{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JQY5","uniProtkbId":"A0ACC1JQY5_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765502.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"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"}}],"flag":"Fragment"},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765502.1"}],"value":"GGI18_006202"}]}],"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":"KAJ2765502.1"}],"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":29,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765502.1"}]}],"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":"UP001140066"}],"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":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765502.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765502.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003957","properties":[{"key":"ProteinId","value":"KAJ2765502.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"SFTLGGGWNSFLHINSELVKLRFGANDSVAAWSASVSQIMPIFLVPFLGWFFDVFGLRTDMLVLSAGLFTVSMALLGFTMINPLVGLVIFSVSLALGPLAEITAISLILPNSSLGTGLGIYKSAMNTGSTIVDIVVGVLQDRGSKTLEETAHSYDYAMAFFVAWGLLSTFVAVTVFVVDRLKWSSLLRSNFELRREALHAVKDRINRPMVHVTASNWRDYVHPWSYTPLIVLSGTLVVSWILFAIKLA","length":248,"molWeight":27195,"crc64":"B19724533C77828D","md5":"D6DA34B36AE04B635E9C18AB1F8161A7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":5,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI0022D35BE8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JS85","uniProtkbId":"A0ACC1JS85_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766461.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"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":"KAJ2766461.1"}],"value":"GGI18_005996"}]}],"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":"KAJ2766461.1"}],"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":13,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Nudix hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00293"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"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"}],"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":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766461.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766461.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003694","properties":[{"key":"ProteinId","value":"KAJ2766461.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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: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":"PS00893","properties":[{"key":"EntryName","value":"NUDIX_BOX"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKRGFGRDKLNGFGGKVEANETIAKGAERELAEESGLVTKSIKQCGLLLFYFENDLVAMEVHVFLVDRYEGAAVETDEMRPQWFGIRDMPFELMWADDSHWWPYVLKGQKFVGQFWFKADQVTFTRHTLRAVDSLDFA","length":139,"molWeight":16090,"crc64":"64E3AF3614A96B07","md5":"FAE9EDDD95A719CF0494C83A7695BEDC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":7,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0022D2E961"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1K7B2","uniProtkbId":"A0ACC1K7B2_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2775175.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"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"}}],"flag":"Fragment"},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2775175.1"}],"value":"GGI18_004505"}]}],"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":"KAJ2775175.1"}],"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":85,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2775175.1"}]}],"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":"UP001140066"}],"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":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2775175.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2775175.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010002093","properties":[{"key":"ProteinId","value":"KAJ2775175.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRPHFLSGSSSTAGRDKDIGDAGARIPTPDQPLLDSGSSRDSFGDDGRGSLESGSEAMHRRMSSASSSGDITEFERGLGQSQRGYQVLALACALLISVGSHYSAHTLGALKSTIKKELDITNTQYGALQSTVSAVNTVLPILGGLFIDAFGTTSGSLVATFLIMLGNLIISISTHSRSFSTMVGGRILYGLGSGAITVVQETILGSWFKGKGLAITIAIQITTSRIASFLSMGTAIPVANHFGFYGAAFWANFLVCALSFGINLVYMVTMRRIHRSAPERIVSRLRSKHRFNPRLVLFFFGLYWLFIV","length":309,"molWeight":33102,"crc64":"D5F0F940431DDDF9","md5":"08C12E772E99322A3F3FCF0ECFB149F4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":5,"Domain":1,"Region":1,"Non-terminal residue":1},"uniParcId":"UPI0022CF2B46"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1K9Y8","uniProtkbId":"A0ACC1K9Y8_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2777575.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Phosphatidyl-N-methylethanolamine N-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"2.1.1.71"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Phospholipid methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"PLMT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2777575.1"}],"value":"OPI3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2777575.1"}],"value":"GGI18_004173"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32739"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64572"}],"ecNumber":"2.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051252"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32735"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64572"},{"database":"ChEBI","id":"CHEBI:64573"}],"ecNumber":"2.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052459"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11164"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64573"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"2.1.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004969"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Phospholipid metabolism; phosphatidylcholine biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Mitochondrion membrane","id":"SL-0171"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2777575.1"}],"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":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Intramembrane","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Topological domain","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Domain","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Phospholipid methyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04191"}]},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"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_03216"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"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_03216"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"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_03216"}],"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_03216"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2777575.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2777575.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010001790","properties":[{"key":"ProteinId","value":"KAJ2777575.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0031966","properties":[{"key":"GoTerm","value":"C:mitochondrial membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000773","properties":[{"key":"GoTerm","value":"F:phosphatidyl-N-methylethanolamine N-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004608","properties":[{"key":"GoTerm","value":"F:phosphatidylethanolamine N-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006656","properties":[{"key":"GoTerm","value":"P:phosphatidylcholine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.120.1630:FF:000005","properties":[{"key":"EntryName","value":"Phosphatidylethanolamine N-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.1630","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03216","properties":[{"key":"EntryName","value":"PLMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024960","properties":[{"key":"EntryName","value":"PEMT/MFAP"}]},{"database":"InterPro","id":"IPR007318","properties":[{"key":"EntryName","value":"Phopholipid_MeTrfase"}]},{"database":"PANTHER","id":"PTHR15458","properties":[{"key":"EntryName","value":"PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15458:SF5","properties":[{"key":"EntryName","value":"PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04191","properties":[{"key":"EntryName","value":"PEMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005444","properties":[{"key":"EntryName","value":"PEMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51599","properties":[{"key":"EntryName","value":"SAM_PEMT_PEM2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLVDFSQASLWLALASITFNPTAWNVAARREHHTRWLTNLCGGARQGCYAIAVAIFSMGILRDALYNQALNDQPSAPWLDNSLVRLVAALLFISGMTFVTTSTYALGITGTFLGDYFGILMKERVTGFPFNVLDNPMYVGSTLSFLGTALWHAKPAGLLITVYVWLVYWVALQFEGPFTAMIYENASKNVKSPELGQKKKKKL","length":203,"molWeight":22510,"crc64":"55F62A8F70F3D950","md5":"4347CEAE4BD501464A1637546B96B407"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Topological domain":5,"Intramembrane":1,"Transmembrane":3,"Domain":1,"Binding site":2},"uniParcId":"UPI0022D7B0AB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KC49","uniProtkbId":"A0ACC1KC49_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Inosine triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"ITPase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Inosine triphosphatase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"3.6.1.66"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Non-canonical purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Non-standard purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleoside-triphosphate diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleoside-triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"NTPase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"XTP/dITP diphosphatase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"}],"value":"HAM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"}],"value":"GGI18_003407"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054940"}],"value":"Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ITP + H2O = IMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:61402"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093218"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:29400"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093218"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-hydroxy-dATP + H2O = N(6)-hydroxy-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83971"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:233529"},{"database":"ChEBI","id":"CHEBI:233530"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093271"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:83972"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093271"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XTP + H2O = XMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28610"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:61314"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dITP + H2O = dIMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28342"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61194"},{"database":"ChEBI","id":"CHEBI:61382"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093255"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:28343"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093255"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008023"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003781"}],"value":"Belongs to the HAM1 NTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"}],"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":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2784590.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010001172","properties":[{"key":"ProteinId","value":"KAJ2784590.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0035870","properties":[{"key":"GoTerm","value":"F:dITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036220","properties":[{"key":"GoTerm","value":"F:ITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036222","properties":[{"key":"GoTerm","value":"F:XTP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009204","properties":[{"key":"GoTerm","value":"P:deoxyribonucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009143","properties":[{"key":"GoTerm","value":"P:nucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00515","properties":[{"key":"EntryName","value":"HAM1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.950.10:FF:000003","properties":[{"key":"EntryName","value":"Inosine triphosphate pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.950.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03148","properties":[{"key":"EntryName","value":"HAM1_NTPase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027502","properties":[{"key":"EntryName","value":"ITPase"}]},{"database":"InterPro","id":"IPR029001","properties":[{"key":"EntryName","value":"ITPase-like_fam"}]},{"database":"InterPro","id":"IPR002637","properties":[{"key":"EntryName","value":"RdgB/HAM1"}]},{"database":"NCBIfam","id":"TIGR00042","properties":[{"key":"EntryName","value":"RdgB/HAM1 family non-canonical purine NTP pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067:SF9","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01725","properties":[{"key":"EntryName","value":"Ham1p_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52972","properties":[{"key":"EntryName","value":"ITPase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALRKLTFVTGNVNKLREMQELLHGIVDLHNTPVDLEEIQGSTQEVAIAKCRQAAAIIGGPVITEDVGLGFNAMNGLPGAYIKWFLKELKPAGLHKMLAGFEDKSGFAVCTVAYCAGPNHEPILFEGIHHGTIVEPRGPQVFGWNPVFQPDGHSETYAEMSDELKNKCSHRFLAVEKLKAFLSEQRD","length":187,"molWeight":20598,"crc64":"96A9B8C779A70041","md5":"C0D3C2F9E6C9E7B4B5CA91D2BCE15A2F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Binding site":7},"uniParcId":"UPI0022DAEDB3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KHP6","uniProtkbId":"A0ACC1KHP6_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2790074.