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
|
|---|---|---|---|---|---|---|
C1IC52 | VKT2_WALAE | Protease inhibitor 2 | Walterinnesia | MSSGCLLLLLGLLTLWAELTPVSGRPRLCELPAESGLCNAYIPSFYYNPHSHKCQKFMYGGCGGNANNFKTIDECHRTCVG | Snake venom serine protease inhibitor. | C1IC52 |
Q8CCB4 | VPS53_MOUSE | Vacuolar protein sorting-associated protein 53 homolog | Mus | MMEEEELEFVEELEAVLQLTPEVQLAIEQVFPSQDPLDQADFNAVEYINTLFPTEQSLANIDDVVNKIRLKIRRLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVMNVLEHFHKYMGIPQIRQLSERVKAAQTELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANILDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWVKRQLVDYEEKYGRMFPREWCMTERISVEFCHVTRAELSKIMRARAKEIEVKLLLFAIQRTTNFEGFLAKRFSGCTLTDGTLKKLESPPPSTNPFLEDETTPEMEELALEKGELEQPKKPKAPDNPFHGIVSKCFEPHLYVYIESQDKNLSELIDRFVADFKAQGPPKPNTDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTSSSSGGLTISSLLKEKEGSEVARFTLEELCLICSILSTAEYCLATTQQLEEKLKEKVDVSLTERINLTGEMDTFSTVISSSIQLLVQDLDAACDPALIAMSKMPWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCIKFANSFIPKFITHLFKCKPISMVGAEQLLLDTHSLKMVLLDLPSIGSQVVRKAPASYTKIVVKGMTRAEMILKVVMAPHEPLVVFVDNYIKLLTDCNSETFQKILDMKGLKRSEQSSMLELLRQRLPAPPSGTEGSSTLSLIAPTPEQESSRIRKLEKLIKKRL | Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. | Q8CCB4 |
P18292 | THRB_RAT | Thrombin heavy chain | Rattus | MLHVRGLGLPGCLALAALASLVHSQHVFLAPQQALSLLQRVRRANSGFLEELRKGNLERECVEEQCSYEEAFEALESPQDTDVFWAKYTVCDSVRKPRETFMDCLEGRCAMDLGLNYHGNVSVTHTGIECQLWRSRYPHRPDINSTTHPGADLKENFCRNPDSSTSGPWCYTTDPTVRREECSIPVCGQEGRTTVKMTPRSRGSKENLSPPLGECLLERGRLYQGNLAVTTLGSPCLAWDSLPTKTLSKYQNFDPEVKLVQNFCRNPDRDEEGAWCFVAQQPGFEYCSLNYCDEAVGEENHDGDESIAGRTTDAEFHTFFDERTFGLGEADCGLRPLFEKKSLTDKTEKELLDSYIDGRIVEGWDAEKGIAPWQVMLFRKSPQELLCGASLISDRWVLTAAHCILYPPWDKNFTENDLLVRIGKHSRTRYERNVEKISMLEKIYIHPRYNWRENLDRDIALLKLKKPVPFSDYIHPVCLPDKQTVTSLLQAGYKGRVTGWGNLRETWTTNINEIQPSVLQVVNLPIVERPVCKASTRIRITDNMFCAGFKVNDTKRGDACEGDSGGPFVMKSPYNHRWYQMGIVSWGEGCDRNGKYGFYTHVFRLKRWMQKVIDQHR | Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. | P18292 |
O51710 | TSAD_BORBU | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Borreliella | MKVLGIETSCDDCCVAVVENGIHILSNIKLNQTEHKKYYGIVPEIASRLHTEAIMSVCIKALKKANTKISEIDLIAVTSRPGLIGSLIVGLNFAKGLAISLKKPIICIDHILGHLYAPLMHSKIEYPFISLLLSGGHTLIAKQKNFDDVEILGRTLDDACGEAFDKVAKHYDMGFPGGPNIEQISKNGDENTFQFPVTTFKKKENWYDFSYSGLKTACIHQLEKFKSKDNPTTKNNIAASFQKAAFENLITPLKRAIKDTQINKLVIAGGVASNLYLREKIDKLKIQTYYPPLDLCTDNGAMIAGLGFNMYLKYGESPIEIDANSRIENYKNQYRGKNNEKNFSNA | 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. | O51710 |
Q5R0R3 | TPIS_IDILO | Triose-phosphate isomerase | Idiomarina | MPNASLVIANWKMNGNRELTKTMSAALREKLNQLQQVKLVICPPFTLIGELANQCYYDDIAIGAQNVSEHTGGAFTGEISTAQLQEFGVSYVLVGHSERRQLFAETDKMVNEKALATVNAGMTAVICVGENKAQRDEGNTWEVVAQQAQAALADLPKEQAGKIVLAYEPVWAIGTGETASPEQAQDVHAKLRALLVEQFGAIGEKMPLLYGGSVKADNAAELFAQKDIDGGLIGGASLKESDFVAICQAAQG | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q5R0R3 |
A1JKI8 | UNG_YERE8 | Uracil-DNA glycosylase | Yersinia | MPASLTWHDVIGQEKEQPYFKETLAYVAAERNAGKTIYPAQHDVFNAFRLTELDQVKVVILGQDPYHGPNQAHGLSFSVLPGVPAPPSLVNIYKELATDIPGFQRPNHGFLQSWAEQGVLLLNTVLTVEAGNAHSHANLGWETFTDKVIAALNEHRDGVIFMLWGAHAQKKGRIIDTQRHFILKAPHPSPLSAHRGFLGCKHFSQANQLLQQHGQQPIDWQPKLPTAE | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | A1JKI8 |
Q45612 | YYCI_BACSU | Two-component system WalR/WalK regulatory protein YycI | Bacillus | MEWNKTKSIFIVAFLILDIFLGYQFFQKWQATGKEYEVIKNDVEHDMKADHITYEGLNKEATEGYRITANQKSFSKEEIEALKDQKPLMDMPSDDHKVTSLKMKFANPIALSKKDIEDDAQALVSSKIQDGEKYKLWKVDKSKKEIIFFQTYEGHYIYQKTDNPSNMIGQVVLHLNGKNEVVSYDQTTLETFKQIQKESLITEMDAVELLYYQNQLKEYSTVKSCKFGYVAQYPLTSTQVLAPVWRITVEYEKKVNGEKKTVQEYFTVNALESTILDTDQ | Together with YycH, regulates the activity of the two-component system WalR/WalK. | Q45612 |
Q5HYK9 | ZN667_HUMAN | Zinc finger protein 667 | Homo | MPSARGKSKSKAPITFGDLAIYFSQEEWEWLSPIQKDLYEDVMLENYRNLVSLGLSFRRPNVITLLEKGKAPWMVEPVRRRRAPDSGSKCETKKLPPNQCNKSGQSICQKLVSAQQKAPTRKSGCNKNSVLVKPKKGHSGKKPLKCNDCGKTFSRSFSLKLHQNIHTGEKPFECSNCRKAFRQISSILLHQRIHSGKKSHECNKCGESFNQRTTLILHMRIHDGKEILDCGKALSQCQSFNIHQKIHVVGNVCQCRKCGKAFNQMSSLLLHKKIHNGKKTHKYNKCGRGFKKKSVFVVHKRIHAGEKIPENAKALSQSLQQRSHHLENPFKCRKCGKLFNRISPLMLHQRIHTSEKPYKCDKCDKFFRRLSTLILHLRIHNGEKLYRCNKCEKVCNRHSSLIQHQKVHTKKKKLFECKECGKMFSGTANLKIHQNIHSEEKPFKCNKCSKVFGRQSFLIEHQRIHTGEKPYQCEECGKAFSHRISLTRHKRIHTEDRPYECDQCGKAFSQSAHLAQHERIHTGEKPYTCKTCGKAFSQRTSLILHERSHTGEKPYECNECGKAFSSGSDLIRHQRSHSSEKPYECSKCGKAYSRSSSLIRHQNTHSEEKA | May be involved in transcriptional regulation. | Q5HYK9 |
B6J676 | UBIE_COXB1 | Demethylmenaquinone methyltransferase | Coxiella | MNETEKSTHFGYQTVPTDQKTDKVKHVFESVAAKYDLMNDLMSLGIHRWWKDFAITQCRLRTGQRILDLAGGTGDLAKRISPLVGDEGEVVIADINAAMLNVGRRRLLDQGIFRNIQFIQADAEKLPFPNNFFDRIVIGFGLRNVTNQLAALQSMHRVIKPGGFVVILEFSKPTLAPLKAVYDAYSFQLLPRLGKLVAKDEESYRYLVESIRMHPDQEALLSKMTDARFEDCDYHNLSGGIVAVHRGYKF | Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). | B6J676 |
Q1ARU5 | TRET_RUBXD | Trehalose glycosyltransferring synthase | Rubrobacter | MLQRVNPGHKALADYRSIIRRELYGELQELAGRLRGARVLHINATSFGGGVAEILYTLVPLARDAGLEVEWAIMFGAEPFFNVTKRFHNALQGADYELTIEDRAIYEEYNRRTAQALAESGEEWDIVFVHDPQPALVREFSGGLGEGTRWIWRCHIDTSTPNRQVLDYLWPYIADYDAQVYTMREYTPPGVEMPGLTLIPPAIDPLSPKNMALSRDDASYIVSQFGVDVERPFLLQVSRFDPWKDPLGVIDVYRMVKEEVGEVQLVLVGSMAHDDPEGWDYWYKTVNYAGGDPDIFLFSNLTNVGAIEVNAFQSLADVVIQKSIREGFGLVVSEALWKARPVVASRVGGIPMQITAGGGILIDTIPEAAAACAKLLSDPEFAREMGRRGKEHVRANFLTPRLLRDDLRLFAKLLGV | Synthesizes trehalose from ADP-glucose and glucose. The reaction is reversible, the equilibrium strongly favors trehalose synthesis. | Q1ARU5 |
Q0ZZJ6 | VCO31_AUSSU | AVF-1 beta chain | Austrelaps | MEGMALYLVAALLIGFPGSSHGALYTLITPGVLRTDTEEQILVEAHGDSVPKQAVISIHDFPRRQKTLFQTRVDMNPAGGMLVTPTIKIPAKELNKESRQNQYVVVKVSGLPLELEKVVLLSYQSGFVFIQTDKGIYTPGSPVRYRVFSMDYNMHRMDKTVIVEFQTPEGVVVSSNPVNPSSVLIRPYNLPELVSFGTWKAVAKYEHSPEESYTAYFDVREYVLPSFEVRLQPSDKFLYIDGNKNFHVSITARYLYGKKVEGVAFVLFGVKIDDAKKSIPDSLTRIPIIDGDGEAILKRDTLRSRFQNLNELVGHTLYASVTVMTESGSDMVVTEQSGIHIVTSPYQIYFTKTPKYFKPGMPYELTVYVTNPDGSPAANVPVVSEAIRSEGTTLSDGTAKLILNTPLNTQSLPITVRTNHRDLPSERQATKSMTATAYQTQGGSGNYLHVAITSAEIKAGDNLPVNFNVRGNANSLNQIKYFTYLILTKGKIFKVGRQPKGEGQNLVTMNLRITPDLIPAFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGASSRDNRIQKPGAAMKIKLEGDPGARVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGGGQNNLGVFEDAGLALTTSTNLNTKQRSVATCPQPTNRRRRSSVLLLDSKANKAAQFQDQNLRKCCEDGMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGIRDENQRESELFLARSDFEDELFGEDNIISRSDFPESWLWLTEDLKEPPNSQGISSKTLSFYLRDSITTWEVLAVSIAPTKGICVAEPYEITVMKDFFIDLRVPYSVVKNEQVEIRAVLYNYADEDIYVRVELLYNPAFCSASTEGQRYRVQVPVKALSSWAVPFVIVPLEQGLHDVEVKASVRGELASDGVRKKLKVVPEGERKNIVTVIELDPSVKGVDGTQEQTVIANKLDDKVPETEIETKISVLGDPVAQIIENSIDGSKLNHLIITPSGCGEQNMITMTPSVIATYYLDATGQWENLGVDRRTEAVKQIMKGYAQQMVYKKADHSYAAFPNRASSSWLTAYVVKVFAMAAKIVKDIKHEIICGGVKWLILNRQQPDGVFKENAPVIHGEMLGGTKGAEPEVSLTAFILTALLESRSVCNEHINILDSSINKAIDYLLKKYEKLQRPYTTALTAYALAAAERLNDDRVLMAASTGRDRWEEHNARTHNIEGTSYALLALLKMKKFAEAGPVVKWLIDQKYYGGTYGQTQATVMVFQALAEYEIQIPTHKDLNLDISINLPEREVPLRYSINYGNALVARTAETKLNEDFTVSASGDGKATMTILTVYNAQLREDANVCNKFHLDVSVENAQLNSKQAKGAKDTLRLKICTRYLGEVDSTMTIIDVSMLTGFLADAEDLTRLSKGVDRYISKFEIDNNMVQKGTVVIYLDKVSHSEVECLHFKIHKHFEVGFIQPGSVKVYSYYNLDEQCTKFYHPDKGTGLLNKICHGNICRCAEESCSLLNQQKKIDLQLRIQKACAPNVDYVYKTKLLQIEEKDGNDIYVMDVLEVIKGGTDRNPQAKARQYVSQRKCQEALNLKLNNDYLIWGLSSDLWPRKNDISYLITKNTWIERWPNEDECQDEEFQNLCDDFAQLSNTLTIFGCPT | Complement-activating protein in snake venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex AVF/Bb. AVF/Bb is a C3 convertase that cleaves complement component C3, but not C5 (as does CVF/Bb). | Q0ZZJ6 |
