entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
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A0A0D2UG83 | H2AY_CAPO3 | Histone macroH2A1.1 | MAKSKKIVAATSGSRSRSSRAGLAFPVGRVHRLLRKGHFADRIGSGSAVYLAAVLEYLTAEILELAGNAARDNRKTRINPRHIQLAVRNDEELSKLFTGVVIPSGGTLPHIWPALIPNEAKDSSTASASFNAPAKSATVKALAAAKSAGKKPAAVSSSSAAASSSSSASSSSSVAPKKPVRGFTILSKKTLHLGQTLYVVNGDLTEVRCDAVVHPTNGTMSFAGQVGGAIRAAAGAGVDAEVNSYMSEHSQLQVTKAAITSGHNLPSKWIVHVHSPNYSNAATATDALTQTIRNALTLADTKSIKTIAFPSIGSGNNHFP... | Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA ... |
A0A0D2Y5A7 | ODP2_FUSO4 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (FoDLAT) (DLAT) | MLSAALRRRVLAPTHSALRTGFAAHVVRHYASFPEHQVIKMPALSPTMQAGNIGAWQKKPGDSIAPGDVLVEIETDKAQMDFEFQEEGVIAKILKDAGEKDIPVGSPIAVLVEEGTDISAFEKFSIEDAGGDAAKPAAPKKEEKSESKSESASAPEPTPEPQQYQSQGRLQTALDRLPNISASAKRLAREKGISIDGLKGTGKNGQITEEDVKKAISSPAASSAPSATYEDIPISGMRKTIANRLVESTQTNPHFYVTSSISVSKLLKLRQALNSSADGKYKLSVNDFLIKAIAVASRKVPQVNSSWRDGNIRQFNNVDV... | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). High pyruvate dehydrogenase complex activity is required for sufficient energy production during germination of conidia. |
A0A0D4WTV1 | B1D1_LOXAR | Dermonecrotic toxin LarSicTox-betaID1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) | EGAEQDGSERTDGGRPIWNIAHMVNNKQAIDKYLDKGANSVESDVSFDSDGKPEKMLHGIPCDCGRKCLNQMSFTDYLDYMRQLTTPGDPKFRENLILIMLDLKLKSVAANLAYSSGQEVALQMLNTYWKRGESGARAYIVLSIPTIKRVTFVRGFYDKLHSEGFDQYREKVGVDFSGNEDLDETGRILSSQNILDHIWQSDGITNCIFRVMTRLKKAINKRDSNGYMVKVYYWSVDKYTIMRKTLRAGADGMITNFPDRLVSVLNEREFSGKFRLATYDDNPWERYKA | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate. This toxin acts on sphingomyelin (SM) and on ceramide phosphoethanolamine (CPE) with high activity. It a... |
A0A0D4WV12 | BIB11_SICTE | Dermonecrotic toxin StSicTox-betaIB1i (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) | GDSRRPIWNIAHMVNDLDLVDEYLDDGANSLELDVEFSKSGTALRTYHGVPCDCFRSCTRSEKFSKYLDYIRQLTTPGNSKFRSRLILLVLDLKLNPLSSSAAYNAGADVARNLLDNYWQRGDSKARAYIVLSLETIAGAEFITGFKDTMKKEGFDEKYYDKIGWDFSGNEDLGKIRDVLESHGIREHIWQGDGITNCLPRDDNRLKQAISRRYSPTYVYADKVYTWSIDKESSIENALRLGVDGVMTNYPARVISVLGEREFSGKLRLATYDDNPWEK | Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate. This toxin acts on lysophosphatidylethanolamine (LPE) and ceramide phosphoethanolamine (CPE) with high a... |
A0A0D9S1R0 | APOE_CHLSB | Apolipoprotein E (Apo-E) | MKVLWAALLVTFLAGCQAAADAPIKVEQPVEPETEPELRPQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPS... | APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are a... |
A0A0E3D8M9 | JANG_PENJA | Geranylgeranyl pyrophosphate synthase janG (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (... | MLYFLAETIFGFICQYVPIGFWNGYSPAPTDRYRRLDLKSSQGFRAEPNLAPLPTTKPRRERYYGPNQIIRAPLDYLLSIPGKDIRGKLINAFNEWLQLPDDKLAIVKEVINLLHTASLLIDDIQDGSRLRRGRPVAHEVFGVAQTINAANYAYFLQQERLSEIGDPRAFHIFTNALLDLHRGQGMDLYWREAVVCPTEEEYIRMVIYKTGGLFRLALELMQVQSNSTTDFSELVELLGIIFQIRDDYMNLQSGLYAEKKGSMEDLTEGKFSYPVIHSIHAAPENSMLVDILKQRTEDNVVKVRAVHYMESTGSFQYCRE... | Geranylgeranyl pyrophosphate synthase part of the gene cluster that mediates the biosynthesis of the indole diterpenes janthitremanes such as shearinine K or shearinine A. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in janthitremane biosynthesis via conversion of farnesyl pyrophosphate ... |
A0A0E3D8P4 | PENG_PENCR | Geranylgeranyl pyrophosphate synthase penG (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (... | MLFLAPGYIFPNVATPVTVAIDFAQAVKQGAYNVLDLKASPIPNPELFQPPSRIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLNIIKEIVVILHTASLLIDDIQDSSELRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSNFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDSQLIQILKLKTKDEVIKQYAVRYIESTGSFVYCREKLDMYLEEANETFRG... | Geranylgeranyl pyrophosphate synthase part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl... |
A0A0E3KBH3 | OFOB_SACSO | 2-oxoacid:ferredoxin oxidoreductase subunit beta (OFOR) (EC 1.2.7.11) | MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT | Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives. |
A0A0E3T3B5 | AADH2_MALDO | Aminoaldehyde dehydrogenase 2, peroxisomal (MdAMADH2) (EC 1.2.1.-) (Aminobutyraldehyde dehydrogenase AMADH2) (EC 1.2.1.19) | MAIQIPSRQLFIDGEWREPVLKKRIPIINPATEQIIGDIPAATAEDVEIAVEAARKALARNKGRDWALAPGAVRAKYLRAIAAKIAERKSEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYADLAEGLDAQQKTPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLASHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGIFWTNGQICSATSRLIIHENIAAKFLDRLVQWCKN... | Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. |
A0A0E3T552 | AADH1_MALDO | Aminoaldehyde dehydrogenase 1, peroxisomal (MdAMADH1) (EC 1.2.1.-) (Aminobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.19) | MAIQIPSRLLFIDGEWREPVLKKRIPIINPATEEIIGHIPAATAEDVELAVEAARRALSRNKGRDWASAPGAVRAKYLRAIAAKIGERKPEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYAELAEGLDAQQKAPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLVSHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGCFWTNGQICSATSRLILHENIATEFLDRLLKWCKN... | Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. |
A0A0E4AZP0 | FSA1_FUSSF | Hybrid PKS-NRPS synthetase fsa1 (EC 2.3.1.-) (EC 6.3.2.-) (Fusarisetin A biosynthesis protein 1) | MDASEPIAVIGSACRFPGGSDSPSKLWELLKEPRDLLSKVPPERYNADAFYHADATHHGTTNVRHSYFLSEDPSSFDNNFFNIQPGEAEAIDPQQRLLMEVVYQGLCSAGQTIEGLRGSPTAVYVGVMCDDWSGIITRDLEVFPRYGATGMARSIMSNRISYFFDWHGPSMTIDTACSSSLVAVHQAIQTLRSGESEVAIAAGANLILTPGMYVAESKLSMLSPSGRSKMWDQDVDGYARGEGIAAVVLKPLSAAIRDNDHIDCIIRATGINQDGRTPGLTMPSATAQADLIRSTYARAGLDINKAEDRPQFFHAHGTGT... | Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of HIV-1 integrase inhibitor equisetin and of fusarisetin A, both trans-fused decalin-containing tetramic acids showing also antimicrobial activity. The PKS module of fsa1 together with the enoylreductase fsa3 catalyze the formation of t... |
A0A0F5HNH9 | IMEF_BACTR | Ferritin-like protein (EC 1.16.3.1) (IMEF cargo protein) | MKEELDAFHQIFTTTKEAIERFMAMLTPVIENAEDDHERLYYHHIYEEEEQRLSRLDVLIPLIEKFQDETDEGLFSPSNNAFNRLLQELNLEKFGLHNFIEHVDLALFSFTDEERQTLLKELRKDAYEGYQYVKEKLAEINARFDHDYADPHAHHDEHRDHLADMPSAGSSHEEVQPVAHKKKGFTVGSLIQ | Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like iron-binding protein probably involved in iron mineralization in the encapsulin nanocompartment. Has ferroxidase activity even when encapsulated, the rate is probably controlled by the rate of Fe flux across the nanocompartment pores. Part of the iro... |
A0A0G2JDV3 | GBP6_MOUSE | Guanylate-binding protein 6 (EC 3.6.5.-) (GTP-binding protein 6) (GBP-6) (Guanine nucleotide-binding protein 6) (Macrophage activation 2 like protein) | MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLQYVTELTELIRAKSSPNPAGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQLDPKFQEVTKAFVSYIFTYAKIKTLKEGIKVTGNRLGILVTTYVNAINSGAVPCLDDAVTTLAQRE... | Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens, such as bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii. Confers protection to several pathogens... |
