNGRCPACRRLYTEENVQWRPVTAEEWKMDLHRKNERKKREKERKEVELSNRKHLANIRVVQKNLAYVNGLSPKVANEENINVLKGPEYFGQYGKIIKIAINKKAAANSANGHVGVYITYQRKEDAARAIAAIDGSVSDGRHLRASYGTTKYCTSYLRNQQCPNPSCMYLHEPGDEVDSYTKEDLASLQHTRPLSTKPNVVNGATHSPSPSLPFKTPLLPVTKTPLEEANSSPAAQNQHITTVDHVHPQVSMTPSLSTNNTATSVPAPYSSAASVNVVPGHATTILHHEESSALPPTAAWAKLSPSVLQERLRAAVNQQPLDALKSSSTQTSIPKIQKLKAAKLPSEEENTTKWLNKAINDLVSSLSKINFSTEGTEFDKKQIEMIQNLPPLFVFNARSVIDKEVVPEQEKSAENQPPTSLGINNGNPVMPPPGFQS | May negatively regulate the basal and activated transcription of many genes. | Q09818 |
B4QAF0 | TOTF_DROSI | Protein Turandot F | Sophophora | MKTVILFSFLLVLLGCLEAGHAQRDPEFSSKARQMLAVFGNSEVDRYTKSRNLPALIEFYEKYSSRLPLTVQDRTYANNVVRRYRAQNNQQVDGVPAQGGIGLAFALLLPFAMSIVEGIAKAIRE | A humoral factor that may play a role in stress tolerance. | B4QAF0 |
P04990 | THRC_BACSU | Threonine synthase | Bacillus | MWKGLIHQYKEFLPVTDQTPALTLHEGNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVIIPNGKIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYRIEGQKTAAFEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYHEKNGTGLPKMRGFEAEGAAAIVRNEVIENPETIATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLTGNGLKDPNTAVDISEIKPVTLPTDEDSILEYVKGAARV | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. | P04990 |
B9JR40 | YACG_AGRVS | DNA gyrase inhibitor YacG | Agrobacterium | MSDEPEHTAKVEPLRKPLPCPECGHPSHREHYPFCSDRCRTQDLSRWLKGSYAIPVAEDESNPDDDGRF | 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. | B9JR40 |
P53220 | TIM21_YEAST | Mitochondrial import inner membrane translocase subunit TIM21 | Saccharomyces | MSSSLPRSLLRLGHRKPLFPRYNTFVNSSVITHTSLLRTRLYSNGTGATSGKKDDKTRNKPKPLWPQVKSASTFTFSGILVIGAVGISAIVIYLILSELFSPSGDTQLFNRAVSMVEKNKDIRSLLQCDDGITGKERLKAYGELITNDKWTRNRPIVSTKKLDKEGRTHHYMRFHVESKKKIALVHLEAKESKQNYQPDFINMYVDVPGEKRYYLIKPKLHPVSNSKGFLGIRWGPRKD | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex. | P53220 |
E9Q4P1 | WDFY1_MOUSE | WD40- and FYVE domain-containing protein 1 | Mus | MAAEIHSRPQSSRPVLLSKIEGHQDAVTAALLIPKEDGVITASEDRTIRVWLKRDSGQYWPSIYHTMASPCSAMAYHHDSRRIFVGQDNGAVMEFHVSEDFNKMNFIKTYPAHQNRVSAIIFSLAAEWVISTGHDKCVSWMCTRSGNMLGRHFFSSWASCLQYDLDTQHAFVGDYSGQITLLKLEQNTCSVITTLKGHEGSIACLWWDPIQRLLFSGASDNSVIMWDIGGRKGRTLLLQGHHDRVQSLCYLQLTRQLVSCSADGGIAVWNMDVSREEAPQWLESDSCQKCEQPFFWNIKQMWDTKTLGLRQHHCRKCGQAVCGKCSSKRSSYPVMGFEFQVRVCDSCYDSIKDEDRTSLATFHEGKHNISHMSMDIARGLMVTCGTDRVVKIWDMTPVVGCSLATGFSPH | 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 . | E9Q4P1 |
Q31GK3 | TRUB_HYDCU | tRNA-uridine isomerase | Hydrogenovibrio | MAKKQWQKIDGIVLLNKPEGVTSNGLLQQVRRVYNAKKAGHTGALDPFATGLLPICLGEATKISGLLLDSDKRYIATLQLGLETDSGDKDGNPLKTIAVPALSKAMLETVFSQFEGDVMQVPPMYSALKHQGKPLYEYARKGIHIERAARPIHIYELKLIDFENTVVRFEVLCSKGTYVRTLGEDIAKALGTVGHLTGLHRTQTGALTGDEMATLEEIELNKDAYLQPLDLPLKHLQAIHLNAKDTDKILHGGKLAVEEPETLLVRFYDPQQRFIGVGEWQQEKQLLKPKRLFNLNPIGDDHS | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q31GK3 |
P49368 | TCPG_HUMAN | hTRiC5 | Homo | MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLACNIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPDAGQE | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis . The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance . As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia . The TRiC complex plays a role in the folding of actin and tubulin (Probable). | P49368 |
B2TUS3 | YIDC_SHIB3 | Membrane protein YidC | Shigella | MDSQRNLLVIALLFVSFMIWQAWEQDKNPQPQAQQTTQTTTTAAGSAADQGVPASGQGKLISVKTDVLDLTINTRGGDVEQALLPAYPKELNSTQPFQLLETSPQFIYQAQSGLTGRDGPDNPANGPRPLYNVEKDAYVLAEGQNELQVPMTYTDAAGNTFTKTFVLKRGDYAVNVNYNVQNAGEKPLEISTFGQLKQSITLPPHLDTGSSNFALHTFRGAAYSTPDEKYEKYKFDTIADNENLNISSKGGWVAMLQQYFATAWIPHNDGTNNFYTANLGNGIAAIGYKSQPVLVQPGQTGAMNSTLWVGPEIQDKMAAVAPHLDLTVDYGWLWFISQPLFKLLKWIHSFVGNWGFSIIIITFIVRGIMYPLTKTQYTSMAKMRMLQPKIQAMRERLGDDKQRISQEMMALYKAEKVNPLGGCFPLLIQMPIFLALYYMLMGSVELRQAPFALWIHDLSAQDPYYILPILMGVTMFFIQKMSPTTVTDPMQQKIMTFMPVIFTVFFLWFPSGLVLYYIVSNLVTIIQQQLIYRGLEKRGLHSREKKKS | 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. | B2TUS3 |
P10026 | TRAM1_ECOLI | Relaxosome protein TraM | Escherichia | MAKVNLYISNDAYEKINAIIEKRRQEGAREKDVSFSATASMLLELGLRVHEAQMERKESAFNQTEFNKLLLECVVKTQSSVAKILGIESLSPHVSGNSKFEYANMVEDIREKVSSEMERFFPKNDDE | Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Cooperatively binds 3 regions in the F plasmid oriT locus; 2 are required for autoregulation while the other is required for plasmid transfer. Bends oriT DNA less than 50 degrees. Plasmid specificity is conferred by the TraD-TraM pair. | P10026 |