Q1H1G1 | TIG_METFK | PPIase | Methylobacillus | MQATVETISNLERRMTVSVPVQPLESEVNERINRLARTVKMPGFRPGKVPLNIVRQQYGAQVRNEVLSNAVERSFSDAVEQNKLRVAGYPHIEHKPYAENDPQIEYVATFEVFPEVNIGDLSKAKIERPVLEVGEAEVKKTIDVLLRQRATFEPVKRASKKGDKINISLIAYIDDQEVERTDENGLDLIIGEGGRFPAFESELSGNKAGSNKVFEIAYPEDHKPEQLAGKTVRYDVTFNTVEQAKLPEFDADFARSLGVEDGDVEKMREEITASLKQEVEKRIRVKLKEQAFQALLDNTALEVPKAFINAEVGRLIQSTQDNLKQRGVDLANVNLEPALFEEQATRNASLRLILSELVNRENLQANAEQVRNMVNVFAQSFERPDDVVTWYYADTKRLDEPAALATEDNVVEWVLKSANVVDKKVKFDDLMGNS | 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. | Q1H1G1 |
Q45105 | TACY_BACCE | Hemolysin | Bacillus cereus group | MKNFKGRKFLTCVLVSLCTLNYSSISFAETQAGHANDITKNASSIDTGIGNLTYNNQEVLAVNGDKVESFVPKESINSNGKFVVVDVRKNHLQRHQSIFRLLDSVANRTYPGAVQLANKAFADNQPSLLVAKRKPLNISIDLPGMRKENTITVQNPTYGNVAGAVDDLVSTWNEKYSATHTLPARMQYTESMVYSKAQIASALNVNAKYLDNSLNIDFNAVANGEKKVMVAAYKQIFYTVSAELPNNPSDLFDNSVTFGELTRKGVSNSAPPVMVSNVAYGRTVYVKLETTSKSKDVQAAFKALLKNNSVETSGQYKDIFEESTFTAVVLGGDAKEHNKVVTKDFNEIRNIIKDNAELSFKNPAYPISYTSTFLKDNATAAVHNNTDYIETTTTEYSSAKMTLDHYGAYVAQFDVSWDGFTFDQNGKEILTHKTWEGSGKDKTAHYSTVIPLPPNSKNIKIVARECTGLAWEWWRTIIKMNKMFH | A cholesterol-dependent toxin with hemolytic activity against host red blood cells. Causes cytolysis by forming pores in cholesterol containing host membranes. binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation. | Q45105 |
B9K815 | VATD_THENN | V-ATPase subunit D | Thermotoga | MSVAPTRGNLIALKQQLRLAIQGYDLLERKRTVIMRELVGLIEEAKKLQEELLSTFEEAYRSLQKANLDLGIESVEEYASGIPEFKAMKIIFSSVMGVEVPEIQIERFETEIPYEIYSTNAALDQAYLVFRKALELVARVAVIENKVYRLAHEAKKTKKRVNALENLIIPHLKETIKYIQDTLEELEREELFRLKRLKEKVAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. | B9K815 |
C6DKC9 | UBIA_PECCP | 4-HB polyprenyltransferase | Pectobacterium | MERSVTAGKWLAYCRLMRIDKPIGSLLLLWPTLWALWLAGGGAPAPWTLFVFVAGVFLMRAAGCVINDYADRHFDGHVKRTASRPLPSGEVSEQSAKVLFVVLVLLAFGLVLTLNTMTIWLSVAGLGLAWVYPFMKRVSHLPQFVLGAAFGWSIPMAYAAVSESLPATCWMMFLAYICWTVAYDTQYAMVDRDDDLKIGVKSTAILFGRFDNLIIGLLQFSMLALLLILGTMTGLGMPYYISLLVAGGMFIYQQILTAGRERDACFKAFHNNKYAGMAIFIGVLFGL | 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. | C6DKC9 |
Q8ZP65 | TPX_SALTY | Thioredoxin-dependent peroxiredoxin | Salmonella | MSQTVHFQGNPVTVANVIPQAGSKAQAFTLVAKDLSDVSLSQYAGKRKVLNIFPSIDTGVCAASVRKFNQLATEVENTVVLCVSADLPFAQSRFCGAEGLSNVITLSTLRNNEFLKNYGVEIVDGPLKGLAARAVIVLDENDNVIFSQLVDEITHEPDYDAALNVLKA | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Q8ZP65 |
A0KQI1 | UPPP_AERHH | Undecaprenyl pyrophosphate phosphatase | Aeromonas | MTESYALFVAFVLGIVEGLTEFLPVSSTGHMIIVGHLLGFDGPKAATFEVVIQMGSILAVVAVFWRRLFGLIGIHFGQKPAQGHATLSLVHIILGMLPAVIIGLAIHSWIKAHLFGPQTVMYALVAGGILLIIAEKFRPAVRSETLDDISYKQALGIGLFQCLALWPGFSRSGATISGGMLMGISRQAAAEFSFILAVPMMVAASGLDLYKSRDLLSMADFPMFAVGFITAFVVAMIAIKTFLALIRRLDFIPFAIYRFVVAFAVYLVFVA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A0KQI1 |
P70902 | VLP15_BORHE | Variable large protein 15/16 | Borrelia | MRKRISAIIMTLFMVLVSCNSGGVAEDPKTVYLTSIANLGKGFLDVFVTFGDMVTGAFGIKADTKKSDIGKYFTDIEKTMTSVKKKLQDEVVKNGNYAKVKTVVAKFIEEVLDKIAAGAKEAAKGATGSDAIGNAVHNQDAVAADATSVNALVKGIGEIVEVVLKDGEGDAGATKTGDTEKKSIGKLFAKKDDDRAQEAEASAANASIGAVSGADILKAIAKSGEIADNNKNIEEAKDAASIAAAKQTDDKKEIKDEAAKKDAVIAAGIALRAMAKGGKFTAKQNEEKSANAVNGAAASAVGKTLSTLIIAIRNTVDSGLKTINEALATVKQEDKSVEATNTAEATTSGQQAKN | 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. | P70902 |
A6LMR9 | Y1373_THEM4 | Nucleotide-binding protein Tmel_1373 | Thermosipho | MLKNLVVLTGLSGAGKSTALGLLEDMGFYCIDNLPVKIIDQILPIISINIESLALVIDSRSGDIDDIVSVIENMKAKYPVKVIFLNAKDEVLINRFAHTRRNHPLLKEETSLEKAILEERKLFIKILELSDIVVDTSNLNPHQLRERLVGILTSVKKKFRLRILSFGFKYGVPLDVDFIFDVRFFPNPFYVVGLRQKSGKDKEVKNFLYNTQGVKEFLDLIKKVVDFAIQRYENEGRTELSVGIGCTGGQHRSVFFAEELFKFYNENCKVILEHRDVK | Displays ATPase and GTPase activities. | A6LMR9 |
A4GE69 | XMT1_COFCA | Xanthosine methyltransferase 1 | Coffea | MELQEVLRMNGGEGDTSYAKNSAYNQLVLAKVKPVLEQCVRELLRANLPNINKCIKVADLGCASGPNTLLTVRDIVQSIDKVGQEKKNELERPTIQIFLNDLFPNDFNSVFKLLPSFYRKLEKENGRKIGSCLIGAMPGSFYSRLFPEESMHFLHSCYCLQWLSQVPSGLVTESGISTNKGSIYSSKASRLPVQKAYLDQFTKDFTTFLRIHSEELFSHGRMLLTCICKGVELDARNAIDLLEMAINDLVVEGHLEEEKLDSFNLPVYIPSAEEVKCIVEEEGSFEILYLETFKVLYDAGFSIDDEHIKAEYVASSVRAVYEPILASHFGEAIIPDIFHRFAKHAAKVLPLGKGFYNNLIISLAKKPEKSDV | Involved in the biosynthesis of caffeine . Specific for xanthosine . Cannot use xanthosine 5'-monophosphate (XMP) as substrate . Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled . Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N-methylation activity . | A4GE69 |
P55726 | Y4YR_SINFN | Probable translocation protein y4yR | Sinorhizobium | MANALRRFTEYAPANPDLMVALMLLLAVSMMVMPIPVMAVDALIGFNMGLAVLLLMAALYVSTPLDFSSLPGVILLSTVFRLALTVATTRLILAEGEAGSIIHTFGSFVISGNIVVGFVIFLVVTMVQFMVLAKGAERVAEVAARFTLDALPGKQMAIDAELRNGHIDADESRRRRAALEKESKLYGAMDGAMKFVKGDSIAGLVVICINMLGGISIGLLSKGMSFAQVLHHYTLLTIGDALISQIPALLLSITAATMVTRVTGASKLNLGEDIANQLTASTRALRLAACVLVAMGFVPGFPLPVFFMLAAVFAAASFVKGDVLDADKVDATTVTPAESQTPNVAAQPNPIGVFLAPSLTNAIDQVELRQHIARISQLVSADLGIIVPPIPVDVDQQLPESQFRIDVEGVPVEQDLINPAQLSLADDLKKIESSGIPFRHDPETHRIWVEQSHEPALKAAGIRHHSPSELLAMRVHATLTCHAPRLVGIQETRQLLGRMEQEYSDLVKEVLRTTPIPRIADVLRRLLGEGIPIRNTRLVLEALAEWSEREQNVALLTEHVRSGMKRQICHRYGRHGVLPAFVMERETEDVVRCAVRETAAGPYLALEDRQSEALLSQMRQVFSSTAPGQTRPIVLTSMDVRRFVRGFLTRNGIELAVLSYQDLASDFKIQPVGSIRLPPSNGTSGEPRSIRPSATTG | Could be involved in the secretion of an unknown factor. | P55726 |
Q5TM18 | VATG2_MACMU | Vacuolar proton pump subunit G 2 | Macaca | MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCDVRPQVHPNYRISA | 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. | Q5TM18 |
Q828H7 | TATA_STRAW | Sec-independent protein translocase protein TatA | Streptomyces | MFGRLGAPEIILILVVIILLFGAKKLPDMARSLGKSARILKSEAKAMKSEGQESTPAGPPNTDEQPPAQRTIQAAPGDVTSSRPVSEPTDTTKR | 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. | Q828H7 |
