{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GR38","uniProtkbId":"A0A401GR38_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":28,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84184.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Pentafunctional AROM polypeptide"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.3.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.5.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"5-enolpyruvylshikimate-3-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSPS"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.1.10"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"1.1.1.25"}]}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84184.1"}],"value":"SCP_0601620"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054455"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-dehydroquinate = 3-dehydroshikimate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:32364"}],"ecNumber":"4.2.1.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21256"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57701"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:145989"}],"ecNumber":"2.5.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21968"},{"database":"ChEBI","id":"CHEBI:32364"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58394"}],"ecNumber":"4.2.3.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17737"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004811"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009948"}],"value":"Belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 2nd section; belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006477"}],"value":"In the 2nd section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 3rd section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 4th section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the C-terminal section; belongs to the shikimate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the N-terminal section; belongs to the dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009349"}],"value":"In the N-terminal section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84184.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Domain","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":852,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Domain","location":{"start":{"value":1333,"modifier":"EXACT"},"end":{"value":1414,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]},{"type":"Domain","location":{"start":{"value":1449,"modifier":"EXACT"},"end":{"value":1503,"modifier":"EXACT"}},"description":"Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01488"}]},{"type":"Domain","location":{"start":{"value":1581,"modifier":"EXACT"},"end":{"value":1610,"modifier":"EXACT"}},"description":"SDH C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18317"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Region","location":{"start":{"value":1328,"modifier":"EXACT"},"end":{"value":1616,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1217,"modifier":"EXACT"},"end":{"value":1217,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1245,"modifier":"EXACT"},"end":{"value":1245,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":890,"modifier":"EXACT"},"end":{"value":897,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84184.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000006","properties":[{"key":"ProteinId","value":"GBE84184.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027615097.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027759296.1"}]},{"database":"FunCoup","id":"A0A401GR38","properties":[{"key":"Number of interactors","value":"101"}]},{"database":"STRING","id":"139825.A0A401GR38","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38781101","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GR38","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"197068at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00053","properties":[{"key":"RectionId","value":"UER00085"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00502","properties":[{"key":"EntryName","value":"DHQase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08195","properties":[{"key":"EntryName","value":"DHQS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01556","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01065","properties":[{"key":"EntryName","value":"NAD_bind_Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1090.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000135","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001256","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00210","properties":[{"key":"EntryName","value":"EPSP_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03143","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00222","properties":[{"key":"EntryName","value":"Shikimate_DH_AroE"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR016037","properties":[{"key":"EntryName","value":"DHQ_synth_AroB"}]},{"database":"InterPro","id":"IPR030960","properties":[{"key":"EntryName","value":"DHQS/DOIS_N"}]},{"database":"InterPro","id":"IPR056179","properties":[{"key":"EntryName","value":"DHQS_C"}]},{"database":"InterPro","id":"IPR001381","properties":[{"key":"EntryName","value":"DHquinase_I"}]},{"database":"InterPro","id":"IPR001986","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_dom"}]},{"database":"InterPro","id":"IPR036968","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_sf"}]},{"database":"InterPro","id":"IPR006264","properties":[{"key":"EntryName","value":"EPSP_synthase"}]},{"database":"InterPro","id":"IPR023193","properties":[{"key":"EntryName","value":"EPSP_synthase_CS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008289","properties":[{"key":"EntryName","value":"Pentafunct_AroM"}]},{"database":"InterPro","id":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"InterPro","id":"IPR041121","properties":[{"key":"EntryName","value":"SDH_C"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR010110","properties":[{"key":"EntryName","value":"Shikimate_DH_AroM-type"}]},{"database":"InterPro","id":"IPR022893","properties":[{"key":"EntryName","value":"Shikimate_DH_fam"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"InterPro","id":"IPR023000","properties":[{"key":"EntryName","value":"Shikimate_kinase_CS"}]},{"database":"InterPro","id":"IPR006151","properties":[{"key":"EntryName","value":"Shikm_DH/Glu-tRNA_Rdtase"}]},{"database":"NCBIfam","id":"TIGR01356","properties":[{"key":"EntryName","value":"aroA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01357","properties":[{"key":"EntryName","value":"aroB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01093","properties":[{"key":"EntryName","value":"aroD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01809","properties":[{"key":"EntryName","value":"Shik-DH-AROM"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090","properties":[{"key":"EntryName","value":"AROM/DEHYDROQUINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090:SF5","properties":[{"key":"EntryName","value":"PENTAFUNCTIONAL AROM POLYPEPTIDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01761","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24621","properties":[{"key":"EntryName","value":"DHQS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01487","properties":[{"key":"EntryName","value":"DHquinase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18317","properties":[{"key":"EntryName","value":"SDH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01488","properties":[{"key":"EntryName","value":"Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08501","properties":[{"key":"EntryName","value":"Shikimate_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000514","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00104","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00885","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01128","properties":[{"key":"EntryName","value":"SHIKIMATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTTDVRKVSILGKESIHCGFHLVPYIVDTVLHTLTSSTYVLITDTNIANLHLEAFQAAFNSHKLSCKSRFLTYVIPPGETSKSREGKTEIEDYLLLNKCTRDTVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLLGAFWQPEYIFIDAAFLETLPGREFSNGMAEVVKTAAIWDENEFAALESRSADIFAAIQTPSANLSGRVQSTRSPAQELLLSVIAGSIGVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEAEVARQLGVLSQVAVGRLTRCLNAYNLPVSISDPRISSLPAATSLTVEKLLDIMKIDKKNSGPQKKIVILSRIGATYEPKATIVADKVIAKTLSEAVRIVPGVPTKSPIRMATPGSKSISNRALLLAALGKGTCRLKNLLHSDDTQVMMNALMELKGASFSWEDGGETLVVKGGEGSLSVPLRGREIYLANAGTAARFLTTVCTLAQSTQPDERTVITGNARMKQRPIGPLVDALRANGSDIAYVESLGCLPLSVAPAGLKGSTIQLAASVSSQYVSSILLCAPYALEPVILELTGGQVVSQPYIDMTIAMMKTFGVNVSREVDAATGQLLDVYTIPKGVYSNPSEYNIESDASSATYPLAIAAITGTSCTITNIGSASLQGDARFAKEVLEPMGCKVIQTETETTVEGPPIGQLRAIGFVDMEPMTDAFLTASVLAAVATQPPLEQRRLLDGSPSTTTRIVGIANQRVKECNRIQAMIDQLAKFGVETNELPDGLEIYGRAVGELSENASVHCYDDHRVAMAFSVLGTVIKDTTIEEKRSVEKTWPNWWDDLENKIGLEVEGVELPVSDSASSASRPTDADTLASVVIVGMRGSGKTFIGNLAASILGWNFVDADVAFEDRYQTGVRSFVLENGWPAFRAAETEILRELLSKHPKGHVISLGGGIVETPAAREALKAYAKEGPVVHIVREIDAVVKYLGEETARPAYGEPILDVFQRREPWFNECCSYVFVNYTGVLGAVNGDHIDILNGSGEIRSSRHEVARFFRHVTGQHPNLASNMAAGNRSYFLSLTYPDITPALPRIEELTVGVDAVELRVDLLRSPNDFGNVGPHKPSVAYVTDQIAALRQKTTLPVVFTVRTVSQGGQFPDHAEQEAFELFHTAVRLGIEYIDVEISWSERHIQDLIARKGHSQIIASWHDWSGNMRWSGKMVEAKYRVARGFGDIVKLVGKANSLEDNFELHDFVRRMRSLPEGKPIIALNMGIEGQMSRILNSTLSPVSHPLQLVKAAPGQLSFAEIQTALHLIGQLPAQRFFLFGNPIGHSMSPILHNTAFQLLGLPHTYELLETDNVGEEIKAALTSPDFGGASVTIPFKLDVIPLLDSLSQEAQAIGAVNTIIPRKTADGSLVLYGDNTDWIGIRDCIRAVLPASILKPETALIIGAGGTSRAAIYALHELGVNVIYLYNRTRNSAQVLVNTFPDVKIEIIDELGVWPGQDPPPTVIVSTVPATATTLNLSAQSGLYLPSTIFASPDGGVVVDMAYKPAETPLLALAANEGSHWKTVKGVQVLLEQGYVQFHLWTGRHCPRAAVAERVWETYTA","length":1616,"molWeight":174571,"crc64":"810D577F0D8C1C04","md5":"FD9065A8ADDE6BEA6CEC30C837FE727D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":9,"CAUTION":2},"countByFeatureType":{"Domain":6,"Region":2,"Active site":4,"Binding site":22},"uniParcId":"UPI000FE254B0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GTX9","uniProtkbId":"A0A401GTX9_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":27,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE85678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081752"}],"value":"Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013008"}],"value":"2.1.3.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012918"}],"value":"3.5.1.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044063"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012738"}],"value":"6.3.5.5"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE85678.1"}],"value":"SCP_0802000"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058513"}],"value":"Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20013"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:32814"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048859"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004852"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043998"}],"value":"In the 2nd section; belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043968"}],"value":"In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043979"}],"value":"In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043984"}],"value":"In the N-terminal section; belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE85678.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":599,"modifier":"EXACT"},"end":{"value":791,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1134,"modifier":"EXACT"},"end":{"value":1325,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1391,"modifier":"EXACT"},"end":{"value":1545,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Active site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE85678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000008","properties":[{"key":"ProteinId","value":"GBE85678.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027616591.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027760790.1"}]},{"database":"FunCoup","id":"A0A401GTX9","properties":[{"key":"Number of interactors","value":"546"}]},{"database":"STRING","id":"139825.A0A401GTX9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38782595","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GTX9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1924069at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004070","properties":[{"key":"GoTerm","value":"F:aspartate carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01423","properties":[{"key":"EntryName","value":"MGS_CPS_I_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000002","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000025","properties":[{"key":"EntryName","value":"Bifunctional pyrimidine biosynthesis protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000005","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000005","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000011","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000004","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase (glutamine-hydrolyzing)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase 1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000036","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR002082","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF5","properties":[{"key":"EntryName","value":"CAD PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSLTSPTKIDVSRPVLAHFTSNHPNGFLAPPIATSDSTSLEAVLELADGAAYRGISFGAEGKSVAGECVFQTGMVGYTESLTDPSYEGQILILTYPLIGNYGVPARPTSASVEAIPPDFESSRIHVAAVVVSSYSEEFSHFLAHTSLGVWLKESGIPALYGIDTRALTKKIREKGSILGKVLARQKDSPVDRRLSLMSPASLPASRTPSPGGNGIWREDYIDVPFRDPNQDNLVALVSVSSPHIYKPTVKARMHPSGKRPLRVLAVDVGMKFNQIRCFTHRGIELKVVPWDYDYLASAEEPFDGLFISNGPGDPTMVKPTIARLARAMQGEDRPIFGICLGHQLLALAAGASTSKMKYGNRGHNIPCTDTLSGRCYITSQNHGFQVDTATLPEGWHELFQNANDGSNEGIYCTDKPFFSVQFHPESTPGPRDTEFLFDVFIQNIVDCSTMGKVVPISMPGGMKEDNEKAAPRVNVQKVLVLGSGGLSIGQAGEFDYSGSQAIKALKQESIYTILVNPNIATIATSKGLADKVYFLPVTPEFVRKIIKYEKPDGIYVTFGGQTALNVGIKLKDEFEGLGCKVLGTPIDTIVTTEDRQLFASAMTEIGERCADSKTATTLDEAVAAANTIGFPVIVRAAYALGGLGSGFAKDGKQLKALCSKAFATSPQVLVEKSMKGWKEIEYEVVRDCRDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDADYNMLRTTAINVIRHLGVVGECNIQYALNPISREYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLGIPLNEIRNSVTKVTSACFEPSLDYVVVKIPRWDLKKFSRVSRLLSSSMKSVGEVMSIGRTFEETFQKAIRAIDDQFSGFAKNDFVEDIDEELLNPTDKRIFAIATAFYRGYSVDKIWQMTNIDKWFLTKLQSIHHMEVYLSSYNISSLGKDLLRQAKQLGFSDRQLAACIGSTELAVRRLRQEHGIAPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDITFEDRGVMVLGSGVYRIGSSVEFDWCAVRAIRTLRDNGLPTVMVNYNPETVSTDYDEADRLYFENISLETILDIYDTESSRGVIISMGGQTPNNIALPLYRQNVKIYGTSPEMIDTAENRFKFSRLLDEIGVDQPLWKELSNFDDAHTFCKKVGYPVLVRPSYVLSGAAMNVVFSQDDLSSYLSQATAVSREHPVVITKYIEGAKEIEMDAVAKDGKMIMHYISEHVENAGVHSGDATLIHPPQDLDPETVRQIEEATAKIGNALNVTGPFNIQFIAKNNEIKVIECNLRAARSFPFVSKVTGVDAIEMATKVMLGLPVEPYPHIPLPADYVGVKVPQFSFSRLSGADPVLGVEMASTGEVACFGRDKYEAYLKALISTGIVLPKKNILFSIGGFKEKLELLPSVQKLRAAGYSIFATSGTADFLTEHNVPCKYLETLGEDSEQKSEYSLTQHLANNLIDMYINLPSKNHYRRPASYASKGYRTRRMAVDFAVPLITNVKVAKLFFEALVRKMPLEVSPVDFRTSHETHTFPGLVNIAAFVPGLMQLNNNEIAGATKASLGGGFATVLVLPAGEKDKITDHTSLERVRKAIAGSSYCNYALNVTATATNTKSLDDEIEADVKFLYIPFHYNDADSQVSVVAAHFASWPADKPIVTDAKGSDLAPMLLLAGLHDRSLHIMNVQSKDDMLLISLSKAKQLKVTCDVSVYTLFFTREQFPGVTCLPTIEDQNMLWQNLDAIDTFSIGTVPYQLARELDKEGTVWSGIEEALPLLLTAVAAGRLTMDDIRQRLHDNPIRIFGLPDQSHAGVEIVVGRKSLFSNRGKVWSPLDGTMVNGGVHRVLVHGQTAFLDGEVTTGPVGRDISSATITHAPAERSMSISGPRPEFGVAMPLASKAADAAAQTQPVPATTTAAPFSTAVAPLQGPAAMLSHLLPHPAFHRRHILSVKQFTHKDVHDLFSLAHEMQLQVERNGTLDVLKGKVLCTLFYEPSTRTTSSFDTAMKRCGGEVVNVNVDMSSVLKGETLPDTIRTLGCYADAIVIRHPEIGSSQLAAKFSPVPILNAGDGVGEHPSQALLDVYTIRSELGTVNGRTITLLGDLKNGRTVHSLVTLLCLYSVRLNFVSPPSLAMPTSVVSAARRAGVHVRICESLEDVLGETDVLYVTRLQKERFKYEGAWQSVKDAYRIDHALLSRAKEEMIVMHPLPRVNEIDPDVDFDSRRAVYFRQMRYGLFIRMALLASVMG","length":2249,"molWeight":246450,"crc64":"1C9DFB3C9B7837F0","md5":"7677922A0DEDB1B248C53C678ECB96C0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":3,"Active site":3},"uniParcId":"UPI000FE193CC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G6Y0","uniProtkbId":"A0A401G6Y0_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77907.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77907.1"}],"value":"SCP_0107890"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77907.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":474,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":587,"modifier":"EXACT"},"end":{"value":609,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Region","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77907.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77907.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608820.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027753019.1"}]},{"database":"AlphaFoldDB","id":"A0A401G6Y0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"139825.A0A401G6Y0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774824","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G6Y0","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10255148at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF12","properties":[{"key":"EntryName","value":"TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00260)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MHSTRDHHDSAEADPLLVEAPEQEYEPPFPVRAFIVRALALLCACSLSVGSHYAQYILGPLKSRLSREMGTDNTEFSLLISAFSLNSTWTPLVGGILAGRLGTTYTSILATGVIFLGQTLLLIGNLASSVRLMTFGLFVFGLGVSPLAVVQETIIVRFFRSHGLGVSLALGLVAGKGASFIAARTSYPLSERFGPHAPFYMSTLLTAVSFAVNLVYLFASNWLVRGANAELEPSELRVEALRRKQAGAVESLSEAEALKKVAEKRKVSIRDMSKLGDVFWAYIGLNVLCGAIWAPFAHLAANIIERRFAMTELDASTTASYALSGSVILYPMTGCIVDHVKKRGIVVQLLMISSALTLLCYLWLALPPQWTKTPDPAIASFAIGHGFSPLLLVVIVLQLVPHKYISTTLGAHKALEQTGFVIFQTLAGVMLDLNKKKAVESAASDHGHDVQYLLNAFLVVNLAQLAGIFGLAHLERRQKEAAFRRANALLPPDVHSSDEEEAHDWLKVTDENRCRRGSRVSRSRSRGSIFGQRSDPPTSSSEQVVPLRRDPSLPPSHHRLSRSPIKSYSNGPVRAVRTKVEVRRGQICSVLCGVLICFAWVLFLSTAWLRLRSKEERASTTGFPTTS","length":627,"molWeight":68501,"crc64":"1D541C90FB8EBAB1","md5":"9C2D998BD1B1732D8C0D635A999068C1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":12,"Region":1,"Compositional bias":1},"uniParcId":"UPI000FE2778C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G8C9","uniProtkbId":"A0A401G8C9_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78436.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"ATP-dependent DNA helicase PIF1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"5.6.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA 5'-3' helicase PIF1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA repair and recombination helicase PIF1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"PIF1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78436.1"}],"value":"SCP_0113240"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Belongs to the helicase family. PIF1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78436.