{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P86599","uniProtkbId":"FIBS_EUPSU","entryAudit":{"firstPublicDate":"2010-07-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2010-07-13","entryVersion":29,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"}],"value":"Fibrinolytic protease"},"ecNumbers":[{"value":"3.4.21.-"}]},"flag":"Fragments"},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"Serine protease with fibrinolytic activity"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00771"}],"value":"Secreted, extracellular space","id":"SL-0112"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":40,"modifier":"OUTSIDE"}},"description":"Fibrinolytic protease","featureId":"PRO_0000395363"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":40,"modifier":"OUTSIDE"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":null,"modifier":"UNKNOWN"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00771"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Non-adjacent residues","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"}]}],"keywords":[{"id":"KW-0094","category":"Biological process","name":"Blood coagulation"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0280","category":"Biological process","name":"Fibrinolysis"},{"id":"KW-0356","category":"Biological process","name":"Hemostasis"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8R8RD10J6V1E6","citationType":"submission","authors":["Maehashi K.","Inaba T.","Kashiwagi Y."],"title":"Isolation and characterization of fibrinolytic enzyme from Antarctic krill.","publicationDate":"MAY-2010","submissionDatabase":"UniProtKB"},"referencePositions":["PROTEIN SEQUENCE","FUNCTION"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"AlphaFoldDB","id":"P86599","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P86599","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"IVGGNEVTPHAYPWQVGLFIDDMYFCGGSISVTLTGWGKP","length":40,"molWeight":4314,"crc64":"5AF78CA2F0EC5C43","md5":"634E4804F0267A7F094C7D9BCCAAAD1A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Disulfide bond":1,"Non-adjacent residues":1,"Non-terminal residue":1},"uniParcId":"UPI0001D8973B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2I6BQ08","uniProtkbId":"A0A2I6BQ08_EUPSU","entryAudit":{"firstPublicDate":"2018-03-28","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-03-28","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AUI80372.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AUI80372.1"}],"value":"Shaggy"}}]},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005527"}],"value":"Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"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":"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":"29255161","citationType":"journal article","authors":["Biscontin A.","Wallach T.","Sales G.","Grudziecki A.","Janke L.","Sartori E.","Bertolucci C.","Mazzotta G.","De Pitta C.","Meyer B.","Kramer A.","Costa R."],"citationCrossReferences":[{"database":"PubMed","id":"29255161"},{"database":"DOI","id":"10.1038/s41598-017-18009-2"}],"title":"Functional characterization of the circadian clock in the Antarctic krill, Euphausia superba.","publicationDate":"2017","journal":"Sci. Rep.","firstPage":"17742","lastPage":"17742","volume":"7"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AUI80372.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KY923001","properties":[{"key":"ProteinId","value":"AUI80372.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A2I6BQ08","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0030424","properties":[{"key":"GoTerm","value":"C:axon"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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:0030154","properties":[{"key":"GoTerm","value":"P:cell differentiation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007276","properties":[{"key":"GoTerm","value":"P:gamete generation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0090090","properties":[{"key":"GoTerm","value":"P:negative regulation of canonical Wnt signaling pathway"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032436","properties":[{"key":"GoTerm","value":"P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070507","properties":[{"key":"GoTerm","value":"P:regulation of microtubule cytoskeleton organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007165","properties":[{"key":"GoTerm","value":"P:signal transduction"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd14137","properties":[{"key":"EntryName","value":"STKc_GSK3"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000055","properties":[{"key":"EntryName","value":"Glycogen synthase kinase-3 beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000009","properties":[{"key":"EntryName","value":"Glycogen synthase kinase-3 beta"},{"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":"IPR050591","properties":[{"key":"EntryName","value":"GSK-3"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_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":"IPR039192","properties":[{"key":"EntryName","value":"STKc_GSK3"}]},{"database":"PANTHER","id":"PTHR24057","properties":[{"key":"EntryName","value":"GLYCOGEN SYNTHASE KINASE-3 ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24057:SF0","properties":[{"key":"EntryName","value":"PROTEIN KINASE SHAGGY-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":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGRPRTTSFAEGNKGPPSVTFPGMKISSKDGNKITTVIATPGQGSDRPQEVSYMDTKVIGNGSFGVVFQAKLCETGELVAIKKVLQDKRFKNRELQIMRRLEHCNIVKLKYFFYSSGDKKEEVFLNLVLEFIPETVYKVARHHSKQKQTIPISYIKLYMYQLFRSLAYIHSLGFCHRDIKPQNLLLDPETGVLKLCDFGSAKHLVRGGPNVSYICSRYYRAPELIFGATDYTTNIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKSHPWQKVFRQRTPEDAITLVSRLLEYTPSARITPLQACAHKFFDELRNPDTRLPNNRELPPLFNFTEHEAKIQPELNSKLIPAHYRGEGGSSSSGGGGGGGGSSSVDTAEGAVAATVNDN","length":415,"molWeight":46268,"crc64":"30B315F5E0F720C6","md5":"DCD2CD8BC6CBA5AA0429E6738196CC18"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SIMILARITY":2},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":1},"uniParcId":"UPI000CA28C3E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D0E333","uniProtkbId":"D0E333_EUPSU","entryAudit":{"firstPublicDate":"2009-11-24","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-11-24","entryVersion":67,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33158.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"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"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33158.1"}],"value":"COI"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":391,"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":"ACX33158.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33158.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33158.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"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":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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":"ACX33158.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"20087386","citationType":"journal article","authors":["Goodall-Copestake W.P.","Perez-Espona S.","Clark M.S.","Murphy E.J.","Seear P.J.","Tarling G.A."],"citationCrossReferences":[{"database":"PubMed","id":"20087386"},{"database":"DOI","id":"10.1038/hdy.2009.188"}],"title":"Swarms of diversity at the gene cox1 in Antarctic krill.","publicationDate":"2010","journal":"Heredity","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33158.1"}],"value":"Hap_1","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33159.1"}],"value":"Hap_2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33158.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"GQ305462","properties":[{"key":"ProteinId","value":"ACX33158.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"GQ305463","properties":[{"key":"ProteinId","value":"ACX33159.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"D0E333","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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"IRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFP","length":391,"molWeight":42446,"crc64":"E46B9C5168981B03","md5":"D88D27D54D6B160585A921A6DB3FD0A5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":10,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0001B8920F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D0E3A3","uniProtkbId":"D0E3A3_EUPSU","entryAudit":{"firstPublicDate":"2009-11-24","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-11-24","entryVersion":64,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33228.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"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"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33228.1"}],"value":"COI"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":391,"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":"ACX33228.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33228.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33228.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"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":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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":"ACX33228.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"20087386","citationType":"journal article","authors":["Goodall-Copestake W.P.","Perez-Espona S.","Clark M.S.","Murphy E.J.","Seear P.J.","Tarling G.A."],"citationCrossReferences":[{"database":"PubMed","id":"20087386"},{"database":"DOI","id":"10.1038/hdy.2009.188"}],"title":"Swarms of diversity at the gene cox1 in Antarctic krill.","publicationDate":"2010","journal":"Heredity","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33228.1"}],"value":"Hap_71","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33228.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"GQ305532","properties":[{"key":"ProteinId","value":"ACX33228.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"D0E3A3","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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"IRAELGQPGSLIGDDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFP","length":391,"molWeight":42460,"crc64":"0ECCA6F87FDE4260","md5":"3B2A42D776EB1A462F6A8060085BE63B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":10,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0001B89215"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D0E3T4","uniProtkbId":"D0E3T4_EUPSU","entryAudit":{"firstPublicDate":"2009-11-24","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-11-24","entryVersion":64,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33409.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"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"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33409.1"}],"value":"COI"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":391,"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":"ACX33409.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33409.