ID   Q6SZW2_9HYME            Unreviewed;       440 AA.
AC   Q6SZW2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 2.
DT   19-JAN-2010, entry version 35.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   Flags: Fragment;
GN   Name=COI;
OS   Crematogaster sp. K SPQ-2003.
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Formicidae; Myrmicinae; Crematogaster; Decacrema.
OX   NCBI_TaxID=254728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SPQ.Z;
RX   PubMed=15119439;
RA   Quek S.P., Davies S.J., Itino T., Pierce N.E.;
RT   "Codiversification in an ant-plant mutualism: stem texture and the
RT   evolution of host use in Crematogaster (Formicidae: Myrmicinae)
RT   inhabitants of Macaranga (Euphorbiaceae).";
RL   Evolution 58:554-570(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SPQ.Z;
RA   Quek S.-P., Davies S.J., Itino T., Pierce N.E.;
RL   Submitted (JAN-2007) 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
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DR   EMBL; AY444008; AAR17000.2; -; Genomic_DNA.
DR   SMR; Q6SZW2; 2-435.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000883; Cyt_c_oxidase_su1.
DR   PANTHER; PTHR10422; COX1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Respiratory chain; Transmembrane; Transport.
FT   NON_TER       1      1
SQ   SEQUENCE   440 AA;  49146 MW;  B1F198BB93355FB2 CRC64;
     FMIGGFGNFL IPLMLGSPDM AYPRMNNMSF WLLPPSILLL LLSSFLSSGV GTGWTIYPPL
     ASNMFHSGPS IDLTIFSLHI AGMSSILGAI NFIATILNMH HSSISLDKIS LLSWSILITA
     ILLLLSLPVL AGAITMLLTD RNLNTSFFDP SGGGDPILYQ HLFWFFGHPE VYILILPGFG
     LISHIIMSES GKKETFGSLG MIYAMIAIGF LGFIVWAHHM FTIGLDVDTR AYFTSATMII
     AIPTGIKIFS WISTLHGMKI TYNPTLWWAM GFIFLFTMGG LTGIMLSNSS IDIILHDTYY
     VVAHFHYVLS MGAVFAIIAS FIHWFPLISG FTLNKFYLNI QFISMFIGVN LTFFPQHFLG
     LSGMPRRYSD YPDNFLSWNI ISSIGSLISI LSLSILIYSI WEALSSKRKI INMFFMAPSL
     EWLSSYPPQN HCFNEIPSIF
//