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"DNA binding","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":636,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]},{"type":"Region","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":530,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78436.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE78436.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401G8C9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"139825.A0A401G8C9","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G8C9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"432234at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18037","properties":[{"key":"EntryName","value":"DEXSc_Pif1_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18809","properties":[{"key":"EntryName","value":"SF1_C_RecD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.970.10","properties":[{"key":"EntryName","value":"Ribonuclease H1, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03176","properties":[{"key":"EntryName","value":"PIF1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR010285","properties":[{"key":"EntryName","value":"DNA_helicase_pif1-like_DEAD"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR051055","properties":[{"key":"EntryName","value":"PIF1_helicase"}]},{"database":"InterPro","id":"IPR048293","properties":[{"key":"EntryName","value":"PIF1_RRM3_pfh1"}]},{"database":"InterPro","id":"IPR009027","properties":[{"key":"EntryName","value":"Ribosomal_bL9/RNase_H1_N"}]},{"database":"InterPro","id":"IPR011320","properties":[{"key":"EntryName","value":"RNase_H1_N"}]},{"database":"InterPro","id":"IPR037056","properties":[{"key":"EntryName","value":"RNase_H1_N_sf"}]},{"database":"PANTHER","id":"PTHR47642","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47642:SF5","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01693","properties":[{"key":"EntryName","value":"Cauli_VI"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05970","properties":[{"key":"EntryName","value":"PIF1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55658","properties":[{"key":"EntryName","value":"L9 N-domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MPKANKMKYYAVRNGREGAKVYTTWEEAKENVSRYPGAVHKSFTSQTEAQRWLNVAAPLQRTYLEGPPKDWTPPPPQDPAAGPSRRSKSFNGQPNPGTAMNIPADSFLGNLPPALPQQPPEPKVALSSEQRAVLDMVQQGRSVFFTGSAGTGKSVLLREIIKFCTEHSGKRPAVTAATGIASVNIGGCTLHSWAGIGLGKEDAKVLVGKLLGKHKQLLKKDKEKGRQAEDDMDWYDETGTEKNSWSVNRWREVKTLIIDEISMIDGNLFDKLEYIARILRRNKAPFGGIQLVLSGDFCQLPPVPDRMNGVSKDIRFAFDAHSWEDCVGRPVILTHVFRQKDQAFVDMLNEMRFGRLSPKTITEFRKLSRDVEYDDGIEPTDLFPTRREVDNANDYRLANLSDPRHEYKARDVPGYDDNNAPISEKKMEAMLDRLIAPKAVTLKVIFHPFAPNIQLTYIRKQVGAQVMLIKNLIQGELVNGSVGRVVAFSKVKDAINGGALVAHDQGVSGGGSSLPIPGGSMMAGGSTSSGDRNKDQGKIPEHILLSNDVWPVVKFQKGLMVVCIPTAFEQTNAIGTMEAMREQVPLILAWALSIHKSQGQTLERVRVDLGRIFEKGQAYVALSRATSMQALQVLKFDPGKVMAHPRVLEWTRQVTAKRGVIEDDMEFETNLDDDLEFWADYL","length":682,"molWeight":75763,"crc64":"E6AD60F6A81FB315","md5":"95D7D7D17E6F496E351A013CC3C90D37"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"DNA binding":1,"Region":2,"Compositional bias":3,"Binding site":1},"uniParcId":"UPI000FE215FD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G9S8","uniProtkbId":"A0A401G9S8_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78918.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039850"}],"value":"Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039036"}],"value":"1.3.8.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042821"}],"value":"2-methyl branched chain acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041537"}],"value":"2-methylbutyryl-coenzyme A dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78918.1"}],"value":"SCP_0201150"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094237"}],"value":"Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the proR-proR stereospecific alpha,beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA). Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (butanoyl-CoA). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway. Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = ethylacryloyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156439"},{"database":"ChEBI","id":"CHEBI:156440"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65297"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48256"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:88166"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:48257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43780"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57336"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"ecNumber":"1.3.8.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43781"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = 2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44180"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62500"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:44181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:47197"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24005"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43465"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"valproyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65344"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156457"},{"database":"ChEBI","id":"CHEBI:156458"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65345"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037895"}],"value":"Amino-acid degradation; L-isoleucine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005198"}],"value":"Lipid metabolism; mitochondrial fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78918.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE78918.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000002","properties":[{"key":"ProteinId","value":"GBE78918.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027609831.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027754030.1"}]},{"database":"AlphaFoldDB","id":"A0A401G9S8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"139825.A0A401G9S8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38775835","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G9S8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10262177at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003853","properties":[{"key":"GoTerm","value":"F:short-chain 2-methyl fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046395","properties":[{"key":"GoTerm","value":"P:carboxylic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006631","properties":[{"key":"GoTerm","value":"P:fatty acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01158","properties":[{"key":"EntryName","value":"SCAD_SBCAD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.540.10:FF:000012","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.10:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006089","properties":[{"key":"EntryName","value":"Acyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR43884","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43884:SF1","properties":[{"key":"EntryName","value":"SHORT_BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016578","properties":[{"key":"EntryName","value":"HsaA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00072","properties":[{"key":"EntryName","value":"ACYL_COA_DH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00073","properties":[{"key":"EntryName","value":"ACYL_COA_DH_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLRTAARVIKPSASRLRSAALASNVSSSRSFSCSHARASEGVLNSLDTFTEEEQMLRESVARFAQEVIAPKVRDMDEAELMDPSVIKGLFEQGLMGIETSADYGGAESSFTSAIIAIEELAKVDPSVSVLCDVHNTLVNTIFRKYGTKEQKDKYLPELAESKVGSFCLSEPASGSDAFALQTRARKDGDHWVINGTKMWITNSYEADIFLIFANVDPSKGYKGITCFVANKDMGIQIAKKEQKLGIRASSTCSLSFDDLRIPAENVIGGEGKGYKIAIEILNEGRIGIAAQMLGLAQGAFDKAVPYTYQRSQFGQPVGTFQGMAFQQAEAAIEIEAARLLTYNAARRKEEGRSFVREAAIAKYYASQVAQHVSGAAIEWAGGVGFTRETGIEKYWRDSKIGAIYEGTSNIQLQTIAKFIQKQYS","length":424,"molWeight":46300,"crc64":"DE6DD0B1DD3410CA","md5":"377BF116FF0950CA5E430572E17280AD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI000FE22F74"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GEQ3","uniProtkbId":"A0A401GEQ3_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE80674.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"histone acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE80674.1"}],"value":"SCP_0303930"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045805"}],"value":"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. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. 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. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. 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"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011353"}],"value":"Component of the NuA4 histone acetyltransferase complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004286"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE80674.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022454"}],"id":"KW-0158","category":"Cellular component","name":"Chromosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE80674.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000003","properties":[{"key":"ProteinId","value":"GBE80674.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027611587.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027755786.1"}]},{"database":"AlphaFoldDB","id":"A0A401GEQ3","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401GEQ3","properties":[{"key":"Number of interactors","value":"737"}]},{"database":"STRING","id":"139825.A0A401GEQ3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38777591","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GEQ3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"787137at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000785","properties":[{"key":"GoTerm","value":"C:chromatin"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004402","properties":[{"key":"GoTerm","value":"F:histone acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0106226","properties":[{"key":"GoTerm","value":"F:peptide 2-hydroxyisobutyryltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0140064","properties":[{"key":"GoTerm","value":"F:peptide crotonyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04301","properties":[{"key":"EntryName","value":"NAT_SF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000022","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000002","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR025995","properties":[{"key":"EntryName","value":"Tudor-knot"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF218","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE ESA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11717","properties":[{"key":"EntryName","value":"Tudor-knot"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAPHTPAKDEAPQEPPPITPGGTYSIQTVSVGCKIYIRRQNPDGEEERLAEILSIRDKPVNPYAARLQGGVKQEEAQRPEDRLEFFVHWDQFNKRLDEWVSGSRLVLSKDLEWPRPKLPPATKKYVGKKTPARAQSLLKKAATTNALAVAGSKVDFGTPAPSAPSTPSARASPSPAPSGSLKRKFPQDEEEEDEDLDADADGEMDVDAEGEVMEIDETPTPLPPPPPSAFSKEQEIEKLRTSGSMTQSISEIARVKNLNRLQIGRHEVESWYFSPYPQEYAHLPVLYICEFCLSYFASPFMLSRHRKRCNLLHPPGNEIYRYEDISVFELDGKRQLTWCRNLSLLSKCFLDHKTLYYDVTPFLYYVMCHRDSSGCHIIGYFSKEKESADNYNVACILTLPQHQRHGYGKLLMEFSYELSKKEGKLGSPEKPLSDLGLLSYRAFWAETIIELLLNTNDDISIDEIAQKTSITHADVMNTCTTLQLFKHYKGQHVISIPEAVQERYKKGIAKRKRRIHADQLTAWKPPVFTRDQLRFGW","length":537,"molWeight":61074,"crc64":"4052A34655E42AE6","md5":"62100BC7EF60FFEC74AA5E72B2E4AAC9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":3,"Active site":1,"Binding site":1,"Modified residue":1},"uniParcId":"UPI000FE20AE8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GIV1","uniProtkbId":"A0A401GIV1_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE82053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068518"}],"value":"Glutamate synthase [NADH]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012079"}],"value":"1.4.1.13"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024383"}],"value":"1.4.1.14"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE82053.1"}],"value":"SCP_0404310"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057049"}],"value":"Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13753"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"1.4.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048867"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15501"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"1.4.1.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048151"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001917"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"[3Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:21137"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"value":"Binds 1 [3Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004944"}],"value":"Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004802"}],"value":"Energy metabolism; nitrogen metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004909"}],"value":"Nitrogen metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011233"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009716"}],"value":"Belongs to the glutamate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE82053.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51278"}]},{"type":"Domain","location":{"start":{"value":1666,"modifier":"EXACT"},"end":{"value":1699,"modifier":"EXACT"}},"description":"4Fe-4S ferredoxin-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51379"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1589,"modifier":"EXACT"},"end":{"value":1614,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-1"}]},{"type":"Active site","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}]},{"type":"Binding site","location":{"start":{"value":1181,"modifier":"EXACT"},"end":{"value":1181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:21137"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"ligand":{"name":"[3Fe-4S] cluster","id":"ChEBI:CHEBI:21137"}},{"type":"Binding site","location":{"start":{"value":1187,"modifier":"EXACT"},"end":{"value":1187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:21137"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"ligand":{"name":"[3Fe-4S] cluster","id":"ChEBI:CHEBI:21137"}},{"type":"Binding site","location":{"start":{"value":1192,"modifier":"EXACT"},"end":{"value":1192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:21137"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"ligand":{"name":"[3Fe-4S] cluster","id":"ChEBI:CHEBI:21137"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023291"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"id":"KW-0003","category":"Ligand","name":"3Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023164"}],"id":"KW-0314","category":"Biological process","name":"Glutamate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE82053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000004","properties":[{"key":"ProteinId","value":"GBE82053.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027612966.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027757165.1"}]},{"database":"FunCoup","id":"A0A401GIV1","properties":[{"key":"Number of interactors","value":"169"}]},{"database":"STRING","id":"139825.A0A401GIV1","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38778970","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GIV1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4327079at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00045","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00634","properties":[{"key":"RectionId","value":"UER00690"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016040","properties":[{"key":"GoTerm","value":"F:glutamate synthase (NADH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004355","properties":[{"key":"GoTerm","value":"F:glutamate synthase (NADPH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051536","properties":[{"key":"GoTerm","value":"F:iron-sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016639","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019676","properties":[{"key":"GoTerm","value":"P:ammonia assimilation cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0097054","properties":[{"key":"GoTerm","value":"P:L-glutamate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd00982","properties":[{"key":"EntryName","value":"gltB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00713","properties":[{"key":"EntryName","value":"GltS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02808","properties":[{"key":"EntryName","value":"GltS_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1060.10:FF:000006","properties":[{"key":"EntryName","value":"Glutamate synthase (NADPH/NADH)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000031","properties":[{"key":"EntryName","value":"Glutamate synthase 1 [NADH]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000017","properties":[{"key":"EntryName","value":"Glutamate synthase [NADH], amyloplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000113","properties":[{"key":"EntryName","value":"Glutamate synthase [NADH], amyloplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.50.60:FF:000022","properties":[{"key":"EntryName","value":"Glutamate synthase [NADH], amyloplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.160.20.60:FF:000001","properties":[{"key":"EntryName","value":"Glutamate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.20.10:FF:000001","properties":[{"key":"EntryName","value":"Glutamate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1060.10","properties":[{"key":"EntryName","value":"Alpha-helical ferredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.160.20.60","properties":[{"key":"EntryName","value":"Glutamate synthase, alpha subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.20.10","properties":[{"key":"EntryName","value":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017896","properties":[{"key":"EntryName","value":"4Fe4S_Fe-S-bd"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR028261","properties":[{"key":"EntryName","value":"DPD_II"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR023753","properties":[{"key":"EntryName","value":"FAD/NAD-binding_dom"}]},{"database":"InterPro","id":"IPR017932","properties":[{"key":"EntryName","value":"GATase_2_dom"}]},{"database":"InterPro","id":"IPR002489","properties":[{"key":"EntryName","value":"Glu_synth_asu_C"}]},{"database":"InterPro","id":"IPR036485","properties":[{"key":"EntryName","value":"Glu_synth_asu_C_sf"}]},{"database":"InterPro","id":"IPR006982","properties":[{"key":"EntryName","value":"Glu_synth_centr_N"}]},{"database":"InterPro","id":"IPR012220","properties":[{"key":"EntryName","value":"Glu_synth_euk"}]},{"database":"InterPro","id":"IPR002932","properties":[{"key":"EntryName","value":"Glu_synthdom"}]},{"database":"InterPro","id":"IPR006005","properties":[{"key":"EntryName","value":"Glut_synth_ssu1"}]},{"database":"InterPro","id":"IPR051394","properties":[{"key":"EntryName","value":"Glutamate_Synthase"}]},{"database":"InterPro","id":"IPR009051","properties":[{"key":"EntryName","value":"Helical_ferredxn"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"NCBIfam","id":"NF008730","properties":[{"key":"EntryName","value":"gltB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01317","properties":[{"key":"EntryName","value":"GOGAT_sm_gam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43100","properties":[{"key":"EntryName","value":"GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43100:SF1","properties":[{"key":"EntryName","value":"GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14691","properties":[{"key":"EntryName","value":"Fer4_20"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00310","properties":[{"key":"EntryName","value":"GATase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04898","properties":[{"key":"EntryName","value":"Glu_syn_central"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01645","properties":[{"key":"EntryName","value":"Glu_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01493","properties":[{"key":"EntryName","value":"GXGXG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07992","properties":[{"key":"EntryName","value":"Pyr_redox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000187","properties":[{"key":"EntryName","value":"GOGAT"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00419","properties":[{"key":"EntryName","value":"ADXRDTASE"}]},{"database":"SUPFAM","id":"SSF69336","properties":[{"key":"EntryName","value":"Alpha subunit of glutamate synthase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46548","properties":[{"key":"EntryName","value":"alpha-helical ferredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51971","properties":[{"key":"EntryName","value":"Nucleotide-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51379","properties":[{"key":"EntryName","value":"4FE4S_FER_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51278","properties":[{"key":"EntryName","value":"GATASE_TYPE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAIADSATISPATSAENNTQNGFHAVQRDPNSWDSTLPASQGLYDNSYEKDSCGVGFICHIKGEQSHKIVSDARQLLCAMTHRGATGADSRDGDGAGVMTGIPHLFFKREAERDLGCELPDVGRYAVGNVFFKANDPVGLQKQQSVFSKIAGELGLRVLGWREVPTDGTILGPAAASKEPAILQPFVVLRSHYGDGATCRGGPFDATHFESQLYVLRKHATHSITLSKGFYVCSLSSKNIVYKGQLSPPQVYNYYHDLNHVLYCSHFTLVHSRFSTNTFPSWDRAQPMRWAAHNGEINTIRGNKNWMRAREGVLSSTLFGEQLDLLYPIIESGGSDSAAFDNVLELLVVNGVLTLPEAIMMLIPEAWQGNENMEPGKRAFYNWAACLQEPWDGPALFAFSDGRYCGANLDRNGLRPCRYVVSNEDIIVCASEVGAVYIPPEKVISKGRLKPGRMLLVDTEEGRIVDDKELKRNTANKQNFASWIETHVLHVPNIVKRVKRVHPIEIDVDDYTLSTDPKLLAFGYTVEQLNLLILPMVTEGKEALGSMGNDAPLACISTQPRVIYDYFRQLFAQVTNPPIDPIREDIVMSLNAYVGPEGNLLEMKPEQCHRILLHSPILTVEEMNAMKNLKYAYSSWPSQTIDITFPKEQGLPGYRLALERVCSEATQAIDDGMKVIILSDRQTGPNRVPLSALVACGGVHHHLVSQKKRAKVAMMIETGEAREVHHLCVLLGYGADAICPWLAIEVIHKVEREGLVKNNKTFEDLLHNYRHSVDNGILKVMSKMGISTLQSYKGAQIFEALGLHTEIIESCFTGTASRVQGATFDLLAMDAFEMHERGWPSRETIIPPGMPESGEYHWRSGGEAHINDPTAIAHLQDAVREKNQRAYDAYAKNSNDQTRAVQLRGLLDFRYESATPIPIEQVEPWNEIVRRFVTGAMSYGSISMEAHSTLAIAMNRLGGKSNTGEGGEDAERSQLLPNGDSMRSAIKQVASGRFGVTSNYLADADELQIKMAQGAKPGEGGELPGHKVSGSIARTRHSTAGVGLISPPPHHDIYSIEDLKQLIYDLKCSNPRARVSVKLVSEVGVGIVASGVAKAKADHILISGHDGGTGASRWTGIKNAGLPWELGLAETHQTLVLNDLRGRVTVQTDGQVRTGRDVAIACLLGAEEWGFATTPLIAMGCIMMRKCHLNTCPVGIATQDPQLRAKFAGQPEQVINFFYYIAEDLRSYMAKLGFRTINEMVGRADMLKVDEKLRTRKTAHLDLSAILKPAWQMRPGAATYRVRAQDHKLYIRLDNKFIDESEPALTKGLPVHIDCDVTNTDRALGTSLSYKVSKLYGEEGLPKDTIHISMRGSAGQSLGAFLAPGITIELEGDANDYVGKGLSGGRLIVYPPKASTFKAEENIIVGNVCLYGATSGEAFVRGVAAERFAVRNSGAFAVVEGTGDHGCEYMTGGRVVVLGSTGRNFAAGMSGGIAYVLDTAHTFASKVNLEMVELGKVTDPREIAELRGLIEDHRHYTGSEVADRVLHDFHHLLPLFVRVMPGDYKRVLEEQAAKLKEEKLRQNVIDLVPSRTASQVDLASEGLEDILLPKEPPSWHGSRSTSRGRLEPSVTDMEDSLVDDATTKQRLNKLDKTRGFMKYKRLTEAYRPPRKRVKDWKEISTRLTEGELKYQSARCMDCGVPFCQSDTGCPVSNIIPKWNDLVFKDQWQDALNRLLLTNNFPEFTGRVCPAPCEGACVLGINEQPVGIKSIECAIIDKGFEMGWMAPNPPKIRTGRKIAIVGSGPSGLACADQLNKAGHSVTVYDRNDRMGGLLMYGIPNMKLDKAVVQRRLDLMTAEGVTFVPNVHVGKDLDVNDLRAENDAVVICTGATWPRDLKIPNREVDGIHFAMEYLQLNTKSLLDSELQNGNYINAKGKDVIVIGGGDTGNDCIGTSMRHGAKSVTNFELLPKPPAGRGRDNPWPQWPRIFRTDYGHTEVAAHFGNDPREYCISTKDFVIDEEGKLMGLNTVRVEWTKDSGGRWKMEEVPGSEKFFPAQLVFLALGFLGPESEAIKALGVKQDARSNIQTPNKQYSTNVEGVFAAGDCRRGQSLIVWGINEGRGAAAEVDAWLSGGKTRLPADGGIKQRVFIPPASTLTSDTQVVEVEA","length":2145,"molWeight":235692,"crc64":"1B24003256FD9B63","md5":"6D20331AEDC9898C37C1A63B2F11DA7A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Compositional bias":1,"Active site":2,"Binding site":3},"uniParcId":"UPI000FE1DA04"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GRN2","uniProtkbId":"A0A401GRN2_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":32,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84888.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"protein kinase C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"2.7.11.13"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84888.1"}],"value":"SCP_0700680"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047470"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047272"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005490"}],"value":"Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84888.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"REM-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51860"}]},{"type":"Domain","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":587,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":789,"modifier":"EXACT"},"end":{"value":1048,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Domain","location":{"start":{"value":1049,"modifier":"EXACT"},"end":{"value":1116,"modifier":"EXACT"}},"description":"AGC-kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51285"}]},{"type":"Zinc finger","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Zinc finger","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":587,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Region","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":608,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":651,"modifier":"EXACT"},"end":{"value":683,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":747,"modifier":"EXACT"},"end":{"value":776,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":625,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":666,"modifier":"EXACT"},"end":{"value":677,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":914,"modifier":"EXACT"},"end":{"value":914,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":818,"modifier":"EXACT"},"end":{"value":818,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":1090,"modifier":"EXACT"},"end":{"value":1090,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]},{"type":"Modified residue","location":{"start":{"value":1108,"modifier":"EXACT"},"end":{"value":1108,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01207"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022527"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE84888.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000007","properties":[{"key":"ProteinId","value":"GBE84888.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027615801.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027760000.1"}]},{"database":"AlphaFoldDB","id":"A0A401GRN2","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401GRN2","properties":[{"key":"Number of interactors","value":"186"}]},{"database":"STRING","id":"139825.A0A401GRN2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38781805","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GRN2","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"63267at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019992","properties":[{"key":"GoTerm","value":"F:diacylglycerol binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004697","properties":[{"key":"GoTerm","value":"F:diacylglycerol-dependent serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0106310","properties":[{"key":"GoTerm","value":"F:protein serine kinase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0009272","properties":[{"key":"GoTerm","value":"P:fungal-type cell wall biogenesis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007165","properties":[{"key":"GoTerm","value":"P:signal transduction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd20822","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd20823","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08689","properties":[{"key":"EntryName","value":"C2_fungal_Pkc1p"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd11620","properties":[{"key":"EntryName","value":"HR1_PKC-like_2_fungi"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05570","properties":[{"key":"EntryName","value":"STKc_PKC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.160:FF:000004","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000101","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000103","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.20:FF:000014","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.20:FF:000034","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.160","properties":[{"key":"EntryName","value":"HR1 repeat"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.510.10","properties":[{"key":"EntryName","value":"Transferase(Phosphotransferase) domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000961","properties":[{"key":"EntryName","value":"AGC-kinase_C"}]},{"database":"InterPro","id":"IPR046349","properties":[{"key":"EntryName","value":"C1-like_sf"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR037778","properties":[{"key":"EntryName","value":"C2_fungal_PKC"}]},{"database":"InterPro","id":"IPR011072","properties":[{"key":"EntryName","value":"HR1_rho-bd"}]},{"database":"InterPro","id":"IPR036274","properties":[{"key":"EntryName","value":"HR1_rpt_sf"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR037312","properties":[{"key":"EntryName","value":"PKC-like_HR1"}]},{"database":"InterPro","id":"IPR002219","properties":[{"key":"EntryName","value":"PKC_DAG/PE"}]},{"database":"InterPro","id":"IPR017892","properties":[{"key":"EntryName","value":"Pkinase_C"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"InterPro","id":"IPR017441","properties":[{"key":"EntryName","value":"Protein_kinase_ATP_BS"}]},{"database":"InterPro","id":"IPR008271","properties":[{"key":"EntryName","value":"Ser/Thr_kinase_AS"}]},{"database":"PANTHER","id":"PTHR24351","properties":[{"key":"EntryName","value":"RIBOSOMAL PROTEIN S6 KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00130","properties":[{"key":"EntryName","value":"C1_1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02185","properties":[{"key":"EntryName","value":"HR1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00433","properties":[{"key":"EntryName","value":"Pkinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00109","properties":[{"key":"EntryName","value":"C1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00742","properties":[{"key":"EntryName","value":"Hr1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00133","properties":[{"key":"EntryName","value":"S_TK_X"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57889","properties":[{"key":"EntryName","value":"Cysteine-rich domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF46585","properties":[{"key":"EntryName","value":"HR1 repeat"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51285","properties":[{"key":"EntryName","value":"AGC_KINASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51860","properties":[{"key":"EntryName","value":"REM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00479","properties":[{"key":"EntryName","value":"ZF_DAG_PE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50081","properties":[{"key":"EntryName","value":"ZF_DAG_PE_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MAHELDQKIQDVYKRIQTERKVLEASHLLRQATTNPDVLRRNDAKIREAERSLSYFEDTLRELQSRKMMQAQRDDHSRSGSPVLSTASGRGGRSSDSPRMHQPTLSDVSSGRGARNPQGSAGSADDIPGVPKAKTYTKLDLIKADTPHTTAKISRMLHQLEFKLLVEKQYKSGIDKMAKLYQADGDKKSRADAESKKVESERKIQLLQSALKRYKNLHILDDAEDDDDDAGGVPGAPGIDGERKDNLRSKNLSGKLQVTLKGARELDHAPIVTGRSRSASKQVETYVSLKVEGTERARSHPTRTDRWLEDFEITIEKANEVEIAVYDKQSNETHPTPIGLLWIKISDLVDAQRRQKVMMENGQGGWVTAGAMNGDGSAISMQAQTGNVGDMNAPIGFGDNRVVPPGSGMPPVGQSEGIDAWFAVEPAGALALHLNFIKENVRKRPLDTPGGLGRQGAVRKRKDEVHEMNGHKFVQRQFYQIILCAFCNEFLLNAVGYQCEDCRYTCHRKCYEKVVTKCISKSNTGEDDAEKINHRIPHRFEPITNIGANWCCHCGYMLPLGRKNARRCTECDITCHANCAHLVPDFCGMSMETANQLLRDWRDINRARGAKSTAQARPIAHYQQPPRPPMPPPEPQVDHIITDVERVKLGEPAVPPKGADYPYGRQQVQSPQETTPPDQRMVQPPLPVTGAYAPPQPRPLPGGRIPLVPAFPSETLQQQVPSGRPGSMLYEDSYAYQKTVQQAVPPKDYAPPPSPGRAIQPERQASLAPSIQQQYRPPAHKRKVGLDDFNFLAVLGKGNFGKVMLAEEKKTSSLYAIKVLKKEFIIDNDEVESTRSEKRVFLAAARERHPFLLGLHSCFQTETRVYFVMEYVSGGDLMLHIQRRQFSLRQAKFYACEVLLALEYFHANGIVYRDLKLDNILLTLDGHVKVADYGLCKEDMYYDKTTSTFCGTPEFMAPEILLEQRYGRAVDWWAFGVLMYEMLLGQSPFRGDDEDEIFDAILEDEPLYPITMPRDAVSILQKLLTRDPKRRLGSTEADAEEIKRHAFFKDVSFDDVVNKRIPPPYFPTVNGTADTSNFDEEFTKEQPTLTPVHAQLSSRDQAEFNGFSWVATWAEI","length":1116,"molWeight":125339,"crc64":"F1910DEE433D2FF4","md5":"E6C6A45F66E863825858EF17F065460B"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":4,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":6,"Zinc finger":2,"Region":5,"Coiled coil":1,"Compositional bias":2,"Active site":1,"Binding site":1,"Modified residue":2},"uniParcId":"UPI000FE1EECB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GVM6","uniProtkbId":"A0A401GVM6_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86278.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Arginine biosynthesis bifunctional protein ArgJ, mitochondrial"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Glutamate N-acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"GAT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"2.3.1.35"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Ornithine acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"OATase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Ornithine transacetylase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Amino-acid acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"2.3.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"N-acetylglutamate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"AGS"}]}]}],"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Arginine biosynthesis bifunctional protein ArgJ alpha chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Arginine biosynthesis bifunctional protein ArgJ beta chain"}}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86278.1"}],"value":"SCP_0901570"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24292"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"}],"ecNumber":"2.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15349"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:46911"},{"database":"ChEBI","id":"CHEBI:57805"}],"ecNumber":"2.3.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Heterodimer of an alpha and a beta chain"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006774"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"value":"Belongs to the ArgJ family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86278.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Arginine biosynthesis bifunctional protein ArgJ alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"featureId":"PRO_5023269991"},{"type":"Chain","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"Arginine biosynthesis bifunctional protein ArgJ beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"featureId":"PRO_5023269992"},{"type":"Region","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}]},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":476,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}]},{"type":"Site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}]},{"type":"Site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Cleavage; by autolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022813"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0068","category":"PTM","name":"Autocatalytic cleavage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03124"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86278.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000009","properties":[{"key":"ProteinId","value":"GBE86278.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027617191.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027761390.1"}]},{"database":"AlphaFoldDB","id":"A0A401GVM6","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401GVM6","properties":[{"key":"Number of interactors","value":"166"}]},{"database":"STRING","id":"139825.A0A401GVM6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38783195","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GVM6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"2017946at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00106"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004042","properties":[{"key":"GoTerm","value":"F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004358","properties":[{"key":"GoTerm","value":"F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006592","properties":[{"key":"GoTerm","value":"P:L-ornithine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02152","properties":[{"key":"EntryName","value":"OAT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.340:FF:000002","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.2330.10:FF:000001","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.2330.10","properties":[{"key":"EntryName","value":"arginine biosynthesis bifunctional protein suprefamily"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.340","properties":[{"key":"EntryName","value":"ArgJ beta chain, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.70.12","properties":[{"key":"EntryName","value":"L-amino peptidase D-ALA esterase/amidase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01106","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002813","properties":[{"key":"EntryName","value":"Arg_biosynth_ArgJ"}]},{"database":"InterPro","id":"IPR016117","properties":[{"key":"EntryName","value":"ArgJ-like_dom_sf"}]},{"database":"InterPro","id":"IPR042195","properties":[{"key":"EntryName","value":"ArgJ_beta_C"}]},{"database":"PANTHER","id":"PTHR23100","properties":[{"key":"EntryName","value":"ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23100:SF0","properties":[{"key":"EntryName","value":"ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01960","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56266","properties":[{"key":"EntryName","value":"DmpA/ArgJ-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFPVRLPSIWKRFTSTIISRTPPPKAHHHAAIPDSVFPAGYVVTGLHCGIKKNPEQLDLALIQSISPQPAAAAACFTRNAFKAAPVVVSEAVLRRGDGRVRAIVINSGCANAVTGKQGTEDAWAMVRATDALDEEHAGDGATVVMSTGVIGQTLPIAKVLAGIQSQALSTPTRNLGSTFEAWERAARAFMTTDTFPKLRARNFIVGGREYHMAGMDKGAGMIHPDMGPPRVASTPAGSPSPSSPSSSSPAGQLHATLLGCILTDAPVSPRSLQSALTYAVDRSFNSISVDGDMSTNDTIIALANGAAAADAHEIDEEHNRGEYEAFRDELTAFAAELAQLVVRDGEGATKFVTVSVEGAATYADAHNVASRISTSALVKTALYGEDANWGRILAATGSVPLSVPLDPARVTVSFVPADGSAPLPLLVNGEPENVDEVRAKEIVSAEDLQIKVELGLGFEAAKYWTCDLSYEYVRINGDYRS","length":481,"molWeight":50748,"crc64":"A76D93A36CABAF39","md5":"6142ED1C757B71EC4279A06A70B6AE20"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":6,"Site":3},"uniParcId":"UPI000FE24577"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401GW87","uniProtkbId":"A0A401GW87_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86460.