ID   COXM1_YEAS7             Reviewed;         111 AA.
AC   A6ZZI5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=COX assembly mitochondrial protein;
DE   AltName: Full=COX biogenesis factor CMC1;
DE   AltName: Full=Mitochondrial metallochaperone-like protein CMC1;
GN   Name=CMC1; ORFNames=SCY_3245;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Required for mitochondrial cytochrome c oxidase (COX)
CC       assembly and respiration. Binds copper. May be involved in copper
CC       trafficking and distribution to mitochondrial COX and SOD1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CMC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN60033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000151; EDN60033.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZZI5; -.
DR   EnsemblFungi; EDN60033; EDN60033; SCY_3245.
DR   HOGENOM; CLU_147575_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR013892; Cyt_c_biogenesis_Cmc1-like.
DR   PANTHER; PTHR22977; PTHR22977; 1.
DR   Pfam; PF08583; Cmc1; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Chaperone; Copper; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane.
FT   CHAIN           1..111
FT                   /note="COX assembly mitochondrial protein"
FT                   /id="PRO_0000377672"
FT   DOMAIN          39..82
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           42..52
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           64..74
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        42..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        52..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   111 AA;  13007 MW;  8934C73F1AB75632 CRC64;
     MEQNKDPQMI SKHSSRLPIW VLSPREEQQA RKNLKTETYK KCANFVQAMA DCAKANGMKV
     FPTCDKQRDE MKSCLLFYQT DEKYLDGERD KIVLEKINKL EKLCQKQSST K