Datasets:
Synthyra
/
SwissProt

Dataset card Data Studio Files Community
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Entry
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Entry Name
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11
Sequence
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2
35.2k
EC number
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7
118
⌀
Cofactor
stringlengths
38
1.77k
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Gene Ontology (biological process)
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18
11.3k
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Gene Ontology (cellular component)
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17
1.75k
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Gene Ontology (molecular function)
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24
2.09k
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Pfam
stringlengths
8
232
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Gene3D
stringlengths
10
250
⌀
Protein families
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9
237
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Post-translational modification
stringlengths
16
8.52k
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Subcellular location [CC]
stringlengths
29
6.18k
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Catalytic activity
stringlengths
64
35.7k
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Kinetics
stringlengths
69
11.7k
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Pathway
stringlengths
27
908
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pH dependence
stringlengths
64
955
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Temperature dependence
stringlengths
70
1.16k
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Function [CC]
stringlengths
17
15.3k
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Organism
stringlengths
8
196
C5H8J1
EME1B_ARATH
MNDHILISDGEDQTTPLPSLSKRARKYPISAILISDSDPTPQKQPPESSFTPIFVPETPLSDDFSVVKCSFGSRALASNREDKFSGKRIISLDSEFEDSPRPETSKKNESVLAGLREPRFGLEAETSEAYYKNTRIPETNLDDDTSWMHEVSFRSSPTNDTIEVVSDQEKEDISVEKIGRKKKIRTTTLPVPGEALPKKRQSKEDKTSAMEEKKLRKEQERLEKAASKAEEAERKRLEKEKKKWEKGKLALKSIVAEIDTKVLEGSIGGLLLSRFSEKGITIHVGPNPIERSIVWTMTIPEDIAPLFPQGPKIPYLLLVYDAEEFCNLVANGKFLEIISRVQDRYPSYTVCCLTNKLMSYVKKREKEEYKNPGNWRRPPIDEVLAKLTTHYVKVHSRHCVDEAEVAEHIVGLTSSLASCQFRKKLTMLSVSANGALVSKDSVDKHLIKKSPWLKALVAIPKVQPRYALAVWKKYPSMKSLLKVYMDRNKSVHEKEFLLKDLKVEGLVGGDIRLGEICSKRIYRVLMSHDGAIKTDDVENGAAFFTDSPGVN
3.1.22.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
cell division [GO:0051301]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712]
Holliday junction resolvase complex [GO:0048476]; nucleus [GO:0005634]
crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]
PF21292;PF02732;
3.40.50.10130;1.10.150.670;
EME1/MMS4 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference. {ECO:0000269|PubMed:19339504}.
Arabidopsis thaliana (Mouse-ear cress)
C5I9W9
WTS_ARATH
METVSAVNQTLPISGGEPVKFTTYSAAVHKVLVMINAGILGLLQLVSQQSSVLETHKAAFLCFCVFILFYAVLRVREAMDVRLQPGLVPRLIGHGSHLFGGLAALVLVSVVSTAFSIVLFLLWFIWLSAVVYLETNKPSACPPQLPPV
null
null
calcium ion transport [GO:0006816]; defense response to fungus [GO:0050832]; monoatomic cation transport [GO:0006812]; protein complex oligomerization [GO:0051259]; response to fungus [GO:0009620]; sodium ion transport [GO:0006814]
endoplasmic reticulum membrane [GO:0005789]
calcium channel activity [GO:0005262]; monoatomic cation channel activity [GO:0005261]; protein self-association [GO:0043621]; sodium channel activity [GO:0005272]
null
null
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:37295403}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:37295403}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:37295403};
null
null
null
null
FUNCTION: Calcium-permeable cation-selective channel conferring a broad-spectrum clubroot resistance by supporting cytosolic Ca(2+) increase in root pericycle cells (PubMed:37295403). Triggers immunity toward fungal pathogens such as Plasmodiophora brassicae (Pb) and induces defenses (PubMed:37295403). Also permeable to sodium ion Na(+) and possibly other cations (PubMed:37295403). {ECO:0000269|PubMed:37295403}.
Arabidopsis thaliana (Mouse-ear cress)
C5I9X1
ALDH1_ARTAN
MSSGANGSSKSASHKIKFTKLFINGEFVDSISGNTFDTINPATEEVLATVAEGRKEDIDLAVKAAREAFDNGPWPRMSGEARRKIMLKFADLIDENADELTTLEVIDGGKLFGPVRHFEVPVSSDTFRYFAGAADKIRGATLKMSSNIQAYTLREPIGVVGHIIPWNGPAFMFATKVAPALAAGCTMVIKPAEHTPLTVLFLAHLSKLAGVPDGVINVVNGFGKTAGAAVSSHMDIDMVTFTGSTEVGRTVMQAAALSNLKPVSLELGGKSPLIVFDDADVDKAAEFAILGNFTNKGEMCVAGSRVFVQEGIHDVFVKKLEGAVKAWATRDPFDLATRHGPQNNKQQYDKVLSCINHGKKEGATLVTGGKPFGKKGYYIEPTLFTNVTDDMTIAKEEIFGPVISVLKFKTVEEVIKRANATKYGLASGVFTKNIDVVNTVSRSIRAGAVWVNCYLALDRDAPHGGYKMSGFGREQGLEALEHYLQIKTVATPIYDSPWL
1.2.1.-
null
null
cytosol [GO:0005829]
aldehyde dehydrogenase (NAD+) activity [GO:0004029]
PF00171;
null
Aldehyde dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20000}.
CATALYTIC ACTIVITY: Reaction=(+)-artemisinic aldehyde + H2O + NADP(+) = (+)-artemisinate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64688, ChEBI:CHEBI:64782; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60681; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=(11R)-dihydroartemisinic aldehyde + H2O + NADP(+) = (11R)-dihydroartemisinate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64691, ChEBI:CHEBI:143905; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60685; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=(11R)-dihydroartemisinic aldehyde + H2O + NAD(+) = (11R)-dihydroartemisinate + 2 H(+) + NADH; Xref=Rhea:RHEA:60688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64691, ChEBI:CHEBI:143905; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60689; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) + octanal = 2 H(+) + NADPH + octanoate; Xref=Rhea:RHEA:59904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59905; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=(E)-non-2-enal + H2O + NADP(+) = (E)-non-2-enoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142592, ChEBI:CHEBI:143908; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60693; Evidence={ECO:0000269|Ref.1};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.58 uM for artemisinic aldehyde (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; KM=8.79 uM for dihydroartemisinic aldehyde (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=11.1 nmol/min/mg enzyme with artemisinic aldehyde as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=17.3 nmol/min/mg enzyme with 2-nonenal as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=11.6 nmol/min/mg enzyme with octanal as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=0.05 nmol/min/mg enzyme with sinapaldehyde as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=0.02 nmol/min/mg enzyme with 2-phenylpropanal as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=72 nmol/min/mg enzyme with dihydroartemisinic aldehyde as substrate (in the presence of NAD) {ECO:0000269|Ref.1}; Vmax=75 nmol/min/mg enzyme with dihydroartemisinic aldehyde as substrate (in the presence of NADP) {ECO:0000269|Ref.1}; Note=kcat is 1.53 sec(-1) with artemisinic aldehyde as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) (Ref.1). kcat is 7.74 sec(-1) with dihydroartemisinic aldehyde as substrate (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) (Ref.1). {ECO:0000269|Ref.1};
PATHWAY: Sesquiterpene biosynthesis. {ECO:0000303|PubMed:30468448}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|Ref.1};
null
FUNCTION: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:27488942, Ref.1). Catalyzes the NAD(P)-dependent oxidation of artemisinin precursors, artemisinic and dihydroartemisinic aldehydes, thus producing artemisinic and dihydroartemisinic acids, respectively (Ref.1). Can use both NAD and NADP as proton donors (Ref.1). {ECO:0000269|Ref.1, ECO:0000303|PubMed:27488942}.
Artemisia annua (Sweet wormwood)
C5JKE6
ARO1_BLAGS
MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDERIRKLTADKHCSVEQLITYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKNLNVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWENEGEVLVVNGKGGKMKASPDELYLGNAGTASRFLTTVATLAQKSSVDSSVLTGNARMKQRPIGDLVDALAANGAGVEYLENSGSLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKKPVTLRLVGGKPISQTYIDMTTTMMRSFGIDVKKSETEEHTYHIPLGFYISPAEYIVESDASSSTYPLAVAAITGTSCTVPNIGSKSLQGDARFAVEVLRPMGCTVDQKDFSTTVTGPANGILRPLPNVDMEPMTDAFLTASVLAAVARGGGSNHTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPSDGVYCYDDHRVAMSFSVLSLVAPQPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVEKKTGTGGIVHLDKPAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWEGFREAELSLLRRVMTEKPTGYIFACGGGIVETPEARKLLIQYHKTKGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNVQYFSRLTGLDGMAQVLGGFNRFLKVITGQVDSLAQMRSKENTFFVSLTLPDLAPAAPILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRTSVPLVFTIRTKAQGGRFPDDAYDAALQLYRLAIRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGELSWANGSWIQFYNKALQYGDVIKLVGVARSLDDNASLKKFKTWAEEKHDVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKSKKFAVIGNPVSASRSPAMHNALFRQMGLPHTYGTLETEDPEIVKKFIRSPDFGGASITIPLKLDIMPLLDEIAPEAVSIGAVNTIVCAPPAPDDQSQAPRLIGRNTDWQGMVRCLSDAGAYPAATPTTTSAGLVIGGGGTARAAIFALQSMGYSPIYVVGRSPDKLSSMTSTFAPDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREVLCELFDLCEKANSDAEQARGISTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTDITPVYEDARNAVMGVQPKDDDIST
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis)
C5M1X2
ARO1_CANTT
MSIEKVPILGKETIHVGYGIQDHIVTEVVDNLASSTYVIVTDTNVEKTPQFSKLTNDFTKVLNEKRPDSRVLTYSVPPGENNKNRATKAAVEDFLLQQGCTRDTVIIAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPQYVFIDVSYLESLPTRQFINGMAEVVKTAAIWNEEEFTRLENFSKQFLSVVTAKNPDLLSIKEELVKTVLESVRVKAEVVSSDEKESSLRNLLNFGHTIGHAIEAIVTPEALHGECVSIGMIKEAELARYLGILPPVAVARLSKCLVAYGLPVTIDDKLFLQRVGPKRHNIEIDLLLKKMSIDKKNDGSKIRSVILESIGKCYQLKAHEVSKQDLTFVLTDEVLVHPFKQPPQENVITPPGSKSISNRALILAALGTGTVRIKNLLHSDDTKHMLAAVAALKGAEITTEDNGETIVLKGNGGDLVTCDEELYLGNAGTASRFLTTVASLVGKSESNDHVVLTGNARMQERPIGPLVDALRSNGSEVQYLNKEGSLPLKITAGNGLKGGRIELAATISSQYVSSILMCAPYAKEPVTLALVGGKPISQLYIDMTCAMMKSFGIEVTKSTTEDYTYHIPKGTYKNPAEYVIESDASSATYPLAFAAMTGTSCTVPNIGSSSLQGDARFAVDVLKPMGCKVEQTATSTTVTGPPRGQLKPLPHVDMEPMTDAFLTASVVAAVAQGDSSTTITGIANQRVKECNRIEAMITELAKFGVKADELPDGIEIHGIDIADLKTPSIEKRGVCSYDDHRVAMSFSLLSGLCKEPVLILERSTTGKTWPGWWDILHSKFNIELDGYEPPFGTDKEGTKASDKSIIIIGMRGTGKSTLSEWLASFMGFKSLDMDVYLEEKLGNDIKSLIKEKGWEYFREQEAAIAKECFSKFSKGYVLSTGGGIVEGAENRQRLKDYITAGGIVLHLHRDLEETVSFLSVDTTRPAYTSEVKEVWLRREQWYDDCSNYHFYSSHCNTEEEFDHLRKSFVNFIKIITGTEKASIPSGRSAALSLTVPDLNAISSQLGDIAVGAEAVELRVDLLKETSSSFIADQIAVIRKHIDLPIIYTVRTESQGGKFPDNKVEELRNLLLLGVKLGVAFIDVELTAPVEVIEEIIIKKGYTRVIASYNDIAGKLGWSNVEWTNKYNQGVSINADIVKLIGRASSLQDNLELEVFRKQNTLKPLLAVNLGSQGKLSQVLNTIFTPITQESLPNEDGLLTIKEINQIYFDIGGLTAKKFWVIGSPIQHSRSPNLHNAAYKALNLPFTFDRFESTDADQVYKELINKPDFGGLAITMPLKLDIMKYATELSDAAQKIGAVNTLVPLEGGYLGDNTDWVGITSSFTRAGVPPNPRVNGLVIGAGGTSRAAIYALHQIGCEKIYLANRTTSKLNEIKDSFPKEYNLEVLETEDQAEKAQNVGLAVSCVPADKPLDESLLQKVEKILANGEKSSNGFKSTLLEASYKPRVTPMMKIADEKFKWRAIPGVEMLVNQGDRQFQIHTGFTAPYDVIHRAVVEE
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
C5MSH2
POLG_SALVA
MEGSNGFSSSLAGLSSSRSSLRLLTHFLSLPTLPVNIYLNARRHSGWYRSPPTLPVNIYLNEQFDNLCLAALRYPGHKLYPSVHTLFPDVSPLKIPHSVPAFAHLVQRQGLRRQGNSITNIYGNGNDVTTDVGANGMSLPIAVGDMPTASTSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGAAKLSNKLSGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTLSWSETIAPLTVFSGPKALTPGVYPPTIEPNTGVYPLPAALCVSHPESVFSTAYNAHAYFNCGFDVTVVVNASQFHGGSLIVLAMAEGLGDITPADSSTWFNFPHTIINLANSNAATLKLPYIGVTPNTSTEGLHNYWTILFAPLTPLAVPTGSPTTVKVSLFVSPIDSAFYGLRFPVPFPAPQHWKTRAVPGAGTYGSVVAGQEIPLVGYAPAAPPRDYLPGRVHNWLEYAARHSWERNLTWTSADEVGDQLVSYPIQPEALANTQTNTAFVLSLFSQWRGSLQISLIFTGPAQCYGRLLLAYTPPSANPPTTIDEANNGTYDVWDVNGDSTYTFTIPFCSQAYWKTVDIGTSSGLVSNNGYFTVFVMNPLVTPGPSPPSATVAAFLHVADDFDVRLPQCPALGFQSGADGAEVQPAPTSDLSDGNPTTDPAPRDNFDYPHHPVDPSTDLAFYFSQYRWFGLNESLTPLDATGGLFYHISLNPINFQQSSLLSVLGAFTYVYANLSLNINVSAPSQPCTFYVFYAPPGASVPSVQTLAELSFFTHTATPLNLAAPTNITVSIPYSSPQSVLCTSFGGFGLQNGGDAGNLHSNTWGTLILYVDLPQSDSVSVSAYISFRDFEAYVPRQTPGVGPVPTSTSIVRVARPTPKPRTARRQGGTLADLILSPESRCFIVAHTTAPFYSILLVNPDEEYAISMFSHGDESILQYSSRSGTRLTPTAPAFFLCAAASVDTVLPYSISQSHLWLTDLTGIPLRAVPPLTLFLSAGAALCAGAQTLIAVAQGGSTPETPPTPNRALLRRQGLGDLPDAAKGLSAALESVARVAGDANIATSSQAIATSINSLSNSIDGATSFMQNFFSGLAPRNPTSPLQHLFAKLIKWVTKIIGSLIIICNNPTPSALIGVSLMLCGDLAEDITEFFSNLGNPLAAVFYRCARALGLSPTPQSAAQAAGGRQGVRDYNDIMSALRNTDWFFEKIMTHIKNLLEWLGVLVKDDPRTKLNGQHEKILELYTDSVTASSTPPSELSADAIRSNLDLAKQLLTLSHAANSVTHIQLCTRAITNYSTALSAISLVGTPGTRPEPLVVYLYGPPGTGKSLLASLLASTLAQALSGDPNNYYSPSSPDCKFYDGYSGQPVHYIDDIGQDPDGADWADFVNIVSSAPFIVPMADVNDKGRFYTSRVVIVTSNFPGPNPRSARCVAALERRLHIRLNVTARDGVAFSAAAALQPSNPPSATRYCKFANPLTQFSMFNLAVDYKSVVLPNTPLTCFDELVDFVLSSLRDRASVNSLLSGMVRTDVTRQGGNADAPAPSAAPLPSVIPSVPSQDPFTRAVNENRPVSFLSKIWSWRAPIFAASSFLSLIAATLTIVRCLRDLRSTQGAYSGTPVPKPRKKDLPKQPVYSGPVRRQGFDPAVMKIMGNVDSFVTLSGTKPIWTMSCLWIGGRNLIAPSHAFVSDEYEITHIRVGSRTLDVSRVTRVDDGELSLLSVPDGPEHKSLIRYIRSASPKSGILASKFSDTPVFVSFWNGKSHSTPLPGVVDEKDSFTYRCSSFQGLCGSPMIATDPGGLGILGIHVAGVAGYNGFSARLTPERVQAFLSHLATPQSVLYFHPPMGPPAHVSRRSRLHPIPPAFGAFPITKEPAALSRKDPRLPEGTDLDAITLAKHDKGDIATPWPCMEEAADWYFSQLPDNLPVLSQEDAIRGLDHMDAIDLSQSPGYPWTTQGRSRRSLFDEDGNPLPELQEAIDSVWDGGSYIYQSFLKDELRPTAKARAGKTRIVEAAPIQAIVVGRRLLGSLINHLQGNPLQHGSAVGCNPDIHWTQIFHSLTSFSNVWSIDYSCFDATIPSVLLSAIASRIAARSDQPGRVLDYLSYTTTSYHVYDSLWYTMIGGNPSGCVGTSILNTIANNIAVISAMMYCNKFDPRDPPVLYCYGDDLIWGSNQDFHPRELQAFYQKFTNFVVTPADKASDFPDSSSIFDITFLKRYFVPDDIHPHLIHPVMDEQTLTNSIMWLRGGEFEEVLRSLETLAFHSGPKNYSAWCEKIKAKIRENGCDATFTPYSVLQRGWVSTCMTGPYPLTG
2.7.7.48; 3.4.22.28; 3.6.4.13
null
DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
PF00680;PF00073;PF00910;
1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10;
null
PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The leader protein-VP0 junction is cleaved by 3C proteinase (By similarity). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (By similarity). {ECO:0000250|UniProtKB:O91464, ECO:0000250|UniProtKB:P03300}.; PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.
SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Single-pass membrane protein {ECO:0000255}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:O91464}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P03300};
null
null
null
null
FUNCTION: [Leader protein]: Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Protein 2A]: Required for viral RNA replication (By similarity). Does not have any proteolytic activity (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Protein 2B]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. {ECO:0000250|UniProtKB:P03304}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity). {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity). {ECO:0000250|UniProtKB:P12296}.
Salivirus A (isolate Human/Nigeria/NG-J1/2007) (SV-A)
C5PA86
ARO1_COCP7
MAAPTTIKILGRDSIVADFGIWKRHVADDLLTNCSSSTYILISDTTLTPLYVPSFQAAFENAASGLTPKPRLLTYAIPPGELSKSRQTKADIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPHGKNLIGAIWQPQKIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEDFAALEKNADAILSAVKSENTPERPRFGGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGLLKNVAVPRLVKCLASYGLPTSLKDSRIRRLSAGKHCSVDQLLAFMAVDKKNAGPKKKVVLLSAIGRTHEQQASVVSNEDIKIVLAPSIEVSPGVPKSLQVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVHGNGGTLKASPEELYLGNAGTASRFLTTVATLANNGTVSSTVLTGNARMKQRPIGALVDSLRANGAGVEYLETNGCLPLKIDASGGFAGGEISLAAKISSQYVSSLLMCAPYAKEPVTLKLVGGKPISQQYIDMTTAMMRSFGIDVKRSTTEEHTYHIPQGKYVNPAEYIIESDASSATYPLAVAAITGTTCTIPNIGSKSLQGDARFAVDVLRPMGCEVSQSEYSTTVTAPKDGVLKPLPNVDMEPMTDAFLTASVLAAVATGSPNRTTRIFGIANQRVKECNRIRAMKDELAKFGVICREHDDGLEIDGIDRSTLLQPPHGVHCYDDHRVAMSFSVLSLTAPKPTLILEKECVGKTWPGWWDTLAQLFKAKLEGVELKSSTKQKAEKPAASIFIIGMRGAGKTTSGLWAAKALKRPFIDLDVELESTIGKTIPEIIKERGWEGFREAELALLQKVIREKPTGYVFACGGGIVETQEGRDLLVQYHKANGNVLLLMRDIKEVMDFLKIDKTRPAYVEDMMGVWLRRKPWYQQCSNFQFYSQQSTQDEMGRALESFSRFLRVITGEVDHLSLLKKKPQSFFVSLTLPDLRPSAEILGDVTLGSDAVELRVDLLVDPSSANDIPSVDYVAEQISMLRSRVSLPLVFTIRTKSQGGRFPDDAHDAALDLYRLAVRMGSEFVDLEVTFPEHILRAVTEMKGFSKIIASHHDVSGSLSWANGSWGQFYNKALQYGDIIKLVGVAKCLDDNIALRKFKTWAQDAHEIPVIAINMGEKGRLSRILNGFMTPVSHPKLPFKAAPGQLSAQDIRKGLSLMGEIEPRKFAIFGKPVSASRSPAMHNALFAQVGLPHAYSRLETDNVEDVREFIHAPDFGGASVTIPLKLDIMPLLDEISPEAQVIGAVNTIVPIPRGPGDMTGYPRLIGYNTDWQGMVRCLRHGKAISPSFADTAVPGLVIGGGGTARAAIHALYSMSYSPIYLIGRSEAKVAEMASTFPEKYSVQVLKDATSLENLPMVAIGTIPGDRPIDPSMREVLCRLFENAARVDSELSAKGEVPAKRVLLEMAYKPDITPLSQLASDSGWSTIPGLEALVGQGVHQFELWTGITPVYQDARAAVMNPGTDNRG
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF18317;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Coccidioides posadasii (strain C735) (Valley fever fungus)
C6DS31
LYSX_MYCTK
MGVGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSLGYFATRRDKSVVFASSGRACITYRVEVGVCLASGDPVGDHRAWPQAVDAWLRLCQTYGWAPGVMGASSQGAQTYREAGLTALELGDEAILRPADFKLSGPEMRGVRQAVTRARRAGLTVRIRRHRDIAEDEMAQTITRADSWRDTETERGFSMALGRLGDPADSDCLLVEAIDPHNQVLAMLSLVPWGTTGVSLDLMRRSPQSPNGTIELMVSELALHAESLGITRISLNFAVFRAAFEQGAQLGAGPVARLWRGLLVFFSRWWQLETLYRSNMKYQPEWVPRYACYEDARVIPRVGVASVIAEGFLVLPFSRRNRVHTGHHPAVPERLAATGLLHHDGSAPDVSGLRQVGLTNGDGVERRLPEQVRVRFDKLEKLRSSGIDAFPVGRPPSHTVAQALAADHQASVSVSGRIMRIRNYGGVLFAQLRDWSGEMQVLLDNSRLDQGCAADFNAATDLGDLVEMTGHMGASKTGTPSLIVSGWRLIGKCLRPLPNKWKGLLDPEARVRTRYLDLAVNAESRALITARSSVLRAVRETLFAKGFVEVETPILQQLHGGATARPFVTHINTYSMDLFLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHADYLEWIDGCRELIQNAAQAANGAPIAMRPRTDKGSDGTRHHLEPVDISGIWPVRTVHDAISEALGERIDADTGLTTLRKLCDAAGVPYRTQWDAGAVVLELYEHLVECRTEQPTFYIDFPTSVSPLTRPHRSKRGVAERWDLVAWGIELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGIDRVVMLITGRSIRETLPFPLAKPH
2.3.2.3; 6.1.1.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677]
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049]
PF09924;PF00152;PF16995;PF01336;
2.40.50.140;
LPG synthetase family; Class-II aminoacyl-tRNA synthetase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3;
null
null
null
null
FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}.
Mycobacterium tuberculosis (strain KZN 1435 / MDR)
C6EVG7
VNHP_HELSC
MNPRLACSTWLPLLLVLFTLDQGRANPVERGQEYRSLSKRFDDDSTELILEPRASEENGPPYQPLVPRASDENVPPAYVPLVPRASDENVPPPPLQMPLIPRASEQKGPPFNPPPFVDYEPRAANENALRKLIKRSFERSPGRNKRLSPGDGCFGQKIDRIGAVSGMGCNSVSSQGKK
null
null
blood vessel diameter maintenance [GO:0097746]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; toxin activity [GO:0090729]
PF00212;
null
Natriuretic peptide family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19837656}.
null
null
null
null
null
FUNCTION: Helokinestatins antagonize the vasodilatory actions of bradykinin at the B2 bradykinin receptor (BDKRB2), with helokinestatin-1 being the most potent antagonist. {ECO:0000269|PubMed:19837656}.; FUNCTION: [Natriuretic peptide]: exhibits hypotensive and vasodepressor activities, possibly by targeting natriuretic peptide receptors NPR1 and NPR2. {ECO:0000269|PubMed:19837656}.
Heloderma suspectum cinctum (Banded Gila monster)
C6HCG7
ARO1_AJECH
MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVTADEREGGLRNLLNFGHSIGHSIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDQRIKKLTAGKHCSVEQLIAYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKGLDVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVSGKGGRMEASPSELYLGNAGTASRFLTTVATLARKSSVDSSVLTGNARMKQRPIGDLVDALAANGASIEYLENLGCLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKTPVTLRLMGGKPISQSYIDMTTAMMRSFGVEVKKSETEEHTYHIPLGFYTNPVEYIVESDASSATYPLAAAAITGTSCTVPNIGSKSLQGDARFAVDVLRPMGCAVDQSDFSTRVTGPPGGILSPLPNIDMEPMTDAFLTASVLASVARGKGSNHTTRIFGIANQRVKECNRIKAMKDELAQFGVVCREHDDGLEIDGIDRATLHHPSDGVYCYDDHRVAMSFSVLSLVTPEPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVGKRIETNPIVHVNKSAASIFIIGMRGAGKTTSGFWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWGGFREAELSLLRRVMTEKPTGYIFACGGGVVETPEARKLLTQYHKTTGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYEECSNVQYYSRLTGLDGMTQVSGGFNRFLKVITGEVDSLAKMRRKENTFFVSLTLPDLGLAAHILKEVTLGSDAVELRVDLLKDPQSDNEIPSVDYVAEQISVLRSRASVPLVFTIRTKGQGGRFPDDAYDAALQLYRLAVRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGQLSWVNGSWIQFYNKALQYGDVIKLVGVARSIDDNISLKKFKTWAEEKHNVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKAKKFAVIGNPVSASRSPAMHNTLFRQMGLPHTYGTLETDNPEVAKEFIRSPDFGGASVTIPLKLSIMPLLDEIAPEAMSIGAVNTIVCAPPAPDGKSQTPRLIGHNTDWQGMVRCLSDAGAYAAATPTTASAGLVIGGGGTARAAIFALQNMGYSPIYVLGRSPDKLSSMTSTFHTDHDIRILEDLKALESLPTVAIGTIPGDKPIEPHMREILCRLFDLCEKANSDTEQARGVSTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTNITPVYEYARNAVMGVLPSEDIS
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Ajellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum)
C6K2K4
NETO2_RAT
MALEQLCAVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHVPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDERYYIEPSFECRFDHLEVRDGPFGFSPLIDRYCGMKSPALIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSAIENLKAKFCSTVANDVMLKTGVGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQNCAYPWDENHCKEKKKAGLFEQITKTHGTIIGVTSGIVLVLLIISILVQVKQPRKKVMACKTAFNKTGFQEVFDPPHYELFSLREKEISADLADLSEELDNYQKLRRSSTASRCIHDHHCGSQASSVKQSRTNLSSMELPFRNDFAQPQPMKTFNSTFKKSSYTFKQTHDCPEQALEDRVMEEIPCEIYVRGRDDSAQASISIDF
null
null
neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]
glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; synapse [GO:0045202]
ionotropic glutamate receptor binding [GO:0035255]
PF00431;PF00057;
4.10.400.10;2.60.120.290;
null
PTM: N-glycosylated. {ECO:0000269|PubMed:19217376}.
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the agonist sensitivity of kainate receptors. Slows the decay of kainate receptor-mediated excitatory postsynaptic currents (EPSCs), thus directly influencing synaptic transmission. {ECO:0000269|PubMed:19217376}.
Rattus norvegicus (Rat)
C6KEF6
POLG_HKV1
MMEGSNGFSSSLAGLSSSRSSLRLLTHLLSLPPPNRDARRHSGWYRSPPTLPVNVYLNEQFDNLCLAALRYPGCKLYPSVYTLFPDVSPFKIPQSIPAFAHLVQRQGLRRQGNPTTNIYGNGNEVTTDVGANGMSLPIAVGDMPTASSSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGATKLSNKLAGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTIPWSETTPPLTVFSGPKALTPGTYPPTIEPNTGVYPLPAALCVSHPESVFTTAYNAHAYFNCGFDVTVVVNASQFHGGSLIVLAMAEGLGDITPADSSTWFNFPHAIINLANSNSATLKLPYIGVTPNTSTEGLHNYWTILFAPLTPLAVPTGSPTSVKVSLFVSPIDSAFYGLRFPIPFPTPQHWKTRAVPGAGSYGSVVAGQEIPLVGYAPAAPPRDYLPGRVRNWLEYAARHSWERNLPWTAADEVGDQLVSYPIQPETLANTQTNTAFVLSLFSQWRGSLQISLIFTGPAQCYGRLLLAYTPPSANPPTTIEEANNGTYDVWDVNGDSTYTFTIPFCSQAYWKTVDIGTSSGLVSNNGYFTIFVMNPLVTPGPSPPSATVAAFLHVADDFDVRLPQCPALGFQSGADGAEVQPAPTSDLSDGNPTTDPAPRDNFDYPHHPVDPSTDLAFYFSQYRWFGLNEDLTPLNVTGGLFYHVSLNPVNFQQNSLLSVLGAFTYVYANLSLNINVSAPLQACTFYIFYAPPGASVPSTQTLAELSFFTHTATPLNLAAPTNITVSIPYASPQSVLCTSFGGFGLQNGGDPGNLHSNTWGTLILYVDLPQSDSVSVSAYISFRDFEAYVPRQTPGVGPIPTSTSIVRVARPTPKPRTVRRQGGTLADLILTPESRCFIVAHTTAPYYSILLVNPDEEYAISMFTHGDESILRYSSRGGTRLAPTAPAFFLCAAASVDTILPYPISQSHLWLSDLTGIPLRAVPPLTLFLSAGAALCAGAQTLIAVAQGGSAPDTPPTPNRALFRRQGLGDLPDAAKGLSAALENVAKVAGDADIATSSQAIASSINSLSNSIDGATTFMQNFFSGLAPKNPTSPLQHLFAKLIKWVTKIIGSLIIICNNPTPSALIGVSLMLCGDLAEDITEFFSNLGNPLAAVFYRCARALGLSPTPQSAAQAAGGRQGVRDYNDIMSALRNTDWFFEKIMSHIKNLLEWLGVLVKDDPRTKLNSQHEKILELYTDSVTASSTPPSELSADAIRSNLDLAKQLLTLSHAANSVTHIQLCTRAITNYSTALSAISLVGTPGTRPEPLVVYLYGPPGTGKSLLASLLASTLAQALSGDPNNYYSPSSPDCKFYDGYSGQPVHYIDDIGQDPDGADWADFVNIVSSAPFIVPMADVNDKGRFYTSRVVIVTSNFPGPNPRSARCVAALERRLHIRLNVTARDGAAFSAAAALKPSEPLAATRYCKFSNPLTQFSMFNLAVDYKSIVLPNTPLSCFDELIDFILGSLRDRASVNSLLSGMVRTDVARQGGNADAPAPSAAPLPSVLPSVPSQDPFVRAVNENRPVSFLSKIWSWRAPIFAASSFLSLIAATLTIVRCLRDLRSTQGAYSGTPVPKPRKKDLPKQPVYSGPVRRQGFDPAVMKIMGNVDSFVTLSGSKPIWTMSCLWIGGRNLIAPSHAFVSDDYEITHIRVGSRTLDVSRVTRVDDGELSLISVPDGPEHKSLIRYIRSASPKSGILASKFSDTPVFVSFWNGKPHSTPLPGVVDEKDSFTYRCSSFQGLCGSPMIATDPGGLGILGIHVAGVAGYNGFSARLTPERVQAFLSNLATPQSVLHFHPPMGPPAHVSRRSRLHPSPAFGAFPITKEPAALSRKDPRLPEGTDLDAITLAKHDKGDIATPWPCMEEAADWYFSQLPDSLPVLSQEDAIRGLDHMDAIDLSQSPGYPWTTQGRSRRSLFDEDGNPVPELQKAIDSVWDGGSYIYQSFLKDELRPTAKARAGKTRIVEAAPIQAIVVGRRLLGSLINHLQGNPLQYGSAVGCNPDIHWTQIFHSLTPFSNVWSIDYSCFDATIPSVLLSAIASRIASRSDQPGRVLDYLSYTTTSYHVYDSLWYTMVGGNPSGCVGTSILNTIANNIAIISAMMYCNKFDPRDPPVLYCYGDDLIWGSNQDFHPRELQAFYQKFTNFVVTPADKASDFPDSSSIYDITFLKRYFVPDDIHPHLIHPVMDEATLTNSIMWLRGGEFEEVLRSLETLAFHSGPNNYSTWCEKIKAKIRENGCDATFTPYSVLQRGWVSTCMTGPYPLTG
2.7.7.48; 3.4.22.28; 3.6.4.13
null
DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
PF00680;PF00073;PF00910;
1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10;
null
PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The leader protein-VP0 junction is cleaved by 3C proteinase (By similarity). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (By similarity). {ECO:0000250|UniProtKB:O91464, ECO:0000250|UniProtKB:P03300}.; PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.
SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Single-pass membrane protein {ECO:0000255}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:O91464}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P03300};
null
null
null
null
FUNCTION: [Leader protein]: Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Protein 2A]: Required for viral RNA replication (By similarity). Does not have any proteolytic activity (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Protein 2B]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. {ECO:0000250|UniProtKB:P03304}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity). {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity). {ECO:0000250|UniProtKB:P12296}.
Human klassevirus 1 (HKV-1)
C6KEM4
AADH2_MAIZE
MAPPQTIPRRGLFIGGAWREPCLGRRLPVVNPATEATIGDIPAGTAEDVEIAVAAARDAFSRDGGRHWSRAPGAVRANFLRAIAAKIKDRKSELALLETLDSGKPLDEASGDMDDVAACFEYYADLAEALDGKQQSPISLPMENFKSYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTTILKPSELASVSCLELGAICMEIGLPPGVLNIITGLGPEAGAPLSSHSHVDKVAFTGSTETGKRIMISAAQMVKPVSLELGGKSPLIVFDDIGDIDKAVEWTMFGIFANAGQVCSATSRLLLHEKIAKKFLDRLVAWAKNIKVSDPLEEGCRLGSVISEGQYEKIKKFISTARSEGATILYGGGRPQHLRRGFFLEPTIITDVSTSMQIWQEEVFGPVICVKEFRTESEAVELANDTHYGLAGAVISNDQERCERISKALHSGIIWINCSQPCFVQAPWGGNKRSGFGRELGEWGLDNYLTVKQVTKYCSDEPWGWYQPPSKL
1.2.1.-; 1.2.1.19; 1.2.1.47; 1.2.1.54
null
cellular detoxification of aldehyde [GO:0110095]; cellular response to anoxia [GO:0071454]; glycine betaine biosynthetic process from choline [GO:0019285]
peroxisome [GO:0005777]
1-pyrroline dehydrogenase activity [GO:0033737]; 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; gamma-guanidinobutyraldehyde dehydrogenase activity [GO:0047107]; protein homodimerization activity [GO:0042803]; sodium ion binding [GO:0031402]
PF00171;
null
Aldehyde dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-(trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244, ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540, ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382; Evidence={ECO:0000269|PubMed:23408433};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433}; KM=98 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433}; KM=16 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433}; KM=11 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433}; KM=86 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:23408433};
PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}.
null
null
FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). 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 (PubMed:23408433). Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively (PubMed:23408433). {ECO:0000269|PubMed:23408433, ECO:0000305}.
Zea mays (Maize)
C6KFA3
AGRG6_DANRE
MISFISGRWWRWKFQNTLAVFLLLICLSTSVAQSCQSSTSCNVVLTDSQGSFTSPCYPNDYPPSQSCNWTIQAPAGFIVQITFLDFELEEAQGCIYDRVVVKTGTSDAKFCGLTANGLTLNSTGNVMEVFFNSDFSVQKKGFHISYKQVAVTLRNQKVTMPKSSKTILRVSNSISIPVLTAFTVCFEIARTAQKATETIFTLSDAAGTSILAFEKTSNGMELFIGASYCSVDNLLTSSDITATMKPLCLTWTKSSGLIGVYFGGHYFSSICSASQIYTLQSGGLLQIAGKGSSSVSVDDQNLDGFIYNFRLWDHAMLSSELSALTCDTVGNVVDWDHSYWTIPGSSTQTDSTLSCSTAITTLSPGTAGCASGLGCPATLTVTITSIATTNIIPTNATTHEDIFYRSTLVVTDEQTPDRDATAIISQWLNQTFQNWMYRVYVDGISLQLITVLSRITTTRQTYLALLVYKNTTDVNLAEVEIESMLRSAPAIGNGLTLDSVTVNLMENCQADEFPVHYRWPESRPTVTQYVPCFPYKDRNASRTCMINRDNYTSFWALPDRGNCTNITSITVSQENAMDVAVQLADISNNGLSKEELTQVVTKVMELVNIAKINATLASTVVTIISNVMVSSEDAQKDASETALKAVDELVQKIEFDGPSLTISSKNLVVGVSALDTTNFNGSTLSAFIATNTTDPQIDFDSEAHNALAVVTLPPTLLQNLSLSQIEKVSRINFMFFGRTGLFQDHQNNGLTLNSYVVASSVGNFTIKNLQDPVRIEIAHLEYQKDPNPQCVFWDFNLQNYSGGCNSDGCKVGSDSNSNRTVCLCNHLTHFGILMDVSRAAELIDEKNNRVLTFITYIGCGISAIFSAATLLTYIAFEKLRRDYPSKILMNLSTSLLFLNMVFLLDGWLASYEIKELCVTVAVFLHFFLLTSFTWMGLESIHMYIALVKVFNTYIRRYILKFCIVGWGVPAAIVGIVLAVSKDSYGKNYYGKGKDGQGTSEFCWILNPVVFYVTCVAYFSIIFLMNVAMFIVVMIQICGRNGKRSNRTLREDILRNLRSVVSLTFLLGMTWGFAFFAWGPVSLAFMYLFTIFNSLQGLFIFVFHCALKENVQKQWRRYLCCGKLRLADNSDWSKTATNNTKKVSSDNLGKSLSSSSFGSTTANWTSKAKATLNPFARHSNADSTLQ
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP-mediated signaling [GO:0019933]; cell surface receptor signaling pathway [GO:0007166]; ear development [GO:0043583]; G protein-coupled receptor signaling pathway [GO:0007186]; heart development [GO:0007507]; heart trabecula formation [GO:0060347]; mitochondrion organization [GO:0007005]; myelination [GO:0042552]; myelination in peripheral nervous system [GO:0022011]; myelination of posterior lateral line nerve axons [GO:0048932]; ossification [GO:0001503]; peripheral nervous system myelin formation [GO:0032290]; regulation of sprouting angiogenesis [GO:1903670]; Schwann cell differentiation [GO:0014037]; semicircular canal fusion [GO:0060879]
plasma membrane [GO:0005886]
collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; G protein-coupled receptor activity [GO:0004930]; laminin binding [GO:0043236]
PF00002;PF00431;PF01825;PF00354;
2.60.120.200;2.60.220.50;1.20.1070.10;2.60.120.290;
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25118328}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Couples to G(i)-proteins as well as G(s)-proteins (PubMed:25118328). Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:19745155). Also plays a role in inner ear development (PubMed:24067352). {ECO:0000250|UniProtKB:Q86SQ4, ECO:0000269|PubMed:19745155, ECO:0000269|PubMed:24067352, ECO:0000269|PubMed:25118328}.; FUNCTION: [ADGRG6 N-terminal fragment]: Plays an important role in heart development (PubMed:24082093). Necessary and sufficient for axon sorting by Schwann cells independently of the ADGRG6-CTF (PubMed:25695270). {ECO:0000269|PubMed:24082093, ECO:0000269|PubMed:25695270}.
Danio rerio (Zebrafish) (Brachydanio rerio)
C6KI89
CTSG2_MOUSE
MVSRPAMSPVSPVWPRKPNLWAFWVLRLVLLLSLKSWAEDALQHCTWLLVLNKFEKVGLHLSKDRFQDHEPIDTVAKVFQKLTDSPIDPSENYLSFPYYLQINFSCPGQNIEELARKGHLMGMKPMVQINYMYSVNFYRWEMENVQILMEAAPMRSTGYCPAEAMCVLNWYTPMPFKNGSVVSSVDIYTNGIGPFVSKKRFYVNMNGFLKRDASGKSLFAIGYESLVLKSSHFRLSKSRPLWYTVNHAPVFILGGFYDEKSILFSDSNFQDYVLLELSIDSCWVGSFYCPILGFSATIHDAIATESTLFIRQNQLVYYFTGTYITLFDKSHGSSRWVRVLPSECIKRLCPVYASGNGSEYVLALTTGKNEGYIHIGTITDGLVSFEMVPDGWSVCEKLPGKNCSIDWATYIADERNLLLLVKIDSGQFYLVNFNTEFKTLNILYKIPEFIPEAKELDFLVLLDTVTYTNTPMTPKGLFFNTLNNMLYIWGNFILQSYNREEFIFLADFPKESTIKYMVNSFKGQMAVVTENEEIWYFLEGGYDVYQVVPSQGWETYHNLQKMQKSSFHSEDESLVSLFFEDGKLFQLVYLFDVGKERLVKRLLPVGTLMEYNLPKPFTVVNQGNYQAISFTHTCPFKEIHLIDVPKKHHASRTESYVALPPLVSESLGFHNNNTLAVYQGLVYYLLWLHSKYDKPYADPVHDPTWRWWQHKTKDKDYFFYLFSNRLAAEGIYINMNAYQKLYNMSGDYGIPDLFFLDKGNWFTITVVLLSHQDTFTSSDSQGPTINVDKKLAIAVTIADPECLSVTVTQDVLLNRNAVINKIKVIDKKRCSEQGMIGRNIKKTSMMLKVLGAPGNCIQRTYLGGIIQGFKVVPIFIGCPPGKRLAFDVSYTIMHSEEINKHYFDCVIKDAEMPCFLFRDLFQPFFLVQDLVTGDSGSFLGSYVLKVVGGGRTLNTIRDYTEEEIFRYNSPLDTTNSLIWKTKVERTTEDKKFYIMSHESPGVEWLCLENSPCYDIIPQSIYPPEFFFKLLVSNRGVDNSTYCDYKLTFIVHIHGLPLSSKRTSFIVMVSTSFFIALVVFYILFCLVWPHIVKAWVSLRWRINNIMASESYYTYASSTAGFSLQSHSFEGPSRAGSKEDNVQAKTA
null
null
cell differentiation [GO:0030154]; spermatogenesis [GO:0007283]
CatSper complex [GO:0036128]; motile cilium [GO:0031514]; sperm principal piece [GO:0097228]
null
PF15064;
null
CATSPERG family
null
SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:19516020, PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:19516020). {ECO:0000269|PubMed:19516020, ECO:0000269|PubMed:34225353}.
Mus musculus (Mouse)
C6KIE6
XLG2_ARATH
MAAVIRKLLPFPSPNPKRDNRESDDDDETSSGYRIEYSFASEYKGPLIANVPRALPVEVDQIPTALPVSFSSLRSGISYPVAPLVMTKDTKRPPDSGIEKKNGFVDSAAGSSVVLIGRDVVSGSSSSSSSKRLDVPEEVKSPADFRLSPSSPLSASAREEDHLDDDRVSDVGPRAVRFVEPFQSSECDESSYVSDGESIAATHRAERKGKRGSCYRCQLGNRFTEKEVCIVCDAKYCFNCVRRAMGAMPEGRKCQACIGYRIDESKRASLGKCSRMLKRHLTDSELRQVMNAEITCKANQLPSRLIIVNDKPLSEDELYTLQTCPNPPKKLKPGHYWYDKVAGYWGKIGEKPSQIISPNNSIGGYISEKVSNGDTEIYINGREITKPELTMLKWAGVQCEGKPHFWVDSDGSYREEGQKHPIGNIWSKKRAKIACAVFSLPVPPASSAVEPYDVPLYEQKMLNKLLLIGSEKGGATTIYKQARSLYNVSFSLEDRERIKFIIQTNLYTYLAMVLEAHERFEKEMSNDQSSGNVGDETSAKPGNSINPRLKHFSDWVLKEKEDGNLKIFPPSSRENAQTVADLWRVPAIQATYKRLRDTLPRNAVYFLERILEISRSEYDPSDMDILQAEGLSSMEGLSCVDFSFPSTSQEESLESDYQHDTDMKYQLIRLNPRSLGENWKLLEMFEDADLVIFCVSLTDYAENIEDGEGNIVNKMLATKQLFENMVTHPSLANKRFLLVLTKFDLLEEKIEEVPLRTCEWFEDFNPLISQNQTSRHNPPMAQRAFHYIGYKFKRLYDSILEPVNMRGRSFKPKLFVCQVSLESDTVDNALRYAREILKWHVEETSMFQEMSTTSIEASSSS
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:22232549};
defense response to bacterium [GO:0042742]; G protein-coupled receptor signaling pathway [GO:0007186]; response to bacterium [GO:0009617]
nucleus [GO:0005634]
G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
PF00503;
1.10.400.10;3.40.50.300;
G-alpha family, XLG subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17999646}.
null
null
null
null
null
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Binds GTP with specificity. Plays a role in the root morphogenesis by regulation of the cell proliferation. Acts as a positive regulator in resistance to pathogen that triggers the salicylic acid (SA) pathway. Promotes the DNA binding activity of RTV1 specifically to promoter regions of FT and SOC1 in vivo leading to the activation of floral integrator genes. {ECO:0000250, ECO:0000269|PubMed:17999646, ECO:0000269|PubMed:19825634, ECO:0000269|PubMed:22232549}.
Arabidopsis thaliana (Mouse-ear cress)
C6KRL6
ZHP3_CAEEL
MDFVHCNKCFNRKPPDGFFISSCFHIFCTKCAKADLAVCLICKKNVRLVRLDGNISSGIKIYFADPIKMVADSLAKIQKKIDFQQSTRDHLVKYLTKEKEKKRQMEVYFRTKGQEFDSQRKKLAEATAWIQMAEKKLQASEEERVKAEREIEECQAKLKSMTNLMSADTLGMNSQTPFPFSLAESQETAPSLVESSANSTFNMVSPLVSSPASSPNSINYNSFFENGSRTRPESLNEEAMFNTMLQSSGQSANANTSESSAFSVAFNNIFTPSRNNMGDSSMINKTTANQTIMDKTSMSLENWRQNRANSFGVHDISKRDSSLPTGGGSAIRVHHFKQNSRITPIAQNRRSAAGFDRQQIQEMRRISSQPGYLAQRKPINGRSFIGPAD
null
null
chiasma assembly [GO:0051026]; embryo development ending in birth or egg hatching [GO:0009792]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic chromosome segregation [GO:0045132]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131]; synaptonemal complex disassembly [GO:0070194]
chromosome [GO:0005694]; synaptonemal complex [GO:0000795]
metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789]
PF14634;
null
null
null
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042, ECO:0000269|PubMed:29521627, ECO:0000269|PubMed:30379819}. Note=Co-localizes with zhp-4 to chromosomes from mitosis to early diakinesis in the germline (PubMed:29521627, PubMed:30379819). Co-localizes with syp-1, a component of the synaptonemal complex, throughout the gonad from early prophase to mid-pachytene (PubMed:15340062, PubMed:18949042, PubMed:29521627, PubMed:30379819). In early pachytene, co-localizes with syp-1 as puncta along chromosomes (PubMed:18949042). In pachytene nuclei, localizes in linear arrays in the space in between synapsed chromosomes (PubMed:15340062). Does not localize to unsynapsed chromosomes (PubMed:18949042). From mid-pachytene, co-localizes with cosa-1 at crossover sites of recombination intermediates, and gradually disassociates from syp-1 along both chromosome arms (PubMed:15340062, PubMed:18949042, PubMed:29521627, PubMed:30379819). Co-localizes with brc-1 at crossover sites in mid-late pachytene nuclei (PubMed:30383754). At late pachytene, localizes asymmetrically on synapsed chromosomes (PubMed:18949042). At late pachytene and early diplotene localizes to a single focus at the boundary between the long and short arm of each pair of homologous chromosomes (PubMed:18949042). At late pachytene, localization at chromosomes is not dependent on syp-1 (PubMed:18949042, PubMed:29521627). In diakinesis, does not localize to chromosomes, but is dispersed between chromosomes (PubMed:15340062). {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042, ECO:0000269|PubMed:29521627, ECO:0000269|PubMed:30379819, ECO:0000269|PubMed:30383754}.
null
null
null
null
null
FUNCTION: Recruited co-dependently with zhp-4 to the synaptonemal complex between homologous chromosome pairs to regulate the formation and number of crossover events between homologs during meiotic recombination (PubMed:15340062, PubMed:18949042, PubMed:29521627, PubMed:30379819). In the early stages of pachytene, in complex with zhp-4, recruited by the zhp-1-zhp-2 heterodimer to designated crossover sites along the homolog pair to stabilize other pro-crossover factors such as rmh-1, msh-5 and cosa-1 (PubMed:29521627, PubMed:30379819). This in turn facilitates crossover and promotes the formation of chiasma in each meiotic nucleus at the late pachytene stage of meiosis (PubMed:29521627, PubMed:30379819). Plays a role in the segregation of homologous chromosomes following the completion of crossovers (PubMed:18949042). Together with him-14 and msh-5 plays a role in the activation of DNA damage-dependent apoptosis at the DNA damage checkpoint in pachytene cells (PubMed:23832114). {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042, ECO:0000269|PubMed:23832114, ECO:0000269|PubMed:29521627, ECO:0000269|PubMed:30379819}.
Caenorhabditis elegans
C6KRN1
SAO1_CAEEL
MHKNGNNGPVIDTKWHYLGPDSEKYGPYMSKDMLFWLQAGYFNDGLQLKTENEPNYHTLGEWSQLLGTHPFSMPVHSLDATIAQMNSMRPHGAMMMVPPGLQNQFQPPMPMRFPPFLPMPLLHQMNQNGPPMGAQMHSQPPSEPIDAGSLSHTPDSENETRLNEQTLQQPPSWLIALGLAGHGRKPHHHQQILAHQHIPQMQHANVATDQVVMKSVECQTEPVEISKEQASRVLSELLGQMVIIN
null
null
negative regulation of Notch signaling pathway [GO:0045746]; Notch signaling pathway [GO:0007219]; regulation of protein deneddylation [GO:0060625]
cell cortex [GO:0005938]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]
WD40-repeat domain binding [GO:0071987]
PF02213;
3.30.1490.40;
null
null
null
null
null
null
null
null
FUNCTION: Involved in negative regulation of early and late embryonic Notch signaling. {ECO:0000269|PubMed:22209900}.
Caenorhabditis elegans
C6KSX0
PF12_PLAF7
MIKLSKKYCLGISFVLYILLSVCEGHKNLTCDFNDVYKLEFHPNQQTSVTKLCNLTPNVLEKVTIKCGSDKLNYNLYPPTCFEEVYASRNMMHLKKIKEFVIGSSMFMRRSLTPNKINEVSFRIPPNMMPEKPIYCFCENKKTITINGSNGNPSSKKDIINRGIVEIIIPSLNEKVKGCDFTTSESTIFSKGYSINEISNKSSNNQQDIVCTVKAHANDLIGFKCPSNYSVEPHDCFVSAFNLSGKNENLENKLKLTNIIMDHYNNTFYSRLPSLISDNWKFFCVCSKDNEKKLVFTVEASISSSNTKLASRDNTYQDYISNSSFLTLSSYCAFITFIITSFLSFIL
null
null
symbiont entry into host [GO:0044409]
apical part of cell [GO:0045177]; cell surface [GO:0009986]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; symbiont-containing vacuolar space [GO:0020004]
null
PF07422;
2.60.40.2860;
null
PTM: Processed into a soluble form. {ECO:0000269|PubMed:22848665}.
SUBCELLULAR LOCATION: [Merozoite surface protein P12]: Cell surface. Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=Present on the surface of merozoite. {ECO:0000269|PubMed:22848665}.; SUBCELLULAR LOCATION: [Merozoite surface protein P12, processed form]: Cell surface. Cell membrane. Note=Shed from the merozoite surface. {ECO:0000269|PubMed:22848665}.
null
null
null
null
null
null
Plasmodium falciparum (isolate 3D7)
C6KT50
PDX1_PLAF7
MENHKDDAVLLKHGWCEMLKGGVIMDVKSVEQAKIAEEAGAIGVMVLENIPSELRNKEGVARSVDPSKVEEIKKCVSINVLAKVRIGHFVEAQILEELKIDMIDESEVLTIADEMHHIDKHKFKTPFVCGCTNLGEALRRISEGASMIRTKGEAGTGNIIEAIKHIRTVNNEIKYLCSLSDSEVYHFAKKINAPIDLVLLTKKLKRLPVVNFAAGGVATPADAAMCMQLGMDGVFVGSGIFESENPRKMAASIVSAVSNFNNPKILLDVSMNLGKAMCGSTRVSDKWKNKNEEHTKFLTPQ
4.3.3.6
null
amino acid metabolic process [GO:0006520]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615]; response to singlet oxygen [GO:0000304]; vitamin B6 biosynthetic process [GO:0042819]
cytosol [GO:0005829]
amine-lyase activity [GO:0016843]; catalytic activity [GO:0003824]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity [GO:0036381]
PF01680;
3.20.20.70;
PdxS/SNZ family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16339145}.
CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6; Evidence={ECO:0000269|PubMed:16339145, ECO:0000269|PubMed:22244765};
null
PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
null
null
FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by Pdx2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. {ECO:0000269|PubMed:16339145}.
Plasmodium falciparum (isolate 3D7)
C6KT68
FENR_PLAF7
MKIRFVFILSVLISGVCCISKNVSRRVANRMTAHSRFLFVHDKYKRNKNFKLKNNKEENNFINLYTVKNPLKCKIVDKINLVRPNSPNEVYHLEINHNGLFKYLEGHTCGIIPYYNELDNNPNNQINKDHNIINTTNHTNHNNIALSHIKKQRCARLYSISSSNNMENLSVAIKIHKYEQTENAPNITNYGYCSGFIKNLKINDDIYLTGAHGYFNLPNDAIQKNTNFIFIATGTGISPYISFLKKLFAYDKNNLYNRNSNYTGYITIYYGVYNEDSILYLNELEYFQKMYPNNINIHYVFSYKQNSDATSFYVQDEIYKRKTEFLNLFNNYKCELYICGHKSIRYKVMDILKSHDQFDEKKKKRVHVEVY
1.18.1.2
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17251200, ECO:0000269|PubMed:17258767, ECO:0000269|PubMed:19736991};
electron transport chain [GO:0022900]; regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway [GO:0010322]
apicoplast [GO:0020011]; chloroplast thylakoid membrane protein complex [GO:0098807]
electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; ferredoxin-NAD(P) reductase activity [GO:0008937]; ferredoxin-NADP+ reductase activity [GO:0004324]; identical protein binding [GO:0042802]; NADPH dehydrogenase activity [GO:0003959]
PF00175;
3.40.50.80;2.40.30.10;
Ferredoxin--NADP reductase type 1 family
null
SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.2; Evidence={ECO:0000305|PubMed:16289098, ECO:0000305|PubMed:17251200, ECO:0000305|PubMed:17258767, ECO:0000305|PubMed:19736991};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 uM for NADPH {ECO:0000269|PubMed:17258767, ECO:0000269|PubMed:19736991}; KM=720 uM for NADH {ECO:0000269|PubMed:17258767};
null
null
null
FUNCTION: May play a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. {ECO:0000269|PubMed:16289098}.
Plasmodium falciparum (isolate 3D7)
C6KTB8
PK4_PLAF7
MCNFIKKGIRFNGDKYIFLFDIFIKKYLLNVFVANILWEEENNICFLNRLKNKRKKSILFLKEEYLRYLMILNKEEKNKKKRLKKIYECIKVFSIKEFRWLINKLEIIYFYFFCHLLLLCIFQNIFLLTYMSKEYFLKNIHDYMINILSNDIKFNTCIEFTHNDKYEQKCITMAYYDFLLNKKGKLKKRNKYYDIKNIEPLTGKDKNLYSYYNFSPFFPMSSSDIINVNTNDKISNILWNDKYIDTLNHVNMKKKDIPLNIHSNNILMNNYAYRKYVRSYMIKKRINDLILYNLKNIFEKINNIEKLTNINNFMNFKKEYEKVSKEVCNNNNNNYDPSDYMLILPNSSKDHALYNNINNDEYMYKKFCNFISQAREIKKQREKEKCHRDEKCDRGENYDRGEKYDRDEKYDKEEKGLKEDNYRDVNEWNSNKSERCNKIYPSDYKFFLSEDKKYDTPYYSNERVDFHNSDIYMNDMDEELYYSSYHNNHHNNDITYNSNVYKRMLNEVIHPSVESNDVKKGPLNNDNIKNKESNVYEINDIIYQLNGEKKMNTNMCEKRGNKIFDSNNFHNINERKKKILDENDMITIDNNIDKKENILFPYFHMEILKDNEMNITKYYKDKQYYGQYKYDENIYIYDLIVLDTSGYIYKVSTDGSYHWKRKIVDHIQDYSNIEEKDDERKVLKKRNKLNEKDMYESNNKYESNMYDMNTYESNKYDINTYDKNISDSTKAHQNIYVLKKNVYDMNYDSKRALKISPYHNYFNTSIINSINRDKLKHSKPLYKNNIKTNDDNKKLRENKTKNKRLVSNYLGNLFYINENNEVIPLNINIKDVVNNSPFKSPLFPNMVFIGSRESTIINLDYDTGHVLRKYDEASNELLDKPPKKKSRKNKSIKNVKDINDNMKLYKEGSQNVEELSFTEEENKKKSILEGEKIEVASLNNEENMNKGFVCEKDDKINNYDNDEDDLFYEQYEDNNDNDNNKNDNNKNDNNKNDNNKNDNNNNNNNNNNNSYYYYNINGNASDDILVHSKNELLNNTYINKTNIKDENSNNNESFLNKIDGMNNFKLLPKRNMKRNRKKNLLKRLMVSTNKLSMLLNRYHLINRSLERMRKDIKRGKNKRILKKRQLQISLIKWVIKAVDENTLKKKWITTWVDVGSIFMTDVHRKDTSFINSLIEIVGNKLILRPIEKDKMKSTTYQILKIMNNDTDEIQMYRNEDMKYEVINNVDDINNVDNINNANNMNNVNNINNMNNMNNMNNMNNMNNMNNINNMNNINNMNNINNINNINNMNNILNDRLKNRINNKDNSNIKSKIFIFSESISSVFAVKYKNLSNIFTLDIIAKPNIKLYSDYDNLNNFTYNPVHVKKERTLFLPFSKDISDLDGDKFSCSFEDNIIYGKRLIHRLNSISVNISSIEKDMKYLLSNIIYVYDKNKRIPISYIYDMKNLIYEYQKVKQEFLYHLPWDEGDQKYLSRTDDVLNNSIIDNIGKKGPIFICEYINKFMDLYFEENDICYDYCSMLNIWDKIFNNTVSDGDSLLLSNLYRVVHNAFKNNNKYNNNNIYFDNNINININSSSSSSSRSRRNIYNFDNYYNNRRDYNSFWEDRHNILMNRENFLINTSTDKVFSGGKNNELKEFTSIRYKRRRWYWRVFYTIMFIIFFPVLFIYRRIIKRRKGSSKGNKIGTSSNNKLIKKNRTFKDYEDDENNIMSEDEEDDLDMNYDLIFDDDRLKVKKIKRMRKNYNNNNNNNNNKNNNNISNNNSNSNSKSNRFLSKLSNIDLANIDLNLIKKSHGKKMDNFEQPTLVDILARHARDSTHNDGVSYYPFNENETYNMLSLNYAWGGNHKHMNVERTSEYNMGNISHQLNYNNIRNLGDNKISAYELDIYEKELFHLYRRRAASQDVLNKKSFVMKKRIRSSYKVGSSNKYHKKNYTDNEKDKKKYRSYKEKHINEKMFDKKEFLNFLTNFNKKFMKKNSLVDHLIKMNDKAEDNYDGYNSSGSRYNNINDDGVELCGTKRYTNNKNNSDYDNYNNNNNMKNKRYSNKKHNNDNIIINNNNNKYTDERKYRNKSIKEDVDYTNDYYNIQLNNNKINNNQTKNKIDTIRNISHEKLGNNKSSSARNLSLIQTSHIPYDAPLADFLENGRFLRTFENISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVSSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMHLMPKEIQNLVKKNKDTFKKRLTKNKKYSNNCISDSSNNNNSSCYSASSYNSSINSNYRNMKLWIKKKEQSPDMKRYKEVLRKNNAPNLVFYSDNDGLTSKNKENPEKNHNPFLSDKNFSDSIYKKKKSHDYNSSSHKLKKRKNKKKKSKKKRKSKSKIKTNAQGIYEESENDEGRDHFQYKKGKEQFSKFIGKHNSMGFTQSFQEYDPFDNGYLSEEDRDLIVFADNEESNGNDQQMIRHDNMNNENVIIKHRNEDDKNGLDGDKNGLDGDKNGLDGDKNGLDGDKNGLDGDKNELDGDKNGLDGDKNGLDGDKNGLDGDKNELDDNTKKLDDNTKKLDDLLMKQKINSLTRNDIVNIENENPAPHATNNIKNKKVDLNGELTYYDYVGKNEVIPNSRTETNVESINTNGMFNNKFSVMKDEGGEYKKKENMTWGDTKRDGLYENGKHEKDGLGVNKCITNKYIENDDDDDDDDDNNNNNNNIDERKKDLKKKQKNAITKGNEDLLATNGTNNKEKRKKDDDINKNMEKIKSYKKKTPVPEFSIVLLLQMELCKGYTLRKWLDRSTRSDKPLHFTYSDKKMNHPLEFDLFKQLIKGLKDIHATCFIHRDLKPENIFVDPDTYTLKIGDLGLVRFIEEKKREKDFNNIDCYKDNIYTDINQNAITSQISIKGQIIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFTTIMERYKRLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADVYSKIKVLLDPHLTDFAFSFNDIHNEHMNKPPQGTNNFERITDNKDKFVIQSVVDMKNKVENEEIPIEKGLNSNVENIKNENNGADK
2.7.11.1
null
negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; protein phosphorylation [GO:0006468]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]
ATP binding [GO:0005524]; elongation factor-2 kinase activity [GO:0004686]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily
PTM: Auto-phosphorylated. {ECO:0000269|PubMed:29241041}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A509AMC3}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22355110, ECO:0000269|PubMed:29241041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:22355110, ECO:0000269|PubMed:29241041}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A509AMC3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:A0A509AMC3};
null
null
null
null
FUNCTION: During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition (PubMed:22355110, PubMed:29241041). Plays a role in trophozoite differentiation into schizonts (PubMed:29241041). {ECO:0000269|PubMed:22355110, ECO:0000269|PubMed:29241041}.
Plasmodium falciparum (isolate 3D7)
C6XZB6
HEPB_PEDHD
MKRQLYLYVIFVVVELMVFTTKGYSQTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR
4.2.2.7; 4.2.2.8
null
heparin catabolic process [GO:0030211]
periplasmic space [GO:0042597]
heparin binding [GO:0008201]; heparin lyase activity [GO:0047488]; heparin-sulfate lyase activity [GO:0015021]; metal ion binding [GO:0046872]
PF16332;PF07940;PF18675;
2.60.40.2750;2.70.98.70;1.50.10.100;
Polysaccharide lyase 12 family
null
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8702264}.
CATALYTIC ACTIVITY: Reaction=Elimination of sulfate, appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.; EC=4.2.2.8; Evidence={ECO:0000269|PubMed:8702264}; CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.7; Evidence={ECO:0000269|PubMed:8702264};
null
null
null
null
FUNCTION: Cleaves both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Cleaves heparin at alpha-D-GlcNp2S6S(1->4) alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp. {ECO:0000269|PubMed:8702264}.
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
C6Y4D0
DPB3_SCHPO
MEKTYGKTVLPLSRVKRIIKQDEDVHYCSNASALLISVATELFVEKLATEAYQLAKLQKRKGIRYRDVEDVVRKDDQFEFLSDLFSI
null
null
CMG complex assembly [GO:0140529]; DNA strand elongation involved in mitotic DNA replication [GO:1902983]; DNA-templated DNA replication [GO:0006261]; heterochromatin formation [GO:0031507]; mitotic DNA replication initiation [GO:1902975]; regulation of DNA-templated transcription [GO:0006355]
epsilon DNA polymerase complex [GO:0008622]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
protein heterodimerization activity [GO:0046982]; transcription cis-regulatory region binding [GO:0000976]
PF00808;
1.10.20.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27344}.
null
null
null
null
null
FUNCTION: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair (By similarity). The dpb3-dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation and H3K9 methylation in heterochromatin (PubMed:29109278). The dpb3-dpb4 dimer is also required for the recruitment of sir2 to heterochromatin (PubMed:29109278). {ECO:0000250|UniProtKB:P27344, ECO:0000269|PubMed:29109278}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
C6ZJZ3
IF4E1_SOYBN
MVVEDTQKSVITEDQYPSRVVSDNNNDDDDDDLEEGEIPVDGEDSGATATTKPPAALARNPHPLENSWTFWFDNPSSKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLGLGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLAMIGEQFDHGDEICGAVVNVRSRQDKIAIWTKNASNEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKLDRGAKNKYVV
null
null
defense response to virus [GO:0051607]; response to virus [GO:0009615]; translational initiation [GO:0006413]
cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]
RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]
PF01652;
3.30.760.10;
Eukaryotic initiation factor 4E family
PTM: According to the redox status, the Cys-135-Cys-173 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31860775}. Cytoplasm {ECO:0000269|PubMed:31860775}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31860775}. Cytoplasm {ECO:0000269|PubMed:31860775}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with potyvirus nuclear inclusion protein A (NIa-Pro) and nuclear inclusion protein B (NIb) in the cytoplasm. {ECO:0000269|PubMed:31860775}.
null
null
null
null
null
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (e.g. soybean mosaic virus (SMV), bean common mosaic virus (BCMV) and watermelon mosaic virus (WMV), but not bean pod mottle virus (BPMV)) (PubMed:31860775). {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:31860775}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:31860775}.