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33409.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"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":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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":"ACX33409.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"20087386","citationType":"journal article","authors":["Goodall-Copestake W.P.","Perez-Espona S.","Clark M.S.","Murphy E.J.","Seear P.J.","Tarling G.A."],"citationCrossReferences":[{"database":"PubMed","id":"20087386"},{"database":"DOI","id":"10.1038/hdy.2009.188"}],"title":"Swarms of diversity at the gene cox1 in Antarctic krill.","publicationDate":"2010","journal":"Heredity","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33409.1"}],"value":"Hap_252","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACX33409.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"GQ305713","properties":[{"key":"ProteinId","value":"ACX33409.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"D0E3T4","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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"IRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNITFFP","length":391,"molWeight":42460,"crc64":"E46B9C517A081B03","md5":"A2219BF2FFE567DAA47477825AF1AA9C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":10,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0001B8921C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D2SM45","uniProtkbId":"D2SM45_EUPSU","entryAudit":{"firstPublicDate":"2010-03-02","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2010-03-02","entryVersion":63,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACH78205.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACH78205.1"}],"value":"cox1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW68998.1"}],"value":"COI"}]}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":511,"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":"ACH78205.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACH78205.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"ACH78205.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"19578978","citationType":"journal article","authors":["Shen X.","Wang H.","Ren J.","Tian M.","Wang M."],"citationCrossReferences":[{"database":"PubMed","id":"19578978"},{"database":"DOI","id":"10.1007/s11033-009-9602-7"}],"title":"The mitochondrial genome of Euphausia superba (Prydz Bay) (Crustacea: Malacostraca: Euphausiacea) reveals a novel gene arrangement and potential molecular markers.","publicationDate":"2010","journal":"Mol. Biol. Rep.","firstPage":"771","lastPage":"784","volume":"37"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACH78205.1"}]},{"referenceNumber":2,"citation":{"id":"CI-B8OD1MUSLKH50","citationType":"submission","authors":["Zhao M.D.","Ma C.Y.","Ma L.B."],"title":"The complete mitochondrial genome of Euphausia superba (Eucarida: Euphausiacea).","publicationDate":"APR-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW68998.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"EU583500","properties":[{"key":"ProteinId","value":"ACH78205.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KX029326","properties":[{"key":"ProteinId","value":"AOW68998.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"YP_009559296.1","properties":[{"key":"NucleotideSequenceId","value":"NC_040987.1"}]},{"database":"AlphaFoldDB","id":"D2SM45","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"39119080","properties":[{"key":"Description","value":"-"}]},{"database":"CTD","id":"4512","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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"TQQRWLFSTNHKDIGTLYFIFGAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFPQHFLGLNGMPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":512,"molWeight":56064,"crc64":"4A7BB0476ADE5C6E","md5":"C83EABA844AD3CA959048CB042A062EE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":12,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI0001C3011C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"H2FEC1","uniProtkbId":"H2FEC1_EUPSU","entryAudit":{"firstPublicDate":"2012-03-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-03-21","entryVersion":55,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54939.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54939.1"}],"value":"cox1"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":494,"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":"AEX54939.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54939.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"AEX54939.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AESOV34Q1OKN3","citationType":"submission","authors":["Johansson M.L.","Duda E.","Sremba A.","Banks M.","Peterson W."],"publicationDate":"DEC-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54939.1"}]},{"referenceNumber":2,"citation":{"id":"22219085","citationType":"journal article","authors":["Johansson M.","Duda E.","Sremba A.","Banks M.","Peterson W."],"citationCrossReferences":[{"database":"PubMed","id":"22219085"},{"database":"DOI","id":"10.1007/s11033-011-1385-y"}],"title":"Assessing population-level variation in the mitochondrial genome of Euphausia superba using 454 next-generation sequencing.","publicationDate":"2012","journal":"Mol. Biol. Rep.","firstPage":"5755","lastPage":"5760","volume":"39"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54939.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JQ286347","properties":[{"key":"ProteinId","value":"AEX54939.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"SXXXGAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMXGAPDMAFPRMNNMSFWLXPXSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPXWLKLXFLVMFTGVNVTFFPQHFLGLNGXPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":495,"molWeight":53835,"crc64":"41D12151BFB7FB4F","md5":"4B78438B99FC61920C7F6472730CD7F2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI000246B284"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"H2FED3","uniProtkbId":"H2FED3_EUPSU","entryAudit":{"firstPublicDate":"2012-03-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-03-21","entryVersion":55,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54940.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54940.1"}],"value":"cox1"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":490,"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":"AEX54940.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54940.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"AEX54940.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AESOV34Q1OKN3","citationType":"submission","authors":["Johansson M.L.","Duda E.","Sremba A.","Banks M.","Peterson W."],"publicationDate":"DEC-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54940.1"}]},{"referenceNumber":2,"citation":{"id":"22219085","citationType":"journal article","authors":["Johansson M.","Duda E.","Sremba A.","Banks M.","Peterson W."],"citationCrossReferences":[{"database":"PubMed","id":"22219085"},{"database":"DOI","id":"10.1007/s11033-011-1385-y"}],"title":"Assessing population-level variation in the mitochondrial genome of Euphausia superba using 454 next-generation sequencing.","publicationDate":"2012","journal":"Mol. Biol. Rep.","firstPage":"5755","lastPage":"5760","volume":"39"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54940.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JQ286348","properties":[{"key":"ProteinId","value":"AEX54940.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"GAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPXSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFPQHFLGLNGMPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":491,"molWeight":53480,"crc64":"9809D7B68B5B293D","md5":"7BEB0FD298DC1CBFEF154E16B1FC3AFC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI000246B289"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"H2FEE5","uniProtkbId":"H2FEE5_EUPSU","entryAudit":{"firstPublicDate":"2012-03-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-03-21","entryVersion":55,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54963.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54963.1"}],"value":"cox1"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":494,"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":"AEX54963.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54963.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"AEX54963.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AESOV34Q1OKN3","citationType":"submission","authors":["Johansson M.L.","Duda E.","Sremba A.","Banks M.","Peterson W."],"publicationDate":"DEC-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54963.1"}]},{"referenceNumber":2,"citation":{"id":"22219085","citationType":"journal article","authors":["Johansson M.","Duda E.","Sremba A.","Banks M.","Peterson W."],"citationCrossReferences":[{"database":"PubMed","id":"22219085"},{"database":"DOI","id":"10.1007/s11033-011-1385-y"}],"title":"Assessing population-level variation in the mitochondrial genome of Euphausia superba using 454 next-generation sequencing.","publicationDate":"2012","journal":"Mol. Biol. Rep.","firstPage":"5755","lastPage":"5760","volume":"39"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54963.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JQ286349","properties":[{"key":"ProteinId","value":"AEX54963.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"LXFXGAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPXSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFPQHFLGLNGMPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":495,"molWeight":53963,"crc64":"7809D7AB200842AB","md5":"F2F663EDD1E77F88B1614622F44A3F8E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI000246B038"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"H2FEF7","uniProtkbId":"H2FEF7_EUPSU","entryAudit":{"firstPublicDate":"2012-03-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-03-21","entryVersion":55,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54964.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54964.1"}],"value":"cox1"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":490,"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":"AEX54964.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54964.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"AEX54964.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AESOV34Q1OKN3","citationType":"submission","authors":["Johansson M.L.","Duda E.","Sremba A.","Banks M.","Peterson W."],"publicationDate":"DEC-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54964.1"}]},{"referenceNumber":2,"citation":{"id":"22219085","citationType":"journal article","authors":["Johansson M.","Duda E.","Sremba A.","Banks M.","Peterson W."],"citationCrossReferences":[{"database":"PubMed","id":"22219085"},{"database":"DOI","id":"10.1007/s11033-011-1385-y"}],"title":"Assessing population-level variation in the mitochondrial genome of Euphausia superba using 454 next-generation sequencing.","publicationDate":"2012","journal":"Mol. Biol. Rep.","firstPage":"5755","lastPage":"5760","volume":"39"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54964.