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Ubiquinone biosynthesis O-methyltransferase, mitochondrial"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"3-demethylubiquinol 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.64"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"3-demethylubiquinone 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Polyprenyldihydroxybenzoate methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.114"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"COQ3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86460.1"}],"value":"SCP_0903390"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"O-methyltransferase required for two non-consecutive steps during ubiquinone biosynthesis. Catalyzes the 2 O-methylation of 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoic acid into 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoic acid. Also catalyzes the last step of ubiquinone biosynthesis by mediating methylation of 3-demethylubiquinone into ubiquinone. Also able to mediate the methylation of 3-demethylubiquinol into ubiquinol"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoate + S-adenosyl-L-methionine = a 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoate + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44452"},{"database":"Rhea","id":"RHEA-COMP:10930"},{"database":"Rhea","id":"RHEA-COMP:10931"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64694"},{"database":"ChEBI","id":"CHEBI:84443"}],"ecNumber":"2.1.1.114","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44380"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"Rhea","id":"RHEA-COMP:10914"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:84422"}],"ecNumber":"2.1.1.64","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinone + S-adenosyl-L-methionine = a ubiquinone + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:81215"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:19654"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:231825"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Cofactor biosynthesis; ubiquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Matrix side","id":"SL-9913"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86460.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86460.1"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022688"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0831","category":"Biological process","name":"Ubiquinone biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE86460.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000009","properties":[{"key":"ProteinId","value":"GBE86460.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401GW87","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401GW87","properties":[{"key":"Number of interactors","value":"280"}]},{"database":"STRING","id":"139825.A0A401GW87","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401GW87","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"3265906at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00232","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031314","properties":[{"key":"GoTerm","value":"C:extrinsic component of mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0061542","properties":[{"key":"GoTerm","value":"F:3-demethylubiquinol 3-O-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0120537","properties":[{"key":"GoTerm","value":"F:3-demethylubiquinone 3-O-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0010420","properties":[{"key":"GoTerm","value":"F:polyprenyldihydroxybenzoate methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00472","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR010233","properties":[{"key":"EntryName","value":"UbiG_MeTrfase"}]},{"database":"NCBIfam","id":"TIGR01983","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464","properties":[{"key":"EntryName","value":"METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464:SF19","properties":[{"key":"EntryName","value":"UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13489","properties":[{"key":"EntryName","value":"Methyltransf_23"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRQLKLNIHSPSRRCCPRSSPHRVRNIHPARFFSSTPSASTSLAPQLSPESSVNPDEIAHFSRLSSLWWDERGEFYFLHKMNPVRMQFIREKLVEMSHEDDIELSDATNILNGLDVLDVGCGGGLLSESLARLGASTLGIDASPSNIAIASLHASADPQFVASPVSHPHHRRLAYEHISIEELLARRGPKQFDVVCSMEVLEHVDNPSAFLRDCAQLVKPGGHLFLSTISRSPLAYLLTIFAAEHVLGLIAKGTHTYSKFVRPEELLAFFQKHRSPLTPTAPIVEAAGTLGCPWISRLYGGVPARTEAETRGVVYTPWQGQWKLVPRGAPGAALWGEACNYLFWVRRPVE","length":350,"molWeight":38808,"crc64":"78DF5D09A1AA207E","md5":"E5AB368160BA2B4A4484985079DCFF67"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Binding site":7},"uniParcId":"UPI000FE1ED9F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H0E7","uniProtkbId":"A0A401H0E7_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":26,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87906.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Lon protease homolog, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"3.4.21.53"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"PIM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87906.1"}],"value":"SCP_1201310"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Homohexamer or homoheptamer. Organized in a ring with a central cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87906.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":861,"modifier":"EXACT"},"end":{"value":1048,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":791,"modifier":"EXACT"},"end":{"value":814,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":953,"modifier":"EXACT"},"end":{"value":953,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Active site","location":{"start":{"value":996,"modifier":"EXACT"},"end":{"value":996,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Binding site","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87906.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000012","properties":[{"key":"ProteinId","value":"GBE87906.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401H0E7","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401H0E7","properties":[{"key":"Number of interactors","value":"270"}]},{"database":"STRING","id":"139825.A0A401H0E7","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H0E7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"2411602at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051131","properties":[{"key":"GoTerm","value":"P:chaperone-mediated protein complex assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007005","properties":[{"key":"GoTerm","value":"P:mitochondrion organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070407","properties":[{"key":"GoTerm","value":"P:oxidation-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19500","properties":[{"key":"EntryName","value":"RecA-like_Lon"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000021","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000019","properties":[{"key":"EntryName","value":"Lon protease homolog 2, peroxisomal"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000184","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.5270:FF:000001","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.130.40:FF:000010","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.5270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1480","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.130.40","properties":[{"key":"EntryName","value":"LON domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03120","properties":[{"key":"EntryName","value":"lonm_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR004815","properties":[{"key":"EntryName","value":"Lon_bac/euk-typ"}]},{"database":"InterPro","id":"IPR054594","properties":[{"key":"EntryName","value":"Lon_lid"}]},{"database":"InterPro","id":"IPR008269","properties":[{"key":"EntryName","value":"Lon_proteolytic"}]},{"database":"InterPro","id":"IPR027065","properties":[{"key":"EntryName","value":"Lon_Prtase"}]},{"database":"InterPro","id":"IPR003111","properties":[{"key":"EntryName","value":"Lon_prtase_N"}]},{"database":"InterPro","id":"IPR046336","properties":[{"key":"EntryName","value":"Lon_prtase_N_sf"}]},{"database":"InterPro","id":"IPR027503","properties":[{"key":"EntryName","value":"Lonm_euk"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"NCBIfam","id":"TIGR00763","properties":[{"key":"EntryName","value":"lon"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718","properties":[{"key":"EntryName","value":"LON PROTEASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718:SF2","properties":[{"key":"EntryName","value":"LON PROTEASE HOMOLOG, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05362","properties":[{"key":"EntryName","value":"Lon_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22667","properties":[{"key":"EntryName","value":"Lon_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02190","properties":[{"key":"EntryName","value":"LON_substr_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00830","properties":[{"key":"EntryName","value":"ENDOLAPTASE"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00464","properties":[{"key":"EntryName","value":"LON"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51787","properties":[{"key":"EntryName","value":"LON_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51786","properties":[{"key":"EntryName","value":"LON_PROTEOLYTIC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFLGSLRATTLPSSLSCSRRLLSYPEPGPSRLVLQLASGKSARPRVPPRRSFYSSTVTDCASTQPLRYPRWINGKLNGARDHSPAPTHSEQSQTVQLDGSQDEQAPVDSAPPASSSSSGSSSSSGDNPDDSDPPPSTPPESPSQPQTSISKQSVPEVYPQVLALPIARRPLFPGFYKAVVVRNPAVVAAIKEMMRRGQPYLGAFLLKDEHTDSDVITDISSVHPVGVFAQITSVFTASGTREDDKEEGLTAVLYPHRRIRITELVKAGGAKVEPTEESLPTPPPEPIAPAPIQTSFLQNYNISVVNVENLVTQPYNKDDQYIRAFMSEIVSVFKDIAQLNPLFRDQITNFSINQVASNVFDEPDKLADFAAAVSTGDVNELQDVLESLVVADRLQKALLVLKKELINAQLQSKLARDVDSKIAKRQREYYLMEQLKGIKKELGMESDGKDKLIEKFKERAATLKMPELVRKVFDEELSKLMGLEPSASEANVTRNYLEWLTQIPWGQHSEENYSITHAQKVLDEDHYGMKDVKDRILEFLAVGKLRGTVEGKIICLAGPPGVGKTSVGKSIARALNRQFFRFSVGGLTDVAEIKGHRRTYVGALPGKIIQALKRVGTENPLVLIDEIDKIGRGINGDPASALLEMLDPEQNSAFLDHYMDVPVDLSRVLFVCTANVLDTIPAPLLDRMEVLELSGYVSEEKSVIADKYLGPQAKEASGLKDADVMIDPATVDMLIKYYCRESGVRSLKKFIEKIYRKAALKLVQDLGEEVFPESVATSAMDHDIEAKTVEKQDAPQNEPAASETTVLLTDEDQSAERKVTTVVRKPLKVPDSVHVRITPENLKDYVGPPIYHKDRMYVKPPPPGVSTGLGYLGNGSGAVMPIEAMTMPGKGQLQLTGKLGEVIRESAQIAMSWVKSHAYELGITASPDEQFLVERDIHVHMPEGSIGKEGPSAGTAILSAFVSLFTKTKINPDIAMTGEISLVGQVLPVGGLKEKILAAHRAGIKTIIAPEANRPDIEENVPESVKTGIRFVYVEDVREVLQEVFRGEPIAERWKDTLSLS","length":1062,"molWeight":116456,"crc64":"3E9E2FF27EB73CFA","md5":"FDBDBE37139D5351000360C4525EAF56"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Compositional bias":3,"Active site":2,"Binding site":1},"uniParcId":"UPI000FE254E4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H0F5","uniProtkbId":"A0A401H0F5_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87869.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00014008"}],"value":"Fatty acid synthase subunit alpha"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012948"}],"value":"1.1.1.100"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013191"}],"value":"2.3.1.41"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012878"}],"value":"2.3.1.86"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87869.1"}],"value":"SCP_1200940"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17397"},{"database":"Rhea","id":"RHEA-COMP:9916"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:78776"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"1.1.1.100","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048508"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] + holo-[ACP] + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22836"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9916"},{"database":"Rhea","id":"RHEA-COMP:14125"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78449"},{"database":"ChEBI","id":"CHEBI:78776"},{"database":"ChEBI","id":"CHEBI:138651"}],"ecNumber":"2.3.1.41","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049541"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).","ecNumber":"2.3.1.86","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048237"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:47942"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033756"}],"value":"[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007485"}],"value":"Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87869.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2208,"modifier":"EXACT"},"end":{"value":2283,"modifier":"EXACT"}},"description":"Carrier","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50075"}]},{"type":"Domain","location":{"start":{"value":3158,"modifier":"EXACT"},"end":{"value":3692,"modifier":"EXACT"}},"description":"Ketosynthase family 3 (KS3)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS52004"}]},{"type":"Region","location":{"start":{"value":2640,"modifier":"EXACT"},"end":{"value":2668,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":3340,"modifier":"EXACT"},"end":{"value":3340,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10022"}]},{"type":"Modified residue","location":{"start":{"value":2243,"modifier":"EXACT"},"end":{"value":2243,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022450"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"id":"KW-0596","category":"PTM","name":"Phosphopantetheine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023026"}],"id":"KW-0843","category":"Biological process","name":"Virulence"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87869.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000012","properties":[{"key":"ProteinId","value":"GBE87869.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027618782.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027762981.1"}]},{"database":"FunCoup","id":"A0A401H0F5","properties":[{"key":"Number of interactors","value":"22"}]},{"database":"STRING","id":"139825.A0A401H0F5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38784786","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H0F5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4251012at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005835","properties":[{"key":"GoTerm","value":"C:fatty acid synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019171","properties":[{"key":"GoTerm","value":"F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004316","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004315","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004318","properties":[{"key":"GoTerm","value":"F:enoyl-[acyl-carrier-protein] reductase (NADH) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004312","properties":[{"key":"GoTerm","value":"F:fatty acid synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004321","properties":[{"key":"GoTerm","value":"F:fatty-acyl-CoA synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008897","properties":[{"key":"GoTerm","value":"F:holo-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00828","properties":[{"key":"EntryName","value":"elong_cond_enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03447","properties":[{"key":"EntryName","value":"FAS_MaoC"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08950","properties":[{"key":"EntryName","value":"KR_fFAS_SDR_c_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.470.20:FF:000005","properties":[{"key":"EntryName","value":"Fatty acid synthase alpha subunit FasA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.930.70:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000078","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.366.10:FF:000006","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.2490:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000168","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.25.70:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.3330:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.366.10:FF:000003","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000058","properties":[{"key":"EntryName","value":"Sterigmatocystin biosynthesis fatty acid synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1050.120","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.930.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1120.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.2490","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.3330","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.90.25.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1400","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.1930","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.60.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.20.240.