Glycine max (Soybean) (Glycine hispida)
C7A2A0
BALDH_ANTMA
MAAHRFSSLLSRSVPLLSRGGKQSYLGRGVYRYGTAAAAALEEPIKPPVSVQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTALKNPAWL
1.2.1.28; 1.2.1.3; 1.2.1.39
null
circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]
mitochondrion [GO:0005739]
acetaldehyde dehydrogenase (acetylating) activity [GO:0008774]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; phenylacetaldehyde dehydrogenase activity [GO:0008957]
PF00171;
null
Aldehyde dehydrogenase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19292760}.
CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:19292760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186; Evidence={ECO:0000269|PubMed:19292760}; CATALYTIC ACTIVITY: Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH; Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:19292760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295; Evidence={ECO:0000269|PubMed:19292760}; CATALYTIC ACTIVITY: Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH; Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.28; Evidence={ECO:0000269|PubMed:19292760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841; Evidence={ECO:0000269|PubMed:19292760}; CATALYTIC ACTIVITY: Reaction=2-phenylacetaldehyde + H2O + NAD(+) = 2-phenylacetate + 2 H(+) + NADH; Xref=Rhea:RHEA:21392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16424, ChEBI:CHEBI:18401, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.39; Evidence={ECO:0000269|PubMed:19292760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21393; Evidence={ECO:0000269|PubMed:19292760};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.37 uM for benzaldehyde {ECO:0000269|PubMed:19292760}; KM=2.01 uM for acetaldehyde {ECO:0000269|PubMed:19292760}; KM=5.35 uM for phenylacetaldehyde {ECO:0000269|PubMed:19292760}; Vmax=1.32 nmol/sec/mg enzyme with benzaldehyde as substrate {ECO:0000269|PubMed:19292760}; Vmax=8.93 nmol/sec/mg enzyme with acetaldehyde as substrate {ECO:0000269|PubMed:19292760}; Vmax=1 nmol/sec/mg enzyme with phenylacetaldehyde as substrate {ECO:0000269|PubMed:19292760}; Note=kcat is 0.31 sec(-1) with benzaldehyde as substrate (PubMed:19292760). kcat is 2.08 sec(-1) with acetaldehyde as substrate (PubMed:19292760). kcat is 0.23 sec(-1) with phenylacetaldehyde as substrate (PubMed:19292760). {ECO:0000269|PubMed:19292760};
PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:19292760}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. Active in a broad range of pH varying from 6 to 9. {ECO:0000269|PubMed:19292760};
null
FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway (PubMed:19292760). Catalyzes the oxidation of benzaldehyde to benzoic acid (BA) (PubMed:19292760). Capable of oxidizing a broad spectrum of aliphatic aldehydes; increased carbon chain length results in a decrease in its efficiency (PubMed:19292760). {ECO:0000269|PubMed:19292760}.
Antirrhinum majus (Garden snapdragon)
C7AE94
FAOMT_VITVI
MSSSSHRGILKTEALTKYLLETSAYPREHEQLKGLREATVEKHKYWSLMNVPVDEGLFISMLLKIMNAKKTIELGVFTGYSLLATALALPQDGKIIAVDPDKEAYQTGVPFIKKAGVEHKINFIQSDAMSVLNDLIADGKEEGTLDFAMVDADKENYLNYHELLLKLVRVGGIIAYDNTLWFGSVARSEEEEMMDFERAGRVHLMKLNKFLASDPRVELSHLSIGDGVALCRRLY
2.1.1.267
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
anthocyanin-containing compound biosynthetic process [GO:0009718]; cyanidin 3-O-glucoside biosynthetic process [GO:0033485]; delphinidin 3-O-glucoside biosynthetic process [GO:0033486]; methylation [GO:0032259]; pigmentation [GO:0043473]
cytoplasm [GO:0005737]
laricitrin 5'-O-methyltransferase activity [GO:0070448]; metal ion binding [GO:0046872]; myricetin 3'-O-methyltransferase activity [GO:0033799]; O-methyltransferase activity [GO:0008171]
PF01596;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family, CCoAMT subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19525322}.
CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid.; EC=2.1.1.267; Evidence={ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3',5'-dimethoxyflavonoid.; EC=2.1.1.267;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43 uM for cyanidin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=7.6 uM for cyanidin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=44 uM for delphinidin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=24 uM for quercetin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=2.7 uM for quercetin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=74 uM for cyanidin {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=33 uM for quercetin {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=19 uM for myricetin {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; Note=kcat is 0.090 sec(-1) with cyanidin 3-glucoside (PubMed:19525322). kcat is 2.3825 sec(-1) with cyanidin 3-glucoside (PubMed:20580386). kcat is 0.118 sec(-1) with delphinidin 3-glucoside (PubMed:19525322). kcat is 0.1 sec(-1) with quercetin 3-glucoside (PubMed:19525322). kcat is 0.8976 sec(-1) with quercetin 3-glucoside (PubMed:20580386). kcat is 0.084 sec(-1) with cyanidin (PubMed:19525322). kcat is 0.112 sec(-1) with quercetin (PubMed:19525322). kcat is 0.128 sec(-1) with myricetin (PubMed:19525322). {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 49 degrees Celsius. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
FUNCTION: Mediates O-methylation of anthocyanins. Anthocyanins are major pigments in grapes: at ripening initiation in red grapevine berries, the exocarp turns color from green to red and then to purple due to the accumulation and extent of methylation of anthocyanins. Catalyzes both 3' and 5' O-methylation of anthocyanins, with a preference for glycosylated substrates. Active on both anthocyanins and flavonols in vitro. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. Not able to methylate flavan type skeletons with chiral centers, such as catechins or dihydroquercetin. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}.
Vitis vinifera (Grape)
C7AJA4
TUT7_TRYBB
MNVAKREFIRGMMAHYRASLPPPEHSVVIHELQKRVLDIGMLAVNKAHVELFGSHVSGFCTPHSDADISLTYRNFSPWLQGMERVDEQNNKRMTRFGKEASAMGMEDVRYIRARIPVVQFTDGVTGIHCDVSIGNIGGVENSKILCAIRQVFPDFYGAYIHLVKAWGKAREVIAPERSTFNSFTVTTMALMVLQELGLLPVFSKPTGEFGELTVADAEMLLQEFKLPPIYDSLHDDDEKLGEAVFFCLQRFAEYYAKYDFSAGTVSLIHPRRHRTVYERVVRRHLELLGSRKRLEWEKHIAEHKEDGPLDENDFSASMQNETTQRPSNSPYVVEDFVNYVNCGRRVQASRVRHIQQEFNRLREMLIDKESELKFDEVFRESDTVPRFQGFEGVGTRDHRVKTFRPQ
2.7.7.52
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19465686}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:20403364};
mRNA processing [GO:0006397]; RNA 3' uridylation [GO:0071076]
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA uridylyltransferase activity [GO:0050265]
null
1.10.1410.10;3.30.460.10;
DNA polymerase type-B-like family
null
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:19465686}.
CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:19465686, ECO:0000269|PubMed:20403364};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 uM for UTP (with 6(U) single-stranded RNA as substrate) {ECO:0000269|PubMed:19465686}; KM=1 uM for UTP (with double-stranded RNA as substrate) {ECO:0000269|PubMed:19465686}; Note=kcat is 0.18 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.04 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686). {ECO:0000269|PubMed:19465686};
null
null
null
FUNCTION: Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core-like complex (RECC-like), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:19465686). Specifically, catalyzes the addition of U to single-stranded RNA with a preference for a 3'-terminal U and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates (PubMed:19465686, PubMed:20403364). Essential for insect and bloodstream developmental forms viability (PubMed:19465686). {ECO:0000269|PubMed:19465686, ECO:0000269|PubMed:20403364}.
Trypanosoma brucei brucei
C7ASJ5
BGAL2_ARTSP
MGKRFPSGWFSPRVHPPRRQRSPMTNQATPGTASVWNNIEGIGFGGDYNPEQWPVSVRLEDLELMQEAGVNFLSVGIFSWALLEPAEGQYDFGWLDDVMDNLHGIGVKVALATATAAPPAWLVRKHPEILPVTADGTTLGPGSRRHYTPSSAVYRKYAAGITRVLAERYKDHPALALWHVDNELGCHVSEFYGEEDAAAFRLWLERRYGTIDALNAAWGTAFWSQHYGSFEEILPPGVAPSTLNPGQQLDFQRFNSWALMDYYRSLVAVLREVTPAVPCTTNLMASSATKSMDYFSWAKDLDVIANDHYLVAADPERHIELAFSADLTRGIAGGDPWILMEHSTSAVNWQPRNQPKMPGEMLRNSLAHVARGADAVMFFQWRQSFAGSEKFHSAMVPHGGRDTRVWREVVDLGAALQLLAPVRGSRVESRAAIVFDYEAWWASEIDSKPSIDVRYLDLLRAFHRSLFLRGVSVDMVHPSASLDGYDLVLVCTLYSVTDEAAANIAAAAAGGATVLVSYFSGITDEKDHVRLGGYPGAFRELLGVRVEEFHPLLAGSQLKLSDGTVSSIWSEHVHLDGAEAFQTFTGYPLEGVPSLTRRAVGTGAAWYLATFPDRDGIESLVDRLLAESGVSPVAEADAGVELTRRRSADGGSFLFAINHTRAAASVRASGTDVLSGERFTGTVEAGSVAVIAED
3.2.1.23
null
galactose metabolic process [GO:0006012]
beta-galactosidase complex [GO:0009341]
beta-galactosidase activity [GO:0004565]
PF02449;PF08533;PF08532;
3.40.50.880;3.20.20.80;2.60.40.1180;
Glycosyl hydrolase 42 family
null
null
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:19631003};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.75 mM for ONPG (at 10 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=4.86 mM for ONPG (at 20 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=3.46 mM for ONPG (at 30 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=3.15 mM for ONPG (at 40 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=2.62 mM for ONPG (at 50 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=5.11 mM for ONPG (at 55 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=77.54 mM for lactose (at 10 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=67.82 mM for lactose (at 20 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=52.67 mM for lactose (at 30 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=44.31 mM for lactose (at 40 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=39.73 mM for lactose (at 50 degrees Celsius) {ECO:0000269|PubMed:19631003};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with ONPG as substrate. Over 90% of activity in the pH range 6.5-8.5. Highly efficient at pH range 4.5-9.5. {ECO:0000269|PubMed:19631003};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with ONPG as substrate. Active at 4-8 degrees Celsius. 60% of the maximum activity is detected at 25 degrees Celsius and 15% at 0 degrees Celsius. Over 50% activity at 30 degrees Celsius. {ECO:0000269|PubMed:19631003};
FUNCTION: Hydrolyzes p-nitrophenyl-beta-D-galactopyranoside (PNPG), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), with highest activity against PNPG. Also acts on p-nitrophenyl-beta-D-glucopyranoside (PNPGlu) and o-nitrophenyl-beta-D-glucopyranoside (ONPGlu), but with significantly lower activity. {ECO:0000269|PubMed:19631003}.
Arthrobacter sp
C7AU21
D27_ORYSJ
METTTLVLLLPHGGAGGVRPAAAATAKRSYVMRRCCSTVRAVMARPQEAPASAPAKKTETAAMMSTVQTETAAAPPATVYRDSWFDKLAIGYLSRNLQEASGLKNEKDGYESLIDAALAISRIFSLDKQSEIVTQALERALPSYILTMIKVMMPPSRFSREYFAAFTTIFFPWLVGPCEVMESEVEGRKEKNVVYIPKCRFLESTNCVGMCTNLCKIPCQKFIQDSLGMKVYMSPNFEDMSCEMIFGQQPPEDDPALKQPCFRTKCVAKQNHGVNCSI
5.2.1.14
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:19470589}; Note=Recombinant protein contains about 1.7 mole of iron per mole of protein. {ECO:0000269|PubMed:19470589};
secondary shoot formation [GO:0010223]; strigolactone biosynthetic process [GO:1901601]
chloroplast [GO:0009507]
beta-carotene isomerase activity [GO:0106365]; cis-trans isomerase activity [GO:0016859]; iron ion binding [GO:0005506]
PF13225;
null
null
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:19470589}.
CATALYTIC ACTIVITY: Reaction=all-trans-beta-carotene = 9-cis-beta-carotene; Xref=Rhea:RHEA:34455, ChEBI:CHEBI:17579, ChEBI:CHEBI:67188; EC=5.2.1.14; Evidence={ECO:0000269|PubMed:22422982}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34456; Evidence={ECO:0000269|PubMed:22422982};
null
null
null
null
FUNCTION: Involved in strigolactones biosynthesis by catalyzing the isomerization of the C9-C10 double bond in all-trans-beta-carotene leading to 9-cis-beta-carotene and providing the substrate for CCD7. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signals that stimulate hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds. {ECO:0000269|PubMed:19470589, ECO:0000269|PubMed:22422982}.
Oryza sativa subsp. japonica (Rice)
C7B178
VPY_PETHY
MDRLLSLEPSNVVTIRLEPGQKCSGVLTLRNVMYTMPVAFRLQPLNKIRYSIRPQSGIISPLTTITLEIIYHLPPNTTLPDSFPHCDDSFLLHSVVAPGATAKDTSSTLDMVPSDWFTTKRKQVFIDSAIKIMFVGSPVLCYLVRKGYMDEIREVLEKSDTTWKSVDSVNFEGQTLLHLAISQGRPDLVQLLLEFGPNIEAHSRSCSSPLEAASATGEALIVELLLAKKASTERTEFSASGPIHLAAGNGHLEVLKLLLLKGANVNSLTKDGNTALHLAVEERRRDCARLLLANGARADICSTGNGDTPLHIAAGLGDEHMVRVLLQKGAEKYIRNKYGKTAYDVAAEHGHNKLFDALRLGDSLCVAARKGEVRTVQRLLENGASINGRDQHGWTALHRACFKGRIEVVKALIDNGIDVNARDEDGYTALHCAVESGHVDVAELLVKKGADIELRTSKGITALQIAQSLHYSGLTRVLMQGGATKEVGTMETNIVKSSGKIAVRDLDIGTIKKRSVNKSRTRRSSFDRNAPLAVL
null
null
arbuscular mycorrhizal association [GO:0036377]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of JNK cascade [GO:0046330]; protein targeting to chloroplast [GO:0045036]; response to inorganic substance [GO:0010035]; response to symbiotic fungus [GO:0009610]
cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
chloroplast targeting sequence binding [GO:0030941]
PF00023;PF12796;PF13857;PF00635;
1.25.40.20;2.60.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20804456}. Nucleus {ECO:0000269|PubMed:20804456}. Cell membrane {ECO:0000250|UniProtKB:D3J162}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Associated with mobile spherical structures that are associated with the tonoplast referred to as 'tonospheres'. In mycorrhizal roots, tonospheres are observed in the vicinity of intracellular hyphae (arbuscules) (PubMed:20804456). Observed associated with EX70I in zones adjacent to the periarbuscular membrane (PAM) around the arbuscule hyphal tips (By similarity). {ECO:0000250|UniProtKB:D3J162, ECO:0000269|PubMed:20804456}.
null
null
null
null
null
FUNCTION: Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus intraradices, G. mosseae and Gigaspora margarita) both during fungal passage across root epidermis and for arbuscule formation in cortical cells; this symbiosis promotes phosphorus (P) and copper (Cu) uptake (PubMed:17573800, PubMed:20804456). Essential for infection by symbiotic nitrogen-fixing rhizobial bacteria leading to the formation of root nodules (By similarity). {ECO:0000250|UniProtKB:D3J162, ECO:0000269|PubMed:17573800, ECO:0000269|PubMed:20804456}.
Petunia hybrida (Petunia)
C7BKP9
PATOX_PHOAA
MKGIEGVIMLSHDILPEKLLVSEKKHENVGSYFSDDIGEQSEQTEVSHFNLSLDDAFDIYADISIENQQELKNKDNNTNIWSSLGRGDDDHNLKKIINDAFKEKLPQLMEYRRKGYNVIGLDKEGIKKLEGMLKAVPPEIQQPTMKNLYSAAQELLNTLKQHPLLPENQDMIQQSNLVIRNLSDALEAINAVSKVNQVEWWEEVHKTNKAQSDRLIAATLEELFFKVKDKRLPGSNDDYCQQEREETERKIKDLLLYDGYQLTAEHFKFGRLRKSLLAESRVTRLKLAEYLEKKSVGILTAARDAKMYAMKILLAQTRNNGFNAKDLINAGQVNDRLLSFQQYARHIRAVDGEIDGIILSNPLVVACIKETNDEPAHIKIARAILPVSEELGTVSKVLRETKEKVQPSKPKEELNHPHQDWWNRGDELWKYIKKTSWNIKETSVHVTQMVGYEASKTASRAKHKLKESSYSESINGAVKGTALLLLDEIQQAENRIRQIPQFAWDVQEAVEQHSSVIQRTAYPDELPELSELLNEQLKHEEARWQAVKKQSRDKLQELIAPITRLAQEKWAQDLYFQLGEELRKERQDRWKDIQQFDEIMAEAVGQFAEMARELDSEAVRLAEHGHSGGKELQEKVAKWLRDLSKLKGKVKAGVAKITGTSLDNFSRSGMLARGMSEWAEDLKQSYLQETLQEGSAVAAELFERTLMEVVEENRTHFAKESDPEAERFLKRLALALKHAAENTTVYPPTPEEILAGSRSLPEDIRHWAEKKVVSGAISAAFRGGFKLVTGTFSLPVRVVIRGAKTGGTLYRGVRAINRSVRLGQGPATQVKSKFINQELSKTAFRLTLSLSPLVAWGMAASITAGRLYNEKDYPEKIIKNIVIDLPEELLWIGGYAGINAAIRAHAEKAIQQAIQHALDEQADKLALRINKEIAGKSADVNVEIIPQETSVSPAETAQSTPEPLSDFASTSQLTMPELIDIQDNNSAQQPKVRRKRDVSVESEISIDNLNIINANTREDKVNSEIKSELRSELKRFENSDANSPMSDVERAIFIDLFLYKNKYEVSESQQDYKNTWLKFRRELESQENKEIKEYLRFRSIIEAYEIYDKKRLDDDTIPEAGTIIKEVIDFFQKLKKENPITFMKLAEAMVKFQYYYEEEDENEDRYFKMAEIYYFLNKTENEKKSKTFHLDIIDKYPNENNRLLDEFFLNKNNNNPDLDEIIYKLQSMQEKYRESYEMLSKVENIHQVLSDDSKNEENIFLDNRIIAAQVFDGSINISLQDKKKWLNRYDQIRNEEGSDGWKLMHIESILINLRRINTAINLTAMKSESALLLIDKLLNFQKKARENILHISETPHEDFTSYSQFKTRKELGNDDSKYYAQFDNYKDNHDAEKEAKEILSQVVARASLSFSELFDKVESIKLFSFVYKNRDGGAPLAAPGRTVVIKFPGKDTGGLVISNLFLRNHVKRISTKEMEDLKPLTEGMYTRATQHRSLGSYYHIGSQSEHTNALEILSGMNKEELKTHLKKQGIWFGEPALFSNEYPKQENTGHLENTTLKNAIIGVSTIQNNAAANYLRSTMYESTGWEKLGDRFIPFYEIGRRKHYDREYEINSEQLTLDIITSIAIAYPAARGIVATIRSSAIPSILKSGLRGSALFKSLSLELGKMGFNASKVFGGAVYELIEPYPINSHLNRHNVFNKVKDTAWEFHTDVGLKGGGLKDFIDRFTKEPKEITISGYKFKRIKYNQENFDTMQRMALDYAYNPDSKGKIAQAQQAYKTGKEDYNAPQYDNFNGLSLDKKIERYISPDTDATTKGVLAGKMNESIKDINAFQTAKDAQSWKKSANKANKVVLTPQNLYLKGKPSECLPESVLMGWALQSSQDAKLSKMLMGIYSSNDITSNPLYKSLKELHANGNASKFNASATSISNINVSNLATSETKLFPTEISSVRVDAPKHTMLISKIKNRENKIKYVFYDPNYGMAYFDKHSDMAAFFQKKMQQYDFPDDSVSFHPLDYSNVSDIKISGRNLNEIIDGEIPLLYKQEGVQLEGITPRDGIYRVPPKNTLGVQETKHYIIVNNDIYQVEWDQTNNTWRVFDPSNTNRSRPTVPVKQDTNGEWFKHSETGLKGGGPIDDIRKYIARKSAIKIFNQSINYSATKWPPEPIDKNIHMIWIGTKNISEKNIKLSIDTAKKNPDYNTSIIYDSGISGHEGAKKFMLEKFQDSNVNIIDFRKKSYFSQLKQEPSFAYYEQVIAENKYAQASDILRLLVLKYEGGIYKDIDDIQVKGFGSLTFPKGIGVMREYAPEAGKATAFPNTPIAVTKNNPIINKTLDLAVSNYQRGEKNVLKLAGPDVFTQALYQEIPGLDSKVLNAQLYQLELAKRQALGVPLEKPKNFADEQLTSAEKEKINRPYQSIRGLSGYVENGADHSWAVDTNIPSTSTQTSTIVTPLAPKTEMLPPVPSSSTKSSTSAPVLQEKISYNLATDIDATDYLNQLKQKTNINNKISSPAGQCESLMKPVSDFMRENGFTDIRYRGMFIWNNATEQIPMNHFVVVGKKVGKDYVFDVSAHQFENKGMPDLNGPLILAAEDWAKKYRGATTRKLIYYSDFKNASTATNTYNALPRELVLESMEGKTFITSPNWYQTFKRTHNIHPEVTVSDPATFSLNYSVNPTAENLSPPPPPPIPSHGQVPKTVTPPPPPMRSPLSLSQPLERLPANKTKPIGFNPGENKASFSKLEEAGKHYYKDDKSRQAAPVNTMSDFDNRYLSHTTEAPAPSNVAHLAPGNIYNTKVTAKGAEKPAYDIYISKDGESLITSSSYKVDDITTDSKFGKPLPYSEIMFNSLKKSGVDPKNLKRSVQASIENKVTQDVISAIGTRIQRGQVIRVSPTENPDAFYTLLGTDNCKATLHMLNQHAEEFGHKVVTSIEFKGTGYLVMNIGTSTQTSTIVTPPPMPGTSQLVQ
2.4.1.-; 3.5.1.44
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:24141704}; Note=A Ca(2+) ion is seen in the structure. {ECO:0000269|PubMed:24141704};
mannosyl-inositol phosphorylceramide biosynthetic process [GO:0051999]; symbiont-mediated perturbation of host Rho signal transduction [GO:0044083]
extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
calcium ion binding [GO:0005509]; mannosyltransferase activity [GO:0000030]; protein N-acetylglucosaminyltransferase activity [GO:0016262]; protein-glutamine glutaminase activity [GO:0050568]; toxin activity [GO:0090729]
PF04488;PF15645;
3.90.550.20;3.10.670.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:25782990}; Peripheral membrane protein {ECO:0000269|PubMed:25782990}; Cytoplasmic side {ECO:0000269|PubMed:25782990}. Note=Associates with the negatively charged inner leaflet of the plasma membrane via interaction with phosphatidylserine and phosphatidylinositolphosphates. Plasma membrane localization of PaTox is essential for cytotoxicity. The glycosyltransferase domain alone is sufficient to localize at the plasma membrane. {ECO:0000269|PubMed:25782990}.
CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + O-(N-acetyl-alpha-D-glucosaminyl)-L-tyrosyl-[protein] + UDP; Xref=Rhea:RHEA:51536, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13016, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:134208; Evidence={ECO:0000269|PubMed:24141704}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000269|PubMed:24141704};
null
null
null
null
FUNCTION: Toxin that acts on host cells by modifying Rho proteins by tyrosine GlcNAcylation and heterotrimeric G alpha proteins by deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases of the Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in eukaryotic host cells at the conserved tyrosine residue located in the switch I region (Tyr-32/34), using UDP-N-acetylglucosamine (UDP-GlcNAc) as the sugar donor; other GTPases of the Rho, Ras or Rab families are not substrates. Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis, cell rounding, and toxicity toward insects and mammalian cells. Also catalyzes the deamidation of the catalytic glutamine in heterotrimeric G alpha proteins (Gi, Gq/11), which blocks GTP hydrolysis and arrests the G proteins in a permanent active state leading to activation of Rho GTPases. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases. {ECO:0000269|PubMed:24141704}.
Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2))
C7C422
BLAN1_KLEPN
MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
3.5.2.6
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530};
antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677]
periplasmic space [GO:0042597]
beta-lactamase activity [GO:0008800]; zinc ion binding [GO:0008270]
PF00753;
3.60.15.10;
Metallo-beta-lactamase superfamily, Class-B beta-lactamase family
null
SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:19770275};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for cefuroxime {ECO:0000269|PubMed:19770275}; KM=10 uM for cefotaxime {ECO:0000269|PubMed:19770275}; KM=10 uM for cephalothin {ECO:0000269|PubMed:19770275}; KM=12 uM for piperacillin {ECO:0000269|PubMed:19770275}; KM=16 uM for penicillin G {ECO:0000269|PubMed:19770275}; KM=22 uM for ampicillin {ECO:0000269|PubMed:19770275}; KM=49 uM for cefoxitin {ECO:0000269|PubMed:19770275}; KM=49 uM for meropenem {ECO:0000269|PubMed:19770275}; KM=77 uM for cefepime {ECO:0000269|PubMed:19770275}; KM=94 uM for imipenem {ECO:0000269|PubMed:19770275}; KM=181 uM for ceftazidime {ECO:0000269|PubMed:19770275}; Note=No activity detected against the monobactam aztreonam. {ECO:0000269|PubMed:19770275};
null
null
null
FUNCTION: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin. {ECO:0000269|PubMed:19770275}.
Klebsiella pneumoniae
C7DLJ6
OLHYD_ELIME
MNPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMPFSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYFIRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIRGGREMDMTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSKARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDLTIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHRFLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNIHLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKNDYVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLWKNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDKLKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFPEQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELCYHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPRVVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKLLNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLRKVLKGTYFEHVLPAGAAEEEEHESFIAEHVNKFREWVKGIRG
4.2.1.53
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26077980}; Note=Binds 1 FAD per subunit. It is presumed that reduced FAD (FADH2) rather than oxidized FAD is involved in OhyA catalysis in vivo. It seems that FAD does not undergo changes in reduction/oxidation state during substrate turnover. {ECO:0000269|PubMed:26077980};
fatty acid metabolic process [GO:0006631]; response to fatty acid [GO:0070542]; response to toxic substance [GO:0009636]
null
FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; oleate hydratase activity [GO:0050151]
PF06100;
3.30.9.80;3.50.50.60;
Oleate hydratase family
null
null
CATALYTIC ACTIVITY: Reaction=(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O; Xref=Rhea:RHEA:21852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15683, ChEBI:CHEBI:30823; EC=4.2.1.53; Evidence={ECO:0000269|PubMed:19465645, ECO:0000269|PubMed:26077980}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21854; Evidence={ECO:0000305|PubMed:19465645};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.21 mM for oleate (at 30 degrees Celsius) {ECO:0000269|PubMed:19465645}; KM=0.11 mM for oleate (at 25 degrees Celsius) {ECO:0000269|PubMed:26077980}; KM=0.07 mM for oleate (at 25 degrees Celsius) with OhyA harboring two-electron-reduced FAD {ECO:0000269|PubMed:26077980}; Vmax=0.17 umol/min/mg enzyme (at 30 degrees Celsius) {ECO:0000269|PubMed:19465645}; Vmax=1 umol/min/mg enzyme (at 25 degrees Celsius) {ECO:0000269|PubMed:26077980}; Vmax=2.1 umol/min/mg enzyme (at 25 degrees Celsius) with OhyA harboring two-electron-reduced FAD {ECO:0000269|PubMed:26077980}; Note=kcat is 1.2 sec(-1). kcat is 2.6 sec(-1) with OhyA harboring two-electron-reduced FAD (PubMed:26077980). Due to the low solubility of oleate in Tris buffer, the values given in PubMed:19465645 are approximate, the real Vmax is most likely significantly higher, whereas the real KM is expected to be much lower. {ECO:0000269|PubMed:19465645, ECO:0000269|PubMed:26077980};
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. {ECO:0000269|PubMed:19465645, ECO:0000269|PubMed:26077980};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:26077980};
FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to yield (R)-10-hydroxyoctadecanoate (PubMed:19465645, PubMed:26077980). The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments. {ECO:0000269|PubMed:19465645, ECO:0000269|PubMed:26077980}.
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
C7E9W0
SCH21_STACH
ASVTFWTLDNVDRTLVFTGNPGSAAIETITVGPAENTTVEFPGSWVGNWYAYPTDAEDVPGMLGEVQFGGWNGLTYFDVSAIVNPTDHDNVKQMWPAESRKPMSGCEVFPCDNAYWLPDDIQTKVTHEVDLWTTLGAGSTGLTF
3.1.11.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21109751};
DNA metabolic process [GO:0006259]
extracellular region [GO:0005576]
DNA exonuclease activity [GO:0004529]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
null
null
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22424314}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.00329 mg/ml for salmon testes dsDNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:21109751};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. No activity between pH 3-6. {ECO:0000269|PubMed:21109751};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Activity is about 80% of the maximum activity at 35 and 50 degrees Celsius. {ECO:0000269|PubMed:21109751};
FUNCTION: Has exodeoxyribonuclease activity with lambda-DNA and salmon testes dsDNA. No activity with circular plasmid DNA. The physiological role of this enzyme may be to degrade environmental DNA, and thus mobilize nitrogen for uptake. {ECO:0000269|PubMed:21109751}.
Stachybotrys chartarum (Toxic black mold) (Stilbospora chartarum)
C7EXK4
AT8A2_BOVIN
MSRATSVGDQLDVPARTIYLNQPHLNKFCDNQISTAKYSVVTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWQTIVWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSPVALGPDQILLRGTQLRNTQWGFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSVGALYWNGSQGGKNWYIKKMDATSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYLGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELTREPSSDDFSRIPPPPSDSCDFDDPRLLKNIEDHHPTAPCIQEFLTLLAVCHTVVPERDGDSIVYQASSPDEAALVKGARKLGFVFTARTPYSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGQLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSERDYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCADLGSLLGKENDAALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCSQESMLRFPQLYKITQNAEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLANGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLIWLVFFGIYSTIWPTIPIAPDMKGQATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELEMKSRVMGRAMLRDSNGKRMNERDRLLKRLSRKTPPTLFRGSSLQQSMPHGYAFSQEEHGAVTQEEIVRAYDTTKQKSRKK
7.6.2.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
aminophospholipid translocation [GO:0140331]; neuron development [GO:0048666]; phospholipid translocation [GO:0045332]
endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; photoreceptor disc membrane [GO:0097381]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylserine flippase activity [GO:0140346]; phosphatidylserine floppase activity [GO:0090556]
PF13246;PF00122;PF16212;PF16209;
3.40.1110.10;2.70.150.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19778899, ECO:0000305|PubMed:21454556}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P98200}. Endosome membrane {ECO:0000250|UniProtKB:P98200}. Cell membrane {ECO:0000250|UniProtKB:P98200}. Photoreceptor outer segment membrane {ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:21454556}. Photoreceptor inner segment membrane {ECO:0000269|PubMed:21454556}. Note=Localizes to the Golgi and endosomes in photoreceptor cells (By similarity). Localizes to disk membranes of rod photoreceptor outer segments (ROS) (PubMed:21454556). {ECO:0000250|UniProtKB:P98200, ECO:0000269|PubMed:21454556}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:22307598, ECO:0000269|PubMed:24706822, ECO:0000269|PubMed:26592152, ECO:0000269|PubMed:31371510}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:24706822, ECO:0000269|PubMed:26592152, ECO:0000269|PubMed:31371510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:24706822, ECO:0000269|PubMed:26592152, ECO:0000269|PubMed:31371510}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:36439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24706822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36440; Evidence={ECO:0000305|PubMed:24706822};
null
null
null
null
FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:19778899, PubMed:24706822, PubMed:26592152, PubMed:31371510). Able to translocate phosphatidylserine, but not phosphatidylcholine (By similarity). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE) (PubMed:19778899, PubMed:24706822, PubMed:26592152, PubMed:31371510). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP (PubMed:31371510). ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth. Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival. {ECO:0000250|UniProtKB:Q9NTI2, ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:21454556, ECO:0000269|PubMed:24706822, ECO:0000269|PubMed:26592152, ECO:0000269|PubMed:31371510}.
Bos taurus (Bovine)
C7F6X3
IBP_LEUSY
MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL
null
null
null
extracellular region [GO:0005576]
ice binding [GO:0050825]
PF11999;
null
Ice-binding protein family
PTM: Glycosylated (PubMed:20067781, PubMed:22303017, PubMed:22426061, PubMed:23203635). Glycosylation is not required for the thermal hysteresis (TH) activity (PubMed:22426061). Glycosylation may increase stability and secretion of this protein (Probable). {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22303017, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:23203635, ECO:0000305|PubMed:22303017}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:23203635}.
null
null
null
null
null
FUNCTION: Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point (PubMed:20067781, PubMed:22303017, PubMed:22426061, PubMed:22622645, PubMed:23203635, PubMed:24699650). The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM (PubMed:24699650). {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22303017, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:22622645, ECO:0000269|PubMed:23203635, ECO:0000269|PubMed:24699650}.