A0A0G2JTR4 | ABR_RAT | Active breakpoint cluster region-related protein | MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGESISPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEMSESSRKLRH... | Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the ... |
A0A0G2JTZ2 | SOX6_RAT | Transcription factor SOX-6 | MSSKQATSPFACTVDGEETMTQDLTSREKEEGSDQHPASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSREREIMNSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINLLQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGITYKPGDNYPVQFIPSTMAAAAASGL... | Transcription factor that plays a key role in several developmental processes, including neurogenesis, chondrocytes differentiation and cartilage formation (By similarity). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesi... |
A0A0G2JUG7 | IQEC1_RAT | IQ motif and SEC7 domain-containing protein 1 | MACRRRYLSSLETGSSLSTDRYSVEGEAPSSETGTSLDSPSAYHQGPLVPGSSLSPDHYEHTSVGAYGLYAGPGPQQRTRRPRLQHSTSVLRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVPSECGDLSDPALKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHSEEVPASDTARARDTEPKPGLHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQA... | Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine nucleotide exchange factor activity is enhanced by lipid binding. Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalization of beta-1 integrin. Involved in neuronal development (By similarit... |
A0A0G2JV04 | GGA3_RAT | ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, gamma ear-containing, ARF-binding protein 3) | MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEAVQALTVLEACMKNCGRRLHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKAKVIELLFSWTLALPEEAKIKDAYHMLKRQGIVQSDPPIPMDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLRSKNPDDLQEANQLIKSMVKEDEARIQKVTKRLHTLEEVNNNVKLLHEMLLHYSQEFSSEADKELMKELFDRCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQIINGEVTTSTVPDSEGNSHC... | Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor A... |
A0A0G2JXN2 | TRI46_RAT | Tripartite motif-containing protein 46 | MAEGEDMQTFTSIMDALVRISTSMKNMEKELLCPVCQEMYKQPLVLPCTHNVCQACAREVLGQQGYIGHGGDPSSEPTSPASTPSTRSPRLSRRTLPKPDRLDRLLKSGFGTYPGRKRGALHPQTILFPCPACQGDVELGERGLSGLFRNLTLERVVERYRQSVSVGGAILCQLCKPPPLEATKGCSECRATFCNECFKLFHPWGTQKAQHEPTLPTLSFRPKGLMCPDHKEEVTHYCKTCQRLVCQLCRVRRTHSGHKITPVLSAYQALKDKLTKSLAYILGNQDTVQTQICELEETIRHTEVSGQQAKEEVSQLVRGL... | Microtubule-associated protein that is involved in the formation of parallel microtubule bundles linked by cross-bridges in the proximal axon. Required for the uniform orientation and maintenance of the parallel microtubule fascicles, which are important for efficient cargo delivery and trafficking in axons. Thereby al... |
A0A0G2JXT6 | MTMR6_RAT | Myotubularin-related protein 6 (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64) | MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQ... | Phosphatase that acts on lipids with a phosphoinositol headgroup. Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phospha... |
A0A0G2JZ79 | SIR1_RAT | NAD-dependent protein deacetylase sirtuin-1 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) | MIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITE... | NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation... |
A0A0G2K047 | ACSS3_RAT | Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 3) (Acyl-CoA synthetase short-chain family member 3) (Propionate--CoA ligase) (EC 6.2.1.17) | MKPSWLQCRKVTGAGTLGAPLPGSPSVRGAGVARRALVAGFGGRGCRALTTSSGGGEYKTHFAASVADPERFWGKAAEQISWYKPWTKTLENRYPPSTSWFVEGMLNICYNAIDRHIENGQGDKIAIIYDSPVTDTKATISYKEVLEQVSKLAGVLVKQGVKKGDTVVIYMPMIPQAIYAMLACARIGAIHSLIFGGFASKELSTRIDHVKPKVVVTASFGIEPGRKVEYMPLLEEALRIGQHKPDRLLIYNRPNMEKVPLMSGRDLDWEEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTM... | Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Propionate is the preferred substrate but can also utilize acetate and butyrate with a much lower affinity. |
A0A0G2K1Q8 | ABCA3_RAT | Phospholipid-transporting ATPase ABCA3 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 3) (Xenobiotic-transporting ATPase ABCA3) (EC 7.6.2.2) [Cleaved into: 150 Kda mature form] | MVVLRQLRLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATVYPDQHIQELPLFFSFPPPGGSWELAYVPSHSDAARTITEAVRREFMIKMRVHGFSSEKDFEDYVRYDNHSSNVLAAVVFEHTFNHSKDPLPLAVRYHLRFSYTRRNYMWTQTGNLFLKETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVV... | Catalyzes the ATP-dependent transport of phospholipids such as phosphatidylcholine and phosphoglycerol from the cytoplasm into the lumen side of lamellar bodies, in turn participates in the lamellar bodies biogenesis and homeostasis of pulmonary surfactant. Transports preferentially phosphatidylcholine containing short... |
A0A0G2K2P5 | ZO1_RAT | Tight junction protein ZO-1 (Tight junction protein 1) (Zona occludens protein 1) (Zonula occludens protein 1) | MSARAAAAKSTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSHPDPDPVSDNEDDSYDEDVHDPRSGRGALANRRGEKSWARDRSASRDRSLSPRSDRRSVASSQPAKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSVRSHDRPPRRSQSRSPDQRS... | TjpP1, Tjp2, and Tjp3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between th... |
A0A0G2K309 | ORNT1_RAT | Mitochondrial ornithine transporter 1 (Solute carrier family 25 member 15) | MKSNPAIQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGLTDCCLRTYSQVGFRGFYKGTSPALIANIAENSVLFMCYGFCQQVVRKVVGLDRQAKLSDLQNAAAGSFASAFAALVLCPTELVKCRLQTMYEMETSGKIAASQNTVWSVVKEIFRKDGPLGFYHGLSSTLLREVPGYFFFFGGYELSRSFFASGRSKDELGPIPLMLSGGFGGICLWLAVYPVDCIKSRIQVLSMTGKQTGLIRTFLSIVKNEGITALYSGLKPTMIRAFPANGALFLAYEYSRKLMMSQLEAC | Mitochondrial ornithine-citrulline antiporter. Catalyzes the exchange between cytosolic ornithine and mitochondrial citrulline plus an H(+), the proton compensates the positive charge of ornithine thus leading to an electroneutral transport. Plays a crucial role in the urea cycle, by connecting the cytosolic and the in... |
A0A0G2K344 | PK3CA_RAT | Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alph... | MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLVTIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFVIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPIDSFTMPSYSRRISTATPYMNG... | Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key... |
A0A0G2KQY6 | S39AE_DANRE | Metal cation symporter ZIP14 (Solute carrier family 39 member 14) (Zrt- and Irt-like protein 14) (ZIP-14) | MTLRRASGCRQLTLTIGLALTLGLLQWPIGDVRGQDGASPAQVLQELLTRYGDNASISVPQLRSLLVRLNGGQSEDHDSKTQPTRTNASKCLAADTLAVYGMSEQSRIDERGLQQICPTMIQQLDSQACKTQPNQESESSPRPTEAEVWGYGLLCVTVISLCSLVGASVVPFMRKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFDPMEDYYVPKSAVVFGGFYLFFFTEKILKMILKPKDTGGHGHGHSHFPAERYANSNGDLEDGVMEKLQNGEAGGAALPRAEADGRGVGEDDKMLSTGQTVQDTQSSGGGGTG... | Broad-scope metal ion transporter with a preference for zinc uptake. Also mediates cellular uptake of nontransferrin-bound iron. Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, ... |