Q7V906 | THIC_PROMM | Thiamine biosynthesis protein ThiC | Prochlorococcus | MRASWVAARKGQANVSQLHFARQGVVTQEMDYVAKRENLPESLVMEEVARGRMIIPANINHENLEPMAIGIASSCKVNANIGASPNASDVAEELKKLELAVKYGADTVMDLSTGGVNLDEVRTAIINASPVPIGTVPVYQALESVHGSIEQLDEDDFLHIIEKHCQQGVDYQTIHAGLLIEHLPLVKGRLTGIVSRGGGILAQWMLYHHRQNPLFTRFDDICEIFKRYDCSFSLGDSLRPGCQHDASDAAQLAELKTLGELTKRAWAHDVQVMVEGPGHVPMDQIEFNVRKQMEECNEAPFYVLGPLVTDIAPGYDHITSAIGAAMAGWYGTAMLCYVTPKEHLGLPNPEDVREGLIAYKIAAHAADIARHRPGARDRDDELSRARYNFDWNKQFELSLDPERAKQYHDETLPADIYKQAEFCSMCGPKHCPMQTKITDEDLEGLEKSLKSKGKAKLSA | 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. | Q7V906 |
P49957 | TRM9_YEAST | tRNA methylase 9 | Saccharomyces | MEINQAAEKEQEYVHKVYNEIAPHFSQTRYKPWPIVTQFLKTRPMGSIGIDVGCGNGKYLGVNPDIYIIGSDRSDGLIECARGINPSYNLLVADGLNLPHKNETFDFAISIAVVHHWSTRERRVEVIRHVLSKLRQGGQALIYCWALEQGSSRRGYHEGMEQDVFVPWVLPKSKSKPKTKSTPPAKVKTRPKPNLMNIPPKERSEYLQRWKEEQQRSKSLDDNDEKQQQDQEQEREEVKYRYYHLYREGELAEDCRQAGAAVHSEGFERDNWWVVAQKR | Required for the methylation of the wobble bases at position 34 in tRNA. Appears to have a role in stress-response. | P49957 |
B2HXY4 | UPPP_ACIBC | Undecaprenyl pyrophosphate phosphatase | Acinetobacter calcoaceticus/baumannii complex | MENFEVIKALFLGFVEGLTEFLPISSTGHLILFGHIIDFHSDGGRVFEVVIQLGAILAVCWLYRQKIINLIKGFFSGDVESRHFAISVLIAFFPAVIIGVLAVDFIKSVLFSPIVVAIALIVGALIIFWVESKQFEHKTDDATKITFKQALLVGLAQCVAMIPGTSRSGATIVGGMFAGLSRKAATEFSFFLAMPTMLGAATFDLIKNADVLTSDNMVNIGVGFVAAFIAALLVVKALVLFVERHTLRVFAWYRIVLGVIILIAAMFFNLSA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | B2HXY4 |
A9KLV5 | TRMB_LACP7 | tRNA(m7G46)-methyltransferase | Lachnospiraceae | MRLRNIPGSREYIAQNDYVVHDPEQKKGKWHEVFGNNNPIHIEIGMGKGQFITSLAMQNPNINYIGIEKYSSVLLRAIEKREEYEGDNLYFLRFDAESITDIFAPSEVDRIYLNFSDPWPKDRHSKRRLTSSEFLARYDQFLVKDGYVAFKTDNRDLFDFSLEQVTLSGWQLRDVTFDLHHSEYVEGNIMTEYEERFSSMGNPIHRLVAFREKE | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | A9KLV5 |
A3PM58 | TOLB_CERS1 | Tol-Pal system protein TolB | Cereibacter | MTLFRTLAPMGLALALLLPAAVPAAAQQGPLRIQITEGVIEPLPFAVPDFVAENAGASELARDMARVIASDLSGTGLFREIPASAHISRVTSFEAPVAYGDWKAINAQALITGSVSASGDRVVVKFRLYDVFSDQPLGEGLQFAGSASGWRRMAHKVADVAYSRITGEGGYFDSRVVFVSESGPKNARAKRLAVMDYDGANVQYLTDSSSIVLAPRFSPTGDRILFTSYSTGFPRIYLMDVGSLATRGLAEQPGTMTFAPRFAPDGRTVAFSLEQGGNTDIYTLDTGSGTRRQLTNSPSIETAPSYSPDGSQIVFESDRSGGQQLYIMPAGGGEPRRISNGAGRYGTPVWSPRGDLIAFTKQHQGRFHIGVMRTDGSEERLLTASFLDEGPTWAPNGRVLMFTREGAGAGGQPALYSVDISGRNLKKVPLSVPASDPAWSPLLP | 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. | A3PM58 |
Q8K2T4 | UQCC3_MOUSE | Ubiquinol-cytochrome-c reductase complex assembly factor 3 | Mus | MEVARKALVAVAVLGGGAGVGSILFALVTPGELQKQSMLQEMPERDSRRRDEAVRTTELVMATLKDAAATKENVAWRRNWTVSGDGRSA | Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology. | Q8K2T4 |
P26651 | TTP_HUMAN | Zinc finger protein 36 | Homo | MDLTAIYESLLSLSPDVPVPSDHGGTESSPGWGSSGPWSLSPSDSSPSGVTSRLPGRSTSLVEGRSCGWVPPPPGFAPLAPRLGPELSPSPTSPTATSTTPSRYKTELCRTFSESGRCRYGAKCQFAHGLGELRQANRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPSEDLAAPGHPPVLRQSISFSGLPSGRRTSPPPPGLAGPSLSSSSFSPSSSPPPPGDLPLSPSAFSAAPGTPLARRDPTPVCCPSCRRATPISVWGPLGGLVRTPSVQSLGSDPDEYASSGSSLGGSDSPVFEAGVFAPPQPVAAPRRLPIFNRISVSE | (Microbial infection) Negatively regulates HTLV-1 TAX-dependent transactivation of viral long terminal repeat (LTR) promoter. | P26651 |
P0DQJ5 | VSTX1_ACAGO | U1-theraphotoxin-Agm3a | Acanthoscurria | MKFSVLVFILGLVLLLALSSATEMEENARACGSFMWKCSERLPCCQEYVCSPQWKWCQNP | Inhibits sodium channels Nav1.7/SCN9A and potassium channels Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) with very slow apparent binding kinetics and affects channel gating. Reaches its target by dynamically partitioning into anionic or zwitterionic headgroup lipid membranes. May bind to the open state of KvAP. | P0DQJ5 |
Q9SZH0 | VATG3_ARATH | Vacuolar proton pump subunit G3 | Arabidopsis | MDSLRGQGGIQMLLTAEQEAGRIVSAARTAKLARMKQAKDEAEKEMEEYRSRLEEEYQTQVSGTDQEADAKRLDDETDVRITNLKESSSKVSKDIVKMLIKYVTTTAA | Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. | Q9SZH0 |
P55730 | Y4ZC_SINFN | Putative cysteine protease YopT-like y4zC | Sinorhizobium | MHSPISGSFTSSTQVHDPIHPANSDGFRETLANVELRTKSPSAECPDKMGCCASKPQASDPNNPSTSSPARPSTSLFRYRTAELAQANADGICVGLTAEWLRNLNSHPSIRMEALVPGSQRHASATVRQKEYENLKVHLRRQGAGPSEADFAAQNTMLQKAGLAPSGKEKVYKVGEPNFPRMLTKITADGSNHLLSLYFAEGGAHTVATSAMDGNTTLFDPNFGEFTVQSDQIDDLFRSLANRYSNPNRQHLTTVTTQKMT | Potential cysteine protease, which may play a central role after invasion of host cell. | P55730 |
Q5MYW4 | ZN667_RAT | Myocardial ischemic preconditioning up-regulated protein 1 | Rattus | MPAARGKSKSKAPVTFGDLAIYFSQEEWEWLSPNQKDLYEDVMLENYHNLVSVGLACRRPNIIALLEKGKAPWMVEPSRKRRGPELGSKDETKKLPPSQCNKSGPSICKKPDSSQQKVPTEKAKHNKNAVPRKNKKGHSGKKSLKCNSCGKTFFRSLSLKLHQGFHTGERSYECSTCGQVFRQILSLILHQRVHTQNKSYECDKCGDIFNKKLTLMIHRRSHNGKENFHHEKTSDSCPSLSPHHNNHAIDSIHQCRKCGKVFSRMSSLLLHKKIHNRKRIQKYSACGRGFKKKPVLVHKRICIGKKTHENKALIQSLRQRTYQSENPFTCRKCRKSFSRISALMLHQRAHTSGNPYKCDKCQKDFGRLSTLILHLRIHSGEKQFKCNKCEKVCNRLSSFIQHKKIHKRKKKLIECKECGKMFGGMKNLKVHLNIHSEEKPFKCNKCSKVFGRQSFLSEHQRIHTGEKPYQCEECGKAFSHRISLTRHKRIHSEDRPYECDLCGKAFSQSAHLAQHERIHTGEKPYACKICKKSFTQRISLILHERSHTGEKPYECNECGKAFSSGSDLIRHQRSHSSEKPYECSKCGKAYSRSSSLIRHQSIHSEEMS | May be involved in transcriptional regulation. | Q5MYW4 |