Leucosporidium sp. (strain AY30) (Arctic yeast)
C7G3A0
MPPE1_CRIGR
MALVRWRLRRGNFHLLSRVLLLKLTVVIISVLLFCEYFIYHLVIFQCHWPEVKTLAHGDRQKPVLKAMFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWWLQPEVIFILGDIFDEGKWSTTEAWADDVQRFRKIFRHGSHVQLKVVIGNHDIGFHYQMSKYRIKRFEKVFSSERLFSWKGVNFVMVNSVAMEGDGCSICSEAEAELREISRKLNCSREVQGSSQCEGEQRLPFSAPVLLQHYPLYRASDANCSGEDAAPPEERNVPFEEKYDVLSREASQKLLWWLQPRLVLSGHTHSACEVLHPGGVPEVSVPSFSWRNRNNPSFIMGSLTSKDYALSKCYLPFEDRVLATYGAAAVFLVVLILAHLERLPSSFLFGWKLRKMHMRG
3.1.-.-
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:19837036}; Note=Binds 2 manganese ions per subunit. {ECO:0000305|PubMed:19837036};
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; GPI anchor biosynthetic process [GO:0006506]
cis-Golgi network [GO:0005801]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; nucleoplasm [GO:0005654]
GPI anchor binding [GO:0034235]; GPI-mannose ethanolamine phosphate phosphodiesterase activity [GO:0062050]; manganese ion binding [GO:0030145]
PF00149;
3.60.21.10;
Metallophosphoesterase superfamily, MPPE1 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane protein {ECO:0000269|PubMed:19837036}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane protein {ECO:0000269|PubMed:19837036}. Note=Also localizes to endoplasmic reticulum exit site.
null
null
null
null
null
FUNCTION: Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins. {ECO:0000269|PubMed:19837036}.
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
C7G3K3
KBX2_LIOAU
MAKHLIVMFLVIMVISSLVDCAKKPFVQRVKNAASKAYNKLKGLAMQSQYGCPIISNMCEDHCRRKKMEGQCDLLDCVCS
null
null
defense response to bacterium [GO:0042742]
extracellular region [GO:0005576]
toxin activity [GO:0090729]
PF14866;
null
Long chain scorpion toxin family, Class 2 subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19966481}.
null
null
null
null
null
FUNCTION: Dual-function toxin that acts both as an insecticidal and an antimicrobial peptide (PubMed:19966481, PubMed:30393903, PubMed:35490851). May inhibit voltage-gated potassium channels (Kv) (By similarity). This amphipathic peptide causes significant antimicrobial activity against E.coli (MIC=7 uM) but does not show any activity against S.aureus even at high concentration (PubMed:19966481, PubMed:30393903, PubMed:35490851). In vivo, causes paralysis or death to crickets (PubMed:19966481, PubMed:30393903, PubMed:35490851). {ECO:0000250|UniProtKB:Q0GY41, ECO:0000269|PubMed:19966481, ECO:0000269|PubMed:30393903, ECO:0000269|PubMed:35490851}.
Liocheles australasiae (Dwarf wood scorpion)
C7GIN5
ARO1_YEAS2
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMIAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALIIAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREEWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTKKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFAPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKAPFKAIFDAVTKE
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Saccharomyces cerevisiae (strain JAY291) (Baker's yeast)
C7IVR4
PQN41_CAEEL
MKPKKLQQGSDSAHTSDTESTKTCEKTAKKLPKTQKKLQKSKKTAKKRRDEEFRIFFPPPRVNPPIKTPFRLHNTNCEHRDWISDNLCLPKYASYQTGWRISHKSMKSLVLMDKRRAEWLKMHNLYRKSEIRKAIWTIERKGAKKLDEMPGNWRISREKRNSLDLQEFPIKIEQFPVKKREKTAKNWRKIAVLVCFKRKTTTKNRYLRRPKTKNQRKIEFRRPKTSKNRKLRLKIRPRVRFIDRKLIRRRECLVDPQNLISWIRRQEKAENLRIFQEKQKRLQEQQEDAEWEQIEAQRANSDDVIEDKSLKMEVLDIVKHKNRNWIVVEKKGCEIQGMEYLLVLESEFNEQQTVRYDRQNVDHKFRKMRDEKKEIVEFVSSLPFYKPKPPKINYPTNAGEYEEQEIELERRRLEEEERDQNDKKLEIEDRNHFKKWQKRRNLIKIYRNSIRREIWRRRRGRNSTENSDSESSSEASEPPDDVITKEEPTDFSEENLVKKEEICDDFEHKIEEDVKPDVYKLNINKMISPPSPPPKKGILLKKDTKKRGEKRVKTVQFKLTKRQKLAKLWKPPTWQIRQILRAAADAKGYKIRSGRSRYNEKIRRLNHFNGQKLGFKSAPTRIDTFEKGIDVREQPIPFVEEFVLDDHALLTFASFDDLKAYEEAYSLRQQDVIDEFWRHQCLKNIESFEKDDVERAEMRHEIEKLETEMRCQKMNENAEIDQENIESFETAGRQIENIIKNTGDCAFETLEEYFSISADFEKNEELRAEEEQLEIEMEHWERELEEMIDVIKREFSIENLMMRMLKNRHLLTMRLVVSGTNQSSIDRENLLRKTKKLLEELKNLRIAAQNRLKIDFDRNERMLYRLRNAKQKAAKRARKLVKNWKKSAQNKSGVLKINGNHVINHDVVVKKWKVELKIEGNGESPRKVVRKAKETSGYWDFRWNFTKFAWKSDVLKRKQRFGKHSARRAIAFGVKIEEIHSETEFEKLLSEYVEYEESDIQNQVSIDRKIDIITKIKTITLNDVRAKAIEMQKQIVEKAVDLMIKSRLDEAAREHQEWLQSDECKRENQLRQRQQNFFDLTSSSPATSSFVTTQVVVPRLTHLEERLIELGVEHEVVQHTQRLQSEFENYHHLQQQHNHQNFQQQQQGNHDFVTPKAPQDKQKRKYTKRKALLNTAVASSSDQNGMKSPGSSAMENAAAAAQAAQAQAQATIPTPTVNLPDVVAIAAAAATAQPSAAAAKRPASETPPNGLPKVPRHDEQQQQQNNAHSIVMGAREGFLAMNPSLAGHVFPASSASTSGAPGAHSATTSGGAGLIGISAATQAQLQAQQAAQAAAAAAAAAAAQATQSLYINTSVAPGAQAASAQGGGGGQVVAAQQSNQAATAEAIRLLQGLPPFLTAGSGSAGIPYFSALSQQLNQLGAAAPGAPGTLNGLQFPANAALGPQLAGAALLAAVPGAQQQIKRPGRWSGMHVKIATDIQNYKQSQEKKLPTDIQSTSSSSAAPASAPAPRAGAGAGATSSSAASSSTSTPSSSSHHKKSSPPHHQKSAAPSAPPRDVTSAHAPPPPASSAPIVGAPRQGATPQAAPATTPATTSQHQQSIQFSQFPPPQLSGGAAYAGNPQLMAAAINEATRRVAATPKPPVVRPPSAATQQQPVSVTSQASQQQQQFQQIQQQRAAAIAAAAAATSQQAPPAQASQATSAAQQIATSMGLQPAQVTDLVNQHAQQYLLLQQQQQQQQREQQQQQQLQAQQVQQQLIAHLLGGGHQAQQAAPAVSVAQQQQQQVAAAAAAQQQHNAQLQNIMILTALQQQMERGAAAGAAASLPYQLQLAQAQAQAQAQQAPPTSQPSQAATPQQQQQLDLIRQMEAVAQVQQAHAQAQAQAQAQAQQMQQQQIQQMLMAGQGGPNGQDLIRLLQAAQQQSQAQQQQQQQQAVVAAAQQQQQQQQHNQQLAAAQAAAAAAAAGRPTQNQYEALLQQQRLLAAQQQAAAGASAQQQAAAAAAQAQAQQFQQQLLGLQPNLLLAQVQQAQQAQAQAQAQAQQKPPQMPNGR
null
null
null
cytoplasm [GO:0005737]
null
null
null
null
null
SUBCELLULAR LOCATION: [Isoform d]: Cytoplasm {ECO:0000269|PubMed:22363008}. Note=Forms aggregates. {ECO:0000269|PubMed:22363008}.; SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm {ECO:0000269|PubMed:22363008}. Note=Does not form aggregates. {ECO:0000269|PubMed:22363008}.; SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm {ECO:0000269|PubMed:22363008}. Note=Does not form aggregates. {ECO:0000269|PubMed:22363008}.
null
null
null
null
null
FUNCTION: [Isoform d]: In males, required for non-apoptotic death of the linker cell once it has finished guiding gonad elongation at the end of larval development. May be involved in nuclear envelope crenellation in the linker cell. {ECO:0000269|PubMed:22363008}.; FUNCTION: [Isoform a]: In males, promotes linker cell survival. {ECO:0000269|PubMed:22363008}.; FUNCTION: [Isoform b]: In males, promotes linker cell survival. {ECO:0000269|PubMed:22363008}.
Caenorhabditis elegans
C7IW64
ROS1A_ORYSJ
MQDFGQWLPQSQTTADLYFSSIPIPSQFDTSIETQTRTSAVVSSEKESANSFVPHNGTGLVERISNDAGLTEVVGSSAGPTECIDLNKTPARKPKKKKHRPKVLKDDKPSKTPKSATPIPSTEKVEKPSGKRKYVRKKTSPGQPPAEQAASSHCRSELKSVKRSLDFGGEVLQESTQSGSQVPVAEICTGPKRQSIPSTIQRDSQSQLACHVVSSTSSIHTSASQMVNAHLFPPDNMPNGVLLDLNNSTSQLQNEHAKFVDSPARLFGSRIRQTSGKNSLLEIYAGMSDRNVPDLNSSISQTHSMSTDFAQYLLSSSQASVRETQMANQMLNGHRMPENPITPSHCIERAALKEHLNHVPHAKAAVMNGQMPHSYRLAQNPILPPNHIEGYQVMENLSELVTTNDYLTASPFSQTGAANRQHNIGDSMHIHALDPRRESNASSGSWISLGVNFNQQNNGWASAGAADAASSHAPYFSEPHKRMRTAYLNNYPNGVVGHFSTSSTDLSNNENENVASAINSNVFTLADAQRLIAREKSRASQRMISFRSSKNDMVNRSEMVHQHGRPAPHGSACRESIEVPDKQFGLMTEELTQLPSMPNNPQREKYIPQTGSCQLQSLEHDMVKGHNLAGELHKQVTSPQVVIQSNFCVTPPDVLGRRTSGEHLRTLIAPTHASTCKDTLKALSCQLESSRDIIRPPVNPIGPSSADVPRTDNHQVKVSEETVTAKLPEKRKVGRPRKELKPGEKPKPRGRPRKGKVVGGELASKDSHTNPLQNESTSCSYGPYAGEASVGRAVKANRVGENISGAMVSLLDSLDIVIQKIKVLDINKSEDPVTAEPHGALVPYNGEFGPIVPFEGKVKRKRSRAKVDLDPVTALMWKLLMGPDMSDCAEGMDKDKEKWLNEERKIFQGRVDSFIARMHLVQGDRRFSPWKGSVVDSVVGVFLTQNVSDHLSSSAFMALAAKFPVKPEASEKPANVMFHTISENGDCSGLFGNSVKLQGEILVQEASNTAASFITTEDKEGSNSVELLGSSFGDGVDGAAGVYSNIYENLPARLHATRRPVVQTGNAVEAEDGSLEGVVSSENSTISSQNSSDYLFHMSDHMFSSMLLNFTAEDIGSRNMPKATRTTYTELLRMQELKNKSNETIESSEYHGVPVSCSNNIQVLNGIQNIGSKHQPLHSSISYHQTGQVHLPDIVHASDLEQSVYTGLNRVLDSNVTQTSYYPSPHPGIACNNETQKADSLSNMLYGIDRSDKTTSLSEPTPRIDNCFQPLSSEKMSFAREQSSSENYLSRNEAEAAFVKQHGTSNVQGDNTVRTEQNGGENSQSGYSQQDDNVGFQTATTSNLYSSNLCQNQKANSEVLHGVSSNLIENSKDDKKTSPKVPVDGSKAKRPRVGAGKKKTYDWDMLRKEVLYSHGNKERSQNAKDSIDWETIRQAEVKEISDTIRERGMNNMLAERIKDFLNRLVRDHGSIDLEWLRYVDSDKAKDYLLSIRGLGLKSVECVRLLTLHHMAFPVDTNVGRICVRLGWVPLQPLPESLQLHLLEMYPMLENIQKYLWPRLCKLDQRTLYELHYQMITFGKVFCTKSKPNCNACPMRAECKHFASAFASARLALPGPEEKSLVTSGTPIAAETFHQTYISSRPVVSQLEWNSNTCHHGMNNRQPIIEEPASPEPEHETEEMKECAIEDSFVDDPEEIPTIKLNFEEFTQNLKSYMQANNIEIEDADMSKALVAITPEVASIPTPKLKNVSRLRTEHQVYELPDSHPLLEGFNQREPDDPCPYLLSIWTPGETAQSTDAPKSVCNSQENGELCASNTCFSCNSIREAQAQKVRGTLLIPCRTAMRGSFPLNGTYFQVNEVFADHDSSRNPIDVPRSWIWNLPRRTVYFGTSIPTIFKGLTTEEIQHCFWRGFVCVRGFDRTSRAPRPLYARLHFPASKITRNKKSAGSAPGRDDE
3.2.2.-
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P0AB83}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand. {ECO:0000250|UniProtKB:P0AB83};
base-excision repair [GO:0006284]; DNA demethylation [GO:0080111]; epigenetic regulation of gene expression [GO:0040029]
nucleus [GO:0005634]
4 iron, 4 sulfur cluster binding [GO:0051539]; cytosine C-5 DNA demethylase activity [GO:0051747]; DNA binding [GO:0003677]; DNA demethylase activity [GO:0035514]; DNA N-glycosylase activity [GO:0019104]; metal ion binding [GO:0046872]
PF15629;PF15628;
1.10.1670.10;
DNA glycosylase family, DEMETER subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B8YIE8}.
null
null
null
null
null
FUNCTION: Bifunctional DNA glycosylase/lyase, which excises 5-methylcytosine (5-meC) and 5-hydroxymethylcytosine (5-hmeC), leaving an apyrimidinic (AP) site that is subsequently incised by the lyase activity (Probable). DNA demethylase that is indispensable in both male and female gametophyte development (PubMed:22448681). Involved in the regulation of DNA methylation in the promoters of RISBZ1/BZIP58 and DOF3/RPBF, two transcription factors that functions synergistically to positively regulate genes that are key players in the development of aleurone layers (PubMed:30275307). Active DNA demethylation carried out by ROS1A in rice endosperms may restrict the number of aleurone cell layers (PubMed:30275307). {ECO:0000269|PubMed:22448681, ECO:0000269|PubMed:30275307, ECO:0000305|PubMed:22448681}.
Oryza sativa subsp. japonica (Rice)
C7NBY4
CS13A_LEPBD
MKVTKVGGISHKKYTSEGRLVKSESEENRTDERLSALLNMRLDMYIKNPSSTETKENQKRIGKLKKFFSNKMVYLKDNTLSLKNGKKENIDREYSETDILESDVRDKKNFAVLKKIYLNENVNSEELEVFRNDIKKKLNKINSLKYSFEKNKANYQKINENNIEKVEGKSKRNIIYDYYRESAKRDAYVSNVKEAFDKLYKEEDIAKLVLEIENLTKLEKYKIREFYHEIIGRKNDKENFAKIIYEEIQNVNNMKELIEKVPDMSELKKSQVFYKYYLDKEELNDKNIKYAFCHFVEIEMSQLLKNYVYKRLSNISNDKIKRIFEYQNLKKLIENKLLNKLDTYVRNCGKYNYYLQDGEIATSDFIARNRQNEAFLRNIIGVSSVAYFSLRNILETENENDITGRMRGKTVKNNKGEEKYVSGEVDKIYNENKKNEVKENLKMFYSYDFNMDNKNEIEDFFANIDEAISSIRHGIVHFNLELEGKDIFAFKNIAPSEISKKMFQNEINEKKLKLKIFRQLNSANVFRYLEKYKILNYLKRTRFEFVNKNIPFVPSFTKLYSRIDDLKNSLGIYWKTPKTNDDNKTKEIIDAQIYLLKNIYYGEFLNYFMSNNGNFFEISKEIIELNKNDKRNLKTGFYKLQKFEDIQEKIPKEYLANIQSLYMINAGNQDEEEKDTYIDFIQKIFLKGFMTYLANNGRLSLIYIGSDEETNTSLAEKKQEFDKFLKKYEQNNNIKIPYEINEFLREIKLGNILKYTERLNMFYLILKLLNHKELTNLKGSLEKYQSANKEEAFSDQLELINLLNLDNNRVTEDFELEADEIGKFLDFNGNKVKDNKELKKFDTNKIYFDGENIIKHRAFYNIKKYGMLNLLEKIADKAGYKISIEELKKYSNKKNEIEKNHKMQENLHRKYARPRKDEKFTDEDYESYKQAIENIEEYTHLKNKVEFNELNLLQGLLLRILHRLVGYTSIWERDLRFRLKGEFPENQYIEEIFNFENKKNVKYKGGQIVEKYIKFYKELHQNDEVKINKYSSANIKVLKQEKKDLYIRNYIAHFNYIPHAEISLLEVLENLRKLLSYDRKLKNAVMKSVVDILKEYGFVATFKIGADKKIGIQTLESEKIVHLKNLKKKKLMTDRNSEELCKLVKIMFEYKMEEKKSEN
3.1.-.-
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:27669025}; Note=Pre-crRNA processing is metal independent, while crRNA-guided target RNA cleavage is dependent on divalent metal (i.e. inhibited by EDTA) (PubMed:27669025). {ECO:0000269|PubMed:27669025};
defense response to virus [GO:0051607]
null
endonuclease activity [GO:0004519]; RNA binding [GO:0003723]
null
null
CRISPR-associated endoribonuclease Cas13a family
null
null
null
null
null
null
null
FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements (spacer sequences) and target invading nucleic acids. Unlike many single-component effectors, this CRISPR-Cas system targets RNA (PubMed:27669025). CRISPR clusters are transcribed from pre-CRISPR RNA (crRNA) and processed into crRNA by this protein (PubMed:27669025, PubMed:28475872, PubMed:28757251). pre-crRNA processing yields a 5'-OH and probably a 2',3'-cyclic phosphate (PubMed:27669025). Also cleaves pre-crRNA from several other type VI-A CRISPR systems (PubMed:28475872). Cleaves linear target ssRNA in a crRNA-dependent fashion, preferentially before U residues (PubMed:27669025, PubMed:28475872). Cleavage of target ssRNA is about 80-fold faster than pre-crRNA processing and uses a different active site (PubMed:27669025). Binding a viable target RNA target activates this protein for non-specific RNA degradation in vitro (called collateral RNA degradation) (PubMed:27669025, PubMed:28475872, PubMed:28757251). Activation occurs with 10 fM target RNA (PubMed:28475872). crRNA maturation is not essential for activation of RNA degradation, but lack of mature crRNA (due to mutagenesis) decreases activation levels (PubMed:28475872). This system has a 3' protospacer flanking site in the target RNA (PFS), which is C and unavailable to base pair with crRNA (PFS is equivalent to PAM, the protospacer adjacent motif) (PubMed:28757251). {ECO:0000269|PubMed:27669025, ECO:0000269|PubMed:28475872, ECO:0000269|PubMed:28757251}.
Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b)
C7S340
CABC2_PROVU
LPTLSHEAFGDIYLFEGELPNTLTTSNNNQLSLSKQHAKDGEQSLKWQYQPQATLTLNNIVNYQDDKNTATPLTFMMWIYNEKPQSSPLTLAFKQNNKIALSFNAELNFTGWRGIAVPFRDMQGSATGQLDQLVITAPNQAGTLFFDQIIMSVPLDNRWAVPDYQTPYVNNAVNTMVSKNWSALLMYDQMFQAHYPTLNFDTEFRDDQTEMASIYQRFEYYQGIRSDKKITPDMLDKHLALWEKLVLTQHADGSITGKALDHPNRQHFMKVEGVFSEGTQKALLDANMLRDVGKTLLQTAIYLRSDSLSATDRKKLEERYLLGTRYVLEQGFTRGSGYQIITHVGYQTRELFDAWFIGRHVLAKNNLLAPTQQAMMWYNATGRIFEKNNEIVDANVDILNTQLQWMIKSLLMLPDYQQRQQALAQLQSWLNKTILSSKGVAGGFKSDGSIFHHSQHYPAYAKDAFGGLAPSVYALSDSPFRLSTSAHERLKDVLLKMRIYTKETQIPVVLSGRHPTGLHKIGIAPFKWMALAGTPDGKQKLDTTLSAAYAKLDNKTHFEGINAESEPVGAWAMNYASMAIQRRASTQSPQQSWLAIARGFSRYLVGNESYENNNRYGRYLQYGQLEIIPADLTQSGFSHAGWDWNRYPGTTTIHLPYNELEAKLNQLPAAGIEEMLLSTESYSGANTLNNNSMFAMKLHGHSKYQQQSLRANKSYFLFDNRVIALGSGIENDDKQHTTETTLFQFAVPKLQSVIINGKKVNQLDTQLTLNNADTLIDPTGNLYKLTKGQTVKFSYQKQHSLDDRNSKPTEQLFATAVISHGKAPSNENYEYAIAIEAQNNKAPEYTVLQHNDQLHAVKDKITQEEGYAFFEATKLKSADATLLSSDAPVMVMAKIQNQQLTLSIVNPDLNLYQGREKDQFDDKGNQIEVSVYSRHWLTAESQSTNSTITVKGIWKLTTPQPGVIIKHHNNNTLITTTTIQATPTVINLVK
4.2.2.21
null
carbohydrate metabolic process [GO:0005975]; glycosaminoglycan catabolic process [GO:0006027]
extracellular region [GO:0005576]; periplasmic space [GO:0042597]
carbohydrate binding [GO:0030246]; chondroitin-sulfate-ABC endolyase activity [GO:0034000]; chondroitin-sulfate-ABC exolyase activity [GO:0034001]
PF02278;PF02884;PF09093;PF09092;
2.70.98.10;1.50.10.100;2.60.120.430;2.60.220.10;
Polysaccharide lyase 8 family
null
null
CATALYTIC ACTIVITY: Reaction=Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.; EC=4.2.2.21; Evidence={ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33 uM for chondroitin 6-sulfate tetrasaccharide {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; KM=80 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; KM=9.8 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; KM=16.1 uM for chondroitin 4-sulfate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; KM=19.2 uM for dermatan sulfate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; Vmax=155 umol/min/mg enzyme with chondroitin 6-sulfate tetrasaccharide as substrate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; Vmax=34 umol/min/mg enzyme with chondroitin 6-sulfate as substrate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (PubMed:9083041). Optimum temperature is 37 degrees Celsius (PubMed:18849565). {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the respective disaccharides. To a lesser extent, is also able to split off disaccharide residues directly from polymeric chondroitin 4- and 6-sulfate, dermatan sulfate, chondroitin, and hyaluronan. Is not active against keratan sulfate, heparan sulfate, and heparin. {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}.
Proteus vulgaris
C7SG33
IF4E1_CITLA
MVVEETIKATSTEDLSNTIANQNPRGRGGDEDEELEEGEIVGDDDLDSSNLSAAIVHQPHPLEHSWTFWFDNPSAKSKQATWGASIRPIYTFSTVEEFWSVYNNIHHPSKLALRADLYCFKHKIEPKWEDPVCANGGKWTVNFSRGKSDNGWLYTLLAMIGEQFDCGDEICGAVVNVRSGQDKISIWTKNASNEAAQASIGKQWKEFLDYNDSIGFIFHEDAKKFDRHAKNKYSV
null
null
defense response to virus [GO:0051607]; translational initiation [GO:0006413]
cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]
RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]
PF01652;
3.30.760.10;
Eukaryotic initiation factor 4E family
PTM: According to the redox status, the Cys-133-Cys-171 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.
null
null
null
null
null
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (PubMed:19820912). {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:19820912}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:19820912}.
Citrullus lanatus (Watermelon) (Citrullus vulgaris)
C7YZ74
ARO1_FUSV7
MAEAKKPGPERISILGEANIIVDHGLWLNFVVDDLLQNTPTSTYVLITDTNLFDTYVPAFQAQFEAAAEGKATRLLTYTIPPGEASKSRETKAEIEDWMLSQQCTRDTVIIALGGGVMGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPKRIYIDLAFLETLPVREFINGMAEVVKTAAIWNETEFTVLEESAAHILECVRSKGEGRLTPIKDVLKRIVIGSAGVKAEVVSSDEREGGLRNLLNFGHSIGHAIEAILTPQLLHGEAVAIGMVKEAELARYLGVLRPGAVARLVKCIASYDLPTSIHDKRVVKLTAGKKCPVDVLLQKMGVDKKNDGQKKKIVLLSAIGKCHEPRASVVDDKTIRTILSPSIQVTPGVPSNLDVTVTPPGSKSISNRALVLAALGLGSCRIKNLLHSDDTEYMLSAIHQLGGASYSWQDAGEVLVVDGKGGNLQASKEALYLGNAGTASRFLTTVVALCSPSESASSTILTGNARMKVRPIGPLVDALRSNGVEIEYQGKENSLPLRVDAAGGLKGGVIELAATVSSQYVSSILMAAPYAKNPVTLRLVGGKPISQPYIDMTISMMASFGVHVTASSDEPNTYHIPQGQYQNPSEYIIESDASSATYPLAIAAITGTTCTIPNIGSKSLQGDARFAVDVLQPMGCTVNQSDYSTTVTGPAPGELKGLPHVDMEPMTDAFLTASVLAAVASGKTQITGIANQRVKECNRIAAMKDQLAKFGVQCNELDDGIEVLGKGQDGGISAPTVGIHCYDDHRVAMSFSVLAVASPSPVIVTERECVGKTWPGWWDILSQAFKVDMIGHEPDANADEEDSKSSVMERSVFIIGMRGAGKTTAGNWMAKMLGWKFIDLDQELERRAGCTIPEMIRGSRGWEGFRADELSLLKDVMAKNSHGHIFSCGGGLVETPEARQLLKDYGRNGGNVLLIHRDTEQVVEYLMRDKTRPAYTSEIREVYLRRKDFYQECSNLLYYSPHSESSGSKSEIPCDFQQFVSSISGRSTHLKDVMEKDHSFFVSLTVPDVSEAASLIPEVVVGSDAVELRVDLLQDRSVDSVTRQVSILRALAKKPIVFTLRTVSQGGKFPDEAYEEGLELYRLALRMGMEYVDVEMTLPENIIQTVTESRGHSRIIASHHDPQGTMSWKNASWIPFYNRALQFGDIIKLVGVARSSEDNFDLAKFKSRMQEAQKTPMIAMNMGKAGKLSRVLNKFLTPVSHPALPFKAAPGQMSAAEIRRGLALLGDLDPCNFYLFGKPISASRSPALHNTLFGQTGLPHQYHRLETDNIQDVREVLQAPDFGGASVTIPLKLDVMGQVDELSEAARTIGAVNTVVPIGKADASDRRRLLGDNTDWRGMVHALRDEGVEEQADSETKGAAMVVGSGGTTRAAIFALHSLGFGPIYIAARNQAKVDALAADFPAEYQLQGLSQPSDADKVSSNLNVVISTIPADRPIDPSLQELVGALLSRPAVGTERRVLLEMAYKPSHTPIMQLADEAGNWTTVPGLEVLASQGWYQFELWTGITPLYRDARSAVLGL
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF18317;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4) (Fusarium solani subsp. pisi)
C8KI33
SUV2_ARATH
MSGNDEEFNDEFLLAIDSIETTLKKADMYRPLPPPYLPTFLPAPPPSTKISSSLSHPMQLQSSAGQQRKQIQVPDPFLSYSPPRELSQRVVSGFNDALMDYSNSTVVTAAKPISPTTSNRRCDSEKDLEIDRLKKELERVSKQLLDVEQECSQLKKGKSKETESRNLCADDNRGQCSTVHASKRIDLEPDVATSSVNHRENDSRMALDDKRSFKTTGVQADVANHSDLSKKLLDIWRTSNYQDPRKNLISELLLACSTDLQILFSFMKISTPPQELNKQEAKTSSDRQSSKALESEKVYQLYSAVTKISYGFVNLKTLVEPLLDLCKAETAVLVHRSLRVLHVLLEHICGDEKRFEASWDANWHSLFKLMNQIASKRTEQDVKQEALSIMNIIVMSTDAYTARESFVSKEVFESISLLLRKEGGLHVRKEAIHLFYLLLNCPKLYDTFDSLHEEKNSSDTENDSEGNFFALEAFGKIFEGLADCLTSPRKTSEDLELCRNVIMILALAASSGNSGYELLSSHKLPQDSSFLMLILHLLVAEIDSESTEFHPKAEIFKARTLLMREILILLNRLVSGLSSSATILKELTTSRDMASLTVDAATRLSRKRNLLGKPESSVERMRNTEIMDLARIFKKRVFAFLGDNTI
null
null
DNA damage response [GO:0006974]; positive regulation of cell cycle G2/M phase transition [GO:1902751]; regulation of cell cycle [GO:0051726]; response to aluminum ion [GO:0010044]; response to cisplatin [GO:0072718]; response to gamma radiation [GO:0010332]; response to hydroxyurea [GO:0072710]; response to ionizing radiation [GO:0010212]; response to UV-B [GO:0010224]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
phosphoprotein phosphatase activity [GO:0004721]; protein dimerization activity [GO:0046983]
null
null
Serpin family
PTM: Probably phosphorylated by ATR. {ECO:0000269|PubMed:28556304}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:28556304}. Cytoplasm {ECO:0000269|PubMed:28556304}.
null
null
null
null
null
FUNCTION: Required for tolerance to DNA-damaging and cross-linking agents such as UVB irradiation, gamma-radiation, aphidicolin, ionizing radiation and hydroxyurea (HU), cisplatin (CDDP) and mitomycin C (MMC) (PubMed:19619158, PubMed:19619159, PubMed:28556304). Involved in cell-cycle G2/M arrest in response to DNA damage (PubMed:19619158, PubMed:19619159). Required for aluminum-dependent gene regulation and root growth inhibition in an ATR-dependent manner by halting cell cycle progression and triggering loss of the quiescent center (QC) (PubMed:28556304). {ECO:0000269|PubMed:19619158, ECO:0000269|PubMed:19619159, ECO:0000269|PubMed:28556304}.