P14726 | UFOG_HORVU | UDP-glucose flavonoid 3-O-glucosyltransferase | Hordeum | MAPPPPHIAVVAFPFSSHAAVLFSFARALAAAAPAGTSLSFLTTADNAAQLRKAGALPGNLRFVEVPDGVPPGETSCLSPPRRMDLFMAAAEAGGVRVGLEAACASAGGARVSCVVGDAFVWTADAASAAGAPWVAVWTAASCALLAHLRTDALRRDVGDQAASRADELLVAHAGLGGYRVRDLPDGVVSGDFNYVISLLVHRQAQRLPKAATAVALNTFPGLDPPDLIAALAAELPNCLPLGPYHLLPGAEPTADTNEAPADPHGCLAWLDRRPARSVAYVSFGTNATARPDELQELAAGLEASGAPFLWSLRGVVAAAPRGFLERAPGLVVPWAPQVGVLRHAAVGAFVTHAGWASVMEGVSSGVPMACRPFFGDQTMNARSVASVWGFGTAFDGPMTRGAVANAVATLLRGEDGERMRAKAQELQAMVGKAFEPDGGCRKNFDEFVEIVCRV | In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. | P14726 |
A8AED8 | YEGS_CITK8 | Probable lipid kinase YegS-like | Citrobacter | MATFPASLLILNGKGADNQPLRDAIGLLRDEGVEIHVRVTWEKGDAQRYVDEARQLGVETVIAGGGDGTINEVSAALIQCQGGNVPALGILPLGTANDFATSAGIPEALDKALKLAIAGNAVAIDIAQVNDKTCFINMATGGFGTRITTETPEKLKAALGGVSYFIHGLMRMDTLKPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPGALINDGLLQLRIFTGEELLPALFSTLTQPEENPNIVDGASAWFDIQAPHEITFNLDGEPLSGQEFHIEILPNALRCRLPPDCPLLR | Probably phosphorylates lipids; the in vivo substrate is unknown. | A8AED8 |
Q6ZJK7 | TDC1_ORYSJ | 5-hydroxytryptophan decarboxylase TDC1 | Oryza sativa | MGSLDTNPTAFSAFPAGEGETFQPLNADDVRSYLHKAVDFISDYYKSVESMPVLPNVKPGYLQDELRASPPTYSAPFDVTMKELRSSVVPGMTHWASPNFFAFFPSTNSAAAIAGDLIASAMNTVGFTWQASPAATEMEVLALDWLAQMLNLPTSFMNRTGEGRGTGGGVILGTTSEAMLVTLVAARDAALRRSGSDGVAGLHRLAVYAADQTHSTFFKACRLAGFDPANIRSIPTGAETDYGLDPARLLEAMQADADAGLVPTYVCATVGTTSSNAVDPVGAVADVAARFAAWVHVDAAYAGSACICPEFRHHLDGVERVDSISMSPHKWLMTCLDCTCLYVRDTHRLTGSLETNPEYLKNHASDSGEVTDLKDMQVGVGRRFRGLKLWMVMRTYGVAKLQEHIRSDVAMAKVFEDLVRGDDRFEVVVPRNFALVCFRIRAGAGAAAATEEDADEANRELMERLNKTGKAYVAHTVVGGRFVLRFAVGSSLQEEHHVRSAWELIKKTTTEMMN | Involved in serotonin biosynthesis . Catalyzes the decarboxylation of L-tryptophan to produce tryptamine, which is converted to serotonin by tryptamine 5-hydroxylase . May play a major role in serotonin biosynthesis during senescence . Accumulation of serotonin attenuates leaf senescence . Catalyzes the decarboxylation of 5-hydroxy-L-tryptophan to produce serotonin . | Q6ZJK7 |
Q927X9 | Y2658_LISIN | DegV domain-containing protein lin2658 | Listeria | MNEKIAVVTDSTTYLPDEVKEQLRINVVPLSVIIDGKSYREGEELSTADFYKKVKEAENFPTSSQPAPGEFIQLFEKLKEQGFDTVISIHLSSGISGTFQNAASAGELIDGLNVVAYDSELSCMAQGMFAVKAAEMALANEPLERIISELDKIKKAQDAYFMVDDLNNLQRGGRLNGAQALVGSLLQIKPILHFNDKQIVLFEKVRTQKKALKRIEDILEVAIKNKNAEKAYVIHGNDPEKGETWRKHLESKFPEVEFELSYFGPVIGTHLGEGALGLTWSIK | May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | Q927X9 |
J9R5V4 | TPS2_VALOF | Terpene synthase 2 | Valeriana | MESCLSFSSPPPTKKNIQEPVRPNAKFHKSVWGNHFLKYASNPEQIDYDADEQHEQLKEELRKKLVVNVTNERVEEQLKLIDAIQRLGVAYHFQREIDAVLNNLLLFRSNKDSDDIYMVSLRFRLLRQQGHNVSCSVFEKFKNIDGRFKDSLRDDVRGLLSLYEATHMRVHKEDILEEALEFTIYELEQVVKLSSNDTLLASEVIHALNMPIRKGLTRIEARHFISVYQHDKSHDETLLKFSKIDFNMLQKLHQRELADLTIWWEKLNVAEKMPYARDRFVECYFWGLGVYFEPQYSRARKMFVKVINLTSLIDDTYDSYGTFDELDLFTDAVKRWNVNETDKLPEYMRPLFMELLNVYNAMEEELKEEGVSYRVEYAKQSMIQIVTAYNDEAIWYHNGYVPTFDEYLKVALISCGYMLLSTISFVGMGVTTVTKPAFDWVTNNPLILIASCTINRLADDKVGHELEQERGHVASGVECYMKHNNATKQEVVIEFNKRISNAWKDINQECLHPLPVPLHLVVRPLYLACFMNVFYKDEDWYTHSNTQMKECINSLLVESVPY | Catalyzes formation of valerena-4,7(11)-diene, one of the active ingredients responsible for the sedative effect extracted from Valeriana officinalis root. | J9R5V4 |
B1W3X8 | TRUA_STRGG | tRNA-uridine isomerase I | Streptomyces | MSDQAEPGFVRVRLDLSYDGKDFSGWAKQTSRRTVQGEIEDALRTVTRSSVTYDLTVAGRTDAGVHARGQVAHVDLPEAVWAEHEEKLLRRLAGRLPLDVRIWRAAPAPAGFNARFSALWRRYAYRVGDRPGGVDPLTRGHVLWHDRPLDLDAMNEAAALMVGEHDFAAYCKKREGATTIRTLQKLRWVRDPATGVLTATVQADAFCHNMVRALIGAALFVGDGRRPAAWPAEVLAAKVRDPGVHVVRPHGLTLEEVAYPADALLAARAAEARNVRTLPGAGCC | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | B1W3X8 |
P39077 | TCPG_YEAST | CCT-gamma | Saccharomyces | MQAPVVFMNASQERTTGRQAQISNITAAKAVADVIRTCLGPKAMLKMLLDPMGGLVLTNDGHAILREIDVAHPAAKSMLELSRTQDEEVGDGTTTVIILAGEILAQCAPYLIEKNIHPVIIIQALKKALTDALEVIKQVSKPVDVENDAAMKKLIQASIGTKYVIHWSEKMCELALDAVKTVRKDLGQTVEGEPNFEIDIKRYVRVEKIPGGDVLDSRVLKGVLLNKDVVHPKMSRHIENPRVVLLDCPLEYKKGESQTNIEIEKEEDWNRILQIEEEQVQLMCEQILAVRPTLVITEKGVSDLAQHYLLKGGCSVLRRVKKSDNNRIARVTGATIVNRVEDLKESDVGTNCGLFKVEMIGDEYFSFLDNCKEPKACTIMLRGGSKDILNEIDRNLQDAMAVARNVMLSPSLSPGGGATEMAVSVKLAEKAKQLEGIQQWPYQAVADAMECIPRTLIQNAGGDPIRLLSQLRAKHAQGNFTTGIDGDKGKIVDMVSYGIWEPEVIKQQSVKTAIESACLLLRVDDIVSGVRKQE | Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. | P39077 |
Q85FL9 | YCF3_ADICA | Photosystem I assembly protein Ycf3 | Adiantum | MPRSQRNDNFIDKTFTILADILIRILPTTKREREAFIYYRDGMSAQSEGEYAEALGSYYKAMRLEIDSYDRSYILYNIGLIHTSNGNHAKALEYYFQALERNSFLPQAFNNMAVICHYRGEQAIYQGDLEISEAWFDQAAEYWRRAIALSPDNYAEAQNWLKITGRFSPSHRWESWNNSTRVA | Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits. | Q85FL9 |
O59258 | UPPS_PYRHO | Undecaprenyl pyrophosphate synthase | Pyrococcus | MIYRIISHIPKIFFKPAYDLYERYLIEKVKSGVLPKHVAIIMDGNRRWARKHEKPPWYGHLFGSKKLEEILEWCHELGIRILTVYAFSTENFKRSKEEVDRLMKLFEEKFRELVTDKRVHEYGVRVNVIGRKELLPKSVRDAVEEAERATRKYNNYILNVALAYGGRSEIVDAVKDIARDVISGKLRIEEIDEELLRRYLYVPNMPDPDIVIRTGGEVRISNFLLYQIAYSELFFVDVYFPEFRKIDFLRIIREFQKRERRFGR | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids. | O59258 |
P18733 | ZG66_XENLA | Gastrula zinc finger protein XlCGF66.1 | Xenopus | MGMWEEASDTGMKGKKKKKDKNEEEEERGKKERMVNLTLEMIYLLTGEHYIPRKKSDDGGALHAPGSVIQKENNKNDKKILELMSNIIQLLTGEVAIRTHHVSIYFSLDEWDYIKGNKDLYEDGMKEEPQQLHPLAVCEYKDESNVTAHMESTLGCNNDGNLTKMSPVEQPPPANGIKEEVASCEEINQSDCSINPFTEQIQGTDTPTPIMGCSHFKTKVNKYDINSYWSPDESGITKSTLHSKDSCNEGHKHLSHKSDYNKHQNPHKRQKSFSCSKCGKCFSNLTSLHCHQKTHKGKKLLCLKCGKCFATSSKLIIHRQTHMDKKHFSCSECRICFSKQSSLARHQITHTEEKPLASSECGKCFASLSELTVHQRTNTGEKHDFCSECGKCFATSSQLIAHQQQVHIEVKPFSCTKCGKCFSYRSRLVRHQRTHTGVKPYSCSECGKCFASSSHLIGHRQQVHMEGKTFFCSECGKYFLYQSQLVRHQRTHTGEKPYSCSECGKCFATSSQLMAHQQQVHIEVKPFSCSECGKYFLYRAHLVRHQRTHTGEKPDFCFECGKCFATSLQLIAHQQQVHMEVKQFSCSECGKSFLYRSHLARHHRTH | May be involved in transcriptional regulation. | P18733 |
A0A0B4J184 | T3A_TERVA | Teretoxin v3a | Terebra | TRICCGCYWNGSKDVCSQSCC | Injections of 20 uM of this synthetic peptide (Ile) causes partial paralysis to polychaete worms (Nereis virens), the natural prey of terebrid snails . This paralysis may be due to an inhibition of nicotinic receptors at the neuromuscular junction (Probable). | A0A0B4J184 |
Q8UJ08 | TYPH_AGRFC | TdRPase | Agrobacterium tumefaciens complex | MSLIPQEIIRRKRDGLSLAPQEIAAFIEALSKDGISEGQAAAFAMAVFFRGMNRDEMVALTLAMRDSGDVLSWRDIGRPVADKHSTGGVGDNVSLMLAPIVAACGLAVPMISGRGLGHTGGTLDKLEAIPGYDVMPDEALFRRTVQSVGCAIIGQTGDLAPADKRLYAIRDVTATVDSIPLITASILSKKLAAGLETLVLDVKVGNGAFMQSLEDARILARALVDVANGAGLPTTALITDMNQPLCDAAGNAVEIVNCLEFLAGGKAGTRLEKVVLSFAAEMLVQARKAATLEEGEALASAALSSGRAMEIFARMVSVLGGPSDFIENPSRYLACAPIILPVPAARSGWLASCATRDLGMVVVELGGGRTKPSDTINPAVGISDILPLGVRVEKGEPIAVVHAASSEDAERAVKRIEDCFGIADNAPEIAASVLERIT | 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. | Q8UJ08 |