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JQ286350","properties":[{"key":"ProteinId","value":"AEX54964.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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":"GAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMXGAPDMAFPRMNNMSFWLXPXSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITXLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHXFTVGMDVXTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNXSPSLIWALGFVFLFTVGGXTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFPQHFLGLNGMPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":491,"molWeight":53380,"crc64":"07B3F8E360D8E517","md5":"13883E5E16629C3985E805469C32EA5E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI000246B040"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"H2FEG9","uniProtkbId":"H2FEG9_EUPSU","entryAudit":{"firstPublicDate":"2012-03-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-03-21","entryVersion":55,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54976.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54976.1"}],"value":"cox1"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":490,"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":"AEX54976.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54976.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"AEX54976.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AESOV34Q1OKN3","citationType":"submission","authors":["Johansson M.L.","Duda E.","Sremba A.","Banks M.","Peterson W."],"publicationDate":"DEC-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54976.1"}]},{"referenceNumber":2,"citation":{"id":"22219085","citationType":"journal article","authors":["Johansson M.","Duda E.","Sremba A.","Banks M.","Peterson W."],"citationCrossReferences":[{"database":"PubMed","id":"22219085"},{"database":"DOI","id":"10.1007/s11033-011-1385-y"}],"title":"Assessing population-level variation in the mitochondrial genome of Euphausia superba using 454 next-generation sequencing.","publicationDate":"2012","journal":"Mol. Biol. Rep.","firstPage":"5755","lastPage":"5760","volume":"39"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AEX54976.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JQ286351","properties":[{"key":"ProteinId","value":"AEX54976.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"GAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMXGAPDMAFPRMNNMSFWLXPXSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFPQHFLGLNGMPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":491,"molWeight":53477,"crc64":"92A2CA7F4717A782","md5":"900F5CD48D58F17C6CDCA2664892D655"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI000246B048"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q76L79","uniProtkbId":"Q76L79_EUPSU","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":99,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAD16761.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAD16761.1"}],"value":"cox1"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001935"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"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"}},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":511,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit I profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50855"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAD16761.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"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":"BAD16761.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"15136912","citationType":"journal article","authors":["Machida R.J.","Miya M.U.","Yamauchi M.M.","Nishida M.","Nishida S."],"citationCrossReferences":[{"database":"PubMed","id":"15136912"},{"database":"DOI","id":"10.1007/s10126-003-0016-6"}],"title":"Organization of the mitochondrial genome of Antarctic krill Euphausia superba (Crustacea: Malacostraca).","publicationDate":"2004","journal":"Mar. Biotechnol.","firstPage":"238","lastPage":"250","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAD16761.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB084378","properties":[{"key":"ProteinId","value":"BAD16761.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q76L79","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:0045277","properties":[{"key":"GoTerm","value":"C:respiratory chain complex IV"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"CDD","id":"cd01663","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"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":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR033944","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su1_dom"}]},{"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"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQQRWLFSTNHKDIGTLYFIFGAWAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPAFGMISHIISQESGKKQAFGTLGMIYAMMAIGVLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLGTLHGAQLNYSPSLIWALGFVFLFTVGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFGIFAGIAHWFPLFTGLTMNPKWLKLHFLVMFTGVNVTFFPQHFLGLNGMPRRYSDYPDAYTPWNVLSSIGSTISLIAVLGFMLIVWEALVSARPVLFSLFLPTSLEWEHNLPPADHSYMEIPMISA","length":512,"molWeight":56094,"crc64":"549680476ADE5C6A","md5":"F66114BD7CBC35B03A8A878E137DC016"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":12,"Domain":1},"uniParcId":"UPI00003596B4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A089V818","uniProtkbId":"A0A089V818_EUPSU","entryAudit":{"firstPublicDate":"2014-11-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2014-11-26","entryVersion":33,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72274.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72274.1"}],"value":"Hsp70D"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72274.1"}],"value":"HSP70"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007381"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"value":"Belongs to the heat shock protein 70 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Region","location":{"start":{"value":657,"modifier":"EXACT"},"end":{"value":688,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":610,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":663,"modifier":"EXACT"},"end":{"value":676,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":677,"modifier":"EXACT"},"end":{"value":688,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"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":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9PUF9AA0UIKEK","citationType":"submission","authors":["Cascella K.","Jollivet D.","Papot C.","Leger N.","Corre E.","Ravaux J.","Clark M.S.","Toullec J.Y."],"title":"Diversification, evolution and sub-functionalization of 70kDa heat-shock proteins in two sister species of Antarctic krill: Differences in thermal habitats, responses and implications under climate change.","publicationDate":"JUN-2014","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72274.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KM067148","properties":[{"key":"ProteinId","value":"AIR72274.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A089V818","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006457","properties":[{"key":"GoTerm","value":"P:protein folding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd11733","properties":[{"key":"EntryName","value":"ASKHA_NBD_HSP70_HSPA9"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.34.10:FF:000006","properties":[{"key":"EntryName","value":"Heat shock protein cognate 5"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000004","properties":[{"key":"EntryName","value":"Molecular chaperone DnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.640.10:FF:000003","properties":[{"key":"EntryName","value":"Molecular chaperone DnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1270.10:FF:000011","properties":[{"key":"EntryName","value":"stress-70 protein, mitochondrial isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1270.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.30.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.90.640.10","properties":[{"key":"EntryName","value":"Actin, Chain A, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.34.10","properties":[{"key":"EntryName","value":"Substrate Binding Domain Of DNAk, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00332","properties":[{"key":"EntryName","value":"DnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR012725","properties":[{"key":"EntryName","value":"Chaperone_DnaK"}]},{"database":"InterPro","id":"IPR018181","properties":[{"key":"EntryName","value":"Heat_shock_70_CS"}]},{"database":"InterPro","id":"IPR029048","properties":[{"key":"EntryName","value":"HSP70_C_sf"}]},{"database":"InterPro","id":"IPR029047","properties":[{"key":"EntryName","value":"HSP70_peptide-bd_sf"}]},{"database":"InterPro","id":"IPR013126","properties":[{"key":"EntryName","value":"Hsp_70_fam"}]},{"database":"NCBIfam","id":"NF001413","properties":[{"key":"EntryName","value":"dnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02350","properties":[{"key":"EntryName","value":"prok_dnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19375","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 70KDA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00012","properties":[{"key":"EntryName","value":"HSP70"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00301","properties":[{"key":"EntryName","value":"HEATSHOCK70"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF100934","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100920","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00297","properties":[{"key":"EntryName","value":"HSP70_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00329","properties":[{"key":"EntryName","value":"HSP70_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01036","properties":[{"key":"EntryName","value":"HSP70_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLSKAKFIATNVGALSSKSHVGAILNKAAVPTYLTQRDVLQTQIRHKSDGVKGAVIGIDLGTTNSCVAVMEGKTAKVITNAEGDRTTPSVVAFGKDGERLVGIQAKRQAVTNAGNTFYGTKRFIGRRFEDAEIQKEKDIVAFKIVKASNGDAWVESTEGKMYSPSQIGAFTLMKMKETAESYLGTSVKNAVVTVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGMDKSEDKIIAVYDLGGGTFDVSILEIQKGVFEVKSTNGDTFLGGEDFDNHLVQFLASEFKKEQGLDVTKDNMAMQRLKEAAEKAKIELSAGQQTDINLPYLTMDASGPKHMMLKLTRAKFESIVDKLIKRTVDPCVKAIKDAEVAKSEIGEVLLVGGMTRMPKVQATVRDLFGREPSKAVNPDEAVAMGASIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVMTKLINRNTTIPTRKSQVFSTAADGQTQVEIKIHQGEREMAADNKVLGQFSLIGIPPAPRGVPQVEVTFDIDANGIVHVSARDKGTGKEQQVVIQSSGGLSKEEIENMIKKAEQMADEDRKKKDLVEAINQGESIMHDTESKMDEYKDQLPEEETTKIKEQITKVKDLLANKDSVDPETIKKEVSDLQQSSLKLFEMAYKKMAAERESSGSSSSGSSESSSDSSEKKEDSGEKK","length":688,"molWeight":74439,"crc64":"6E202306CB356C8E","md5":"49A42EA56A06E3117F304B5BEEDF012C"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Region":1,"Coiled coil":1,"Compositional bias":2},"uniParcId":"UPI00050D6AE1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A089VES1","uniProtkbId":"A0A089VES1_EUPSU","entryAudit":{"firstPublicDate":"2014-11-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2014-11-26","entryVersion":30,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72271.