GenomeNet

Database: UniProt
Entry: A0A1Y2IJQ9_PYCCO
LinkDB: A0A1Y2IJQ9_PYCCO
Original site: A0A1Y2IJQ9_PYCCO 
ID   A0A1Y2IJQ9_PYCCO        Unreviewed;       134 AA.
AC   A0A1Y2IJQ9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Cytochrome c oxidase subunit 6, mitochondrial {ECO:0000256|RuleBase:RU368103};
DE   AltName: Full=Cytochrome c oxidase polypeptide VI {ECO:0000256|RuleBase:RU368103};
GN   ORFNames=PYCCODRAFT_1446042 {ECO:0000313|EMBL:OSD00874.1};
OS   Trametes coccinea BRFM310.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=1353009 {ECO:0000313|EMBL:OSD00874.1, ECO:0000313|Proteomes:UP000193067};
RN   [1] {ECO:0000313|EMBL:OSD00874.1, ECO:0000313|Proteomes:UP000193067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM310 {ECO:0000313|EMBL:OSD00874.1,
RC   ECO:0000313|Proteomes:UP000193067};
RX   PubMed=26692083; DOI=10.1186/s13068-015-0407-8;
RA   Couturier M., Navarro D., Chevret D., Henrissat B., Piumi F.,
RA   Ruiz-Duenas F.J., Martinez A.T., Grigoriev I.V., Riley R., Lipzen A.,
RA   Berrin J.G., Master E.R., Rosso M.N.;
RT   "Enhanced degradation of softwood versus hardwood by the white-rot fungus
RT   Pycnoporus coccineus.";
RL   Biotechnol. Biofuels 8:216-216(2015).
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:RU368103}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU368103}.
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of a catalytic core of 3 subunits and
CC       several supernumerary subunits. {ECO:0000256|RuleBase:RU368103}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443,
CC       ECO:0000256|RuleBase:RU368103}; Matrix side
CC       {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC       {ECO:0000256|ARBA:ARBA00007972, ECO:0000256|RuleBase:RU368103}.
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; KZ084115; OSD00874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2IJQ9; -.
DR   STRING; 1353009.A0A1Y2IJQ9; -.
DR   OrthoDB; 2876967at2759; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000193067; Unassembled WGS sequence.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:UniProtKB-UniRule.
DR   CDD; cd00923; Cyt_c_Oxidase_Va; 1.
DR   Gene3D; 1.25.40.40; Cytochrome c oxidase, subunit Va/VI; 1.
DR   InterPro; IPR003204; Cyt_c_oxidase_su5A/6.
DR   InterPro; IPR036545; Cyt_c_oxidase_su5A/6_sf.
DR   PANTHER; PTHR14200; CYTOCHROME C OXIDASE POLYPEPTIDE; 1.
DR   PANTHER; PTHR14200:SF11; CYTOCHROME C OXIDASE POLYPEPTIDE VA; 1.
DR   Pfam; PF02284; COX5A; 1.
DR   SUPFAM; SSF48479; Cytochrome c oxidase subunit E; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU368103};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368103};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368103};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368103};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU368103};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU368103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193067};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU368103}.
SQ   SEQUENCE   134 AA;  15197 MW;  2017255DDC29A7CC CRC64;
     MLRAQLVSSL LRARPAATRV APTFARASSS AHGQETFESF NERYVQFFQS AQDLFEVQRG
     LNNCFAHDLV PSPSVVEAAV RAARRVNDYA TAVRVFEGIK EKVENKQQYQ AYLDELKPLR
     EELGINIKEE LYTS
//
DBGET integrated database retrieval system