ID   F1CWZ5_9NEOP            Unreviewed;       211 AA.
AC   F1CWZ5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   18-JAN-2017, entry version 32.
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:ADT70893.1};
OS   Biston stratarius.
OG   Mitochondrion {ECO:0000313|EMBL:ADT70893.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia;
OC   Geometroidea; Geometridae; Ennominae; Biston.
OX   NCBI_TaxID=722658 {ECO:0000313|EMBL:ADT70893.1};
RN   [1] {ECO:0000313|EMBL:ADT70893.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21423340; DOI=10.1371/journal.pone.0017134;
RA   Hausmann A., Haszprunar G., Hebert P.D.;
RT   "DNA barcoding the geometrid fauna of Bavaria (Lepidoptera):
RT   successes, surprises, and questions.";
RL   PLoS ONE 6:E17134-E17134(2011).
RN   [2] {ECO:0000313|EMBL:ADT70893.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hausmann A., Haszprunar G., Segerer A.H., Speidel W., Behounek G.,
RA   Hebert P.D.N.;
RT   "Now DNA-barcoded: the butterflies and larger moths of Germany.";
RL   Spixiana 34:47-58(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; HQ601074; ADT70893.1; -; 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; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
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:ADT70893.1};
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     38     59       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     80    102       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    122    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    159    186       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    211       COX1. {ECO:0000259|PROSITE:PS50855}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ADT70893.1}.
FT   NON_TER     211    211       {ECO:0000313|EMBL:ADT70893.1}.
SQ   SEQUENCE   211 AA;  22648 MW;  A894506FE2F35ED7 CRC64;
     WAGMVGTSLS LLIRAELGNP GSLIGDDQIY NTIVTAHAFI MIFFMVMPIM IGGFGNWLVP
     LMLGAPDMAF PRMNNMSFWL LPPSITLLIS SSIVESGAGT GWTVYPPLSS NIAHGGSSVD
     LAIFSLHLAG ISSILGAINF ITTIINMRLN KLSFDQMPLF VWAVGITAFL LLLSLPVLAG
     AITMLLTDRN LNTSFFDPAG GGDPILYQHL F
//