Q5NZR9 | TRUB_AROAE | tRNA-uridine isomerase | Aromatoleum | MKASKQFRHQRRIVDGVLLLDKPRGLTSNAALQTARRLLNAAKAGHTGTLDPMATGLLPLTLGEATKFSQMLLDADKAYEATVRLGIETDTGDAEGAAIATAPVHVTDDSIRQALAALTGEIEQVPPMYSALKRDGKPLYEYARAGIEVERAARPVTIHSLELLGVEGDSLRIRVDCSKGTYVRTLAIDLGRLLGCGGHLTELRRTRIGPFNVDEAVTLTALEALPAESRVGLLAPVDALVGHLPRIELDAFQAGLLLQGRVLAAPCGAAGLVRIYGEGRYLGLGECDGNGTLSPKRLVSTVATAQQS | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q5NZR9 |
A8QL56 | VSP1_OPHHA | Snake venom serine protease | Ophiophagus | MALIRVLASLLILQLSYAVTPFDRIIGGFECNEYEHRSLVHLYNSSGFFCSGTLLNHEWVLTAAHCNRDDIQIKLGVHNVSVNYEDEQIRVPKEKLCCHSTNNCTQLGQDIMLIRLNSSVNYSEHIAPLSLPSNRPSMGSVCRVMGWGLLTSPEVTFPKVPHCVDINILHIQVCQAAYPSMSENYLLCAGVLEGGKDSCKGDSGGPLICNREIQGIVSWGGFPCAQLLEPGVYTKVFDYIDWIEGIIAGNTSVTCPSDNF | Snake venom serine protease that possesses potent fibrinogenolytic (on both alpha- (FGA) and beta-chains (FGB)) and amidolytic activities. Selectively cleaves Arg-|-Xaa or Lys-|-Xaa bonds. | A8QL56 |
A5UZW4 | TPIS_ROSS1 | Triose-phosphate isomerase | Roseiflexus | MRTPLLAGNWKMYKTTGEARELVEGLLHGLGDVSDRKVLVCPPFTALHTVRDLVQGTPIALGAQDVYIEPQGAFTGAISPVMLRDLGCTYVIVGHSERRAIFGEGDELIGKKVRAALAHDLTPILCVGETKPQRDAGEAETIVVAQVRAALAGMTPDQIARIVIAYEPVWAIGTGDTATPADAQAMHVTIRQTLGELAGSDVADAINILYGGSVKPDNIDDLMAQPDIDGALVGGASLKADSFLRIVHFLPIQG | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A5UZW4 |
Q9LU01 | Y3IP1_ARATH | Protein CHLOROPLAST ENHANCING STRESS TOLERANCE | Arabidopsis | MTTQIFQLPLKYCASSFSSTGQRNYGASSSPSPIVICKSNGISDGLWVKRRKNNRRFGSLIVKQEKGDVTEIRVPVPLTLEQQEKEKQNRDDEEDEIDEGDVDPEDLKYVNEIKRVIELLRRNRDMIFSEVKLTIMIEDPRELERRRLLGIEDADTPSRDDLAEALEQVNDGKIPKDRATLRMLHEEMIRWPNLEVEVSKKQRGKSMYAKSTDTGIDPKEAAKRLNVEWDSAAAIEEVDVDDEQGVVTKVAGYGALYFVSALPVIIGISVVLILFYNSLQ | Nuclear genome-encoded factor that participates in photosystem I (PSI) biogenesis. Cooperates with the plastid genome-encoded protein PSI assembly Ycf3 in the assembly of stable PSI units in the thylakoid membrane . Involved in light-induced chloroplast development and growth. Involved in the plant response to abiotic and photooxidative stresses. May be involved in the suppression of photooxidative damage . | Q9LU01 |
Q02YX4 | TRHO_LACLS | tRNA hydroxylation protein O | Lactococcus cremoris subsp. cremoris | MTQDYRVLLYYQYVPIEDGESFAQKHLSDCKALGLKGRILVADEGINGTVSGTVEQTNAYMSLMKNDSRFTSTIFKIDEAKQNAFKKMHVRYRPELVNLSLEDDVNPLELTGAYLDPKEFREAMLDENTVVIDARNDYEFDLGHFRGAIRPEIRSFRELPQWIRDNKEQFMEKRVLTYCTGGIRCEKFSGWLVREGFKDVGQLHGGIATYGKDPEVQGDLWYGQMYVFDSRIAVPINQKEHVIVGRDWFDGSPCERYINCGNPECNRQMLASKENEAKYLGACSHECRVHPDNRYIKAHQLSNQEVQERLALLEKDLAS | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q02YX4 |
C5D5R1 | ZAPA_GEOSW | Z ring-associated protein ZapA | unclassified Geobacillus | MAEQQKTRVTVDIYGQQYTIVGTESSSHIRLVASIVDDKMREISEKNPTLDISKLAVLTAINIVHDYIKLKEEYDRLLQKLHKEKDE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. | C5D5R1 |
P87129 | VPS53_SCHPO | GARP complex subunit vps53 | Schizosaccharomyces | MSNGNDNSLIIKNIGNNEFKFVETLHELLPEDITYDDLGSLRLSLSERLQESVKKLDANKKTYEDAKLSMGEKMDDLNSSIVSLLQELSTLQSVAENTQSSIVQMTSEIKNLDFAKQNLATSMTMLKRLQMLVTAYEKLRTLRQNQKFGEAISLMQATLQLLNFFKKYRSVERIASLSRSISEFQKSFYEQVFDTFQSQFKKESGMRGGFSPSSVQYLNELCRFIDIFAGDPPESVIRWYCRHQLEDFMKVFRENEEAGSLENLPRRYTWFKKLLQTYDQLHKPIFPPHWKVDFRLYEVFCEETKNDLSKLLKDDRLSLQVFVASLEQTLEFESFIDHRFYNTKSRFNSNFEPKERQAYNALSSVFEPHYTLYFNQQSQEFSILFENFALEKQTSTDESSQVLSSSIKLFQAYRKTLTQFVRLTRSSPLVGLKNLFIKWLRRYTQVELLDYQESSTFKDIAIRLNTAEYIYRTTIELEKRFQEISNKEFKDKMSFSEVLEVISSSRGTLLKFATGKFENVLNSDLEPLSKMDLKNIETVGDQSSYVGGAVQNMTAKASEFLSVVDLNMFARNFCDRSCESFTRQFLNAIYLAKPISEVGAEQLLLDLYSFKNALLKLPDLKQDYSITDSYINHLTIFMGYIETVLKTLLTPASPKAGFIQSYIFLVKDRSVTNFTVLLELKGVGKSDISSFLQQFSDFVKKTPQLEESSPIFKYLTINTAVEQAATRSRLSLDLAPESSRTLQNLGRLFTSKKKHV | Involved in retrograde transport from early and late endosomes to late Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. | P87129 |
P58843 | U6AA_CONQU | Conotoxin QcVIA | Lividoconus | DQSCPWCGFTCCLPNYCQGLTCTVI | Causes scratching and restlessness in mice. | P58843 |
Q5PD68 | UPPS_SALPA | Undecaprenyl pyrophosphate synthase | Salmonella | MLSATQPVSENLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIDALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDISRFNSRLQERIRKSEALTAHNTGLTLNIAANYGGRWDIVQGVRQLAEQVQAGVLRPDQIDEERLGQQICMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALHAFANRERRFGGTEPGDDKA | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. | Q5PD68 |
P02557 | TBB_YEAST | Beta-tubulin | Saccharomyces | MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE | 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. | P02557 |
A6H7F7 | TPC2L_BOVIN | Trafficking protein particle complex subunit 2-like protein | Bos | MAVCVAVIAKENYPLYIRSIPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDGMVTSMMIQVC | May play a role in vesicular transport from endoplasmic reticulum to Golgi. | A6H7F7 |
Q06442 | WNT5A_AMBME | Protein Wnt-5a | Ambystoma | MATTHLTAALALLCALLQVDIEASSWWSLAMNPVQIPEAYIVGAQPLCSQLPGLSPGQKKLCQLYQDHMPYIGEGAKTGIKECQYQFRHRRWNCSTVDNASVFGRVMQIGSRETAFTYSISAAGVVNAVSRACREGELSTCGCSRAARPKDLQRDWLWGGCGDNLEYGYRFAKEFVDAREREKIHTKGSYESSRTLMNIHNNEAGRRTVYNLADAACKCHGVSGSCSLKTCWLQLADFRKVGDFLKEKYDSAASMRLNARGKLVQVNSRFNPPTTNDLVYVDTSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK | Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Required during embryogenesis for extension of the primary anterior-posterior axis. | Q06442 |
B5FEZ9 | TORD_ALIFM | Chaperone protein TorD | Aliivibrio | MNELTAFNEQRAEIYWWLSSLLSAELTTEQLEQYGSFEVRTFLSNLAETPELSDSVNALIEKLNAVQGREDAQLELSADFCDAFLGSDKSSALPYASMYLDKSGLLNAKPAQDMREWLTKYNIAQKAEFNEPADHIAIELDFLGNLIVMTNQQASEDEFEAYMNAQLTFINEQLLSWTPRFNEICIERDKFGFYAAVTGLLVTFLKLDVKFLAGE | 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. | B5FEZ9 |
Q15ZT9 | UBIA_PSEA6 | 4-HB polyprenyltransferase | Pseudoalteromonas | MSRSVLQGFWLLMRADKPVGSYLLLWPTLWALMIAAQGLPPWHITGIFMAGVFVMRSAGCVINDYADRKVDGKVDRTKARPLVSGVVTEKQALGLFATLVGVAFLLVLALNWQTIVLSLGALALASVYPFMKRYTHFPQVVLGAAFGWAIPMAFMAVTEAVPAIAWWLFAINVLWTVAYDTQYAMVDRNDDLQIGVKSTAVLFGQYDRLIIGLLQLSVVVMLLGMGQYLGFTLSFYVGVLLASVLFIHQQRLISGRARQACFSAFLNNNYVGMAIALGIAGHYFM | 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. | Q15ZT9 |
A7HVX4 | TYSY_PARL1 | Thymidylate synthase | Parvibaculum | MQQYLDLMRLARDTGVTKTDRTGTGTRSIFGHQMRFDLSEGFPLVTTKKLHLKSIIHELLWFIAGDTNTRYLKANGVSIWDDWADENGELGPVYGHQWRSWPTPDGGKIDQIRNLVEQIKTNPDSRRLIVSAWNVADVDSMALPPCHCLFQFYVAEGKLSCQLYQRSADIFLGVPFNIASYALLTMMVAQVTGLKPGEFIHTFGDAHLYLNHLEQADKQLAREPKKLPVMHINPDVKSLFDFTYDDFTLEGYEAHPHISAPVAV | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | A7HVX4 |