A0A0G2KTI4 | S12A2_DANRE | Solute carrier family 12 member 2 (Na-K-Cl cotransporter 1) | MSASPPISAGDYLSAPEPDALKPAGPTPSQSRFQVDLVTESAGDGETTVGFDSSPPEYVAEPPPDGLRDSVSGGEEAKGRFRVVNFAASSPDAAPAETAQNGDTVMSEGSLHSSTGGQQHHHYDTHTNTYYLRTFGHNTIDAVPKIDFYRQTAAPLGEKLIRPTLSELHDELDKEPFEDGFANGEELTPAEESAAKDVSESKGVVKFGWIKGVLVRCMLNIWGVMLFIRMTWIVGQAGIAYSCIIVIMATVVTTITGCSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVELLMDS... | Cation-chloride cotransporter which mediates the electroneutral transport of chloride, potassium and/or sodium ions across the membrane. Plays a vital role in the regulation of ionic balance and cell volume. Important for maintenance of endolymph volume in the otic vesicle, probably by regulating ion homeostasis. Also ... |
A0A0G2L7I0 | SPRTN_DANRE | DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan) | MMEDEDFLLALRLQEQFDQETPAAGWPDEDCPSSKRRRVDPSGGLDVIPFTQPRAERPLSIVDESWETLDPNPDVRAMFLQFNDKFFWGKLSGVEVKWSPRMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTQNNRDRDGHGPEFCKHMNRINQASGTNITIYHSFHDEVDVYRQHWWRCNGPCQNRRPFFGYVKRAMNRPPSARDPWWADHQRSCGGTYTKIKEPENYGKTGKSDKQRDKMPATEMPKKSKPPSSTSSSGSQDIRNIIPFSGRGFVLGGNAQIPTNKQIQSPPKAPPEPL... | DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (By similarity). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replicat... |
A0A0G2Q9D6 | GYRB_MYCBP | DNA gyrase subunit B (EC 5.6.2.2) | MGKNEARRSALAPDHGTVVCDPLRRLNRMHATPEESIRIVAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGK... | A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Relaxes negatively supercoiled DNA in an ATP-independent manner. A li... |
A0A0G2Q9F8 | GYRA_MYCBP | DNA gyrase subunit A (EC 5.6.2.2) | MTDTTLPPDDSLDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEETLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSRGRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVIEIKR... | A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted r... |
A0A0G2QC33 | ATG4B_RAT | Cysteine protease ATG4B (EC 3.4.22.-) (Autophagy-related protein 4 homolog B) | MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRRNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFLDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRASLPCAGAAALSMESERHCNGLPAGAEVTNRPLAWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVELTDSCFIPDESFHCQHPPCRMGIGELDPSIAVG... | Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. The protease activity is required for proteolytic activation of ATG8 family protein... |
A0A0G2UGT2 | LEC_MYTTR | D-galactose-binding lectin (GalNAc/Gal-specific lectin) (MTL) | MTTFLIKHKASGKYFHPKGGTSNPPNGTNLVLHSDIHERMYFQFEVVNERWRYIKHVASEKIVHPFGGKADPLNGTNMVLHQDRHDRALFAMDFFNDNIRHKGGKYIHPKGGSKNPSNGNLTVMHGDEHGAMEFIFVSPKNKDKRVLVYA | D-galactose-binding lectin (PubMed:26802895, Ref.2). Binds both alpha and beta anomer of galactose (Gal). Binds strongly to branched beta-Gal-terminated glycans and weakly to unbranched glycans with alpha-Gal on the end of chains. Has strong affinity for both Gal and GalNAc. Binds glycoproteins containing mucin-type ch... |
A0A0H2UNG0 | PULA_STRPN | Pullulanase A (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha-glucosidase) (Pullulan 6-glucanohydrolase) | MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAAGSGKNESDISSPGNANASLEKTEEKPAASPADPAPQTGQDRSSEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIR... | Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-branchpoints of glycogen. Hydrolyzes pullulan. Does not hydrolyze dextran. Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate... |
A0A0H2URG7 | GTFA_STRPN | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit (EC 2.4.1.-) (Glycosyltransferase GtfA) (O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase) | MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKP... | Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encode... |
A0A0H2URJ6 | GLYE_STRPN | Glycosyltransferase GlyE (PsrP glycosyltransferase GlyE) | MRNTKRAVVFAGDYAYIRQIETAMKSLCRHNSHLKIYLLNQDIPQEWFSQIRIYLQEMGGDLIDCKLIGSQFQMNWSNKLPHINHMTFARYFIPDFVTEDKVLYLDSDLIVTGDLTDLFELDLGENYLAAARSCFGAGVGFNAGVLLINNKKWGSETIRQKLIDLTEKEHENVEEGDQSILNMLFKDQYSSLEDQYNFQIGYDYGAATFKHQFIFDIPLEPLPLILHYISQDKPWNQFSVGRLREVWWEYSLMDWSVILNEWFSKSVKYPSKSQIFKLQCVNLTNSWCVEKIDYLAEQLPEVHFHIVAYTNMANELLALT... | Involved in the polymorphic O-glycosylation of the serine-rich repeat protein PsrP. Catalyzes the third step in glycosylation of PsrP in this bacteria. Transfers galactose from UDP-galactose to the terminal glucose moiety of already-glycosylated PsrP (using the short substrate PsrP-GlcNAc-Glc). Has a very marked prefer... |
A0A0H2URK1 | PSRP_STRPN | Pneumococcal serine-rich repeat protein (PsrP) (Adhesin PsrP) (Serine-rich repeat protein PsrP) | MTETVEDKVSHSITGLDILKGIVAAGAVISGTVATQTKVFTNESAVLEKTVEKTDALATNDTVVLGTISTSNSASSTSLSASESASTSASESASTSASTSASTSASESASTSASTSISASSTVVGSQTAAATEATAKKVEEDRKKPASDYVASVTNVNLQSYAKRRKRSVDSIEQLLASIKNAAVFSGNTIVNGAPAINASLNIAKSETKVYTGEGVDSVYRVPIYYKLKVTNDGSKLTFTYTVTYVNPKTNDLGNISSMRPGYSIYNSGTSTQTMLTLGSDLGKPSGVKNYITDKNGRQVLSYNTSTMTTQGSGYTWGN... | Protein that allows bacteria to adhere to mammalian host cells. Required for full virulence in mouse infection models when infected intranasally. Required for adhesion to host cells in vitro and for persistence in the lower respiratory tract. Binds host keratin 10 (KRT10) on lung cells which mediates adhesion via the C... |
A0A0H2US87 | OSPC3_SHIFL | Arginine ADP-riboxanase OspC3 (EC 4.3.99.-) | MKIPEAVNHINVQNNIDLVDGKINPNKDTKALQKNISCVTNSSSSGISEKHLDHCADTVKSFLRKSIAAQSYSKMFSQGTSFKSLNLSIEAPSGARSSFRSLEHLDKVSRHYLSEIIQKTHPLSSDERHLLSIIINSDFNFRHQSNANLSNNTLNIKSFDKIKSENIQTYKNTFSEDIEEIANHDFVFFGVEISNHQETLPLNKTHHTVDFGANAYIIDHDSPYGYMTLTDHFDNAIPPVFYHEHQSFFLDNFKEVVDEVSRYVHGNQGKTDVPIFNTKDMRLGIGLHLIDFIRKSKDQRFREFCYNKNIDPVSLDRIIN... | ADP-riboxanase effector that inhibits host cell pyroptosis. Acts by mediating arginine ADP-riboxanation of host CASP4/CASP11, blocking CASP4/CASP11 autoprocessing. This prevents CASP4 activation and ability to recognize and cleave GSDMD, thereby inhibiting LPS-induced pyroptosis. ADP-riboxanation takes place in two ste... |
A0A0H2V871 | IROE_ECOL6 | Apo-salmochelin esterase (EC 3.1.1.107) (Enterobactin hydrolase IroE) | MYAREYRSTRPHKAIFFHLSCLTLICSAQVYAKPDMRPLGPNIADKGSVFYHFSATSFDSVDGTRHYRVWTAVPNTTAPASGYPILYMLDGNAVMDRLDDELLKQLSEKTPPVIVAVGYQTNLPFDLNSRAYDYTPAAESRKTDLHSGRFSRKSGGSNNFRQLLETRIAPKVEQGLNIDRQRRGLWGHSYGGLFVLDSWLSSSYFRSYYSASPSLGRGYDALLSRVTAVEPLQFCTKHLAIMEGSATQGDNRETHAVGVLSKIHTTLTILKDKGVNAVFWDFPNLGHGPMFNASFRQALLDISGENANYTAGCHELSH | Catalyzes the hydrolysis of both the apo and Fe3(+)-bound forms of enterobactin (Ent), monoglucosyl-C-Ent (MGE), diglucosyl-C-Ent (DGE) and triglucosyl-C-Ent (TGE). It prefers apo siderophores as substrates and hydrolyzes the Fe3(+)-bound siderophores very inefficiently. Tends to hydrolyze the trilactone just once to p... |
