ID A0A386R1I4_RAJCL Unreviewed; 197 AA. AC A0A386R1I4; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 11-DEC-2019, entry version 4. 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=COI {ECO:0000313|EMBL:AYE56185.1}; OS Raja clavata (Thornback ray). OG Mitochondrion {ECO:0000313|EMBL:AYE56185.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Batoidea; Rajiformes; Rajidae; Raja. OX NCBI_TaxID=7781 {ECO:0000313|EMBL:AYE56185.1}; RN [1] {ECO:0000313|EMBL:AYE56185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G201 {ECO:0000313|EMBL:AYE56184.1}, G202 RC {ECO:0000313|EMBL:AYE56185.1}, G521 {ECO:0000313|EMBL:AYE56178.1}, RC G522 {ECO:0000313|EMBL:AYE56181.1}, G523 RC {ECO:0000313|EMBL:AYE56183.1}, G615 {ECO:0000313|EMBL:AYE56179.1}, RC G616 {ECO:0000313|EMBL:AYE56180.1}, and G617 RC {ECO:0000313|EMBL:AYE56182.1}; RA Ramirez-Amaro S., Ordines F., Picornell A., Castro J.A., Ramon C., RA Massuti E., Terrasa B.; RT "The evolutionary history of Mediterranean Batoidea (Chondrichthyes: RT Neoselachii)."; RL Zool. Scr. 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 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={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; KY949088; AYE56178.1; -; Genomic_DNA. DR EMBL; KY949089; AYE56179.1; -; Genomic_DNA. DR EMBL; KY949090; AYE56180.1; -; Genomic_DNA. DR EMBL; KY949091; AYE56181.1; -; Genomic_DNA. DR EMBL; KY949092; AYE56182.1; -; Genomic_DNA. DR EMBL; KY949093; AYE56183.1; -; Genomic_DNA. DR EMBL; KY949094; AYE56184.1; -; Genomic_DNA. DR EMBL; KY949095; AYE56185.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. 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}; 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, ECO:0000313|EMBL:AYE56185.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 31..56 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 77..101 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 121..144 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 156..183 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..197 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AYE56185.1" FT NON_TER 197 FT /evidence="ECO:0000313|EMBL:AYE56185.1" SQ SEQUENCE 197 AA; 20977 MW; B969550009A0EEAF CRC64; MVGTGLSLLI RAELSQPGTL LGDDQIYNVI VTAHALVMIF FMVMPIMIGG FGNWLVPLMI GSPDMAFPRM NNMSFWLLPP SFLLLLASAG VEAGAGTGWT VYPPLAGNLA HAGASVDLTI FSLHLAGVSS ILASINFITT IINMKPPAIS QYQTPLFVWS ILVTTVLLLM ALPVLAAGIT MLLTDRNLNT TFFDPAG //