(data stored in ACNUC7421 zone)

SWISSPROT: COX2_ASHGO

ID   COX2_ASHGO              Reviewed;         248 AA.
AC   Q7YFV7; Q75G36;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
DE   Flags: Precursor;
GN   Name=COX2; Synonyms=CoxII; OrderedLocusNames=AMI001W; ORFNames=AgCOX2;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-233.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=12748053; DOI=10.1016/s1567-1356(03)00012-6;
RA   Kurtzman C.P., Robnett C.J.;
RT   "Phylogenetic relationships among yeasts of the 'Saccharomyces complex'
RT   determined from multigene sequence analyses.";
RL   FEMS Yeast Res. 3:417-432(2003).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex. Subunit 2 transfers the
CC       electrons from cytochrome c via its binuclear copper A center to the
CC       bimetallic center of the catalytic subunit 1.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC         + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC         COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds a copper A center.;
CC   -!- SUBUNIT: Composed of at least 11 subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- PTM: The signal sequence of COX2 is processed by IMP1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
DR   EMBL; AE016821; AAS50168.1; -; Genomic_DNA.
DR   EMBL; AF442273; AAP57840.1; -; Genomic_DNA.
DR   RefSeq; NP_987078.1; NC_005789.1.
DR   STRING; 33169.AAS50168; -.
DR   EnsemblFungi; AAS50168; AAS50168; AGOS_AMI001W.
DR   GeneID; 2760769; -.
DR   KEGG; ago:AGOS_AMI001W; -.
DR   HOGENOM; HOG000264988; -.
DR   InParanoid; Q7YFV7; -.
DR   KO; K02261; -.
DR   OMA; WSYEYTD; -.
DR   Proteomes; UP000000591; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:EnsemblFungi.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:EnsemblFungi.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR034210; CcO_II_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   TIGRFAMs; TIGR02866; CoxB; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7YFV7.
DR   SWISS-2DPAGE; Q7YFV7.
KW   Copper; Electron transport; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Respiratory chain; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..12
FT                   /evidence="ECO:0000250"
FT   CHAIN           13..248
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000006037"
FT   TOPO_DOM        13..39
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..79
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..248
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   METAL           183
FT                   /note="Copper A"
FT                   /evidence="ECO:0000250"
FT   METAL           218
FT                   /note="Copper A"
FT                   /evidence="ECO:0000250"
FT   METAL           222
FT                   /note="Copper A"
FT                   /evidence="ECO:0000250"
FT   METAL           226
FT                   /note="Copper A"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   248 AA;  28676 MW;  5DC760E717804240 CRC64;
     MLLMNLFTII NNDVPTPYNM YFQDSTTPHQ EGILELHDNI MFYMLTVLGL VSWMMIIIIK
     DYKNNPITYK YIKHGQMIEI IWTILPAIIL LMIAFPSFIL LYLCDEVISP AMTIKVIGLQ
     WYWKYEYSDF INDNGETIEY ESYMIPEELL EEGQLRMLDT DTSIVIPVDT HVRFIVTATD
     VIHDFAVPSL GIKIDTTPGR LSQVSTLIQR EGIFYGQCSE LCGAQHSAMP IKIETVKLPT
     FLTWLNEQ
//

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