A0A0H2V8B5 | TCPC_ECOL6 | NAD(+) hydrolase TcpC (EC 3.2.2.6) (NADP(+) hydrolase TcpC) (EC 3.2.2.-) (TIR domain-containing protein in E.coli) (tcpC) | MIAYENIEFFICLVNVLGNNMYNILFFIFLSIAIPFLLFLAWKQHLKTKEIRSYLLKEGYNIIFNGEGNSYLAFNISNATFRAGNLTSNDYFQASISYIHDYRWEWKEVEAKKINNIFIIYISNIDFPSQKLFYRNNKSLAEIDWAKLQAIFHQPYEIQNDVMQDNNNTHYDFFISHAKEDKDTFVRPLVDELNRLGVIIWYDEQTLEVGDSLRRNIDLGLRKANYGIVILSHNFLNKKWTQYELDSLINRAVYDDNKIILPIWHNINAQEVSKYSHYLADKMALQTSLYSVKEIARELAEIAYRRR | Virulence factor that suppresses host Toll-like receptor (TLR)-mediated cytokine production upon infection, thereby increasing bacterial burden in the urinary tract and promoting renal tissue damage. Acts as a NAD(+) hydrolase (NADase) by catalyzing cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. Also abl... |
A0A0H2VG78 | GLCP_STAES | Glucose transporter GlcP (Glucose/H(+) symporter) | MKANKYLIFILGALGGLLYGYDNGVISGALLFIHKDIPLNSTTEGIVVSSMLIGAIVGAGSSGPLADKLGRRRLVMLIAIVFIIGALILAASTNLALLIIGRLIIGLAVGGSMSTVPVYLSEMAPTEYRGSLGSLNQLMITIGILAAYLVNYAFADIEGWRWMLGLAVVPSVILLVGIYFMPESPRWLLENRNEEAARQVMKITYDDSEIDKELKEMKEINAISESTWTVIKSPWLGRILIVGCIFAIFQQFIGINAVIFYSSSIFAKAGLGEAASILGSVGIGTINVLVTIVAIFVVDKIDRKKLLVGGNIGMIASLLI... | Transporter highly specific for glucose uptake. |
A0A0H2WWV6 | TARM_STAAC | Poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase (EC 2.4.1.70) (WTA GlcNAc-transferase) | MKKIFMMVHELDVNKGGMTSSMFNRSKEFYDADIPADIVTFDYKGNYDEIIKALKKQGKMDRRTKMYNVFEYFKQISNNKHFKSNKLLYKHISERLKNTIEIEESKGISRYFDITTGTYIAYIRKSKSEKVIDFFKDNKRIERFSFIDNKVHMKETFNVDNKVCYQVFYDEKGYPYISRNINANNGAVGKTYVLVNKKEFKNNLALCVYYLEKLIKDSKDSIMICDGPGSFPKMFNTNHKNAQKYGVIHVNHHENFDDTGAFKKSEKYIIENANKINGVIVLTEAQRLDILNQFDVENIFTISNFVKIHNAPKHFQTEKI... | Attaches N-acetyl-alpha-D-glucosamine residues to poly(RboP)-wall teichoic acids (WTAs). |
A0A0H2WZ38 | GATD_STAAC | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD (EC 6.3.5.13) (Lipid II isoglutaminyl synthase glutaminase subunit) (EC 3.5.1.2) | MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR | The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT. |
A0A0H2Z7X0 | TPBB_PSEAB | Diguanylate cyclase TpbB (EC 2.7.7.65) | MNRRRRYTGSNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAIVYDRQGQPLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLLTALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDASEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRE... | Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Important for the regulation of biofilm maintenance when exposed to peroxide. Part of the YfiB-TpbB-YfiR (or yfiBNR) system, encoding a tripartite signaling module that modulates intracellular c-di-GMP levels. The system is a ... |
A0A0H2ZFK2 | TPBA_PSEAB | Dual specificity protein phosphatase TpbA (DUSP) (EC 3.1.3.16) (EC 3.1.3.48) (Dual specific tyrosine phosphatase) (Protein tyrosine phosphatase) (Tyrosine phosphatase related to biofilm formation) | MHRSPLAWLRLLLAAVLGAFLLGGPLHAAETAAPRSPAWAQAVDPSINLYRMSPTLYRSALPNAQSVALLQRLQVKTVVSFIKDDDRAWLGQAPVRVVSLPTHADRVDDAEVLSVLRQLQAAEREGPVLMHCKHGNNRTGLFAAMYRIVVQGWDKQAALEEMQRGGFGDEDDMRDASAYVRGADVDGLRLAMANGECSPSRFALCHVREWMAQALDRP | Phosphatase that regulates diverse phenotypes in P.aeruginosa via regulation of the concentration of cellular c-di-GMP. Acts by dephosphorylating the membrane-anchored diguanylate cyclase TpbB at tyrosine and serine/threonine sites, leading to inactivation of TpbB and reduced c-di-GMP production. The reduced cellular c... |
A0A0H2ZL64 | PULA_STRP2 | Pullulanase A (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha-glucosidase) (Pullulan 6-glucanohydrolase) | MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAADSGKNESDISSPRNANASLEKTEEKPATEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQI... | Virulence factor. Involved in the degradation of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-branchpoints of glycogen. Hydrolyzes pullulan. Does not hydrolyze dextran. Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein... |
A0A0H2ZMF9 | PBP2A_STRP2 | Penicillin-binding protein 2a (PBP2a) (Cell wall synthase PBP2a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase) (Peptidoglycan glycosyltransferase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] | MKLDKLFEKFLSLFKKETSELEDSDSTILRRSRSDRKKLAQVGPIRKFWRRYHLTKIILILGLSAGLLVGIYLFAVAKSTNVNDLQNALKTRTLIFDREEKEAGALSGQKGTYVELTDISKNLQNAVIATEDRSFYKNDGINYGRFFLAIVTAGRSGGGSTITQQLAKNAYLSQDQTVERKAKEFFLALELSKKYSKEQILTMYLNNAYFGNGVWGVEDASKKYFGVSASEVSLDQAATLAGMLKGPELYNPLNSVEDSTNRRDTVLQNMVAAGYIDKNQETEAAEVDMTSQLHDKYEGKISDYRYPSYFDAVVNEAVSK... | Cell wall formation. Synthesis of cross-linked peptidoglycan (PG) from the lipid intermediates (By similarity). Binds dansylated lipid II and catalyzes the polymerization of glycan chains. Hydrolyzes S2d (N-benzoyl-D-alanylmercaptoacetic acid) molecule, a synthetic thiolester analog of cell wall stem peptide. Active ag... |
A0A0H2ZNH9 | WALK_STRP2 | Sensor histidine protein kinase/phosphatase WalK (EC 2.7.13.3) (EC 3.9.1.-) | MLDLLKQTIFTRDFIFILILLGFILVVTLLLLENRRDNIQLKQINQKVKDLIAGDYSKVLDMQGGSEITNITNNLNDLSEVIRLTQENLEQESKRLNSILFYMTDGVLATNRRGQIIMINDTAKKQLGLVKEDVLNRSILELLKIEENYELRDLITQSPELLLDSQDINGEYLNLRVRFALIRRESGFISGLVAVLHDTTEQEKEERERRLFVSNVSHELRTPLTSVKSYLEALDEGALCETVAPDFIKVSLDETNRMMRMVTDLLHLSRIDNATSHLDVELINFTAFITFILNRFDKMKGQEKEKKYELVRDYPINSIW... | Member of the two-component regulatory system WalK/WalR that regulates genes involved in cell wall metabolism (By similarity). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to WalR (By similarity). In turn, WalR binds to the upstream promoter r... |
A0A0H2ZQL5 | CCRZ_STRP2 | Cell cycle regulator CcrZ (EC 2.7.1.15) (EC 2.7.1.229) (Cell cycle regulator protein interacting with FtsZ) | MDLGDNELTLTPIPGKSGKAYMGSYPDGKRIFVKMNTSPILPGLAREQIAPQLLWSRRLADGRDMCAQEWLTGKILTPYDMNRKQIVNILTRLHRSRPLMTQLSRLGYAMETPVDLLQSWQETAPDALRKNHFISEVMADLRQTIPGFREDHATIVHGDVRHSNWIETDSGLIYLVDWDSVRLTDRMFDVAHMLCHYISEHQWKEWLTYYGYKYNQTVLSKLYWYGQLSYLSQISKYYMNQDLENVNREIHGLRHFRDKYGKRR | Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle. May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, an... |
A0A0H3AIG7 | VGRG1_VIBC3 | Actin cross-linking toxin VgrG1 (EC 6.3.2.-) | MATLAYSIEVEGLEDETLVVRGFHGQESLSNSVFLGQACYGFRYEVQLASRVSNLTAEQMVDKRAELKLYRNSQLVQRVHGIVRAFSQGDIGHHHTFYQLTLVPALERLSLRHNSRIFQKQTVPEILSILLQEMGINDYAFALKRDGVQREFCVQYRESDIDFLHRLAAEEGLVYSFVHEAGKHTLYFSDASDSLSKLPEPIPYNALVGGAIDTPYIHGLTYRTQAEVSEVQLKDYSFKKPAYSFLQTVQGTELDYQQTRYQHFDAPGRYKDDVNGAAFSQIRLDYLRRHAHTATGQSNEPLLRAGYKFDLQEHLDPAMN... | Part of the type VI secretion system (T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (By similarity). Forms the spike at the tip of the elongating tube probably formed by hemolysin co-regulated protein/Hcp. Allows the delivery of th... |
