ID   E2GE66_EPIPO            Unreviewed;       499 AA.
AC   E2GE66;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   01-OCT-2014, entry version 21.
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 {ECO:0000313|EMBL:ADN64858.1};
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; Endopterygota; 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}.
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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: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; IPR023615; Cyt_c_Oxase_su1_BS.
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.
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   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   Transport {ECO:0000256|RuleBase:RU000369}.
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
//