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072095"}],"value":"Heat shock 70 kDa protein cognate 4"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72271.1"}],"value":"HSP70"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007381"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"value":"Belongs to the heat shock protein 70 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Region","location":{"start":{"value":615,"modifier":"EXACT"},"end":{"value":654,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":632,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":633,"modifier":"EXACT"},"end":{"value":647,"modifier":"EXACT"}},"description":"Gly 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":"AIR72271.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"27087928","citationType":"journal article","authors":["Papot C.","Cascella K.","Toullec J.Y.","Jollivet D."],"citationCrossReferences":[{"database":"PubMed","id":"27087928"},{"database":"DOI","id":"10.1002/ece3.1989"}],"title":"Divergent ecological histories of two sister Antarctic krill species led to contrasted patterns of genetic diversity in their heat-shock protein (hsp70) arsenal.","publicationDate":"2016","journal":"Ecol. Evol.","firstPage":"1555","lastPage":"1575","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72271.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KM067145","properties":[{"key":"ProteinId","value":"AIR72271.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A089VES1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006950","properties":[{"key":"GoTerm","value":"P:response to stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd10233","properties":[{"key":"EntryName","value":"ASKHA_NBD_HSP70_HSPA1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.34.10:FF:000002","properties":[{"key":"EntryName","value":"Heat shock 70 kDa"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.30.30:FF:000001","properties":[{"key":"EntryName","value":"heat shock 70 kDa protein-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000028","properties":[{"key":"EntryName","value":"heat shock 70 kDa protein-like"},{"key":"MatchStatus","value":"2"}]},{"database":"FunFam","id":"3.90.640.10:FF:000134","properties":[{"key":"EntryName","value":"Heat shock cognate 71 kDa protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1270.10:FF:000003","properties":[{"key":"EntryName","value":"heat shock cognate 71 kDa protein-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1270.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.30.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.90.640.10","properties":[{"key":"EntryName","value":"Actin, Chain A, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.34.10","properties":[{"key":"EntryName","value":"Substrate Binding Domain Of DNAk, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR018181","properties":[{"key":"EntryName","value":"Heat_shock_70_CS"}]},{"database":"InterPro","id":"IPR029048","properties":[{"key":"EntryName","value":"HSP70_C_sf"}]},{"database":"InterPro","id":"IPR029047","properties":[{"key":"EntryName","value":"HSP70_peptide-bd_sf"}]},{"database":"InterPro","id":"IPR013126","properties":[{"key":"EntryName","value":"Hsp_70_fam"}]},{"database":"NCBIfam","id":"NF001413","properties":[{"key":"EntryName","value":"dnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19375","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 70KDA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00012","properties":[{"key":"EntryName","value":"HSP70"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00301","properties":[{"key":"EntryName","value":"HEATSHOCK70"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF100934","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100920","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00297","properties":[{"key":"EntryName","value":"HSP70_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00329","properties":[{"key":"EntryName","value":"HSP70_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01036","properties":[{"key":"EntryName","value":"HSP70_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"PKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPCNTVFDAKRLIGRKFEDPIVQADMKHWPFDVIDDGGGKPKLQVEFKGEKKNFFPEEISSMVLNKMRDTAEAYLGSTVKDAVITVPAYFNDSQRQATKDAGTISGLNVLRIINEPTAAAIAYGLDKKVGGERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFLQEFKRKYKKDPQDNKRALRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKSLRDAKMDKATIHDIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSEAVQDLLLLDVAPLSMGIETAGGVMTSLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERTMTKDNHLLGKFELTGIPPAPRGVPQIEVTFDVDANGILNVSAVDKSTGKENKITITNDKGRLSKEEIERMVQDAEKFKADDEKQKERIASKNSLESYCFNMKSTVEDDKFKDKVPEDDRTKIMEACNEAIKWLDANQLGEKEEYEHKQKEIEQICNPIITKMYQAAGGAPGGMPSGFPGSDAGAPGAGAPPGAGSGGSGPTIEEVD","length":654,"molWeight":71510,"crc64":"E691B3826858E77D","md5":"24868E17502CD6D3B5C058802A00FA42"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Region":1,"Compositional bias":2,"Non-terminal residue":1},"uniParcId":"UPI00050D1C41"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A089WXJ2","uniProtkbId":"A0A089WXJ2_EUPSU","entryAudit":{"firstPublicDate":"2014-11-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2014-11-26","entryVersion":28,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72272.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072095"}],"value":"Heat shock 70 kDa protein cognate 4"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72272.1"}],"value":"HSP70"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007381"}],"value":"Belongs to the heat shock protein 70 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Region","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"Gly 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":"AIR72272.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9PUF9AA0UIKEK","citationType":"submission","authors":["Cascella K.","Jollivet D.","Papot C.","Leger N.","Corre E.","Ravaux J.","Clark M.S.","Toullec J.Y."],"title":"Diversification, evolution and sub-functionalization of 70kDa heat-shock proteins in two sister species of Antarctic krill: Differences in thermal habitats, responses and implications under climate change.","publicationDate":"JUN-2014","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AIR72272.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KM067146","properties":[{"key":"ProteinId","value":"AIR72272.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A089WXJ2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"2.60.34.10:FF:000002","properties":[{"key":"EntryName","value":"Heat shock 70 kDa"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.640.10:FF:000058","properties":[{"key":"EntryName","value":"Heat shock 70 kDa protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000135","properties":[{"key":"EntryName","value":"Heat shock cognate 71 kDa protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1270.10:FF:000003","properties":[{"key":"EntryName","value":"heat shock cognate 71 kDa protein-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1270.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.640.10","properties":[{"key":"EntryName","value":"Actin, Chain A, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.34.10","properties":[{"key":"EntryName","value":"Substrate Binding Domain Of DNAk, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR018181","properties":[{"key":"EntryName","value":"Heat_shock_70_CS"}]},{"database":"InterPro","id":"IPR029048","properties":[{"key":"EntryName","value":"HSP70_C_sf"}]},{"database":"InterPro","id":"IPR029047","properties":[{"key":"EntryName","value":"HSP70_peptide-bd_sf"}]},{"database":"InterPro","id":"IPR013126","properties":[{"key":"EntryName","value":"Hsp_70_fam"}]},{"database":"PANTHER","id":"PTHR19375","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 70KDA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00012","properties":[{"key":"EntryName","value":"HSP70"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00301","properties":[{"key":"EntryName","value":"HEATSHOCK70"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100934","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100920","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01036","properties":[{"key":"EntryName","value":"HSP70_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"DFDNRMVNFFVQEFKRKYKKDLSSNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELCSDLFRGTLEPVEKSIRDAKMDKSAIHDIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILGGDKSEAVQDLLLLDVTPLSLGIETAGGVMTSLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQVEVTFDIDANGILNVTACDKSTGKENKITITNDKGRLSKEDIEKMVNEAEKYKSEDEAQRERINGKNALESYCFNMKSTVEDEKFKDKVPDSDRQTILEKCNETIQWLDANQLAEKEEYEHKQKDVEKVCSPIISKMYEAAGGAPGDMPGGMPGGMPGGMPGGAPGGAPGAGQGGAGGPTIEEVD","length":427,"molWeight":46741,"crc64":"F86697E1244B905E","md5":"F7AA8970F142ABE070C71BE5A4A23BD1"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Non-terminal residue":1},"uniParcId":"UPI00050D7451"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Y0R1G6","uniProtkbId":"A0A0Y0R1G6_EUPSU","entryAudit":{"firstPublicDate":"2016-04-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-04-13","entryVersion":32,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66846.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"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"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66846.1"}],"value":"COI"}}],"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":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"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":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":185,"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":"AMB66846.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66846.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66846.