ID M7SVM9_EUTLA Unreviewed; 162 AA.
AC M7SVM9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=UCREL1_4633 {ECO:0000313|EMBL:EMR68352.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR68352.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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; KB706254; EMR68352.1; -; Genomic_DNA.
DR RefSeq; XP_007792549.1; XM_007794358.1.
DR AlphaFoldDB; M7SVM9; -.
DR STRING; 1287681.M7SVM9; -.
DR KEGG; ela:UCREL1_4633; -.
DR eggNOG; KOG4077; Eukaryota.
DR HOGENOM; CLU_099086_0_0_1; -.
DR OMA; ENKNQYQ; -.
DR OrthoDB; 2876967at2759; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000012174; 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 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:UP000012174};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU368103}.
SQ SEQUENCE 162 AA; 18083 MW; 4C4000566AB52030 CRC64;
MSSTSLLRIA ARAGPSKSFF RANRPVAPAR ASASFVPGLV AGSSLNFSTS VSRPSEHHEE
TFEEFSARYE KEFDGVQDVF ELQRNLNNAF AYDLVPSPTV LQAALKAARR VNDYPTAVRI
FEGIKAKVEN KGQYEEYVQE LKPLKEELGI LLKEELFPEE AK
//
