ID   CCS1_DEBHA              Reviewed;         250 AA.
AC   Q6BK66;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone;
GN   Name=CCS1; OrderedLocusNames=DEHA2F24486g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89816.2; -; Genomic_DNA.
DR   RefSeq; XP_461405.2; XM_461405.1.
DR   AlphaFoldDB; Q6BK66; -.
DR   SMR; Q6BK66; -.
DR   STRING; 4959.XP_461405.2; -.
DR   PRIDE; Q6BK66; -.
DR   EnsemblFungi; CAG89816; CAG89816; DEHA2F24486g.
DR   GeneID; 2903791; -.
DR   KEGG; dha:DEHA2F24486g; -.
DR   VEuPathDB; FungiDB:DEHA2F24486g; -.
DR   eggNOG; KOG4656; Eukaryota.
DR   HOGENOM; CLU_056632_0_0_1; -.
DR   InParanoid; Q6BK66; -.
DR   OMA; KGMGSDQ; -.
DR   OrthoDB; 1527306at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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..250
FT                   /note="Superoxide dismutase 1 copper chaperone"
FT                   /id="PRO_0000239062"
FT   DOMAIN          4..67
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         15
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         18
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         229
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT   BINDING         231
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT   DISULFID        229
FT                   /note="Interchain (with C-58 in apo-SOD1)"
FT                   /evidence="ECO:0000250|UniProtKB:P40202"
SQ   SEQUENCE   250 AA;  26199 MW;  6BD6EA5D6946CFEF CRC64;
     MTKSFEIVFA VPMECQSCVD SVSSSLKSLN GISKYDIDLK SNLVTTEGSV PPSEIVKAIQ
     STGKDAIIRG TGAPNSAAVC ILESFDPKDI QQPVKGLARI VSVGANDLVV DLTVNGLPQG
     VYYPSIRKSG NLSKGALSTG ECFYPLGPLE VDQPVSESTT INSLGAASPT VEEGSLYAGQ
     GFLHADLNIS DLIGRSVILS KLKDKTAPDS LCGVIARSAG AWENDKQVCS CSGKTVWQER
     SEALAKGLKS