{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"E5F081","uniProtkbId":"E5F081_9BASI","entryAudit":{"firstPublicDate":"2011-02-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-02-08","entryVersion":46,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Puccinia pseudostriiformis","taxonId":327555,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51607.1"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Pucciniomycotina","Pucciniomycetes","Pucciniales","Pucciniaceae","Puccinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51607.1"}],"value":"Beta-tubulin 1"}}],"flag":"Fragment"},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034296"}],"value":"Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin"}],"commentType":"FUNCTION"},{"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":"ARBA00011747"}],"value":"Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004245"}],"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009636"}],"value":"Belongs to the tubulin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Tubulin/FtsZ 2-layer sandwich","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00865"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51607.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51607.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023212"}],"id":"KW-0206","category":"Cellular component","name":"Cytoskeleton"},{"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":"ARBA00022701"}],"id":"KW-0493","category":"Cellular component","name":"Microtubule"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"20943198","citationType":"journal article","authors":["Liu M.","Hambleton S."],"citationCrossReferences":[{"database":"PubMed","id":"20943198"}],"title":"Taxonomic study of stripe rust, Puccinia striiformis sensu lato, based on molecular and morphological evidence.","publicationDate":"2010","journal":"Fungal Biol.","firstPage":"881","lastPage":"899","volume":"114"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51607.1"}],"value":"DAOM 220657","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51607.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HM067984","properties":[{"key":"ProteinId","value":"ADR51607.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"E5F081","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005874","properties":[{"key":"GoTerm","value":"C:microtubule"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005200","properties":[{"key":"GoTerm","value":"F:structural constituent of cytoskeleton"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007017","properties":[{"key":"GoTerm","value":"P:microtubule-based process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.30.1330.20:FF:000009","properties":[{"key":"EntryName","value":"Tubulin beta chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1330.20","properties":[{"key":"EntryName","value":"Tubulin/FtsZ, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1440","properties":[{"key":"EntryName","value":"Tubulin/FtsZ, GTPase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002453","properties":[{"key":"EntryName","value":"Beta_tubulin"}]},{"database":"InterPro","id":"IPR008280","properties":[{"key":"EntryName","value":"Tub_FtsZ_C"}]},{"database":"InterPro","id":"IPR000217","properties":[{"key":"EntryName","value":"Tubulin"}]},{"database":"InterPro","id":"IPR037103","properties":[{"key":"EntryName","value":"Tubulin/FtsZ-like_C"}]},{"database":"InterPro","id":"IPR018316","properties":[{"key":"EntryName","value":"Tubulin/FtsZ_2-layer-sand-dom"}]},{"database":"InterPro","id":"IPR036525","properties":[{"key":"EntryName","value":"Tubulin/FtsZ_GTPase_sf"}]},{"database":"PANTHER","id":"PTHR11588","properties":[{"key":"EntryName","value":"TUBULIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03953","properties":[{"key":"EntryName","value":"Tubulin_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01163","properties":[{"key":"EntryName","value":"BETATUBULIN"}]},{"database":"SMART","id":"SM00865","properties":[{"key":"EntryName","value":"Tubulin_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55307","properties":[{"key":"EntryName","value":"Tubulin C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52490","properties":[{"key":"EntryName","value":"Tubulin nucleotide-binding domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"SDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIPNNVQTA","length":157,"molWeight":17771,"crc64":"53C9B8205C31ABCD","md5":"381466A076FE142A40DD6397675D3267"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0001F3B37B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"E5F093","uniProtkbId":"E5F093_9BASI","entryAudit":{"firstPublicDate":"2011-02-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-02-08","entryVersion":46,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Puccinia pseudostriiformis","taxonId":327555,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51619.1"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Pucciniomycotina","Pucciniomycetes","Pucciniales","Pucciniaceae","Puccinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51619.1"}],"value":"Beta-tubulin 1"}}],"flag":"Fragment"},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034296"}],"value":"Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin"}],"commentType":"FUNCTION"},{"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":"ARBA00011747"}],"value":"Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004245"}],"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009636"}],"value":"Belongs to the tubulin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Tubulin/FtsZ 2-layer sandwich","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00865"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51619.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51619.