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022255"}],"value":"Histone acetyltransferase ESA1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074445"}],"value":"Histone acetyltransferase esa1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031065"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075313"}],"value":"protein 2-hydroxyisobutyryltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031553"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076782"}],"value":"protein acetyltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031133"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077673"}],"value":"protein crotonyltransferase ESA1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2790074.1"}],"value":"ESA1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2790074.1"}],"value":"GGI18_002025"}]}],"comments":[{"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":"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":"KAJ2790074.1"}],"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":199,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":375,"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":379,"modifier":"EXACT"},"end":{"value":379,"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":"Binding site","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":455,"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":299,"modifier":"EXACT"},"end":{"value":299,"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:0000313","source":"EMBL","id":"KAJ2790074.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"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:0000313","source":"Proteomes","id":"UP001140066"}],"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":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2790074.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2790074.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000415","properties":[{"key":"ProteinId","value":"KAJ2790074.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0035267","properties":[{"key":"GoTerm","value":"C:NuA4 histone acetyltransferase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010485","properties":[{"key":"GoTerm","value":"F:histone H4 acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006974","properties":[{"key":"GoTerm","value":"P:DNA damage response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"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:000526","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":"MGGGSRPGTPSSMGGGASGGSGSVGPKAEPVTVSIVSGAAMLSIGCKAFFEKDGEIRQAEILSIRDKAKRQIIQRTADDAPIDNSDGTVEYEFYVHYVEFNKRLDEWVIDTRARLDKPVTFPKKKNKATIAGTQQSVRDKRRKTNIGGSVAAGSVPQTPEAIRHDDSVYTAPVETFSKEKEIEKLRTQGSMTQSTSEVARMKNLNIIEMGQFQVEPWYFSPYPLEYAYTPTLYICEFCLCFYANRTQYGRHRTKCTLQHPPGNEIYRKDEISFFEIDGRRQKTYCRNLCLLSKCFLDHKTLYYDVDPFLFYILTKRDERGCHIIGYFSKEKESADNYNLACILTLPQYQRMGFGRVLIQFSYELSKAEGKVGSPEKPLSDLGLLSYRTYWSEILVDVLIGYDGEISIDELSHITSFTTQDIMHALFNLDALRYYHGQHCIVLSERVVEAYDRFQKKKHRKIDSGCLKWSPKVFSQAELRYL","length":481,"molWeight":54812,"crc64":"7BE8DF53ADA24E4A","md5":"B3B28B0E13AF98A93B5C59230EBBAD97"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":2,"Modified residue":1},"uniParcId":"UPI0022D6AD5E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KKM1","uniProtkbId":"A0ACC1KKM1_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"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":"KAJ2791145.1"}],"value":"GGI18_001343"}]}],"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":"KAJ2791145.1"}],"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":40,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":444,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":554,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]}],"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":"UP001140066"}],"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":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791145.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791145.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000194","properties":[{"key":"ProteinId","value":"KAJ2791145.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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":"MTAKPNTKVPNIGGKRMGSSLMSPLKSTLKHDLEINNTQWASLISMVWVVGTVSPFIAGLLIDTMGAPLAGALSISLILIGNGVCAIAVGTKSVNAFLIGRAIYSTGGGAVLLVGEVIMLKWFKQKQLPLAFGCASTIGGLFSFSGPAAVTAILSRHANVAIPFWLATGLSGFGLVCFGAYALIHYSHYAQDIELVNQCPVDHIDIQDKRTSNGGKTNGQGTSLQSLEYASAVETQDSKLLVVPSQESGVYVGTEQRRHPKMHSAISLSIASKPESPEGQPGVAARTWLKSKQLFLDLSSLPEAYWHVLLCITVQGTLFIPLHEIVPEMMETEWGYSRAESSKLFVYLHIIPIVLHICLGVFINKVGHRLNLFLVGSMFVFLASIFITFVRQVPIMLSLVMMNLSGSMVPASIFSMMNLVIDNDEIAGAALGLIRSAEFASVTLMEMLDGLLQDADHNRYDTVLIGLVVFAGILLLVAIASLVVDYTLNNGVLNSANPYVSSRSSTSPSYTDCAADKVQVTKTRATSTNSEESSTRASLGLAARGLNRIPKRRFVYMGTIGLLLATAWTLFIMSLTRI","length":578,"molWeight":62179,"crc64":"6318BBC423A85B6B","md5":"6830480428F661911473ABC630015548"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":12},"uniParcId":"UPI0022D4BE2F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KM08","uniProtkbId":"A0ACC1KM08_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00020932"}],"value":"1,4-alpha-glucan-branching enzyme"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012541"}],"value":"2.4.1.18"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012511"}],"value":"2.7.7.79"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031979"}],"value":"Glycogen-branching enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032480"}],"value":"tRNA-histidine guanylyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}],"value":"GLC3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}],"value":"GGI18_000867"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002939"}],"value":"Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049618"}],"value":"Glycogen-branching enzyme participates in the glycogen biosynthetic process along with glycogenin and glycogen synthase. Generates alpha-1,6-glucosidic branches from alpha-1,4-linked glucose chains, to increase solubility of the glycogen polymer"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.","ecNumber":"2.4.1.18","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000826"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 5'-end ribonucleotide-tRNA(His) + GTP + ATP + H2O = a 5'-end phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54564"},{"database":"Rhea","id":"RHEA-COMP:14193"},{"database":"Rhea","id":"RHEA-COMP:14917"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:138282"},{"database":"ChEBI","id":"CHEBI:141847"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.7.79","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047281"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004964"}],"value":"Glycan biosynthesis; glycogen biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009000"}],"value":"Belongs to the glycosyl hydrolase 13 family. GlgB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010113"}],"value":"Belongs to the tRNA(His) guanylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}],"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":774,"modifier":"EXACT"},"end":{"value":1093,"modifier":"EXACT"}},"description":"Glycosyl hydrolase family 13 catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00642"}]},{"type":"Region","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":594,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":528,"modifier":"EXACT"},"end":{"value":570,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023056"}],"id":"KW-0320","category":"Biological process","name":"Glycogen biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"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":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791821.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000092","properties":[{"key":"ProteinId","value":"KAJ2791821.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0003844","properties":[{"key":"GoTerm","value":"F:1,4-alpha-glucan branching enzyme activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004553","properties":[{"key":"GoTerm","value":"F:hydrolase activity, hydrolyzing O-glycosyl compounds"},{"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:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008193","properties":[{"key":"GoTerm","value":"F:tRNA guanylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006520","properties":[{"key":"GoTerm","value":"P:amino acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005978","properties":[{"key":"GoTerm","value":"P:glycogen biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006400","properties":[{"key":"GoTerm","value":"P:tRNA modification"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd11321","properties":[{"key":"EntryName","value":"AmyAc_bac_euk_BE"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02854","properties":[{"key":"EntryName","value":"E_set_GBE_euk_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.80:FF:000001","properties":[{"key":"EntryName","value":"1,4-alpha-glucan branching enzyme"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.1180:FF:000003","properties":[{"key":"EntryName","value":"1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.3000:FF:000001","properties":[{"key":"EntryName","value":"tRNA(His) guanylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.3000","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1180","properties":[{"key":"EntryName","value":"Golgi alpha-mannosidase II"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006048","properties":[{"key":"EntryName","value":"A-amylase/branching_C"}]},{"database":"InterPro","id":"IPR006047","properties":[{"key":"EntryName","value":"GH13_cat_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR004193","properties":[{"key":"EntryName","value":"Glyco_hydro_13_N"}]},{"database":"InterPro","id":"IPR013780","properties":[{"key":"EntryName","value":"Glyco_hydro_b"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR014756","properties":[{"key":"EntryName","value":"Ig_E-set"}]},{"database":"InterPro","id":"IPR000634","properties":[{"key":"EntryName","value":"Ser/Thr_deHydtase_PyrdxlP-BS"}]},{"database":"InterPro","id":"IPR025845","properties":[{"key":"EntryName","value":"Thg1_C_dom"}]},{"database":"InterPro","id":"IPR024956","properties":[{"key":"EntryName","value":"tRNAHis_GuaTrfase_cat"}]},{"database":"InterPro","id":"IPR038469","properties":[{"key":"EntryName","value":"tRNAHis_GuaTrfase_Thg1_sf"}]},{"database":"InterPro","id":"IPR001926","properties":[{"key":"EntryName","value":"TrpB-like_PALP"}]},{"database":"InterPro","id":"IPR036052","properties":[{"key":"EntryName","value":"TrpB-like_PALP_sf"}]},{"database":"PANTHER","id":"PTHR43651","properties":[{"key":"EntryName","value":"1,4-ALPHA-GLUCAN-BRANCHING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43651:SF3","properties":[{"key":"EntryName","value":"1,4-ALPHA-GLUCAN-BRANCHING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00128","properties":[{"key":"EntryName","value":"Alpha-amylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02806","properties":[{"key":"EntryName","value":"Alpha-amylase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02922","properties":[{"key":"EntryName","value":"CBM_48"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00291","properties":[{"key":"EntryName","value":"PALP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04446","properties":[{"key":"EntryName","value":"Thg1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14413","properties":[{"key":"EntryName","value":"Thg1C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00642","properties":[{"key":"EntryName","value":"Aamy"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81296","properties":[{"key":"EntryName","value":"E set domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51011","properties":[{"key":"EntryName","value":"Glycosyl hydrolase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53686","properties":[{"key":"EntryName","value":"Tryptophan synthase beta subunit-like PLP-dependent enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00165","properties":[{"key":"EntryName","value":"DEHYDRATASE_SER_THR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLSQGGAPLTADSGRPLLHTPTPLLYSASMSKLAGCNVWLKLENMQPTQSFKIRGLGYTCIKAALEQGAKLFVAVGDSNAALAVAYSGRRLGVPVTVFVPSGVQPSAVRAKIELEGACIQEGGRSIKDAYEAACALVRQTEGAVLVDKADDAAAIAGNATIVPEINVQLQRQAPAAIITAVGSGGLLSGLITGLGHCHWQQVPVIAVETHNTNTFQQALLFDSAHSSDSDTAADAGSDGPADHMKASAQPSLLPPLDEDADSKYTYVRDFEREERLLPATWLVVRIDGQGFTGFTTKHGFTKPNDIRALHLMNRAAKVVMESMVEIVLAYGESDEYSFVFSKKAKAYDRRTSKIITLLVSKFTAAYVFYWSEFFPATPLQFPPAFDGRVVVYPSDRIMRDYLCWRQADCHINNMYNTCFWLLVNQGGMSQRDAEKRLNGTLSRDKHELLFSEFGVNYNNELEIFKKGSVLVRELTPIDVVDKDGKSVQRQKMVVQIQHCDIIGDAFWREHPEILSKAEVSMPAKKKSTSGNKAKQQDNPLSTSSSTQDLAESHSGISTPGSPALQDNFTGPPTRVADSSYLTGSDPEISGDGTDVIKTDGYLEDHRAYFGQRFAHFKRWVRDIELNEGGIDKFSRGYEKFGLHVTAEGVSYREWAPGAREASLVGDFNGWDVAANPLTRNEYGVWETVVPNTESGEVAIAHGSHIKVTFITDKGERVYRLPAWSRYVTQDLSKSPIYESVFYNPPNKYEFKHKRLVPPADLRIYEAHVGISSPEARVATFKEFTQNVLPMISDLGYNAVQLMAVMEHAYYASFGYQVTSFFAPSSRYGEPDDLRELVDTAHSLGIVVFLDVVHSHACNNVEDGLNQFDGTDHCYFHEGGRGRHELWNSRLFNYGHHEVTRFLLSNLRYWIEEFGFDGFRFDGVTSMMYKHHGIAYGFSGHYNEYFGGNTDEEAVVYLMLANYMCHKLYPGFVTIAEDVSGMPAMCRSVQEGGVGFDYRLTMSVPDMWIKLLKESKDEDWSMDHIAHQLTNRRYQERAITYCESHDQALVGDKTLAFWMMDKEMYTNMSDHTHLTPVIERGMALHKMIRLVTCGLGGEGYLTFEGNEFGHPEWLDFPREGNGSSFHYARRQFNLVKDENLRYKYLYRFDKAMMHLEQQHKWLSGHDQWVTLKHEGDKVLAFERGGLVWIFNFHPTNSYTDYRVGAGWAGKYMVALSTDDHEFLGQGRVAHDTEHFSTPMEWNGRPNYIQVYLPARTAVVLRHFN","length":1263,"molWeight":141895,"crc64":"CE31C87766CBFFE0","md5":"D51467BFA9B1C6501EA938A808A9457F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2},"uniParcId":"UPI0022D5D2AD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KM45","uniProtkbId":"A0ACC1KM45_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791872.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"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":"KAJ2791872.1"}],"value":"GGI18_000826"}]}],"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":"KAJ2791872.1"}],"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":43,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":412,"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":"UP001140066"}],"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":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791872.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2791872.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000085","properties":[{"key":"ProteinId","value":"KAJ2791872.