A0A0H3AMJ9 | CHEY3_VIBC3 | Chemotaxis protein CheY-3 (Chemotaxis response regulator CheY-3) | MEAILNKNMKILIVDDFSTMRRIVKNLLRDLGFNNTQEADDGLTALPMLKKGDFDFVVTDWNMPGMQGIDLLKNIRADEELKHLPVLMITAEAKREQIIEAAQAGVNGYIVKPFTAATLKEKLDKIFERL | Acts as a response regulator to control chemotaxis. Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Switches the flagellar rotation by binding to the flagellar motor switch protein FliM. In its active (phosphorylated or acetylated) form, exhibits enhanced binding to a sw... |
A0A0H3GDH9 | PGDA_LISM4 | Peptidoglycan-N-acetylglucosamine deacetylase PgdA (Peptidoglycan GlcNAc deacetylase) (EC 3.5.1.104) (N-acetylglucosamine deacetylase Pgd) (Peptidoglycan N-deacetylase) (PG N-deacetylase) (Petptidoglycan deacetylase) (PG deacetylase) | MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQ... | Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does not deacetylate N-acetylmuramic acid (By similarity). Confers host lysozyme resistance. Critical for virulence and escape from innate immune response of the host. Required for intracellula... |
A0A0H3GGY3 | PGPH_LISM4 | Cyclic-di-AMP phosphodiesterase PgpH (c-di-AMP phosphodiesterase) (EC 3.1.4.59) | MKLAKKWRDWYIESGKKYLFPLLLVCFAVIAYFLVCQMTKPESYNVKLFQVAEKTIRSPQTVEDTEKTKEERTKASDAVEDVYVYNRETGQNRVALIQSLFAYVNEVNAEAQEKDTKNKEKAKKENKPAPAPTSTEDKLKNLKDKLSSNVSEKITSNISDEVFTTLIEAKSKDFNVMEDVVTTEVEKSMENKIRDENLNSVKIRARDDIELSAIPAYYKNVSKALVSYAIVPNEVYDEEQTDARRKEAAQSVVPVKILQGQVIVQEGQIVDRETYRQLKMLHLLDQKMPVKQYAGFAIFIIALAAILFLYTKKQTQPKAK... | A phosphodiesterase (PDE) that hydrolyzes cyclic di-3',5'-adenylate (c-di-AMP) there are at least 2 PDEs for c-di-AMP in this bacteria (this and pdeA), this may be the major PDE for growth in liquid culture. During host infection c-di-AMP is secreted into the host cytoplasm which leads to interferon-beta production and... |
A0A0H3JN63 | GATD_STAAN | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD (EC 6.3.5.13) (Lipid II isoglutaminyl synthase glutaminase subunit) (EC 3.5.1.2) | MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR | The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT. |
A0A0H3JNB0 | TARP_STAAN | Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarP (EC 2.4.1.-) (WTA glycosyltransferase) | MKKVSVIMPTFNNGEKLHRTISSVLNQTMKSTDYELIIIDDHSNDNGETLNVIKKYKGLVRFKQLKKNSGNASVPRNTGLKMSKAEYVFFLDSDDLLHERALEDLYNYGKENNSDLIIGKYGVEGKGRSVPKAIFEKGNVAKADIIDNSIFYALSVLKMFKKSVIDKNKIKFKTFSKTAEDQLFTIEFLMNSKNYSIKTDYEYYIVVNDFESSNHLSVNKSTGNQYFATINEIYKAIYKSPIYKNQEKRHQLAGKYTTRLLRHGQKKNFANSKMKYEDKIEWLNNFSKTINKVPRDSDKYVTQIFNLKLEAIRQNDLLAV... | Attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine) residues to the C3 position of poly(RboP)-wall teichoic acids (WTAs). Attenuates immunogenicity of WTA and protects S.aureus against adaptative host defenses by allowing bacteria to evade recognition by preexisting anti-S.aureus antibodies. Also protects the cell f... |
A0A0H3JPC6 | TARS_STAAM | Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS (EC 2.4.1.355) (Beta-O-GlcNAc transferase) (Beta-O-GlcNAc-WTA transferase) (WTA glycosyltransferase) (Wall teichoic acid beta-glycosyltransferase) | MMKFSVIVPTYNSEKYITELLNSLAKQDFPKTEFEVVVVDDCSTDQTLQIVEKYRNKLNLKVSQLETNSGGPGKPRNVALKQAEGEFVLFVDSDDYINKETLKDAAAFIDEHHSDVLLIKMKGVNGRGVPQSMFKETAPEVTLLNSRIIYTLSPTKIYRTALLKDNDIYFPEELKSAEDQLFTMKAYLNANRISVLSDKAYYYATKREGEHMSSAYVSPEDFYEVMRLIAVEILNADLEEAHKDQILAEFLNRHFSFSRTNGFSLKVKLEEQPQWINALGDFIQAVPERVDALVMSKLRPLLHYARAKDIDNYRTVEESY... | Attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine) residues to the C4 position of poly(RboP)-wall teichoic acids (WTAs). Mediates beta-lactam resistance in methicillin resistant Staphylococcus aureus (MRSA) strains. |
A0A0H3JRU9 | PYC_STAAM | Pyruvate carboxylase (EC 6.4.1.1) | MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAG... | Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. |
A0A0H3JUU7 | MURT_STAAN | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (EC 6.3.5.13) | MRQWTAIHLAKLARKASRAVGKRGTDLPGQIARKVDTDVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMAAGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQMDRFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAHAHEFEQSTMNESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSFDVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFETYTSDNGRMQYFKKERKEAMINLAKNPAGM... | The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue. |
A0A0H3K686 | SPA_STAAE | Immunoglobulin G-binding protein A (IgG-binding protein A) (Staphylococcal protein A) (SpA) | MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKL... | Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (By similarity). In turn, Staphylococcus aureus is pr... |
A0A0H3KB22 | QUEE_BURM1 | 7-carboxy-7-deazaguanine synthase (CDG synthase) (EC 4.3.99.3) (Queuosine biosynthesis protein QueE) | MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP | Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}. |
A0A0H3LKL4 | 6HN3M_BORBR | 6-hydroxynicotinate 3-monooxygenase (6-HNA monooxygenase) (EC 1.14.13.114) | MQGKPRIAVIGAGLGGTAGAALMARAGFNVRLYEQAPAFSRLGAGIHLGPNVMKIMRRIGIEDELNRQGSHPDYWYSRDWQSGAELARIPLGDYAVSHYGATYLTVHRGDFHALMTAALPAGLLQFNKRLTRVDEDDDVVRLHFADGSVEEAEIVIGADGVNSRLREHLLGAELPKYTGYVAHRAVFPTPLDSGSLPFDMCVKWWSDDRHMMVYFVTGKRDEIYYVTGVPEQQWDMGKSWVPSSKAEMRAAFAGWHPTVQALIEATPEVSKWPLLERDPLPLWSRGRIVLLGDACHPMKPHMAQGAAMAIEDAAMLTRIF... | Flavin-dependent monooxygenase (FMO) that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH, a step in the aerobic nicotinate degradation pathway. Is also active on the non-natural substrate 5-chloro-6-hydroxynicotinate, ... |
A0A0H3LM39 | ZIP_BORBR | Zinc transporter ZIPB (BbZIP) | MNQPSSLAADLRGAWHAQAQSHPLITLGLAASAAGVVLLLVAGIVNALTGENRVHVGYAVLGGAAGFAATALGALMALGLRAISARTQDAMLGFAAGMMLAASAFSLILPGLDAAGTIVGPGPAAAAVVALGLGLGVLLMLGLDYFTPHEHERTGHQGPEAARVNRVWLFVLTIILHNLPEGMAIGVSFATGDLRIGLPLTSAIAIQDVPEGLAVALALRAVGLPIGRAVLVAVASGLMEPLGALVGVGISSGFALAYPISMGLAAGAMIFVVSHEVIPETHRNGHETTATVGLMAGFALMMFLDTALG | Selective electrodiffusional channel that mediates the uptake of Zn(2+). Exploits in vivo zinc concentration gradients (maintained by cellular zinc homeostasis) to passively move zinc ions into the cytoplasm. ZIPB-mediated zinc flux is dependent upon pH, but independent of the proton motive force. Is also able to impor... |