P9WPI5 | Y106_MYCTU | Zinc chaperone Rv0106 | Mycobacterium tuberculosis complex | MRTPVILVAGQDHTDEVTGALLRRTGTVVVEHRFDGHVVRRMTATLSRGELITTEDALEFAHGCVSCTIRDDLLVLLRRLHRRDNVGRIVVHLAPWLEPQPICWAIDHVRVCVGHGYPDGPAALDVRVAAVVTCVDCVRWLPQSLGEDELPDGRTVAQVTVGQAEFADLLVLTHPEPVAVAVLRRLAPRARITGGVDRVELALAHLDDNSRRGRTDTPHTPLLAGLPPLAADGEVAIVEFSARRPFHPQRLHAAVDLLLDGVVRTRGRLWLANRPDQVMWLESAGGGLRVASAGKWLAAMAASEVAYVDLERRLFADLMWVYPFGDRHTAMTVLVCGADPTDIVNALNAALLSDDEMASPQRWQSYVDPFGDWHDDPCHEMPDAAGEFSAHRNSGESR | Zinc chaperone that directly transfers zinc cofactor to target proteins, thereby activating them. Zinc is transferred from the CXCC motif in the GTPase domain to the zinc binding site in target proteins in a process requiring GTP hydrolysis. | P9WPI5 |
Q1IN69 | TATC_KORVE | Sec-independent protein translocase protein TatC | Candidatus Koribacter | MPSPTIDPAIRARLSQEALKGMSFLEHLEELRRRIIWTFVYIAAGFGVCWWWHEQIYDFMQRPIMKALAANHLDQKLVYLNPTEPFNMYLKMAFIAGLFVASPFVLYQVWLFIAPGLYKRERRYVLPFMFSTVLLFLGGGVFGYYMVYPNALTFLIGYSHQFSPMITISEYTDLFLTIILGLGIVFEMPILVFFLALMGIVSAGWMWRNLRYSILVIFVIAAIITPTTDIMNMCVFAAPMILLYILSIGVAFLVHPKNRRKRREAQEAQEG | 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. | Q1IN69 |
B4II52 | TOTX_DROSE | Protein Turandot X1/X2 | Sophophora | MRLYIGSLLICVLLGIVPFATANTNRSGYEEHRNYLLNIFHNPLVNDSIKEKNIPELIAFYQRYPTDIPLSDADRQQFERFIHDYREYREVLVDGVPPQGGSFGNIFGHFLGRVGTRYISSLFNKKREEGQSNHANSPTTSPSRIQKMTK | A humoral factor that may play a role in stress tolerance. | B4II52 |
T1NXB5 | VSTM4_MOUSE | Peptide Lv | Mus | MRLRLLALAAAVLLGPAPEVCGALNVTVSPGPVVDYLEGENATLLCHVSQKRRKDSLLAVRWFFAPDGSQEALMVKMTKLRIIQYYGNFSRTANQQRLRLLEERRGVLYRLSVLTLRPTDQGQYVCKVQEISKHRNKWTAWSNGSSATEMRVISLKAGEDSSFEKKKVTWAFFEDLYVYAVLVCCVGILSVLLFTLVIAWQSVFHKRKSRVRHYLVKCPQNSSGETVTSVTSLAPLQPQKGKRQKKKVDVPPAVPAKAPIATTFHKPKLLKPQRKVALPKITEENLTYAELELIKPHRAAKGVPTSTVYAQILFEENQL | Peptide Lv enhances L-type voltage-gated calcium channel (L-VGCC) currents in retinal photoreceptors. | T1NXB5 |
B5FA99 | TYPH_ALIFM | TdRPase | Aliivibrio | MYLPQEIIRKKRDNKELTTEEINFFIQGVAKETVSEGQIAAFAMAVYFNEMTMPERIALTCAMRDSGMVIDWSHMNFDGPIVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLESIAGYNITPSNDVFGKVTKEAGVAIIGQTGDLAPADKRVYATRDVTATVDNISLITASILSKKLAAGLDSLVMDVKVGSGAFMPTYEASEELAKSIVAVANGAGTKTTALLTDMNQVLASTAGNALEVREAIRFLTGEYRNPRLYEVTMALCAEMLVIANLAKDEQDARAKLQTVLDNGKAAECFGKMVFGLGGPSDIIENYDNHLESAQIIKPVFADTTGFVHAMDTRDLGMAVVGMGGGRRVASDTIDYAVGLSDMIRLGQTADNQQPLAMIHARNEEQWQQAANAVKAAIVISEKQPEATPEVYRKIRPEDV | 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. | B5FA99 |
B9JXE1 | TATA_AGRVS | Sec-independent protein translocase protein TatA | Agrobacterium | MGSFSMWHWLIVLAIVLLLFGRGKIPELMGDVAKGIKSFKKGMSDDDTAPDGTPKPADQSKTVDHRADDHK | 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. | B9JXE1 |
P0DTB6 | TSI5_PSEAE | Immune protein Tsi5 | Pseudomonas | MPTEGRRRGVSAAMIKHYLLMTLVCIPLALLYVCLEWFFGNTWVTVGVFFGVLVVLRLGLYLYRRSKGIRDGYLDE | Immunity protein that plays a role in preventing early activation of toxin Tse5. | P0DTB6 |
C3K2K2 | THIE_PSEFS | Thiamine-phosphate pyrophosphorylase | Pseudomonas | MKLRGLYAITDSQLLAGKFLAYVEAALDGGVTLLQYRDKSSDEARRLREAEKLRELCSRYKTQLIINDDAELAARLGVGVHLGQTDGPLTPARALLGSKAIIGSTCHSQIELAEQAAKEGASYVAFGRFFNSNTKPGAPAATVEMLAQARARVQLPICVIGGITLENAEPLVAHGADLLAVVHGLFGADSTQEVTRRARAFNDLLKISV | 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). | C3K2K2 |
Q03327 | UGO1_YEAST | Mitochondrial fusion and transport protein UGO1 | Saccharomyces | MNNNNVTEATSRAQIRPYYDPDSFNAGYSAVFKPDEGVVDPHGYTIASKLNVINSSPTTKRMANALFKSSPMKKLSNSVNDGLSLEGSNGEITGLNNFEWAELVNIQKWRKIFEQLLDMFFRKYFQLLIQQPFDVARLLIQVGEFKIFKTTVDTNKPQAPIILRDEEGDGAAREGEEDAYDEEEIDFFPIERKIAEANSTAPIMAEETDHSHHEPTDISLTIAPQSLHTIDVINALFDQEGIRGLWKANNTTFIYNFLSLSIDTWFTGLLSSFLGVPDPYFMEVINSPDISKSFILALGAGVFTSIILLPVDLIRTRLIVTSFKKKKNVKTDGKNMVTNTRSLRQLIRCWSWRKNGVSIPLDMWSLTILQSINNSFFNKLFDLVIYNQFHIEKYSQTVMYNTMKFFSKSLELFIKLPLENLLRRCQLNYLLNDQRLSFKVDSTELIVKPKKYNGIWDVIRNNSNTNRGQLWNGWKVGVISLICGYGLQMMNKVDINMEQEKF | Required for mitochondrial fusion as well as normal mitochondrial morphology by bridging the essential interaction between FZO1 and MGM1. May coordinate fusion of inner and outer membranes during mitochondrial fusion. | Q03327 |
B2VES1 | ZAPB_ERWT9 | Cell division protein ZapB | Erwinia | MSFEVFEKLEAKVQQAIDTITLLQMEIEELKEQNGSLNHQVQQASGNSEALVRENQQLKEEQHVWQERLRALLGKMEEV | Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. | B2VES1 |