Q9FIS2 | ZIP12_ARATH | ZRT/IRT-like protein 12 | Arabidopsis | MSRFRKTLVSAFVLCLVIFPLLVSAAEEENQCGGSKGGSAAEKASALKYKIIAFFSILIAGVFGVCLPIFGLKTESNFFMYVKAFAAGVILATGFVHILPDATESLTSSCLGEEPPWGDFPMTGLVAMAASILTMLIESFASGYLNRSRLAKEGKTLPVSTGGEEEHAHTGSAHTHASQGHSHGSLLIPQDDDHIDMRKKIVTQILELGIVVHSVIIGISLGASPSVSTIKPLIAAITFHQLFEGFGLGGCISEAKFRVKKIWVMLMFFALTAPIGIGIGIGVAEIYNENSPMALKVSGFLNATASGILIYMALVDLVAPLFMNQKTQSSMKIQVACSVSLVVGAGLMSLLAIWA | Zinc transporter involved in zinc uptake in roots. Targeted by BZIP23 transcription factor in response to zinc-deficient conditions. | Q9FIS2 |
Q59182 | TPIS_BORBU | Triose-phosphate isomerase | Borreliella | MRKTFLAGNWKMHYTSAEASIVAKKIATEVKTLKDDVVIMITPPFTALSKVSECIKGSNILLGAQNMSYMESGARTSEISPSMLLEFGVEYVILGHSECRLYLAETDEIINKKILAGLKHPFKYLILCVGETLDERDSGKTLEVVLNQVKKGLNCVSESDIQRIILAYEPVWAIGTGKTATKEEAEEVHKAIRLEITKLYSKSASDNIIIQYGGSVNSNNVKELMNEPNIDGALIGGASLKAESFLSIINNVL | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q59182 |
A0KPE3 | TYPH_AERHH | TdRPase | Aeromonas | MFLPQEIIRKKRNGEALSTQEIQFFVQGITNNTIGEGQIAALAMAVYFKDMTMDERVALTCAMRDSGMVLTWDHLNLGGPIVDKHSTGGVGDVVSLMLGPMVAACGGFVPMISGRGLGHTGGTLDKLDAIPGYQTSVDNDRFLKVVKEAGVAIIGQTGDLAPADKRIYAVRDITATVESIAMITGSILSKKLASGLEALVMDVKVGSGAFMPTFEASEELAKSIVAVANGAGCRTSALLTDMNQVLASSAGNAVEVREAVRYLTGEYRNPRIHAVTMALCAEMLISAGLASDDGEARRKLQAVLDNGKAAEIFGRMVTGLGGPSDFMERYDHHLPKAAIVRPVYAANSGFVTAMDTRELGLAVVAMGGGRRAAGDKLDYAVGLTDFIRLGQSVEADKPLALIHAQTEEQFAQAASMVQAAVKIGDTRPEALPEVYRRIGLADL | 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. | A0KPE3 |
Q57HL1 | YIHI_SALCH | Der GTPase-activating protein YihI | Salmonella | MKKPTSAPRSKAFGKQRRKTREELNQEARDRKRLKKHRGHAPGSRAAGGNSASGGGNQNQQKDPRIGSKTPVPLGVTEKVTQQHKPKSEKPMLSPQAELDLLETDERLDALLERLEAGETLSAEDQAWVDAKLDRIDELMQKLGLSYDDDDEDDEEDEKQEDMMRLLRGGN | A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis. | Q57HL1 |
Q3SZ13 | UQCC2_BOVIN | Mitochondrial protein M19 | Bos | MAASRYRRFLKLCEEWPVDETKRGRDLGAYLRQRVAQAFREGENTQVAEPEACDEMYESLARLHSNYYKHKYPRPRETSFSGLSLEEYKLILSTDTLDEFKEMNKGTWKKLQEKFAPGSPEGKHTAWARALPRPRT | Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability. | Q3SZ13 |
B7NCD4 | THIM_ECOLU | 4-methyl-5-beta-hydroxyethylthiazole kinase | Escherichia | MQVDLLSSAQSAHALHLFHQHSPLVHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAIASALLINVGTLTQPRAQAMRAAVEQAKRSQTPWTLDPVAVGALDYRRCFCLELLSHKPTAIRGNASEIMALAGIANGGRGVDTTDAAANAIPAAQTLARETGAIVVVTGEVDYVTDGHRIIGIHGGDPLMTKVVGTGCALSAVVAACCALPGDMLENVASACHWMKQAGERAVARSEGPGSFVPHFLDALWQLTPEVQA | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | B7NCD4 |
P53377 | TBG_NEUCR | Gamma-tubulin | Neurospora | MPREIITIQAGQCGNSIGSQFWQQLCLEHGISQDGTIEDFATEGGDRKDVFFYQSDDTRYIPRSILIDLEPRVINTIQTGPYRNIYNPENFYVGKSGLGAGNNWGDGYQTGEQVHEEIMEMIEREADGSDSLEGFMMLHSIAGGTGSGLGSFLLERLNDRFPKKIIQTYSVFPDTTSAGDVVVHPYNSLLAMRRLTQNADSVVVLDNGALSHIAADRLHVQEPSFQQTNQLVSTVMSASTTTLRYPGYMHNDLVSILASLIPTPRCHFLMTSYTPFTGDQVEQAKTVRKTTVLDVMRRLLQPKNRMVSTVPGKKSCYISILNVIQGDVDPTDVHKSLLRIRERRLATFIPWGPASIQVALTKRSPYVTMAHRVSGLMLANHTSIATLFKRIVRQYDGMRKRNAFMEAYKKTAPFSENLNEFDEAREVVMDLIADYEAAEDANYLNPELGENASADTDKRMA | Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. | P53377 |
Q1I7G7 | TAL_PSEE4 | Transaldolase | Pseudomonas | MTSKLEQLKQFTTVVADTGDLDAITRLKPVDATTNPSLLLKAAAIPGYADLLEQVKADTKGNVDLACDKFAVSVGAGILKVIPGRISTEVDARLSFDEPALLKKAHQLIELYEAAGIKRDRVLIKLASTWEGIRAAEKLEKEGIQTNLTLLFSFAQAQACADAGVFLISPFVGRIYDWYKKSTGKEYIGAEDPGVQSVTRIYDYYKANGYNTVVMGASFRNIGQIEQLAGCDRLTISPELLVQLSDDQGELPRILKPGNAGEAKQQLNESQFRWAMNEDAMATEKLAEGIRQFARDQEKLEALMADKA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q1I7G7 |
Q82DM1 | TRUA_STRAW | tRNA-uridine isomerase I | Streptomyces | MSDEVQPGFVRVRLDLSYDGTEFSGWAKQAAGRRTVQGEIEDALRTVTRSGETTYELTVAGRTDAGVHARGQVAHVDLPGELWAEHQEKLLKRLAGRLPKDVRVWSLTEAPSGFNARFSAIWRRYAYRVTDNTGGVDPLLRSHVLWHDWPLDVDAMNEAARRLVGEHDFAAYCKKREGATTIRTLQELSLVRGDDGVITATVCADAFCHNMVRSLIGALLFVGDGHRGPDWPGKVLAVGVRDSAVHVVRPHGLTLEEVGYPADELLAARNKEARNKRTLPAAGCC | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q82DM1 |
P18006 | TRBI_ECOLI | Protein TrbI | Escherichia | MSSTQKPADVTAERRSHWWWTVPGCLAMVLLNAAVSYGIVRLNAPVTVAFNMKQTVDAFFDSASQKQLSEAQSKALSARFNTALEASLQAWQQKHHAVILVSPAVVQGAPDISREIQQDIARRMRAEP | May influence the kinetics of pilus outgrowth and/or retraction . Overexpression phenocopies the deletion mutation; i.e. causes resistance to F-pilus-specific phage and CdiA-CT toxin . | P18006 |
B3LWP6 | WRNXO_DROAN | Werner Syndrome-like exonuclease | Sophophora | MDKYLIKLPNKNINDMVSDKKEVVKKETPKMTGRQAKKDTPKQEKEKENTQEDNTPKQNKAGRTGRSSIKRKNLDTPEVTQEKESVESENPPKRRSTRTTRSTRSMADGGTPSPEKEKPEKLPFIKYKGAIKYYTESQDIAASADDVMQWVEKQKEDVVPMAFDMEWPFSFQTGPGKSSVIQICVDEKCCYIYQLTNLKKLPSALVALINHPKVRLHGVNIKADFRKLQRDFPEVSADALIEKCVDLGVWCNVICQTGGRWSLERLANFICRKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRDLEQREKTKLANEEKFKEENGETAFKAVKALGEKFLSKMNEVTL | Has exonuclease activity on both single-stranded and duplex templates bearing overhangs, but not blunt ended duplex DNA, and cleaves in a 3'-5' direction. Essential for the formation of DNA replication focal centers. Has an important role in maintaining genome stability. | B3LWP6 |
A7NL64 | TRPD_ROSCS | Anthranilate phosphoribosyltransferase | Roseiflexus | MPIRDQIIQIVRGHDLTEEQAAEAMEEIMTGVATPAQVAALLTALHLKGETDAEIAGMARVMRAKAIPVHFDGPLLDTCGTGGDSAGTFNISTTAAFIAAGAGATVAKHGNRAMSSVCGSADVLEGLGVTIDLDAAGVARCLEQAGIGFMFAQKFHPAMRFVGPVRREIGIRTIFNALGPLSNPAQARHQTLGVADPALAEKMARALYLLGAQHALVVHGHGGLDELTLSGPNLVIEVRAGHKPRRYEVSAGDLGLTPAPREALLGGDVSTNVAIVRAILSGEERGARRDVALLNAAAALVAADYAADLREGLQQARQSLESGAALARLERLITVSSINR | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A7NL64 |
A8MRY9 | UGNT1_ARATH | Nucleotide-sugar uncharacterized transporter 3 | Arabidopsis | MRNNPVLPVSDPPLAGENDSDGKGVDDRLFKGSAMTKRGAYAALSYMACAVMLVLFNKAALSSYDFPCVNVITLFQMVSSSLFLYALRRRKIISFTAADSFSIDSASTFVPVKTLFHTLPLAIAYLLYMLASMASVRGVNVPMYTTLRRTTVAFTMVIEYMLTGQRYTRSIIGSVGIILLGAFFAGARDLSFDFYGYGVVFLANISTAVYLATIARTGKSSGLNSFGLMWSNGIICGPILMIWTFICGDLEKTINFPHLLTPGFMVVLLCSCVLAFVLNYCIFLNTTLNSALTQTICGNMKDLFTVGLGWMLFGGLPFDLMNVIGQLFGFFGSGLYAYYKIIGR | Mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc) across the Golgi apparatus membrane . Delivers an essential substrate for the maturation of N-glycans and the GlcNAc-containing glycosyl inositol phosphorylceramide (GIPC) class of sphingolipids in the Golgi apparatus . | A8MRY9 |
