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Database: UniProt
Entry: A0A093PII5_9PASS
LinkDB: A0A093PII5_9PASS
Original site: A0A093PII5_9PASS 
ID   A0A093PII5_9PASS        Unreviewed;       117 AA.
AC   A0A093PII5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial {ECO:0000256|ARBA:ARBA00021968, ECO:0000256|RuleBase:RU368103};
DE   AltName: Full=Cytochrome c oxidase polypeptide Va {ECO:0000256|ARBA:ARBA00031049, ECO:0000256|RuleBase:RU368103};
DE   Flags: Fragment;
GN   ORFNames=N305_10623 {ECO:0000313|EMBL:KFW76216.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW76216.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW76216.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW76216.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC       complex, complex III, CIII). {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; KL669396; KFW76216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093PII5; -.
DR   STRING; 328815.ENSMVIP00005019519; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000053258; 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:UP000053258};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU368103}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW76216.1"
FT   NON_TER         117
FT                   /evidence="ECO:0000313|EMBL:KFW76216.1"
SQ   SEQUENCE   117 AA;  13284 MW;  4D4E8198F12B20E6 CRC64;
     AVLHARCYSH GSQESDEEFD ARWVTYFNKP DIDAWELRKG INTLVGYDLV PEPKIIDAAL
     RACRRLNDFA STVRILEVVK DKAGPHKEIY PYVIQELRPT LSELGISTPE ELGLDKA
//
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