Q18319 | VPS55_CAEEL | Vacuolar protein sorting-associated protein 55 homolog | Caenorhabditis | MGGVRAVAALAFAGVVGLTFLVLGCALPRYGTWTPMFVITFYVLSPVPLLIARRFQEDMTGTNACIELALFITTGIVISAFALPIVLAHAGTIANSACFLVNTGSVIMFGTIIAYFYLHRDDDSGSWSQSLF | Involved in endosomal protein transport. | Q18319 |
Q25457 | TPM_MYTED | Tropomyosin | Mytilus | MDAIKKKMVAMKMEKENALDRAEQLEQKLRETEEAKAKIEDDYNSLQKKSIQTENDLDNTQTQLQDVQAKYETTEKQIAEHEQEIQSLTRKISMLEEDIMKSEERYTTAASKLEEASKAADESERNRKVLENLNCGNDERIDQLEKQLTEAKWIAEEADKKYEEAARKLAITEVDLERAEARLEAAEAKVIDLEEQLTVVGANIKTLQVQNDQASQREDSYEETIRDLTNRLKDAENRATEAERTVSKLRKEVDRLEDELLTEKEKYKAISDELDATFAELAGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q25457 |
Q0AC96 | UREF_ALKEH | Urease accessory protein UreF | Alkalilimnicola | MSTETNPGLAQRRLWQLISPTLPIGAYSYSAGLEYAVEAGWLRNADAVADWLQGQLHHALAPVDIPALARLHAAWQSDDAVAVHYWSQWLRACRETKELREEDRHVGQALARLLRDLDLPEAAPWVDDPIAGWPTLYALAVARWAIPLETAAEAYLWAWCENQVSAAIKLVPLGQTAGQRLLLEMAEPVGEAARQGLALEDEEMGGGLPGVALASSLHETQYSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q0AC96 |
Q92LH8 | TSAD_RHIME | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Sinorhizobium | MRILGIETSCDETAASVVLRDEEGRGRILGDVVLSQLEEHSAYGGVVPEIAARAHVEALDALIEEALLRAGVTLRDIDAVAATSGPGLIGGLIVGLMTGKAIARATGKPLYAVNHLEGHALTARLTDGLSFPYLMLLVSGGHTQLILVKGVGEYERWGTTIDDALGEAFDKTAKLLGLPYPGGPAVERAAQAGNAERFDFPRPLVGDARLDFSFSGLKTAVRQAAQSLGPVTDQDIADVCASFQRAISRTLRDRVGRGLKRFRADFASVDQPALVVAGGVAANQTLRRTLQSLCDEHGFRFIAPPLQLCTDNAAMIAWAGAERLAAGLPADGLDAAPRSRWPLDSEAKALIGSGRRGAKA | 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. | Q92LH8 |
Q99JR5 | TINAL_MOUSE | Tubulointerstitial nephritis antigen-related protein | Mus | MWGCWLGLLLLLLAGQAALEARRSRWRRELAPGLHLRGIRDAGGRYCQEQDMCCRGRADECALPYLGATCYCDLFCNRTVSDCCPDFWDFCLGIPPPFPPVQGCMHGGRIYPVFGTYWDNCNRCTCHEGGHWECDQEPCLVDPDMIKAINRGNYGWQAGNHSAFWGMTLDEGIRYRLGTIRPSSTVMNMNEIYTVLGQGEVLPTAFEASEKWPNLIHEPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPILSPQNLLSCDTHHQQGCRGGRLDGAWWFLRRRGVVSDNCYPFSGREQNEASPTPRCMMHSRAMGRGKRQATSRCPNGQVDSNDIYQVTPAYRLGSDEKEIMKELMENGPVQALMEVHEDFFLYQRGIYSHTPVSQGRPEQYRRHGTHSVKITGWGEETLPDGRTIKYWTAANSWGPWWGERGHFRIVRGTNECDIETFVLGVWGRVGMEDMGHH | May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein. | Q99JR5 |
Q9FII5 | TDR_ARATH | Tracheary element differentiation inhibitory factor receptor | Arabidopsis | MKKKNISPSLVLHPLLLLLLPFFAFNSLALKFSPQLLSLLSLKTSLSGPPSAFQDWKVPVNGQNDAVWCSWSGVVCDNVTAQVISLDLSHRNLSGRIPIQIRYLSSLLYLNLSGNSLEGSFPTSIFDLTKLTTLDISRNSFDSSFPPGISKLKFLKVFNAFSNNFEGLLPSDVSRLRFLEELNFGGSYFEGEIPAAYGGLQRLKFIHLAGNVLGGKLPPRLGLLTELQHMEIGYNHFNGNIPSEFALLSNLKYFDVSNCSLSGSLPQELGNLSNLETLFLFQNGFTGEIPESYSNLKSLKLLDFSSNQLSGSIPSGFSTLKNLTWLSLISNNLSGEVPEGIGELPELTTLFLWNNNFTGVLPHKLGSNGKLETMDVSNNSFTGTIPSSLCHGNKLYKLILFSNMFEGELPKSLTRCESLWRFRSQNNRLNGTIPIGFGSLRNLTFVDLSNNRFTDQIPADFATAPVLQYLNLSTNFFHRKLPENIWKAPNLQIFSASFSNLIGEIPNYVGCKSFYRIELQGNSLNGTIPWDIGHCEKLLCLNLSQNHLNGIIPWEISTLPSIADVDLSHNLLTGTIPSDFGSSKTITTFNVSYNQLIGPIPSGSFAHLNPSFFSSNEGLCGDLVGKPCNSDRFNAGNADIDGHHKEERPKKTAGAIVWILAAAIGVGFFVLVAATRCFQKSYGNRVDGGGRNGGDIGPWKLTAFQRLNFTADDVVECLSKTDNILGMGSTGTVYKAEMPNGEIIAVKKLWGKNKENGKIRRRKSGVLAEVDVLGNVRHRNIVRLLGCCTNRDCTMLLYEYMPNGSLDDLLHGGDKTMTAAAEWTALYQIAIGVAQGICYLHHDCDPVIVHRDLKPSNILLDADFEARVADFGVAKLIQTDESMSVVAGSYGYIAPEYAYTLQVDKKSDIYSYGVILLEIITGKRSVEPEFGEGNSIVDWVRSKLKTKEDVEEVLDKSMGRSCSLIREEMKQMLRIALLCTSRSPTDRPPMRDVLLILQEAKPKRKTVGDNVIVVGDVNDVNFEDVCSVDVGHDVKCQRIGV | Acts with CLE41p and CLE44p peptides as a ligand-receptor pair in a signal transduction pathway involved in the regulation of procambium maintenance and polarity during vascular-tissue development . Mediates repression of tracheary element differentiation and the promotion of procambial cells formation and polar division adjacent to phloem cells in the veins . | Q9FII5 |
Q7WB52 | UBID_BORPA | Polyprenyl p-hydroxybenzoate decarboxylase | Bordetella | MKYRDLRDFLAQLERQGELKRITAPVSTRLEMTEIADRVLRAGGPALLFENARHNDAPADMPVLANLFGTPRRVAWGMGADDVGALRETGELLASLREPEAPKGLRDALAKVSMLKAALWDMSPKTVRSAACQEIVWEGADVDLGRLPIQTCWPGDVAPLLAWGLVITRGPNARRQNLGIYRQQPLGPNKLIMRWLSHRGGALDFRDHAQAHPGKSFPIAVALGADPATILDAVTPVPDTLSEYQFAGLLRGSRTEVVKALGSDLSVPASAEIVLEGHLLPADDPRAVAAAVPEGANPPPATGYEMALEGPYGDHTGYYNEQDWFPVFTVDRITMRRNPIYHSTYTGKPPDEPAVLGVALNEVFVPLLRRQLPEIVDFYLPPEGCSYRLAVVSIRKQYAGHAKRVMFGLWSVLRQFMYTKFIVVVDEDIDPRDWTEVVWAMTTRMDPVRDTVLVENTPIDYLDFASPVSGLGGKMGLDATNKWPGETSREWGTPIHMDEAVKRRVDAMWDTLGL | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | Q7WB52 |
B2JFD3 | YQGF_PARP8 | Putative pre-16S rRNA nuclease | Paraburkholderia | MSGVAGREATLLAFDYGEKRIGVAVGNSLTRSARPLVVLQNRNREYRFEAVGKLIDEWKPDALVVGLPMHPDGTPHERTQLAKRFGNQLNGRFNLPVTWIDERYSSVEAEAGIRSGTRQAGMLDAEAACIILQQYLDGLSLEGPSDDHEFR | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B2JFD3 |