P43072 | TF3B_CANAL | B-related factor 1 | Candida | MSKPRKQQKCKTCGHTQFDVNRYTAAGDVSCLRCGTVLEENPIVSEVQFGESSSGAAMVQGAMVGADQARATFAGGRQNAMESREQTLSNGKRKIKRIAAALKIPDYIAEAAGEWFRLALTLNFVQGRRSNNVLATCLYVACRKERTHHMLIDFSSRLQISVYSLGATFLKMVKALHITSLPLADPSLFIQHFVEKLDFKDKATKVAKDAVKLAHRMAADWIHEGRRPAGIAGACVLLAARMNNFRRSHAEIVAVSHVGEETLQRRLNEFKKTKAGTLSVKSFREVENLESSNPPSFEKNRAMELKISKKLQQQQTDNFEDLSKMTEEEKQSVFGKLSKEEAQKQLLMNTILSDITITTENLNDQMDRILKMKKSSLENSLYKTPYELALANGSEQDPSKIWNINKPKNLVANLPKTDDILQNVSSEVELNSDDDDEIVLESKLTEEEVAIKERIWTGLNHDYLVEQEKKRLKQEADELTGNTSKSSSGNRRKRNKSSLPAELRKELGDIDLDEDGTPRSAADSAKMYISKTSVSKKINYDSLKGLLGGNMGF | General activator of RNA polymerase III transcription. Interacts with TBP. Binds to Pol III subunit C34 and to the TAU135 component of TFIIIC. | P43072 |
Q68F38 | VAC14_XENLA | Protein VAC14 homolog | Xenopus | MNAERDLSPLTPNIVRALNDKMYEKRKVAALEIEKLVREFVSQNNTAQIKHVIQILSQEFALSQHPHSRKGGLIGLAACSIALGKDSGQYLRELIEPVLTCFNDADSRLRYYACEALYNIVKVARGSVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESSKFDLVGFVPLLRERIYSNNQYARQFIISWILVLESVPDINLLDYLPEILDGLFQILGDNSKEIRKMCEVSLGEFLKEIKKLPDSVKFAEMANILVIHCQSTDDLIQLTAMTWMREFLQLAGRVMLPYSSGILTAVLPCLSYDDRKKNIKEVANVCNQSLMKLITPEDDETDEVRQSPATQPDEDFSSNHENSSQHTTYNRTLPSAPDSSLDNANIFAPSSMNTCPVSLNLDGIVHVLDRHLHESTTGMMTRICVLKWLYHLYIKTPRKMFRHTDSLFPILLKTLSDESDEVILKDLEVLAEIASSPAGQTDIVTDCNDLPTGMSELHVPVPTKVTQAHGSVIRGLECSPSTPTMNSYFHRFMVNLLKRFSNERKLLEIRGAFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVQNLNSILLTSSELFQLRSQLKDLQTPESCNLFCCLYRSWCHNPVATVSLCFLTQNYQHAYNLIQKFGDLEVTVDFLTEVDKLVQLIECPIFTYLRLQLLDVENNPYLIRALYGLLMLLPQSSAFQLLSHRLQCVPNPQLMRPGHKQEESSRAPKEDPARIDYVELLQHFEKVQNKHLEIRHQRSGAGELLERRLVQ | Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. | Q68F38 |
Q3BJY7 | TPM_PSOOV | PoTRO | Psoroptes | MEAIKKKMQAMKLEKDNAIDRAEIAEQKARDANLRAEKSEEEVRGLQKKIQQIENELDQVQEQLSAANTKLEEKKKALQTAEGDVAALNRRIQLIEEDLERSEERLKIATAKLEEASQSADESERMRKMLEHRSITDEERMDGLENQLKEARMMAEDADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAQQREEAHEQQIRIMTAKLKEAEARAEFAERSVQKLQKEVDRLEDELVHEKEKYKSISDELDQTFAELTGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q3BJY7 |
B5FB78 | UPPP_ALIFM | Undecaprenyl pyrophosphate phosphatase | Aliivibrio | MTYFEAFFLALLQGFTEFLPISSSAHLILPSAILGWPDQGLAFDVAVHVGTLAAVVIYFRKEVVTLLTAWVGSIVKKEHNKESNLAWLIVLATIPAALFGLLFKDFIEIYLRSAWVIAATTIVFGLLLWWVDKNATLAKDEYQMTWKKALFLGIAQAMAMIPGTSRSGITITAALYLGFTREAAARFSFLMSIPIITLAGSYLGLKLAMSDISIHLGLLSTGVIVSFISAYICIHFFLKLISSMGMMPFVIYRILLGSSLLVWLALH | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | B5FB78 |
Q1I419 | THIC_PSEE4 | Thiamine biosynthesis protein ThiC | Pseudomonas | MSKQEKAISLSESAQVDQQSVQPLPNSRKVYVEGSRPDIRVPMREISLHDTPTDFGGEKNAPVLVYDTSGPYTDPNVVIDVRKGLGDVRSAWIDARGDTERLEGLSSNFGLQRLNDAELAKLRFAHVRNPRRAKAGANVSQMHYARQGIITAEMEYVAIRENMKLQEARAAGLLDQQHAGHSFGASIPKEITPEFVREEIARGRAIIPANINHTELEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGVAEDLTWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFDEICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTKIAWKHDVQCMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARSFHDETLPKESAKVAHFCSMCGPKFCSMKITQEVREYAAKIETVDVTVEQGMREQSERFRQEGSQLYQKV | 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. | Q1I419 |
Q2NYH1 | TSAD_XANOM | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Xanthomonas | MKVLGIESSCDETGVAVYDTALSGVPALRAHAVYSQIALHAEYGGVVPELASRDHVRKLLPLIRQTLGEAGVGIDELDGVAYTAGPGLVGALLVGAGVARSLAWALDVPAIGVHHMEGHLLAPLMEDDPPEPPFVALLVSGGHTQLVSVKALGSYEVLGETLDDAAGEAFDKTAKMMGLPYPGGPQLAALAETGTPGRYRFARPMTDRPGLDFSFSGLKTQVLLAWRSSDQSDTTRADIARGFEDAVVDTLVIKCLRALDAAECNTLVVAGGVGVNKRLRARLQEAAQRRGGRVCFPRPALCTDNGAMIAFAGALRLQAGERADAAVHVTPRWDMAALPPLAAGRDSGVEIREW | 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. | Q2NYH1 |
Q83WJ5 | TRUA_BURM1 | tRNA-uridine isomerase I | Burkholderia cepacia complex | MRIALGIQYDGAAFCGWQAQPHGNTVQDALERALAEFARVPLHTTVAGRTDTGVHGLGQVVHFDTELDRADFSWVRGTNAFLPPTVAVQWAKSMPDAFHARFSAFERTYYYALYVHPVRSPMLDGRAGWIHTPLDDDAMRAAAAHLLGEHDFSAFRSSECQSKTPVKHLYEIDIRRVGHFLHFRFRANAFLHHMVRNLMGCLVAVGRGRYPADWVADVLAGRDRNRAAPTFMADGLYLAHVGYPAEFAVPPAQLGSVPWSSVWADLDPQP | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q83WJ5 |
Q8DJ44 | TATA_THEVB | Sec-independent protein translocase protein TatA | Thermosynechococcus | MNVFGIGLPELIVILVVALLIFGPKKLPEIGRSLGKTKRAFEEASREFQDEIKRQTAALEEEQQAKAEAESPREISP | 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. | Q8DJ44 |
Q6UX27 | VSTM1_HUMAN | Signal inhibitory receptor on leukocytes-1 | Homo | MTAEFLSLLCLGLCLGYEDEKKNEKPPKPSLHAWPSSVVEAESNVTLKCQAHSQNVTFVLRKVNDSGYKQEQSSAENEAEFPFTDLKPKDAGRYFCAYKTTASHEWSESSEHLQLVVTDKHDELEAPSMKTDTRTIFVAIFSCISILLLFLSVFIIYRCSQHSSSSEESTKRTSHSKLPEQEAAEADLSNMERVSLSTADPQGVTYAELSTSALSEAASDTTQEPPGSHEYAALKV | Inhibitory immune receptor involved in the regulation of phagocytes. | Q6UX27 |
B9E052 | YBEY_CLOK1 | Endoribonuclease YbeY | Clostridium | MIFLDNRQDKIEVTDKLEKIVTSSIECALKEEKVNFPCEISVVFVDNENIKDINRENRNIDRVTDVLSFPMLEYPESKVFKEVYLNYKFPEYDMNDGNLVLGDIVVSLEKCEEQSREFGHSFFRETCYLIVHSVLHLLGYDHTEDSDKKIMREREEYILKKAKL | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B9E052 |
A0QM44 | TAM_MYCA1 | Trans-aconitate 2-methyltransferase | Mycobacterium avium complex (MAC) | MWDPDVYLAFADHRARPFYDLLSRVGAERARRVVDLGCGPGHLTKYLGRRWPDAVIEAMDSSPEMVAAAKERGIDAVTGDLRNWKPKPDTDVVVSNAALHWVPEHSDLLLRWAGQLAPGSWIGVQMPGNFESPSYAAVRALARREPYAKLLRDIPFRVGAVVQPPTHYANMLLDAGCKVDVWETTYLHQLTGEHPVLEWITGTALVPVRERLDDDAWEQFREELIPLLRDAYPPRADGTTIFPFRRVFIVAEVGSGRPAA | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | A0QM44 |
B5XQT8 | TAM_KLEP3 | Trans-aconitate 2-methyltransferase | Klebsiella | MADWNPSLYLQFDAERTRPAADLLSRIAHLQVEHVVDLGCGPGNSTRLLRAAWPLAAITGIDNSPAMLAQAAQALPDCEFIDADIARWRPAQPVDVIYANASLQWLADHETLFPHLVAQLAVNGTLAVQMPDNWQEPSHTLMRQVADEQGLPDRGRQPLLPPDAWYDMLTRQGCEVDIWRTTYFHPLASHQAISDWLQGTGLRPYLAGLDEQSRNAFLTRYVELLAEHYPLQCNGKVLLRFPRLFIVARKIDV | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | B5XQT8 |
P0C7N3 | VM3CR_CROVV | Snake venom metalloproteinase | Crotalus | AMVTKNNGDLDKSGTECRLYCKDNSPGQNNSCKMFYSNEDEHKGMVLPGTK | Snake venom zinc metalloproteinase-disintegrin-like that blocks the interaction between platelets and collagen fibers through its binding to collagen fibers, resulting in the blockade of collagen-mediated platelet functions such as adhesion, release reaction, thromboxane formation, and aggregation. Binds selectively to collagen type I with high affinity. Also exerts proteolytic activity to matrix. | P0C7N3 |
A6MMD3 | YCF4_CHLSC | Photosystem I assembly protein Ycf4 | Chloranthus | MNWRSERIWIELITGSRKTSNFCWACILFLGSLGFLLVGTSSYLGKNLISLLPSQQILFFPQGIVMSFYGIAGLFISSYLWCTISWNVGSGYDRFDRKEGIVCIFRWGFPGINRRIFLRFLMRDIQSIRMEVKEGLYSRRVLYMEIRGQGAIPLTRTDDNLTPREIEQKAAELAYFLRVPIELK | Seems to be required for the assembly of the photosystem I complex. | A6MMD3 |