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"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":"AMB66846.1"}],"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":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"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":"27087928","citationType":"journal article","authors":["Papot C.","Cascella K.","Toullec J.Y.","Jollivet D."],"citationCrossReferences":[{"database":"PubMed","id":"27087928"},{"database":"DOI","id":"10.1002/ece3.1989"}],"title":"Divergent ecological histories of two sister Antarctic krill species led to contrasted patterns of genetic diversity in their heat-shock protein (hsp70) arsenal.","publicationDate":"2016","journal":"Ecol. Evol.","firstPage":"1555","lastPage":"1575","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66854.1"}],"value":"ES100COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66852.1"}],"value":"ES128COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66850.1"}],"value":"ES14bCOI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66861.1"}],"value":"ES35COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66859.1"}],"value":"ES36COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66847.1"}],"value":"ES37COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66855.1"}],"value":"ES38COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66848.1"}],"value":"ES40COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66857.1"}],"value":"ES44COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66856.1"}],"value":"ES45COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66858.1"}],"value":"ES46COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66853.1"}],"value":"ES50COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66862.1"}],"value":"ES56COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66863.1"}],"value":"ES63COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66865.1"}],"value":"ES65COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66851.1"}],"value":"ES69COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66849.1"}],"value":"ES73COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66866.1"}],"value":"ES75COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66860.1"}],"value":"ES77COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66867.1"}],"value":"ES78COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66868.1"}],"value":"ES85COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66846.1"}],"value":"ES97COI","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66864.1"}],"value":"ES99COI","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMB66846.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT586572","properties":[{"key":"ProteinId","value":"AMB66846.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586573","properties":[{"key":"ProteinId","value":"AMB66847.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586574","properties":[{"key":"ProteinId","value":"AMB66848.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586575","properties":[{"key":"ProteinId","value":"AMB66849.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586576","properties":[{"key":"ProteinId","value":"AMB66850.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586577","properties":[{"key":"ProteinId","value":"AMB66851.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586578","properties":[{"key":"ProteinId","value":"AMB66852.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586579","properties":[{"key":"ProteinId","value":"AMB66853.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586580","properties":[{"key":"ProteinId","value":"AMB66854.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586581","properties":[{"key":"ProteinId","value":"AMB66855.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586582","properties":[{"key":"ProteinId","value":"AMB66856.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586583","properties":[{"key":"ProteinId","value":"AMB66857.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586584","properties":[{"key":"ProteinId","value":"AMB66858.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586585","properties":[{"key":"ProteinId","value":"AMB66859.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586586","properties":[{"key":"ProteinId","value":"AMB66860.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586587","properties":[{"key":"ProteinId","value":"AMB66861.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586588","properties":[{"key":"ProteinId","value":"AMB66862.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586589","properties":[{"key":"ProteinId","value":"AMB66863.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586590","properties":[{"key":"ProteinId","value":"AMB66864.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586591","properties":[{"key":"ProteinId","value":"AMB66865.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586592","properties":[{"key":"ProteinId","value":"AMB66866.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586593","properties":[{"key":"ProteinId","value":"AMB66867.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT586594","properties":[{"key":"ProteinId","value":"AMB66868.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A0Y0R1G6","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":"WAGMVGTSLSLIIRAELGQPGSLIGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLGSGLVESGVGTGWTVYPPLSAGIAHAGASVDMGIFSLHIAGASSILGAVNFITTVINMRSAGMTMDRIPLFVWSVFITAILLLLSLPVLAGAITML","length":185,"molWeight":19525,"crc64":"EB297C8723A95745","md5":"8EE3D32329A30E6E9A6776AD5CE89AD6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":4,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI000764FB15"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1D8QLQ0","uniProtkbId":"A0A1D8QLQ0_EUPSU","entryAudit":{"firstPublicDate":"2017-01-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-01-18","entryVersion":26,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41606.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41606.1"}],"value":"Trypsin"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41606.1"}],"value":"3.4.21.4"}]}]},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.","ecNumber":"3.4.21.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10078"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004613"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":619,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5053018846"},{"type":"Domain","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":611,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Region","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":563,"modifier":"EXACT"},"end":{"value":563,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":533,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":587,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1EKITGHMU5KBC","citationType":"submission","authors":["Zhou T.","Wang X."],"title":"Analysis on Gene and Cold-Adaptation of Trypsin from the Krill, Euphausia superba (Dana, 1852).","publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41606.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT826547","properties":[{"key":"ProteinId","value":"AOW41606.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1D8QLQ0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00190","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.10:FF:000003","properties":[{"key":"EntryName","value":"Transmembrane serine protease 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001314","properties":[{"key":"EntryName","value":"Peptidase_S1A"}]},{"database":"InterPro","id":"IPR050127","properties":[{"key":"EntryName","value":"Serine_Proteases_S1"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"InterPro","id":"IPR018114","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"}]},{"database":"InterPro","id":"IPR033116","properties":[{"key":"EntryName","value":"TRYPSIN_SER"}]},{"database":"InterPro","id":"IPR000884","properties":[{"key":"EntryName","value":"TSP1_rpt"}]},{"database":"PANTHER","id":"PTHR24264:SF65","properties":[{"key":"EntryName","value":"SRCR DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24264","properties":[{"key":"EntryName","value":"TRYPSIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00722","properties":[{"key":"EntryName","value":"CHYMOTRYPSIN"}]},{"database":"SMART","id":"SM00020","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00209","properties":[{"key":"EntryName","value":"TSP1"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50240","properties":[{"key":"EntryName","value":"TRYPSIN_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00134","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50092","properties":[{"key":"EntryName","value":"TSP1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVNRLLMMILYGSVCLCYLSHVTSATRRTRIKSKHQTDQNDSDITTNIAVKSHRGLGDSILKSILSSKRNVRLNSRLSARRLTKRKGGNKRRHKKHRRNQMRSKKNDKVTLSVGSSSMEVSVAGYNVGDSGLYSSWSPWSHCTRHCRQRRQKACKSKHICGTSLLKEERSCSSGRCNKGKPFHVIRREDIGRYNAQDDVRVLLNFNSMFYTGWGRWSPCSRSCLTRRYRSCKYGSFCGGSVVHEEAYCYTTGSLCEQWYKRNKQSSEQPSEQPQQLHILSLNDNNQHHTLNKDKNGRSTEKDDKNAYSMIVYEKETTPATTTQPAFSNYFKASTLSTGLQGATKTHLPSSISPYSGYGTSDAPKSNHKCGISTKNLSLKIIGGQEAIKGKWPWQVVILNRYKEAFCGGTLVAPRWVLTAAHCVRKKLFVRIGEHDLAIPEGTEQEFKVVEAVIHPKYDSTTVDNDVALLKLPVALKPGNSPASPACLPEQGSSLPVGSACTIIGWGKERDTHIFGTDILHEAQVPVISAQSCRQVYKDYFITNNMFCAGFKKGRIDSCAGDSGGPLLCQRQGRWFIYGITSFGEGCGKRGKFGIYSRVSNYYKWIQDVIKDHYRSSNS","length":619,"molWeight":69461,"crc64":"C4810E2D54D41E06","md5":"68FCE09B540FC037F0BE56749FFAD211"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Region":2,"Compositional bias":2,"Active site":3,"Disulfide bond":3},"uniParcId":"UPI00087CCBCE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1D8QLQ2","uniProtkbId":"A0A1D8QLQ2_EUPSU","entryAudit":{"firstPublicDate":"2017-01-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-01-18","entryVersion":25,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41605.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066707"}],"value":"limulus clotting factor C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066707"}],"value":"3.4.21.84"}]}},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.","ecNumber":"3.4.21.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates.","ecNumber":"3.4.21.84","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052079"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004613"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Region","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022820"}],"id":"KW-0353","category":"Biological process","name":"Hemolymph clotting"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022659"}],"id":"KW-0768","category":"Domain","name":"Sushi"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1EKITGHMU5KBC","citationType":"submission","authors":["Zhou T.","Wang X."],"title":"Analysis on Gene and Cold-Adaptation of Trypsin from the Krill, Euphausia superba (Dana, 1852).","publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41605.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT826546","properties":[{"key":"ProteinId","value":"AOW41605.