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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":"MFTALASSRRLAQPLVLRSVRAFTASTIAKQDAFVPKSLHTLSEDEEMMKDAVSRFAREVVQPRVSSMDEAETMEPSVIRGLFDAGLMGVETPVELGGAGASFTSAIVVVEELAKIDPSVSVLCDVHNTLVNTVFRTYASSFLQEKYLPALSTSALGCFCLSEPTAGSDAFALQTRATADGTDYVLNGAKMWITNSNEADVFLVFATIDPTLGYRGITCFVVDRNAPGLTVAKKEKKLGIRASSTCQVSFDDVRVPASHVIGEVGKGYKIAIEILNEGRIGIAAQMLGLAQGAFDHVMPYLFQRKQFGSRIGDFQAMQHQYAQIATEIEAARLLTYNAARMKEEGKPFAREAAMAKLYASQVAERAASKAVEWMGGVGFTRDMPVEKYYRDCKIGAIYEGTSNIQLQTIAKILAKQYQE","length":419,"molWeight":45631,"crc64":"77A6549AE8E65AED","md5":"89903FCA547D092DA5A2CEE4B874546D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0022D40D19"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KML2","uniProtkbId":"A0ACC1KML2_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792050.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00071938"}],"value":"Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013012"}],"value":"1.1.1.41"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032920"}],"value":"Beta'-coat protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030683"}],"value":"Isocitric dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030631"}],"value":"NAD(+)-specific ICDH"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792050.1"}],"value":"SEC27"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792050.1"}],"value":"GGI18_000692"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025536"}],"value":"The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23632"},{"database":"ChEBI","id":"CHEBI:15562"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.41","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000837"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011567"}],"value":"Octamer of two non-identical subunits IDH1 and IDH2"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004347"}],"value":"Cytoplasmic vesicle, COPI-coated vesicle membrane","id":"SL-0076"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004347"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004347"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004255"}],"value":"Golgi apparatus membrane","id":"SL-0134"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004255"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004255"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004173"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010844"}],"value":"Belongs to the WD repeat COPB2 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007769"}],"value":"Belongs to the isocitrate and isopropylmalate dehydrogenases family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792050.1"}],"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":"Repeat","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]},{"type":"Repeat","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]},{"type":"Repeat","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]},{"type":"Repeat","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]},{"type":"Repeat","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]},{"type":"Domain","location":{"start":{"value":799,"modifier":"EXACT"},"end":{"value":1122,"modifier":"EXACT"}},"description":"Isopropylmalate dehydrogenase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01329"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023329"}],"id":"KW-0968","category":"Cellular component","name":"Cytoplasmic vesicle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022892"}],"id":"KW-0931","category":"Biological process","name":"ER-Golgi transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023034"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022927"}],"id":"KW-0653","category":"Biological process","name":"Protein transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"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":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022532"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022574"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}],"id":"KW-0853","category":"Domain","name":"WD repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792050.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792050.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000061","properties":[{"key":"ProteinId","value":"KAJ2792050.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030663","properties":[{"key":"GoTerm","value":"C:COPI-coated vesicle 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:0030117","properties":[{"key":"GoTerm","value":"C:membrane coat"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004449","properties":[{"key":"GoTerm","value":"F:isocitrate dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005198","properties":[{"key":"GoTerm","value":"F:structural molecule activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006886","properties":[{"key":"GoTerm","value":"P:intracellular protein transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006102","properties":[{"key":"GoTerm","value":"P:isocitrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006099","properties":[{"key":"GoTerm","value":"P:tricarboxylic acid cycle"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016192","properties":[{"key":"GoTerm","value":"P:vesicle-mediated transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd22947","properties":[{"key":"EntryName","value":"Coatomer_WDAD_beta-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00200","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.130.10.10:FF:000016","properties":[{"key":"EntryName","value":"Coatomer alpha subunit, putative"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.25.40.470:FF:000001","properties":[{"key":"EntryName","value":"Coatomer subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.718.10:FF:000001","properties":[{"key":"EntryName","value":"Isocitrate dehydrogenase [NAD] subunit, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.25.40.470","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.718.10","properties":[{"key":"EntryName","value":"Isopropylmalate Dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.130.10.10","properties":[{"key":"EntryName","value":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006692","properties":[{"key":"EntryName","value":"Beta-prop_COPA/B_2nd"}]},{"database":"InterPro","id":"IPR019818","properties":[{"key":"EntryName","value":"IsoCit/isopropylmalate_DH_CS"}]},{"database":"InterPro","id":"IPR004434","properties":[{"key":"EntryName","value":"Isocitrate_DH_NAD"}]},{"database":"InterPro","id":"IPR024084","properties":[{"key":"EntryName","value":"IsoPropMal-DH-like_dom"}]},{"database":"InterPro","id":"IPR056176","properties":[{"key":"EntryName","value":"TPR_COPA_B"}]},{"database":"InterPro","id":"IPR015943","properties":[{"key":"EntryName","value":"WD40/YVTN_repeat-like_dom_sf"}]},{"database":"InterPro","id":"IPR020472","properties":[{"key":"EntryName","value":"WD40_PAC1"}]},{"database":"InterPro","id":"IPR036322","properties":[{"key":"EntryName","value":"WD40_repeat_dom_sf"}]},{"database":"InterPro","id":"IPR001680","properties":[{"key":"EntryName","value":"WD40_rpt"}]},{"database":"NCBIfam","id":"TIGR00175","properties":[{"key":"EntryName","value":"mito_nad_idh"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11835","properties":[{"key":"EntryName","value":"DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11835:SF42","properties":[{"key":"EntryName","value":"ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT BETA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04053","properties":[{"key":"EntryName","value":"B-prop_COPA_B_2nd"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00180","properties":[{"key":"EntryName","value":"Iso_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23953","properties":[{"key":"EntryName","value":"TPR_COPA_B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00400","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"5"}]},{"database":"PRINTS","id":"PR00320","properties":[{"key":"EntryName","value":"GPROTEINBRPT"}]},{"database":"SMART","id":"SM01329","properties":[{"key":"EntryName","value":"Iso_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00320","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"6"}]},{"database":"SUPFAM","id":"SSF53659","properties":[{"key":"EntryName","value":"Isocitrate/Isopropylmalate dehydrogenase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50978","properties":[{"key":"EntryName","value":"WD40 repeat-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00470","properties":[{"key":"EntryName","value":"IDH_IMDH"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50082","properties":[{"key":"EntryName","value":"WD_REPEATS_2"},{"key":"MatchStatus","value":"5"}]},{"database":"PROSITE","id":"PS50294","properties":[{"key":"EntryName","value":"WD_REPEATS_REGION"},{"key":"MatchStatus","value":"3"}]}],"sequence":{"value":"MRLDIKRKLSARTDRVKSVDMHPVEPWVLASLYSGQVHIWNYETQAQVKTFEVSDLPVRAAKFIARKNWIITGSDDMQLRVYNYNTHERVTAFDAHQDYIRCIAVHPTLPYVLTGSDDMSIKLWDWEKNWKCVQMFEGHTYFVMGLSINPKDTNTFASASLDKTIKVWSLGSPVPNYTIEGHAKGVNAVDYYHGSDKPYLASGADDFFGKVWDYQNNSCVQTLEGHSQNVVTVAFHPTLPIILTGSEDGTCRIWNSSTYRMESSLNYGMDRVWAIGYGHHSNTVAIGHEEGVVVLSLGRDDPAVSMDTSGRIIWSKHNEIRSANVKASMDSGLGDGERIMLSVKDLGSCEVYPYTLKHSPNGRFVVVCGDGEYIIYTALAWRNKSFGSGQEFVWAQNSNEYAVRESSSSIRIFKSFKEKARPATSALTTLGYAAEEIFGGCLLGVRGSGGTLTLYDWETEQIVRRIDVEAKSIYWSESGELFAVATEDSYFVLRLNRDAFAEYSQQNGGATGDEGVEDAIEFVTEIQESVKSGCWIGDCFIYTSTANRLNYLVGGQVFTISHFDTSMTMLGYVARDNRIYLADKEVGVVSYVLPLPVIEYQTAILRGDLDMAQGLLPSIPSDQRSKIAQFLEAEDMKELALEVTTDPEQRFDLAVQLNQLETAYALAEESDAEAKWRIVGDCALRTWNFDLAERCMVKAKDLSGLLLLYTSSGNATGMSKLAEMAEAAGANNIAFACYQSLKQDEKCLELLLRIDRIPEAALFARTYLPDKVASRLAARNMGTVVEDSVGPKCYGGTYTVTLIPGDGIGQETAAAVKSVFGAAKVPVEFEQFDLSGFTPENDKLMQEALASLRRNKVGLKGILYTPIRLGHSSFNVAMRKELDIYASVAHCKNIPGINARHKDVDFVIIRENTEGEYSGLEHQSFPGVVESLKIITRPKTERIARYAFDYALRHGRKRVTIVHKANIMKLADGLFLNTCRAVAKEYPTIQHNDMIVDNTAMQLVSKPQQFDVMVMPNLYGSIVSNIGAGLIGGPGIVPGANYGREFAIFEPGSRHVAKDIQGRNTANPSSLILSSVMMLRHLQLNEHADQIEKAVNKTLSVDGIRTPDLGGSQSTTDFTKAVIRNL","length":1126,"molWeight":124873,"crc64":"BF99D5FC2C79B9DF","md5":"29C28F65F54ED973156169B214883485"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Repeat":5,"Domain":1},"uniParcId":"UPI0022DB8E66"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KN00","uniProtkbId":"A0ACC1KN00_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792225.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"ATP-sulfurylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"SAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792225.1"}],"value":"MET3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792225.1"}],"value":"GGI18_000574"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Homohexamer. Dimer of trimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the N-terminal section; belongs to the sulfate adenylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792225.1"}],"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":4,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"ATP-sulfurylase PUA-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14306"}]},{"type":"Domain","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Sulphate adenylyltransferase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01747"}]},{"type":"Domain","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":547,"modifier":"EXACT"}},"description":"APS kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01583"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"N-terminal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Region","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":574,"modifier":"EXACT"}},"description":"Allosteric regulation domain; adenylyl-sulfate kinase-like","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Induces change in substrate recognition on ATP binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0198","category":"Biological process","name":"Cysteine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"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_03106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792225.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792225.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000044","properties":[{"key":"ProteinId","value":"KAJ2792225.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00517","properties":[{"key":"EntryName","value":"ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000802","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000052","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"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":"3.10.400.10","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03106","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR025980","properties":[{"key":"EntryName","value":"ATP-Sase_PUA-like_dom"}]},{"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":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR027535","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"}]},{"database":"InterPro","id":"IPR050512","properties":[{"key":"EntryName","value":"Sulf_AdTrans/APS_kinase"}]},{"database":"InterPro","id":"IPR024951","properties":[{"key":"EntryName","value":"Sulfurylase_cat_dom"}]},{"database":"InterPro","id":"IPR002650","properties":[{"key":"EntryName","value":"Sulphate_adenylyltransferase"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004040","properties":[{"key":"EntryName","value":"PRK05537.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00339","properties":[{"key":"EntryName","value":"sopT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700:SF1","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01747","properties":[{"key":"EntryName","value":"ATP-sulfurylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14306","properties":[{"key":"EntryName","value":"PUA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"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"}]}],"sequence":{"value":"MANSPHGGVLKDLYIRDEPLKATLQAEAETLPHVVLTERQLCDLELILNGGFSPLQGFHTQAEYTSVVTTSRLPSGALWTIPIYLDIDRAHLDTLGAVPGSRLTLRDPRDDQPLAIITISDIYTVDRTQEALQVYGTTDEAHPAVHYLRHNTRDTLVGGDVQAVNAPQHYDYVAIRRSPNEVRQLFKKLNWTRVVAFQTRNPMHRAHRELTVRAARMRHANVLIQPVVGLTKPGDIDHFTRVRVYQAIMPKYPNGMAQLSLLPLAMRMGGPREAVWHAIIRKNFGATHFIVGRDHAGPGSNSQGVDFYGPYEAQDLVLKYRDELDIEVVPFQMLTYLPDTDEYQPINEVAEGVKTLNISGTELRRRLKTGAPIPEWFSYPEVVRILREANPPRDHQGFTVFLTGLHASGKESIARALQVALNQEGGRSVSLLLGETIRQELSSELGYTKRERDINVARIGFVAAELTRSGAACIAAPIAPYDEARQQVRKQVARAGGFYLVHVATPLEACIKNDRAGVYARAIAGDIKGFTGIDDVYEAPSNADLVADVTKTSISQIVHEIILLLERDGYIGDR","length":574,"molWeight":63816,"crc64":"4DACCAA485FD5ACF","md5":"C11B2BB985E55FF8B96AEC0E0B99971C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Active site":3,"Binding site":7,"Site":3},"uniParcId":"UPI0022D6C7A9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KN77","uniProtkbId":"A0ACC1KN77_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792122.