Arabidopsis thaliana (Mouse-ear cress)
C8V7P4
IVOA_EMENI
MASPIIQPAGAGIHDIFTQLELWESIDKGLSMITILRDNDVLWKPFLQLTLFNQLNIVRKAWSATIQKASESDKVPTLKDVYTSESSFIAQALLDTKNLQITPPATPRTALSGALLAKTIVIFHHSERAQEELGTELPEEVRSLVNQNAICLKVLYNANQWHIDLHYKRDSLSSAQAGEVAEIFEQYLEEALEAVASAIPPSPPVEDDNAGHGGLCKERTDCPKVNRCIHDLIEEQAIARPDQEGICAYDGSLSYAGLSKLSSVLAEQLKTFGARPEQRVAILMNKSFWYPVVVLAVLKSGAAFVPLDPSHPKNRLKQLISEIEPCALITTSVLSELADDLGCPSLAIDSDLTRSKEGSTTALLPNTSASPNNAAYIIFTSGSTGKPKGVVVEHSALSTSAITRGVVLGLGPDSRVLQYAPHTFDVSVDEILTTLIHGGCVCVPSEDDRFSIAHFMESARVTVALLTPTSARTLHPDEVPSLRILQTGGEVLTEDVNDKWSNRVTLFNVYGPTEASVACVISNRTGLKGAGHVLGQAVGGKLWIVDPDDIERHLPDNEVGELVISGAILARGYFRDPSRTESSFVRMRNGERVYRTGDLASMDSAGTIIYHGRKDLEVKIRGQRINIAEIEIAILQCDLVHSVVVEYPRSGLFEKKLVAVLRFEDSSSDAEDGLFGGAKGLTEDIYCLLLSHVSSVLTPAMIPSKWLSLPCVPQMPSGKADRKQVRGWLEDMDKRTYTRIFHPNGTDNLISDPSDSMVAIWLKVLKLEPQSLRLDQSFIRNGGDSIMAMEARHQAHEAGINIDVRELLGSRALQEIGEMATKTSAVEEVSKIEDDRDEPFPLSPVQQMYFDKVSDPSLGLQQRVCVEIMTKIQPDMLREALNHVIQKHRMLAARFTKHMGQWMQQVPFGKNLKHLSRCHIYSQAVGSLGDFCSEPMALEDGTLLHAHLQSSGERQTLVLCVHHLVVDFVSWRVILQDLHDALAAAQNGLPSGISRSTLTFQQWCREQTKYASTLIPEAVLPFAPGPVNLRFWQPSNVQAVSNTYSEIVQHDFRLSSTQTTQMLEKFTTATVHPTDLMLATFALAFKRIFTERDTPTIFIEGHGREPWHASLDVSQTVGWFTAAFPIHLPKDTLLNTTTAILGASERRRSVLANGHPYWACRYLSPNGQKVFGDDPRHQEMEFVFNYAGSIVQRAPGQTLFAENVRIAEIGHPNCERFSLFDIGAAIEMPSSELVVSFTFPKGIAHRERVAELVKTYQELLETAVERDLDLSAKLSSPLVCPADVVRSLEVNGVCIERDVEIVYTPSSIQQHMLWRQSQEPWFYRVQGDWTIEKTTTQSEPVDIDRLSHAWNQVVHRHTTLRTVFRYSSEEERFVAIVLHEVKPAISIIRKGIQTSGSLCRDDDLSPPHRMVLREKDNGSVVCELEFSHTIIDAASRSIVVQDLLDAYDGKLAHRPLDFPPFWEYIRLAQSSTPSARKEELHRAGRVVTLPFQPTHVLSKVPEACKKNEITISSFFMTAWSIVLAKHFVAHNQRVDSTSSQAVAFDYVLSDRSANIPGIESAVGPYIRLPTLETHVKEGVSLKNIARGLHAQCTFQSLSQSTQDGSSLELPSKATALQKYSTLVNIRNSGSDSLDLVSDSGEWKWILQGFSDPWDYDLVFAVNVHAGKVTGWTVEYADGVVEHSAADEIAKDLNDVVERMVCEII
5.1.-.-
null
amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; conidium formation [GO:0048315]; pigment biosynthetic process [GO:0046148]; positive regulation of conidium formation [GO:0075307]; secondary metabolic process [GO:0019748]; secondary metabolite biosynthetic process [GO:0044550]
cytoplasm [GO:0005737]; fungal-type cell wall [GO:0009277]
isomerase activity [GO:0016853]; phosphopantetheine binding [GO:0031177]
PF00501;PF00668;PF00550;
3.30.300.30;1.10.1200.10;3.30.559.10;3.40.50.12780;3.30.559.30;
NRP synthetase family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-tryptophan = AMP + D-tryptophan + diphosphate + H(+); Xref=Rhea:RHEA:63892, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57719, ChEBI:CHEBI:57912, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:31573806}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63893; Evidence={ECO:0000269|PubMed:31573806};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for L-tryptophan {ECO:0000269|PubMed:31573806};
PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:28108400, ECO:0000269|Ref.3}.
null
null
FUNCTION: Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment (PubMed:23617571, PubMed:28108400). The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion (PubMed:31573806). While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function (PubMed:31573806). D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC (PubMed:28108400). N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment (PubMed:2126551, PubMed:28108400, Ref.3). {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:23617571, ECO:0000269|PubMed:28108400, ECO:0000269|PubMed:31573806, ECO:0000269|Ref.3, ECO:0000305|PubMed:31573806}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VBH4
ESA1_EMENI
MGVRDSHGEAAGTPDPVEKGIATLNTIRIGVKAMVHKDGALRKAEILSIKQRKDGLAFYVHYVDFNKRLDEWVASSRLDLSQEVEWPQPEKPEKKKSGPAKAPSKNKRVRAGSRDVSATPDTLTGKNTNVGKAQRPSKAGGKENRGDETPADLSMLASEAVSADGTPKAVSEDIDMMDASFTDAKEIKEEERALGLMSREEEIEKLRTSGSMTQNPTEVHRVRNLDRLQMGKYDIEPWYFSPYPASFSDAEVVYIDEFCLSYFDNKRAFERHRTKCTLTHPPGNEIYRDDNISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKESGEGYNLACILTLPQYQRRGYGRLLISFSYELSKREGKVGSPEKPLSDLGLLGYRQYWRETLVEILLDSGRETVSENELAMLTSMTEKDVHETLVTFKMLRYNKGQWIIVLTDEVIEERNKRLEKEKIKGSRKIDPARLQWKPPVFTASSRTWNW
2.3.1.-; 2.3.1.48
null
DNA repair [GO:0006281]; DNA-templated transcription elongation [GO:0006354]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of triglyceride biosynthetic process [GO:0010867]; rDNA heterochromatin formation [GO:0000183]; regulation of cell cycle [GO:0051726]; regulation of secondary metabolite biosynthetic process [GO:1900376]; regulation of transcription by RNA polymerase II [GO:0006357]
NuA4 histone acetyltransferase complex [GO:0035267]; nucleosome [GO:0000786]; nucleus [GO:0005634]; piccolo histone acetyltransferase complex [GO:0032777]
chromatin binding [GO:0003682]; histone crotonyltransferase activity [GO:0140068]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K16 acetyltransferase activity [GO:0046972]; peptide 2-hydroxyisobutyryltransferase activity [GO:0106226]; transcription coregulator activity [GO:0003712]
PF01853;PF11717;PF17772;
2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10;
MYST (SAS/MOZ) family
PTM: Autoacetylation at Lys-320 is required for proper function. {ECO:0000250|UniProtKB:Q08649}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94446}. Chromosome {ECO:0000250|UniProtKB:O94446}. Note=Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs). {ECO:0000250|UniProtKB:O94446}.
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:O94446}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000250|UniProtKB:O94446}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q08649}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; Evidence={ECO:0000250|UniProtKB:Q08649}; CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:O94446}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; Evidence={ECO:0000250|UniProtKB:O94446}; CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q08649}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; Evidence={ECO:0000250|UniProtKB:Q08649};
null
null
null
null
FUNCTION: Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (By similarity). Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (By similarity). {ECO:0000250|UniProtKB:O94446, ECO:0000250|UniProtKB:Q08649}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VG90
ACON_EMENI
MITTRLARMGALAPKSRLLFGTRGMATVADLDKKVEMCNLEKGNYINYKKMSENLDVVRRRLTRPLTYAEKILYSHLDDPQNQDIERGKSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTVHCDHLIEAQLGGEKDLARANEINKEVYDFLASSTAKYNIGFWKPGSGIIHQIILENYAFPGGLMIGTDSHTPNAGGLAIAAIGVGGADAVDVMAGLPWELKAPKVIGVRLTGEMSGWTAPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSATGMATICNMGAEIGATTSLFPFNDRMYDYLKATKRQQIGDFARSYAKDLREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISQFKEAVKANGWPEELKVGLIGSCTNSSYEDMSRAASIAQDALDHGLKAKSIFTVTPGSEQIRATIERDGQLKTLEEFGGVILANACGPCIGQWDRKDVKKGTPNSIVSSYNRNFTGRNDANPATHAFVTSPDLVVALSIAGTLNFNPLTDTLKDKDGKEFKLKAPTGDGLPSRGYDPGRDTYQAPPTDRSSVDVAVSPSSDRLQLLAGFQPWDGKDATGIPILIKCQGKTTTDHISMAGPWLKYRGHLDNISNNMLIGAVNAENGEANKIKNVFTGEYGAVPATARDYKARGVKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFSDPADYDRIPPDATVDLLCTELAVDKPMTLRVHPKDGASFDVKLSHTFNESQIEWFKDGSALNTMARKSGN
4.2.1.-; 4.2.1.3
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
lysine biosynthetic process via aminoadipic acid [GO:0019878]; mitochondrial genome maintenance [GO:0000002]; tricarboxylic acid cycle [GO:0006099]
cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]
4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]
PF00330;PF00694;
3.40.1060.10;3.30.499.10;3.20.19.10;
Aconitase/IPM isomerase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:23106124}; CATALYTIC ACTIVITY: Reaction=(2R)-homocitrate = cis-homoaconitate + H2O; Xref=Rhea:RHEA:26101, ChEBI:CHEBI:15377, ChEBI:CHEBI:58174, ChEBI:CHEBI:58884; Evidence={ECO:0000269|PubMed:23106124};
null
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.; PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 2/5.
null
null
FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Also catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. {ECO:0000269|PubMed:23106124}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VJQ3
ASQI_EMENI
MTCTLRDLNSLLEICCRCPAHNPSTAFAPTTKVRVSSDVRGIFALPVQKDHKPYNGLSPEHLETMKAVSLMLDAAGPKLEDGISKAKELLEERINPELMRDALGIYLTHSKDAQQRKIFPPPLKNHPFFSTKTRRPANVAGEICTADTLHGHALLSYWRDDYDLNDSHYYWHMVYRGAGGDNSKNVGDFDRHGEVFLYVHSQMVARYETESLCWSLPLVRPWNQYDDFLENGYAPISSLIEHYGGYPPFSTWYSIRNPDMPDTLNVTIPRARLEEWRDNIYAAIRKGQFETTSKDKPLVLTRDNCLNFVGGILDAQYPSLNKLLGGCSLDEERYGNLHNYGLGKFAEMAYRNKPGEKSPYGLTISNFGAPRDPCFWRWYKHLQYYGRLAATRYPQDITAHRAEVVLSNLVVRLQDRSSPHYLDGHITTFLGPPAVNFMESKAKLGHEPYEWNVQVKSCRRSPPSKENPQTLTLRLFIAAEDLMNDYHSWIEMDRATVQLTDESAITKVRLDTDSSVARKMGNYGEPDPRYASAVFRHGWPQNLMLPVGKVEGMPFVAFCIATDDGIPDPAPAPPFHHYHDPRGMGYPFNRAWTQLTEDSTGKASIRTIISNAELYPFITSTTFKIYRTTKFETKQIIQPTTVTWFNTIRGYFKDADRACMRSEYGYDLYNYDHVMLHADAILDATASKRMPLQMGKYTQDNPDPEHPLWTVKMCENFRAWLLNGCPKGTDPA
4.1.99.27
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30026518}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:30026518};
null
null
lyase activity [GO:0016829]; metal ion binding [GO:0046872]
PF03723;PF00372;
1.10.1280.10;2.60.40.1520;
Tyrosinase family
null
null
CATALYTIC ACTIVITY: Reaction=(-)-cyclopenine = H(+) + methyl isocyanate + viridicatin; Xref=Rhea:RHEA:73415, ChEBI:CHEBI:15378, ChEBI:CHEBI:59059, ChEBI:CHEBI:193522, ChEBI:CHEBI:193553; EC=4.1.99.27; Evidence={ECO:0000269|PubMed:30026518}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73416; Evidence={ECO:0000269|PubMed:30026518}; CATALYTIC ACTIVITY: Reaction=(-)-4'-methoxycyclopenine = 4'-methoxyviridicatin + H(+) + methyl isocyanate; Xref=Rhea:RHEA:74463, ChEBI:CHEBI:15378, ChEBI:CHEBI:59059, ChEBI:CHEBI:193535, ChEBI:CHEBI:193536; EC=4.1.99.27; Evidence={ECO:0000269|PubMed:30026518}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74464; Evidence={ECO:0000269|PubMed:30026518};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.068 mM for (-)-Cyclopeptin {ECO:0000269|PubMed:30026518}; KM=2.86 mM for 4'-methoxycyclopenin {ECO:0000269|PubMed:30026518};
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30026518}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:30026518}.; PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30026518}.
null
null
FUNCTION: Cyclopenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934, PubMed:30026518). Within the pathway, the cyclopenase asqI catalyzes the conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). The first step of the pathway is catalyzed by the nonribosomal peptide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin. 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ. AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI. 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B. The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain. The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin. Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (Probable). {ECO:0000269|PubMed:25251934, ECO:0000269|PubMed:30026518, ECO:0000305}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VJW0
HXNR_EMENI
MKAKMKKHACTYPGCSKAFTRAEHLRRHSLNHETISNSQGYTCQRCMTHFSRADLLSRHLDRHAKKDAEAGGFGKGVLETRKRMRRAEDGSIVLRPPKRPSRHQQKTGPPVGAPLSSSGSVSAGSGRSSRSPDVSLHAAQAPVSPPRSASDPVSVSGVSIDDDGTDPDPMLAPMMPGGPFEPYVEPIPGQFDAADGSWGGFDALGDGMMLDTATDFNLPFAATGNYNWLFDVSSLDDAFHHLELPLGPDLVPFANSHGNYASVNTMELSGAGAENVQDSMLNLDLDIDLNGLPAGFVHDQGPDGSSASVLLQAASFVERGNINGSDPKRDFPDLDWMAGAPPIESTVPLRPQLSEDARRGILTLIAQSPPVDIHGQPLNLDSPLLSLSALQSYSDLFFSRFNTTYPLIHSATFDPNKTEPVFLASILSMGATYSSREAHQLAVGIHDGLRNQLFCHGAFSPQPDELWVLQAMLLIDCFGKMRAGPKQRERAQLFHCVLIKLIRRSTCCSIRADTHSDPGLGGLELEDAWKRAMDAEQRKRLAFQCFMWDTEHSVLFSQSLCMSAFEIRSSLPCSPAAWEAHTAEEWSRHASRDTEHAFLPVLKGYITPGSVSRPRDLNRFSRMVVLHGLMSISADLKRRDQTTLRAETPERVGAWTPRMGRAYDLWKADFDADCLNMKLGPVQVSADETRRFTSLKAAAMALYRAASLALHVEVLDLQIAAGASHILGRVVKQHDRERSRVMLSRWLSGPSPAATTASRHAAALLQDAVLSLHDWDQTDAFHFPWCLYLATLTVWAFHAREGCVPKPTDLSSLIVAMTTSNAADLEGLAGQYDTRPLIRAMAQQLATVRWAVVHDAMKVLLNLGV
null
null
DNA-templated transcription [GO:0006351]; regulation of transcription by RNA polymerase II [GO:0006357]
chromatin [GO:0000785]; nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
PF04082;
3.30.160.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:29212709}.
null
null
null
null
null
FUNCTION: Transcription factor that specifically regulates the expression of the hxn gene cluster that mediates the degradation of nicotinate and related metabolites (PubMed:29212709, PubMed:4581274). {ECO:0000269|PubMed:29212709, ECO:0000269|PubMed:4581274}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VQG9
LAEA_EMENI
MFEMGPVGTRLPAMTSPAHNHYSYHSPTSSDRGRSRQNSDAMDIQSITEREPATRYAVAGGPAPWNRNGSPSMSPMYSNNSERNQFHEENGRTYHGFRRGMYFLPCDEQEQDRLDIFHKLFTVARVSESLIYAPHPTNGRFLDLGCGTGIWAIEVANKYPDAFVAGVDLAPIQPPNHPKNCEFYAPFDFEAPWAMGEDSWDLIHLQMGCGSVMGWPNLYRRIFAHLRPGAWFEQVEIDFEPRCDDRSLDGTALRHWYDCLKQATAETMRPIAHSSRDTIKDLQDAGFTEIDHQIVGLPLNPWHQDEHERKVARWYNLAVSESIENLSLAPFSRVYRWPLERIQQLAADVKSEAFNKEIHAYNILHIYQARKPLR
2.1.1.-
null
ascospore formation [GO:0030437]; biological process involved in interaction with host [GO:0051701]; methylation [GO:0032259]; penicillin metabolic process [GO:0042316]; positive regulation of ascospore formation [GO:0075296]; positive regulation of penicillin metabolic process [GO:0033246]; positive regulation of sterigmatocystin biosynthetic process [GO:0010914]; regulation of secondary metabolite biosynthetic process [GO:1900376]; sterigmatocystin metabolic process [GO:0045460]
nucleus [GO:0005634]
methyltransferase activity [GO:0008168]
PF13489;
3.40.50.150;
Methyltransferase superfamily, LaeA methyltransferase family
PTM: Self-methylates at Met-207. {ECO:0000269|PubMed:23532849}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18556559}.
CATALYTIC ACTIVITY: Reaction=L-methionyl-[protein] + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionyl-[protein]; Xref=Rhea:RHEA:60560, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:15592, ChEBI:CHEBI:16044, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:142742; Evidence={ECO:0000269|PubMed:23532849}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60561; Evidence={ECO:0000269|PubMed:23532849};
null
null
null
null
FUNCTION: Methyltransferase that performs automethylation at Met-207 (PubMed:23532849). No other methyl-accepting substrate has been identified yet (PubMed:23532849). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (PubMed:15075281, PubMed:20132440). Controls the expression of the sterigmatocystin, penicillin, and lovastatin gene clusters (PubMed:15075281, PubMed:16968230). Controls light-dependent formation of the velB-vosA complex, veA protein modification, and is required for light-mediated inhibition of sexual development (PubMed:21152013). Within the velvet complex, controls light-dependent secondary metabolism (PubMed:18556559). Involved in the defense response against Drosophila melanogaster larval grazing (PubMed:24023705). {ECO:0000269|PubMed:15075281, ECO:0000269|PubMed:16968230, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:20132440, ECO:0000269|PubMed:21152013, ECO:0000269|PubMed:24023705}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VQY7
YPT7_EMENI
MSSRKKVMLKVIILGDSGVGKTSLMNQYVNKKFSGSYKATIGADFLTKEVLVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFEALDSWRDEFLIQASPRDPESFPFVVIGNKIDMEESKRMISSKRAMTFCQSKGNIPYFETSAKEAVNVEQAFEVIARSALAQEEAEEYGGDYTDPINIHDTTERDGCAC
null
null
endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]; regulation of vacuole fusion, non-autophagic [GO:0032889]; vacuole fusion, non-autophagic [GO:0042144]
fungal-type vacuole membrane [GO:0000329]; late endosome [GO:0005770]; phagocytic vesicle [GO:0045335]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
PF00071;
3.40.50.300;
Small GTPase superfamily, Rab family
null
null
null
null
null
null
null
FUNCTION: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). AvaA functions in vacuolar biogenesis (PubMed:12095681). {ECO:0000250|UniProtKB:P32939, ECO:0000269|PubMed:12095681}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VSZ2
XANA_EMENI
MPAITVKPLTPPAGSAIDFGAVITDVDLEHLTDGDFSTIRSALYTHLVVVLKNQHQLTPKAQYELTRRFDPSATQYGHGKTLDAKRSILHPDLKTIPHQPQVQVIGHGFIDSYEGLENITLKHPHHRTFHRDPIPQEDDYDSTRFYRWHIDAALYGLNPPIVTTLLAVKVPGGRRQTVRYDDGSGETMDVPLGTTAFASGERMFELLSEEDKEFALSSRVEYAPHPYIWMSPARSLPTGLGLHSDDLELPLSELPPIDESAIQILPMVWKNPATGKPALQIHPSAVRKIHCGDGTVIDDLKKVREIAYKLQRPAISPQYVYAHDWEEGDLVLFHNRGVLHSVVGAFGEGEVRLFRQCNLAAGEGVVPYRE
1.14.11.48
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610};
heterocycle metabolic process [GO:0046483]; organic cyclic compound metabolic process [GO:1901360]
cytosol [GO:0005829]
alpha-ketoglutarate-dependent xanthine dioxygenase activity [GO:0097641]; metal ion binding [GO:0046872]
PF02668;
3.60.130.10;
TfdA dioxygenase family
PTM: Glycosylated (PubMed:17429948). Is subject to both N- and O-linked glycosylation (PubMed:17429948). {ECO:0000269|PubMed:17429948}.; PTM: Phosphorylated. {ECO:0000269|PubMed:17429948}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24970358}.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + xanthine = CO2 + succinate + urate; Xref=Rhea:RHEA:43120, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:30031; EC=1.14.11.48; Evidence={ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43121; Evidence={ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31.1 uM for 2-oxoglutarate (at 25 degrees Celsius) {ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}; KM=50 uM for 2-oxoglutarate (at 30 degrees Celsius) {ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948}; KM=45.2 uM for xanthine (at 25 degrees Celsius) {ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}; KM=46 uM for xanthine (at 30 degrees Celsius) {ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948}; KM=0.16 mM for alpha-ketoadipic acid (at 25 degrees Celsius) {ECO:0000269|PubMed:17429948}; KM=0.4 mM for 9-methylxanthine (at 25 degrees Celsius) {ECO:0000269|PubMed:18036331};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 to 7.4. {ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948};
null
FUNCTION: Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate to succinate and CO(2) while hydroxylating xanthine to generate uric acid (PubMed:15948966, PubMed:17429948, PubMed:18036331). Allows xanthine utilization as a nitrogen source (PubMed:15948966). Whereas xanA is highly specific for xanthine, alpha-ketoadipic acid can replace alpha-ketoglutarate as a cosubstrate (PubMed:17429948). Exhibits ferroxidase activity in the absence of substrates (PubMed:18036331). {ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VTS4
VELB_EMENI
MYAVEDRAHSGHHPPPLSMDRIPPPSTMYPSSAGPSAMVSPAGQPEPESLSTVHDGRIWSLQVVQQPIRARMCGFGDKDRRPITPPPCIRLIVKDAQTQKEVDINSLDSSFYVVMADLWNADGTHEVNLVKHSATSPSISTAMSSSYPPPPHPTSSDYPASYQTNPYGQPVGQPVGQPVGYAGVGNYYGGSTQLQYQNAYPNPQAQYYQPMYGGMAQPQMPAAQPVTPGPGGMFTRNLIGCLSASAYRLYDTEDKIGVWFVLQDLSVRTEGIFRLKFSFVNVGKSVSDLPQSDIAEVINKGTAPILASTFSEPFQVFSAKKFPGVIESTPLSKVFANQGIKIPIRKDGVKGQGSRGRHSDEDDGLDNEY
null
null
cellular response to light stimulus [GO:0071482]; conidium formation [GO:0048315]; negative regulation of conidium formation [GO:0075308]; positive regulation of sexual sporulation resulting in formation of a cellular spore [GO:0043941]; positive regulation of sterigmatocystin biosynthetic process [GO:0010914]; sexual sporulation resulting in formation of a cellular spore [GO:0043935]; sterigmatocystin biosynthetic process [GO:0045461]; trehalose biosynthetic process [GO:0005992]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
null
PF11754;
2.60.40.3960;
Velvet family, VelB subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18556559}. Cytoplasm {ECO:0000269|PubMed:18556559}. Note=VeA increases the nuclear localization of VelB. {ECO:0000269|PubMed:18556559}.
null
null
null
null
null
FUNCTION: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (PubMed:18556559, PubMed:23049895). The velvet complex acts as a global regulator for secondary metabolite gene expression (PubMed:18556559). Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (PubMed:21152013, PubMed:24391470). The velB-VosA complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (PubMed:24391470). The vosA-velB complex binds to the beta-glucan synthase fksA gene promoter in asexual spores for repression (PubMed:25960370). {ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:21152013, ECO:0000269|PubMed:23049895, ECO:0000269|PubMed:24391470, ECO:0000269|PubMed:25960370}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8VTV4
VEA_EMENI
MATLAAPPPPLGESGNSNSVSRITREGKKITYKLNIMQQPKRARACGQGSKSHTDRRPVDPPPVIELNIFESDPHDDSNKTDITFVYNANFFLFATLEPERPIATGKLMTNQGSPVLTGVPVAGVAYLDKPNRAGYFIFPDLSVRNEGSYRFSFHLFEQIKDPKDATEGTQPMPSPVPGKLSSPQEFLEFRLEVISNPFIVYSAKKFPGLTTSTPISRMIAEQGCRVRIRRDVRMRRRGDKRTEDYDYDNERGYNNRRPDQYAGSDAYANAPERPRSTSISTNMDPYSYPSRRPSAVEYGQPIAQPYQRPMASTPAPSSTPIPAPIPMPGPVALPPSTPSPASAHAPAPPSVPLAAPPPLHTPSYQSHLSFGATQTQYPAPQLSHIPQQTTTPTHPYSPRSSISHSRNQSISEYEPSMGYPGSQTRLSAERPSYGQPSQTTSLPPLRHSLEPSVNSRSKTPSNMITSLPPIQSLSELPSTTSQPSSAIGSSPANEPGPRLWETNSMLSKRTYEESFGHDDRPLYNGMRPDSESYPGGMQRRPSYERSSLLDGPDQMAYKRANGRMVSKPATMR
null
null
sporulation resulting in formation of a cellular spore [GO:0030435]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
null
PF11754;
2.60.40.3960;
Velvet family, VeA subfamily
PTM: Phosphorylated at Thr-167, Thr-170, Ser-183 and Tyr-254 (PubMed:26564476). Thr-167 should be phosphorylated and T170 and S183 should be dephosphorylated to achieve light induction of conidiation (PubMed:26564476). Phosphorylation of Ser-183 and Tyr-254 influence sterigmatocystin production in a light-independent manner (PubMed:26564476). Phosphorylation of Thr-167 and Thr-170 modulates expression of veA (PubMed:26564476). {ECO:0000269|PubMed:18936976, ECO:0000269|PubMed:26564476}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:19318129, ECO:0000269|PubMed:20816830, ECO:0000269|PubMed:23341778}. Cytoplasm {ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:19318129, ECO:0000269|PubMed:20816830, ECO:0000269|PubMed:23341778}. Note=Enriched in the nucleus in the dark (PubMed:17163983, PubMed:18556559, PubMed:20816830). Migration to the nucleus depends on the importin alpha carrier protein KapA (PubMed:17163983, PubMed:19318129). Migration to the nucleus is also controlled by llmF (PubMed:23341778). {ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:19318129, ECO:0000269|PubMed:23341778}.
null
null
null
null
null
FUNCTION: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (PubMed:12223191, PubMed:14665453, PubMed:18556559, PubMed:19210625, PubMed:2076818, PubMed:2253875). The velvet complex acts as a global regulator for secondary metabolite gene expression (PubMed:18556559). Controls the expression of the sterigmatocystin and penicillin gene clusters (PubMed:14665453, PubMed:17375284). Represses the cryptic ors gene cluster producing orsellinic acid and its F9775 derivatives in a laeA-independent manner (PubMed:23841751). Required for full induction of faoA gene expression by fructosyl amines (PubMed:12375102). Positively regulates the expression of the early sexual development gene esdC (PubMed:17977758). Controls the expression of mannoprotein mnpA (PubMed:12620259). {ECO:0000269|PubMed:12223191, ECO:0000269|PubMed:12375102, ECO:0000269|PubMed:12620259, ECO:0000269|PubMed:14665453, ECO:0000269|PubMed:17977758, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:19210625, ECO:0000269|PubMed:2076818, ECO:0000269|PubMed:2253875, ECO:0000269|PubMed:23841751}.
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
C8WLM1
CGR2_EGGLE
MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAELCMQQAVCMNDSIYVGGISDWGMSEILGKDVNIHDSSNIDAILVDKTGRRFCQDDAEWGYVMHECAQAAWKQGFTPDDPTTGYIFYVYDATGAPFFEMKGHTPDTCDTTFSADSVDGLAEFIGCDPTALASEVERWNSFCEAGLDADFGRRANMAPIATPPFYCDVVRPGPMGTFAGAKSNVEAEIIGLDGNPIPRLYGAGCIIGGNVSGAFYFGCGWSITNTVVWGREAGRNVAALEPWE
1.3.2.-
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29761785}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:29761785};
response to toxic substance [GO:0009636]; steroid metabolic process [GO:0008202]
plasma membrane [GO:0005886]
4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; steroid dehydrogenase activity, acting on the CH-CH group of donors [GO:0033765]
PF00890;
3.50.50.60;3.90.700.10;
FAD-dependent oxidoreductase 2 family
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}.
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side {ECO:0000305|PubMed:29761785}.
CATALYTIC ACTIVITY: Reaction=digoxin + 2 Fe(II)-[cytochrome c] + 3 H(+) = dihydrodigoxin + 2 Fe(III)-[cytochrome c]; Xref=Rhea:RHEA:62528, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:71002, ChEBI:CHEBI:145795; Evidence={ECO:0000269|PubMed:29761785, ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62529; Evidence={ECO:0000305|PubMed:29761785}; CATALYTIC ACTIVITY: Reaction=digitoxin + 2 Fe(II)-[cytochrome c] + 3 H(+) = dihydrodigitoxin + 2 Fe(III)-[cytochrome c]; Xref=Rhea:RHEA:62532, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145796, ChEBI:CHEBI:282234; Evidence={ECO:0000269|PubMed:29761785, ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62533; Evidence={ECO:0000305|PubMed:29761785}; CATALYTIC ACTIVITY: Reaction=digoxigenin + 2 Fe(II)-[cytochrome c] + 3 H(+) = dihydrodigoxigenin + 2 Fe(III)-[cytochrome c]; Xref=Rhea:RHEA:62536, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:71004, ChEBI:CHEBI:145797; Evidence={ECO:0000269|PubMed:29761785, ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62537; Evidence={ECO:0000305|PubMed:29761785}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome c] + 3 H(+) + ouabain = dihydroouabain + 2 Fe(III)-[cytochrome c]; Xref=Rhea:RHEA:62540, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:131146, ChEBI:CHEBI:145798; Evidence={ECO:0000269|PubMed:29761785, ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62541; Evidence={ECO:0000305|PubMed:29761785}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome c] + 3 H(+) + ouabagenin = dihydroouabagenin + 2 Fe(III)-[cytochrome c]; Xref=Rhea:RHEA:62544, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145789, ChEBI:CHEBI:145799; Evidence={ECO:0000269|PubMed:29761785, ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62545; Evidence={ECO:0000305|PubMed:29761785};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=94.6 uM for digoxin {ECO:0000269|PubMed:29761785}; Note=kcat is 0.23 sec(-1) for the reduction of digoxin. {ECO:0000269|PubMed:29761785};
null
null
null
FUNCTION: Involved in the inactivation of the cardiac medication and plant natural product digoxin, thus decreasing drug efficacy and toxicity. Catalyzes the reduction of the alpha,beta-unsaturated butyrolactone ring of digoxin to the inactive metabolite dihydrodigoxin. Likely uses the cytochrome Cgr1 as the physiological electron donor, encoded by the adjacent gene in the locus. Only reduces digoxin and other cardenolide toxins, such as digitoxin, digoxigenin, ouabain and ouabagenin. Therefore is a specialized enzyme present in some gut bacteria E.lenta that protects their human host against ingested plant toxins. {ECO:0000269|PubMed:29761785}.
Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum)
C8WR67
ILVC_ALIAD
MEKIYYDADISIQPLADKRIAVIGYGSQGHAHAQNLRDSGFDVVIGLRPGSSWAKAEADGFRVMAVGEAVEESDVIMILLPDERQPAVYEREIRPYLTAGKALAFAHGFNIHFSQIQPPKDVDVFMVAPKGPGHLVRRVYEAGGGVPALIAVHQDASGQAKDLALAYARGIGAGRAGILTTTFREETETDLFGEQAVLCGGLSALIKAGFETLVEAGYQPEIAYFECLHEMKLIVDLIYEGGLEYMRYSISDTAQWGDFTSGPRIINEETKKEMRRILADIQSGAFAKSWILENQANRPMFNAINRRELEHPIEVVGRKLRSMMPFIKAKRPGDDRVPATADRA
1.1.1.86
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365};
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
cytosol [GO:0005829]
ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661]
PF01450;PF07991;
6.10.240.10;3.40.50.720;
Ketol-acid reductoisomerase family
null
null
CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:25849365}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
null
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
null
null
FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}.
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) (Bacillus acidocaldarius)
C8XPA8
POLG_BANV
MVNPKGVNVMAARVKRAAQKTKKKAVQVSRGLRGFVLFVLTQLFMGRKLTPNVRRLWKSSDKNSLIHVLTKIKKIVGNLLMGVSRRKKRRSATTSGTVFMAMLGLTLAASVARHAHHTLINITKDDAHKLLTLRNGNCTVVATDIGNWCPDNVEYDCVTLQDNEDPDDVDCWCYRVNNVRVTYGRCKDGNTPRRSKRAVVITAHLDQGLTTKKETWLGSSHFETQVQKVEKWIIRNPTYAIAAILMSWYIGNSLKQRVVLLLLTLALGPAYATHCVGIPKRDFVQGVQGTTWVNLVLEQGGCVTIMAEGKPSVDVWMDNIKFTSPTLVRRISHTATISDTKIATACPSNGEAKLDEEHIKEYACKRLYSDRGWGNGCGLFGKGSLVACAKYESTGHMDVYEMDMTKVEYTVKTQVHSGAKSGDLSGVKTVSFAPTSGSQPVEFSGYGNMGLQCMIQSNVDFSTHYLVVMGNDAWLVHKAWVEDITLPWKHGEGGTWKDKQYMVEFGEPHATTVKVLALGPQEGALRNALAGAMIVTYESSGKTFKLHGGHVTCKATVSGLALKGTTYTNCRGGLSFVKTPTDTGHGTVVMQVKVAKSAPCRLTAIAADDASGHVNRGTLVTSNPIAASNNDEVMIEINPPYGTSYLIVGVGDDKLVYQWKKSGSTIGSLFSETVKGAQRMAIVGSSSWDFSSTSGFFSSVGKAIHTVFGTAFHGIFGGLSWMTRILIGVLLVWLGLNSRNGTATTLMMLTGFIILFLSLGVGAEVGCSVNWGQKELKCGDGIFVYNDVDDWMHKYKYHPEDPKVMAGLIAKAWEKGACGLTSVSELEHVMWVKIASEINAILEENEIDLTVVVHENKSVYRRGSRRFPRVETELTYGWESWGKNFITDGKVSNNTFHVDGKEDQCASKNRVWNSLEIEEFGFGVFHTNVFLRQKADKTNSCDTTLMGAAVKGNVAAHADPGFWMESQENNGTWEIQSIEFTAYRECEWPVSHTVHGTQVMESDMFMPKGIGGPVSHLNRMQGYKVQTNGAWAYGKTVVQRELCPDTSVVVDSSCSDRGKSIRSTTTEGKVIKEWCCRSCTLPPVSYWTSEGCWYAMEVRPMKTPEKHLVRSWVTAGDSYPAWSIGLVAMFLFVDIMARSRPTRKMMIGGTMLLLAIMIMGELSYLDLLRYIIVVGEHFIERENGGDVAYMAIMAASHLRPGLMAMVFAKSMWSPKQRVLLALGCAILQPFLTAQASALVWEWADSIGLVLLIVQGMVRNKEKNWALVLLALCSPVSMPVIRKASMIIGTGGLLLSLWKGGGSSMRKGLPLFAASAARVLGLTKAHLSVLFILLITKNGKRTWPISECLAAVGIFGAAFGTMFSEDETLLGPLALVGVVLIVYTMFTQSDGLELVKAADISWSDEAVVSGEARRFDVALNDSGEFKLLDEPPVSWLNVSFLVVAIVASSLHPIALVVTLVAWTYWRTEKRSGVLWDVPLAPKVEACEHLEDGVFRIIQKGLFGSSQVGIGVAKDGVFHTMWHVTRGAFLMHSGKQLTPTWGSVRKDLVCYGGTWKLDGAWNGVDEVQLIAVPPGKPATNVQTKPGTFVLPTGDEAGAVLLDFPSGTSGSPIIDRHGNILGLYGNGIVLENGAYASAISQAQPGSVAEVETPGLDKMLRKGEFTMLDYHPGAGKTRKHLPNILKECERKRLRTLVLAPTRVVLSEMKEALTSVQAKFHTQAFNSTTTGREIIDVMCHATFVHRMLEGLRSGNWEVIIMDEAHFLDPTSIAARGWAHHKSKTKESAVIFMTATPPGTSNEFPESNAEIEDVKKEIPSEPWSKGHEWILEDRRPTVWFLPSIKAANVMAACLRKAERSVVVLNRSTFENVYPTIKTKKPDFILATDIAEMGANLPVERVIDCRTAYKPVLVDERVALKGPLRIAAAAAAQRRGRVGRNPDRDGDTYVYSEDTCEQNDHLVCWTEGSMLLDNMQVKGGFVAPLYEEEASKTTMTPGECRLRDDQRKVFRTLIRKHDMPVWLSWQVAKSGLAADDRKWCFDGEDDNAILGDNGEVIKARSPGGQRKELKPRWSDARIASDNTSLMNFIAFAEGRRSLPLSILWSVPNQLSEKLVQSIDTLTILLRSEEGSRAHKLALQQAPEAVSTLLLLGMMAICTLGLVILLMKPKATDKMSMAMVTMAITGYLLKLGGMTHAQVGGILLVFFIMMVVIIPESGTQRSINDNKLAYVIILVGLVIGGVACNELGWLEKTKADLFGNNMTHAQTVVLPTINWNWLDFRPGAAWSLYVGMATFLTPVFVHWIKNEYGNASLTGITPTAGILGALNQGVPFVKLNTSVGVLLLSVWNNFTTSSMLAAMVMLACHCLFVLPGVRAQCLREAQIRVFHGVAKNPMVDGNPTVDLEKENDMPDLYEKKLALVALGMAAVLNAAMVRTALTTAEMVVLGSAAVGPLLEGNTSAFWNGPLAVAVAGVMRGNHYALIGIVYNLWLLKTARRGGSSALTYGEVWKRQLNLLGKQEFMNYKVSDILEVDRSHAREVLNSGNDAVGVAVSRGSSKLNWLIERGYLRPTGRVVDLGCGRGGWSYTCAAERQVTSVKAYTLGKEGHEKPRLIQSLGWNIIKFKDKSDITRMTPHASDTLLCDIGESSSNPEVEKERTLRVIEAVEKWMSPTTVSFCFKVLAPYKPDVIEALERFQLKHGGGIIRNPYSRNSTHEMYYVSGVRNNILHMVNSTSRMLMRRMSRPSGRSTVVPDLIYPTGTRSVASEAGPLDLEKVKARINRLKEEQESTWFVDSDHPYRTWHYHGSYVAKQSGTAASMINGVVKLLSGPWDRIEEVTNMAMTDTTPFGQQRVFKEKVDTRAPEPPQGTREIMKVVNQWLFDYLGRTKQPRICTKEEFINKVRSHAALGGILTEQEGWSSAAEAVADPRFWSLVDKERQAHLEGRCETCIYNMMGKREKKPSEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWLGRENSKAGVEGIGLQYLGYVVEEVARKGNGLVYADDTAGWDTRITEADLEDEQYIMKRMSAEHRQLAWAVMELTYRNKVVKVPRPGPGGKILMDVISRRDQRGSGQVVTYPLNTATNMKVQLIRMAEAENVITRNDVEKVSLITLKELQLWLEVNGVNRLERMAVSGDDCIVAPVDESFAGALHHLNAMSKTRKDISEWENSRGWTDWESVPFCSHHFHTLYLKDGRTIIAPCRCQDELIGRARISPGNGWMIKETAGLSKAYTQMWTLMYFHRRDLRLMANAICSAVPIDWVPTGRTTWSIHATGEWMSSDDMLEVWNKVWIQDNPHVKDKTPIFAWRDVPYIQKGQDRACGSLVGTSLRASWAESIMTSVHRVRMLIGNERYVNYMESMDRYATQRCSAYGELL
2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13
null
fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]
PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;
1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10;
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.
SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
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FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
Banzi virus (BANV)
C8XPB2
POLG_EHV
MPVRPRNKPKGVNVMAAGKVAQKIKNKLKSKAKAIGNISKGLRGFILFILAQIFWARKLTPRVRTMWKKVDKAKATRVLKGIRNIATQLITGLAGRKKRRSMTHGIILSLGVTMVIGASLHHHGGRYLLNVTHADLGKTFTIGSGNCTANIVEAGSWCSDSMEYECVTLAEAEEPDDIDCWCRGVERVRVTYGRCKNGLDSRRSRRAAVITAHIDKGLTTRQEKWLSTSMGERQIQRIERWMMRNPFYAAISLLLAWWVGSDIKQKVLIAFLVLAIGPAYSTHCVGIPKRDFVQGVQGNTWVNLVLDQGSCVTLSSDNKPSVDIWLDSIFISSPVLVRRVSHTATISDTKVQTACPTNGEAKLEEEASAEYECKKTYSDRGWGNGCGLFGKGSIVACAKYTSTGHMDVYEIDSTKIEYVTKAQVHAGMKHDDTTMVKEVKFEPTTGSMDVEFTGYGTLGLECHVQTMVDMANYYLVVMGQEAWLVHKQWVEDITLPWKIGEGGFWRDKHYMVEFTEPHATTMTVMVLGAQEGALRTALAGAMVVTYTDSSGTKKFSLKGGHVSCKARMNGLVLKGSTYTMCKGGFSFVKTPTDTGHGTAVMQVKVSKGTPCRIPVQAVDSSNGGTNRATLITANPIAATTEDEVMIELSPPYGESYIMIGTGDDKLTYHWHKSGSTIGSLFTETYKGAQRMAIIGDDAWDFSSSSNFFNSIGKALHTVFGNVFHSIFGGLSWITKIILGGMFLWLGVNSRNQTMCMVLMAVGGILLFMTLGVSGEVGCSLDIKRRELKCGDGLFLFNDVNDWTHKYKFHPEDPKLLASLIKKSHQEGRCGLSSVNEVEHRMWNSIKTEINAMFEENGVDLSVVVKDSKLHYKMGSHAFPKVEEGLSLGWKNWGKSLVFEPKQSNVSFIIDGTSEDCPFTNRIWNAFVVEEFGIGMFTTNVFLTHKVDFTKQCDASLLGAGVKGDVAVHGDPTLWMESRKENGTWQLHTIQMNGLRECFWPQTHTIHGSSVMESAMFLPKQYGGPVSHHNHYTGYAVQTAGPWNVQPLIVKRETCPGTQVRVDEQCRDRGNSVRSTTSEGKIIPEWCCRSCTLPPVSFWGPDSCWYAMEIRPQNVHEEHLVRSWASAGTGMAESSLGLVALFLFTDIFARKRMTRKFMVIGCLGVLSVMIVGGFTALDLIRYIIVVGQHFASMNHGGDVAYLAIIAVGKLRPGLLMMYSFKAAWSPKERVMVALGLLVFQAVLGDFVHTGLWEWADAAGMCILIIQGMATRKEKTYIMPILALLTPLSMEIIRKTGIFACVGLLGLSLWRGGDTTMRKGMPLLAGAATAASGLTRASLSVVFILCATAASRRSWPIGEIMAIVGIVGTGFGMAVNDQASLAGPMLVFGLIMIVYATLGRADGLTLKRVGDITWEEEAVHSGSSTRYDVTLNEAGEFKLVHEEPVVWSHVVFLVVALIAASVHPIALVVVTIIWTYGKKHLRGGVLWDIPIAPPVEEAEPLEDGVYAILQSGLMGKAQAGVGVAQEGVFHTMWHVTRGGFLMVGGKRLTPHWASVKRDLICYGGNWKLDGKWDGVEEVQLIAVAPGKAPTNVQTKPGVFRMADGTEIGAVALDYPSGTSGSPIVNEKGQVIGLYGNGIVIGGSGYVSSIAQIAGGEGVTEEPLLDTATMLRKGKLTVLDYHPGAGKTRIFLPYILKECVRRKLRTLVLAPTRVVLSEMREALRDVAVKYHTQAFQAAGTGRELVDAMCHATLSHRMLESSRSVNWEVIIMDEAHYMDPTSIAARGWAAHKANNHESAVIFMTATPPGSANEFPESNGEIEDLRRDIPTEPWNKGHEWILEDRRPTVWFLPSIRAANNIAACLRRSERSVVVLNRQTFETVYPTIKTKKPDFILATDIAEMGANLGVERVIDCRTSYKPVLTTDGRVVIKGPLRIPASAAAQRRGRVGRCKDRDTDSYVYSEETSEDNGHYVCWTEASMLLDNMEVKGGMVAPLYDVEAQKTEMVPGEARLRDDQRKVFRTLIKRYDLPVWVSWQVAKSGLMLEDRKWCFDGDDENTILNDNGEKILARSPGGQRKFLCPRWNDSRLYYDNASLMSFLAFAEGRRSYLGVWHAVQMAPLKLGEKLTESLDTMVMLMRSEEGTRAYKLASTNAPEAVTILLMTGIVVACTLGVGLAFMWPKGVDKMSMGMITMSIAGYLMLQGGLTPVQVASVLLIFFIFMVVLIPEAGTQRSINDNKTLYVLLGVALLIGAITANEMGYLEKTKRDLLGERVQNEWKLELPMFDLRPGAAWSIYVGLATLVMPVLDHWIRTEYGSLSLTGIAQQASILQAMDKGVPFFKLNMSVIVLLVSVWNNFSMLSVLCGVGLLGVHCAFVLPGLRAQAAKQAQRRVYHGVAKNPVVDGQTTAEIETAPEMPPLYEKKLALVLLGVVAIANGVMVRSAFSMAETVVLLSAAVGPLLEGNTSAIWNGPMAVAMAGIMRGNYYAGIGLAYNLWILQSPKRGRSTTMTLGELWKRQLNLMGKREFELYKITDIHEVDRSQAQAVMKAGIDNVGISVSRGTSKLKWMVDRNYVEPLGRVVDLGCGRGGWSYLCAASKRVSSVKAYTLGITGHEKPVNVQSLGWNIIKFKDKTDVFKMEPHACETLLCDIGESSSNPLVEMERTLKVIDNVERWMSPTTESYCFKVLAPYRPEVIERLERFQLKYGGGIVRVPFSRNSTHEMYYVSGVKNNLTHMVSCVSRLLLRRMTHPDGRCKVEADVVFPTGTRNVASDLGPMDLSKVKDRVNRLRSEQGTWFQDDSHPYRTWHYLGSYVAKQSGSAATMVNGVVKMLSMPWDRIENVTQLAMTDTTPYGQQRVFKEKVDTRAPPPPPGTRAIMEVVNKWMFDFLAREKAPRICTKEEFINKVRSNAALGNMLEEQDGWKDAATAVQDPRFWALVDRERQVHLEGRCETCIYNMMGKREKKPAEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSLAGVEGVGLQYLGYVVKNVWEKSNGIMYADDTAGWDTRVTEADLDDEQYLLSKMEGYHKKLASAVMNMTYKYKVVKVPRPGPGGKVFMDVIARQDQRGSGQVVTYPLNTGTNMKVQLIRMAEGEGVISRHDIERVTIKTLNALRVWLAENGAERLSRMAVSGDDCVVAPLDERFGLALHHLNAMSKIRKDIDDWTESIPWRSWESVPFCSHHFHQLFLKDGRSIVVPCRDQDELVGRARVSPGNGWKLKETACLSKAYAQMWLLMYFHKRDLRLMGNAICSSVPAHWVPTGRTTWSIHAHNEWISSERMLDVWNKVWIVDNPHMPDKTCIDDWRDVPYLPKSQDRLCGSLIGITARASWAENIRAVVNKIRGMIGNEVYSDHLSVMGRYTYSVQEVGTVL
2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13
null
fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]
PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949;
1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10;
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.
SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
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FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
Edge Hill virus (EHV)
C8YUV0
FFAR4_MACFA
MSPECARAAGDAPLRSLEQANRTRFSFFSDVKGDHRLLLAAVETTVLALIFAVSLLGNVCALVLVARRRRRGTTACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYLMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLTLIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIAGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSVISG
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; brown fat cell differentiation [GO:0050873]; cellular response to hormone stimulus [GO:0032870]; ghrelin secretion [GO:0036321]; inflammatory response [GO:0006954]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cytokine production [GO:0001818]; negative regulation of inflammatory response [GO:0050728]; negative regulation of somatostatin secretion [GO:0090275]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of glucagon secretion [GO:0070094]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of glucose transmembrane transport [GO:0010827]; white fat cell differentiation [GO:0050872]
ciliary membrane [GO:0060170]; cilium [GO:0005929]; endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
fatty acid binding [GO:0005504]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277]; taste receptor activity [GO:0008527]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Phosphorylated at two clusters of Ser and Thr residues located in the intracellular C-terminus. Prerequisite for FFAR4 internalization via an ARRB2-dependent pathway. {ECO:0000250|UniProtKB:Q5NUL3}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7TMA4}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q5NUL3}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q5NUL3}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q7TMA4}; Multi-pass membrane protein {ECO:0000255}. Note=Sorted to late endosome/lysosome compartments upon internalization (By similarity). Specifically localizes to the primary cilium of undifferentiated adipocytes. Ciliary trafficking is TULP3-dependent. As the cilium is lost during adipogenesis, moves to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q5NUL3, ECO:0000250|UniProtKB:Q7TMA4}.
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FUNCTION: G-protein-coupled receptor for long-chain fatty acids (LCFAs) with a major role in adipogenesis, energy metabolism and inflammation. Signals via G-protein and beta-arrestin pathways. LCFAs sensing initiates activation of phosphoinositidase C-linked G proteins GNAQ and GNA11 (G(q)/G(11)), inducing a variety of cellular responses via second messenger pathways such as intracellular calcium mobilization, modulation of cyclic adenosine monophosphate (cAMP) production, and mitogen-activated protein kinases (MAPKs). After LCFAs binding, associates with beta-arrestin ARRB2 that acts as an adapter protein coupling the receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis (By similarity). In response to dietary fats, plays an important role in the regulation of adipocyte proliferation and differentiation. Acts as a receptor for omega-3 polyunsaturated fatty acids (PUFAs) at primary cilium of perivascular preadipocytes, initiating an adipogenic program via cAMP and CTCF-dependent chromatin remodeling that ultimately results in transcriptional activation of adipogenic genes and cell cycle entry. Induces differentiation of brown and beige adipocytes probably via autocrine and endocrine functions of FGF21 hormone. Contributes to the thermogenic activation of brown adipose tissue and the browning of white adipose tissue. Activates brown adipocytes by initiating intracellular calcium signaling leading to mitochondrial depolarization and fission, and overall increased mitochondrial respiration. Consequently stimulates fatty acid uptake and oxidation in mitochondria together with UCP1-mediated thermogenic respiration, eventually reducing fat mass. Regulates bi-potential differentiation of bone marrow mesenchymal stem cells toward osteoblasts or adipocytes likely by up-regulating distinct integrins. In response to dietary fats regulates hormone secretion and appetite. Stimulates GIP and GLP1 secretion from enteroendocrine cells as well as GCG secretion in pancreatic alpha cells, thereby playing a role in the regulation of blood glucose levels. Negatively regulates glucose-induced SST secretion in pancreatic delta cells. Mediates LCFAs inhibition of GHRL secretion, an appetite-controlling hormone. In taste buds, contributes to sensing of dietary fatty acids by the gustatory system. During the inflammatory response, promotes anti-inflammatory M2 macrophage differentiation in adipose tissue (By similarity). Mediates the anti-inflammatory effects of omega-3 PUFAs via inhibition of NLRP3 inflammasome activation (By similarity). In this pathway, interacts with adapter protein ARRB2 and inhibits the priming step triggered by Toll-like receptors (TLRs) at the level of TAK1 and TAB1 (By similarity). Further inhibits the activation step when ARRB2 directly associates with NLRP3, leading to inhibition of pro-inflammatory cytokine release (By similarity). Mediates LCFAs anti-apoptotic effects (By similarity). {ECO:0000250|UniProtKB:Q5NUL3, ECO:0000250|UniProtKB:Q7TMA4}.
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
C8Z543
ARO1_YEAS8
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKHIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
C9JE40
PATL2_HUMAN
MNCLEGPGKTCGPLASEEELVSACQLEKEEENEGEEEEEEEDEEDLDPDLDPDLEEEENDLGDPAVLGAVHNTQRALLSSPGVKAPGMLGMSLASLHFLWQTLDYLSPIPFWPTFPSTSSPAQHFGPRLPSPDPTLFCSLLTSWPPRFSHLTQLHPRHQRILQQQQHSQTPSPPAKKPWSQQPDPYANLMTRKEKDWVIKVQMVQLQSAKPRLDDYYYQEYYQKLEKKQADEELLGRRNRVESLKLVTPYIPKAEAYESVVRIEGSLGQVAVSTCFSPRRAIDAVPHGTQEQDIEAASSQRLRVLYRIEKMFLQLLEIEEGWKYRPPPPCFSEQQSNQVEKLFQTLKTQEQNNLEEAADGFLQVLSVRKGKALVARLLPFLPQDQAVTILLAITHHLPLLVRRDVADQALQMLFKPLGKCISHLTLHELLQGLQGLTLLPPGSSERPVTVVLQNQFGISLLYALLSHGEQLVSLHSSLEEPNSDHTAWTDMVVLIAWEIAQMPTASLAEPLAFPSNLLPLFCHHVDKQLVQQLEARMEFAWIY
null
null
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; negative regulation of translation [GO:0017148]; P-body assembly [GO:0033962]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]
RNA binding [GO:0003723]
PF09770;
null
PAT1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:28965849}. Nucleus {ECO:0000250|UniProtKB:A2ARM1}.
null
null
null
null
null
FUNCTION: RNA-binding protein that acts as a translational repressor. {ECO:0000250|UniProtKB:Q4V7K4}.
Homo sapiens (Human)
C9JLW8
MCRI1_HUMAN
MTSSPVSRVVYNGKRTSSPRSPPSSSEIFTPAHEENVRFIYEAWQGVERDLRGQVPGGERGLVEEYVEKVPNPSLKTFKPIDLSDLKRRSTQDAKKS
null
null
regulation of epithelial to mesenchymal transition [GO:0010717]
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634]
null
PF14799;
null
MCRIP family
PTM: Phosphorylation by MAPK3/1 (ERK1/2) regulates MCRIP1 binding to CTBP(s) (PubMed:25728771). {ECO:0000269|PubMed:25728771}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25728771, ECO:0000269|PubMed:26184334}. Cytoplasm, Stress granule {ECO:0000269|PubMed:26184334}.
null
null
null
null
null
FUNCTION: The phosphorylation status of MCRIP1 functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in transcriptional silencing of the E-cadherin gene and induction of epithelial-mesenchymal transition (PubMed:25728771). {ECO:0000269|PubMed:25728771}.
Homo sapiens (Human)
C9JR72
KBTBD_HUMAN
MARGPQTLVQVWVGGQLFQADRALLVEHCGFFRGLFRSGMRETRAAEVRLGVLSAGGFRATLQVLRGDRPALAAEDELLQAVECAAFLQAPALARFLEHNLTSDNCALLCDAAAAFGLRDVFHSAALFICDGERELAAELALPEARAYVAALRPSSYAAVSTHTPAPGFLEDASRTLCYLDEEEDAWRTLAALPLEASTLLAGVATLGNKLYIVGGVRGASKEVVELGFCYDPDGGTWHEFPSPHQPRYDTALAGFDGRLYAIGGEFQRTPISSVERYDPAAGCWSFVADLPQPAAGVPCAQACGRLFVCLWRPADTTAVVEYAVRTDAWLPVAELRRPQSYGHCMVAHRDSLYVVRNGPSDDFLHCAIDCLNLATGQWTALPGQFVNSKGALFTAVVRGDTVYTVNRMFTLLYAIEGGTWRLLREKAGFPRPGSLQTFLLRLPPGAPGPVTSTTAEL
null
null
actin filament organization [GO:0007015]; protein ubiquitination [GO:0016567]; regulation of the force of skeletal muscle contraction [GO:0014728]; relaxation of skeletal muscle [GO:0090076]
cytosol [GO:0005829]
actin filament binding [GO:0051015]
PF00651;PF01344;
2.120.10.80;
null
PTM: Autoubiquitinated. {ECO:0000269|PubMed:22542517}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21109227, ECO:0000269|PubMed:22542517}.
null
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. {ECO:0000269|PubMed:22542517}.
Homo sapiens (Human)
C9JRZ8
AK1BF_HUMAN
MATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY
1.1.1.-; 1.1.1.216; 1.1.1.300; 1.1.1.54; 1.1.1.64
null
estrogen biosynthetic process [GO:0006703]
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; farnesol dehydrogenase activity [GO:0047886]; NADP-retinol dehydrogenase activity [GO:0052650]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; testosterone 17-beta-dehydrogenase (NADP+) activity [GO:0047045]
PF00248;
3.20.20.100;
Aldo/keto reductase family
null
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:25577493}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:25577493}.
CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:25577493}; CATALYTIC ACTIVITY: Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.64; Evidence={ECO:0000269|PubMed:25577493}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = 5alpha-androstan-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:42120, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:25577493}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxyandrost-5-en-17-one + H(+) + NADPH = androst-5-en-3beta,17beta-diol + NADP(+); Xref=Rhea:RHEA:46628, ChEBI:CHEBI:2710, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:25577493}; CATALYTIC ACTIVITY: Reaction=androsterone + H(+) + NADPH = 5alpha-androstane-3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:42156, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:25577493}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH; Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH; Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH; Xref=Rhea:RHEA:14697, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894, ChEBI:CHEBI:16619, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.216; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=acetoin + NADP(+) = diacetyl + H(+) + NADPH; Xref=Rhea:RHEA:35607, ChEBI:CHEBI:15378, ChEBI:CHEBI:15688, ChEBI:CHEBI:16583, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:26222439}; CATALYTIC ACTIVITY: Reaction=(E)-4-hydroxynon-2-en-1-ol + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + NADPH; Xref=Rhea:RHEA:58416, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:142617; Evidence={ECO:0000269|PubMed:26222439};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 uM for androsterone (tested with isoform 1 in the reductive reaction) {ECO:0000269|PubMed:25577493}; KM=1.9 uM for delta-4-androstenedione (tested with isoform 1 in the reductive reaction) {ECO:0000269|PubMed:25577493}; KM=2.5 uM for estrone (tested with isoform 1 in the reductive reaction) {ECO:0000269|PubMed:25577493}; KM=63.4 uM for acetoacetyl-CoA (tested with isoform 1 in the reductive reaction) {ECO:0000269|PubMed:25577493}; KM=19.2 uM for 3-alpha,17-beta-androstandiol (tested with isoform 1 in the oxidative reaction) {ECO:0000269|PubMed:25577493}; KM=7.1 uM for testosterone (tested with isoform 1 in the oxidative reaction) {ECO:0000269|PubMed:25577493}; KM=9.1 uM for 17-beta-estradiol (tested with isoform 1 in the oxidative reaction) {ECO:0000269|PubMed:25577493}; KM=1 uM for all-trans-retinal {ECO:0000269|PubMed:26222439}; KM=0.16 uM for 9-cis-retinal {ECO:0000269|PubMed:26222439}; KM=880 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:26222439}; KM=2.9 uM for pyridine-3-aldehyde {ECO:0000269|PubMed:26222439}; KM=3.1 uM for hexanal {ECO:0000269|PubMed:26222439}; KM=36 uM for acrolein {ECO:0000269|PubMed:26222439}; KM=5 uM for trans-2-hexenal {ECO:0000269|PubMed:26222439}; KM=2.2 uM for 4-hydroxy-2-nonenal {ECO:0000269|PubMed:26222439}; KM=1.7 uM for 3-nonen-2-one {ECO:0000269|PubMed:26222439}; KM=1 uM for 2,3-butanedione {ECO:0000269|PubMed:26222439}; KM=1 uM for farnesal {ECO:0000269|PubMed:26222439}; KM=5.7 uM for NADPH {ECO:0000269|PubMed:26222439}; Note=kcat is 1.7 min(-1) using isoform 1 for the reduction of androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for the reduction of estrone. kcat is 0.5 min(-1) using isoform 1 for the reduction of acetoacetyl-CoA. kcat is 3.0 min(-1) using isoform 1 for the oxidation of 3-alpha,17-beta-androstandiol. kcat is 0.6 min(-1) using isoform 1 for the oxidation of testosterone. kcat is 0.5 min(-1) using isoform 1 for the oxidation of 17-beta-estradiol (PubMed:25577493). kcat is 10.7 min(-1) with D,L-glyceraldehyde as substrate. kcat is 9 min(-1) with pyridine-3-aldehyde as substrate. kcat is 7.3 min(-1) with hexanal as substrate. kcat is 9 min(-1) with acrolein as substrate. kcat is 11.3 min(-1) with trans-2-hexenal as substrate. kcat is 5.2 min(-1) with 4-hydroxy-2-nonenal as substrate. kcat is 4.8 min(-1) with farnesal as substrate. kcat is 1.7 min(-1) with 2,3-butanedione as substrate. kcat is 5.4 min(-1) with all-trans-retinaldehyde as substrate. kcat is 3.8 min(-1) with 9-cis-retinal as substrate (PubMed:26222439). {ECO:0000269|PubMed:25577493, ECO:0000269|PubMed:26222439};
null
null
null
FUNCTION: [Isoform 1]: Catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds (PubMed:21276782, PubMed:26222439). In addition, catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs (PubMed:25577493). Displays strong enzymatic activity toward all-trans-retinal and 9-cis-retinal (PubMed:26222439). May play a physiological role in retinoid metabolism (PubMed:26222439). {ECO:0000269|PubMed:21276782, ECO:0000269|PubMed:25577493, ECO:0000269|PubMed:26222439}.; FUNCTION: [Isoform 2]: No oxidoreductase activity observed with the tested substrates. {ECO:0000269|PubMed:25577493}.
Homo sapiens (Human)
C9K4X8
GSS_PATPE
MTSNNRHLFQATCLVLLLLHAAFHGGALGEKYCDDDFHMAVFRTCAVSKRSQPGMSLSDVLTMNRFRGHNIKRSIDSTLEDNAFFMSGLEKRSEYSGIASYCCLHGCTPSELSVVC
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; positive regulation of oocyte maturation [GO:1900195]; positive regulation of ovulation [GO:0060279]
extracellular space [GO:0005615]; plasma membrane [GO:0005886]
hormone activity [GO:0005179]
null
null
Insulin family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23829221}.
null
null
null
null
null
FUNCTION: Induces oocyte maturation and ovulation in vitro in ovarian fragments and induces spawning behavior and gamete release in vivo (PubMed:19470645). Probably mediates its effects by binding to a G-protein coupled receptor located in follicle cell membranes (PubMed:21295575, PubMed:21967225, PubMed:24929230). Following receptor binding, stimulates GTP-dependent adenylyl cyclase activity in follicle cell membranes of fully grown ovaries at stage V but not in young ovaries at stage IV, leading to the production of cAMP (PubMed:21967225, PubMed:22134181). This stimulates the production of the maturation-inducing hormone, 1-methyladenine, in stage V but not stage IV ovaries (PubMed:19470645, PubMed:21295575, PubMed:22134181). The lack of activity in stage IV ovaries may be due to the very low levels of the G-protein alpha s subunit which is not expressed at high levels in follicle cells until stage V (PubMed:24929230). {ECO:0000269|PubMed:19470645, ECO:0000269|PubMed:21295575, ECO:0000269|PubMed:21967225, ECO:0000269|PubMed:22134181, ECO:0000269|PubMed:24929230}.
Patiria pectinifera (Starfish) (Asterina pectinifera)
C9SE96
ARO1_VERA1
MSCSNNTEPTRIAILGTDNIVVDHGIWLNWVTKDLFDNVKSSTYVLVTDTNLYDTYVPPFKHAFDGATDTTAGPRLLTLAIPPGEISKSRQSKAHIEDWMLSQQCTRDTVIIALGGGVIGDMLGYVAATFMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPSRIYIDLAFLETLPSREFINGMAEVIKTAAIWDENEFATLEANAPSIVAAVNQPTGPGRLSPIREILKRIVLGSARVKAEVVSSDEREGGLRNLLNFGHSIGHAYEALLTPQLLHGEAVAIGMVKEAELARYLGVLRPSAVARLAKCISSYGLPTSLGDKRVIKLTAGKRCPVDILLQKMAVDKKNDGRKKKIVLLSAIGKTHEPRATTVEDAAIKVMLSASTLITPGVSTKLATTVTPPGSKSISNRALILAALGEGTCRIKNLLHSDDVEFMLTAITRLGGASYAWEDAGEVLVLTGKGGQLRASSDPLYLGNAGTASRFLTTVVALCSPADVSSTVLTGNARMQVRPIGPLVDALRSNGVSIDYLGPGKSLPLRIDAAGGFAGGVIELAATVSSQYVSSILMAAPYAKEPVTLRLVGGKPISQPYIDMTLAMMKTFGVQVERSSSDPNTYHIAKGTYKNPAEYTIESDASSATYPLAIAAITGTTCTVPNIGSSSLQGDARFAIDVLQPMGCTVQQTASSTTVTGPAPGGLLGLPHVDMEPMTDAFLTASVLAAVAAGTTKISGIANQRVKECNRIAAMREQLGKFGIATDEFDDGIIVTGQPLDTLKTPDAGVFCYDDHRVAMSFSVLSTVANAPVTILERECTGKTWPGWWDTLSQSFGLRLNGDDKHPGVEGRHQQDHTTRSVFIVGMRGAGKTTTGRWMAKLLKRPFIDLDEELERRSGMTIPEMIHGTKGWEGFRRDELQLLHDVMENQASGHVFSCGGGIVESPEARKLLIAYKEKGGCVLLVHRDTKQVVDYLLQDKTRPAYREDIEDVYYRRKPLYDECSNFQYFSPHPAASVASRDAPLDFRCFVDAICGDGSKVTKMTAKEQSFFVSLTVPSVDSAVDVIPQVVVGSDAVELRVDLLQDQTPESVARQVSALRSAAGMPIIFTLRTVSQGGCFPDADHTQALSLYILALRMGVEFIDLEMTWPEHILQTVTNLKGRSRIIASHHDPRGELSWKNGSWTPFYNRALQWGSVIKLVGTAQSMEDNYDLARFKSDMLASHPTPVIALNMGALGKLSRVLNGFLTPVSHPALPFKAAPGQLSAAEIRRALFLLGNINAQSFHLFGKPISKSRSPALHNSLFNLTGLPHKYGLVETDQADEVAAVIREPDFGGASVTIPLKLDVMPLLDEVSESAKVIGAVNTIIPMPLDGSQKRRLLGDNTDWRGMVHCLESIGVASESTASTTTASALVIGSGGTTRAAIFALKSHGYHPIYMLARNEQSLETIRASFPTDFDLRALGGPAEVFTLAVAPTVVISTIPADKPMDPSLRETLEVVLKSPVSEQRTRVLLEMAYQPRHTAAMRLAEDAGWRTIPGAEVLAAQGWHQFQMWTGITPRFIDAQAAVNGDEIPTSTD
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136) (Verticillium wilt of alfalfa) (Verticillium albo-atrum)
C9X0M5
RNC_NEIM8
MKDDVLKQQAHAAIQKKLGYAFRDISLLRQALTHRSHHAKHNERFEFVGDSILNYTVARMLFDAFPKLTEGELSRLRASLVNEGVLAEMAAEMNVGDGLYLGAGELKSGGFRRPSILADAMEAMFAAVSFDADFNTAEKVVRHLFADRVRRADFQNQAKDGKTALQEALQARRFALPKYRIEEQIGYANDSMFVISCDLGELGFVCRAKGTSRKAAEQEAAKEALKWLEEKLPLKRKKK
3.1.26.3
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
mRNA processing [GO:0006397]; pre-miRNA processing [GO:0031054]; rRNA processing [GO:0006364]; siRNA processing [GO:0030422]; tRNA processing [GO:0008033]
cytoplasm [GO:0005737]; RISC complex [GO:0016442]
deoxyribonuclease I activity [GO:0004530]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525]; rRNA binding [GO:0019843]
PF00035;PF14622;
3.30.160.20;1.10.1520.10;
Ribonuclease III family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}.
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
null
null
null
null
FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. {ECO:0000269|PubMed:23706818}.; FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In this organism endogenous ribonuclease 3 and Cas9 are required for correct coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA). Cas9, crRNA and tracRNA are required for cleavage of invading DNA. Involved in 3'-end processing but not 5'-end processing of crRNA and tracrRNA (PubMed:23706818). {ECO:0000269|PubMed:23706818}.