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1D8QLQ2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00190","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.10:FF:000120","properties":[{"key":"EntryName","value":"Putative serine protease"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001314","properties":[{"key":"EntryName","value":"Peptidase_S1A"}]},{"database":"InterPro","id":"IPR050127","properties":[{"key":"EntryName","value":"Serine_Proteases_S1"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"InterPro","id":"IPR018114","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"}]},{"database":"InterPro","id":"IPR033116","properties":[{"key":"EntryName","value":"TRYPSIN_SER"}]},{"database":"PANTHER","id":"PTHR24264:SF65","properties":[{"key":"EntryName","value":"SRCR DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24264","properties":[{"key":"EntryName","value":"TRYPSIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00722","properties":[{"key":"EntryName","value":"CHYMOTRYPSIN"}]},{"database":"SMART","id":"SM00020","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50240","properties":[{"key":"EntryName","value":"TRYPSIN_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00134","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVVVVVEGSDDNPLDVSLASLIYYPPDMWSRCTRSCLTRRFRKCKFPELCGKEKLQEEAFCYAPGSTCEEKVQLLLQEEGYIIVDEEELDIGQEHENNINEGEDERGQPEDAMGPNQQDYDYESVVYDNDQGGEEKIESNDDEEYIHSSDEQTSDYYDEVVDNYDDGRDWVPQAYDDYEYYETEEDSLDNNPIGFDYNYDYTFLVPDDFVEYDENHVDHAEEDYDYSWSDWVTGGKFEYDYETPDYENEYTSHTTEEQSIQMPSEYAHKIDTDENTAAQCGTPSVKSRSNFLRIIGGKEAIPGEFPWQVAVLNRFKEVFCGGVVIAPQWILTAAHCVRKKLYVRLAEHDIRDYEGRELEIKVHKIFKHPEYDLETIENDIALLKLPKKVQLGKHIQQICLPVQATPPPVGNKCMIAGWGKERESHIFGSDILNYAKVPIVSRKVCRAAYPEHPITRNHVCAGYQRGNIDSCAGDSGGPLLCKGENGLWTVHGVTSFGEGCGETGKFGVYTKVANYIHWIRKTMKENVT","length":528,"molWeight":60497,"crc64":"79152267D131F72C","md5":"2C87F453AD2DC007F59C71D65D79616E"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Active site":3,"Disulfide bond":2},"uniParcId":"UPI00087D16C7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1D8QLQ3","uniProtkbId":"A0A1D8QLQ3_EUPSU","entryAudit":{"firstPublicDate":"2017-01-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-01-18","entryVersion":27,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41607.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066707"}],"value":"limulus clotting factor C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066707"}],"value":"3.4.21.84"}]}},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.","ecNumber":"3.4.21.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates.","ecNumber":"3.4.21.84","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052079"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004613"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Domain","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":544,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022820"}],"id":"KW-0353","category":"Biological process","name":"Hemolymph clotting"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022659"}],"id":"KW-0768","category":"Domain","name":"Sushi"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1EKITGHMU5KBC","citationType":"submission","authors":["Zhou T.","Wang X."],"title":"Analysis on Gene and Cold-Adaptation of Trypsin from the Krill, Euphausia superba (Dana, 1852).","publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41607.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT826548","properties":[{"key":"ProteinId","value":"AOW41607.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1D8QLQ3","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A1D8QLQ3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00190","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"2"}]},{"database":"FunFam","id":"2.40.10.10:FF:000120","properties":[{"key":"EntryName","value":"Putative serine protease"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.10:FF:000038","properties":[{"key":"EntryName","value":"Serine protease"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001314","properties":[{"key":"EntryName","value":"Peptidase_S1A"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"InterPro","id":"IPR018114","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"}]},{"database":"InterPro","id":"IPR033116","properties":[{"key":"EntryName","value":"TRYPSIN_SER"}]},{"database":"PANTHER","id":"PTHR24252","properties":[{"key":"EntryName","value":"ACROSIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24252:SF7","properties":[{"key":"EntryName","value":"HYALIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00722","properties":[{"key":"EntryName","value":"CHYMOTRYPSIN"}]},{"database":"SMART","id":"SM00020","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50240","properties":[{"key":"EntryName","value":"TRYPSIN_DOM"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00134","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSGSGWCPAGATPATPAPTETPTGTCTCGRVNRASRIVGGVETEVNEYPWMVALAWSASSNNAFCGASIINERWILTASHCADVMSTSNVVVVGEHSWSSSSESSATQKYAIEQILMHPNYDSGTLENDVALVKLATSLSFDDNNNVAPVCPPDATNLYEDVDAIVSGWGTLSSGGSQPDSLQEVVVPTMSNSACQSGYGSSITDNMLCAGFDAGGKDSCQGDSGGPLVTADGSIYRQIGVVSWGYGCASAGYPGVYARVNSQLAWITASISGTSWCDAGTAVTSGPINTTPAPTETPTGDCKCGRVNRQTRIINGQETEVLEYPWQAGLVGYGGDRTFCGGSLVNSKWVLTAAHCTDGTSPSQIQVLLGEHTIYDTDATEERFSVTQVINHPSYITNPWNNGHDVSLLELSGEVDFSSSRIRPICLPSTVDLFAGAEATITGWGTTNSGSQSLVLMEVDIPVVTNTVCENTYGPSNIDDTMICAGEGAGNGACMGDSGGPLITSLGDYHVQIGVVSFGSSNCDALGVYARVTALKSWIEGYAMAGSAEVCST","length":553,"molWeight":57512,"crc64":"8B36826FC7A6388F","md5":"BA0BBEF8233BF5DC1013C2D4A6914861"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Active site":6,"Disulfide bond":4},"uniParcId":"UPI00087AAC48"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1D8QLQ4","uniProtkbId":"A0A1D8QLQ4_EUPSU","entryAudit":{"firstPublicDate":"2017-01-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-01-18","entryVersion":22,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41609.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41609.1"}],"value":"Trypsin"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41609.1"}],"value":"3.4.21.4"}]}]},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.","ecNumber":"3.4.21.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10078"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007664"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5009111354"},{"type":"Domain","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Active site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1EKITGHMU5KBC","citationType":"submission","authors":["Zhou T.","Wang X."],"title":"Analysis on Gene and Cold-Adaptation of Trypsin from the Krill, Euphausia superba (Dana, 1852).","publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41609.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT826551","properties":[{"key":"ProteinId","value":"AOW41609.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1D8QLQ4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A1D8QLQ4","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00190","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.10:FF:000077","properties":[{"key":"EntryName","value":"Predicted protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001314","properties":[{"key":"EntryName","value":"Peptidase_S1A"}]},{"database":"InterPro","id":"IPR050127","properties":[{"key":"EntryName","value":"Serine_Proteases_S1"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"InterPro","id":"IPR018114","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"}]},{"database":"InterPro","id":"IPR033116","properties":[{"key":"EntryName","value":"TRYPSIN_SER"}]},{"database":"PANTHER","id":"PTHR24264:SF83","properties":[{"key":"EntryName","value":"COMPLEMENT FACTOR I"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24264","properties":[{"key":"EntryName","value":"TRYPSIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00722","properties":[{"key":"EntryName","value":"CHYMOTRYPSIN"}]},{"database":"SMART","id":"SM00020","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50240","properties":[{"key":"EntryName","value":"TRYPSIN_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00134","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRSLLVLLVSITVAAAFPRVQEIPLEYRLPDNRIVGGVIAEDGEFPWQISMQHKGLFGYSHMCGGSVHSENYIITAGHCTDGQNAAKILVIAGTNVLSDLTGAEVQQIAADELVHHEHYDSSTITNDISLIHLSTPLVMNAKVQPVPLPDQMDTIEAGTECIISGWGTLHEGALGLPDNLMKVTVPVVTDEVCREAYSITQIGDGMICAGLDEGGKDSCQGDSGGPFVCDGVLHGVVSWGRGCAEPHYPGVYTEVAYYRDWIDAHAV","length":267,"molWeight":28626,"crc64":"162847E53A27A27F","md5":"E4256AF7870574CC8CCB3E08D5FD37B8"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Active site":3,"Disulfide bond":2},"uniParcId":"UPI00087B0249"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1D8QLQ5","uniProtkbId":"A0A1D8QLQ5_EUPSU","entryAudit":{"firstPublicDate":"2017-01-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-01-18","entryVersion":18,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41610.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41610.1"}],"value":"Trypsin"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41610.1"}],"value":"3.4.21.4"}]}]},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.","ecNumber":"3.4.21.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10079"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5009111411"},{"type":"Domain","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Active site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41610.1"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1EKITGHMU5KBC","citationType":"submission","authors":["Zhou T.","Wang X."],"title":"Analysis on Gene and Cold-Adaptation of Trypsin from the Krill, Euphausia superba (Dana, 1852).","publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41610.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT826552","properties":[{"key":"ProteinId","value":"AOW41610.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1D8QLQ5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A1D8QLQ5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00190","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.10:FF:000111","properties":[{"key":"EntryName","value":"Blast:Serine protease nudel"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001314","properties":[{"key":"EntryName","value":"Peptidase_S1A"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"InterPro","id":"IPR033116","properties":[{"key":"EntryName","value":"TRYPSIN_SER"}]},{"database":"PANTHER","id":"PTHR24252","properties":[{"key":"EntryName","value":"ACROSIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24252:SF7","properties":[{"key":"EntryName","value":"HYALIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00722","properties":[{"key":"EntryName","value":"CHYMOTRYPSIN"}]},{"database":"SMART","id":"SM00020","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50240","properties":[{"key":"EntryName","value":"TRYPSIN_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRGICKMKGFVICLLVAGACAAPSRKPTFRKGLNKIVGGDEAAPGELPYQLSFQDLSYGDPWHFCGASIYNENWAICAGHCVAGEDMNNPDYLQVVAGEHNQDIVEGNEQTIILSKIIQHEGYNAFTVSNDISVLQLSQPLTFNDYVQPIALPEAGHTASGDCIVSGWGTTSEGGNTPSVLMKVAVPIVTDEECRDAYGAGEIEDSMICAGLPEGGKDSCQGDSGGPFACSDTGSPYLAGVVSWGYGCARPNYPGVYTEVSYFVDWIMTNTA","length":272,"molWeight":28917,"crc64":"134661BD6CFB11B6","md5":"60D908DFAC20C0DFE0D2434466402716"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Active site":3,"Disulfide bond":4},"uniParcId":"UPI00087A327A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1D8QLQ6","uniProtkbId":"A0A1D8QLQ6_EUPSU","entryAudit":{"firstPublicDate":"2017-01-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-01-18","entryVersion":18,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41608.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41608.1"}],"value":"Trypsin"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41608.1"}],"value":"3.4.21.4"}]}]},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.","ecNumber":"3.4.21.