P31489 | YADA1_YEREN | Type 5 secretion system autotransporter YadA | Yersinia | MTKDFKISVSAALISALFSSPYAFADDYDGIPNLTAVQISPNADPALGLEYPVRPPVPGAGGLNASAKGIHSIAIGATAEAAKGAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGAASTAQKDGVAIGARASTSDTGVAVGFNSKADAKNSVAIGHSSHVAANHGYSIAIGDRSKTDRENSVSIGHESLNRQLTHLAAGTKDTDAVNVAQLKKEIEKTQENTNKRSAELLANANAYADNKSSSVLGIANNYTDSKSAETLENARKEAFAQSKDVLNMAKAHSNSVARTTLETAEEHANSVARTTLETAEEHANKKSAEALASANVYADSKSSHTLKTANSYTDVTVSNSTKKAIRESNQYTDHKFRQLDNRLDKLDTRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNENVALKAGVAYAGSSDVMYNASFNIEW | Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance. | P31489 |
Q06490 | THI22_YEAST | Thiamine biosynthesis protein THI22 | Saccharomyces | MVIILLGLCTLGFPRTAFCPSIMTNSTVSINTPPPYLTLACNEKLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGMLTVDAIEVLHEKLLQLGENRPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGENREVSKLQDVLEIAKDLSRITNCSNILVKGGHIPCDDGKEKHITDVLYLGAEQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQNAIAIGCDVTKKAVKVGPINHVYAVEIPLEKMLTDECFTASDAVPKKPIEGSLDKIPGGSFFNYLINHPKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELNEHERRLREEFGVKDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTCASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAAMEYE | Is not required for thiamine biosynthesis. | Q06490 |
A1SVA9 | UPP_PSYIN | UPRTase | Psychromonas | MKVIEVKHPLIQHKIGLMREADISTKRFREIAREVGSLLTYEATKNLELETVKIQGWNGEVEVQQIKGKKATVVPILRAGLGMMDGVLEHMPSAKISVVGIYRDEKTLEPVPYFQKLVSNIDERLAIVVDPMLATGGSMISTIDLIKKAGCTRIVVLVLVAAPEGLKALEAAHPDLEVYTASIDDHLDEQGYIVPGLGDAGDKIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | A1SVA9 |
P55332 | XYNA_EMENI | Xylanase X22 | Aspergillus subgen. Nidulantes | MVSFKSLLVLCCAALGAFATPVGSEDLAAREASLLERSTPSSTGWSNGYYYSFWTDGGGDVTYTNGAGGSYTVQWSNVGNFVGGKGWNPGSTRTINYGGSFNPSGNGYLAVYGWTQNPLIEYYIVESYGTYNPGSGGQHRGTVYSDGATYDIYTATRYNAPSIEGTATFEQFWSVRQSKRTGGTVTTANHFNAWAALGMRLGTHNYQIVATEGYQSSGSASITVY | Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. | P55332 |
A1AXX3 | TPIS_RUTMC | Triose-phosphate isomerase | Candidatus Ruthia | MRQIIIAGNWKMNASKEATNTLVIGILSGMADVKSKVIVCVPSLYMSQVEVLVVDSQLNLGAQNLNVNKLGAFTGEISADMIKDFGAKYVIVGHSERRSLYGETDEIVAQKVQVALDNNLTPLFCIGELLEDRESNNTKSVVSKQIQVVIDRVGIEAFKNIIVAYEPVWAIGTNVTATPQQAQDTHAFIRSMLAEYDADIAQITSILYGGSMNSRNAAELLNCKDIDGGLIGGASLKAQDFLQICKAG | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A1AXX3 |
Q5LJ29 | TRUB_BACFN | tRNA-uridine isomerase | Bacteroides | MNFKEGEVLYFNKPLGWTSFKVVGHARYHMCRRMKVKKLKVGHAGTLDPLATGVMIVCTGKATKRIEEFQYHTKEYVATIQLGATTPSYDLEHEIDATYPTEHITRELVEKTLKTFVGEIQQIPPAFSACKVDGARAYDLARKGQEVELKPKLLVIDEIELLECNLPEIKIRVVCSKGTYIRALARDIGEALQSGAHLTGLIRTRVGDVKLEQCLDPAKFAEWIDQQDVEISD | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q5LJ29 |
P39800 | XLYA_BACSU | Cell wall hydrolase | Bacillus | MVNIIQDFIPVGANNRPGYAMTPLYITVHNTANTAVGADAAAHARYLKNPDTTTSWHFTVDDTEIYQHLPLNENGWHAGDGNGSGNRASIGIEICENADGDFAKATANAQWLIKTLMAEHNISLANVVPHKYWSGKECPRKLLDTWDSFKAGIGGGGSQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIVSAPSAAEKPELYPLPDGIIQLTTPYTSGEHVFQVQRALAALYFYPDKGAVNNGIDGVYGPKTADAVARFQSVNGLTADGIYGPATKEKIAAQLS | Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. | P39800 |
Q5RER9 | ZN813_PONAB | Zinc finger protein 813 | Pongo | MALSQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMMKEFLSTAQGNREVFHTGTLERHESHHIGDFCFQETDKDIHNLEFQWQEDERNGHEVLMTEIKKLTGSTDQYNQSHARNKPIKDQLGSSFYSHLPELHIFQTQGKIDNQVEKSINNASSISTAQRISCRPKTHISNNYGNNFLNSLLLTQKQEVRMREKSFQYNESGKAFNYSSLLRKHQIIHLGEKQYKCDVCGKVFNRKRNLACHRRCHTGEKPYRCNECGKTFSQTYSLTCHRRLHTGEKPYKCEECDKAFSFKSNLKRHRRIHAGEKPYKCNECGKTFSQTSSLTCHRRLHTGEKPYKCNECGKTFSWKSSLTCHHRLHTGEKPYKCNECGKTFSQELTLKCHRRLHTGEKPYKCNECGKVFNKKANLARHHRLHSGEKPYKCTECVKTFSRNSALVIHKAIHIGEKRYKCNECGKTFSRISALVIHTAVHTGEKPYKCNECGKGFYRKAHLVCHHRLHTGEKPYKCNECGKVFNRKTHLAHHHRLHTGDKPYKCNECGKVFNQKAHLARHHRLHTGEKPYKCTECGKVFNQKANLARHHRLHTGEKPYKFSECGTVLN | May be involved in transcriptional regulation. | Q5RER9 |
Q5HRX4 | XPT_STAEQ | Xanthine phosphoribosyltransferase | Staphylococcus | MESLGRKVKEDGVVIDEKILKVDGFLNHQIDAKLMNDVGKTFYESFKDAGITKILTIEASGIAPAIMASFHFDVPCLFAKKAKPSTLKDGFYSTDIHSFTKNKTSTVIVSEEFLGADDKVLIIDDFLANGDASLGLNDIVKQANATTVGVGIVVEKSFQNGRQRLEDAGLYVSSLCKVASLKGNKVTLLGEA | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q5HRX4 |
Q95JV5 | ZN512_MACFA | Zinc finger protein 512 | Macaca | MSSRLGAVPATSGPTTFKQQRSTRIVGAKNRTQCSIKDNSFQYTIPHDDSLSGSSSASSCEPVSDFPASFRKSTYWMKMRRIKPAATSHVEGSGGVSAKGKRKPRQEEDEDYREFPQKKHKLYGRKQRPKTQPNPKSQARRIRKEPPVYAAGSLEEQWYLEIVDKGSVSCPTCQAVGRKTIEGLKKHMENCKQEMFTCHHCGKQLRSLAGMKYHVMANHNSLPILKAGDEIDEPTERERLRTVLKRLGKLRCMRESCSSSFTSIMGYLYHVRKCGKGAAELEKMTLKCHHCGKPYRSKAGLAYHLRSEHGPISFFPESGQPECLKEMNLESKSGGRVQRRSAKIAVYHLQELASAELAKEWPKRKVLQDLVPDDRKLKYTRPGLPTFSQEVLHKWKTDIKKYHRIQCPNQGCEAVYSSVSGLKAHLGSCTLGNFVAGKYKCLLCQKEFVSESGVKYHINSVHAEDWFVVNPTTTKSFEKLMKIKQRQQEEEKRRQQHRSRRSLRRRQQPGIELPETELSLRVGKDQRRNEELVVSASCKEPEQEPVPAQFQKVKPPKTNHKRGRK | May be involved in transcriptional regulation. | Q95JV5 |