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012639"}],"value":"ATP citrate synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012639"}],"value":"2.3.3.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030151"}],"value":"ATP-citrate (pro-S-)-lyase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076189"}],"value":"ATP-citrate (pro-S-)-lyase 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030982"}],"value":"Citrate cleavage enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00083544"}],"value":"Citrate cleavage enzyme subunit 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792122.1"}],"value":"acl1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792122.1"}],"value":"GGI18_000642"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093367"}],"value":"Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054002"}],"value":"Catalyzes the formation of cytosolic acetyl-CoA, which is mainly used for the biosynthesis of fatty acids and sterols"}],"commentType":"FUNCTION"},{"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":"oxaloacetate + acetyl-CoA + ADP + phosphate = citrate + ATP + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21160"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:16947"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.3.3.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047593"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062455"}],"value":"Composed of two subunits"}],"commentType":"SUBUNIT"},{"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":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"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":"ARBA","id":"ARBA00060724"}],"value":"Belongs to the succinate/malate CoA ligase alpha subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005899"}],"value":"In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010719"}],"value":"In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit 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":"KAJ2792122.1"}],"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":1154,"modifier":"EXACT"},"end":{"value":1415,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Domain","location":{"start":{"value":1416,"modifier":"EXACT"},"end":{"value":1485,"modifier":"EXACT"}},"description":"AGC-kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51285"}]},{"type":"Active site","location":{"start":{"value":1277,"modifier":"EXACT"},"end":{"value":1277,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":1183,"modifier":"EXACT"},"end":{"value":1183,"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":1475,"modifier":"EXACT"},"end":{"value":1475,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792122.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"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":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"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":"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:0000313","source":"EMBL","id":"KAJ2792122.1"}],"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":"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":"UP001140066"}],"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":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792122.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792122.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000052","properties":[{"key":"ProteinId","value":"KAJ2792122.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003878","properties":[{"key":"GoTerm","value":"F:ATP citrate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006085","properties":[{"key":"GoTerm","value":"P:acetyl-CoA biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06100","properties":[{"key":"EntryName","value":"CCL_ACL-C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05123","properties":[{"key":"EntryName","value":"STKc_AGC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.261:FF:000003","properties":[{"key":"EntryName","value":"ATP-citrate synthase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.261:FF:000004","properties":[{"key":"EntryName","value":"ATP-citrate synthase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.230.10:FF:000005","properties":[{"key":"EntryName","value":"ATP-citrate synthase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.110:FF:000003","properties":[{"key":"EntryName","value":"ATP-citrate synthase subunit 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000024","properties":[{"key":"EntryName","value":"Probable ATP-citrate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000469","properties":[{"key":"EntryName","value":"Serine/threonine-protein kinase 32B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.110","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.230.10","properties":[{"key":"EntryName","value":"Cytochrome P450-Terp, domain 2"},{"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":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.261","properties":[{"key":"EntryName","value":"Succinyl-CoA synthetase domains"},{"key":"MatchStatus","value":"2"}]},{"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":"IPR017440","properties":[{"key":"EntryName","value":"Cit_synth/succinyl-CoA_lig_AS"}]},{"database":"InterPro","id":"IPR032263","properties":[{"key":"EntryName","value":"Citrate-bd"}]},{"database":"InterPro","id":"IPR016143","properties":[{"key":"EntryName","value":"Citrate_synth-like_sm_a-sub"}]},{"database":"InterPro","id":"IPR056749","properties":[{"key":"EntryName","value":"Citrate_synth_N"}]},{"database":"InterPro","id":"IPR002020","properties":[{"key":"EntryName","value":"Citrate_synthase"}]},{"database":"InterPro","id":"IPR036969","properties":[{"key":"EntryName","value":"Citrate_synthase_sf"}]},{"database":"InterPro","id":"IPR033847","properties":[{"key":"EntryName","value":"Citrt_syn/SCS-alpha_CS"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"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":"InterPro","id":"IPR045270","properties":[{"key":"EntryName","value":"STKc_AGC"}]},{"database":"InterPro","id":"IPR017866","properties":[{"key":"EntryName","value":"Succ-CoA_synthase_bsu_CS"}]},{"database":"InterPro","id":"IPR005811","properties":[{"key":"EntryName","value":"SUCC_ACL_C"}]},{"database":"InterPro","id":"IPR016102","properties":[{"key":"EntryName","value":"Succinyl-CoA_synth-like"}]},{"database":"PANTHER","id":"PTHR23118","properties":[{"key":"EntryName","value":"ATP-CITRATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23118:SF42","properties":[{"key":"EntryName","value":"ATP-CITRATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16114","properties":[{"key":"EntryName","value":"Citrate_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00285","properties":[{"key":"EntryName","value":"Citrate_synt"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24948","properties":[{"key":"EntryName","value":"Citrate_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00549","properties":[{"key":"EntryName","value":"Ligase_CoA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48256","properties":[{"key":"EntryName","value":"Citrate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-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":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52210","properties":[{"key":"EntryName","value":"Succinyl-CoA synthetase domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51285","properties":[{"key":"EntryName","value":"AGC_KINASE_CTER"},{"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":"PS01216","properties":[{"key":"EntryName","value":"SUCCINYL_COA_LIG_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00399","properties":[{"key":"EntryName","value":"SUCCINYL_COA_LIG_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01217","properties":[{"key":"EntryName","value":"SUCCINYL_COA_LIG_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSAKAIREYDGKLLLAHYLQQSPSMAAAQPTAAFAQPQTRLAQVNLSEVSTADASDKISAAVEAALSRAERLNPWLTSTKLVAKPDQLIKRRGKSGLLLLNADWAQVKEWIRERAVKEVAVGEISGVLKTFLVEPFVPHPADVEYYVCIQSHRDGDEILFTHEGGVEIGDVDAKALRLQVPISQPLPDSESIAAKLLADIASPTQRAALATFVERLYAVYVDLNFTYLEINPLVVLETADGGLPQVVYLDLAAKLDQTAEFESGDKWAKARSDAVVYGTTDAGAGPAMDFPAPFGRELSREEAYIQELDAKTGASLKLTILNKEGRIWTMVAGGGASVVYSDAIAALGFAGELANYGEYSGAPSEAQTYEYAKTILDLMTRTQRAEGKVLIIGGGIANFTNVATTFKGIIRALKEYRQALIATNVRVFVRRAGPNWQEGLRAMRELGETLGVEIRVYGPETHVTAIVPLALGQASPAAVGAGFRDSMAKQIPDSTAASSPGTPAAMDVSASVVPPAATPSAAAASAAAASDDKPSWYAPFTANTRAIVYGMQPRAVQGMLDFDFICKRAVPSVACMVYPFGGNHVQKFYWGTKETLLPVFASLSEAASQFPDADVVVNFASCRSVFASTSEMLGLPQIRTVAIIAEGVPERHARKLISLAQTAGVTLIGPATVGGIKPGCFKIGNTGGMMDNIASSKLYRAGSVAYVSKSGGMSNELNNIVARTTDGVYEGVAIGGDRYPGTTFLDHMLRYEADPGCKLLLLLGEVGGAEEYKVAEAVRSGRITKPVVAWCIGTCAGLFTTEVQFGHAGALANSDNETADAKNAAMRAAGIHVPETFEALPALLNRIYGDLVQSGQIVPRAEPEPPKIPIDYAWAQELGLVRKPAAFVSTICDDRGQELLYAGMRISDVFKEDIGIGGVLSLLWFKRRLPAYACKFIEMVLMLTADHGPAVSGAHNTIVTARAGKDLVSALCSGLLTIGDRFGGALDGAADLFSSAYDKGLTPRQFVDSMRKQNKLILGIGHKIKSRTNPDLRVSIITEYAKRHFPTTPILDYARAVESITTAKKDNLILNVDGAIGVLFVDLLRHSGAFSREEADEYARIGTLNGLFVLGRSIGFIGHYLDQKRLKQGLYRHPWDDISYLNPATTQRLGLHNFVLRHDIGRGAFGKVRLAEHVETRRSYALKYISKRLCAEQHSEGNILQERAILEEISHAYVASLRFSFQTTHHVFLVLDLMQGGDLRFHLRREKRFPESVVRLWVAELACALNYLHAIGVVHRDIKPENVLMDCEGHVALTDFNAAIRITKEAPVHCGVAGTTSYMAPELISGGSYAGSVDWWSLGVLMYECVYGHRPYRRKNRDDLKRSIMEDDAVFPVTTDSRVSLDCISAIRGLLHKSPERRLGCGDDGFERLKGHAFFASIDWDALEGRRVGPLFVPETSGFEKSRVSSVPAGNGSEDTVAGGEGGGVLDREFANFNYIEYLTFKAYVEQHGSVTAEAVSQAISTAACGGSGVPHSLLQLRLDGRPLVRSLPGAHMSAVSLVPSQAGSVRRRITGRAVARLKRMNPSMASLNHSLSEQSSDDTLPRPATLLDGEMPPSDVPIDAAAWMAMLPSQRMLATRFCTKMALDKVTASLINRPRPPAAKPPISQGAAKPRSFSVITETPSLPDLQLRVNAMRGRIRHSPSMSGTGKDTMPRLVPIAAQWKAPPTRDGRVERALVRKTNYPQLNSDPVIVAMAEEIAAEGWEVVPKSAAASGTPWRILSPKQSAFEKVAIL","length":1772,"molWeight":191510,"crc64":"E075D2C4F3368021","md5":"EEB06BE73CAEFDED30A8474D4261E8A9"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"SUBUNIT":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":1,"Modified residue":1},"uniParcId":"UPI0022D71E6A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1KPB6","uniProtkbId":"A0ACC1KPB6_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019805"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"Chromatin-remodeling ATPase INO80"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"3.6.4.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"}],"value":"INO80"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"}],"value":"GGI18_000177"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair"}],"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"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.","ecNumber":"3.2.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10053"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"Component of the INO80 chromatin-remodeling complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"The DBINO region is involved in binding to DNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007025"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368001"}],"value":"Belongs to the SNF2/RAD54 helicase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"}],"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":826,"modifier":"EXACT"},"end":{"value":951,"modifier":"EXACT"}},"description":"DBINO","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51413"}]},{"type":"Domain","location":{"start":{"value":1060,"modifier":"EXACT"},"end":{"value":1232,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":1616,"modifier":"EXACT"},"end":{"value":1766,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":494,"modifier":"EXACT"},"end":{"value":687,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":759,"modifier":"EXACT"},"end":{"value":789,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1890,"modifier":"EXACT"},"end":{"value":1978,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":898,"modifier":"EXACT"},"end":{"value":927,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":502,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":613,"modifier":"EXACT"},"end":{"value":623,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":624,"modifier":"EXACT"},"end":{"value":633,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":634,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":968,"modifier":"EXACT"},"end":{"value":968,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10053"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00746"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2792711.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010000009","properties":[{"key":"ProteinId","value":"KAJ2792711.