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10078"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5009111357"},{"type":"Domain","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"CUB","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS01180"}]},{"type":"Domain","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"Peptidase S1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50240"}]},{"type":"Active site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Active site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]},{"type":"Disulfide bond","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00274"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1EKITGHMU5KBC","citationType":"submission","authors":["Zhou T.","Wang X."],"title":"Analysis on Gene and Cold-Adaptation of Trypsin from the Krill, Euphausia superba (Dana, 1852).","publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AOW41608.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT826549","properties":[{"key":"ProteinId","value":"AOW41608.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1D8QLQ6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A1D8QLQ6","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00041","properties":[{"key":"EntryName","value":"CUB"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00190","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.10:FF:000006","properties":[{"key":"EntryName","value":"Serine proteinase stubble"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.290","properties":[{"key":"EntryName","value":"Spermadhesin, CUB domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000859","properties":[{"key":"EntryName","value":"CUB_dom"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR001314","properties":[{"key":"EntryName","value":"Peptidase_S1A"}]},{"database":"InterPro","id":"IPR035914","properties":[{"key":"EntryName","value":"Sperma_CUB_dom_sf"}]},{"database":"InterPro","id":"IPR001254","properties":[{"key":"EntryName","value":"Trypsin_dom"}]},{"database":"InterPro","id":"IPR018114","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"}]},{"database":"InterPro","id":"IPR033116","properties":[{"key":"EntryName","value":"TRYPSIN_SER"}]},{"database":"PANTHER","id":"PTHR24252","properties":[{"key":"EntryName","value":"ACROSIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24252:SF7","properties":[{"key":"EntryName","value":"HYALIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00431","properties":[{"key":"EntryName","value":"CUB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00089","properties":[{"key":"EntryName","value":"Trypsin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00722","properties":[{"key":"EntryName","value":"CHYMOTRYPSIN"}]},{"database":"SMART","id":"SM00042","properties":[{"key":"EntryName","value":"CUB"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00020","properties":[{"key":"EntryName","value":"Tryp_SPc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49854","properties":[{"key":"EntryName","value":"Spermadhesin, CUB domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01180","properties":[{"key":"EntryName","value":"CUB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50240","properties":[{"key":"EntryName","value":"TRYPSIN_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00134","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRALLQQLLGLVLVLVAANAQVSEEYFTLKDGTHVQPRAGNWSIEPRASGTYACSRRPRLVTLRAGDVATFTSPGYPSPYTAKQNCGWRFKAPGRTDQITITCSSFALQPSGRRCQDFLAIGSRSLRQKYCGSNGPSSVSVIRYVRLTFRSDRSRNFAGFTCTATLAGTNPVVTSAPVTNPPVTSGRCVCGQANRATRIVGGQTTEVNEYPWQVALVSRGSTQVFCGGSLINDRWVLTAAHCTQSGVQQVILGNHLQSSTDTGERRVNVRRVVDHPNYNSRNLDNDFSLLELSTPQNLENVDPQIRPVCLPSASNPSQYEDVMAIVSGWGTTSAGGSQPNALRDTAVRTQTNAQCNQAYGSGSITNSMICAATSGRDSCQGDSGGPLVRNVGGYFRQIGVVSWGSGCADARFPGVYSRVTNQINWITSTSSSGTTCAPPS","length":440,"molWeight":47143,"crc64":"726FE9200E331BBF","md5":"CCE6A6B744438A63FE2998AB75A31C6C"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":2,"Active site":3,"Disulfide bond":3},"uniParcId":"UPI0008796589"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1I9KRC9","uniProtkbId":"A0A1I9KRC9_EUPSU","entryAudit":{"firstPublicDate":"2017-02-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-02-15","entryVersion":23,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMK05617.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000077"}],"value":"Thioredoxin"}}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000077"}],"value":"Belongs to the thioredoxin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Thioredoxin","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51352"}]},{"type":"Active site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-1"}]},{"type":"Active site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-1"}]},{"type":"Site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-1"}]},{"type":"Site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-1"}]},{"type":"Site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-1"}]},{"type":"Disulfide bond","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-4"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00691"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-4"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000077-4"}],"id":"KW-0676","category":"Domain","name":"Redox-active center"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-91FFN088KN818","citationType":"submission","authors":["Murphy D."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMK05617.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR006965","properties":[{"key":"ProteinId","value":"AMK05617.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A1I9KRC9","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0015035","properties":[{"key":"GoTerm","value":"F:protein-disulfide reductase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0045454","properties":[{"key":"GoTerm","value":"P:cell redox homeostasis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02947","properties":[{"key":"EntryName","value":"TRX_family"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.30.10:FF:000245","properties":[{"key":"EntryName","value":"Thioredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.30.10","properties":[{"key":"EntryName","value":"Glutaredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005746","properties":[{"key":"EntryName","value":"Thioredoxin"}]},{"database":"InterPro","id":"IPR036249","properties":[{"key":"EntryName","value":"Thioredoxin-like_sf"}]},{"database":"InterPro","id":"IPR017937","properties":[{"key":"EntryName","value":"Thioredoxin_CS"}]},{"database":"InterPro","id":"IPR013766","properties":[{"key":"EntryName","value":"Thioredoxin_domain"}]},{"database":"PANTHER","id":"PTHR46115","properties":[{"key":"EntryName","value":"THIOREDOXIN-LIKE PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00085","properties":[{"key":"EntryName","value":"Thioredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000077","properties":[{"key":"EntryName","value":"Thioredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00421","properties":[{"key":"EntryName","value":"THIOREDOXIN"}]},{"database":"SUPFAM","id":"SSF52833","properties":[{"key":"EntryName","value":"Thioredoxin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00194","properties":[{"key":"EntryName","value":"THIOREDOXIN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51352","properties":[{"key":"EntryName","value":"THIOREDOXIN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQYDDFAEQMKAAGGKLVVVDLFAVWCGPCKQIAPKLEAMDSEMADVVFLKVDVDECEELAMEHQISCMPTFMFFKGGEKVATFSGANEAKIKETIEANK","length":100,"molWeight":11076,"crc64":"B40DDA1388BBC662","md5":"FAA67236CC1356BAE31618C6F4CD3DF8"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":2,"Site":3,"Disulfide bond":1},"uniParcId":"UPI00090BC223"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A286Q179","uniProtkbId":"A0A286Q179_EUPSU","entryAudit":{"firstPublicDate":"2017-11-22","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-11-22","entryVersion":25,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANW48376.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00021159"}],"value":"Cryptochrome-1"}}},"comments":[{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004556"}],"value":"Cytoplasm, perinuclear region","id":"SL-0198"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005862"}],"value":"Belongs to the DNA photolyase class-1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Photolyase/cryptochrome alpha/beta","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51645"}]},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":397,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Electron transfer via tryptophanyl radical","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-2"}]},{"type":"Site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Electron transfer via tryptophanyl radical","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-2"}]},{"type":"Site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Electron transfer via tryptophanyl radical","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-2"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023108"}],"id":"KW-0090","category":"Biological process","name":"Biological rhythms"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022991"}],"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602081-1"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022543"}],"id":"KW-0600","category":"Molecular function","name":"Photoreceptor protein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023170"}],"id":"KW-0675","category":"Molecular function","name":"Receptor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022491"}],"id":"KW-0678","category":"Molecular function","name":"Repressor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022543"}],"id":"KW-0716","category":"Biological process","name":"Sensory transduction"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-768B1MB45T8EU","citationType":"journal article","authors":["Hunt B.J.","Ozkaya O.","Davies N.J.","Gaten E.","Seear P.","Kyriacou C.P.","Tarling G.","Rosato E."],"title":"The Euphausia superba transcriptome database, SuperbaSE: an online, open resource for researchers.","publicationDate":"2017","journal":"Ecol. Evol.","firstPage":"6060","lastPage":"6077","volume":"7"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANW48376.1"}]},{"referenceNumber":2,"citation":{"id":"29255161","citationType":"journal article","authors":["Biscontin A.","Wallach T.","Sales G.","Grudziecki A.","Janke L.","Sartori E.","Bertolucci C.","Mazzotta G.","De Pitta C.","Meyer B.","Kramer A.","Costa R."],"citationCrossReferences":[{"database":"PubMed","id":"29255161"},{"database":"DOI","id":"10.1038/s41598-017-18009-2"}],"title":"Functional characterization of the circadian clock in the Antarctic krill, Euphausia superba.","publicationDate":"2017","journal":"Sci. Rep.","firstPage":"17742","lastPage":"17742","volume":"7"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AUI80370.