O96014 | WNT11_HUMAN | Protein Wnt-11 | Homo | MRARPQVCEALLFALALQTGVCYGIKWLALSKTPSALALNQTQHCKQLEGLVSAQVQLCRSNLELMHTVVHAAREVMKACRRAFADMRWNCSSIELAPNYLLDLERGTRESAFVYALSAAAISHAIARACTSGDLPGCSCGPVPGEPPGPGNRWGGCADNLSYGLLMGAKFSDAPMKVKKTGSQANKLMRLHNSEVGRQALRASLEMKCKCHGVSGSCSIRTCWKGLQELQDVAADLKTRYLSATKVVHRPMGTRKHLVPKDLDIRPVKDSELVYLQSSPDFCMKNEKVGSHGTQDRQCNKTSNGSDSCDLMCCGRGYNPYTDRVVERCHCKYHWCCYVTCRRCERTVERYVCK | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. | O96014 |
Q94A09 | TRM9_ARATH | tRNA methyltransferase 9 homolog | Arabidopsis | MILDVLRTFSTRTRNLPSSGFYSISTSIMRDIKVKSDSKEFLTSSDEEEESVSIRVSSSSSLSSVKSTPEIEKKYVHRVYDAIAPHFSSTRFAKWPKVAAFLESLPSGSVILDAGCGNGKYLGLNPSCFFIGCDISHPLIKICSDKGQEVLVADAVNLPYREEFGDAAISIAVLHHLSTENRRKKAIEELVRVVKPGGFVLITVWAAEQEDTSLLTKWTPLSAKYVEEWVGPGSPMNSPRVRNNPFFSLESIPETEVSTKEQKVENSQFIGLESIPESEESTREQKGESIIPETKASIVEQKDEKSVEESLEALKKSQQEYFVPWHLPYHRAEVSGASASALASGLAKKDDRKGAVVYNRYYHVFSEGELERLASGVGNAMIVDRFFDKSNWCIVLQKEALNQD | Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA. | Q94A09 |
P9WKX6 | Y3660_MYCTO | Uncharacterized protein MT3760 | Mycobacterium tuberculosis complex | MLTDPGLRDELDRVAAAVGVRVVHLGGRHPVSRKTWSAAAAVVLDHAAADRCGRLALPRRTHVSVLTGTEAATATWAAAITVGAQHVLRMPEQEGELVRELAEAAESARDDGICGAVVAVIGGRGGAGASLFAVALAQAAADALLVDLDPWAGGIDLLVGGETAPGLRWPDLALQGGRLNWSAVRAALPRPRGISVLSGTRRGYELDAGPVDAVIDAGRRGGVTVVCDLPRRLTDATQAALDAADLVVLVSPCDVRACAAAATMAPVLTAINPNLGLVVRGPSPGGLRAAEVADVAGVPLLASMRAQPRLAEQLEHGGLRLRRRSVLASAARRVLGVLPRAGSGRHGRAA | May play a role in septum formation. | P9WKX6 |
O75191 | XYLB_HUMAN | Xylulose kinase | Homo | MAEHAPRRCCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKLEQRILSQTRGPPE | Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. | O75191 |
Q6U1I3 | VIOA_SHIDY | dTDP-4-amino-4,6-dideoxy-D-glucose transaminase | Shigella | MEKPIFVTQPNLPPLEEFIPYLEIIWQNKQFTNNGPMHQKLEKKLCEFLGVEYISLFNNGTIALITAVQALGVKGEVITTPYSFVATAHSLVLNGLKPVFVDIDPKTLNIDPRRIEEAITPETQAIMPVHCYGNPCDTQAIADIAQKYNLKVIYDAAHAFGVEDDDGSVLRHGDLSVLSFHATKVFSTFEGGAIVCNSKEMKEKIDRLKNFGYIDETNINIIGSNGKMSEVNAAFGLLQLEHMDTFLRGRMNADMFYRQKLKDITGISIVIPSGQKISNFSYFPILVESDFPLSRDELFNYLKNQNIFARRYFYPVIPDFQAYLNVGEVCDVKNAREIASKVLCLPMHAELSSDILEYIVSTIREIK | Catalyzes the conversion of dTDP-4-dehydro-6-deoxy-D-glucose (dTDP-D-Glc4O) to dTDP-4-amino-4,6-dideoxy-D-glucose (dTDP-D-Qui4N). L-glutamine can also be used as amino donor. | Q6U1I3 |
A8ACU6 | WZYE_CITK8 | Probable ECA polymerase | Citrobacter | MSLMQFSGLLVVWLLSTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQALLSAACFYAVYYVTYKTRLRKRVTDVPRKPLFTMNRVETHLTWVMLMGIALVSVGIFFMHNGFLLFRLHSYSQIFSSEVSGVALKRFFYFFIPAMLVIYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLVAAGVLGIVGMFWLALKRYGLNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYDNIDFQGLAPIVRDFYVFIPSWLWPGRPGIVLNSANYFTWEVLNNHSGLAISPTLIGSLVVMGGALFIPLGAVAVGLIIKWFDWLYELGNRETNRYKAAILHSFCFGAIFNMIVLAREGLDSFVSRVVFFLVIFGACLLVAKLLFWLFDCAGLVHQRAKPQPQTQVEG | Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. | A8ACU6 |
P32777 | VLP17_BORHE | Variable major outer membrane lipoprotein 17 | Borrelia | MRKRISAIIMTLFMVLVSCNSGGVAEDPKTVYLTSIANLGKGFLDVFVTFGDMVTGAFGIKADTKKSDIGKYFTDIESTMTSVKKKLQDEVAKNGNYPKVKTAVDEFVAILGKIEKGAKEASKGATGDVIIGNTVKNGDAVPGEATSVNSLVKGIKEIVGVVLKEGKADADATKDDSKKDIGKLFTATTDANRADNAAAQAAAASIGAVTGADILQAIVQSKENPVANSTDGIEKATDAAEIAVAPAKDNKKEIKDGAKKDAVIAAGIALRAMAKNGTFSIKNNEDAAVTTINSAAASAVNKILSTLIIAIRNTVDSGLKTINEALATVKQEDKSVEATNTAEATTSGQQAKN | 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. | P32777 |
Q2G639 | TGT_NOVAD | tRNA-guanine transglycosylase | Novosphingobium | MTRFSFKIHATDGKARTGAIQMMRGEIRTPAFMPVGTAATVKAMKVEDVRASGADIILGNTYHLMLRPGAERVARLGGLHKFMGWDRPILTDSGGYQVMSLSDLRKITEEGVTFASHLDGSRHLLSPERSMEIQRLLGSDIVMCFDECPRADQPREVIARSMEMSMRWARRSRDAFDAGGEHAERSALFGIQQGALDEGLRKTSADALTDIGFDGYAIGGLAVGEGQEAMFATLDFAPQQLPADRPRYLMGVGKPDDLVGAVERGVDMFDCVLPTRSGRNGQAFTWNGPLNMRNARHAEDTGPLDERCPCPTCTKYSRAYLHHLHKSGEMLGAMLLTEHNLWFYQQLMAGMRAAIAEGRFAAFAADFRRDYFAR | 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). | Q2G639 |
O82703 | VATG2_TOBAC | Vacuolar proton pump subunit G 2 | Nicotiana | MESNRGSQNGIQLLLGAEQEAQHIVNAARTGKQARMKQAKEEAEKEIAEFRAYMEAEFQRNVEQTSGDSGANVKRLEQETFAKIQHLKTEAESISHDVVQMLLRQVTTVKN | Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. | O82703 |
A7SXK3 | TMED_NEMVE | Transmembrane emp24 domain-containing protein | Nematostella | MASIRLLPSCIVLMFLARSSLCYFITIDAHGEECFHDKVTSGTKMGLIFEVAEGGFLDIDVKIIGPDQKVIYSGERETSGKYTFAAHMDGTYNYCFSNKMSTMTPKVLKFSMDIGEAPKDTSKEDNAGHDKLSEMVSQLSEAMTGVKHEQEYMEVRERIHRSINDNTNSRVVWWSFFESLVLVAMTLGQVYYLKRFFEVRRVV | Could have a role in the budding of coatomer-coated and other species of coated vesicles. | A7SXK3 |