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.470.20","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.366.10","properties":[{"key":"EntryName","value":"Malonyl-Coenzyme A Acyl Carrier Protein, domain 2"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00101","properties":[{"key":"EntryName","value":"AcpS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008278","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom"}]},{"database":"InterPro","id":"IPR037143","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom_sf"}]},{"database":"InterPro","id":"IPR001227","properties":[{"key":"EntryName","value":"Ac_transferase_dom_sf"}]},{"database":"InterPro","id":"IPR002582","properties":[{"key":"EntryName","value":"ACPS"}]},{"database":"InterPro","id":"IPR014043","properties":[{"key":"EntryName","value":"Acyl_transferase_dom"}]},{"database":"InterPro","id":"IPR016035","properties":[{"key":"EntryName","value":"Acyl_Trfase/lysoPLipase"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR039569","properties":[{"key":"EntryName","value":"FAS1-like_DH_region"}]},{"database":"InterPro","id":"IPR013565","properties":[{"key":"EntryName","value":"Fas1/AflB-like_central"}]},{"database":"InterPro","id":"IPR041099","properties":[{"key":"EntryName","value":"FAS1_N"}]},{"database":"InterPro","id":"IPR040899","properties":[{"key":"EntryName","value":"Fas_alpha_ACP"}]},{"database":"InterPro","id":"IPR047224","properties":[{"key":"EntryName","value":"FAS_alpha_su_C"}]},{"database":"InterPro","id":"IPR040883","properties":[{"key":"EntryName","value":"FAS_meander"}]},{"database":"InterPro","id":"IPR041550","properties":[{"key":"EntryName","value":"FASI_helical"}]},{"database":"InterPro","id":"IPR003965","properties":[{"key":"EntryName","value":"Fatty_acid_synthase"}]},{"database":"InterPro","id":"IPR050830","properties":[{"key":"EntryName","value":"Fungal_FAS"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"InterPro","id":"IPR014031","properties":[{"key":"EntryName","value":"KAS_C"}]},{"database":"InterPro","id":"IPR014030","properties":[{"key":"EntryName","value":"KAS_N"}]},{"database":"InterPro","id":"IPR018201","properties":[{"key":"EntryName","value":"Ketoacyl_synth_AS"}]},{"database":"InterPro","id":"IPR002539","properties":[{"key":"EntryName","value":"MaoC-like_dom"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR020841","properties":[{"key":"EntryName","value":"PKS_Beta-ketoAc_synthase_dom"}]},{"database":"InterPro","id":"IPR009081","properties":[{"key":"EntryName","value":"PP-bd_ACP"}]},{"database":"InterPro","id":"IPR004568","properties":[{"key":"EntryName","value":"Ppantetheine-prot_Trfase_dom"}]},{"database":"InterPro","id":"IPR032088","properties":[{"key":"EntryName","value":"SAT"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"NCBIfam","id":"TIGR00556","properties":[{"key":"EntryName","value":"pantethn_trn"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982:SF21","properties":[{"key":"EntryName","value":"FATTY ACID SYNTHASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982","properties":[{"key":"EntryName","value":"MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01648","properties":[{"key":"EntryName","value":"ACPS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00698","properties":[{"key":"EntryName","value":"Acyl_transf_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08354","properties":[{"key":"EntryName","value":"Fas1-AflB-like_hel"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13452","properties":[{"key":"EntryName","value":"FAS1_DH_region"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22235","properties":[{"key":"EntryName","value":"FAS1_thioest_ins"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18325","properties":[{"key":"EntryName","value":"Fas_alpha_ACP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18314","properties":[{"key":"EntryName","value":"FAS_I_H"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17951","properties":[{"key":"EntryName","value":"FAS_meander"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17828","properties":[{"key":"EntryName","value":"FAS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00109","properties":[{"key":"EntryName","value":"ketoacyl-synt"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02801","properties":[{"key":"EntryName","value":"Ketoacyl-synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01575","properties":[{"key":"EntryName","value":"MaoC_dehydratas"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16073","properties":[{"key":"EntryName","value":"SAT"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01483","properties":[{"key":"EntryName","value":"FASYNTHASE"}]},{"database":"SMART","id":"SM00827","properties":[{"key":"EntryName","value":"PKS_AT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56214","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52151","properties":[{"key":"EntryName","value":"FabD/lysophospholipase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51412","properties":[{"key":"EntryName","value":"Inosine monophosphate dehydrogenase (IMPDH)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50075","properties":[{"key":"EntryName","value":"CARRIER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00606","properties":[{"key":"EntryName","value":"KS3_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS52004","properties":[{"key":"EntryName","value":"KS3_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVSSTSPTSIPTRPILIQSGQTRFSIPVSTQSDEWIAAEVLRDEFTLSQPAALDTTFDTEEQATLELYARFLGFVAQKLDEDADSSAARTTVLLKILQHFTTSYLSHQDVHTVAASFDTDTREAILAAYFRAVCSLEEKKGGDVPQQPTPALLSAAAQKDASVYAIFGGQGTNEVYFDELQSLYDIYKPYVASFLETVTRDVLVPLASASESTYYAYGLDAISWLTGAAPRPPTAYLATVPVSFPLIGLTQLTQYLIVCRVAKLSPGELCVRLRGATGHSQGLVSAVCISASNTLESFFENAQKALKWLFFCGFRGQQAFPVLALEPSIVEDAVEGGEGVPSPMLSVTGLLLKDLEVHIKKTNVHLPENSQLHISLYNGSKAFVVTGPPRALFGLVNSLRKVRAPSGLDQSKVPFSQRKPVFSVRFLVVGVPFHSHYLEGMTKKMFEEDLEGEELWTKEELAIPVYNTEDGSDLRKLSTSLTCALCDLIFTLPIHWDKATNFPETATHAVDFGPGGLSGIGPLTARNLDGRGVRIIIGGDKTKGVVEMYDAQNVKREEWWSKRFMPGLVKTSDGSIHIDTPFSRLLGKPPIMVAGMTPTTVKAGFVSAVLDAGYHVELAGGGHYNAAALRAKVAEIQSKIPAGVGLTLNSLYINPRQFGFQFPLWQEMRREGLPIEGFCVAAGIPSTEKAAEIIDGLRTAGIKHVSFKPGSVDGIRQVVNIAAAHPDFPVILQWTGGRAGGHHSCEDFHQPIISTYSSIRQHINISLVGGSGFGGADDLWPYLSGDWSVQQYGLQPMPFDGFLFASRVMVAKEAHTSSSVKDLIVAAKGVDDAQWEGTYAKETGGILTVRSELGEPIHKIANRAVKLWKEFDNTVFNLPKEKRAAWLVEHRSEVIAKLNKDFSKPWFGWKKDGSVTEDIADMTYEEVAMRMVRLMYVAKEERWVDLSLRNLTGDWLRRVEERFAGVNGGGEKSSILQSFNSLDKPRAVIEEFFKTYPLATEQLLASEDKAYFLTIVQRPGQKPVPFIPVLDASFEVWFKKDSLWAAEDIEAVFDQDPQRVCILQGPVAVKHSKAKDEPIKEMLDNITSLLVKKLIDRLYGGDVSKIPTVDYLSPGPSALATPLHVERSVSRNTITYKLGQTLPETSSWLETLAGPELCWVRALLTSPTVVQGALYIDNPIRRLFAPRRGQKVVVETDGVSPIGISVYGAARSYGAHKSDFKAVDVKYNAYSHTINVTVYEDCRDVAIPLKLQFVHKPSMGFAPIHEVTTDRNRRIKEFYWKLWLGPEENLPEIDLRATFTGPEVTIDADEIEAFCSVIGNDGEAFKTVRAENVQAPMDFAIVTGWQAIIKAIFPSTIDGDLLKLVHLSNGFRLVDDAKPLQAGDVCKIEARIVSVINSDAGKTVRVKGFVIRDGKPVIEVVSAFLYRGRYSEYDNTFELLEAPDYSVELATEADVGVLQSKEWFEWDDPSKPLQAGTTLVFRVKSEVTYRNKTCYKSVSVSGDIFVRDQIKRLIKVGGVDFLQDDSRGNPVIAYLERHGKPQGLWAPLPNDGYTMTKTGAAVFNSSATNESYSKVSGDFNPIHVNPYFADLAALPATITHGMWSSAATRRYVETVVAQGRPERVVAYDVAFVGMVIPGDSLQVKIKHSGMRDGNIVVKVETFNGKGEKVLEGTAEVAQPKTVYVFTGQGSQEPGMGMDLYNSSPAARSVWDAADAHLTAVYGFSIVQIVKDNPKEKTIHFGGIKGQAIRQRYMDMTYDTMDKDGNVKTLPLFGDINVRTQRYTFSHPSGLLFATQFAQIALVVTERAAFEDMRSKGFVQKDSAFAGHSLGEYSALASIADVLPISSLVDVVFYRGITMQRAVERDAHNRSNYAMCAVNPSRISKTFTDAALREVIDDIAHRTQCLLEIVNYNVEGQQYVCAGELVALQTMTNVLNYLKMEKVDIAKLTEKFTVEQVKEMLGEIINSCFTRAKDQQKAEGYIKLERGFATIPLPGIDVPFHSRYLWAGVMPFRAYLSKKINAAHLNPDTLVGKYVPNLIAKPFQVTKDYVQLIYDQTLSPRLDKVLRKWDTENWGSAEQRQKLAYITLVELLAYQFASPVRWIETQDILFKHYDFERFIEIGPSPTLTGMATRTLKAKYEVQDDSVSRIRAILCHAKHTKEVYYQFEDEAEAAADESAPEAAAIPAPVAVPVAAPVSAAAAVSVEDVPLKAIEILSVVVAQKLKKKVEEIPLSKSIKDLVGGKSTLQNEILGDLQLEFTSAPEKGEELPLEELGSALGVGFSGSLGKYSSGLVSRVVGSKMPGGFNISAIKAYLSKTWGLGPTRADGVLLLSTTMEPPKRLGSDAEAKAWLDTVVTLYAQRSGISLATGAANGGGGGGAGGPTINSEEFLQFQADQEQFAAQQIELYMRYLKRDSRAGEIKYDAEKANVVTLQSKLDAISREHGDTYIDGIQPVFDALKARHFDSSWNWVRQDALLMFYDIIFGRLTTVDREITSRCIAIMNRADPELVTYMQYYIDQCDPNRGDTYKLAKQFGQQLIDNCREVLALPPLYKDVTFPTAPHTEVTAKGDIVYSEVVRENVRKLEAYVEEMASGDTISAPTNIQKIQDDVLKLWNVVKSQPEISEEQKNRIKALYEGVVRSLRKRPESRPRPGAPRPRRSSSQFLRPQVSGVASVTADKVPLLHLKRKVGTNWEYSSNLTGVYLDILHEIATSGTTFKDKNALLTGVGKASIGVEVVKGLLSGGAHVVITTSRYSRATVEYYQGIFQRFGSRGSALTVVPFNQGSKQDVEALIDYIYSTLGLDLDYVLPFAAVPENGRQIDGLDDKSELAHRIMLVNLLRLLGAVKLKKASRQILTRPTQVILPLSPNHGLFGNDGLYSESKISLETLFNRWNSESWGEYLCLAGAVIGWTRGTGLMDATNIVAHDVESHGVRTFSAKEMAFNIMGLMHPLLFSITQVEPIWADLNGGMDRLPDLADITTRIRTDLNKKSELRRAIARDNAADFKMVNGVEAERVLQTVNVVPRANFKFEYPALESYESLADVSKLRGMLDLEKVIVVTGFAEVGPWGSSRTRWEMEARGEFTIEGCIEMAWMMGYIKHFDGRLKDGSLHVGWVDAKSGEPVDDKDVRGRYEKDILSHAGVRLIEPELFRGYDPKKKVFNQEIQLLHDLEPFEAAEVDAQKFKLEHGDNCDIWAGEGGQWFVKFKKGARVFVPKAFKFNRLVAGQIPTGWDAGRYGIPQDIIAQTDRTSLWALVCAAEALNTSGITDPYELYKHMHPSEVGSSIGSGMGGMESLSKMFKDRRDEKEVQNDILQETFINTTAGWVNLLLLSSSGPIKIPVGACATALQSIEIACDTLLSGKAKVMLAGGFDDLSEEGSYEFGNMKATSNAETELAMGREPTEMSRPATTTRAGFMEAQGTGVHVLMNAKTALELGCPIRGIIGFTSTSTDKAGRSVPAPGRGALSIAREVPSKHPLPMLDLVYRSRQLAFRRSQISEWLANEQQQLQEDIEFRKSRNEVVDEEYLASRVADVEKEAARQEKDALATYGMLEGADARVAPLRRALAVFGLTADDIGVLSIHGTGTGANEANETHIWNDVLGAISRTPHNAVPIMAQKSLCGHSKGGSAAWQLAGLLQSVHSGIVPGNRNADNVDADFKQYTYLMFPSKTIHTDGIRAGLMSSFGFGQVGGTCMIINPRYVLGSLEPSAYEAYKGKNLTRAHLSYKAMSEMMINNCLVKVKDAPPYSKDLEAPVLMNPLARACLDPKTGSYAFPAKLNLQPAVDIANVKAISQILAAQGSTAGVGVDQELISAVPSSNPTFVSRNFTDAEIEYCRSQPSPAASFAARWVGKEAVFKSLGVSSKGAAAPMKDIEILKDDSGVPTVILRGDAKSAAEAKGITRVHLSLSHSETVAVAFAQAASS","length":3917,"molWeight":430469,"crc64":"9F87A6CA0E92B041","md5":"7FB3022638771F394630B640C0E97E4B"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":1,"Modified residue":1},"uniParcId":"UPI000FE19DAB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H0P9","uniProtkbId":"A0A401H0P9_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":26,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87994.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphohexokinase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87994.1"}],"value":"SCP_1202200"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade \"E\" sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87994.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Domain","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Domain","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":811,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"N-terminal catalytic PFK domain 1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Region","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":886,"modifier":"EXACT"}},"description":"C-terminal regulatory PFK domain 2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Compositional bias","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":591,"modifier":"EXACT"},"end":{"value":591,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":648,"modifier":"EXACT"},"end":{"value":652,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":686,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":693,"modifier":"EXACT"},"end":{"value":695,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":753,"modifier":"EXACT"},"end":{"value":753,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":779,"modifier":"EXACT"},"end":{"value":779,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":860,"modifier":"EXACT"},"end":{"value":860,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE87994.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000012","properties":[{"key":"ProteinId","value":"GBE87994.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027618907.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027763106.1"}]},{"database":"AlphaFoldDB","id":"A0A401H0P9","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401H0P9","properties":[{"key":"Number of interactors","value":"281"}]},{"database":"STRING","id":"139825.A0A401H0P9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38784911","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H0P9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"537915at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.460:FF:000007","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.460:FF:000008","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_03184","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_E"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009161","properties":[{"key":"EntryName","value":"6-Pfructokinase_euk"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02478","properties":[{"key":"EntryName","value":"6PF1K_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"3"}]},{"database":"PIRSF","id":"PIRSF000533","properties":[{"key":"EntryName","value":"ATP_PFK_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"3"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MCPLVFEVPCVFQESTPQENSLLTHSDGHPSTACTPSSSSMTSTPSTPPATAAMPRPATPAPTASTSPPAIKKPKMKIAVLTSGGDSAGMNAVVRAVVKTAIIKGCEAWIVREGYEGLVRGNSQEIQKPAATPASEKGTPAPEERRASDASFVHNLRFGDGELLRDGTGDHPGGRSLRGRYIVRVGWDDVRGWFAQGGTLIGTARSTAFRTPEGRLTAAHNLIKEGIDALVVCGGDGSLSGADVFRSEWPKLVVELLTQEKITQEQAMLHAHLKVVGLVGSIDNDMSLTDMTIGAPTALHRICESIDNINSTAVSHSRAFVLEVMGRNCGWLALMAGVSCGADFIFIPEHPPTENPWEDEMCSEIQSHRDIGKRKTIVIVAEGALDSNLNPIHANYVKDVLSERLGLDTRVTTLGHTQRGGAPCAIDRIMPTLQGVEAVEALLEATPDTPSYMIGMRENKITRVPLMEAVAMTRSVSTAIAEKDFAKAMSLRDPEFSETLEGFYATSILEKEPRLPHHLRMRVAIMHIGAPAGGMNAATRAAVRYCIRQGHKPFAVHNGFTGLLDDNVHTLSWLGVDNWITHGGSELGTNRHLPDIDLGAVAAKFQQFNFHALLMIGGFEAFSSLLILEGARKHYPAFHIPMVHLPATISNNVPLTEFSLGSDTSLNALVNACDAIKQSASASRNRVFVVETQGGKCGYIATLGALATGACIVYTPERGINLDMLRHDVKFLKKRYALDAKGKAEGRLVLRNEVASDVYTTDFITRMLKEEGGSLFDSRSASLGHTLQGGIPSPTDRARAVRLSLKCMAFIEQYHKELLKQPVKTRQAPPESAAVITVQGSTVKWMPVEEMVEHADMKNRRGKTAFWDELTDLVEALVARPQLLAK","length":886,"molWeight":95840,"crc64":"608DC327F50A533F","md5":"EE5679AEE8190093F6D43D882E0077BA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":4,"Compositional bias":1,"Active site":1,"Binding site":17},"uniParcId":"UPI000FE264D6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H114","uniProtkbId":"A0A401H114_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2019-05-08","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE88108.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase proenzyme 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"PSD2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE88108.1"}],"value":"SCP_1203370"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Golgi apparatus membrane","id":"SL-0134"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Endosome membrane","id":"SL-0100"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE88108.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1071,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5023246810"},{"type":"Chain","location":{"start":{"value":1072,"modifier":"EXACT"},"end":{"value":1126,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5023246809"},{"type":"Domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":559,"modifier":"EXACT"}},"description":"EF-hand","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50222"}]},{"type":"Region","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":598,"modifier":"EXACT"},"end":{"value":619,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":654,"modifier":"EXACT"},"end":{"value":727,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":689,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":696,"modifier":"EXACT"},"end":{"value":727,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":927,"modifier":"EXACT"},"end":{"value":927,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":985,"modifier":"EXACT"},"end":{"value":985,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":1072,"modifier":"EXACT"},"end":{"value":1072,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":1072,"modifier":"EXACT"},"end":{"value":1072,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Site","location":{"start":{"value":1071,"modifier":"EXACT"},"end":{"value":1072,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Modified residue","location":{"start":{"value":1072,"modifier":"EXACT"},"end":{"value":1072,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0967","category":"Cellular component","name":"Endosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE88108.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000012","properties":[{"key":"ProteinId","value":"GBE88108.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401H114","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401H114","properties":[{"key":"Number of interactors","value":"59"}]},{"database":"STRING","id":"139825.A0A401H114","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H114","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"67700at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00558","properties":[{"key":"RectionId","value":"UER00616"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0010008","properties":[{"key":"GoTerm","value":"C:endosome membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000139","properties":[{"key":"GoTerm","value":"C:Golgi membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005795","properties":[{"key":"GoTerm","value":"C:Golgi stack"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00030","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04039","properties":[{"key":"EntryName","value":"C2_PSD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.238.10","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00663","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR011992","properties":[{"key":"EntryName","value":"EF-hand-dom_pair"}]},{"database":"InterPro","id":"IPR002048","properties":[{"key":"EntryName","value":"EF_hand_dom"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033179","properties":[{"key":"EntryName","value":"PSD_type2_pro"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF17","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00239","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF47473","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50222","properties":[{"key":"EntryName","value":"EF_HAND_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVKPPSMRNKKAIKFGRAIRSAARFPVRVSGGRGSGRNTFSPAQGEVPVVLLRVQILGCTNLVAKDRNGYSDPFVVVSLLRDRHRTPVIKRSLNPVYAPKDATFDFPIYMSLAEKLGVIELVVWDKDVIKKDYLGEACIPLEDWFRDGNAFSFDDANNKAITAPIVSTRTSTQASGTIHLKLGFVPAAKSAPLMDYDQLYSELNKRSRPSLVSAPPTAGIGTVRSQEGGPAFEDDGLTSDEGEYNSEDDEEDSPEKFITTPIAQPIPRTASMPSTPTTAKPLLSAPAIAYSLSKPPSPLPSSFNIPKIFPRRASGARSPSVDWSMTGSSSPRAVTPTPTGTPTPTQKTKFRRSWISKRKDFNFSAANDILGIVMLEIQSARDLPRLKNMTRTGYDMDPFVVVSFGKKVFRTRVIRHSLNPAWDEKLLFHVRRYESAFKVQLTVLDWDKLSSNDHVGDASFDVAELIANAPQKDEATGLYPANEDGLSPMKEFCLPLTTAKEVPWESKHAPVLIFRAKYQPYDALRQRFWRQYLKQYDTDDMGMLSHVELTSMLDSLGSTLSHETVNSFFTRFGKKPHEDVITVNQAIQSLETELCRPRSEKKRINPDETGIDTSAPVTPAIHSNADKQLLLNLDLLDFSGPPLDLSAYIRDLEHDPLQKPSPPASYPTEPMQQPLADVAASSSSSSVSANFNHQISGSYSDPEESSGSASGGSSSSSNTTSPSSTSTDDLFERVINIKNCPLCHRPRLNSKAEVDIVTHLAICASQDWAAVDRIMVGNFVTASQAQRKWYTRVISKVSSGNYKLGANSANIIVQDRLTGQLEEEKMQVYVRLGIRLLYKGWKSRMEGARARRLLRSMSIKQGIKYDSLESALYIPTFIAFHHLNVDEILEPLSSFKNFNEFFYRKLKPTARPTECPDDPYRLVSSADCRLMTFETVHEATSLWIKGRDFTVARLLGEAYRSQADRYVHGALCIFRLAPQDYHRFHSPVDGIIGPMTYVAGEYYTVNPQAIRTALDVYGENARKIVPVDSPQFGRVMIVCVGAMMVGTIKTTVKEGDRVARGQELGYFAFGGSTLVVLFEKGVVEWDEDLLDNGRACLETRVRVGMGIGRGQRAPSLGSDNNTRAAP","length":1126,"molWeight":124811,"crc64":"BE4973064A0FA7B7","md5":"D306BBC11618D419AFF738C3DCBF802C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Domain":3,"Region":4,"Compositional bias":5,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI000FE222C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H3T3","uniProtkbId":"A0A401H3T3_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89088.