ID A0A098BVR8_9APIC Unreviewed; 308 AA. AC A0A098BVR8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 23-MAY-2018, entry version 13. 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:CEA10036.1}; OS Parahaemoproteus sp. CP-2014. OG Mitochondrion {ECO:0000313|EMBL:CEA10036.1}. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Haemoproteidae; Parahaemoproteus; unclassified Parahaemoproteus. OX NCBI_TaxID=1539139 {ECO:0000313|EMBL:CEA10036.1}; RN [1] {ECO:0000313|EMBL:CEA10036.1} RP NUCLEOTIDE SEQUENCE. RA Borner J., Pick C., Thiede J., Kolawole O.M., Kingsley M.T., RA Schulze J., Cottontail V., Wellinghausen N., Schmidt-Chanasit J., RA Bruchhaus I., Burmester T.; RT "Phylogeny of haemosporidian blood parasites revealed by a multi-gene RT approach."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. 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; LN483047; CEA10036.1; -; 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: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:CEA10036.1}; 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 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 200 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 220 239 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 251 271 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283 305 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 308 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:CEA10036.1}. FT NON_TER 308 308 {ECO:0000313|EMBL:CEA10036.1}. SQ SEQUENCE 308 AA; 33217 MW; EA436E58AC6BAFA8 CRC64; SELAYPRINS ISLLLQPIAF GLVILSTTAE FGGGTGWTLY PPLSTSLMSL SPVAVDVIVI GLLVSGVASI MSSLNFLTTV VHLRAKGLTL GILSVSTWSI VLTAIMLLLT LPVLTGGVLM LLSDLHFNTL FFDPTFSGDP VLYQHLFWFF GHPEVYILIL PAFGIISHVI STNYCRSLFG NQSMILAMAC IAVLGSLVWA HHMYTTGLEV DTRAYFTSTT ILISIPTGTK VFNWLCTYMS SNFGITHSSS LLALLFICTF TFGGTTGVIL GNAAIDIALH DTYYVIAHFH FVLSIGAIIA LFTAVSAF //