A0A0H3M5A8 | PPMNT_MYCBP | Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase [Includes: Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.269); Polyprenol monophosphomannose synthase (PPM synthase) (Polyprenol-P-Man synthase) (Ppm1) (EC 2.4.1.-) (Dolichol-phosphate mannose synthase) (EC 2.4.1.8... | MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGA... | Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Transfers mannose from GDP-mannose to lipid acceptors to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacyla... |
A0A0H3MDW1 | CHXR_CHLT2 | Atypical response regulator protein ChxR (Transcriptional regulatory protein) | MAGPKHVLLVSEHWDLFFQTKELLNPEEYRCTIGQQYKQELSADLVVCEYSLLPREIRSPKSLEGSFVLVLLDFFDEETSVDLLDRGFWYLIRPITPRILKSAISLFLSQHSLHSVPESIRFGPNVFYVLKLTVETPEGSVHLTPSESGILKRLLINKGQLCLRKHLLEEIKNHAKAIVARNVDVHIASLRKKLGAYGSRIVTLRGVGYLFSDDGDKKFSQQDTKLS | May be a global positive regulator of transcription. Binds a cis-acting element of its own promoter DNA sequence and is hence probably also involved in its own transcription activation. The recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-3', where W is A/T, H is C/A/T, N is G/C/A/T and the linker length in the middle... |
A0A0H3NK84 | SSEK1_SALTS | Protein-arginine N-acetylglucosaminyltransferase SseK1 (Arginine GlcNAcyltransferase SseK1) (EC 2.4.1.-) (Salmonella secreted effector K1) | MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNII... | Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins TRADD and, to ... |
A0A0H3PEK7 | TLYA_CAMJJ | 23S rRNA (cytidine-2'-O)-methyltransferase TlyA (EC 2.1.1.226) (23S rRNA (cytidine1920-2'-O)-methyltransferase) (Hemolysin A) | MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN | Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S rRNA. Enhances motility. Enhances biofilm formation. Involved in the assembly of 70S ribosomes. Involved in virulence by promoting adherence and invasion to host cells. Involved in pathogenicity by modulating secretion of host-protective chemokine interleukin 8 ... |
A0A0H3PJK4 | DLP2_CAMJJ | Dynamin-like protein 2 (DLP2) | MQINLLNDFIKAYENTYSVSFDDSFKGRIQELCKELNEPFMHASYALENELKELVFSLDKNVNIAIIGQFSSGKSSLLNLILGRDCLPTGVVPVTFKPTFLRYAKEYFLRVEFEDGSDIITNIEKLAFYTDQRNEVKQAKSLHIFAPIPLLEKITLVDTPGLNANENDTLTTLDELKNIHGAIWLSLIDNAGKKSEEDAIKANLELLGENSICVLNQKDKLSAEELDNVLNYAKSVFLKYFNELIAISCKEAKDEQSYEKSNFQSLLDFLTQLDTTVLKEKFVKRKILNLCEILEDENQLFVGIFDRLLNQFQSYEKHLL... | The heterotetrameric DLP1(2)-DLP2(2) complex tethers liposomes and may mediate their fusion. Initial binding is probably mediated by DLP1, while DLP2 couples DLP1 subunits and increases the effective reach of the complex up to 45 nm. The role of the nucleotide is unknown. This subunit alone very weakly binds to liposom... |
A0A0H5BMX5 | TCEB1_TULGE | Tuliposide B-converting enzyme 1, amyloplastic (TgTCEB1) (EC 4.2.99.23) | MSIVSFCSSLPAGPHGFKHGRGTRDMVHMPCIVRRTARSPAQACRLLRWNKYHCAAVPTNSSLSPSPTPLDVEIELDLEPFLIKYKSGRIERLGRFGDRTDYVEASLDPATEVTSRDAITDTGVPVRIYLPKVDDSPPNSLRVLVYFHGGAFLVEDSASPPYHNYLNNLASKANILIVSVNYRLAPEYPLPVAYDDCMEALNWVNKHSDGTGQEDWINKHGDFDHLFISGDSAGGNITHNIAMSTDAPKNIEGIALVHPYFFGKVALETELQDPTNLLLHRKLWSFITPESEGLDDPRVNPLGPTAPSLEKIKCKRAVVF... | Lactone-forming carboxylesterase, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide B > 6-tuliposide A. |
A0A0J5ZXG5 | PYCC_BURCE | Uridylate cyclase (EC 4.6.1.26) (BcPycC) (Cyclic UMP synthase) (cUMP synthase) | MALADDLKKWVGETFTGKWEVQETTSVPNPEDLRLNSNHAKDLKAATVLYADLDGSTDMVNTKKWQFSAQIYKTFLKCASDIIRDEGGNITAYDGDRVMAVFTGNSKNTSAARCALKINSAVLDIIQPAIAKKWQTDFVLRHVVGIDTSQLRTARIGIRGDNDLVWIGRAANYAAKLTNLAGKPTRITADVYNKLADKLKYANGVDMWAPEHWDDMGIWTYTSTWKWTV | Pycsar (pyrimidine cyclase system for antiphage resistance) provides immunity against bacteriophage. The pyrimidine cyclase (PycC) synthesizes cyclic nucleotides in response to infection these serve as specific second messenger signals. The signals activate the adjacent effector, leading to bacterial cell death and abo... |
A0A0J9UVG7 | SIR5_FUSO4 | NAD-dependent protein deacylase SIR5 (EC 2.3.1.-) (FoSIR5) (NAD-dependent protein deacetylase SIR5) (EC 2.3.1.286) (Protein decrotonylase SIR5) (EC 2.3.1.-) | MRLLRPTPRLSSIFSSKTATSNLRFFTAMAPHNDVGAFHEALRSSKRILALCGAGLSASSGLPTFRGAGGLWRNHDATSLATLSAFKNDPGLVWLFYNYRRHMCLRAEPNPAHYALAALAEKNKDFLCLTQNVDNLSQQAGHPQDQLRTLHGSLFDIKCTNCDWIQRGNYDDPFCPALAPASVDVEPGKPFPLLDASLPLDPISPDDIPKCPQCKIGFQRPGVVWFGENLDEVMMMGITNWLLEDKVDLMLVIGTSAQVYPAAGYIDKAKRKGARIAVINPEAENEEEMYKVKPGDFAFGKDAAEYLPLLLEPVIGKLET... | NAD-dependent protein-lysine deacylase that decrotonylates the PDC (pyruvate dehydrogenase complex) subunit LAT1 at 'Lys-148' to inhibit PDC activity and consequently ATP production. Also decrotonylates histone H3 crotonylated at 'Lys-18' (H3K18cr), to repress the expression of genes involved in aerobic respiration. Ma... |
A0A0K0JFP3 | HXK_BRUMA | Hexokinase (BmHK) (EC 2.7.1.1) | MLGLLTITSVFRNWRNSLQRKEDYDECHMRGINNENEISGKSEKNFKLDEPPISLETVMAEFKLSNETLRRMMAHMSRNMDKGLEGGPENSTISMLPSFVPELPNGTEEGRFIAMDLGGTNLRVMLMDIKPGEELKTEQFNTRIPNWAMRGTGEQLFDYITKCLAEFLIEKGIENDGLPVGFTFSYPCDQKSLRSATLLRWTKGFETTGVVGEDVVELLEQSIARRGDIKVEVVALINDTVGTMVAAAHESGGECHIGVIIATGTNASYMEDTSKIKYGLSKAIAAYNYPEMIIDTEWGGFGDRSEADYILTQYDKIVDS... | Active against glucose, fructose, mannose, maltose and galactose. |
A0A0K0MJN3 | FABP4_PYGPA | Fatty acid-binding protein, adipocyte (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (AFABP) (Fatty acid-binding protein 4) | MCDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYERA | Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Has the highest binding affinity for linoleic acid and decreasing relative affinity for eicosapentaenoic acid (EPA), al... |
A0A0K0PVW1 | UGT10_PANGI | UDP-glycosyltransferase 100 (UGTPg100) (EC 2.4.1.367) | MKSELIFLPVPAFGHLVGMVEMAKLFISRHENLSVTVLISKFFIDTGIDNYNKSLLAKPTPRLTIINLPEIDPQKYLLKPRCAIFPSLIENQKTHVRDVMSRMTQSESTRVVGLLADILFVDIFDIADEFNVPTYVYSPAGAGFLGLAFHLQTLNDDKKQDVTEFRNSDTELLVPSFANPVPAEFLPSIFLEKDGRHDVLLSLYWRCREAKGIIVNTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGEGQNSDEAAVILGWLDDQPPSSVVFLCFGSFGSFPENQVKEIAMGLERSGHRFLWSLRPCISEGETTLQLK... | Component of the dammarane-type triterpene saponins (e.g. PPT-type ginsenosides or panaxosides) biosynthetic pathway. Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh1 from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to ginsenoside Rg1. |
A0A0K1YW63 | SECP_APICE | Secapin (AcSecapin-1) | MRFQVYILHLCFFILVVLTYLSQGQSYTTTTTTSTTEQPTFLQKIHETFKKVKENAKIHNLYIFDPPTWIYTTTTEKPVESTENFDITNRQLITVPVRCPPNYDFIKGRCREKIP | Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities. Displays antimicrobial activity against bacteria and fungi. Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent. The recombinant form inhibit... |