P54786 | ZDS2_YEAST | Protein ZDS2 | Saccharomyces | MVLMEDMQNKDGHNTVENSSGGTDSNNNIQMRRMRKTQLSKKELFEKRKSDVLIAAKSLDTEIQNVKNLKRLSIGSMDLVIDPELEFKVNSRNSYSSDSSKESLQESLHEENIIRSEQKEEQGSEDNDAYEEGDATNVDDSIDITQTEYLHDEETLEKEKIIRNASSSTSSSARVTSRNRRLSGVKTLAHDVVLDVENDHDSKMVDLTQNLLWVPADQHPNVKPENYLELIQDTLQNIQISTNQDIDENKLELGNNHVISNRKRTGSVVRRPSRLKTSYTKFDDEPPLADKPQEGEIQVDKRISSSDIKTIRSVSLKEITEELTKISNNAGLTDSDAVTLARSLSMSGSFTNESLHLNGNHTENDNEFASNMFNETGLTIPERSSLRRSKFNTYKIRLEGSSLPQAVKLNSLMNIQTNDNRRSASSPASYTQVPQEQASLNDFHEIFDHYRRTSTDWSTENEKYVDSTNYYSDEEDLTHASISQESSLLSTDSSNNSVLIKPHNTGSMISEKLDQHVSSSEKSNTNNSEANHGWSWLNSSNGSLNANEQTYQQLTDDEDDEECVDNEKADFVNLSVSRRAKSTKRASERINHSKNRHSPIFQIHSEEAKSVVITPSVVSSSESQPSKPTAPAVVEKKVELPTDTQASTHKKNSLEKRLAKLFKRKQHNGTCKSDVKVIKKSVKKELKKKASHSSLSKFRKSPKKKPQEAEVERPSSPTKTITTEDIDTASVIEPEVRSSNASTLLPDSHTSHSSEFVVETISELDGDDSFDISGGDVNYDVEVHSSISRDTTAGLEEDIGAEREDNTSPTAPQISTLPPRKLTFEDVVKPDYSNAPIKFTDSAFGFPLPMITNSTVIMFDHRLGINVERAIYRLSHLKLSDPGRELRQQVLLSNFMYSYLNLVNHTLYMEQVGTGDIAFNGDSALGMMDKNDSDGTILIPDI | Acts as a negative regulator of polarized growth via an alternative mechanism to ZDS1. In heat-stressed cells appears to play a role in localizing BCY1 to the cytoplasm. Seems to interact with, and down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an integration point for distinct signaling pathways helping to maintain a balance among these different pathways. | P54786 |
Q8DVQ4 | TRMB_STRMU | tRNA(m7G46)-methyltransferase | Streptococcus | MRVRRRKGAKEHLENNPRYVILKPEEVKGHWQEVFGNDHPIHIEVGSGKGRFITGMAAKNPQINYIGIDIQVSVLSHALDKVLDSQLPNVKLMLADGSSLMHYFADGEIDLLYLNFSDPWPKKRHEKRRLTYKSFLDTYKKILPEKGEIHFKTDNRELFEYSLASFSQYGMILEQVWLDLHASDYENNVMTEYEEKFSQKGQVIYRVEARF | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q8DVQ4 |
Q31RR1 | TATA_SYNE7 | Sec-independent protein translocase protein TatA | Synechococcus | MNFFGIGLPEMLVILAIALLVFGPKKLPEIGRSLGKALRGFQDASREFESEIKREIDRTPATPAEATVEPPVLDSAPTEAVTVEKQTETQV | 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. | Q31RR1 |
A1T3J8 | Y910_MYCVP | Putative S-adenosyl-L-methionine-dependent methyltransferase Mvan_0910 | Mycolicibacterium | MADNDRDGWDPASGVGLSATEGAAARAVVGRRKTPLVRDPFAEPLVCAVGVDSLTRLAQQSGVDGESGFAIPRMVDWIAARTRFFDDYFNAGQTDGIRQSVILGAGLDSRTYRLPWLPGATVYEIDQPGVVEFKNETMDRLQAQPLADRRPVAADLRGDWAPPLRIRGFDPSLPTMWSAEGLLPYLRAEDQMQVLDEISALSSKGSRLAADTVDDIGELAARIALSRGPRNPVAESDADLGGASSSHAVAQRLQSHGWLSNTRPAPQLFAAYAMPPLAEDQELYRKITVVTAMLR | Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | A1T3J8 |
B0CLM0 | TRMFO_BRUSI | Folate-dependent tRNA(M-5-U54)-methyltransferase | Brucella | MSNNTDLSPVHVIGGGLAGSEAAWQIAQAGVPVVLHEMRPVRGTDAHKTEQLAELVCSNSFRSDDAETNAVGVLHAEMRLAGSLIMACADAHQVPAGGALAVDREGFSQAVTARLEAHPLITIEREEITGLPPTEWGTTIIATGPLTAPSLAEAIAAETDADALAFFDAIAPIIHFDSINMDVCWFQSRYDKVGPGGTGKDYINCPMDKEQYEAFVAALIEGDKTDFKEWEGTPYFDGCLPIEVMAERGPETLRHGPMKPMGLTNAHNPTVKPYAVVQLRQENALGTLYNMVGFQTKLKYGSQTGIFKMIPGLENAEFARLGGLHRNTYLNSPVLLDNVLRLKSRQTLRFAGQVTGCEGYVESSAIGLLAGRFTAAEKLSQAAVPPPPTTAFGALLGHITGGHIVTDDEPGKRSFQPMNVNFGLFPPVDVPKPEGKRLRGKEKTIAKKRALSARALADCRNWLSLY | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | B0CLM0 |
G5EGQ6 | TEN1_CAEEL | Teneurin-1 | Caenorhabditis | MFQHRTTNAQGPPPNRPMPRPPAGMPMMTSSHEHDYTNDYEDPEEMARSRGEGFSNHLLIKTTPPPQPHPNFNSYEMSMSQQRRSQQHQQPMAPPLSDCWGSGVHDSGVLHKNADGAYYIPSGSLRTTSSTLSPASGQRYLDQPHTSGGAPNPTYSDASTTLLKYPLAAGTNQNRRRQQVGTMNNGDPVAGGPMALSKKKKKFDDDSDTCSRWPSKWNILLAAALLVALFVICILLFRAPNYVYTQPAPSSDATSSAAAAASRYQDLGLRALPPAISLGERVDVEFFPKSMATTELTVTKPSRIRFNATVGSGAQLVLLMSAGVHPSLSLHDALFPIRADRIRDSKSPTHIVEEFGSRSRRSLGASSSRHRNIEILSPRSATFEQFVLEGRHYLTFINERSRVEPISFVAEELQRPTTPPKTSSSGTSGAKEHPLASVLVCESNCNQRGECVHGKCHCAPGFTGRTCDEAVCPVVCSGNGVFSGGICVCKSGFKGKECEMRHNWCEVADCNGRGRCDTDGRCRCNPGWTGEACELRACPHASCHDRGVCVNGTCYCMDGWRGNDCSVFADAIVHVPQAQSPPRRGQEPTESSKTRKAQVKPTPTSEKKKESRELQKPIIATVQVPTESSHPCSAHGQLIDDICQCESGWDSVDCSQQACQCVNGDCLDDGSCQCWKGWRGSNCTDKKCAIGCEDRGKCASDGSCKCSSGWNGENCAIDGCPNQCSGKGECGMDRRSSEWSCRCQAGSTGVDCSVSVEMHCDDGLDNDSDGLIDCDDPECCSSSSCSSESVCSTAASPIEVLMRMPPIFNANFAQRVGFLIMEKSVQSYTDSSQFNENLISVIRGRVMWGGSPTGSDDLSTYSNKSTVPLVGVRVSDAAHPLYGFTLTREDGYFDLTVNGARSVTLQFLRTQFQSVKKSVFVSPRQIIHIDDIVLYRQSGGSPPAISMAPARAKCSPTLRRIPDVVLISNWQYTSDGIETDETSDSSRIVVDSRSIFESLPIQGTDVRLVYDSARSPAAPSTMLIGLLYDRVDKELRKVHINIRIAGRRFDRVLAPRTNLTYVFAWDKMNAYRQSESGLVPVTVRVGYEYQGCDRTSERVWQTRRSQMMGATARKMIGTMWTLDIHHHLDIVNNVVEMGNGGYRLITESEPRVSTFAGLDGVKRDVECLKCEGKVDSISLFRPTTVVYAQDGSLIIGDHNMIRRVSQDGQVSTILTLGLADTSHSYYIAVSPVDGTIAISLPLHKQVWRISSLEPQDSRNNYDVLAGDGTVCASAVDSCGDGALAQNAQLIFPKGISFDKMGNLYLADSRRIRVIDTTGHIRSIGETTPDQHPIRTCAQITKLVDLQMEWPTSLTIDPITGSVLVLDTNVVYEIDVVHDVVTIALGSPTTCDLANATSSASAKSLDHRRHLIQNARDITVGTDGAIYVVESDGRRLNQVRKLSSDRSTFSILTGGKSPCSCDVAACGCDDAVSLRDVAASQAHLSSPYAVCVSPSGDVIIADSGNSKIKKVSARMAKYDGRSRTYEVTDAERQEKYTFNRHGQHSSTVSLITGRTFFNFSYQVDSPISMISEIRAASGVVLRVLKRNDSLFDLETTLGQRTTLTMSAYDGTLEQVSKRDSATSRDATKLFYKKGLLTSRIDVATAVGFEYDEYGRAIGLKRDREYWRLGEETISMGSVNTEVLLNGQRFQQVRLGEGNLAVHSTNGATTRLISLRNEGYSLASPLGTSTLYDKSSSIPDSNGEPLISRRRTKVPAIGNPQRRELTTRWDWRHVARRGDDSDGSLGRRKVAEINGVNMFSMEYDVKSNQDTLRLGSTTDDAQALLFIDYTSSGRIRRISAPEDSQMAEMNITWDGAGRKSEVTWGSWKIRLTYDNSNRLTEHAIDGARVPIKMSYAGASRRPNEIQHDGAKWNIQYDNYDRIKEVISKSQEATSFSSIALGGDEWVLKRRTSLNSKPSLVRLSREGKVLESTTPDENHYWLERKDPITGRTTEILNDEETTVVTCWSPEGAPMCSRSRNLQENTTMQGHLVARKSVTIMTPTSSEPSITSSFTYEYDDMLRVTTIQPVIEQSVLESIQLSYDERRGHVAAINGFKWARDASTSRCQGHGLMYETSKANDHRQVVERKLIFGDARASIKIIRDKAGRASESHLEISSSGTQRNQKITRTFDAAGRVASVEQNDQEPVRIIWNSDARVEKINDRVVEWNRGGALKTFQDISYQVDSIGWVVKRDNTTVFGYDGKGRLVSARSSQLRINIFYDREDRVVQIQNSKDFIHFYYGYIDTPKLVSHFSKNGKISTLFYDDDSVPFAMQSDDGTRYALLTDETSTIKAIIGDSNVLRIIDRSVFGALLPSSSSSHPFLPIGYLGGIEISEISVSILNNGRPLDLYSERYMSISPEAVVRLELNEKFSNSIDLMALEIDRQPFRVENVPEDFETWFSLAGLSPNLLPSAHLGLPASSAIVHRLLSSFPRKLRPLTHLTTVLPTRLASDISLTSPTSETSWSIDDVGFSNLLILNEDATTGEVMVEMLSDLKSEEREVISKLFDGVKSLDFATWGLVPTRHLWRAPNSKLELSSTSFSHFTMAVNKDSVELRNGKSKIVVHFSENKAEIVKKIVEELKTRENIAVWRAERKRAEAGEKTWRQWSDRETRELTSKGSVSGYDIEMKPAHQSGLLASVHSWKFRKSE | Plays a role in the gonadal basement membrane maintenance and/or adhesion early in development. Contributes to the guidance of pharyngeal neurons. | G5EGQ6 |
B0UDF4 | URED_METS4 | Urease accessory protein UreD | Methylobacterium | MSSHPTPSWPRRQRSEGRVALGAGLVAGGTTRLTDLAETGPLRLRLPRVEGAALEGVLLNSAGGLACGDRFAVAAEIGEGADMVLTTTAAEKIYRSDGPVTEIAAELRLGPRARLAWLPQETILYDGARLSRRLTAEIAPDAALTLFEALVFGRSARGETVREGEIRDAWRLARGGRLVYADTLRLDGAVAAHLARPAIAGGARAVATLVHAAPDAESRLDGLRGLIAAAGCAALGVEAGASAWNGLLVLRLLAPESAPLRRAATRILEGFRGLPLPRVWQT | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B0UDF4 |
B7NK87 | XGPT_ECO7I | Xanthine phosphoribosyltransferase | Escherichia | MSEKYIVTWDRLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGVVFVPPISGR | Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine. | B7NK87 |
