ID A0A2Z5WJA3_9ANNE Unreviewed; 219 AA. AC A0A2Z5WJA3; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 07-NOV-2018, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COX1 {ECO:0000313|EMBL:BBC08986.1}; OS Sternaspis sp. 4 GK-2017. OG Mitochondrion {ECO:0000313|EMBL:BBC08986.1}. OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Polychaeta; Scolecida; OC Terebellida; Sternaspidae; Sternaspis. OX NCBI_TaxID=2060733 {ECO:0000313|EMBL:BBC08986.1}; RN [1] {ECO:0000313|EMBL:BBC08986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GK49 {ECO:0000313|EMBL:BBC08986.1}; RA Kobayashi G., Mukai R., Alalykina I., Miura T., Kojima S.; RT "Phylogeography of benthic invertebrates in deep waters: A case study RT of Sternaspis cf. williamsae (Annelida: Sternaspidae) from the RT northwestern Pacific Ocean."; RL Deep Sea Res. Part II Top. Stud. Oceanogr. 0:0-0(2018). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LC341930; BBC08986.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:BBC08986.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 46 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 194 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 219 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:BBC08986.1}. FT NON_TER 219 219 {ECO:0000313|EMBL:BBC08986.1}. SQ SEQUENCE 219 AA; 23647 MW; 27B3B5F5E62F40ED CRC64; TMYFIFGIWS GLLGTSMSLL VRIELSQPGA LMGNDQIYNV LVTAHAFLMI FFLVMPVLMS GFGNWLIPTL LSAPDMAFPR LNNMSFWLLP PSLILLTMSA VVEGGVGTGW TVYPPLSNNI FHSGPSVDLA IFSLHLAGVS SILGSLNFIT TALNMRPAGM TPERTPLFVW AVAITGLLLV LSIPVLAAGI TMLLTDRNLN TSFFDPTGGG DPVLFQHLF //