ID Q8HBS8_9SAUR Unreviewed; 170 AA. AC Q8HBS8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 12-SEP-2018, entry version 71. 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:AAM81041.1}; OS Elaphe taeniura (beauty snake). OG Mitochondrion {ECO:0000313|EMBL:AAM81041.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Colubridae; Colubrinae; Elaphe. OX NCBI_TaxID=74398 {ECO:0000313|EMBL:AAM81041.1}; RN [1] {ECO:0000313|EMBL:AAM81041.1} RP NUCLEOTIDE SEQUENCE. RA Utiger U., Helfenberger N., Schaetti B., Schmidt C., Ruf M., RA Ziswiler V.; RT "Molecular systematics and phylogeny of Old and New World ratsnakes, RT Elaphe auct., and related genera (Reptilia, Squamata, Colubridae)."; RL Russ. J. Herpetol. 9:105-124(2002). 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; AY122723; AAM81041.1; -; Genomic_DNA. DR EMBL; AY122724; AAM81042.1; -; Genomic_DNA. DR EMBL; AY122725; AAM81043.1; -; Genomic_DNA. DR ProteinModelPortal; Q8HBS8; -. DR HOVERGEN; HBG003841; -. 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: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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 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:AAM81041.1}; 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 24 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 89 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 168 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 170 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AAM81041.1}. FT NON_TER 170 170 {ECO:0000313|EMBL:AAM81041.1}. SQ SEQUENCE 170 AA; 18510 MW; 6FA06BFE78C547B4 CRC64; AGTGWTVYPP LSGNLVHSGP SVDLAIFSLH LAGASSILGA INFITTCINM KPKSMPMFNI PLFVWSVLIT AIMLLLALPV LAAAITMLLT DRNLNTSFFD PCGGGDPVLF QHLFWFFGHP EVYILILPGF GIVSSIITFY TGKKNTFGYT SMIWAMMSIA ILGFVVWAHH //