A8FTH8 | TIG_SHESH | PPIase | Shewanella | MQVSVETTQGLERRLTISVPAEQIEKAVTDSLKNEAKRARIPGFRPGKVPVSVINKRYGKAIRQDITGEVMQRNFIEAIIAEKLNPAGAPTFVAGDTDTENFNFVATFEIYPEVELTGLDAITVEQPTSEVTDADVDTMIETLRKQHATFEAVERESVVGDKAKINFVGSIDGEEFEGGKAEDFELELGSGRMIPGFESGVEGHKAGEEFDIEVTFPEDYHAENLKGKVANFVITLNEVLAANLPEVNDEFAKLFGVTDGGLEALKAEIRKNMGRELEQALKANVKEQVLNGLLEQNNIELPKPLIDGEVEVLRKQAMQRFGDQAANMPELPADLFTEQAERRVKVGLLLGEVIKTNELKAEDDRVQSLIASMASAYEDPSEVVAYYNGNEEMLQNMRNVALEEQAVEALLKTAKLTEKAVNFEEFMNKATQQG | 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. | A8FTH8 |
Q6G5K3 | UBIG_BARHE | 3-demethylubiquinone 3-O-methyltransferase | Bartonella | MINETRTTLDQSEVDHFSRIAAEWWNPHGKFRPLHQFNPTRLAYIREKICLELHRDPVSLKPFENLKILDIGCGGGLLCEPMARLGAMVVGADASQTNIEVAKIHAAQNGLSIDYRTTTAEALATEGEQFDIILNMEVVEHVADVNLFIEATAKMLKPQGLMFISTLNRTWKAWGLAIIGAEYILRWLPKGTHNYKKFLKPRELKNLLLQNALTVVDEIGVTYNPLNDSWNRSKDMNVNYLLLAKKS | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q6G5K3 |
Q9DAI4 | ZBT43_MOUSE | Zinc finger protein 297B | Mus | MEPGTNSFQVEFPDFSSTILQKLNQQRQQGQLCDVSIVVQGHIFQAHKAVLAASSPYFCDQVLLKNSRRIVLPDVMNPRVFENILLFSYTGRLVMPAPEIVSYLTAASFLQMWHVVDKCTEVLEGNPTVLCQKLNHGSDHQSPSSSNYNGLVESFELGSGGHTDFPKAQELRDGENEEESTKDELSSQVTEHEYLPSNSSTEHDRLSTEMASQDGEEGTNDSTEFHYTRPLYSKPSIMAHRRWIHVKPERLEQAWDGMDVHAAYDEHQVTESVNTMQTDHSAQPSGAEEEFQIVEKKVEVEFDEQAEGSSYDEQVDFYGSSMEEFSGEKLGGNLIGHKQEAALAAGYSENIEMAMGIKEEASHLGFSATDKLYPCQCGKSFTHKSQRDRHMSMHLGLRPYGCSVCGKKFKMKHHLVGHMKIHTGIKPYECNICAKRFMWRDSFHRHVTSCTKSYEAAKAEQNTTEAN | May be involved in transcriptional regulation. | Q9DAI4 |
P73009 | Y1045_SYNY3 | Probable ABC transporter permease protein slr1045 | unclassified Synechocystis | MSDRGSRHSLSLWFQRLVAAFFLTGQVFLHILQGRINRRNTLEQMNMVGPESMAIALITAGFVGMVFTIQVAREFIYYGATTTIGGVLSLSLTRELAPVLTAVVIAGRVGSAFAAEIGTMRVTEQLDALYMLRTDPIDYLVVPRVIACGLMLPILTGLSLFVGMAGGLVISSSLYAINPTIFLNSVQNFTQLWDVFACLFKSLVFGVIIAIIGCSWGLTTTGGAKGVGESTTTAVVTSLLAIFISNFFLSWLMFQGTGDTALG | Could be part of an ABC transporter complex. | P73009 |
Q47SS3 | ZFPP_THEFY | Z-isoprenyl diphosphate synthase | Thermobifida | MGLLRIPLYRLYERRLERALSNAPKPRHVGVILDGNRRWARLSGLSSPKEGHRAGAEKIFELLDWCDEVGVQVVTLWLLSTDNLARPPEELEPLFEIIENTVRRLCNEGRRVNPMGALDLLPASTAQVMKEAGTTTERNPGLLVNVAVGYGGRREIADAVRSLLLEEAAKGTTLEELAERLDLDDIAKHLYTRGQPDPDLLIRTSGEQRLSGFLLWQSAHSEFYFCEVFWPAFRKIDFLRALRSYSVRQRRFGC | Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Only geranyl diphosphate (GPP) can be used as isoprenyl acceptor. | Q47SS3 |
A4QNE9 | VATG3_XENTR | V-type proton ATPase subunit G 3 | Silurana | MASQSQGIQQLLQAEKRAKDKLEEAKKRKNKRLRQAKEEATADIDQYRLKREGDFRRIQTSVMGSQGNLAVKIEEQTVEKIQLYSSSFHKYKEGVLQQLLDLAYNIKPELHTNFQYKL | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. | A4QNE9 |
A4XQL9 | Y867_PSEMY | Nucleotide-binding protein Pmen_0867 | Pseudomonas | MRLIIVSGRSGSGKSTALDVLEDNGFYCIDNLPAGLLPDLAERALLNTEMLLPQVAVSIDARNLQSHLRRFPELLEQVRQRNIRCDILYLDADDETLLKRFSETRRRHPLTDENRSLAEAIADETQVLAPIVDLADLKIDTTHLNLYQLRDSLKLRLLNQPEPGTAFLFESFGFKRGMPVDADLVFDARCLPNPYWKPELRDFSGLQQPVIDYLAAQPEVEEMYQDILAYLEKWLPRFAASNRAYVTIAIGCTGGHHRSVYLANRLSQALKKPLKNVQVRHRDLS | Displays ATPase and GTPase activities. | A4XQL9 |
Q9WYS1 | UXAE_THEMA | Tagaturonate/fructuronate epimerase | Thermotoga | MVLKVFKDHFGRGYEVYEKSYREKDSLSFFLTKEEEGKILVVAGEKAPEGLSFFKKQRAEGVSFFFCERNHENLEVLRKYFPDLKPVRAGLRASFGTGDRLGITTPAHVRALKDSGLFPIFAQQSVRENERTGRTWRDVLDDATWGVFQEGYSEGFGADADHVKRPEDLVSAAREGFTMFTIDPSDHVRNLSKLTEKERNEKFEEILRKERIDRIYLGKKYSVLGEKIEFDEKNLRDAALVYYDAIAHVDMMYQILKDETPDFDFEVSVDETETPTSPLFHIFVVEELRRRGVEFTNLALRFIGEWEKGIDYKGDLAQFEREIKMHAEIARMFEGYKISLHSGSDKFSVYPAFASATGGLFHVKTAGTSYLEAVKVISMVNPELFREIYRCTLDHFEEDRKSYHISADLSKVPEVEKVKDEDLPGLFEDINVRQLIHVTYGSVLKDASLKERLFKTLEQNEELFYETVAKHIKRHVDLLEG | Catalyzes the epimerization of D-tagaturonate (D-TagA) to D-fructuronate (D-FruA). | Q9WYS1 |
Q2JAL9 | TATA_FRACC | Sec-independent protein translocase protein TatA | Frankia | MGDIGAPELIIIILVVVVLFGSKRLPDAARSLGRSLRIFKSEIKGLHDDEAPAPTAAVAAAPTQVTGPAPAAPHTPPSAEPATPATGGSGNRSA | 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. | Q2JAL9 |
A9WT69 | UVRC_RENSM | Excinuclease ABC subunit C | Renibacterium | MANPASYRPKTGEIPTDPGVYRFRDEHGRVIYVGKAKNLRSRLTSYFANPVTLLPKTFAMVHTATSVQWTIVGSELEALQLEYTWIKEFAPRYNLAFRDDKSYPYLAVTMGEEFPRVQVMRGERRKGTRYFGPFTAGAIRETVDTLLRVFPVRTCSPSTFKRAQQSGRPCLLGYIDKCAVPCVGRVSAEEHRTLADEFCAFMGGEAKRFIGTLEKQMAEAVAELDYERAARLRDDVIALRKVFERNAVVLAEDTSADIFAVHQDELEAAVQVFNVRSGRIRGQRGWVVEKVEDLVPAELIEHLLQQVYGDERADEDRIPRQILVPELPANVEQLTEWLSGLRGAKVEIKVPQRGDKAALMETVALNAEQAMKLHKSKRAGDLTQRSLALRELQDALDLPLPLLRIECYDISHVQGTNVVASMVVVEDGIAKKSEYRRFSITGDAARDDTASMYDVITRRFRNYLQEQQDRAEALTRPVEFEISDAAETAPKSKFAYPPNLVVVDGGPPQVAATSRALADLGITDVAVIGLAKRLEEVWLPEDDFPVILPRTSQGLYLLQRIRDEAHRFAISFHRQKRGKSMTASLLDGVPGLGESKQKALLKHFGSVKKLQSADVSQISEVKGIGPVLAEAVRSALESVDAQPAINMATGEILES | 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. | A9WT69 |
