ID A0A0K1GVV3_9ACAR Unreviewed; 182 AA. AC A0A0K1GVV3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 06-JUL-2016, entry version 7. 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:AKT70983.1}; OS Parasitidae sp. BOLD:AAF9285. OG Mitochondrion {ECO:0000313|EMBL:AKT70983.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Parasitiformes; Mesostigmata; Gamasina; Parasitidae. OX NCBI_TaxID=1474019 {ECO:0000313|EMBL:AKT70983.1}; RN [1] {ECO:0000313|EMBL:AKT70983.1} RP NUCLEOTIDE SEQUENCE. RA Strauss C., Perreten V.; RT "New MLSB resistance gene variant erm(44)v in Staphylococcus RT saprophyticus."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKT70983.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26175299; RA Blagoev G.A., deWaard J.R., Ratnasingham S., deWaard S.L., Lu L., RA Robertson J., Telfer A.C., Hebert P.D.; RT "Untangling taxonomy: a DNA barcode reference library for Canadian RT spiders."; RL Mol. Ecol. Resour. 0:0-0(2015). 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; KM839984; AKT70983.1; -; 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:respiratory chain; 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:0005506; F:iron ion binding; IEA:InterPro. 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; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. 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:AKT70983.1}; 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 130 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 181 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 182 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AKT70983.1}. FT NON_TER 182 182 {ECO:0000313|EMBL:AKT70983.1}. SQ SEQUENCE 182 AA; 19721 MW; 03520A18273917AE CRC64; TMYLIFAAWA GMLGTALSMI IRAELGQPGS LIGDDQIYNV VVTAHAFIMI FFMVMPALIG GFGNWLVPLM VSAPDMAFPR MNNMSFWLLP PSLLLLLSSS MVESGAGTGW TVYPPLAGNL SHSGGAVDLA IFSLHLAGIS SILGSINFIT TIMNMRPKEM SMERMPLFVW SVFITTILLL LS //