Neisseria meningitidis serogroup C (strain 8013)
C9XI63
TEPS3_ANOGA
MWQFIRSRILTVIIFIGAAHGLLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITIDGQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVHVTIRDPQRNVIRKWSTAKLYAGVFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKVELYLDDDKLNQKKELTVYGKGQVELRFDNFAMDADQQDVRVKVSFIEQYTNRTVVKQSQITVYRYAYRVELIKESPQFRPGLPFKCALQFTHHDGTPAKGITGKVEVSDVGFETTKTSDNDGLIKLELQPSEGSEQLGINFNAVDGFFFYEDVNKVETVTDAYIKLELKSPIKRNKLMRFMVTCTERMTFFVYYVMSKGNIIDAGFMRPNKQTKYLLQLNATEKMIPKAKILIATVAGRTVVYDYADLDFQELRNNFDLSIDEQEIKPGRQIELSMSGRPGAYVGLAAYDKALLLFNKNHDLFWEDIGQVFDGFHAINENEFDIFHSLGLFARTLDDILFDSANEKTGRNALQSGKPIGKLVSYRTNFQESWLWKNVSIGRSGSRKLIEVVPDTTTSWYLTGFSIDPVYGLGIIKKPIQFTTVQPFYIVENLPYSIKRGEAVVLQFTLFNNLGAEYIADVTLYNVANQTEFVGRPDTDLSYTKSVSVPPKVGVPISFLIKARKLGEMAVRVKASIMLGHETDALEKVIRVMPESLAQPKMDTSFFCFDDYKNQTFPFNLDINKKADNGSKKIEFRLNPNLLTMVIKNLDNLLAVPTGCGEQNMVKFVPNILVLDYLYATGSKEQHLIDKATNLLRQGYQNQMRYRQTDGSFGVWEKSGSSVFLTAFVATSMQTASKYMNDIDAAMVEKALDWLASKQHSSGRFDETGKVWHKDMQGGLRNGVALTSYVLTALLENDIAKVKHAVVIQNGMNYLSNQLAFINNAYDLSIATYAMMLNGHTMKKEALDKLIDMSISDNNKKERYWGTTNQIETTAYALLSFVMAEKYLDGIPIMNWLVNQRYVTGSFPRTQDTFVGLKALTKLAEKISPSRNDYTVQLKYKKSTKYFNINSEQIDFQNFLEIPEDTKKLEINVGGIGFGLLEVIYQFDLNLVNFEHRFKLDLEKQNTGSDYELRLRVCANYIPELTDSQSNMALIEVTLPSGYVVDRNPISEQTTVNPIQNMEIRYGGTSVVLYYYNMGTERNCFTVTAYRRFKVALKRPAYVVVYDYYNTNLNAIKVYEVDKQNVCEICEEEDCPAEC
null
null
antibacterial innate immune response [GO:0140367]; antifungal innate immune response [GO:0061760]; cell aggregation [GO:0098743]; defense response to symbiont [GO:0140546]; positive regulation of melanin biosynthetic process [GO:0048023]
extracellular region [GO:0005576]; extracellular space [GO:0005615]
endopeptidase inhibitor activity [GO:0004866]
PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678;PF21412;
1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.2950;2.60.40.690;2.60.40.10;
null
PTM: In the hemolymph, the full-length protein is cleaved by an unknow protease into a 75kDa N-terminal (TEP1-N) chain and an 80kDa C-terminal (TEP1-C) chain which remain non-covalently linked (PubMed:15006349, PubMed:19286136, PubMed:24039584, PubMed:25012124). The TEP1-C chain contains the thioester bond which covalently binds to the pathogen surface (By similarity). Cleavage is induced by bacterial infection or aseptic wound injury (PubMed:24039584). During embryonic and pupal development, the cleaved form is the predominant form (By similarity). {ECO:0000250|UniProtKB:Q9GYW4, ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:25012124}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9GYW4}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:23166497, ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:25012124}. Note=Secreted as a full-length protein into the hemolymph. {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:23166497, ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:25012124}.
null
null
null
null
null
FUNCTION: Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection (PubMed:15006349, PubMed:23166497, PubMed:24039584, PubMed:25012124, PubMed:30690067). After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance either by melanization or lysis (PubMed:24039584, PubMed:30690067). Initiate the recruitment and activation of a cascade of proteases, mostly of CLIP-domain serine proteases, which leads to the proteolytic cleavage of the prophenoloxidase (PPO) into active phenoloxidase (PO), the rate-limiting enzyme in melanin biosynthesis (PubMed:23166497, PubMed:24039584, PubMed:25012124). In response to parasite P.berghei-mediated infection, binds to and mediates killing of ookinetes, as they egress from midgut epithelial cells into the basal labyrinth, by both lysis and melanization (PubMed:15006349, PubMed:24039584, PubMed:25012124). During bacterial infection, binds to both Gram-positive and Gram-negative bacteria but only promotes phagocytosis of Gram-negative bacteria (PubMed:24039584, PubMed:30690067). Promotes the accumulation of SPCLIP1 onto the surface of P.berghei ookinetes and bacterium E.coli which leads to the melanization of the pathogen (PubMed:24039584). Recruits CLIPA2 to bacteria surface (PubMed:25012124). In response to bacterial infection, required for periostial hemocyte aggregation, but not for the aggregation of sessile hemocytes in non-periostial regions (PubMed:30690067). During the late stage of fungus B.bassiana-mediated infection, required for the initiation of hyphae melanization by binding to the surface of hyphae and recruiting prophenoloxidase PPO to them (PubMed:23166497). Plays a role in male fertility by binding to defective sperm cells and promoting their removal during spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q9GYW4, ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:23166497, ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:25012124, ECO:0000269|PubMed:30690067}.; FUNCTION: [Thioester-containing protein 1 allele S3]: Binds to and mediates killing of parasite P.bergei ookinetes by lysis. {ECO:0000269|PubMed:15006349}.; FUNCTION: [Thioester-containing protein 1 C-terminal]: Binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance. {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:30690067}.
Anopheles gambiae (African malaria mosquito)
C9XI66
TEPR1_ANOGA
MWQFIRSRILTVIIFIGAAHGLLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITIDGQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVYVTIRDPQRNVIRKWSTAKLYAGVFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKVELYLDDDKLKLKKELTVYGKGQVELRFDNFAMDADQQDVPVKVSFVEQYTNRTVVKQSQITVYRYAYRVELIKESPQFRPGLPFKCALQFTHHDGTPAKGISGKVEVSDVRFETTTTSDNDGLIKLELQPSEGTEQLSIHFNAVDGFFFYEDVNKVETVTDAYIKLELKSPIKRNKLMRFMVTCTERMTFFVYYVMSKGNIIDAGFMRPNKQPKYLLQLNATEKMIPRAKILIATVAGRTVVYDFADLDFQELRNNFDLSIDEQEIKPGRQIELSMSGRPGAYVGLAAYDKALLLFNKNHDLFWEDIGQVFDGFHAINENEFDIFHSLGLFARTLDDILFDSANEKTGRNALQSGKPIGKLVSYRTNFQESWLWKNVSIGRSGSRKLIEVVPDTTTSWYLTGFSIDPVYGLGIIKKPIQFTTVQPFYIVENLPYSIKRGEAVVLQFTLFNNLGAEYIADVTLYNVANQTEFVGRPNTDLSYTKSVSVPPKVGVPISFLIKARKLGEMAVRVKASIMLGHETDALEKVIRVMPESLVQPRMDTRFFCFDDHKNQTFPINLDINKKADSGSTKIEFRLNPNLLTTVIKNLDHLLGVPTGCGEQNMVKFVPNILVLDYLHAIGSKEQHLIDKATNLLRQGYQNQMRYRQTDGSFGLWETTNGSVFLTAFVGTSMQTAVKYISDIDAAMVEKALDWLASKQHFSGRFDKAGAEYHKEMQGGLRNGVALTSYVLMALLENDIAKAKHAEVIQKGMTYLSNQFGSINNAYDLSIATYAMMLNGHTMKEEALNKLIDMSFIDADKNERFWNTTNPIETTAYALLSFVMAEKYTDGIPVMNWLVNQRYVTGSFPSTQDTFVGLKALTKMAEKISPSRNDYTVQLKYKKSAKYFKINSEQIDVENFVDIPEDTKKLEINVGGIGFGLLEVVYQFNLNLVNFENRFQLDLEKQNTGSDYELRLKVCASYIPQLTDRRSNMALIEVTLPSGYVVDRNPISEQTKVNPIQKTEIRYGGTSVVLYYDNMGSERNCFTLTAYRRFKVALKRPAYVVVYDYYNTNLNAIKVYEVDKQNLCEICDEEDCPAEC
null
null
defense response to symbiont [GO:0140546]; immune system process [GO:0002376]; positive regulation of melanin biosynthetic process [GO:0048023]
extracellular space [GO:0005615]
endopeptidase inhibitor activity [GO:0004866]
PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678;PF21412;
1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.2950;2.60.40.690;2.60.40.10;
null
PTM: In the hemolymph, the full-length protein is cleaved by an unknow protease into a 75kDa N-terminal (TEP1-N) chain and an 80kDa C-terminal (TEP1-C) chain which remain non-covalently linked (PubMed:19286136, PubMed:23055931). The TEP1-C chain contains the thioester bond which covalently binds to the pathogen surface (PubMed:23055931). Cleavage is induced by bacterial infection or aseptic wound injury (By similarity). During embryonic and pupal development, the cleaved form is the predominant form (By similarity). {ECO:0000250|UniProtKB:C9XI63, ECO:0000250|UniProtKB:Q9GYW4, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:23055931}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9GYW4}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136}. Note=Secreted as a full-length protein into the hemolymph. {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136}.
null
null
null
null
null
FUNCTION: Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection (PubMed:15006349). After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance either by melanization or lysis (PubMed:15006349, PubMed:19286136). Initiate the recruitment and activation of a cascade of proteases, mostly of CLIP-domain serine proteases, which leads to the proteolytic cleavage of the prophenoloxidase (PPO) into active phenoloxidase (PO), the rate-limiting enzyme in melanin biosynthesis (By similarity). In response to parasite P.berghei-mediated infection, binds to and mediates killing of ookinetes, as they egress from midgut epithelial cells into the basal labyrinth, by both lysis and melanization (PubMed:15006349, PubMed:19286136). During bacterial infection, binds to both Gram-positive and Gram-negative bacteria but only promotes phagocytosis of Gram-negative bacteria (By similarity). Promotes the accumulation of SPCLIP1 onto the surface of P.berghei ookinetes and bacterium E.coli which leads to the melanization of the pathogen (By similarity). Recruits CLIPA2 to bacteria surface (By similarity). In response to bacterial infection, required for periostial hemocyte aggregation, but not for the aggregation of sessile hemocytes in non-periostial regions (By similarity). During the late stage of fungus B.bassiana-mediated infection, required for the initiation of hyphae melanization by binding to the surface of hyphae and recruiting prophenoloxidase PPO to them (By similarity). Plays a role in male fertility by binding to defective sperm cells and promoting their removal during spermatogenesis (PubMed:26394016). {ECO:0000250|UniProtKB:C9XI63, ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:26394016}.; FUNCTION: [Thioester-containing protein 1 allele R1]: Binds to and mediates killing of parasite P.bergei ookinetes by lysis and melanization. {ECO:0000269|PubMed:15006349}.; FUNCTION: [Thioester-containing protein 1 C-terminal]: Binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance. {ECO:0000250|UniProtKB:Q9GYW4}.
Anopheles gambiae (African malaria mosquito)
D0E0C2
SCNA1_PERAM
MADNSPLIREERQRLFRPYTRAMLTAPSAQPAKENGKTEENKDNSRDKGRGANKDRDGSAHPDQALEQGSRLPARMRNIFPAELASTPLEDFDPFYKNKKTFVVVTKAGDIFRFSGEKSLWMLDPFTPIRRVAISTMVQPIFSYFIMITILIHCIFMIMPATQTTYILELVFLSIYTIEVVVKVLARGFILHPFAYLRDPWNWLDFLVTLIGYITLVVDLGHLYALRAFRVLRSWRTVTIVPGWRTIVDALSLSITSLKDLVLLLLFSLFVFAVLGLQIYMGVLTQKCVKHFPADGSWGNFTDERWFNYTSNSSHWYIPDDWIEYPLCGNSSGAGMCPPGYTCLQGYGGNPNYGYTSFDTFGWAFLSVFRLVTLDYWEDLYQLALRSAGPWHILFFIIVVFYGTFCFLNFILAVVVMSYTHMVKRADEEKAAERELKKEKKAASVANNTANGQEQTTIEMNGDEAVVIDNNDQAARQQSDPETPAPSVTQRLTDFLCVWDCCVPWQKLQGAIGAVVLSPFFELFIAVIIVLNITFMALDHHDMNIEFERILRTGNYIFTSIYIVEAVLKIIALSPKFYFKDSWNVFDFIIVVFAILELGLEGVQGLSVFRSFRLLRVFRLAKFWPTLNNFMSVMTKSYGAFVNVMYVMFLLLFIFAIIGMQLFGMNYIDNMERFPDGDLPRWNFTDFLHSFMIVFRALCGEWIESMWDCMLVGDWSCIPFFVAVFFVGNLVILNLLIALLLNNYGSFCTSPTSDEEDSKDEDALAQIVRIFKRFKPNLNAVKLSPMKPDSEDIVESQEIQGNNIADAEDVLAGEFPPDCCCNAFYKCFPSRPARDSSVQRMWSNIRRVCFLLAKNKYFQKFVTAVLVITSVLLALEDIYLPQRPVLVNITLYVDYVLTAFFVIEMIIMLFAVGFKKYFTSKWYWLDFIVVVAYLLNFVLMCAGIEALQTLRLLRVFRLFRPLSKVNGMQVVTSTLVEAVPHIFNVILVGIFFWLVFAIMGVQLFAGKFYKCVDENSTVLSHEITMDRNDCLHENYTWENSPMNFDHVGNAYLSLLQVATFKGWLQIMNDAIDSREVHKQPIRETNIYMYLYFIFFIVFGSFFILKLFVCILIDIFRQQRRKAEGLSATDSRTQLIYRRAVMRTMSAKPVKRIPKPTCHPQSLMYDISVNRKFEYTMMILIILNVAVMAIDHYGQSMEFSEVLDYLNLIFIIIFFVECVIKVSGLRHHYFKDPWNIIDFLYVVLAIAGLMLSDVIEKYFISPTLLRILRILRVGRLLRYFQSARGMRLLLLALRKALRTLFNVSFLLFVIMFVYAVFGMEFFMHIRDAGAIDDVYNFKTFGQSIILLFQLATSAGWDGVYFAIANEEDCRAPDHELGYPGNCGSRALGIAYLVSYLIITCLVVINMYAAVILDYVLEVYEDSKEGLTDDDYDMFFEVWQQFDPEATQYIRYDQLSELLEALQPPLQVQKPNKYKILSMNIPICKDDHIFYKDVLEALVKDVFSRRGSPVEAGDVQAPNVDEAEYKPVSSTLQRQREEYCVRLIQNAWRKHKQQN
null
null
membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]
axon [GO:0030424]; voltage-gated sodium channel complex [GO:0001518]
voltage-gated sodium channel activity [GO:0005248]
PF16905;PF00520;
1.10.287.70;1.10.238.10;1.20.120.350;
Sodium channel (TC 1.A.1.10) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU361132, ECO:0000269|PubMed:28183995}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361132, ECO:0000269|PubMed:28183995}.
null
null
null
null
null
FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. {ECO:0000255|RuleBase:RU361132, ECO:0000305|PubMed:28183995}.
Periplaneta americana (American cockroach) (Blatta americana)
D0E8I5
PHNZ_UNCHF
MSLSNSSKVSVLISLLEKSRDLDYIGEAINQLEHSLQCAYFAQRSGADNEMVLAALLHDLGHYCNDTSFEDMGGYGVWQHEKVGADYLRGLGFSERVACLIEGHVAAKRYLVSSKASYLKNLSDASRKTLEYQGGPMDEGERRLFEEREDFKDCLKIRAWDEKGKQTDLKVPGPEHYRKMMEEHLSENQN
1.13.11.78
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:22564006, ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911}; Note=Binds 2 iron ions per subunit. During catalysis, PhnZ uses a mixed-valent Fe(2+)/Fe(3+) cofactor. {ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911};
null
null
hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]
PF01966;
1.10.3210.10;
null
null
null
CATALYTIC ACTIVITY: Reaction=(1R)-(2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + 2 H(+) + phosphate; Xref=Rhea:RHEA:41444, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:141612; EC=1.13.11.78; Evidence={ECO:0000269|PubMed:22564006, ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for (R,R)-2-amino-1-hydroxypropylphosphonic acid {ECO:0000269|PubMed:24706911}; KM=0.17 mM for (R)-2-amino-1-hydroxyethylphosphonic acid {ECO:0000269|PubMed:24706911}; Note=kcat is 11 min(-1) for (R)-2-amino-1-hydroxyethylphosphonic acid as substrate. kcat is 7 min(-1) for (R,R)-2-amino-1-hydroxypropylphosphonic acid as substrate. {ECO:0000269|PubMed:24706911};
null
null
null
FUNCTION: Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the cleavage of the carbon-phosphorus bond of (2-amino-1-hydroxyethyl)phosphonic acid to yield glycine and phosphate through an oxidative mechanism (PubMed:22564006, PubMed:24198335, PubMed:24706911). It reacts stereospecifically with the R-enantiomer of (2-amino-1-hydroxyethyl)phosphonic acid and is also able to use (R,R)-2-amino-1-hydroxypropylphosphonate as substrate (PubMed:24706911). {ECO:0000269|PubMed:22564006, ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911, ECO:0000305|PubMed:19788654}.
Uncultured bacterium HF130_AEPn_1
D0EM77
KLY_TANFA
MKRFILLFFLSTIAIFKVYSQRLYDNGPLTGDNNYVLQGSKWNKTTLKYYIYNSSSHLTTTERENAIRSAFALWSDKSTLSFIQVYNPNQADIKIKWEKGNHGDGYPFDGNTGILAHAFYPPPAGGNYAGHLHFDGDENWSINGSGIDLITVAAHEIGHLLGIEHSNVSSALMYPYYTGIKRQLDNDDCLAVWDLYGYPFSISGPSSVCDQATYTVENLLSGATVQWSVSNPNIATINSSNGVLTCRGNGICEVRATINNSSVALTPLKICLGTPISQDITLTVESLNSNGTLCTDNPNAIMADHPGGNHLGYIREYEWRISNGWQIAHHPGDNGIYADHFIVTVIPLSPLPGSPTVSVRARSECGWGTWKEVQIPAVSCSRTISPFTLSPNPATDEVILQLMETDEVSGLSVLSTDRSAYEIQIWSGMRMLRSFRTNEPTFQISMTGLPAGLYFVRVVKNGQTYTQKLIKK
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557};
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
PF00413;PF18962;
2.60.40.1080;3.40.390.10;
Peptidase M10A family
PTM: Processes itself into the mature 18-kDa enzyme (Kly18) through sequential autoproteolytic cleavage at both the N- and C-termini. However, the maturation intermediate Kly38 is found to be more active than Kly18 and the rate for its processing is slow, which raises the question as to whether Kly38 is a physiologically relevant entity.
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 for casein degradation. Active in the broad pH range from 6.5 to 8.5. {ECO:0000269|PubMed:19919176};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: In the presence of CaCl(2), the enzyme is fully stable for up to 40 minutes at 70 degrees Celsius, whereas karilysin incubated without calcium loses 50% of its activity within 30 minutes. {ECO:0000269|PubMed:19919176};
FUNCTION: Metalloprotease able to cleave casein, gelatin, elastin, fibrinogen and fibronectin. Shows exclusive preference for hydrophobic residues, especially Leu, Tyr and Met, at the P1' position of substrates, and for Pro or Ala at P3. Can efficiently cleave the antimicrobial peptide LL-37 which is a component of the immune system, leading to a significant reduction of its bactericidal activity. Is also able to inhibit all pathways of the human complement system. The classical and lectin complement pathways are inhibited because of the efficient degradation of mannose-binding lectin, ficolin-2, ficolin-3, and C4 by karilysin, whereas inhibition of the terminal pathway is caused by cleavage of C5. Thus, karilysin appears to be a major virulence factor of T.forsythia that contributes to evasion of the human immune response and periodontal disease. Seems to act synergistically with gingipains from the periodontal pathogen P.gingivalis present at the same sites of infection. {ECO:0000269|PubMed:19919176, ECO:0000269|PubMed:20375548, ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:22287711}.
Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC 5666 / FDC 338) (Bacteroides forsythus)
D0EZM8
NS1_HBOC1
MAFNPPVIRAFSQPAFTYVFKFPYPQWKEKEWLLHALLAHGTEQSMIQLRNCAPHPDEDIIRDDLLISLEDRHFGAVLCKAVYMATTTLMSHKQRNMFPRCDIIVQSELGEKNLHCHIIVGGEGLSKRNAKSSCAQFYGLILAEIIQRCKSLLATRPFEPEEADIFHTLKKAEREAWGGVTGGNMQILQYRDRRGDLHAQTVDPLRFFKNYLLPKNRCISSYSKPDVCTSPDNWFILAEKTYSHTLINGLPLPEHYRKNYHATLDNEVIPGPQTMAYGGRGPWEHLPEVGDQRLAASSVSTTYKPNKKEKLMLNLLDKCKELNLLVYEDLVANCPELLLMLEGQPGGARLIEQVLGMHHINVCSNFTALTYLFHLHPVTSLDSDNKALQLLLIQGYNPLAVGHALCCVLNKQFGKQNTVCFYGPASTGKTNMAKAIVQGIRLYGCVNHLNKGFVFNDCRQRLVVWWEECLMHQDWVEPAKCILGGTECRIDVKHRDSVLLTQTPVIISTNHDIYAVVGGNSVSHVHAAPLKERVIQLNFMKQLPQTFGEITATEIAALLQWCFNEYDCTLTGFKQKWNLDKIPNSFPLGVLCPTHSQDFTLHENGYCTDCGGYLPHSADNSMYTDRASETSTGDITPSDLGDSDGEDTEPETSQVDYCPPKKRRLTAPASPPNSPASSVSTITFFNTWHAQPRDEDELREYERQASLLQKKRESRKRGEEETLADNSSQEQEPQPDPTQWGERLGFISSGTPNQPPIVLHCFEDLRPSDEDEGEYIGEKRQ
3.1.21.-; 3.6.4.12
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03134}; Note=The endonuclease active site can probably bind other divalent cations. {ECO:0000250|UniProtKB:P03134};
DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693]
host cell nucleus [GO:0042025]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]
PF01057;
3.40.1310.20;3.40.50.300;
Parvoviruses initiator protein NS1 family
null
SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:20457462}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P03134};
null
null
null
null
FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5' direction on the longer strand. Participates in the transcriptional regulation of several promoters. {ECO:0000250|UniProtKB:P03134}.
Primate bocaparvovirus 1 (strain Human bocavirus 1 type 1) (HBoV1) (Human bocavirus type 1)
D0FH76
VPS4_BOMMO
MTSSNTLQKAIDLVTKATEEDKNKNYEEALRLYEHGVEYFLHAVKYEAQGERAKESIRAKCLQYLDRAEKLKEYLKKDQKKKPVKDGESKSDDKKSDSDSDSDDPEKKKLQGKLEGAIVVEKPHVKWSDVAGLEAAKEALKEAVILPIKFPHLFTGKRIPWKGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLVSKWLGESEKLVKNLFDLARQHKPSIIFIDEIDSLCSSRSDNESESARRIKTEFLVQMQGVGNDMDGILVLGATNIPWVLDSAIRRRFEKRIYIALPEEHARLDMFKLHLGNTRHQLSEQDMKLLAAKSEGYSGADISIVVRDALMQPVRKVQSATHFKKISGPSPTDPNVIVNDLLTPCSPGDPGAIEMTWIDVPSDKLGEPPVTMSDMLRSLAVSKPTVNDDDMVKLRKFMEDFGQEG
3.6.4.6
null
cell cycle [GO:0007049]; cell division [GO:0051301]; endosomal transport [GO:0016197]; instar larval or pupal development [GO:0002165]; metamorphosis [GO:0007552]; protein complex oligomerization [GO:0051259]; protein transport [GO:0015031]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; vacuole organization [GO:0007033]
cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; midbody [GO:0030496]; vacuolar membrane [GO:0005774]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; protein self-association [GO:0043621]
PF00004;PF17862;PF04212;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family
null
SUBCELLULAR LOCATION: Prevacuolar compartment membrane {ECO:0000250|UniProtKB:Q8VEJ9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8VEJ9}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UN37}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UN37}. Midbody {ECO:0000250|UniProtKB:Q9UN37}. Cytoplasm {ECO:0000269|PubMed:28973578}. Note=Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells. {ECO:0000250|UniProtKB:Q9UN37}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; Evidence={ECO:0000269|PubMed:23053938};
null
null
null
null
FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane. {ECO:0000250|UniProtKB:Q9UN37}.
Bombyx mori (Silk moth)
D0G895
ACE3_MOUSE
MNLPWALLLVLLSHRQLLPWLRTVGETSLNDFYSEAQAKLFLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRKLQNIDKSALPTEDLLEYNRLLTYMETAYNRAEVCLDEGPCLTLEPDLQEIMATSRDQKELLWAWQGWRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYRYYGPELIDLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWIKSMMEKPADGREVECHTSSWNFYKFNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVIALSVSSHKYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCPPVPRSDDDFDPGAKFHIPANVPYIRYFLGLILQFQLHEALCEASGHVGPLHQCDNYNSKVAGKILGDLLKLGSSRPWREVLQEVTGESNISTKAFLTYFKPLMDWLVTENVKQGDTLGWPDFSCSFEEKITSKVSFLGTDTEPEQAYLGQWVLLSMSFFMLVLILALGFRLHYLEKQLLDEDTMILKTLPYSYFLGIAMEPHQAARKQWLLLGLCCILMLCCIGLLIRIVTQNTENTPWMKNEGQS
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01355};
positive regulation of systemic arterial blood pressure [GO:0003084]; proteolysis [GO:0006508]; regulation of systemic arterial blood pressure by renin-angiotensin [GO:0003081]
acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; peptidyl-dipeptidase activity [GO:0008241]
PF01401;
null
Peptidase M2 family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:20421979}; Multi-pass membrane protein {ECO:0000255}. Note=Disappears from acrosome reacted sperm. Co-localizes with IZUMO1 at acrosomal cap area. {ECO:0000269|PubMed:20421979}.
null
null
null
null
null
null
Mus musculus (Mouse)
D0KN27
HELS_SACS9
MSLELEWMPIEDLKLPSNVIEIIKKRGIKKLNPPQTEAVKKGLLEGNRLLLTSPTGSGKTLIAEMGIISFLLKNGGKAIYVTPLRALTNEKYLTFKDWELIGFKVAMTSGDYDTDDAWLKNYDIIITTYEKLDSLWRHRPEWLNEVNYFVLDELHYLNDPERGPVVESVTIRAKRRNLLALSATISNYKQIAKWLGAEPVATNWRPVPLIEGVIYPERKKKEYNVIFKDNTTKKVHGDDAIIAYTLDSLSKNGQVLVFRNSRKMAESTALKIANYMNFVSLDENALSEILKQLDDIEEGGSDEKELLKSLISKGVAYHHAGLSKALRDLIEEGFRQRKIKVIVATPTLAAGVNLPARTVIIGDIYRFNKKIAGYYDEIPIMEYKQMSGRAGRPGFDQIGESIVVVRDKEDVDRVFKKYVLSDVEPIESKLGSERAFYTFLLGILSAEGNLSEKQLENFAYESLLAKQLVDVYFDRAIRWLLEHSFIKEEGNTFALTNFGKRVADLYINPFTADIIRKGLEGHKASCELAYLHLLAFTPDGPLVSVGRNEEEELIELLEDLDCELLIEEPYEEDEYSLYINALKVALIMKDWMDEVDEDTILSKYNIGSGDLRNMVETMDWLTYSAYHLSRELKLNEHADKLRILNLRVRDGIKEELLELVQISGVGRKRARLLYNNGIKELGDVVMNPDKVKNLLGQKLGEKVVQEAARLLNRFH
5.6.2.4
null
DNA repair [GO:0006281]
null
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853]
PF00270;PF00271;PF21280;
1.10.3380.30;1.10.150.20;3.40.50.300;
Helicase family, Hel308 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|Ref.2};
null
null
null
null
FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. A low processivity 3'-5' helicase. Unwinds short dsDNA substrates with 3'-overhangs (25 bp dsDNA with 25 base overhang), less active on longer dsDNA substrates. Also unwinds the lagging strand of a stalled replication fork (but the leading strand was not tested). Binds ssDNA, but dsDNA about 35-fold less well. Able to displace streptavidin from biotinylated ssDNA, which is partially inhibited by DNA-binding proteins, suggesting it may play a role in stripping proteins from stalled replication forks. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:18056710}.
Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus)
D0LB45
LYSX_GORB4
MALDTPSSDLPVSTDDTAEHQPTPAHRPPSAADRRSVDLLEKIRRPRGFGAGAPKIAGTVVGVLAGIALLSSIFPLFRRLIHYPRDFIDNYIVSLPNTSLAWAFVLALVAIALSSRKRIAWWIATIYLVLFMVSNALLLVDPVATDFGVDTDERIQIWIGLGIDAAALIFLIVTYRQFYTRVRRGALFRALGVLIVGLTAATLVGWGLVWAWPGSLERTERLPYAFNRVVTFGSIDSRTFDGHHTHIVIDSALGLLGALALIAAATVLFRSQRLESLMTSDDEKLIRALITRFNDDDSLAYFSTRRDKAVVFSPDGRAAITYRVEIGVGLAGGDPIGDPESWPDAIAEFLTLCDRYGWHPAAMGSSARGAAAYDAAGFGSLSIGDEAILHTREYTISGPAMKAVRQAVTRTRRAGVTVRIRRHGEVPDDEMPQVIARADAWRDTDEERGFAMALSRLGDRADDDCLLVEAVEHAGTPEEKVIGMLSFVPWGRRGVSLDVMRRDRGSVNGVVETMVTELCRNSEQFGITEISLNFATFRAFFEQGPQIGAGPIMRLGYSVLMFGSRFFQMESLYKSNAKYLPDWQPRFLCFEDNRILPRVGLAAIVTEGFVQLPRFGRKQHYIAGQSSIPAGVDADALIAQLESEEDRTAVEVHRPEQVRVRVAKLDRLIEEGFDPYPPADAPTHTIAEAIAEPEGTQVTIAGRVTKMRDFGKVTFADVHDWSGQIQMLVEASRVIPGTPDFGSDVDLGDLVEARGVIGRSRSGELSVLIDAWRFNGKCLRPLPDKWSGLTDPEARVRQRYVDLAINPRSRELLATRSVVVKALRDFLADRGFMEVETPILQQIHGGANATPFQTHINAYNLDLYLRIAPELYLKRLCVGGVEKVFEIGRNFRNEGVDFSHNPEFTSLEAYAAHSDYLKMLDLTREMIQHAATAAHGEPVIIRVDDEGNEQRVDISGDWPVRTVHEVVSEGAGVEITSDTEVSELRGICDRLEIAYRPDWDAGQIVLELYEHLGEDRTTVPTFYTDFPTSTSPLTRAHRSKPGVAERWDLVAWGVELGTAYTELTDPVEQRKRLTAQSILAADGDPEAMELDEDFLTALEYAMPPTGGLGVGVDRVVMLITGQSIRESLAFPMVKPTDA
2.3.2.3; 6.1.1.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677]
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049]
PF09924;PF00152;PF16995;PF01336;
2.40.50.140;
LPG synthetase family; Class-II aminoacyl-tRNA synthetase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3;
null
null
null
null
FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}.
Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis)
D0N4K2
CRE5_PHYIT
MQTIQLIIFVAFVLSRAAASISSFSDPTSIVNINHDANRLSRALAAGQNQTQRSLRQHEGEDRGAIDKADEVVSKMKALMGTAKNVPNNLAALIAKRSKTAGEFVRRPFLVSKLSKRYNIADQLSFSTLKQLDKIDNMRIVDIKNGIKGNKKTPNGMRRKIKHFEGMKTAPQKFLESHVGRDMQRYGKDGSRWLSAGVVTRTTDQGERQILLISSSNPARGDFLLPKGGWDRGEKIKKAALREVMEEGGVCRAL
3.6.1.-
null
adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate metabolic process [GO:0071543]
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; nucleus [GO:0005634]
bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298]; metal ion binding [GO:0046872]
PF00293;
3.90.79.10;
RxLR effector family; Nudix hydrolase family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host cytoplasm {ECO:0000269|PubMed:30329083}. Host nucleus, host nucleolus {ECO:0000269|PubMed:30329083}. Host nucleus {ECO:0000269|PubMed:30329083}.
null
null
null
null
null
FUNCTION: Effector that is involved in host plant infection. Contributes to virulence during the early infection stage, by inhibiting plant defense responses induced by both PAMP-triggered immunity (PTI) and effector-triggered immunity (ETI). {ECO:0000269|PubMed:29312401, ECO:0000269|PubMed:30329083}.
Phytophthora infestans (strain T30-4) (Potato late blight agent)
D0NPN8
A3AEM_PHYIT
MRLAIMLSATAVAINFATSSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTERADAKKLAKQLMGNDKLADAAYMWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY
null
null
effector-mediated activation of plant hypersensitive response by symbiont [GO:0080185]
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]
null
PF16810;
1.10.10.2460;
RxLR effector family
PTM: Proteolytically cleaved. The cleavage site directly after the RxLR sequence and the high conservation among other effector proteins suggest that the RxLR motif might play a crucial role in the intracellular processing before secretion. {ECO:0000269|PubMed:28522546}.; PTM: glycosylated. {ECO:0000269|PubMed:28522546}.; PTM: N-acetylated at Lys-48 after cleavage. {ECO:0000269|PubMed:28522546}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host cytoplasm {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}.
null
null
null
null
null
FUNCTION: Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways (PubMed:19794118, PubMed:20457921, PubMed:21348873, PubMed:26348328). Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. By preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, Avr3a further abolishes host cell death during the biotrophic phase of infection (PubMed:19794118, PubMed:20457921, PubMed:21348873). Associates with and affects also the function of the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis (PubMed:26348328). The Avr3a(EM) form evades recognition by R3a, thus does not trigger R3a-mediated hypersensitivity and does not suppress INF1-induced cell death (PubMed:15894622, PubMed:16965554, PubMed:19245321). {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:19245321, ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:20457921, ECO:0000269|PubMed:21348873, ECO:0000269|PubMed:26348328}.