A0A0K2JL82 | CRED_STRCM | Nitrosuccinate lyase (EC 4.3.99.5) | MTRPPAPPPGAPGADELLDCGLLSPVRAGTPVEALVCDSAWLQAMLDAEAALTRAQARTGFLPAAAAEAITAAARADRIDLLAVARGARETANPVVGLVAALTAAVRRDDPAAAEYVHRGSTSQDVLDTGAMLVARRALRLIGDDLDRAADALAALAADHRDTPMAGRTLALHAVPTTFGLKAAGWLELVSEAAGRVARLRDGLPFSLGGAAGTLAGYFGDRTDRGDPAVLLDRLLDAYAAETGLARPVLPWHVLRTPVADLAAVLAFTAGALGKIAVDVQSLARTEVAEVAEPAVEGRGASSAMPHKRNPVLSTLIRSA... | Part of a gene cluster involved in the biosynthesis of cremeomycin, a light-sensitive o-diazoquinone with antibacterial and antiproliferative effects. Catalyzes the formation of nitrous acid from nitrosuccinic acid (2-nitrobutanedioate) by elimination of its nitro group. |
A0A0K2S4Q6 | CD3CH_HUMAN | Protein CD300H (CD300 antigen-like family member H) | MTQRAGAAMLPSALLLLCVPGCLTVSGPSTVMGAVGESLSVQCRYEEKYKTFNKYWCRQPCLPIWHEMVETGGSEGVVRSDQVIITDHPGDLTFTVTLENLTADDAGKYRCGIATILQEDGLSGFLPDPFFQVQVLVSSASSTENSVKTPASPTRPSQCQGSLPSSTCFLLLPLLKVPLLLSILGAILWVNRPWRTPWTES | May play an important role in innate immunity by mediating a signal for the production of a neutrophil chemoattractant. |
A0A0K3AUE4 | SEA2_CAEEL | Signal element on autosome protein 2 | MGREYKFTGIAAKLNPLNCRLKLEIAEDLDERVPTTSTSCSVASVAAATATINTTAPTVLTKSELQKTLQKTSSSFSSSLATTTTTSSHLNAPVESMEGHSSLASYSHHHPSSSHHHHPGQQQSSSSSSSSHLQDFQSPPSASHPYYHQQQPQHQHQQAQQYGQATGSTNGGGQQQMTSMYGGNDYDQHQLHHQNQQHQASTSTQQFHHPQRPPPPQYDQPSSSTGSSLPPLHTVRYEQLPPPPSNQRTPTQQLQYPVKVVEAGGQAYAQQVQQAQQSNRSGAAGVNSALQPKPLPPLSSITSISSSAAGSSISAPSTSQ... | RNA-binding protein, which regulates the expression of proteins required to control developmental timing of events during the L2 to L3 larval stage switch. Binds to the 3'UTR of the transcript of the heterochronic protein lin-28 to post-transcriptionally negatively regulate its expression in certain tissue types in the... |
A0A0K3AUJ9 | PRDX_CAEEL | Peroxiredoxin prdx-2 (EC 1.11.1.24) (2-Cys peroxiredoxin 2) | MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide. In the intestine, plays a role in protecting cells against oxidative st... |
A0A0K3AV08 | MLK1_CAEEL | Mitogen-activated protein kinase kinase kinase mlk-1 (EC 2.7.11.25) (Mixed lineage kinase homolog 1) | MEQASVPSYVNIPPIAKTRSTSHLAPTPEHHRSVSYEDTTTASTSTDSVPEVRIRSESSQVSRESPPIRASKAFVASYEYEAQKDDELNLPLGAIITLVTVETNEDGWYRGELNGKVGLFPSNYAREVTYKDNLVEFKQDEIMLPVAVRTLSDCQIGHGATATVFKMDIKIKKELQNGRMGEAVGDQMKAALKRFNRHASNFRADVVSTDEQLEQLKREANLVNGLSHNNIVRLLGICLEDPYFGLLLELCEGSSLRNVCRNLNSDAAIPLGVLIDWATQVAEGMEYLTKQGYVHRDLKADNVLVKEEVCLCMDEEMFQY... | Serine/threonine-protein kinase which, by phosphorylating and activating mek-1, plays an important role in the activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1. Involved in the response to environmental stress such as heavy metals. By activating the JNK pathway downstream of tyrosine receptor svh-2, pla... |
A0A0K3AWM6 | MOM5_CAEEL | Protein mom-5 | MHRHILILFLFGCLSADQRLSSTSISSMNGFSTTRKCEHITIPMCKNLDYNQTVFPNLLGHTTQSEAGPAIAQFNPLIKVKCSEDIRLFLCTVYAPVCTVLEKPIQPCRELCLSAKNGCESLMKKFGFQWPDQLDCNKFPVTDLCVGKNSSESSNSKNYRSSNDVTFGVSTIANEVVLSPKKCPHHMHTTSGSHFSLPLLSGRLPECSLTCEADNQVPMMFDGRVRRILRIWTAAWSVACFVCSLFTLVTFLVDLSRFAYPVRPILYLAFCYLAISTVYMIGVVGEDGFACGTYGSTPTTLVTQGGENVGCSALAVVHYF... | Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of gsk-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (Probable). A second signaling pathway involving PKC a... |
A0A0K3AXH1 | ARID1_CAEEL | AT-rich interactive domain-containing protein arid-1 | MSDDPAFLALGTEVSAKFKGAYCEAKIQKVDRSLKVKVSLKESPFGQMIVQDNDLPNAKFEINELTDVVFQRKFIRCQIQSIKDQSKYHVVFNDGDEKELRRTQLVLKGGKHFAADGNLDSMPLTNPESFSTPVIRGAAKRGAQKIRNAISEASGSRGGAVLLHNDDDENDEEDQEDGENEEDADDDDDDTEEQQQPRERRRAAAISAIGVLKKAIEDTQSEESSADSSEERERARSRRKRKDEASSAVTSDEEDQEDLATTDSENPVINGASSAAALSKTLQRKLEKQAMKREKQRLKEEEREEKLRLKEENREKKRRE... | DNA-binding protein which modulates activity of several transcription factors (By similarity). Plays a role in the modulation of endoplasmic reticulum (ER) homeostasis during chemical and pathogen stress, including exposure to the Gram-negative bacterium P.aeruginosa. |
A0A0K8P6T7 | PETH_IDESA | Poly(ethylene terephthalate) hydrolase (PET hydrolase) (PETase) (EC 3.1.1.101) (PET-digesting enzyme) | MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS | Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET. Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthala... |
A0A0K8P8E7 | MHETH_IDESA | Mono(2-hydroxyethyl) terephthalate hydrolase (MHET hydrolase) (MHETase) (EC 3.1.1.102) | MQTTVTTMLLASVALAACAGGGSTPLPLPQQQPPQQEPPPPPVPLASRAACEALKDGNGDMVWPNAATVVEVAAWRDAAPATASAAALPEHCEVSGAIAKRTGIDGYPYEIKFRLRMPAEWNGRFFMEGGSGTNGSLSAATGSIGGGQIASALSRNFATIATDGGHDNAVNDNPDALGTVAFGLDPQARLDMGYNSYDQVTQAGKAAVARFYGRAADKSYFIGCSEGGREGMMLSQRFPSHYDGIVAGAPGYQLPKAGISGAWTTQSLAPAAVGLDAQGVPLINKSFSDADLHLLSQAILGTCDALDGLADGIVDNYRAC... | Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with PETase to depolymerize PET. Catalyzes the hydrolysis of mono(2-hydroxyethyl) terephthalate (MHET) into i... |
A0A0L7KF24 | FCLN_PLAFX | Falcilysin (EC 3.4.24.-) | MNLTKLMKVFGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQ... | In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains. In the apicoplast, degrades apicoplast transit peptides after their cleavage (B... |
A0A0M3Q1Q3 | GTPS1_THYVU | Gamma-terpinene synthase 1 (EC 4.2.3.114) (Alpha-terpinene synthase 1) (EC 4.2.3.115) (Terpene synthase 1) (TvTPS1) | MRRSGNYQAPVWNNDFIQSFSTDKYKDEKFLKKKEELIAQVKVLLNTKMEAVKQLELIEDLRNLGLTYYFEDEFKKILTSIYNEHKGFKNEQVGDLYFTSLAFRLLRLHGFDVSEDVFNFFKNEDGSDFKASLGENTKDVLELYEASFLIRVGEVTLEQARVFSTKILEKKVEEGIKDEKLLAWIQHSLALPLHWRIQRLEARWFLDAYKARKDMNPIIYELGKIDFHIIQETQLQEVQEVSQWWTNTNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYDTLDELQLFTDAIRKWDVE... | Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents. Monoterpene synthase which catalyzes the conversion of geranyl diphosphate (GPP) to gamma... |
A0A0N7CSQ4 | TX41A_SCOMU | Tau-scoloptoxin(04)-Sm1b (Tau-SLPTX(04)-Sm1b) (Toxin RhTx2) [Cleaved into: Tau-scoloptoxin(04)-Sm1a (Tau-SLPTX(04)-Sm1a) (Toxin RhTx)] | MLKSFCILSVFMVLFLAKFPDLCSGEEISPLKIVVRNSEYLNNPCNGVTCPSGYRCSIVDKQCIKKEK | [Tau-scoloptoxin(04)-Sm1a]: Extremely potent agonist and potentiator of TRPV1 (EC(50)=470-521.5 nM (mouse)). It strongly promotes the heat activation process by downshifting the activation threshold temperature. It preferably binds to the activated channel and promotes its opening. Holding the channel closed by cooling... |
A0A0N7KJT8 | APL25_ORYSJ | APETALA2-like protein 5 (Protein SHATTERING ABORTION 1) | MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGAGSDQRV... | Transcription factor. Involved in spikelet transition and development (Probable). Prevents lemma and palea elongation as well as grain growth. Required for seed shattering through specifying abscission zone (AZ) development. |
A0A0N9E2K8 | MMP21_DANRE | Matrix metallopeptidase-21 (MMP-21) (EC 3.4.24.-) | MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHI... | Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. |