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026218"}],"value":"Oxidized purine nucleoside triphosphate hydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026103"}],"value":"3.6.1.56"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031927"}],"value":"2-hydroxy-dATP diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030682"}],"value":"7,8-dihydro-8-oxoguanine triphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030634"}],"value":"8-oxo-dGTPase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032071"}],"value":"Methylated purine nucleoside triphosphate hydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029673"}],"value":"Nucleoside diphosphate-linked moiety X motif 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89088.1"}],"value":"SCP_1500910"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00053094"}],"value":"Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP. Also has a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67392"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:71395"},{"database":"ChEBI","id":"CHEBI:172878"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024596"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67393"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024596"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31583"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:63212"},{"database":"ChEBI","id":"CHEBI:77897"}],"ecNumber":"3.6.1.56","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024459"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31584"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024459"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"8-oxo-dATP + H2O = 8-oxo-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65396"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:71361"},{"database":"ChEBI","id":"CHEBI:172871"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024448"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65397"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024448"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31575"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:63224"},{"database":"ChEBI","id":"CHEBI:77896"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024486"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31576"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024486"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-ATP + H2O = N(6)-methyl-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67608"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:144842"},{"database":"ChEBI","id":"CHEBI:172873"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67609"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-dATP + H2O = N(6)-methyl-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67604"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:169976"},{"database":"ChEBI","id":"CHEBI:172872"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049032"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67605"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049032"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O(6)-methyl-dGTP + H2O = O(6)-methyl-dGMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67600"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:169974"},{"database":"ChEBI","id":"CHEBI:169975"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67601"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048894"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005582"}],"value":"Belongs to the Nudix hydrolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89088.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Nudix hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51462"}]},{"type":"Motif","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Nudix box","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89088.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000015","properties":[{"key":"ProteinId","value":"GBE89088.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027620001.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027764200.1"}]},{"database":"AlphaFoldDB","id":"A0A401H3T3","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"139825.A0A401H3T3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38786005","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H3T3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"447842at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008413","properties":[{"key":"GoTerm","value":"F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008828","properties":[{"key":"GoTerm","value":"F:dATP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042262","properties":[{"key":"GoTerm","value":"P:DNA protection"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03427","properties":[{"key":"EntryName","value":"NUDIX_MTH1_Nudt1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.79.10","properties":[{"key":"EntryName","value":"Nucleoside Triphosphate Pyrophosphohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003563","properties":[{"key":"EntryName","value":"8ODP"}]},{"database":"InterPro","id":"IPR015797","properties":[{"key":"EntryName","value":"NUDIX_hydrolase-like_dom_sf"}]},{"database":"InterPro","id":"IPR020084","properties":[{"key":"EntryName","value":"NUDIX_hydrolase_CS"}]},{"database":"InterPro","id":"IPR000086","properties":[{"key":"EntryName","value":"NUDIX_hydrolase_dom"}]},{"database":"PANTHER","id":"PTHR43758","properties":[{"key":"EntryName","value":"7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43758:SF2","properties":[{"key":"EntryName","value":"OXIDIZED PURINE NUCLEOSIDE TRIPHOSPHATE HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00293","properties":[{"key":"EntryName","value":"NUDIX"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01403","properties":[{"key":"EntryName","value":"8OXTPHPHTASE"}]},{"database":"SUPFAM","id":"SSF55811","properties":[{"key":"EntryName","value":"Nudix"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51462","properties":[{"key":"EntryName","value":"NUDIX"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00893","properties":[{"key":"EntryName","value":"NUDIX_BOX"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSERLDEVARGGVPDWLPFSKIKLYTNAFVRQDGKLLLGYKKRGFGKDLYNGFGGKVEPGETPAQAALRELEEESGIAAPLEHCGVLFFVLPDLEQAFHIDIFRAEEYSGAITESDEMRPQWFDIEPAYATPNAKPAAADGSPKEHNTGLPPIPYDQMWADDPFWLPLMLAGRHFAGRADFGSDGRLQKWWFGAKPV","length":198,"molWeight":22088,"crc64":"A90DBAFD1B3D23CF","md5":"3D2CCB4FEAE0FAF69A341736AEBD5F9A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":7,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Motif":1},"uniParcId":"UPI000FE2346F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H636","uniProtkbId":"A0A401H636_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89851.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"ATP-dependent DNA helicase PIF1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"5.6.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA 5'-3' helicase PIF1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA repair and recombination helicase PIF1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"PIF1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89851.1"}],"value":"SCP_1701760"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Belongs to the helicase family. PIF1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89851.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"DNA binding","location":{"start":{"value":527,"modifier":"EXACT"},"end":{"value":546,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89851.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000017","properties":[{"key":"ProteinId","value":"GBE89851.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401H636","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401H636","properties":[{"key":"Number of interactors","value":"220"}]},{"database":"STRING","id":"139825.A0A401H636","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H636","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"432234at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18037","properties":[{"key":"EntryName","value":"DEXSc_Pif1_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18809","properties":[{"key":"EntryName","value":"SF1_C_RecD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_03176","properties":[{"key":"EntryName","value":"PIF1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR010285","properties":[{"key":"EntryName","value":"DNA_helicase_pif1-like_DEAD"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR049163","properties":[{"key":"EntryName","value":"Pif1-like_2B_dom"}]},{"database":"InterPro","id":"IPR051055","properties":[{"key":"EntryName","value":"PIF1_helicase"}]},{"database":"InterPro","id":"IPR048293","properties":[{"key":"EntryName","value":"PIF1_RRM3_pfh1"}]},{"database":"PANTHER","id":"PTHR47642","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47642:SF5","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05970","properties":[{"key":"EntryName","value":"PIF1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21530","properties":[{"key":"EntryName","value":"Pif1_2B_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MLSGLTNTKKRKSTGSIPDPRQGDAKRPRKTLDTFFSPQVAATGTSRDDKGAKATVELNEEQNNVLRMVVNEEKNVFFTGAAGTGKSLLLRAIINALRKKHAKKPEVISVTASTGMAASNIGGMTIHSWGAVTPGMHNIDRQISCIKTCKPAHRRWKATKVLIIDEVSMVDGQLFDTLAALANSLRKKTAKPFGGIQLVITGDFFQLPPVTKSNTEPFFAFESDAWKKCIDHTVTLSRVYRQKDSQFVSLLNELRRGTISPSAHQTFSRLSRTLPPLPTGLLPTELYPLRAQVERANTTRLAALPGGPVTFAARDSGSSQRVLEQMVAPARLVLKPDAQVMLVKNVDEGLVNGCVGRVLGFFGVSCCVASVTPAEKAPGISATSSSAGPRPKSTAPPSTSGSAKNNGAVRNVRVGADGRTPIAFKTGRTIEEKENVGQKTSDLKGKGKGVRKDDELYPLVEFRTSQVVEIVLLIREEFRVEDNEGKLLARRVQVPLVLAWAMSIHKSQGQTIQHVKIDLGRVFEKGQSYVALSRAASMDGLQVLGFDAGKVKAHPKVIEWSLGLEKTAERKRISA","length":575,"molWeight":62333,"crc64":"7E445E80DE77B090","md5":"0B9799824F8FFFC821D15F1633410D1A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"DNA binding":1,"Region":2,"Compositional bias":4,"Binding site":1},"uniParcId":"UPI000FE25FAB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401H6C6","uniProtkbId":"A0A401H6C6_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2019-05-08","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89923.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase proenzyme 1, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"PSD1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89923.1"}],"value":"SCP_1702490"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 alpha chain","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 beta chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Single-pass membrane protein","id":"SL-9904"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89923.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5023500302"},{"type":"Chain","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5023500301"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Topological domain","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Region","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Site","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Modified residue","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE89923.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000017","properties":[{"key":"ProteinId","value":"GBE89923.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401H6C6","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401H6C6","properties":[{"key":"Number of interactors","value":"280"}]},{"database":"STRING","id":"139825.A0A401H6C6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401H6C6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4330at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00558","properties":[{"key":"RectionId","value":"UER00616"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_03208","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type1_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033661","properties":[{"key":"EntryName","value":"PSD_type1_euk"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF6","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MLRGRVRKNISLHSWRFLERCKRSRITVFVRRAHRSYSTFKQPQQESNSGSQRPPLRQRLASAWKETPTTWYPLPVAVGALLLLAIQFRKKVAETEVHVDNEGREVVKLKGPWHVHVMGALPLRNLSRVWGYVNSFELPVWFRPYGFRFYAWAFGCDLTEIEPEDLTKYASLGEFFYRDLKDGARPVADAVLVSPADGKILHFGTITNGRVEQVKGSTYSLDALLGVESPHVRPAPVTFPRRDMAEVDDRDFADINGIEYSLEELLGASESNTPGSSGTSTPTTSVSPGVHPSHAKKYGAQIDASVSFDASMSDVIAHDASVAAEMGLRPSLERTRSRLSKAPRPGNALYFVVVYLAPGDYHKFHSPTAWVVEKRRHFVGDLFSVSPWMAKRLENLFVLNERVALLGRWKYGFFSMVPVGATNVGSIKIDFDQALRTNVASRRRPPVGTYTEAVYSAASPILNGQPLMKAQKMGGFSLGSTVVVVFEAPQDFQFTIHAGQKIKVGETMGDVATAFESKKQR","length":521,"molWeight":58107,"crc64":"F10BF99A25321E55","md5":"67C36E53250DAD63E37D37566FC7BDB5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":2,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Topological domain":2,"Region":1,"Compositional bias":1,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI000FE18553"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G4L1","uniProtkbId":"A0A401G4L1_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77137.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012411"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}],"value":"Mitogen-activated protein kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012411"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}],"value":"2.7.11.24"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77137.1"}],"value":"SCP_0100090"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.24","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}],"value":"Activated by threonine and tyrosine phosphorylation"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77137.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Active site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361165"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022527"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77137.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77137.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608050.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027752249.1"}]},{"database":"AlphaFoldDB","id":"A0A401G4L1","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401G4L1","properties":[{"key":"Number of interactors","value":"462"}]},{"database":"STRING","id":"139825.A0A401G4L1","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774054","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G4L1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"192887at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004707","properties":[{"key":"GoTerm","value":"F:MAP kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0106310","properties":[{"key":"GoTerm","value":"F:protein serine kinase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0051403","properties":[{"key":"GoTerm","value":"P:stress-activated MAPK cascade"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07856","properties":[{"key":"EntryName","value":"STKc_Sty1_Hog1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000049","properties":[{"key":"EntryName","value":"Mitogen-activated protein kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000050","properties":[{"key":"EntryName","value":"Mitogen-activated protein kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.510.10","properties":[{"key":"EntryName","value":"Transferase(Phosphotransferase) domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR003527","properties":[{"key":"EntryName","value":"MAP_kinase_CS"}]},{"database":"InterPro","id":"IPR050117","properties":[{"key":"EntryName","value":"MAPK"}]},{"database":"InterPro","id":"IPR008352","properties":[{"key":"EntryName","value":"MAPK_HOG-like"}]},{"database":"InterPro","id":"IPR038783","properties":[{"key":"EntryName","value":"MAPK_Sty1/HOG1"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"InterPro","id":"IPR017441","properties":[{"key":"EntryName","value":"Protein_kinase_ATP_BS"}]},{"database":"InterPro","id":"IPR008271","properties":[{"key":"EntryName","value":"Ser/Thr_kinase_AS"}]},{"database":"PANTHER","id":"PTHR24055","properties":[{"key":"EntryName","value":"MITOGEN-ACTIVATED PROTEIN KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01773","properties":[{"key":"EntryName","value":"P38MAPKINASE"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01351","properties":[{"key":"EntryName","value":"MAPK"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFVKLSIFGTSFEVTTRYVDLQPVGMGAFGLVCSAKDQLTGSSVAIKKIMKPFSTPVLSKRTYRELKLLKHIQHENIISLSDVFISPLEDIYFVTDLLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILINENCDLRICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVAVDIWSAGCIFAEMLEGKPLFPGKDHVHQFSIITELLGTPPEDVIRTIASENTLRFVQSLPKRERVPFSEKLHCSDPVAIDLLEKMLVFDPHKRINATDSLAHEYVAPYHDPTDEPEAAEKFDWSFNDAELPVDTWKVMMYSEILDFHQVGDAHLGDGVPEGALAAPEDPPRGTDARAAPAVVPAPAVVVAAAAGVD","length":389,"molWeight":43558,"crc64":"64F54A478B07364D","md5":"B4F30E942A0EB29AD1FCE43C92D97814"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":1},"uniParcId":"UPI000FE22DA3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G4X3","uniProtkbId":"A0A401G4X3_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77221.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012493"}],"value":"RNA-directed DNA polymerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012493"}],"value":"2.7.7.49"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77221.1"}],"value":"SCP_0100930"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002180"}],"value":"The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.49","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22508"},{"database":"Rhea","id":"RHEA-COMP:17339"},{"database":"Rhea","id":"RHEA-COMP:17340"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:173112"}],"ecNumber":"2.7.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage to 5'-phosphomonoester.","ecNumber":"3.1.26.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000077"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77221.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"Reverse transcriptase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50878"}]},{"type":"Domain","location":{"start":{"value":882,"modifier":"EXACT"},"end":{"value":1042,"modifier":"EXACT"}},"description":"Integrase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50994"}]},{"type":"Domain","location":{"start":{"value":1181,"modifier":"EXACT"},"end":{"value":1235,"modifier":"EXACT"}},"description":"Chromo","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50013"}]},{"type":"Binding site","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":893,"modifier":"EXACT"},"end":{"value":893,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":954,"modifier":"EXACT"},"end":{"value":954,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022750"}],"id":"KW-0064","category":"Molecular function","name":"Aspartyl protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022908"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0229","category":"Biological process","name":"DNA integration"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022932"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0239","category":"Molecular function","name":"DNA-directed DNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022918"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0695","category":"Molecular function","name":"RNA-directed DNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00405"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77221.