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031011","properties":[{"key":"GoTerm","value":"C:Ino80 complex"},{"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:TreeGrafter"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008843","properties":[{"key":"GoTerm","value":"F:endochitinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0042393","properties":[{"key":"GoTerm","value":"F:histone binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006338","properties":[{"key":"GoTerm","value":"P:chromatin remodeling"},{"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:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051054","properties":[{"key":"GoTerm","value":"P:positive regulation of DNA metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006355","properties":[{"key":"GoTerm","value":"P:regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd18793","properties":[{"key":"EntryName","value":"SF2_C_SNF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10810:FF:000006","properties":[{"key":"EntryName","value":"Putative DNA helicase INO80"},{"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":"3.40.50.10810","properties":[{"key":"EntryName","value":"Tandem AAA-ATPase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020838","properties":[{"key":"EntryName","value":"DBINO"}]},{"database":"InterPro","id":"IPR001579","properties":[{"key":"EntryName","value":"Glyco_hydro_18_chit_AS"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR050520","properties":[{"key":"EntryName","value":"INO80/SWR1_helicase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR038718","properties":[{"key":"EntryName","value":"SNF2-like_sf"}]},{"database":"InterPro","id":"IPR049730","properties":[{"key":"EntryName","value":"SNF2/RAD54-like_C"}]},{"database":"InterPro","id":"IPR000330","properties":[{"key":"EntryName","value":"SNF2_N"}]},{"database":"PANTHER","id":"PTHR45685:SF2","properties":[{"key":"EntryName","value":"CHROMATIN-REMODELING ATPASE INO80"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45685","properties":[{"key":"EntryName","value":"HELICASE SRCAP-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13892","properties":[{"key":"EntryName","value":"DBINO"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00176","properties":[{"key":"EntryName","value":"SNF2-rel_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51413","properties":[{"key":"EntryName","value":"DBINO"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01095","properties":[{"key":"EntryName","value":"GH18_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAYDHPNPNPHNVNSLLSPRGRSGGTGAEDPAAGAAEQEGPYASSAAYHAGDPAYQAAGTYRSPARGAEYPRYDAAYDYPTQHEAGGGEYAPSGQHYQYPYATAGQHHTHDRHAARAEYADYRDGYTRQEYNYGMPAQQQPSSQSHRSRRPVAYEYEYDQAAYEQARYADASEHRYQYHDQHRPAAAHDEYYSRQYAYANHEGYAQDAAAAGGYAHHSTGATDAGYYDRHHRYQQHQQYDYQPSAGDRSDALRSPSAQVQQQQQGQHKYSSQASATQYDYGAHAERVGSRSADPQRAAVADAASYRGQGRSDAYEQTGGRAHEQTYNLDTHLSRQQQKSHAYRYGTSEGPGYSYEHAGSAEAAQAYYQQRSPVPAAYASRSEHRSPSHGTHLQALRRDAAGYGPTYSGEAEAESHGRAHRLPGIGINSLLADPPTTHEVAYDRHRHRNYDTPPGRYGHEYEEVPGGTYPESHAVMSISQLVGGEVGAYRDEGIRNGHAHSKRPTEHAQQDPSREPILIVSDDDNEAESAGHAVSGAGRGQAEASETDDDTRPLAARPNRAIRPKPGTAEAAQSTLVPKKRRVAAASSGGVGMKSRRRRLAADANTEEAGAGDKRRHGRRARGPKKIELSREYVSDDDDDDDEEAPLELSTASLNSNGGGFPRDSSGDHDVAVPSGGAVPSTAAADEDYSVEEQVQAYIHRVKQRTDRAVAKYEEQSRRKSQRMHDHVVQRYGPYLRGYFENVGADNDYGVQRQQPPPMGYFSPPSRAMSPVRGYGRQYERDGATPESDDSGPLALLAEEGTLVQNGSPKSLWARMAVEHVPLTFFHMQANVQVRNANMQKVAELCKRESRRVLGPPAPRTAQLNAVKPMIVVRPSKDLLSRTRRSMREMLGYWKRHEKEERDMRKRAEKEAAERLKQEEDAREARRQARKLNFLITQTELYSTFVGDKIVDAAAKEAAEFDGINFDDEDEASLAALARQSAKNALALQQAQTRKFDEIQRQHRDDHASASDEPHDANVAEALDSMNFQDPDNTAGADIPQPRMLMCQLKEYQIKGLTWLAHLYEQGINGILADEMGLGKTVQSISFLAYLAETNNVWGPFMVVAPASTLHNWQQELTRFVPEFKVLPYWGTPKDRKVLRTSLNNPNSLSRRDSDFHVLVTSYQLVVQDEAYLNRVKWQYMVLDEAQAIKSSSSARWKTLLGFHCRNRLLLTGTPIQNSMQELWALLHFIMPMLFDSHDEFSDWFSRDIEAHAENRSSLNQHQLQRLHVILKPFMLRRQKRHVQNELGEKIEHLVSCDLTQRQKAMYRGLMSKVSVTDLLDRVQNGGSSSNKDEPDENLMNLVMQFRKVCSHPELFERAEVDSPYVLATYPTTGSLAREGDDLACSYATRSIVAYDMPKLLYRESLEVPRMPTQRRSVLDRLSLWTGESYVSDNNDGLLSLLRLCTPSASSAIGAFRGTLTERLDLLTEESDRVDGFRQHLLMSSEENSGSTPKLTQPGSVLHALSNVMADANLCVSSNLAGLARLTLSEFAHSYMSTIAPAFKPPAVSPPADLVVSDRSAAWESRQVLLEHPLASRLSCGRATAEDWTKPFRSQGMSDIWMPSVDNLIRYSGKMAALDQLLIKLKQENHRVLLYFQMTKTIDLFEEYLAYRKYTYLRLDGASKISDRRDMVMDWQTRDDIFIFLLSTRAGGLGINLTAADTVIFFESDWNPTVDSQAMDRAHRLGQTKQVVVYRLITRGTVEERILQRAQQKNEIHRIVIAGGDSHGESEDGSDVMVEGFSSNFEPSSKEIVSLLLGKPLDDESSAQSDRLSMARLAQETSNRLYGHCVEKYPGVCAAAWEALAEDPDSLVVLPQPLVDVYHPEPPAFAAQKAIDAGVTAQIRNAERLLAEQTSRQRSSRGRGGSAAANGSSGRGGKRGGAVPREKRKPKVKAGKDDSSVAPSPRPDTPDQLSAKRLRIEEVITDPSVAEQVAPNTIT","length":1978,"molWeight":220329,"crc64":"D4449E4A407D0B5E","md5":"91C8E335F37A2BEA5CD4FDDC8FE872AA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":5,"Coiled coil":1,"Compositional bias":6,"Active site":1},"uniParcId":"UPI0022DACDD9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JNE1","uniProtkbId":"A0ACC1JNE1_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764263.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"DNA repair protein RAD51 homolog"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764263.1"}],"value":"RAD51"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764263.1"}],"value":"GGI18_006487"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"Homologous DNA recombinase that catalyzes strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA (ssDNA) in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. RAD51 targeting to ssDNA promotes removal of replication protein-A (RPA) from ssDNA and stabilization of RAD51-ssDNA filaments by blocking ATP hydrolysis. Also required for homologous recombination during meiosis by acting as an non-catalytic accessory factor for DMC1 recombinase, enabling proper chromosome pairing and crossing over"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024641"}],"value":"Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007095"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"Belongs to the RecA family. RAD51 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006876"}],"value":"Belongs to the eukaryotic RecA-like protein family. RadB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764263.1"}],"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":15,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"RecA family profile 1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50162"}]},{"type":"Domain","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"RecA family profile 2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50163"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003422"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003422"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764263.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764263.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010004343","properties":[{"key":"ProteinId","value":"KAJ2764263.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000794","properties":[{"key":"GoTerm","value":"C:condensed nuclear chromosome"},{"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:0140664","properties":[{"key":"GoTerm","value":"F:ATP-dependent DNA damage sensor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003684","properties":[{"key":"GoTerm","value":"F:damaged DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000150","properties":[{"key":"GoTerm","value":"F:DNA strand exchange activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003690","properties":[{"key":"GoTerm","value":"F:double-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070192","properties":[{"key":"GoTerm","value":"P:chromosome organization involved in meiotic cell cycle"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000730","properties":[{"key":"GoTerm","value":"P:DNA recombinase assembly"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042148","properties":[{"key":"GoTerm","value":"P:DNA strand invasion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006312","properties":[{"key":"GoTerm","value":"P:mitotic recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1990426","properties":[{"key":"GoTerm","value":"P:mitotic recombination-dependent replication fork processing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007131","properties":[{"key":"GoTerm","value":"P:reciprocal meiotic recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd19513","properties":[{"key":"EntryName","value":"Rad51"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000092","properties":[{"key":"EntryName","value":"DNA repair protein Rad51 homolog"},{"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":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR011941","properties":[{"key":"EntryName","value":"DNA_recomb/repair_Rad51"}]},{"database":"InterPro","id":"IPR011939","properties":[{"key":"EntryName","value":"DNA_repair_and_recomb_RadB"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR013632","properties":[{"key":"EntryName","value":"Rad51_C"}]},{"database":"InterPro","id":"IPR020588","properties":[{"key":"EntryName","value":"RecA_ATP-bd"}]},{"database":"InterPro","id":"IPR020587","properties":[{"key":"EntryName","value":"RecA_monomer-monomer_interface"}]},{"database":"NCBIfam","id":"NF003301","properties":[{"key":"EntryName","value":"radA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02239","properties":[{"key":"EntryName","value":"recomb_RAD51"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22942:SF39","properties":[{"key":"EntryName","value":"DNA REPAIR PROTEIN RAD51 HOMOLOG 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22942","properties":[{"key":"EntryName","value":"RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08423","properties":[{"key":"EntryName","value":"Rad51"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF003336","properties":[{"key":"EntryName","value":"RadB"},{"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":"1"}]},{"database":"PROSITE","id":"PS50162","properties":[{"key":"EntryName","value":"RECA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50163","properties":[{"key":"EntryName","value":"RECA_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGFTTASDYHQKRSELLHITTGSTELDKLLGGHGIETGSITEIFGEFRTGKSQICHTLAVTCQLDEASGGAMGKCLYIDTEGTFRPERLVEIAERYNLNPGEVLENVAYARAFNSDHQTALLNQASLLMTEARFSLLVVDSATSLYRTDYSGRGELSARQMHLARFLRMLLRLADEFGIAVVITNQVVAQVDGGMAMFAADPKKPIGGNIIAHASTTRLSLRKGRGETRVCKIYDSPCLPESEAVFAITAQGIADAKD","length":258,"molWeight":28066,"crc64":"01F277613A80D636","md5":"3D7E98F9D91EF73C2B8F9A76C5B475B6"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI0022D49D09"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JNU9","uniProtkbId":"A0ACC1JNU9_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764352.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"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":"KAJ2764352.1"}],"value":"GGI18_006467"}]}],"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":"KAJ2764352.1"}],"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":276,"modifier":"EXACT"},"end":{"value":276,"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":89,"modifier":"EXACT"},"end":{"value":131,"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":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764352.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764352.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010004315","properties":[{"key":"ProteinId","value":"KAJ2764352.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0005768","properties":[{"key":"GoTerm","value":"C:endosome"},{"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:0005802","properties":[{"key":"GoTerm","value":"C:trans-Golgi network"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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":"MDATSGKFSGGEIRLGSRGDSYYEYLLKQWLQTRQSEPELLAEYEAAMEGVKKYLVALSPNQKLTYVGEIQQATSDTPYFNPKMDHLVCFLPGSLALGATKGRALSDIPPAQLSARNREDLILARELAETCMHMYLDTKTGLSPELVYFRHIDPATGKEAEFGKGDQLVQPSGDILARGNDRHNLLRPETVESLFVLWSITGEEKWREYGWSIFSAIEKWAKLPAGGYTSLNDITIVPPIREDKMETFFVSETLKYLYLLFSDSDSVPLSQYVFNTEAHPLPQFSWE","length":287,"molWeight":32424,"crc64":"669598F5C59AB823","md5":"A350CAA100B5BD6D54998123056F13FB"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":1,"Disulfide bond":1},"uniParcId":"UPI0022DC3437"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JP69","uniProtkbId":"A0ACC1JP69_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044078"}],"value":"ATP-dependent RNA helicase DRS1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012552"}],"value":"3.6.4.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044094"}],"value":"ATP-dependent RNA helicase drs1"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"}],"value":"DRS1_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"}],"value":"GGI18_006465"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043881"}],"value":"ATP-binding RNA helicase involved in ribosome assembly"}],"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":"3.6.4.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047984"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004604"}],"value":"Nucleus, nucleolus","id":"SL-0188"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043999"}],"value":"Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"}],"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":310,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"Q motif","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00552"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000492"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"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":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022517"}],"id":"KW-0690","category":"Biological process","name":"Ribosome biogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764362.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010004313","properties":[{"key":"ProteinId","value":"KAJ2764362.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0005730","properties":[{"key":"GoTerm","value":"C:nucleolus"},{"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:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase 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:0003724","properties":[{"key":"GoTerm","value":"F:RNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd17947","properties":[{"key":"EntryName","value":"DEADc_DDX27"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000842","properties":[{"key":"EntryName","value":"ATP-dependent RNA helicase DRS1"},{"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":"InterPro","id":"IPR011545","properties":[{"key":"EntryName","value":"DEAD/DEAH_box_helicase_dom"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR000629","properties":[{"key":"EntryName","value":"RNA-helicase_DEAD-box_CS"}]},{"database":"InterPro","id":"IPR014014","properties":[{"key":"EntryName","value":"RNA_helicase_DEAD_Q_motif"}]},{"database":"PANTHER","id":"PTHR47959:SF1","properties":[{"key":"EntryName","value":"ATP-DEPENDENT RNA HELICASE DBPA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47959","properties":[{"key":"EntryName","value":"ATP-DEPENDENT RNA HELICASE RHLE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00270","properties":[{"key":"EntryName","value":"DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"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":"PS00039","properties":[{"key":"EntryName","value":"DEAD_ATP_HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51195","properties":[{"key":"EntryName","value":"Q_MOTIF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEVSEEEKVEEEVSDNDDEVESASDEEEDAEDSAAESTAVAGTPALEGESGSEAESDEEESESEVDSESEESEGESSAEESEVDEIEEARKRAYFAAPEEGPAVDMPESFTTMNLSRQIMKGLTKLGFAQPTPIQARTIPLALLGKDICGGAQTGSGKTAAFLVPILERLLYRPKNTAVTRVLILCPTRELAIQCHNVSTKLAGFTDISTCLCVGGLSLKQQESELKLRPDVVIATPGRLIDHLRNSQSFHLDQIEILVMDEADRMLDDGFEDELTEIIKACPQKRQTMLFSATMTDNVDKLIRLSLQKP","length":310,"molWeight":33876,"crc64":"70DE428A96945A88","md5":"5FFB4F2964FB777B43C5194EDDF18C63"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Motif":1,"Compositional bias":3,"Non-terminal residue":1},"uniParcId":"UPI0022D6022A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JPI7","uniProtkbId":"A0ACC1JPI7_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041823"}],"value":"Cyclin-dependent kinase 8"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012425"}],"value":"2.7.11.22"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012409"}],"value":"2.7.11.23"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}],"value":"SSN3_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}],"value":"GGI18_006414"}]}],"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":"2.7.11.22","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048367"}]}},{"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":"2.7.11.22","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047811"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10216"},{"database":"Rhea","id":"RHEA-COMP:11321"},{"database":"Rhea","id":"RHEA-COMP:11322"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43176"},{"database":"ChEBI","id":"CHEBI:68546"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049280"}]}},{"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":"ARBA00006485"}],"value":"Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}],"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":1,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"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":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022491"}],"id":"KW-0678","category":"Molecular function","name":"Repressor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022527"}],"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2764558.