ID   U5LUW8_9ACAR            Unreviewed;       151 AA.
AC   U5LUW8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   12-OCT-2022, entry version 35.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=cox1 {ECO:0000313|EMBL:AGX31978.1};
OS   Euseius nicholsi.
OG   Mitochondrion {ECO:0000313|EMBL:AGX31978.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Phytoseioidea; Phytoseiidae;
OC   Amblyseiinae; Euseius.
OX   NCBI_TaxID=702746 {ECO:0000313|EMBL:AGX31978.1};
RN   [1] {ECO:0000313|EMBL:AGX31978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DXNS4 {ECO:0000313|EMBL:AGX31963.1}, and JJNS8
RC   {ECO:0000313|EMBL:AGX31978.1};
RA   Xia B., Yang D.L.;
RT   "The phylogeographic structure of Euseius nicholsi (Acari: Phytoseiidea) in
RT   China based on mitochondrial COI sequence data.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000256|ARBA:ARBA00029331};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448,
CC       ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000369}.
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DR   EMBL; KF308626; AGX31963.1; -; Genomic_DNA.
DR   EMBL; KF308641; AGX31978.1; -; 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:respirasome; 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: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}; Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AGX31978.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000369};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..151
FT                   /note="COX1"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGX31978.1"
FT   NON_TER         151
FT                   /evidence="ECO:0000313|EMBL:AGX31978.1"
SQ   SEQUENCE   151 AA;  16873 MW;  43D23C12716FC01E CRC64;
     WFFGHPEVYI LILPGFGIIS HTILSQSMKT QTFGSLGMIY AMSAIGFLGF IVWAHHMFTV
     GMDVDSRAYF TAATMIIAIP TGIKIFSWVS TIFGSYIKWN TVMLWNMGFI FLFSMGGFTG
     VILANSSVDI ILHDTYYVVA HFHYVLSMGA V
//