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77221.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608134.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027752333.1"}]},{"database":"AlphaFoldDB","id":"A0A401G4X3","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401G4X3","properties":[{"key":"Number of interactors","value":"1"}]},{"database":"STRING","id":"139825.A0A401G4X3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774138","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G4X3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"2729552at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003887","properties":[{"key":"GoTerm","value":"F:DNA-directed DNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003964","properties":[{"key":"GoTerm","value":"F:RNA-directed DNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004523","properties":[{"key":"GoTerm","value":"F:RNA-DNA hybrid ribonuclease activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006338","properties":[{"key":"GoTerm","value":"P:chromatin remodeling"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0015074","properties":[{"key":"GoTerm","value":"P:DNA integration"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006313","properties":[{"key":"GoTerm","value":"P:DNA transposition"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00024","properties":[{"key":"EntryName","value":"CD_CSD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00303","properties":[{"key":"EntryName","value":"retropepsin_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd09274","properties":[{"key":"EntryName","value":"RNase_HI_RT_Ty3"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01647","properties":[{"key":"EntryName","value":"RT_LTR"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.370:FF:000001","properties":[{"key":"EntryName","value":"Retrovirus-related Pol polyprotein from transposon 17.6-like protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.270:FF:000020","properties":[{"key":"EntryName","value":"Transposon Tf2-6 polyprotein-like Protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.270:FF:000003","properties":[{"key":"EntryName","value":"Transposon Ty3-G Gag-Pol polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.340.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.370","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.40.70.10","properties":[{"key":"EntryName","value":"Acid Proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.10.10","properties":[{"key":"EntryName","value":"HIV Type 1 Reverse Transcriptase, subunit A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.10","properties":[{"key":"EntryName","value":"Ribonuclease H-like superfamily/Ribonuclease H"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR000953","properties":[{"key":"EntryName","value":"Chromo/chromo_shadow_dom"}]},{"database":"InterPro","id":"IPR023780","properties":[{"key":"EntryName","value":"Chromo_domain"}]},{"database":"InterPro","id":"IPR023779","properties":[{"key":"EntryName","value":"Chromodomain_CS"}]},{"database":"InterPro","id":"IPR043502","properties":[{"key":"EntryName","value":"DNA/RNA_pol_sf"}]},{"database":"InterPro","id":"IPR001584","properties":[{"key":"EntryName","value":"Integrase_cat-core"}]},{"database":"InterPro","id":"IPR041588","properties":[{"key":"EntryName","value":"Integrase_H2C2"}]},{"database":"InterPro","id":"IPR021109","properties":[{"key":"EntryName","value":"Peptidase_aspartic_dom_sf"}]},{"database":"InterPro","id":"IPR063610","properties":[{"key":"EntryName","value":"PRO_PEG10-RTL1"}]},{"database":"InterPro","id":"IPR043128","properties":[{"key":"EntryName","value":"Rev_trsase/Diguanyl_cyclase"}]},{"database":"InterPro","id":"IPR012337","properties":[{"key":"EntryName","value":"RNaseH-like_sf"}]},{"database":"InterPro","id":"IPR036397","properties":[{"key":"EntryName","value":"RNaseH_sf"}]},{"database":"InterPro","id":"IPR000477","properties":[{"key":"EntryName","value":"RT_dom"}]},{"database":"InterPro","id":"IPR041373","properties":[{"key":"EntryName","value":"RT_RNaseH"}]},{"database":"InterPro","id":"IPR056924","properties":[{"key":"EntryName","value":"SH3_Tf2-1"}]},{"database":"PANTHER","id":"PTHR37984","properties":[{"key":"EntryName","value":"PROTEIN CBG26694"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR37984:SF5","properties":[{"key":"EntryName","value":"PROTEIN NYNRIN-LIKE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00385","properties":[{"key":"EntryName","value":"Chromo"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17921","properties":[{"key":"EntryName","value":"Integrase_H2C2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF30863","properties":[{"key":"EntryName","value":"PRO_PEG10-RTL1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17917","properties":[{"key":"EntryName","value":"RT_RNaseH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00665","properties":[{"key":"EntryName","value":"rve"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00078","properties":[{"key":"EntryName","value":"RVT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24626","properties":[{"key":"EntryName","value":"SH3_Tf2-1"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00298","properties":[{"key":"EntryName","value":"CHROMO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56672","properties":[{"key":"EntryName","value":"DNA/RNA polymerases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53098","properties":[{"key":"EntryName","value":"Ribonuclease H-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00598","properties":[{"key":"EntryName","value":"CHROMO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50013","properties":[{"key":"EntryName","value":"CHROMO_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50994","properties":[{"key":"EntryName","value":"INTEGRASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50878","properties":[{"key":"EntryName","value":"RT_POL"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFMNIRFAEENDFIRWELPKPITVMNADGTPNQMGTITHCTWKMMKIGGRKTLTRFLLTGIGKENILLGMPWLKRLNPMINWETGDFWFGKDAKWPPKPTVEDAPDEEVSIFKGDGLPELITTETSPTSFGHSESIREIMTDNTERGELPAVRNDTELDDLPSESPMDQLDDDDLVISYIAGEPVIGIFEPIRKESPLTNEETETAVFTIRRGPAIGRMTHSTRSPLFCNAQNTVFYKPSGKSQELAQQAHKEASAVDKPKTVEELVPNYLHDLKSVFEKKAAERFPETRPWDHAIDLKPDFIPRDCKVYPLLLKEQGAMDDFLEENLRKGYIRPSKSPMASPFFFVGKKDGALRPCQDYRYLNEGTVKNAYPLPLISDLMDQFKGASIFTKMDLRSEYNNVRIKDGDQWKGAFKTNRGLFEPMVMFFRLCNSPATFQMMMNALFKDMIDEGWIVIYMDDILIFSNDLEEHHVRTRHVLQRLKDNDLFLKPEKCFFDVKEVEFLGMIIRENYIGMDPIKLKGIAEWPEPSTVKGVRSFLGFGNFYRKFIANFSDIAKPLTNLTRTAAGSPPFEWTTGCQTAFDTLKQRFSTAPVLLLPDKAKPFIVESDASKFATGAVLRQADINGDLHPCAYISQTLNPAERNYEIYDRELLGIIRALTEWRHYLEGSPHPVEVRSDHKNLTYFRTAQKLNRRQARWSLKLSQFDLHLIHVPGTQMIQSDALSRRNGLDDSESDNEDRVLLPNTLFVRSISPTLFDEIRNHAAKDLIVHEALEAIAHKGPFPMKSSLSDWEVRDGVILYKGKIYVPPSETLRRDLVRLHHDSPAMGHPGKFNTLELLRREFWWPGMYTFVYNYVEGCAACQQMKPNTHPTRIPLEPIPADPHALPFSCCTTDFITDLPISNGFDSIMVVVDHDLTKGVILTPCLKTITAEGTAKIFHDKVYSRFGLPDRIISDRGPQYASKVFQELNRLLQIRSSMSTAYHPQTDGETERVNQELEIYLRLYCGNNPETWADRLPDLEFCHNTREHSARKMSPFRIMMGYEPRGLPSVFPSTNIPSVESRLDMLQKIRLEALAMHELARQQMADRVRQGSPKFTLGQKVWLDSRNLKVNYASRKIAPKREGPFEIVEVIGPANYRLKLLKTWRVHSVFHAALLSPYRENDIHGPNYMNPPPDVVDNEEEYEVEAILNHKMYRGHLRYLVKWKGYSSAENSWEPTHNLQNAKRILDAYKRTRGIQ","length":1235,"molWeight":141843,"crc64":"58BAA8625136941B","md5":"A69353AA9C83FAB609F040BA0F01B8E6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Binding site":5},"uniParcId":"UPI000FE1A72C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G543","uniProtkbId":"A0A401G543_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00071648"}],"value":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012026"}],"value":"5.4.2.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00083354"}],"value":"Cofactor-independent phosphoglycerate mutase homolog"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77285.1"}],"value":"SCP_0101580"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002315"}],"value":"Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15901"},{"database":"ChEBI","id":"CHEBI:58272"},{"database":"ChEBI","id":"CHEBI:58289"}],"ecNumber":"5.4.2.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000370"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004798"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008819"}],"value":"Belongs to the BPG-independent phosphoglycerate mutase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77285.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"Metalloenzyme","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01676"}]},{"type":"Domain","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"BPG-independent PGAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06415"}]},{"type":"Active site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-1"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001492-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77285.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608198.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027752397.1"}]},{"database":"AlphaFoldDB","id":"A0A401G543","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"139825.A0A401G543","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774202","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G543","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1886626at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00186"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004619","properties":[{"key":"GoTerm","value":"F:phosphoglycerate mutase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006007","properties":[{"key":"GoTerm","value":"P:glucose catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd16010","properties":[{"key":"EntryName","value":"iPGM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1450.10:FF:000001","properties":[{"key":"EntryName","value":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.720.10:FF:000001","properties":[{"key":"EntryName","value":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.720.10","properties":[{"key":"EntryName","value":"Alkaline Phosphatase, subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1450.10","properties":[{"key":"EntryName","value":"BPG-independent phosphoglycerate mutase, domain B"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01038","properties":[{"key":"EntryName","value":"GpmI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017850","properties":[{"key":"EntryName","value":"Alkaline_phosphatase_core_sf"}]},{"database":"InterPro","id":"IPR011258","properties":[{"key":"EntryName","value":"BPG-indep_PGM_core"}]},{"database":"InterPro","id":"IPR006124","properties":[{"key":"EntryName","value":"Metalloenzyme"}]},{"database":"InterPro","id":"IPR036646","properties":[{"key":"EntryName","value":"PGAM_B_sf"}]},{"database":"InterPro","id":"IPR005995","properties":[{"key":"EntryName","value":"Pgm_bpd_ind"}]},{"database":"NCBIfam","id":"TIGR01307","properties":[{"key":"EntryName","value":"pgm_bpd_ind"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31637","properties":[{"key":"EntryName","value":"2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31637:SF0","properties":[{"key":"EntryName","value":"2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06415","properties":[{"key":"EntryName","value":"iPGM_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01676","properties":[{"key":"EntryName","value":"Metalloenzyme"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001492","properties":[{"key":"EntryName","value":"IPGAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64158","properties":[{"key":"EntryName","value":"2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53649","properties":[{"key":"EntryName","value":"Alkaline phosphatase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVEVKNKVCLIVHDGWGIAPEKNMKGDAISAGDTPNMDALAKEHNYRTLHAHGISVGLNDGLMGNSEVGHLNIGAGRIVWQDIVRIDVSIKKRQFHKNETIVASCKHAKEGNGRLHLLGLVSDGGVHSHIRHLYALLETAKEQGVPHAYIHFFGDGRDTAPRSAAGYAKELLEFIEKEKYGEIATVVGRYYAMDRDKRWERIKIAVDGLVKGVGGKGEDAVKAIEERYAKDETDEFLKPIIVNGDEGRIKDGDTLFFFNYRSDRMREIATVLGLPDKPMEVDVPKDLHISTMSRYNADFPFPVAFPPQAMTNVLAEWLSKQGIKQAHVAETEKYAHVTFFFNGGVEKQFTAEERHMIPSPKVATYDKQPKMSVQGVADKVAELVKQGKHEFVMCNFAPPDMVGHTGVYDAAVEAIGFTDKAVATVYKACEAAGYVLLVTADHGNAEQMINPETGAPHTAHTTNAVPFIMTGPKELKFAEDKKDGEEEEGALCDVAPTVLAVMGLPQPEEMTGRSLLAKAS","length":520,"molWeight":57118,"crc64":"38A3E3A7AE30664B","md5":"21FEDB605C13E190B2D24335DA8548BA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":13},"uniParcId":"UPI000FE24222"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G554","uniProtkbId":"A0A401G554_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77291.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038890"}],"value":"tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038890"}],"value":"1.3.1.88"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77291.1"}],"value":"SCP_0101640"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(16) in tRNA + NAD(+) = uridine(16) in tRNA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53380"},{"database":"Rhea","id":"RHEA-COMP:13543"},{"database":"Rhea","id":"RHEA-COMP:13544"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.88","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048934"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53382"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048934"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(16) in tRNA + NADP(+) = uridine(16) in tRNA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53376"},{"database":"Rhea","id":"RHEA-COMP:13543"},{"database":"Rhea","id":"RHEA-COMP:13544"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.88","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047652"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53378"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047652"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(17) in tRNA + NAD(+) = uridine(17) in tRNA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53372"},{"database":"Rhea","id":"RHEA-COMP:13541"},{"database":"Rhea","id":"RHEA-COMP:13542"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.88","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047287"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53374"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047287"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(17) in tRNA + NADP(+) = uridine(17) in tRNA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53368"},{"database":"Rhea","id":"RHEA-COMP:13541"},{"database":"Rhea","id":"RHEA-COMP:13542"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.88","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049467"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53370"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049467"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:69851"},{"database":"Rhea","id":"RHEA-COMP:14658"},{"database":"Rhea","id":"RHEA-COMP:17789"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048342"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:69853"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048342"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:69855"},{"database":"Rhea","id":"RHEA-COMP:14658"},{"database":"Rhea","id":"RHEA-COMP:17789"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049447"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:69857"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049447"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001917"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038313"}],"value":"Belongs to the Dus family. Dus1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77291.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"DUS-like FMN-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01207"}]},{"type":"Region","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022664"}],"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77291.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77291.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608204.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027752403.1"}]},{"database":"AlphaFoldDB","id":"A0A401G554","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401G554","properties":[{"key":"Number of interactors","value":"343"}]},{"database":"STRING","id":"139825.A0A401G554","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774208","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G554","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"272303at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0017150","properties":[{"key":"GoTerm","value":"F:tRNA dihydrouridine synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02801","properties":[{"key":"EntryName","value":"DUS_like_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR035587","properties":[{"key":"EntryName","value":"DUS-like_FMN-bd"}]},{"database":"InterPro","id":"IPR018517","properties":[{"key":"EntryName","value":"tRNA_hU_synthase_CS"}]},{"database":"PANTHER","id":"PTHR11082","properties":[{"key":"EntryName","value":"TRNA-DIHYDROURIDINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11082:SF5","properties":[{"key":"EntryName","value":"TRNA-DIHYDROURIDINE(16_17) SYNTHASE [NAD(P)(+)]-LIKE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01207","properties":[{"key":"EntryName","value":"Dus"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01136","properties":[{"key":"EntryName","value":"UPF0034"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPGVTSSDHPSKLGGYDFYRKVLGSPKYVVAPMVDQSELAWRKLSRRYGAQLAYTPMINAKMFAEGARRGFREQQFNITHGEEGGPEDRPLIVQFCGNNPAQLLASARVVEPYCDAVDINLGCPQDIARRGHYGSFLQDEWDLIYDIINMLHRNLSIPVTAKFRVFPTVEKTVEYARMLERAGAQILTCHGRVREQRGHQSGLADWDKIRAVKEAVSIPVFANGNILFHSDIERCLAATGADAVMSAEGNLYNPALFYPGPFHSLPAADDESSTPGASTSTAIAMASSGHHPPLTALAREYLEIVKRQRTPTVLSAVKGHLFKLLRPALAKETDLRAQLGRAQIPRTNSPEVWAPYEEILALLEERTERDALVAEGRPLEALVTIDEATGLPLLPHWLAQPYFRPLPPAAAATESDEEAAELSKDGPAGSKRGHPERTLEPEVAKRVKLETVAGVGAEEVAVAG","length":464,"molWeight":50825,"crc64":"5274D2D0464BBC36","md5":"23197D1BEA3FE0F6ACBB60CCC5A31384"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI000FE202F4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G571","uniProtkbId":"A0A401G571_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77316.