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023212"}],"id":"KW-0206","category":"Cellular component","name":"Cytoskeleton"},{"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":"ARBA00022701"}],"id":"KW-0493","category":"Cellular component","name":"Microtubule"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"20943198","citationType":"journal article","authors":["Liu M.","Hambleton S."],"citationCrossReferences":[{"database":"PubMed","id":"20943198"}],"title":"Taxonomic study of stripe rust, Puccinia striiformis sensu lato, based on molecular and morphological evidence.","publicationDate":"2010","journal":"Fungal Biol.","firstPage":"881","lastPage":"899","volume":"114"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51619.1"}],"value":"PUR 59733","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51619.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HM067996","properties":[{"key":"ProteinId","value":"ADR51619.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"E5F093","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005874","properties":[{"key":"GoTerm","value":"C:microtubule"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005200","properties":[{"key":"GoTerm","value":"F:structural constituent of cytoskeleton"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007017","properties":[{"key":"GoTerm","value":"P:microtubule-based process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.30.1330.20:FF:000009","properties":[{"key":"EntryName","value":"Tubulin beta chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1330.20","properties":[{"key":"EntryName","value":"Tubulin/FtsZ, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1440","properties":[{"key":"EntryName","value":"Tubulin/FtsZ, GTPase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002453","properties":[{"key":"EntryName","value":"Beta_tubulin"}]},{"database":"InterPro","id":"IPR008280","properties":[{"key":"EntryName","value":"Tub_FtsZ_C"}]},{"database":"InterPro","id":"IPR000217","properties":[{"key":"EntryName","value":"Tubulin"}]},{"database":"InterPro","id":"IPR037103","properties":[{"key":"EntryName","value":"Tubulin/FtsZ-like_C"}]},{"database":"InterPro","id":"IPR018316","properties":[{"key":"EntryName","value":"Tubulin/FtsZ_2-layer-sand-dom"}]},{"database":"InterPro","id":"IPR036525","properties":[{"key":"EntryName","value":"Tubulin/FtsZ_GTPase_sf"}]},{"database":"PANTHER","id":"PTHR11588","properties":[{"key":"EntryName","value":"TUBULIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03953","properties":[{"key":"EntryName","value":"Tubulin_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01163","properties":[{"key":"EntryName","value":"BETATUBULIN"}]},{"database":"SMART","id":"SM00865","properties":[{"key":"EntryName","value":"Tubulin_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55307","properties":[{"key":"EntryName","value":"Tubulin C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52490","properties":[{"key":"EntryName","value":"Tubulin nucleotide-binding domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"DETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIPNNVQTAHCD","length":159,"molWeight":18040,"crc64":"157E2A0B19CAAA50","md5":"74FA5F541BE513A439FC4FA63413D3D3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0001F3B384"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"G9B2G3","uniProtkbId":"G9B2G3_9BASI","entryAudit":{"firstPublicDate":"2012-02-22","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-02-22","entryVersion":42,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Puccinia pseudostriiformis","taxonId":327555,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEG78280.1"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Pucciniomycotina","Pucciniomycetes","Pucciniales","Pucciniaceae","Puccinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11436"},{"database":"Rhea","id":"RHEA-COMP:10350"},{"database":"Rhea","id":"RHEA-COMP:14399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"7.1.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit I profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50855"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEG78280.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEG78280.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEG78280.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEG78280.1"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"22492408","citationType":"journal article","authors":["Liu M.","Hambleton S."],"citationCrossReferences":[{"database":"PubMed","id":"22492408"},{"database":"DOI","id":"10.3852/11-251"}],"title":"Puccinia chunjii, a close relative of the cereal stem rusts revealed by molecular phylogeny and morphological study.","publicationDate":"2012","journal":"Mycologia","firstPage":"1056","lastPage":"1067","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEG78280.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HM147440","properties":[{"key":"ProteinId","value":"AEG78280.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"G9B2G3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00705","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006123","properties":[{"key":"GoTerm","value":"P:mitochondrial electron transport, cytochrome c to oxygen"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"1.20.210.10","properties":[{"key":"EntryName","value":"Cytochrome c oxidase-like, subunit I domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023616","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_dom"}]},{"database":"InterPro","id":"IPR036927","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_sf"}]},{"database":"InterPro","id":"IPR000883","properties":[{"key":"EntryName","value":"Cyt_C_Oxase_1"}]},{"database":"PANTHER","id":"PTHR10422","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10422:SF18","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00115","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01165","properties":[{"key":"EntryName","value":"CYCOXIDASEI"}]},{"database":"SUPFAM","id":"SSF81442","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit I-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50855","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"KDIAILYFVFGLFSALLGTGISILIRLELSAPGVGVLHGDNQLYNTIVTAHAFIIIFFFVMPVAVGGFGNYLCPVIVGAPDMAFPRLNNISFWLLCPSLILLVASSLIENG","length":111,"molWeight":11914,"crc64":"2CE162059EAC4766","md5":"66E2EE377A87B5FD6423100A486F5271"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":3,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI000243CCEA"}}]}