Phytophthora infestans (strain T30-4) (Potato late blight agent)
D0P3S7
ABLB1_PHYIT
MRSLLLTVLLNLVVLLATTGAVSSNLNTAVNYASTSKIRFLSTEYNADEKRSLRGDYNNEVTKEPNTSDEERAFSISKSAEYVKMVLYGFKLGFSPRTQSKTVLRYEDKLFTALYKSGETPRSLRTKHLDKASASVFFNRFKKWYDKNVGPS
null
null
null
extracellular region [GO:0005576]; host cell nucleolus [GO:0044196]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
null
null
null
RxLR effector family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host nucleus, host nucleolus {ECO:0000269|PubMed:30329083}. Host nucleus {ECO:0000269|PubMed:30329083}. Host cell membrane {ECO:0000269|PubMed:14999409}.
null
null
null
null
null
FUNCTION: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RGA2/Rpi-blb1 (PubMed:18682852, PubMed:19794118, PubMed:19888819, PubMed:20479869, PubMed:21483488). Enhances P.infestans colonization of plant hosts Nicotiana benthamiana and potato Solanum bulbocastanum leaves (PubMed:28350531, PubMed:30329083). Associates with host legume-type lectin receptor kinases and disrupts attachments between the host plasma membrane and cell wall (PubMed:14999409, PubMed:21483488). {ECO:0000269|PubMed:14999409, ECO:0000269|PubMed:18682852, ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:19888819, ECO:0000269|PubMed:20479869, ECO:0000269|PubMed:21483488, ECO:0000269|PubMed:28350531, ECO:0000269|PubMed:30329083}.
Phytophthora infestans (strain T30-4) (Potato late blight agent)
D0PRN2
NRX1B_CHICK
MGGFLRGSPEPGPAGGSGGSAGGRLALLWIVPLTLSGLLGVAWGASSLGAHHIHHFHGSSKHHSVPIAIYRSPASLRGGHAGTTYIFSKGGGQITYTWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSTGLGDYLELHIHQGKIGVKFNVGTDDIAIEEINAIINDGKYHVVRFTRSGGNATLQVDNWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIKIGGKERGHPFQGQLSGLYYNGLKVLNMAAENDANIVIEGNVRLVGEVPSSMTTESTATAMQSEMSTSVMETTTTLATSTARRGKAPTKEPIGQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRAGGGREYPGSSEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVIKEKQPNSAKSSNKNKKNKDKEYYV
null
null
angiogenesis [GO:0001525]; cell adhesion [GO:0007155]
membrane [GO:0016020]
null
PF02210;PF01034;
2.60.120.200;
Neurexin family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling (By similarity). Plays a role in angiogenesis. {ECO:0000250, ECO:0000269|PubMed:19926856}.
Gallus gallus (Chicken)
D0PV95
DDX3_CAEEL
MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS
3.6.4.13
null
cell differentiation [GO:0030154]; gamete generation [GO:0007276]; masculinization of hermaphroditic germ-line [GO:0042006]; negative regulation of gene expression [GO:0010629]; positive regulation of embryonic development [GO:0040019]; positive regulation of fertilization [GO:1905516]; regulation of translation [GO:0006417]
canonical inflammasome complex [GO:0061702]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; P granule [GO:0043186]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; molecular condensate scaffold activity [GO:0140693]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592]
PF00270;PF00271;
3.40.50.300;
DEAD box helicase family, DDX3/DED1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19361491, ECO:0000269|PubMed:26015579}. Cytoplasmic granule {ECO:0000269|PubMed:19361491, ECO:0000269|PubMed:26015579}. Nucleus {ECO:0000250|UniProtKB:O00571}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O00571}. Inflammasome {ECO:0000250|UniProtKB:Q62167}. Cell membrane {ECO:0000250|UniProtKB:O00571}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O00571}. Note=Localizes to P granules in germline precursor cells. Shuttles between the nucleus and the cytosol (By similarity). {ECO:0000250|UniProtKB:O00571, ECO:0000269|PubMed:19361491}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:27546789};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3156 mM for ATP {ECO:0000269|PubMed:27546789};
null
null
null
FUNCTION: Multifunctional ATP-dependent RNA helicase (PubMed:27546789). Plays a role in RNA remodeling, but is not required for RNA unwinding (PubMed:27546789). Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA (PubMed:26015579, PubMed:27546789). This process is also dependent upon ATP; ATP reduces binding to RNA and subsequently diminishes RNA annealing (PubMed:27546789). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in the regulation of transcription and translation initiation. Involved in innate immunity (By similarity). Involved in both stress and inflammatory responses (By similarity). Promotes liquid-liquid phase separation of P granules, which is a process important for intracellular organization and stress granule assembly (PubMed:26015579). Required for embryonic development (PubMed:19361491, PubMed:26015579). Plays a role in sexual cell fate determination by negatively regulating the translation of the sex determining protein tra-2 (PubMed:26015579, PubMed:9043090, PubMed:9321409). May play a protective role in the response to heat and oxidative stress (PubMed:24844228). May negatively regulate extrinsic apoptotic signaling pathway via death domain receptors. May be involved in mitotic chromosome segregation (By similarity). {ECO:0000250|UniProtKB:O00571, ECO:0000250|UniProtKB:Q62167, ECO:0000269|PubMed:19361491, ECO:0000269|PubMed:24844228, ECO:0000269|PubMed:26015579, ECO:0000269|PubMed:27546789, ECO:0000269|PubMed:9043090, ECO:0000269|PubMed:9321409}.
Caenorhabditis elegans
D0Q0Y7
CNIH3_RAT
MAFTFAAFCYMLSLVLCAALIFFAIWHIIAFDELRTDFKSPIDQCNPVHARERLRNIERICFLLRKLVLPEYSIHSLFCVMFLCAQEWLTLGLNVPLLFYHFWRYFHCPADSSELAYDPPVVMNADTLSYCQKEAWCKLAFYLLSFFYYLYCMIYTLVSS
null
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; regulation of AMPA receptor activity [GO:2000311]; regulation of membrane potential [GO:0042391]; synaptic transmission, glutamatergic [GO:0035249]
AMPA glutamate receptor complex [GO:0032281]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
channel regulator activity [GO:0016247]
PF03311;
null
Cornichon family
null
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:19265014}; Multi-pass membrane protein {ECO:0000269|PubMed:19265014}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells).
null
null
null
null
null
FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. {ECO:0000269|PubMed:19265014}.
Rattus norvegicus (Rat)
D0QMC3
MNDAL_MOUSE
MAEYKKIVLLKGLESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKDLKDLAKKLKTEKAKVQKKKQGKCKTAVKKKGQDELSSSESLFINKESYKSVPSSKKKGKAIAKTEGEKKNKLTQDQDHLPETSGTDIKTEEDCLQNSPKPPPTSPSSSSNKKKRKEITKTEGGKKKKLTQEQAQLPEPLGTDIKKDEDCLQTPPKPPPTPPSSSLNKKRKSRREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSATNQKPQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMFHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVLKADPDQMIEVPNNIIRNANASPKICDIQKGTSGAVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVEGSGQWHNINCKEGDKLHLFCFHLKRERGQPKLVCGDHSFVKIKVTKAGKKKEASTVLSSTKNEEENNYPKDGIKVEMPDYHV
null
null
activation of innate immune response [GO:0002218]; cellular response to interferon-beta [GO:0035458]; negative regulation of cell growth [GO:0030308]
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
double-stranded DNA binding [GO:0003690]
PF02760;PF02758;
1.10.533.10;2.40.50.140;
HIN-200 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19654412}.
null
null
null
null
null
FUNCTION: Suppresses cell growth when expressed ectopically. {ECO:0000269|PubMed:19654412}.
Mus musculus (Mouse)
D0TZF0
ISOA1_ORYSJ
MASLPHCLSARPLVVAAAPGRPGPGPGPWLRGGARRRNAAFSAGNAGRRVGLRRSVASAVEVGVGEDEEEGVEEEEEEVEAVVMPERYALGGACRVLAGMPAPLGATALDGGVNFAVYSAGASAASLCLFTPDDLEADEVTEEVPLDPLFNRTGNVWHVFIEGELHNMLYGYRFDGMFAPHCGQYFDVSNVVVDPYAKAVISRGEYGVPGPGGDCWPQMAGMIPLPYSTFDWQGDLPLRYPQKDLVIYEMHLRGFTKHSSSNVEHPGTYIGAISKLDYLKELGVNCVELMPCHEFNELEYFSCSSKMNFWGYSTINFFSPMIRYSSGGIRNCGRDAINEFKTFVREAHKRGIEVIMDVVFNHTAEGNEKGPILSFRGIDNSTYYMLAPKGEFYNYSGCGNTFNCNHPVVREFIVDCLRYWVTEMHVDGFRFDLASIMTRGCSLWDPVNVYGSPVEGDMTTTGTPLATPPLIDMISNDPILGDVKLIAEAWDAGGLYQVGQFPHWKIWSEWNGKYRDIVRQFIKGTDGFAGGFAECLCGSPHLYQAGGRKPWHSINFVCAHDGFTLADLVTYNKKYNSSNGEDNRDGENHNLSWNCGEEGEFAGLSVKRLRKRQMRNFFVSLMVSQGVPMFYMGDEYGHTKGGNNNTYCHDHYVNYFRWDKKEESSDLQRFCSLMTKFRKQCESLGLADFPTAQRLHWHGHQPGKPDWSETSRFVAFSTKDETKGEIYVAFNASHLPAVVGLPERPGYRWEPLVDTGKPAPYDFLTDDLPDRAHAVHLFSHFLNSNLYPMLSYSSIILELQPDD
3.2.1.68
null
amylopectin biosynthetic process [GO:0010021]; starch biosynthetic process [GO:0019252]; starch catabolic process [GO:0005983]
chloroplast isoamylase complex [GO:0010368]; isoamylase complex [GO:0043033]
isoamylase activity [GO:0019156]
PF00128;PF02922;PF21156;
3.20.20.80;2.60.40.1180;2.60.40.10;
Glycosyl hydrolase 13 family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68; Evidence={ECO:0000269|PubMed:10333591};
null
PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 at 30 degrees Celsius. {ECO:0000269|PubMed:10333591};
null
FUNCTION: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch (PubMed:10517831, PubMed:15618430, PubMed:16953433, PubMed:21436381). Works as ISA1 homooligomer or together with ISA2 as heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms (PubMed:16953433, PubMed:21436381). {ECO:0000269|PubMed:10517831, ECO:0000269|PubMed:15618430, ECO:0000269|PubMed:16953433, ECO:0000269|PubMed:21436381}.
Oryza sativa subsp. japonica (Rice)
D0VWM8
TADBP_CAEEL
MADETPKVKTEPAAEVKSPLDEVKEIRKEAELTQTGSDEKKTTDPEFITVQDPNGDEPIELPTVDGVVLMTTLQASFPGATGLKYKNPKTGANRAVQVDPSGLKLIAPADGWENKTFFVIVAPQSERVRALSSADATSAKRRKVGSSDDSDSDDGRDGRSGRKRAVERDSQPVDLIVLGVDFKTTDECFQKYFEDIGTVVFCEIKRKSDGNSKGFGFVRMSSVGEQNKVLAIPQHMIDGRRCDVKVPDGRSLQDKQGRPSISRIFVGRLTDKVDEHQLRKVFGDEAKSYIETAVVTDVFIPKPFRGFAFVTLSSAEAAERIVSKGSLTVNGLSVGLSIAQPREENNQSVGPDYGLPAGYRNRRERDRPDRRPIQNEAPLPMPFVRPPQDYSYRQQNSPLERRYWAPGDSRGPGW
null
null
determination of adult lifespan [GO:0008340]; hyperosmotic response [GO:0006972]; mRNA processing [GO:0006397]; positive regulation of gene expression [GO:0010628]; regulation of gene expression [GO:0010468]; response to oxidative stress [GO:0006979]; RNA splicing [GO:0008380]
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]
PF00076;PF18694;
3.30.70.330;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22792076}. Cytoplasm {ECO:0000269|PubMed:22792076}. Note=Shuttles from the nucleus to the cytoplasm under stress conditions. {ECO:0000269|PubMed:22792076}.
null
null
null
null
null
FUNCTION: RNA-binding protein which regulates transcription, splicing and RNA-editing (PubMed:25391662). Limits the accumulation of double-stranded RNA by maintaining the abundance of the mature RNA transcripts that are formed from double-stranded precursor RNAs (PubMed:25391662). Stress response protein that acts downstream of daf-16 in the insulin/IGF pathway to regulate longevity and the cellular stress response to osmotic, oxidative, proteotoxic and endoplasmic reticulum stress (PubMed:22232551, PubMed:22792076). Involved in the regulation of physiological processes including aging, fertility, growth and locomotion (PubMed:22232551, PubMed:29760282). Plays a role in maintaining localization of chromobox protein homolog hpl-2 to gene bodies, perhaps acting via binding to nascent RNA transcripts (PubMed:29760282). {ECO:0000269|PubMed:22232551, ECO:0000269|PubMed:22792076, ECO:0000269|PubMed:25391662, ECO:0000269|PubMed:29760282}.
Caenorhabditis elegans
D0VWR8
PSBD_THEVL
ERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLLLNEGIRAWMAPQDQPHENFVFPEEVLPRGNAL
1.10.3.9
COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624};
photosynthetic electron transport in photosystem II [GO:0009772]
photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676]
chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; metal ion binding [GO:0046872]; oxygen evolving activity [GO:0010242]
PF00124;
1.20.85.10;
Reaction center PufL/M/PsbA/D family
null
SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}.
CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01383};
null
null
null
null
FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors (PubMed:19433803, PubMed:23426624). D2 is needed for assembly of a stable PSII complex. {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624}.
Thermostichus vulcanus (Synechococcus vulcanus)
D0VWU3
LAC1_TRAMX
AVGPVADNTITDAATSPDGFSRQAVVVNGVTPGPLVAGNIGDRFQLNVIDNLTNHTMLKTTSVHWHGFFQQGTNWADGPAFINQCPISPGHSFLYDFQVPNQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASRYDVDNDDTVITLADWYHTAAKLGPRFPAGADATLINGKGRAPSDTSAELSVIKVTKGKRYRFRLVSLSCDPNFTFSIDGHNLTIIEVDSSNSQPLSVDSIQIFAAQRYSFVLNANQAVDNYWIRANPNFGNVGFNGGINSAILRYDGAPAVEPTTNQTTSVKPLNEVNLHPLVSTPVPGSPSSGGVDKAINMAFNFNGSNFFINGASFVPPSVPVLLQILSGAQTAQDLLPSGSVYVLPSNASIEISFPATAAAPGAPHPFHLHGHTFAVVRSAGSTVYNYSNPIFRDVVSTGTPAAGDNVTIRFLTNNPGPWFLHCHIDFHLEGGFAVVQAEDVPDVKATNPVPQAWSDLCPTYDANAPSDQ
1.10.3.2
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}; Note=Binds 4 Cu cations per monomer. {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782};
lignin catabolic process [GO:0046274]
extracellular region [GO:0005576]
copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491]
PF00394;PF07731;PF07732;
2.60.40.420;
Multicopper oxidase family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}.
CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782};
null
null
null
null
FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000305}.
Trametes maxima (White-rot fungus) (Cerrena maxima)
D0VWV4
C560_PIG
MAALLLRHVGRHCLRAHLSPQLCIRNAVPLGTTAKEEMERFWNKNLGSNRPLSPHITIYRWSLPMAMSICHRGTGIALSAGVSLFGLSALLLPGNFESHLELVKSLCLGPTLIYTAKFGIVFPLMYHTWNGIRHLIWDLGKGLTIPQLTQSGVVVLILTVLSSVGLAAM
null
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15989954}; Note=The heme b is bound between the two transmembrane subunits SDHC and SDHD. {ECO:0000269|PubMed:15989954};
mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; tricarboxylic acid cycle [GO:0006099]
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; plasma membrane [GO:0005886]
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627]
PF01127;
1.20.1300.10;1.20.5.540;
Cytochrome b560 family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17480203}; Multi-pass membrane protein {ECO:0000269|PubMed:17480203}.
null
null
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
null
null
FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000269|PubMed:17480203}.
Sus scrofa (Pig)
D0VWY5
GASHR_MARGR
MTQHFDLIAIGGGSGGLAVAEKAAAFGKRVALIESKALGGTCVNVGCVPKKVMWYASHLAEAVRDAPGFGVQASGGTLDWPRLVAGRDRYIGAINSFWDGYVERLGITRVDGHARFVDAHTIEVEGQRLSADHIVIATGGRPIVPRLPGAELGITSDGFFALQQQPKRVAIIGAGYIGIELAGLLRSFGSEVTVVALEDRLLFQFDPLLSATLAENMHAQGIETHLEFAVAALERDAQGTTLVAQDGTRLEGFDSVIWAVGRAPNTRDLGLEAAGIEVQSNGMVPTDAYQNTNVPGVYALGDITGRDQLTPVAIAAGRRLAERLFDGQSERKLDYDNIPTVVFAHPPLSKVGLSEPEARERLGDVLTVYETSFTPMRYALNEHGPKTAMKLVCAGPEQRVVGVHVIGDGADEMLQGFAVAVKMGATKADFDNTVAIHPGSAEELVTLKEPVRRPGDPLPEGAA
1.8.1.16
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11399772, ECO:0000269|PubMed:17977556}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11399772, ECO:0000269|PubMed:17977556};
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749]
cytosol [GO:0005829]
flavin adenine dinucleotide binding [GO:0050660]; glutathione-disulfide reductase (NADP) activity [GO:0004362]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]
PF07992;PF02852;
3.30.390.30;3.50.50.60;
Class-I pyridine nucleotide-disulfide oxidoreductase family
null
null
CATALYTIC ACTIVITY: Reaction=2 glutathione amide + NAD(+) = glutathione amide disulfide + H(+) + NADH; Xref=Rhea:RHEA:27433, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:59895, ChEBI:CHEBI:59896; EC=1.8.1.16; Evidence={ECO:0000269|PubMed:11399772};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=97 uM for glutathione amide disulfide (GASSAG) for the reverse reaction (in the presence of 100 uM NADH) {ECO:0000269|PubMed:11399772}; KM=6.9 mM for glutathione disulfide (GSH) for the reverse reaction {ECO:0000269|PubMed:11399772}; KM=13.2 uM for NADH for the reverse reaction (in the presence of 500 uM GASSAG) {ECO:0000269|PubMed:11399772}; KM=1.98 mM for NADPH for the reverse reaction {ECO:0000269|PubMed:11399772};
null
null
null
FUNCTION: Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation. {ECO:0000269|PubMed:11399772}.
Marichromatium gracile (Chromatium gracile)
D0VYS2
HSF3_MOUSE
MEQFRKTMVPHFLTKLWILVDDAVLDHVIRWGKDGHSFQIVNEETFAREVLPKYFKHNKITSFIRQLNMYGSRKVFALQTEKTSQENKISIEFQHPLFKRGEACLLANIKRKVPTIKIEGASLYSDEFQKIVTEMQEFKDMQRKMDAKYTQMKQDYSNLYHEVTNLRKKYCAQQQLLTRVLHFILDLMSENHTVLKKRKRSLSFISEDSDSEWDHQYFRIPEDKKEAMEILKDGYELVEDKYKSLLDRVMPILKESKKLISSGDQPSGDDGEHPKVPVQDKPMNEESLTIQLDLTIPVLPEQITEESVEQEPKDISLELDLSSQDSILMKDKSDNLYNNIINRDKKDMHHTEGNLLELNSLLSRKALNYDSDHFSESLSLMKNEEEKSQLDLSGGKDNHMIQCMETPELFLLDEIPMCDFGENLQDYDRLLEDLKNPPNVISALCDHDYVTSNISTLQEDTIENSIPQLCMEANGESSVFPFLILNPVTNIF
null
null
cellular response to heat [GO:0034605]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
PF00447;
1.10.10.10;
HSF family
null
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:19864465}. Nucleus {ECO:0000269|PubMed:19864465}. Note=Cytoplasmic under normal conditions. Translocates to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19864465}. Note=Does not translocate to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}.
null
null
null
null
null
FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription of non-classical heat-shock genes such as PDZD2 and PROM2. Protects cells against heat shock and proteotoxic stress. {ECO:0000269|PubMed:19864465}.
Mus musculus (Mouse)
D0WGK0
ILVC_SLAES
MSVKTKEKEMAVTILYEQDVDPKVIQGLKVGIIGYGSQGHAHALNLMDSGVDVRVGLREGSSSWKTAEEAGLKVTDMDTAAEEADVIMVLVPDEIQPKVYQEHIAAHLKAGNTLAFAHGFNIHYGYIVPPEDVNVIMCAPKGPGHIVRRQFTEGSGVPDLACVQQDATGNAWDIVLSYCWGVGGARSGIIKATFAEETEEDLFGEQAVLCGGLVELVKAGFETLTEAGYPPELAYFECYHEMKMIVDLMYESGIHFMNYSISNTAEYGEYYAGPKVINEQSREAMKEILKRIQDGSFAQEFVDDCNNGHKRLLEQREAINTHPIETTGAQIRSMFSWIKKED
1.1.1.86
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435};
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
cytosol [GO:0005829]
ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661]
PF01450;PF07991;
6.10.240.10;3.40.50.720;
Ketol-acid reductoisomerase family
null
null
CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for NADPH (at pH 7) {ECO:0000269|PubMed:23776225}; KM=45 uM for NADH (at pH 7) {ECO:0000269|PubMed:23776225}; Note=kcat is 0.8 sec(-1) for reductoisomerase activity with NADPH as substrate (at pH 7). kcat is 0.41 sec(-1) for reductoisomerase activity with NADH as substrate (at pH 7). {ECO:0000269|PubMed:23776225};
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
null
null
FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225}.
Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 / S-7)
D0Z5N4
E2AKB_CAEEL
MTKENQIVLDERVKENQHLQEEEKLALDAVYLNQITYIKAHWHVWVPTNCHILLKALDSCFLNGDPLGKSKLSVILHVKCSEDYPQRKPAVDLLDPQGLSKEDVQNLLTILRQMADTWEGCVVIAELAHRVREFLTDHTPRPAGSFHDDMLANKVRTEAEKQRKRLDTEQKELELLEEEMRQRNAIEMEKTLNGTRQENETRIIGGRRIVVLSNMPNTQLLISEWTFRFSSNRNPAEGKRKDFAPFLQKLDAVYNEIQKLCEIKGLDQNLVEYAFVHLQKISVSPDQILIQLNVAQKIFSSEENMQDTYELIVQKSNLLRLLAAQAICGLRYLHEASMTHKHLTLGSVWTRNSTGDCVFRFSDFGSMGPLLDLVKMFGDICSGKYVARDEDKEKEYDRRRKDLFQLGTLLDGLILATRGSTYSRVPTPVEGNQNTGTNLLGNFIAKCQEAKNIDQLVEDPFLKEECQSESENIFTPFGGAMSPDGRMLADNVIIRVLGRGGFGDVVLVRNKMDSTDYAIKRIPLNAKSDKLNRKIAKEAKFFAKLNHPNMVRYYYAWAEDLIPIVEETSDDDSSLGAVPIPGKEKIGKKGKLKTGKSLEDKENKANLGGGDSLMPMNLRGLVKDHSIGVDAKEWSTPFGKPEGPKCASRMRQSKRSTPSGGLKHLSECSSDDEDDDDSSEIDWDAESEEVEDEESDDSDEEDEDDGERLVQLNTETSTGADSVFERSTADEDVVFTAESEDLNAKRRESIELMEINTTTTSKSKLAIDVVPVRKPRILCIQMEYCDRATLRQYIDENHCFNAPTEVWRIFSEVLCGLKYMHDMAMIHRDIKPLNIFLTSQNGVKIGDFGLATLEAMSSKGKIVGGAAEKSTSIEAMLSPNGVKSKGSDVHQTRDIGTQLYMAPELFVDELVHKAPYTSKIDIYSAGVVLFEMFYRPLPPSMDRVSTLNNLRDDIKIPSDFGAGLAAPMAGLARRTVEKMLQRNPDERPTADDLLNDEDLPMHTKEDATFRNLCEKVIKKRDGRMNAWLLDKQFKEEVPTSLNYCYDVDICLERAKYNNREVLVETLRAEFCKILKIHSFEKLHTHTLMPVSTALAAASVRTKPVEVLDRSGVPVALPMDLRQNFVRFCVRNSVQRMKRFNFGRVYSQTSANGHPHERWECCVDCIGPQCSSPSLEAELLLVACEMMIGSLPGMKFTLKIGHAQLIEAQIRHLKLSDDVRAELLDALHLISVSDRPHSHKEKMDMLTPKIGAKAANIITKLLIPVEDNFGAFKEKVACFRKKLKVDAARVLVDKAIRDLEEIVGTFKFCRTEAIEQISIVYDSQTCYRPRTFGDGLLFQIQVEKPSTIANNKRGRRQNVLAGGRYDSALLRERHPRDFVYEIPLCISGFGVAMDVVSQIRDSINKSANIPKTPQNHCKVLICSMVQPDGSNLITQKFELAKKLWSMGIEADVFHIPVDDLESLTEHRNRASITHILAVYNTLNEVICKTETSSETMDVDSAISSVWRGVQALDGQSIHMTPCGGGPISSISTPGEAHHHDDHHPGTPVIASKCFRSSVSTTVATTSIRPISATVANLNVILVTSADRFHKVMKEKKRVESQVRNHLTEFVAHFTSKTRIEVLVCDIPADVIKKIVSELTKTSSEAEIDKLFDQLIQKHGKVDLSPLRRQFHITLNGISTGSAQVAILFYRQSDNFYRYLV
2.7.11.1
null
cellular homeostasis [GO:0019725]; determination of adult lifespan [GO:0008340]; mitochondrial unfolded protein response [GO:0034514]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of nematode larval development [GO:0061063]; positive regulation of protein oxidation [GO:1904808]; positive regulation of protein phosphorylation [GO:0001934]; regulation of brood size [GO:0060378]; response to heat [GO:0009408]; response to hypoxia [GO:0001666]; response to sodium arsenite [GO:1903935]; response to starvation [GO:0042594]; response to UV [GO:0009411]; stress granule assembly [GO:0034063]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310]
PF00069;PF05773;PF13393;
1.10.510.10;3.10.110.10;
Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q19192}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q19192};
null
null
null
null
FUNCTION: Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis (By similarity). Involved in the unfolded protein response (UPR) triggered by several stresses including mitochondrial, osmotic and oxidative stresses, amino acid deprivation and UV irradiation, probably by phosphorylating and inhibiting eIF2alpha (PubMed:20733002, PubMed:22719267, PubMed:23076791, PubMed:23692540). In addition, leads to the selective translation/transcription of some mRNA including atf-5, pha-4 and gpdh-1 which are part of the UPR (PubMed:23076791, PubMed:23692540). Required for maintaining lifespan during amino acid starvation (PubMed:23692540). Involved in hypoxia-mediated adaptive protective response (PubMed:20733002). {ECO:0000250|UniProtKB:Q19192, ECO:0000269|PubMed:20733002, ECO:0000269|PubMed:22719267, ECO:0000269|PubMed:23076791, ECO:0000269|PubMed:23692540}.
Caenorhabditis elegans
D0ZKX9
RSEP_SALT1
MLSILWNLAAFIIALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRYGTEYVIALIPLGGYVKMLDERAEPVAPELRRHAFNNKTVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVIGEITPNSIAAQAQIAPGTELKAVDGIETPDWDAVRLQLVSKIGDQQTTVSVAPFGSDQRQDKTLDLRHWAFEPDKQDPVSSLGIRPRGPQIEPVLSEVQANSAASKAGLQAGDRIVKVDGQPLTQWMKFVTFVRDNPGKPLALEIERQGSALSLTLTPDTKSVNGKAEGFAGVVPKIIPLPEEYKTIRQYGPFSAILEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAQGAGMSAEFGVIYYLMFLALISVNLGIINLFPLPVLDGGHLLFLAIEKLKGGPVSERVQDFSYRIGSILLVLLMGLALFNDFSRL
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
cellular stress response to acid chemical [GO:0097533]; proteolysis [GO:0006508]; response to temperature stimulus [GO:0009266]
plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
PF17820;PF02163;
2.30.42.10;
Peptidase M50B family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: A site-2 regulated intramembrane protease that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. {ECO:0000269|PubMed:19170886}.
Salmonella typhimurium (strain 14028s / SGSC 2262)
D0ZPH9
SSPH2_SALT1
MPFHIGSGCLPATISNRRIYRIAWSDTPPEMSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVINRFELLRTLAYAGWEESIHSGQHGENYFCILDEDSQEILSVTLDDAGNYTVNCQGYSETHRLTLDTAQGEEGTGHAEGASGTFRTSFLPATTAPQTPAEYDAVWSAWRRAAPAEESRGRAAVVQKMRACLNNGNAVLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPALPSELCKLWAYNNQLTSLPMLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIVSGNRLTSLPVLPSELKELMVSGNRLTSLPMLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALREITSAPGYSGPIIRFDMAGASAPRETRALHLAAADWLVPAREGEPAPADRWHMFGQEDNADAFSLFLDRLSETENFIKDAGFKAQISSWLAQLAEDEALRANTFAMATEATSSCEDRVTFFLHQMKNVQLVHNAEKGQYDNDLAALVATGREMFRLGKLEQIAREKVRTLALVDEIEVWLAYQNKLKKSLGLTSVTSEMRFFDVSGVTVTDLQDAELQVKAAEKSEFREWILQWGPLHRVLERKAPERVNALREKQISDYEETYRMLSDTELRPSGLVGNTDAERTIGARAMESAKKTFLDGLRPLVEEMLGSYLNVQWRRN
2.3.2.27
null
protein secretion by the type III secretion system [GO:0030254]; protein ubiquitination [GO:0016567]
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
ubiquitin-protein transferase activity [GO:0004842]
PF14496;
1.20.58.90;3.80.10.10;3.30.2440.10;1.20.58.360;1.20.1270.130;
LRR-containing bacterial E3 ligase family
PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme UBA1, E2 ubiquitin-conjugating enzyme UBE2D2 and ubiquitin. {ECO:0000269|PubMed:19273841}.
SUBCELLULAR LOCATION: Secreted. Host cytoplasm. Host apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Secreted via type III secretion system 2 (SPI-2 T3SS), and delivered into the host cytoplasm. Localizes at the periphery of the host cell, specifically in areas of actin polymerization. Localizes to the apical membrane of polarized epithelial cells.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
null
null
null
FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Contributes to virulence in calves. {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:19273841}.
Salmonella typhimurium (strain 14028s / SGSC 2262)
D0ZV89
PHOQ_SALT1
MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE
2.7.13.3; 3.1.3.-
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16096064}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16096064}; Note=Binds up to 3 divalent cations (Ca(2+) or Mg(2+)); their binding site probably overlaps with that of cationic antimicrobial peptides that induce the operon. {ECO:0000269|PubMed:16096064};
null
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]
PF02518;PF08918;
1.10.287.130;3.30.450.140;3.30.565.10;
null
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
null
null
null
null
FUNCTION: Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance. {ECO:0000269|PubMed:10084994, ECO:0000269|PubMed:10775270, ECO:0000269|PubMed:14507376, ECO:0000269|PubMed:15948951, ECO:0000269|PubMed:8392513}.
Salmonella typhimurium (strain 14028s / SGSC 2262)
D0ZVG2
SSPH1_SALT1
MFNIRNTQPSVSMQAIAGAAAPEASPEEIVWEKIQVFFPQENYEEAQQCLAELCHPARGMLPDHISSQFARLKALTFPAWEENIQCNRDGINQFCILDAGSKEILSITLDDAGNYTVNCQGYSEAHDFIMDTEPGEECTEFAEGASGTSLRPATTVSQKAAEYDAVWSKWERDAPAGESPGRAAVVQEMRDCLNNGNPVLNVGASGLTTLPDRLPPHITTLVIPDNNLTSLPELPEGLRELEVSGNLQLTSLPSLPQGLQKLWAYNNWLASLPTLPPGLGDLAVSNNQLTSLPEMPPALRELRVSGNNLTSLPALPSGLQKLWAYNNRLTSLPEMSPGLQELDVSHNQLTRLPQSLTGLSSAARVYLDGNPLSVRTLQALRDIIGHSGIRIHFDMAGPSVPREARALHLAVADWLTSAREGEAAQADRWQAFGLEDNAAAFSLVLDRLRETENFKKDAGFKAQISSWLTQLAEDAALRAKTFAMATEATSTCEDRVTHALHQMNNVQLVHNAEKGEYDNNLQGLVSTGREMFRLATLEQIAREKAGTLALVDDVEVYLAFQNKLKESLELTSVTSEMRFFDVSGVTVSDLQAAELQVKTAENSGFSKWILQWGPLHSVLERKVPERFNALREKQISDYEDTYRKLYDEVLKSSGLVDDTDAERTIGVSAMDSAKKEFLDGLRALVDEVLGSYLTARWRLN
2.3.2.27
null
protein secretion by the type III secretion system [GO:0030254]; protein ubiquitination [GO:0016567]
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
ubiquitin-protein transferase activity [GO:0004842]
PF00560;PF14496;
1.20.58.90;3.80.10.10;3.30.2440.10;1.20.58.360;1.20.1270.130;
LRR-containing bacterial E3 ligase family
PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250|UniProtKB:D0ZPH9}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}. Host cytoplasm {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}. Host nucleus {ECO:0000269|PubMed:16611232}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS), and delivered into the host cytoplasm. Localizes predominantly to the host nucleus. {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18005683};
null
null
null
null
FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues (PubMed:10564523, PubMed:16611232, PubMed:18005683, PubMed:24248594). This protein is an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (PubMed:10564523, PubMed:16611232, PubMed:18005683, PubMed:24248594). Can ubiquitinate ubiquitin, giving rise to polyubiquitin chains (in vitro) (PubMed:18005683). Polyubiquitinates host PKN1, leading to its proteasomal degradation (PubMed:16611232, PubMed:24248594). Down-modulates production of host pro-inflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression; this depends only partially on its E3 ubiquitin-protein ligase activity (PubMed:12819095). {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:12819095, ECO:0000269|PubMed:16611232, ECO:0000269|PubMed:18005683, ECO:0000269|PubMed:24248594}.
Salmonella typhimurium (strain 14028s / SGSC 2262)