ID E2GE66_EPIPO Unreviewed; 499 AA. AC E2GE66; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 23-MAY-2018, entry version 34. 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:ADN64858.1}; OS Epiphyas postvittana (Light brown apple moth). OG Mitochondrion {ECO:0000313|EMBL:ADN64858.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Tortricoidea; Tortricidae; Tortricinae; Epiphyas. OX NCBI_TaxID=65032 {ECO:0000313|EMBL:ADN64858.1}; RN [1] {ECO:0000313|EMBL:ADN64858.1} RP NUCLEOTIDE SEQUENCE. RA Tooman L., Rose C.J., Carraher C., Ledezma L.A., Barr N.B.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADN64858.1} RP NUCLEOTIDE SEQUENCE. RA Tooman L.K., Rose C.J., Carraher C., Suckling D.M., Rioux Paquette S., RA Ledezma L.A., Gilligan T.M., Epstein M., Barr N.B., Newcomb R.D.; RT "Patterns of Mitochondrial Haplotype Diversity in the Invasive Pest RT Epiphyas postvittana (Lepidoptera: Tortricidae)."; RL J. Econ. Entomol. 104:920-932(2011). 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; HM346386; ADN64858.1; -; 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:0045277; C:respiratory chain complex IV; IEA:InterPro. 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 CDD; cd01663; Cyt_c_Oxidase_I; 1. 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 InterPro; IPR033944; 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. 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, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:ADN64858.1}; 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|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 5 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 111 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 195 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 276 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 288 312 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 324 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 385 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 397 415 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 435 458 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 497 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:ADN64858.1}. SQ SEQUENCE 499 AA; 55221 MW; B7399333725C80AC CRC64; GTLYFIFGIW AGMVGTSLSL LIRAELGNPG SLIGDDQIYN TIVTAHAFIM IFFMVMPIMI GGFGNWLVPL MLGAPDMAFP RMNNMSFWLL PPSIMLLISS SIVENGAGTG WTVYPPLSSN IAHSGSSVDL AIFSLHLAGI SSILGAVNFI TTIINMRPNN MSLDQMPLFV WSVGITALLL LLSLPVLAGA ITMLLTDRNL NTSFFDPAGG GDPILYQHLF WFFGHPEVYI LILPGFGMIS HIISQESGKK ETFGCLGMIY AMMAIGLLGF VVWAHHMFTV GMDIDTRAYF TSATMIIAVP TGIKIFSWLA TLHGTQINYS PSMLWSLGFV FLFTVGGLTG VILANSSIDV TLHDTYYVVA HFHYVLSMGA VFAIMGGFIH WYPLFTGLAM NPYLLKIQFF TMFIGVNLTF FPQHFLGLAG MPRRYSDYPD TYTSWNIISS LGSYISLIAT MLMLIIIWEP LINKRIILFP LNMNSSIEWY QNLPPAEHSY SELPILSNF //