Q15PR4 | TAL_PSEA6 | Transaldolase | Pseudoalteromonas | MSNQLQALRDITTVVADTGDIEAIKKYQPVDATTNPSLLLKAAEMEQYRSHLENAVAWAKEQSDDADQQIIDAGDKLAVTIGTDIVNIVPGRISTEVDARLSFDTQASIEKAHKLIALYKEAGIDKSRILIKLASTWEGIKAAEHLEKEGINCNLTLLFSFAQAQACAEAGAYLISPFVGRILDWYKAKTGKTEYAASEDPGVQSVTKIYNYYKEHGYKTVVMGASFRNIGEITELAGCDRLTISPGLLEELSNSDAPLEVKLKDTGATTTPGKPLDEAAFRWEMNQDAMATEKLSEGIRNFAADQVKLETLLKSYV | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q15PR4 |
Q6UW78 | UQCC3_HUMAN | Assembly factor CBP4 homolog | Homo | MDSLRKMLISVAMLGAGAGVGYALLVIVTPGERRKQEMLKEMPLQDPRSREEAARTQQLLLATLQEAATTQENVAWRKNWMVGGEGGAGGRSP | 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. | Q6UW78 |
A1T7P4 | TYSY_MYCVP | Thymidylate synthase | Mycolicibacterium | MPIATPYEDLLRLVLDTGTTKSDRTGTGTRSLFGHQMRYDLNAGFPLITTKKVHTKSIVYELLWFLRGDSNVRWLQEHGVTIWDEWASPTGDLGPVYGVQWRSWPTPSGAHIDQISAALDLLRRDPDSRRNIVSAWNVGEIPQMALPPCHAFFQFYVSGGRLSCQLYQRSADLFLGVPFNIASYALLTHMMAAQAGLGVGEFIWTGGDCHIYDNHVEQVTEQLSREPRPYPELVLAQRDSLFDYIYEDVVIKNYDPHPAIKAPVAV | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | A1T7P4 |
Q4R6M8 | TKTL1_MACFA | Transketolase 2 | Macaca | MADAEASAELPEEARPDGGTLRVLRDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCIDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHGKPMPRERADAIIKLIESQIETSRNLDPQLPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHCVSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATEGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCMLLN | Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. | Q4R6M8 |
A1EA19 | YCF4_AGRST | Photosystem I assembly protein Ycf4 | Agrostis | MNWRSEHVWVELLKGSRKRGNFFWACILFLGSLGFLSVGASSYLGKNIISILPSQQILFFPQGVVMSFYGIAGLFISSYLWCTILWNVGSGYDRFDRKEGIVCIFRWGFPGIKRRVFLQFLMRDIQSIRIQVKEGLYPRRILYMEIRGQGVIPLTRTDEKFFTPREIEQKAAELAYFLRVPIEVF | Seems to be required for the assembly of the photosystem I complex. | A1EA19 |
B1KLT8 | TIG_SHEWM | PPIase | Shewanella | MQVSVETTQGLERRLTISVPAEQIEKAVNDSLKNEAKRARIPGFRPGKVPVSVINKRYGKAIRQDITGEVMQRNFVEAIIAEKLNPAGAPTFVPGESDAENFQFVATFEIYPEVELKGLEDIAVEQPTSDVTDADVDTMIETLRKQHATYEAVERAAADGDKAKINFVGSIDGEEFEGGKAEDFELQLGSGRMIPGFESGVEGHKAGEEFDIEVTFPEDYHAENLKGKVAKFAITLNEVQAANLPEVNDEFATLFGVAEGGLEALKAEISKNMGRELEQALKANVKEQVLNGLLEQNEIELPASLIAGEVEVLRKQAMQRFGDQAANMPELPADLFTEQAERRVKVGLLLGEVIKTNELKAEEERVQGLIASMASAYEDPSEVVEYYNGNQEMMQNMRNVALEEQAVEALLKTAKVTEKAVNFEEFMNKATQQG | 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. | B1KLT8 |
Q89AR5 | THRC_BUCBP | Threonine synthase | Buchnera | MKLYNLKKKQDQVNFSKAVKLGLGKNQGLFFPKELPILTKEQLYKLLKMDFLTRSSKILSMFIGDEIHYSELTKRIKNAFSFTTPKIVSISKNIACFELFHGPTLAFKDFGARFMAQILSFLNHDKNDTITILTATSGDTGAAVAHAFFKMKNVRVIILYPKGKISELQEKLFCTLGENIITIAVNGSFDECQKLVKQAFNDDQLRIETGLNSANSINISRLLAQICYYFEAFALLTKKQQKNLVISVPCGNFGNLTAGLLAKALGLPIKSFIASTNSNDTVPRFLKTGFWKPNNTVSTISNAMDISQPNNWPRVEELFKRKFWSLKTLKYGSVSDILTKKSLKKLAFLGYVSEPHAAVAYYTLKNKLKQNEFGLFLGTAHPAKFKKTIEKILQITLFLPSKLRNQIKLPLLSHNIRPDFSKLKKFLLEK | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. | Q89AR5 |
P18317 | UREE_KLEAE | Urease accessory protein UreE | Klebsiella | MLYLTQRLEIPAAATASVTLPIDVRVKSRVKVTLNDGRDAGLLLPRGLLLRGGDVLSNEEGTEFVQVIAADEEVSVVRCDDPFMLAKACYHLGNRHVPLQIMPGELRYHHDHVLDDMLRQFGLTVTFGQLPFEPEAGAYASESHGHHHAHHDHHAHSH | Involved in urease metallocenter assembly. Binds about 6 nickel ions per homodimer. Probably functions as a nickel donor during metallocenter assembly. Its function can be bypassed in vitro in the presence of high nickel concentrations. | P18317 |
Q5HM30 | TRUA_STAEQ | tRNA-uridine isomerase I | Staphylococcus | MRILVEIAYQGNQFLGFQIQQQGRTVQQQFEKILKRMHKHHVRIHPSSRTDRGVHAYQQFFHFDTELNIDNKQWQYAMNRALPDDIYVKNVRNVDEYFHCRYDCVGKRYRYKVYQGNHRNPFKSGTETFVNETLDYDKMNKAAQEFIGTHDFTGFCSQKTEVESKVRTLYQSEIVATKEGFDYVVTGSGFLYNMVRVLVAFLIEVGKGKREPNDVPKLLEDKNRNNVPLTAPPDGLYLEKIYLSPEELIQEYGKDVKIHYKKSLEKH | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q5HM30 |
A4XLM7 | TRPD_CALS8 | Anthranilate phosphoribosyltransferase | Caldicellulosiruptor | MLKEALEVVTAKRDLDYGQVKNLLDSILEGELDEMKFGAFLAALKTKGETKEEISAFVDAFYEKAQKIEYTHPKTIDTCGTGGDGKGTFNISTASAIVLSCFDLKVAKHGNRSITSNSGSADILENLGIDIQAPPQRILEGLEKHNFAFLFAPKYHPATKKVATVRKSLGIRTVFNILGPLLNPVSLNYQVVGAFDFEAQEKIASVLKGKRKRAAIIHSLDGLDEISVSQKTRVLELQGDNIKEYYIDPKEYGIEYTLDDIKGYTPQENAKIFRSILNGEVSAYYWAVVLNSAFALYIAEVANDIEEGIALCQSAIKKGDAMLKLKDLQQHYKVGA | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A4XLM7 |
Q03SD0 | YBEY_LEVBA | Endoribonuclease YbeY | Levilactobacillus | MDLEIYDKTQDGVPAEHVNLIQDVLQYAGKYLKLADNTEMSVTLMNNEDIHRINQQYRGVDRATDVISFAIEDDDEEAADFPLVMDDELAAEIPENIGDIFVSMDKVAEQADYLGHSYERELGFLVVHGFLHLNGYDHMEPEDEKVMFKLQADILDAYGLKR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q03SD0 |
Q8BWP5 | TTPA_MOUSE | Alpha-tocopherol transfer protein | Mus | MAEMRPGPLVGKQLNELPDHSPLLQPGLAELRRRVQEAGVPQTPQPLTDAFLLRFLRARDFDLDLAWRLMKNYYKWRAECPELSADLRPRSILGLLKAGYHGVLRSRDSTGSRVLIYRIAYWDPKVFTAYDVFRVSLITSELIVQEVETQRNGVKAIFDLEGWQVSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKDRIHLHGNNYKSSMLQHFPDILPREYGGKEFSMEDICQEWTNFIMKSEDYLSSISETIQ | Binds (+)-alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol. | Q8BWP5 |
Q493X8 | TSAD_BLOPB | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Candidatus Blochmannia | MRVLGIETSCDETGVAIYDQHKGLLANEVYSQSELHADYGGVVPELAARDHVRKIVPLISCTLNRARLEPKNIDGIAYTAGPGLMGALLVGATVARTLAYAWKIPAIDIHHMEAHLLAPMLEKKVPTFPFIALLVSGGHTQLVSASNIGEYKILGESIDDAVGEVFDKIAILLGLKYPGGALLSKMAQKGISKRYVFPRPMIDRPGLNFSFSGLKTCTVNTIMSNSHDAQNCADIARAFEDAIIETLAIKCRRALNQTGLKCLVISGGVSANHALRSYLLKMMYTLQGSLFYPRPEFCTDNGAMVAYAGLIRLKAGLFSDLPILVRPRWSLEDLPRIKQSL | 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. | Q493X8 |
Q92089 | TDT_ONCMY | Terminal deoxynucleotidyltransferase | Oncorhynchus | MNHAGMLALVKKRKRPVEAGAQGQVEVKFKEVTLELVERKMGSSRRNFLTRLARSKGFRVEDVLSDDVTHVVAEDNQAEVLWAWLMGHGLRDVSRLALLDISWFTDSMREGRPVRVETRHSIQNTPTGTDCSPPTAVANVSQYACQRRTTTENHNNKIFTDVMEELAESSEFNESKGPCLAFRQAASVLKSLPSAVHCLKAIQGLPCLGEHTKAVMEEILTFGRSFKVEEIRCDERYQALKLFTSVFGVGPKTAEKWYRRGLRSLQEILTEPNIQLNRMQRAGFLYYSDISKAVSKAEAKAVGCIIEDTFHWIAPDAILALTGGFRRGKEYGHDVDFLLTMPEIGKDEGLLLHVIDRLKDQGILLYCDYQGSTFDVSKLPSCRFEDMDCFQKCFLILRLEQGQVEGERGLQRDPGDSRGWRAVRVDLVAPPVDRYAFALLGWTGSRFGRDLRTFAQKERQMLLDNHALYDKTKKLCLLATTEEDIFTHLGLEYVEPWQRNA | Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. | Q92089 |
A0JUU8 | TRUB_ARTS2 | tRNA-uridine isomerase | Arthrobacter | MLSGLVIVDKPQGWTSHDVVGRMRRLAGTRKVGHAGTLDPMATGVLVLGINKATRLLTYIVGTSKTYTATIRLGESTVTDDAEGEVVSSHSAAAVTEGAIRAAVAALTGEIQQVPSSVSAIKVNGERAYARVRSGEDVKLAARPVTIHRFDVHAVRPERAGAVLDVDVTVECSSGTYIRALARDLGEALGTGGHLTALRRTQVGPYTLDQARTLEQLAEELEVLEMSQAARALMPNRELSEDEATEISFGRRIAAGAGAGTPEAATADNPAAAFAPDGSLVALLADAGGYAKPVLVFAPSNEQPGK | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A0JUU8 |