A0A0N9HMN6 | POMT3_SINHE | Pluviatolide O-methyltransferase (PhOMT3) (EC 2.1.1.323) | MEMAPTMDLEIRNGNGYGDSGEELLAAQAHIYNHIFNFISSMALKCAVELNIPEILHNHQPKAVTLSELVQALQIPQAKSACLYRLLRILVHSGFFAITKIQSEGDEEGYLPTLSSKLLLKNHPMSMSPCLLGLVNPTMVAPMHFFSDWFKRSDDMTPFEATHGASLWKYFGETPHMAEIFNEAMGCETRLAMSVVLKECKGKLEGISSLVDVGGGTGNVGRAIAEAFPNVKCTVLDLPQVVGNLKGSNNLEFVSGDMFQFIPPADVVFLKWILHDWNDEECIKILKRCKEAIPSKEEGGKLIIIDMVVNDHNKGSYEST... | O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the methylation of (-)-pluviatolide to produce (-)-bursehernin. |
A0A0N9HTA1 | DOMT1_SINHE | Desmethyl-yatein O-methyltransferase (EC 2.1.1.330) | MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDY... | O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein. |
A0A0N9NCU6 | YOPJ_YERPU | Serine/threonine-protein acetyltransferase YopJ (EC 2.3.1.-) (Virulence factor YopJ) | MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV | Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins. Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B ki... |
A0A0P0VIP0 | LRSK7_ORYSJ | L-type lectin-domain containing receptor kinase S.7 (OsLecRK-S.7) (EC 2.7.11.1) (Protein DEFECTIVE IN APERTURE FORMATION 1) (OsDAF1) | MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPH... | Legume-lectin receptor-like kinase required for normal pollen development and male fertility. Regulates pollen exine assembly and aperture development. Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum. May function by regulating th... |
A0A0P0WGX7 | ENL1_ORYSJ | SNF2 domain-containing protein ENL1 (EC 3.6.4.-) (Protein ENDOSPERMLESS 1) | MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLA... | DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm. Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nuclear cycles. |
A0A0P0X9Z7 | CWZF7_ORYSJ | Cysteine-tryptophan domain-containing zinc finger protein 7 (OsCW-ZF7) (Protein WIDE GRAIN 7) | MLSVRRRQEDARGVGLRGGAAAGGMEDDAELEEGEACGDETAFVDPDVALSYIDEKIQDVLGHFQKDFEGAVSAENLGSKFGGYGSFLPTYQRSPLPQTRSPPKAANVSSRSPYHQPTESMSQNTLAVAAPSVSKHNGSMVPLSDDSSKKEVHQSTKVERASSTQDSLNGLSKSSDHNRFKVRIKVGSDNGLARNNAAIYSGLGLDISSPSSIEDSPDGCGSLSPEFNNVPIESPRTILQIMTCFSVPGGFLLSPLRDDLVQLTQKVVPTSKKWETNANTENVQERYEGYAAKRVKSDAKKKKAVDTKRSKSRNDVSAVM... | Transcriptional activator that acts as a positive regulator of grain size. Binds directly to the DNA core sequence 5'-CATTTC-3' found in the promoter of MADS1, and activates MADS1 transcription. Increases grain width via direct up-regulation of MADS1 expression. Promotes active chromatin modification at the MADS1 locus... |
A0A0P0XCU3 | SSY3A_ORYSJ | Soluble starch synthase 3a, chloroplastic/amyloplastic (EC 2.4.1.21) (Protein FLOURY ENDOSPERM 5) (Soluble starch synthase IIIa) (OsSSIIIa) | MEMALRPQSLLCPRSRLKVVIRPASSASGGGLAQYFLMTRRYTGSRIVRCMVSSSDCPNRKAKRTISLHTEVASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEWKKLDTTEVDLSQDVSSSSMRKVDATDEAKLDILEDDLPRNLLNGVTMGEVDMLDEAGAEDDVFEVDLSALHNSTVGKMDAVNEVGTENDLFEVDLSALHSAAVGKVDVVDGAKAKEDLFEMDSLALHSVTMGKVDAINAAGAEGDKFEVDLSALASNNSMIEAVNVMDEAKAIEDTLEVDLSGNATSSSTYGEVKFEVDSLGNTS... | Involved in starch synthesis in endosperm amyloplasts. Plays an important role in the elongation of amylopectin B chains. |
A0A0P0XII1 | CERK1_ORYSJ | Chitin elicitor receptor kinase 1 (OsCERK1) (EC 2.7.11.1) (LysM domain receptor-like kinase 1) (LysM RLK1) (LysM-containing receptor-like kinase 1) (LysM domain receptor-like kinase 9) (OsLysM-RLK9) | MEASTSLLVLVLAAAAFAAGTVTEAAGDGCSAGCDLALASFYVTPNQNVTNMADLFGIGAANYRSLAPYNPNIPNLDFINVGGRVNVYFTCGCRSLPGSPGATYLAGAFPFQMSRGQIYTSVAANYNNLTTAEWLQATNSYPANNIPDTAVINATVNCSCGDASISPDYGLFLTYPLRAEDTLASVAATYGLSSQLDVVRRYNPGMESATGSGIVYIPVKDPNGSYLPLKSPGKGASAGAIAGGVVAGVVVLAAIFLYIIFYRRRKAKQATLLQSSEDSTQLGTISMDKVTPSTIVGPSPVAGITVDKSVEFSYEELSNA... | Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses. Involved in the resistance to pathogenic fungi, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated... |
A0A0P0ZBS7 | MENC_GEOSE | o-succinylbenzoate synthase (OSB synthase) (OSBS) (EC 4.2.1.113) (4-(2'-carboxyphenyl)-4-oxybutyric acid synthase) (N-acylamino acid racemase) (NAAAR) (N-succinylamino acid racemase) (NSAAR) (NSAR) (EC 5.1.1.-) (o-succinylbenzoic acid synthase) | MAINIEYVILRHLQMELKAPFTTSFGTFQRKELILVEVVDRDGVSGWGESVAFSAPWYSEETVKTNWHMLEDFLVPLALAEPIHHPEELSKRFSAIRQNNMAKAALEGAVWDLYAKRLGVPLSQALGGAKKDIEVGVSIGIQPTVADLLQVIERYVAQGYRRIKVKIKPSWDVDVIREVRRVFPDVPLMADANSAYTLVDADRLKALDEFGLLMIEQPLAADDLVDHARLQPLLQTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLGEAKRIHDLCAERGAPVWCGGMLEAGVGRAHNIAITTLENFTLPGDTA... | Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-D/L-phenylalanine. Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl... |
A0A0P6JG37 | ASAH1_HETGA | Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta] | MLGRSRLTFVLLAAAVTCAEAQHAPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKGPMLKIIVNSFKNMVNTFVPSGKVMQMVDQKLPDLLGQFSGPYEEEMKGIADVTEIPLGEIISFNIFYELFTMCTSIITEDKKGHLLHVRNMDFGIFLGWNINNNTWVITEELKPLTVNLDFQRNSKTVFKATSFAGYVGMLTGFKPGQFSLTLNERFSMNGGYLGLLEWILGKKDASWIGFITRSVLENATSYEEAKNILAKTKLLAPAYFILGGNQSGEGCVITRERKDSLDIYELDPKQGRWYVVQTN... | Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell... |
A0A0R4I9Y1 | R213B_DANRE | E3 ubiquitin-protein ligase rnf213-beta (EC 2.3.2.27) (EC 3.6.4.-) (E3 ubiquitin-lipopolysaccharide ligase rnf213-beta) (EC 2.3.2.-) (Mysterin-B) (Mysterin-beta) (RING finger protein 213-B) (RING finger protein 213-beta) | MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTME... | Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS)... |
A0A0R4IBK5 | R213A_DANRE | E3 ubiquitin-protein ligase rnf213-alpha (EC 2.3.2.27) (EC 3.6.4.-) (E3 ubiquitin-lipopolysaccharide ligase rnf213-alpha) (EC 2.3.2.-) (Mysterin-A) (Mysterin-alpha) (RING finger protein 213-A) (RING finger protein 213-alpha) | MKCPKCSHEALEKAPKFCSECGHKLQSQSYETTQGTPHDKSQTPSIVPQITNAEMDETGSESKSLEIQNANVSPKRPNENTSPNPKKKKRKKRKKEKKKKSGVSEGPSSLTSDLSDISLTDKEKKMDTDQSSDSDCSSCIVEDTPTPAEPSSHLSPPENETAGPAQLSASALTTGSSKDGEESIGTTQKPVSASASKAPLGVDQQTKEEKVKCKDEGQKSLSAKAQHTPNANVDQNANVQSDANIDKDSQNVEPQKSSSVKTKPSKSTVADPKKTESEKQKSGERDNENSTQPVSSPKLKRNQTEESQKMVFGPNSAPKK... | Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (By similarity). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopoly... |
A0A0R4IDP3 | ZH15A_DANRE | Palmitoyltransferase ZDHHC15A (EC 2.3.1.225) (Acyltransferase ZDHHC15A) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 15A) | MLLPACLRRCARLLFWIPVLVVIVVVMWSYYAYVVHFCWILLSSATQRVVFLCLFHLCFGMFSWSFWKAVSTPPSSPSVEFQFSTSDSLLYELERDDVAKSPILLEISQKLPVHTRTATGAIRFCHHCQLIKPDRCHHCSVCQTCVLKMDHHCLWLNNCMGFSNYKFFMLFLLYSLLYCLLIVSTVTPTVIQLWRGRLFDSCVKLHVLFLTLVSAIFAITLCFLLIFHIWLLTSNKTTLEWLSVPFFANGPGSKAFDVGVQANFLQVFGKKKRLWLFPVFSSEGDGHSFPLSCQMSSHGPPVMNGHERCATLRTVASPKE... | Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (By similarity). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). May thereby regu... |
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