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010004249","properties":[{"key":"ProteinId","value":"KAJ2764558.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016592","properties":[{"key":"GoTerm","value":"C:mediator complex"},{"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:0004693","properties":[{"key":"GoTerm","value":"F:cyclin-dependent protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008353","properties":[{"key":"GoTerm","value":"F:RNA polymerase II CTD heptapeptide repeat kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"1.10.510.10:FF:000408","properties":[{"key":"EntryName","value":"Serine/threonine-protein kinase SSN3"},{"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":"IPR050108","properties":[{"key":"EntryName","value":"CDK"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"PANTHER","id":"PTHR24056","properties":[{"key":"EntryName","value":"CELL DIVISION PROTEIN KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24056:SF495","properties":[{"key":"EntryName","value":"CYCLIN-DEPENDENT KINASE 8-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"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":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"SACREIGLCRELHHENIVDLCEVVMDDNAIHMVMDYAEFDLLSIMQHHIHHLRKPMSELVVKSILWQLLNGVAYLHANFILQRDLKPANIMITSSGVVKVGDMGLARVFRRPFQTLYNGDKVVVTVWYRAPELLLGSRHYTTAIDLWSVGCIFAEMLALRPIFKGEEVKMEKKQIPFQRGQVNKIIEVLGTPTKEMWPAIELMPDFIQMKQFRHYASALKTWFTNTGHKSETGFQLLSSMLDYDPERRITAADALEHPYFKEEPKPVKHPFLEQNISYPKRRLTLDELCDAKPPPQHTKTHPDSTMPGSTSVNTVS","length":316,"molWeight":36307,"crc64":"00F95E4EBF83FBFD","md5":"774EB1C8068933C814414367C277AB9F"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Non-terminal residue":1},"uniParcId":"UPI0022D5FA37"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JRP2","uniProtkbId":"A0ACC1JRP2_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015135"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"value":"Squalene synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"value":"SQS"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"value":"SS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012373"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"value":"2.5.1.21"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"}],"value":"FDFT1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"}],"value":"GGI18_006094"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045166"}],"value":"Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene. Proceeds in two distinct steps. In the first half-reaction, two molecules of FPP react to form the stable presqualene diphosphate intermediate (PSQPP), with concomitant release of a proton and a molecule of inorganic diphosphate. In the second half-reaction, PSQPP undergoes heterolysis, isomerization, and reduction with NADPH or NADH to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 (2E,6E)-farnesyl diphosphate + NADH + H(+) = squalene + 2 diphosphate + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32299"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15440"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:175763"}],"ecNumber":"2.5.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048854"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:32300"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048854"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 (2E,6E)-farnesyl diphosphate + NADPH + H(+) = squalene + 2 diphosphate + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32295"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15440"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:175763"}],"ecNumber":"2.5.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 (2E,6E)-farnesyl diphosphate = presqualene diphosphate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22672"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57310"},{"database":"ChEBI","id":"CHEBI:175763"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048315"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:22673"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048315"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"presqualene diphosphate + NADH + H(+) = squalene + diphosphate + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22228"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15440"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57310"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047541"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:22229"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047541"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"presqualene diphosphate + NADPH + H(+) = squalene + diphosphate + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22232"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15440"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57310"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047468"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:22233"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047468"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005057"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"value":"Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004477"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004477"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006251"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"value":"Belongs to the phytoene/squalene synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"}],"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":"Non-terminal residue","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022548"}],"id":"KW-0153","category":"Biological process","name":"Cholesterol metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"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":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"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:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023221"}],"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023166"}],"id":"KW-1207","category":"Biological process","name":"Sterol metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368088"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2765989.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003822","properties":[{"key":"ProteinId","value":"KAJ2765989.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0055056","properties":[{"key":"GoTerm","value":"F:D-glucose transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051996","properties":[{"key":"GoTerm","value":"F:squalene synthase [NAD(P)H] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006696","properties":[{"key":"GoTerm","value":"P:ergosterol biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045338","properties":[{"key":"GoTerm","value":"P:farnesyl diphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00683","properties":[{"key":"EntryName","value":"Trans_IPPS_HH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.600.10:FF:000053","properties":[{"key":"EntryName","value":"Squalene synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.600.10","properties":[{"key":"EntryName","value":"Farnesyl Diphosphate Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008949","properties":[{"key":"EntryName","value":"Isoprenoid_synthase_dom_sf"}]},{"database":"InterPro","id":"IPR002060","properties":[{"key":"EntryName","value":"Squ/phyt_synthse"}]},{"database":"InterPro","id":"IPR006449","properties":[{"key":"EntryName","value":"Squal_synth-like"}]},{"database":"InterPro","id":"IPR019845","properties":[{"key":"EntryName","value":"Squalene/phytoene_synthase_CS"}]},{"database":"InterPro","id":"IPR044844","properties":[{"key":"EntryName","value":"Trans_IPPS_euk-type"}]},{"database":"InterPro","id":"IPR033904","properties":[{"key":"EntryName","value":"Trans_IPPS_HH"}]},{"database":"NCBIfam","id":"TIGR01559","properties":[{"key":"EntryName","value":"squal_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11626","properties":[{"key":"EntryName","value":"FARNESYL-DIPHOSPHATE FARNESYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11626:SF2","properties":[{"key":"EntryName","value":"SQUALENE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00494","properties":[{"key":"EntryName","value":"SQS_PSY"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00005","properties":[{"key":"EntryName","value":"Isoprenoid_Synthase_Type_I"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01018","properties":[{"key":"EntryName","value":"Squalene/Phytoene_Synthase_Lik"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48576","properties":[{"key":"EntryName","value":"Terpenoid synthases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01044","properties":[{"key":"EntryName","value":"SQUALEN_PHYTOEN_SYN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01045","properties":[{"key":"EntryName","value":"SQUALEN_PHYTOEN_SYN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAFLDWALHPTELWAAFWYVMRHAPPDEKTNKLQVSGDMRRCYDFLEMTSRSFAAVIQELNPRLRDGICIFYLVLRGLDTVEDDMTIPGAKKRQILETFHEALYVKGWTFKESGPDEKDAMLLVEFDVVINEFLRLPEDYQEVIADITKRMGAGMAKYTRARVETLDDYNEYCHYVAGLVGHGLSRLFAESRLEDKTVGEKLELANSMGLFLQKTNITRDINEDVLDGRCFWPKAIWTKYAESEEELISKRGREKGIEALNEMCVNALEHIPDVMEYLNQIHEPSVF","length":287,"molWeight":33249,"crc64":"3DCCDCDB14BEF5DA","md5":"B02099F04527B0016F9DBEE04A034D3E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Non-terminal residue":1},"uniParcId":"UPI0022D554C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JS39","uniProtkbId":"A0ACC1JS39_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766211.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Pre-mRNA-processing factor 19"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"2.3.2.27"}]},"flag":"Fragment"},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766211.1"}],"value":"GGI18_006046"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.","ecNumber":"2.3.2.27","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006388"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Belongs to the WD repeat PRP19 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766211.1"}],"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":1,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"U-box","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51698"}]},{"type":"Repeat","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]},{"type":"Region","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766211.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022664"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023187"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0508","category":"Biological process","name":"mRNA splicing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022728"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0747","category":"Cellular component","name":"Spliceosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01034"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0833","category":"Biological process","name":"Ubl conjugation pathway"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022574"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}],"id":"KW-0853","category":"Domain","name":"WD repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766211.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766211.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003761","properties":[{"key":"ProteinId","value":"KAJ2766211.