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Acireductone dioxygenase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Acireductone dioxygenase (Fe(2+)-requiring)"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"ARD'"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Fe-ARD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"1.13.11.54"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Acireductone dioxygenase (Ni(2+)-requiring)"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"ARD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Ni-ARD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"1.13.11.53"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"ADI1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77316.1"}],"value":"SCP_0101890"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14161"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:17245"},{"database":"ChEBI","id":"CHEBI:49016"},{"database":"ChEBI","id":"CHEBI:49252"}],"ecNumber":"1.13.11.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24504"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:16723"},{"database":"ChEBI","id":"CHEBI:49252"}],"ecNumber":"1.13.11.54","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}},{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Belongs to the acireductone dioxygenase (ARD) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77316.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022596"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0533","category":"Ligand","name":"Nickel"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77316.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77316.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401G571","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401G571","properties":[{"key":"Number of interactors","value":"75"}]},{"database":"STRING","id":"139825.A0A401G571","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G571","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1867259at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00904","properties":[{"key":"RectionId","value":"UER00878"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0010308","properties":[{"key":"GoTerm","value":"F:acireductone dioxygenase (Ni2+-requiring) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010309","properties":[{"key":"GoTerm","value":"F:acireductone dioxygenase [iron(II)-requiring] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016151","properties":[{"key":"GoTerm","value":"F:nickel cation binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033353","properties":[{"key":"GoTerm","value":"P:L-methionine cycle"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02232","properties":[{"key":"EntryName","value":"cupin_ARD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.120.10:FF:000099","properties":[{"key":"EntryName","value":"1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03154","properties":[{"key":"EntryName","value":"Salvage_MtnD_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004313","properties":[{"key":"EntryName","value":"ARD"}]},{"database":"InterPro","id":"IPR027496","properties":[{"key":"EntryName","value":"ARD_euk"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"PANTHER","id":"PTHR23418","properties":[{"key":"EntryName","value":"ACIREDUCTONE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23418:SF0","properties":[{"key":"EntryName","value":"ACIREDUCTONE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03079","properties":[{"key":"EntryName","value":"ARD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRAYFMDELPGDQRLLHDSGRPATDEILSNIGVLHWHVPLDAAGEWENEINAIAAERDYKNRDIVVVNKEAMGAEFETKTKAFYHEHMHEDEEIRYILEGGGYFDVREHSSDSWIRCHLGPGDLLVLPAGIYHRFSLDMGNKSRTMRLFKDEPKWLAYNRGATTDASPYRLDYLKTLDSVATAA","length":184,"molWeight":21087,"crc64":"A7A2C2B639FCC177","md5":"8C5E094B100FF4E230CA0E8D64AC913E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":8},"uniParcId":"UPI000FE27C72"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G5F4","uniProtkbId":"A0A401G5F4_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2019-05-08","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77390.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"alpha-1,2-Mannosidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"3.2.1.-"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77390.1"}],"value":"SCP_0102630"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56008"},{"database":"Rhea","id":"RHEA-COMP:14356"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:139493"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048605"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 3 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56028"},{"database":"Rhea","id":"RHEA-COMP:14358"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:60628"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047669"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001913"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004922"}],"value":"Protein modification; protein glycosylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007658"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"Belongs to the glycosyl hydrolase 47 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77390.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":483,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Binding site","location":{"start":{"value":570,"modifier":"EXACT"},"end":{"value":570,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Disulfide bond","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77390.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77390.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608303.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027752502.1"}]},{"database":"AlphaFoldDB","id":"A0A401G5F4","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401G5F4","properties":[{"key":"Number of interactors","value":"514"}]},{"database":"STRING","id":"139825.A0A401G5F4","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774307","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G5F4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"8118055at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005783","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004571","properties":[{"key":"GoTerm","value":"F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036503","properties":[{"key":"GoTerm","value":"P:ERAD pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"Gene3D","id":"1.50.10.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012341","properties":[{"key":"EntryName","value":"6hp_glycosidase-like_sf"}]},{"database":"InterPro","id":"IPR001382","properties":[{"key":"EntryName","value":"Glyco_hydro_47"}]},{"database":"InterPro","id":"IPR050749","properties":[{"key":"EntryName","value":"Glycosyl_Hydrolase_47"}]},{"database":"InterPro","id":"IPR036026","properties":[{"key":"EntryName","value":"Seven-hairpin_glycosidases"}]},{"database":"PANTHER","id":"PTHR11742:SF55","properties":[{"key":"EntryName","value":"ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11742","properties":[{"key":"EntryName","value":"MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01532","properties":[{"key":"EntryName","value":"Glyco_hydro_47"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00747","properties":[{"key":"EntryName","value":"GLYHDRLASE47"}]},{"database":"SUPFAM","id":"SSF48225","properties":[{"key":"EntryName","value":"Seven-hairpin glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSSEPTLRKRKRATERQSSRKQKQPAGSANGHPVKFTSVLGLLLLALGFFAYQNLEAIQRYLEAWRKSADWDAATKSSGPLEFSADLPKRNAVVVAFKHAWLAYERDAMGDDEYHPIGHSGTNLTDAGGIGYTVVDSIDSMIIMGLKDEYARARNWIATNMTFDRNGEFNTFETTIRVLGGLLSAYHLTEDPVFLERAKNLADRILPAFDTPSGLPLSSVNLAKRKGVPSKDNKELVSTAEVSTLQLEFKYLSLLTEEDIYWDVVENAMKVIKAARTSMSTGLASIFMSYDEGRFTVAPIRLGSRADSYYEYLLKQYIQTDYTEPVYRTMYDDAMSSVYTHLIKKTERAGLTYTSELIPERNRQGKINWRLVPKQDHLVCFLGGSLMLGAVTTGAVVQPVSVPPLAGELSEQGKRDWTAGIELVRTCMKTHETATGLSPEIVHFKIAGDHIPESNAPEDWYIKGARPDGPNSYDARYILRPETVESLFIAFRLTGDPKYREYGWNIFQAIEKHCRVESGGYASVLNVDRLPVEHEDKMETFLMSETLKYLYLLFDDASVLPLSKYVFNTEAHPFPIFHPMRRTGFS","length":587,"molWeight":66113,"crc64":"A909F9547FEE8055","md5":"2AABA6C9FD18ACD39D96BE562ED73F25"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Active site":4,"Binding site":1,"Disulfide bond":1},"uniParcId":"UPI000FE22F52"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G5H8","uniProtkbId":"A0A401G5H8_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77425.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"value":"Sugar phosphate phosphatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"value":"3.1.3.-"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77425.1"}],"value":"SCP_0103000"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054243"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"value":"Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:35603"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:37721"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:138881"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001326"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate = dihydroxyacetone + D-glyceraldehyde 3-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28002"},{"database":"ChEBI","id":"CHEBI:16016"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:59776"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048809"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"value":"Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009519"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"value":"Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77425.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Damage-control phosphatase ARMT1-like metal-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01937"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367030"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77425.1"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77425.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77425.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77425.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_027608338.1","properties":[{"key":"NucleotideSequenceId","value":"XM_027752537.1"}]},{"database":"AlphaFoldDB","id":"A0A401G5H8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"139825.A0A401G5H8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"38774342","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G5H8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"541375at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0097023","properties":[{"key":"GoTerm","value":"F:fructose 6-phosphate aldolase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0103026","properties":[{"key":"GoTerm","value":"F:fructose-1-phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0004427","properties":[{"key":"GoTerm","value":"F:inorganic diphosphate phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006974","properties":[{"key":"GoTerm","value":"P:DNA damage response"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030643","properties":[{"key":"GoTerm","value":"P:intracellular phosphate ion homeostasis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.40.50.10880:FF:000005","properties":[{"key":"EntryName","value":"DUF89-domain-containing protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.930.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10880","properties":[{"key":"EntryName","value":"Uncharacterised protein PF01937, DUF89, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036075","properties":[{"key":"EntryName","value":"ARMT-1-like_metal-bd_sf"}]},{"database":"InterPro","id":"IPR039763","properties":[{"key":"EntryName","value":"ARMT1"}]},{"database":"InterPro","id":"IPR002791","properties":[{"key":"EntryName","value":"ARMT1-like_metal-bd"}]},{"database":"PANTHER","id":"PTHR12260","properties":[{"key":"EntryName","value":"DAMAGE-CONTROL PHOSPHATASE ARMT1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12260:SF4","properties":[{"key":"EntryName","value":"SUGAR PHOSPHATE PHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01937","properties":[{"key":"EntryName","value":"ARMT1-like_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF111321","properties":[{"key":"EntryName","value":"AF1104-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNEIIPNGAAPPINEPTKTKGMPNRMSLKLSHLPSKKDIKPVYPRTPSSIDPNNPPWPAFRGYHTYSFAYATMGHRLPTILGKAIDDVIETLNQESAEDRIVDLLKCIERMDELKDELNAHAKLRPIVDDGEADVALWNKEIAKYFQGKDFMNAPWLFAEAYKYRRLRECFSVSKYWTSYDVFFRQKCDTFARSNEAVFELSMRFAEPFKHKEGMSPAEQLEAVRLMFMELTQICLWGNSTDLSLLINMTEEQIKSLQSTGGENLAATEKNILGNDMARLWEVVRDLKGKTGGRVDFILDNAGFELYCDCVYADFLIQSGLVNQVRFHGKRYPWFVSDVTKKDWEWLLNSMVYGHLFPKATDQEKASLHRLGLRWKQYEKEGKWVYEQHPFWCTGYTYWDLHSEAPDLFLHLSRSDLVIFKGDLNHRKLTYDCAAPPSTDFEVAIGPMASASGAPKVCSMRTIKSDVVVGLGKDGDALAERLDKAEPGWKISGKYAIVLVSEGRPGEKVRFA","length":513,"molWeight":58534,"crc64":"53A826EE4B4690D2","md5":"5153C1A6ACD3828C662588A6228B6CDD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1},"uniParcId":"UPI000FE25583"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A401G5K5","uniProtkbId":"A0A401G5K5_9APHY","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-05-08","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sparassis crispa","taxonId":139825,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77437.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Polyporales","Sparassidaceae","Sparassis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"tRNA (guanine(37)-N1)-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"2.1.1.228"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"M1G-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"tRNA [GM37] methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"tRNA methyltransferase 5"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"TRM5"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77437.1"}],"value":"SCP_0103120"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine(37) in tRNA + S-adenosyl-L-methionine = N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36899"},{"database":"Rhea","id":"RHEA-COMP:10145"},{"database":"Rhea","id":"RHEA-COMP:10147"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:73542"},{"database":"ChEBI","id":"CHEBI:74269"}],"ecNumber":"2.1.1.228","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047783"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Predominantly in the mitochondria and in the nucleus"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Mitochondrion matrix","id":"SL-0170"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"value":"Belongs to the TRM5 / TYW2 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009775"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01021"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77437.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"SAM-dependent methyltransferase TRM5/TYW2-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51684"}]},{"type":"Region","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01021"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01021"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01021"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01021"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03152"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"30375506","citationType":"journal article","authors":["Kiyama R.","Furutani Y.","Kawaguchi K.","Nakanishi T."],"citationCrossReferences":[{"database":"PubMed","id":"30375506"},{"database":"DOI","id":"10.1038/s41598-018-34415-6"}],"title":"Genome sequence of the cauliflower mushroom Sparassis crispa (Hanabiratake) and its association with beneficial usage.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"16053","lastPage":"16053","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GBE77437.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000287166"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BFAD01000001","properties":[{"key":"ProteinId","value":"GBE77437.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A401G5K5","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"A0A401G5K5","properties":[{"key":"Number of interactors","value":"360"}]},{"database":"STRING","id":"139825.A0A401G5K5","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"A0A401G5K5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"408788at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000287166","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0052906","properties":[{"key":"GoTerm","value":"F:tRNA (guanine(37)-N1)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070901","properties":[{"key":"GoTerm","value":"P:mitochondrial tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0002939","properties":[{"key":"GoTerm","value":"P:tRNA N1-guanine methylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.110:FF:000001","properties":[{"key":"EntryName","value":"tRNA (guanine(37)-N1)-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.110","properties":[{"key":"EntryName","value":"Met-10+ protein-like domains"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03152","properties":[{"key":"EntryName","value":"TRM5"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR030382","properties":[{"key":"EntryName","value":"MeTrfase_TRM5/TYW2"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR056743","properties":[{"key":"EntryName","value":"TRM5-TYW2-like_MTfase"}]},{"database":"InterPro","id":"IPR056744","properties":[{"key":"EntryName","value":"TRM5/TYW2-like_N"}]},{"database":"InterPro","id":"IPR025792","properties":[{"key":"EntryName","value":"tRNA_Gua_MeTrfase_euk"}]},{"database":"PANTHER","id":"PTHR23245:SF36","properties":[{"key":"EntryName","value":"TRNA (GUANINE(37)-N1)-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23245","properties":[{"key":"EntryName","value":"TRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02475","properties":[{"key":"EntryName","value":"TRM5-TYW2_MTfase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25133","properties":[{"key":"EntryName","value":"TYW2_N_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51684","properties":[{"key":"EntryName","value":"SAM_MT_TRM5_TYW2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSIHSLIDTSPPIHRGMVALDRDAFHKPVPVLAAKITPKITGVFIRAPTLKTLLMDLPRVLPVHKAPDNDRLVLFKFSDEADLTPEAAEFLQQHSAQLVKHTLHFHYDDWNADEILNAVLPEDLSEGAPPSSFAVSGHIAHMNLRPEYYPYKYLIGQVILDKNPGIKTVVNKIDNISNQFRIFNMELLAGEPDYKVVHHEANCRFTFDFTQVYWNSRLNHEHERIVQLFSPQDVIADVFAGVGPFSIPAAKKGCGVLANDLNPKSYKYLRQNIDDNKVTQLVRPSCEDGRGFIGDVFNNIYDLPLPPVLPSEPSRSQLRRLSKQQRGSPHANPAPVDAVPLVPPRRRITHFVMNLPDSAIEFLDAFRGVLRPVFGSRDLSGLYYSTSKLPMIHCYCFAREREPESAESDIRRRVEEKLGHALGQEMSLHFVRAVAPHKQMYCISFRLPYKVAYAA","length":455,"molWeight":51497,"crc64":"57E244F6A4CA730C","md5":"A91C8E79ED42BB16E0CF73477AD6A6B0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":4},"uniParcId":"UPI000FE20077"}}]}