ID   CCS1_KLULA              Reviewed;         245 AA.
AC   Q6CIG2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone;
GN   Name=CCS1; OrderedLocusNames=KLLA0F26917g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Copper chaperone for superoxide dismutase 1 (SOD1). Binds
CC       copper ions and delivers them specifically to SOD1 (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCS1 family. {ECO:0000305}.
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DR   EMBL; CR382126; CAG98985.1; -; Genomic_DNA.
DR   RefSeq; XP_456277.1; XM_456277.1.
DR   AlphaFoldDB; Q6CIG2; -.
DR   SMR; Q6CIG2; -.
DR   STRING; 28985.XP_456277.1; -.
DR   PRIDE; Q6CIG2; -.
DR   EnsemblFungi; CAG98985; CAG98985; KLLA0_F26917g.
DR   GeneID; 2894848; -.
DR   KEGG; kla:KLLA0_F26917g; -.
DR   eggNOG; KOG4656; Eukaryota.
DR   HOGENOM; CLU_056632_0_0_1; -.
DR   InParanoid; Q6CIG2; -.
DR   OMA; KGMGSDQ; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0101031; C:chaperone complex; IEA:EnsemblFungi.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:1902693; C:superoxide dismutase complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IEA:EnsemblFungi.
DR   GO; GO:0006825; P:copper ion transport; IEA:EnsemblFungi.
DR   GO; GO:0015680; P:protein maturation by copper ion transfer; IEA:EnsemblFungi.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:EnsemblFungi.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00403; HMA; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..245
FT                   /note="Superoxide dismutase 1 copper chaperone"
FT                   /id="PRO_0000239063"
FT   DOMAIN          8..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         19
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         22
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         224
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT   BINDING         226
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT   DISULFID        29..66
FT                   /evidence="ECO:0000250|UniProtKB:P40202"
FT   DISULFID        224
FT                   /note="Interchain (with C-58 in apo-SOD1)"
FT                   /evidence="ECO:0000250|UniProtKB:P40202"
SQ   SEQUENCE   245 AA;  26630 MW;  2B75EDB7D62A453F CRC64;
     MSGTDENDFE ATYAVEMHCE SCTNDIQKCL KDVNGIKNVT FDIKDNLMNV EGHAAPSAII
     NALKNCGRDG IIRGTGKPNS AAVSILGQYT TGPFENTVKG LVRIVEVAQK KTFFDINLNG
     VEKPGLYYAS VRASGDLSEG VKSTGDPIYK FDQPIDCTSP SDSIPNSFSG SSFVSAPVHV
     WELIGRSFVV TTDPEHNVNK DNDISFGGVI ARSAGIWEND KEVCACSGKT LWQERKDAIQ
     HNIRF