Q8U1B3 | Y1308_PYRFU | Putative antitoxin PF1308 | Pyrococcus | MILKPSKPYSFCFTTYPWKKLKLKEHSKVIIKIIDEEEIEKILDSMIIEKVEGIDYKKLKETHYESL | Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. | Q8U1B3 |
Q3B4A1 | TRMD_CHLL3 | tRNA [GM37] methyltransferase | Pelodictyon | MMDGIRIDVLSVIPGFFDSVLDNGLLAIARKKGYADIVVHNLHDYGLGRYRQVDDSPFGGGAGMVLRPEPVFACVEKLQSERCYDAVIFPTPDARPFLQGDANRLSRMKNLMFLCGHYKALDERVRQSLVTMEYSIGDVVLSGGEIPSLLMMDALLRVVPGVLGDSESALTDSFQTGMLDCAYYTRPPEFRGMKVPEVLLSGHHAKIEQWRQENALERTRRLRPDLLGEDVE | Specifically methylates guanosine-37 in various tRNAs. | Q3B4A1 |
G9N4A5 | VIRH_HYPVG | Virensol biosynthesis cluster protein H | Trichoderma | MVCAWQLWLSPRPKRSVIASGSHIYSNDDAALFEFLKEDDGRWVVRETHYINNPLVKNGLSGPPLHIHWKQAEYFKVEQGVIGIHKNGKQLRVTKDDGVIEVPAGTRHKFWSHPSNQEDLVFKVWAEPQGLDHSFDEKFIRNLIGYQRDCKMANMAPSVFQLMLICYDCATLATPPFWVPLWLLTSIQYVLAYWIGGHLLGYKPSYSEYYREPGDKKTM | Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of virensols and trichoxide, fungal natural products that contain or are derived from a salicylaldehyde core . The pathway begins with the synthesis of the reduced chain in virensol C by the highly reducing polyketide synthase virA via condensation of one acetate and 8 malonate units . VirA has interesting programming rules since the first 2 ketides are fully reduced, the 3 following ketides undergo beta-dehydration, and the last 3 ketides are only reduced to beta-hydroxys to yield the trihydroxy portion . The production of aldehyde virensol C by virA alone is surprising, since virA does not contain a reductase (R) domain that is typically associated with reductive product release in HRPKS . The cupin-domain enzyme virC is involved in enhancing virA product turnover . The short-chain dehydrogenase virB then oxidizes the C-7 alcohol of virensol C to a ketone, yielding virensol D . Virensol D is further transformed to salicylaldehyde 5-deoxyaurocitrin by the short-chain dehydrogenase virD . VirD catalyzes the dehydrogenation of C-3 to form the beta-ketone aldehyde, which is followed by the generation of the nucleophilic C-2 that is required for the intramolecular aldol condensation between C-2 and C-7, itself followed by dehydration and aromatization which leads to salicylaldehyde 5-deoxyaurocitrin . While the dehydrogenation of virensol D is definitely catalyzed by virD, the aldol condensation and dehydration may be uncatalyzed or assisted by virD . The short chain dehydrogenase virG then converts salicylaldehyde 5-deoxyaurocitrin into virensol B which is further hydroxylated by the cytochrome P450 monooxygenase virE to yield the hydroquinone virensol A . VirI then may oxidize virensol A to form the quinone, while virH performs the epoxidation . Finally, the two remaining short-chain dehydrogenases, virK and virL, are probably responsible for reducing the ketones to the corresponding alcohols to furnish the epoxycyclohexanol structure in trichoxide . | G9N4A5 |
Q5LRH8 | TRPD_RUEPO | Anthranilate phosphoribosyltransferase | Ruegeria | MSDALKPLIGAAADRPLTRAEAEQAFTILFDGEATPSQIGGLLMALRTRGETVDEYAAAAAVMRAKCNAVRAPEGAMDIVGTGGDGKNTLNISTATAFVVAGAGVVVAKHGNRNLSSKSGTADLQGQMGINVMVGPQVVEKALNEAGIGFMMAPMHHPATAHVMPTRAELGTRTIFNILGPLTNPAGVKRQLTGAFTRALIRPMAETLGLLGSERAWLVHGSDGTDELTITGVSWVAALEDGTVKEVELHPEDAGLPVHPFEAIIGGTPEENATAFRALLDGAPSAYRDAVLLNAAAALVVADRAADLREGVALAAQSIDSGQARAKVEALSRITQDAR | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q5LRH8 |
Q4VA44 | ZN664_MOUSE | Zinc finger protein 664 | Mus | MIYKCPMCREFFSERADLFMHQKIHTAEKPHKCDKCDKGFFHISELHIHWRDHTGEKVYKCDDCVKDFSTTTKLNRHKKIHTVEKPYKCYECGKAFNWSSHLQIHMRVHTGEKPYVCSECGRGFSNSSNLCMHQRVHTGEKPFKCEECGKAFRHTSSLCMHQRVHTGEKPYKCYECGKAFSQSSSLCIHQRVHTGEKPYRCCGCGKAFSQSSSLCIHQRVHTGEKPFKCDECGKAFSQSTSLCIHQRVHTKERNHLKISVI | May be involved in transcriptional regulation. | Q4VA44 |
B0VL58 | TATA_ACIBS | Sec-independent protein translocase protein TatA | Acinetobacter calcoaceticus/baumannii complex | MAGLSIWHVVIFAIVVILLFGTSKLKNIGKDVGGAVRDFKKSVREEDEAASLNSPRTIDAQAKTSESTSVKS | 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. | B0VL58 |
Q7MKU7 | TTCA_VIBVY | tRNA 2-thiocytidine biosynthesis protein TtcA | Vibrio | MTEQILERTKAQQYNFNKLQKRIRRNTGQAIADFNMIEDGDRIMVCLSGGKDSFTMLDILMSLQKSAPISFSLVAVNLDQKQPGFPAHVLPEYLESLGVEYKIVEEDTYSIVQDKIPEGKTTCSLCSRLRRGILYRTAKELGATKIALGHHRDDILETLFLNMFYGGKMKGMPPKLVSDNGEHVVIRPLAYCREKDIIKYSDMAGYPIIPCNLCGSQPNLQRQNIKQMLNDWDKRFPGRIETMFRAMQNVVPSHLADFELFDFKSINKDSGVINGGDIGFDKEEMPVATVEDEDMVQEFDPSLKLDVTNI | 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. | Q7MKU7 |