ID A0A2G7G3A5_9EURO Unreviewed; 158 AA.
AC A0A2G7G3A5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=AARAC_004332 {ECO:0000313|EMBL:PIG87065.1}, BDV24DRAFT_92144
GN {ECO:0000313|EMBL:KAE8346149.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG87065.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG87065.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG87065.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAE8346149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8346149.1};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) 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: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}.
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DR EMBL; ML737117; KAE8346149.1; -; Genomic_DNA.
DR EMBL; NEXV01000198; PIG87065.1; -; Genomic_DNA.
DR SMR; A0A2G7G3A5; -.
DR STRING; 656916.A0A2G7G3A5; -.
DR OrthoDB; 2876967at2759; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR Proteomes; UP000325558; 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 SUBUNIT 5A, MITOCHONDRIAL; 1.
DR Pfam; PF02284; COX5A; 1.
DR SUPFAM; SSF48479; Cytochrome c oxidase subunit E; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000231358};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU368103}.
FT COILED 124..151
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 158 AA; 17901 MW; 0762EC115ACD8A5C CRC64;
MSPVSVFRVA TRAVRPASLF RAPQLPRARL QTPVALAINR PAFSTSSKRL GGHHEDETYE
EFSARFEKEF DGVQDVFELQ RNLNNCFAYD LVPSVEVLSA ALRAARRVND FPTAVRVFEG
IKAKVETQDQ YKQYLEALEG LRQELGVALR EELYPGEQ
//