ID   A0A1D8GYF6_9SACH        Unreviewed;       534 AA.
AC   A0A1D8GYF6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   15-FEB-2017, entry version 2.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369};
GN   Name=cox1 {ECO:0000313|EMBL:AOT85112.1};
OS   Saccharomyces arboricola.
OG   Mitochondrion {ECO:0000313|EMBL:AOT85112.1}.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=706196 {ECO:0000313|EMBL:AOT85112.1};
RN   [1] {ECO:0000313|EMBL:AOT85112.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 10644 {ECO:0000313|EMBL:AOT85112.1}, and NRRL Y-63701
RC   {ECO:0000313|EMBL:AOT85126.1};
RA   Sulo P., Szaboova D., Szemes T.;
RT   "Divergence of Saccharomyces species is accompanied with the
RT   alterations in mitochondrial gene order.";
RL   Submitted (AUG-2016) 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. {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       ECO:0000256|SAAS:SAAS00672464}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00672508}.
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; KX657740; AOT85112.1; -; Genomic_DNA.
DR   EMBL; KX657741; AOT85126.1; -; Genomic_DNA.
DR   RefSeq; YP_009310804.1; NC_031511.1.
DR   GeneID; 29991780; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 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, ECO:0000256|SAAS:SAAS00675112};
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:0000256|SAAS:SAAS00672487, ECO:0000313|EMBL:AOT85112.1};
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     14     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     56     80       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    127       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    147    172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    184    212       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    244    262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    274    291       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    303    326       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    338    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    379    397       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    409    430       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    450    473       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    534       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   534 AA;  58819 MW;  20F84927232E6DC6 CRC64;
     MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLQG NSQLFNVLVV
     GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE
     SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH
     KLPLFVWSIF ITAFLLLLSL PVLSAGITML LLDRNFNTSF FEVAGGGDPI LYEHLFWFFG
     HPEVYILIIP GFGIISHVVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD
     TRAYFTSATM IIAIPTGIKI FSWLATVYGG SIRLATPMLY AIAFLFLFTM GGLTGVALAN
     ASLDVAFHDT YYVVGHFHYV LSMGAIFSLF AGYYYWSPQI LGLNYNEKLA QIQFWLIFIG
     ANVIFFPMHF LGINGMPRRI PDYPDAFAGW NYVASIGSFI ATLSLFLFIY ILYDQLVNGL
     NNKVTNKSVI YSKTPDFIES NMIFNLNTVK SSSIEFLLTS PPAVHSFNTP AVQS
//