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0000974","properties":[{"key":"GoTerm","value":"C:Prp19 complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071006","properties":[{"key":"GoTerm","value":"C:U2-type catalytic step 1 spliceosome"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000151","properties":[{"key":"GoTerm","value":"C:ubiquitin ligase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0061630","properties":[{"key":"GoTerm","value":"F:ubiquitin protein ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000398","properties":[{"key":"GoTerm","value":"P:mRNA splicing, via spliceosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070534","properties":[{"key":"GoTerm","value":"P:protein K63-linked ubiquitination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.30.40.10:FF:000027","properties":[{"key":"EntryName","value":"Pre-mRNA-processing factor 19, putative"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.130.10.10","properties":[{"key":"EntryName","value":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.40.10","properties":[{"key":"EntryName","value":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR038959","properties":[{"key":"EntryName","value":"Prp19"}]},{"database":"InterPro","id":"IPR013915","properties":[{"key":"EntryName","value":"Prp19_cc"}]},{"database":"InterPro","id":"IPR003613","properties":[{"key":"EntryName","value":"Ubox_domain"}]},{"database":"InterPro","id":"IPR015943","properties":[{"key":"EntryName","value":"WD40/YVTN_repeat-like_dom_sf"}]},{"database":"InterPro","id":"IPR036322","properties":[{"key":"EntryName","value":"WD40_repeat_dom_sf"}]},{"database":"InterPro","id":"IPR001680","properties":[{"key":"EntryName","value":"WD40_rpt"}]},{"database":"InterPro","id":"IPR013083","properties":[{"key":"EntryName","value":"Znf_RING/FYVE/PHD"}]},{"database":"PANTHER","id":"PTHR43995","properties":[{"key":"EntryName","value":"PRE-MRNA-PROCESSING FACTOR 19"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43995:SF1","properties":[{"key":"EntryName","value":"PRE-MRNA-PROCESSING FACTOR 19"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08606","properties":[{"key":"EntryName","value":"Prp19"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00400","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00504","properties":[{"key":"EntryName","value":"Ubox"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00320","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF57850","properties":[{"key":"EntryName","value":"RING/U-box"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50978","properties":[{"key":"EntryName","value":"WD40 repeat-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51698","properties":[{"key":"EntryName","value":"U_BOX"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50082","properties":[{"key":"EntryName","value":"WD_REPEATS_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFICSLSGESPNEPVISAKTGRLYESRLLQKYLSENGQHEPQTTHALTPDDIIPVHSDPPTVKPRPPTLTSIPALLSTFQNEWDALVLETFSLKQQYHQVRQELSQALYQNDAACRVVARLMKERDEARQALATLQAQVAAVEPVAPVAAQPDTMEVDAVADPAQQYYDTAAETAKTLSKGRVKREVPVDLTSPEAWKTAAESSVISSLHSTTKPGITALDVDQSGSLLLTAGMDNHAEVYSRTTDTVVATLKGHTKRLTSALWLGGGGLDASIVTASADKSVRLWVPKPGNAAGWVKKNIVKHHNAEVVGLSLHPSG","length":319,"molWeight":34382,"crc64":"285236E72962E127","md5":"CDB8902AA00F10E79D1C4F2B5D5FD9BF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Repeat":1,"Region":1,"Non-terminal residue":1},"uniParcId":"UPI0022CF808C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JST1","uniProtkbId":"A0ACC1JST1_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"Phosphomannomutase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"5.4.2.8"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}],"value":"PMM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}],"value":"GGI18_005974"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-mannose 1-phosphate = D-mannose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11140"},{"database":"ChEBI","id":"CHEBI:58409"},{"database":"ChEBI","id":"CHEBI:58735"}],"ecNumber":"5.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"value":"Belongs to the eukaryotic PMM family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}],"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":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58409"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-2"}],"ligand":{"name":"alpha-D-mannose 1-phosphate","id":"ChEBI:CHEBI:58409"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58409"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-2"}],"ligand":{"name":"alpha-D-mannose 1-phosphate","id":"ChEBI:CHEBI:58409"}},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58409"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-2"}],"ligand":{"name":"alpha-D-mannose 1-phosphate","id":"ChEBI:CHEBI:58409"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58409"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-2"}],"ligand":{"name":"alpha-D-mannose 1-phosphate","id":"ChEBI:CHEBI:58409"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58409"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-2"}],"ligand":{"name":"alpha-D-mannose 1-phosphate","id":"ChEBI:CHEBI:58409"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361118"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-3"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605002-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766587.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003661","properties":[{"key":"ProteinId","value":"KAJ2766587.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0004615","properties":[{"key":"GoTerm","value":"F:phosphomannomutase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009298","properties":[{"key":"GoTerm","value":"P:GDP-mannose biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006013","properties":[{"key":"GoTerm","value":"P:mannose metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006487","properties":[{"key":"GoTerm","value":"P:protein N-linked glycosylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.40.50.1000","properties":[{"key":"EntryName","value":"HAD superfamily/HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036412","properties":[{"key":"EntryName","value":"HAD-like_sf"}]},{"database":"InterPro","id":"IPR023214","properties":[{"key":"EntryName","value":"HAD_sf"}]},{"database":"InterPro","id":"IPR005002","properties":[{"key":"EntryName","value":"PMM"}]},{"database":"PANTHER","id":"PTHR10466","properties":[{"key":"EntryName","value":"PHOSPHOMANNOMUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10466:SF0","properties":[{"key":"EntryName","value":"PHOSPHOMANNOMUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03332","properties":[{"key":"EntryName","value":"PMM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56784","properties":[{"key":"EntryName","value":"HAD-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"FRQGMVNISPIGRACSRDERNEYEVFDLKHNIRKDFVEALKREFSDYGLKYSIGGQISFDVFPIGWDKTYCLRHLEGEGFNTIHFFGDKTFEGGNDFEIYEHPEVTGHAVKNPLETEAILKSLFSL","length":126,"molWeight":14572,"crc64":"423F00EF911AD1F9","md5":"02D565F36CC647F23E986719D5CA0FFE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":7,"Non-terminal residue":1},"uniParcId":"UPI0022DC7755"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JTG6","uniProtkbId":"A0ACC1JTG6_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Phospholipid-transporting ATPase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"7.6.2.1"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"}],"value":"DRS2_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"}],"value":"GGI18_005892"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.","ecNumber":"7.6.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66132"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:64612"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049128"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66133"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049128"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"}],"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":84,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Active site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-1"}]},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Non-terminal residue","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2766981.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003559","properties":[{"key":"ProteinId","value":"KAJ2766981.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005802","properties":[{"key":"GoTerm","value":"C:trans-Golgi network"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:InterPro"}]},{"database":"GO","id":"GO:0140326","properties":[{"key":"GoTerm","value":"F:ATPase-coupled intramembrane lipid carrier activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032456","properties":[{"key":"GoTerm","value":"P:endocytic recycling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045332","properties":[{"key":"GoTerm","value":"P:phospholipid translocation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006892","properties":[{"key":"GoTerm","value":"P:post-Golgi vesicle-mediated transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.40.50.1000:FF:000001","properties":[{"key":"EntryName","value":"Phospholipid-transporting ATPase IC"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1110.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023299","properties":[{"key":"EntryName","value":"ATPase_P-typ_cyto_dom_N"}]},{"database":"InterPro","id":"IPR018303","properties":[{"key":"EntryName","value":"ATPase_P-typ_P_site"}]},{"database":"InterPro","id":"IPR023298","properties":[{"key":"EntryName","value":"ATPase_P-typ_TM_dom_sf"}]},{"database":"InterPro","id":"IPR006539","properties":[{"key":"EntryName","value":"P-type_ATPase_IV"}]},{"database":"InterPro","id":"IPR001757","properties":[{"key":"EntryName","value":"P_typ_ATPase"}]},{"database":"NCBIfam","id":"TIGR01652","properties":[{"key":"EntryName","value":"ATPase-Plipid"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01494","properties":[{"key":"EntryName","value":"ATPase_P-type"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24092:SF150","properties":[{"key":"EntryName","value":"PHOSPHOLIPID-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24092","properties":[{"key":"EntryName","value":"PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13246","properties":[{"key":"EntryName","value":"Cation_ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81665","properties":[{"key":"EntryName","value":"Calcium ATPase, transmembrane domain M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81660","properties":[{"key":"EntryName","value":"Metal cation-transporting ATPase, ATP-binding domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00154","properties":[{"key":"EntryName","value":"ATPASE_E1_E2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKTELPNDSLYTFEATLVSEGGKIGYRELPLDPTQVLLRGAILRNTDWIYAVAVFTGHETKLMRNATAAPIKRTSVEKTTNRQIIFLFLILILLAVMSALGSQIMTSRNRSQLSYLYLPDGEGAKTFVKNILTFIILYNNLIPISLIVTMEIVKFQQAQLINADMDMYDEGSDTAALARTSSLVEELGQVEYIFSDKTGTLTCNIMEFRQCSIGGVMYSDVVEASKRARIVDGEVVGQYDIAQLKDHIANSERGPMLFEFFQLLATCHTVIPERQESAEGGIEYQASSPDEGALVKGAALADFVFHTRKPRSIAVNIMGVDREYEVLNINEFNSTRKRMSALLRCPDGSIKMYCKGADTVIFERLTSEGGGSPFLQTTLKHLEEYATEGLRTL","length":393,"molWeight":43753,"crc64":"FC95D3E877A82D6D","md5":"697C3DB4E75F178187F41CF7BFC6F860"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Transmembrane":2,"Active site":1,"Binding site":9,"Non-terminal residue":1},"uniParcId":"UPI0022D0B6A6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JTM1","uniProtkbId":"A0ACC1JTM1_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2026-01-28","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767274.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018388"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Glucose-6-phosphate isomerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011952"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"5.3.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"pgi"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767274.1"}],"value":"GGI18_005829"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094319"}],"value":"Isomerase that catalyzes the conversion of alpha-D-glucose-6-phosphate to beta-D-fructose-6-phosphate, the second step in glycolysis, and the reverse reaction in gluconeogenesis, within the cytoplasm. Also shows C2-epimerase activity, interconverting D-glucose-6-phosphate (G6P) and D-mannose-6-phosphate (M6P). Also displays anomerase activity, interconverting alpha and beta-anomeric forms of G6P, D-fructose-6-phosphate and M6P"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glucose 6-phosphate = D-mannose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:85575"},{"database":"ChEBI","id":"CHEBI:58735"},{"database":"ChEBI","id":"CHEBI:61548"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094014"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:85576"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094014"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:85577"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094014"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-fructose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:85579"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:234464"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093826"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:85580"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093826"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:85581"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093826"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093941"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11817"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093941"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:11818"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093941"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16249"},{"database":"ChEBI","id":"CHEBI:58225"},{"database":"ChEBI","id":"CHEBI:58247"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094054"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:16250"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094054"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:16251"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094054"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-mannose 6-phosphate = beta-D-mannose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:85583"},{"database":"ChEBI","id":"CHEBI:60332"},{"database":"ChEBI","id":"CHEBI:234465"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093919"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:85584"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093919"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:85585"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093919"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004926"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006604"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Belongs to the GPI family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767274.1"}],"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":"Active site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767274.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767274.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767274.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003484","properties":[{"key":"ProteinId","value":"KAJ2767274.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004347","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051156","properties":[{"key":"GoTerm","value":"P:glucose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05016","properties":[{"key":"EntryName","value":"SIS_PGI_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1390.10:FF:000001","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000003","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1390.