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KX238951","properties":[{"key":"ProteinId","value":"ANW48376.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"KY922999","properties":[{"key":"ProteinId","value":"AUI80370.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A286Q179","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0048471","properties":[{"key":"GoTerm","value":"C:perinuclear region of cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0071949","properties":[{"key":"GoTerm","value":"F:FAD binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032922","properties":[{"key":"GoTerm","value":"P:circadian regulation of gene expression"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043153","properties":[{"key":"GoTerm","value":"P:entrainment of circadian clock by photoperiod"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045892","properties":[{"key":"GoTerm","value":"P:negative regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"1.25.40.80","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.579.10","properties":[{"key":"EntryName","value":"DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036134","properties":[{"key":"EntryName","value":"Crypto/Photolyase_FAD-like_sf"}]},{"database":"InterPro","id":"IPR036155","properties":[{"key":"EntryName","value":"Crypto/Photolyase_N_sf"}]},{"database":"InterPro","id":"IPR005101","properties":[{"key":"EntryName","value":"Cryptochr/Photolyase_FAD-bd"}]},{"database":"InterPro","id":"IPR002081","properties":[{"key":"EntryName","value":"Cryptochrome/DNA_photolyase_1"}]},{"database":"InterPro","id":"IPR006050","properties":[{"key":"EntryName","value":"DNA_photolyase_N"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"PANTHER","id":"PTHR11455","properties":[{"key":"EntryName","value":"CRYPTOCHROME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11455:SF17","properties":[{"key":"EntryName","value":"CRYPTOCHROME-1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00875","properties":[{"key":"EntryName","value":"DNA_photolyase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03441","properties":[{"key":"EntryName","value":"FAD_binding_7"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00147","properties":[{"key":"EntryName","value":"DNAPHOTLYASE"}]},{"database":"SUPFAM","id":"SSF48173","properties":[{"key":"EntryName","value":"Cryptochrome/photolyase FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52425","properties":[{"key":"EntryName","value":"Cryptochrome/photolyase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51645","properties":[{"key":"EntryName","value":"PHR_CRY_ALPHA_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNTGCVVHWFRHGLRFHDNPALLHGLKLVDDNIKFLAVFIDDGHCAGLKNTGYNRARFLSESLEDLDDTLKKYKSQLYCFQGKPEEIFRILHKEIGIRRLTFEQDCEAIWNERDKVVNKMCQELNIDVVEEVAHTLWNPYDIIELNGGTPPLTYEMFLQVSSTAGKPPKPCSRPQWEIVNFQEINDQLALKLKMHPKVPTPEMFGVYREGGENMQYTGGETSALKHLKERLLVEENAFRDGYILPNQVNADILGAPMSMSAALRFGCLSVRKFYWSVQNTYEKLYAGESPPTYSLTAQLIWREFFYCMSVNNPKFDQMKDNPICIQIPWYDNKEHLKAWTDGQTGYPFIDACMRQLKREGWLHHIGRTAVSCFLTRGDLWISWEEGLKVFYKYLIDADWSVSAGNWMWVSSSAFERQLDCSTCICPVNYGRRVEPTGDYIRRFVPELSSIPLEYLFEPWLAPLRVQEQNGCIIGKDYPTRIVIHKNASKENRRMMQDISAKLEMATPHVCPSNNVETRTFLRLPDQCQHNVC","length":533,"molWeight":61762,"crc64":"46BB24438DDD4CE3","md5":"B8D4EE14AE7C4834CC81523E2172A753"},"extraAttributes":{"countByCommentType":{"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":3},"uniParcId":"UPI000BBF4E47"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A286Q180","uniProtkbId":"A0A286Q180_EUPSU","entryAudit":{"firstPublicDate":"2017-11-22","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-11-22","entryVersion":27,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Euphausia superba","commonName":"Antarctic krill","taxonId":6819,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANW48380.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Communostraca","Malacostraca","Eumalacostraca","Stomatocarida","Euphausiacea","Euphausiidae","Euphausia"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00040849"}],"value":"Period circadian protein"}}},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]}],"features":[{"type":"Domain","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"PAS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50112"}]},{"type":"Domain","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"PAS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50112"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":576,"modifier":"EXACT"},"end":{"value":599,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":616,"modifier":"EXACT"},"end":{"value":692,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":967,"modifier":"EXACT"},"end":{"value":1005,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1021,"modifier":"EXACT"},"end":{"value":1060,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1101,"modifier":"EXACT"},"end":{"value":1126,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1182,"modifier":"EXACT"},"end":{"value":1261,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":578,"modifier":"EXACT"},"end":{"value":599,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":616,"modifier":"EXACT"},"end":{"value":656,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":657,"modifier":"EXACT"},"end":{"value":669,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":690,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1029,"modifier":"EXACT"},"end":{"value":1050,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1182,"modifier":"EXACT"},"end":{"value":1191,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1192,"modifier":"EXACT"},"end":{"value":1206,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023108"}],"id":"KW-0090","category":"Biological process","name":"Biological rhythms"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-768B1MB45T8EU","citationType":"journal article","authors":["Hunt B.J.","Ozkaya O.","Davies N.J.","Gaten E.","Seear P.","Kyriacou C.P.","Tarling G.","Rosato E."],"title":"The Euphausia superba transcriptome database, SuperbaSE: an online, open resource for researchers.","publicationDate":"2017","journal":"Ecol. Evol.","firstPage":"6060","lastPage":"6077","volume":"7"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANW48380.1"}]},{"referenceNumber":2,"citation":{"id":"29255161","citationType":"journal article","authors":["Biscontin A.","Wallach T.","Sales G.","Grudziecki A.","Janke L.","Sartori E.","Bertolucci C.","Mazzotta G.","De Pitta C.","Meyer B.","Kramer A.","Costa R."],"citationCrossReferences":[{"database":"PubMed","id":"29255161"},{"database":"DOI","id":"10.1038/s41598-017-18009-2"}],"title":"Functional characterization of the circadian clock in the Antarctic krill, Euphausia superba.","publicationDate":"2017","journal":"Sci. Rep.","firstPage":"17742","lastPage":"17742","volume":"7"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AUI80368.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KX238955","properties":[{"key":"ProteinId","value":"ANW48380.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"KY922997","properties":[{"key":"ProteinId","value":"AUI80368.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A286Q180","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A286Q180","properties":[{"key":"Description","value":"-"}]},{"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:0000976","properties":[{"key":"GoTerm","value":"F:transcription cis-regulatory region binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0001222","properties":[{"key":"GoTerm","value":"F:transcription corepressor binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032922","properties":[{"key":"GoTerm","value":"P:circadian regulation of gene expression"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043153","properties":[{"key":"GoTerm","value":"P:entrainment of circadian clock by photoperiod"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000122","properties":[{"key":"GoTerm","value":"P:negative regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00130","properties":[{"key":"EntryName","value":"PAS"},{"key":"MatchStatus","value":"2"}]},{"database":"FunFam","id":"3.30.450.20:FF:000066","properties":[{"key":"EntryName","value":"Period circadian protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.450.20","properties":[{"key":"EntryName","value":"PAS domain"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR000014","properties":[{"key":"EntryName","value":"PAS"}]},{"database":"InterPro","id":"IPR035965","properties":[{"key":"EntryName","value":"PAS-like_dom_sf"}]},{"database":"InterPro","id":"IPR022728","properties":[{"key":"EntryName","value":"Period_circadian-like_C"}]},{"database":"InterPro","id":"IPR050760","properties":[{"key":"EntryName","value":"Period_circadian_regulator"}]},{"database":"PANTHER","id":"PTHR11269","properties":[{"key":"EntryName","value":"PERIOD CIRCADIAN PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11269:SF16","properties":[{"key":"EntryName","value":"PERIOD CIRCADIAN PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14598","properties":[{"key":"EntryName","value":"PAS_11"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12114","properties":[{"key":"EntryName","value":"Period_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00091","properties":[{"key":"EntryName","value":"PAS"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55785","properties":[{"key":"EntryName","value":"PYP-like sensor domain (PAS domain)"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50112","properties":[{"key":"EntryName","value":"PAS"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTENERSTLVPTISVEESEQVPVEGHNVKSSRNPEPAPSQMDSAYGSLGSSSLSRSRGESCSGSKSRHSGSSQSSILGDHHAEFRGHAQIIKIKELKKPPVEKKITICEVKEEVKEKIIVEEPVFNVEFAPPKEKIEPEVNRTVITKPEENPNSNSQSQDVYQGISDQPTLVYTQALNYIRKIKERSAEQGLPFASPNLIQLPRDKQHGATLFKSLKSVRGFTVAISIQDGTALQVSPSITDVLGFPKDMMLGQSFIDFVYPKDSINFSSKIIHGLNMPFINESIKDSFGTSLFCRMRMYHSLRNSGFGVRNKRTMYKPCKMILKFHDVSNIETDNPNYGQNSSMILAEVIPIDSVYKYPGEVPAMGCFSIRHSASCNFSDYDTEAIPYLGHLPQDLTGNSVFDCYHPEDLPLLKTIYEDIVMQQGRPHRSKPYRFRTFNGSYVTLETEWLCFVNPWTMKIDSVIGQHRVIKGPEDIQIFLDPGERSYTKFSEEVLKEAQKAQNYIVELLAKPVASYKDPSKEPAEKRRRTLARMMTSIVDELDHMEKKKSNIIQMPSTSKTMVVPAKIQRIVPKLPSTISKGQESLNSSSGTPSSYGQLNYSETIHRFFRSIPKTISSDESGDSKNSPQGSLDDTKSSTQPEFSTSGASGSGNMKSQQSQQFSSCSGSGDTSDNNRNKNPNSVTSNSPGSYRHVQLTEEIMNRHNVDQQHKFVQKQRTHKHSKDRFKIKNIKKATKRPMERTHGLKRPGTIMDRECSAPKQIYMASSADDSGNGKCIKTGSSGVKSRDRPTSVHSINVFNSGGANRGAAIPSSSGLAPNFQHGMMGHGMSGYYQIAAMPNFNLNGPSIENVPVASPNAVFMQPQQQQFLQPQSLMPGMAMQYMGPGMGAFPGIVYQTVGPPYFNAPQLMLPNLMYQHTAMPQPQPVAQHIAAHMDSEEEKTILRTDSEHEIIDSQHITGNRIIISGKPINAHQRPDSRATSVKAEPGSVRGSMARESSHSHAAESIRSYVEDVTHCFAPKESEKHPHSSQLSEFSQSSSVQAEAESVGSPGKIDNKPNDELHASDIIMSVTSSTHESSKDLYYKSTDDSFLLNSESSEMSEGKFNNKWNTSKPKYQPPKLGGPSWLENVDVTPELLYKYQLETKELVDVLRQDMDALKKFRQPVCVDDQLSFLYNEMEREGESTKLHLEEGITSSSSGEEGPCSSKDGAASTSRGRVKKSVYFSTAAMLQEEDAPMPPPESRESSYYLMCEEPGRDSSDS","length":1261,"molWeight":140105,"crc64":"9B58508C497A00D8","md5":"A9EDAB4640C63675D07BB5C26F32024B"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Domain":2,"Region":7,"Compositional bias":8},"uniParcId":"UPI000BC012B8"}}]}