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR001672","properties":[{"key":"EntryName","value":"G6P_Isomerase"}]},{"database":"InterPro","id":"IPR023096","properties":[{"key":"EntryName","value":"G6P_Isomerase_C"}]},{"database":"InterPro","id":"IPR018189","properties":[{"key":"EntryName","value":"Phosphoglucose_isomerase_CS"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"InterPro","id":"IPR035482","properties":[{"key":"EntryName","value":"SIS_PGI_2"}]},{"database":"NCBIfam","id":"NF001211","properties":[{"key":"EntryName","value":"pgi"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11469","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11469:SF1","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00342","properties":[{"key":"EntryName","value":"PGI"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00662","properties":[{"key":"EntryName","value":"G6PISOMERASE"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00765","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51463","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"EAHVAKHFVALSTNNEGVAAFGIDTKNMFQFWDWVGGRYSLWSAIGLSIAIYIGFDNFHALLEGGHAMDRHYRTAPLEENLPAILGLIGIWYNNFFGAETQALLPYDQYLHRFSAYFQQGDMESNGKFISRDSREVNYQTGPIIWGEPGTNGQHAFYQLIHQGTKLIPCDFIAPTHTLNPIRGGIHHDILLSNYFAQPEALMNGKTAAVARAEILKDGTPSNSIEVEALVPHKTFKGNRPTNSILVNKVIDPFALGALIALYEHKIFTQGAIWFINTFSQEGVEEGKRLAKAILSELKQSGDIHAHDSSTNGLINYYKHNRA","length":322,"molWeight":35916,"crc64":"D05FC855C263C3BD","md5":"09FC0550E0B15467E464BDAA96F0959E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":3,"Non-terminal residue":1},"uniParcId":"UPI0022D1D01F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JUB6","uniProtkbId":"A0ACC1JUB6_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"value":"UV excision repair protein RAD23"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"}],"value":"RAD23"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"}],"value":"GGI18_005787"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"value":"Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"value":"Belongs to the RAD23 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00214"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"}],"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":1,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Ubiquitin-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50053"}]},{"type":"Domain","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"UBA","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50030"}]},{"type":"Region","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367049"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767485.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003436","properties":[{"key":"ProteinId","value":"KAJ2767485.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0005654","properties":[{"key":"GoTerm","value":"C:nucleoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003684","properties":[{"key":"GoTerm","value":"F:damaged DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031593","properties":[{"key":"GoTerm","value":"F:polyubiquitin modification-dependent protein binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070628","properties":[{"key":"GoTerm","value":"F:proteasome binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043130","properties":[{"key":"GoTerm","value":"F:ubiquitin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006289","properties":[{"key":"GoTerm","value":"P:nucleotide-excision repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043161","properties":[{"key":"GoTerm","value":"P:proteasome-mediated ubiquitin-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01805","properties":[{"key":"EntryName","value":"Ubl_Rad23"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.90:FF:000254","properties":[{"key":"EntryName","value":"UV excision repair protein Rad23"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.10:FF:000003","properties":[{"key":"EntryName","value":"UV excision repair protein RAD23 homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.10","properties":[{"key":"EntryName","value":"DNA helicase RuvA subunit, C-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.20.90","properties":[{"key":"EntryName","value":"Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.540","properties":[{"key":"EntryName","value":"XPC-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004806","properties":[{"key":"EntryName","value":"Rad23"}]},{"database":"InterPro","id":"IPR015940","properties":[{"key":"EntryName","value":"UBA"}]},{"database":"InterPro","id":"IPR009060","properties":[{"key":"EntryName","value":"UBA-like_sf"}]},{"database":"InterPro","id":"IPR000626","properties":[{"key":"EntryName","value":"Ubiquitin-like_dom"}]},{"database":"InterPro","id":"IPR029071","properties":[{"key":"EntryName","value":"Ubiquitin-like_domsf"}]},{"database":"InterPro","id":"IPR015360","properties":[{"key":"EntryName","value":"XPC-bd"}]},{"database":"InterPro","id":"IPR036353","properties":[{"key":"EntryName","value":"XPC-bd_sf"}]},{"database":"NCBIfam","id":"TIGR00601","properties":[{"key":"EntryName","value":"rad23"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10621","properties":[{"key":"EntryName","value":"UV EXCISION REPAIR PROTEIN RAD23"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10621:SF0","properties":[{"key":"EntryName","value":"UV EXCISION REPAIR PROTEIN RAD23"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00627","properties":[{"key":"EntryName","value":"UBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00240","properties":[{"key":"EntryName","value":"ubiquitin"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09280","properties":[{"key":"EntryName","value":"XPC-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01839","properties":[{"key":"EntryName","value":"RAD23PROTEIN"}]},{"database":"SMART","id":"SM00165","properties":[{"key":"EntryName","value":"UBA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00213","properties":[{"key":"EntryName","value":"UBQ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46934","properties":[{"key":"EntryName","value":"UBA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54236","properties":[{"key":"EntryName","value":"Ubiquitin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101238","properties":[{"key":"EntryName","value":"XPC-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50030","properties":[{"key":"EntryName","value":"UBA"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50053","properties":[{"key":"EntryName","value":"UBIQUITIN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQITLKTLQQKTFKIEVAPENTIGDVKVKVEESQGYPKDTQKLIFSGKILTDKQTVAELNISENDFMVVMAVKPKVAPKVEEKVAPKVEAATPANTAPPASQAAAPVAQRTAAVGAQATTEPATPSPPARNVARPAATGEVAGDQSLLLGEQYATAIGNMVEMGYTREQCERAMRASFNNPDRAVEYLLNGIPEAALRMADQADARRAETAQPAPVEGEAGAEAPASATAETGEARPRPSGNLFHQAGQLTTPNSAAGQRRQHGLNNLAALRNTPQFRQLQQLVRENPPMLSQVLTQLAQQQPELMQLITNHEEEFFQMLMEGMSNEEMSAMAGAASDDDFEGGAEGAPPAQYIRVTPEEKEAIERLQALGFPHEIV","length":377,"molWeight":40515,"crc64":"F0396D4E0B06419C","md5":"A771A21D51ECFCC371DEA04A933BB604"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Compositional bias":3,"Non-terminal residue":1},"uniParcId":"UPI0022D4DA72"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JVA1","uniProtkbId":"A0ACC1JVA1_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767898.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068771"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Adenosine kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"AK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012119"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"2.7.1.20"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Adenosine 5'-phosphotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767898.1"}],"value":"ADO1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767898.1"}],"value":"GGI18_005701"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094166"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + ATP = AMP + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20824"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.20","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051362"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010688"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Belongs to the carbohydrate kinase PfkB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767898.1"}],"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":33,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Active site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601805-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767898.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2767898.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003345","properties":[{"key":"ProteinId","value":"KAJ2767898.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","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:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004001","properties":[{"key":"GoTerm","value":"F:adenosine kinase 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:0044209","properties":[{"key":"GoTerm","value":"P:AMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006144","properties":[{"key":"GoTerm","value":"P:purine nucleobase metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006166","properties":[{"key":"GoTerm","value":"P:purine ribonucleoside salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01168","properties":[{"key":"EntryName","value":"adenosine_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1190.20:FF:000076","properties":[{"key":"EntryName","value":"Adenosine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1110.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001805","properties":[{"key":"EntryName","value":"Adenokinase"}]},{"database":"InterPro","id":"IPR002173","properties":[{"key":"EntryName","value":"Carboh/pur_kinase_PfkB_CS"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"PANTHER","id":"PTHR45769","properties":[{"key":"EntryName","value":"ADENOSINE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45769:SF3","properties":[{"key":"EntryName","value":"ADENOSINE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00989","properties":[{"key":"EntryName","value":"ADENOKINASE"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00584","properties":[{"key":"EntryName","value":"PFKB_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAQDLAGALVGFCNPLLDISAVVDDALLEQYNLKANDAILASPEHLPLFPTLIDSYEAKFLPGGAGQNALRGAQLLLPADSAVFVGAVGEDDYAQRLKGAAEKAGLRTNYMVNKDKPTGTCALLITGPNRSMVANLSAAETYNFSHISEPSNWKLIEQAKVYYITGFFFTVSPDTIDAVAKHALENGKTFTMNISAPFVPQFYKAAVEKTLPYINILFGNETEAASLAAAFEFGTDDIKVIAKRVADLPRAGDKPRMVVLTQGAQSTVVATSDSDEVRVYAVSPVPTEEIGDTNGAGDAFVAAFLAQHLLGQPTDVCVEAGHWLGGEVVRMIGPNYPDGELKFVASGSFAPSVEKI","length":356,"molWeight":37866,"crc64":"057B06C5D0DA85A6","md5":"96F6AA47647B7626D836C3A76147C342"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1},"uniParcId":"UPI0022DA3D2B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ACC1JXM9","uniProtkbId":"A0ACC1JXM9_9FUNG","entryAudit":{"firstPublicDate":"2026-01-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2026-01-28","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia linderi","taxonId":2663919,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"value":"DNA polymerase epsilon catalytic subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"value":"2.7.7.7"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}],"value":"POL2_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}],"value":"GGI18_005448"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"value":"DNA polymerase II participates in chromosomal DNA replication"}],"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":"2.7.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"value":"Belongs to the DNA polymerase type-B family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}],"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":36,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0239","category":"Molecular function","name":"DNA-directed DNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140066"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365029"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}],"value":"BCRC 34191","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2769182.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUK010003053","properties":[{"key":"ProteinId","value":"KAJ2769182.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001140066","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008622","properties":[{"key":"GoTerm","value":"C:epsilon DNA polymerase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003887","properties":[{"key":"GoTerm","value":"F:DNA-directed DNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008310","properties":[{"key":"GoTerm","value":"F:single-stranded DNA 3'-5' DNA exonuclease activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006287","properties":[{"key":"GoTerm","value":"P:base-excision repair, gap-filling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045004","properties":[{"key":"GoTerm","value":"P:DNA replication proofreading"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006272","properties":[{"key":"GoTerm","value":"P:leading strand elongation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000278","properties":[{"key":"GoTerm","value":"P:mitotic cell cycle"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006297","properties":[{"key":"GoTerm","value":"P:nucleotide-excision repair, DNA gap filling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.30.342.10","properties":[{"key":"EntryName","value":"DNA Polymerase, chain B, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029703","properties":[{"key":"EntryName","value":"POL2"}]},{"database":"InterPro","id":"IPR012337","properties":[{"key":"EntryName","value":"RNaseH-like_sf"}]},{"database":"PANTHER","id":"PTHR10670","properties":[{"key":"EntryName","value":"DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10670:SF0","properties":[{"key":"EntryName","value":"DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53098","properties":[{"key":"EntryName","value":"Ribonuclease H-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSRGGLNSKFGTVSSARGRGGNRGRGGWSGRKPQLAYGGMDIEDGETLDALFPGQEPLEDQVSSIGNLDARYEDVRASDEIDSLLGFARHQQGPPRLGWLINMHATSVEDVERNSTKSAVDYYFLEPEGGSFKCTLLFSPYFYLVCAPGHEAEVGDWLARKHERLVERFEIHEREDLDMANHLTGCKRRLVKLVFRNVQDLLAVRRELLPVVRRNEKRSDLVHTYAEERDGVRELEDCILEMREFDVPYYLRVAIDKNIRVGH","length":263,"molWeight":29954,"crc64":"0DD1F2D425C2692B","md5":"BB55401C8ACC86BD11ED10D189AF3C37"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Non-terminal residue":1},"uniParcId":"UPI0022D39371"}}]}