CCS1_ASHGO
ID CCS1_ASHGO Reviewed; 238 AA.
AC Q75DD6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Superoxide dismutase 1 copper chaperone;
GN Name=CCS1; OrderedLocusNames=ABR091C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
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).
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; AE016815; AAS50861.1; -; Genomic_DNA.
DR RefSeq; NP_983037.1; NM_208390.1.
DR AlphaFoldDB; Q75DD6; -.
DR SMR; Q75DD6; -.
DR STRING; 33169.AAS50861; -.
DR EnsemblFungi; AAS50861; AAS50861; AGOS_ABR091C.
DR GeneID; 4619141; -.
DR KEGG; ago:AGOS_ABR091C; -.
DR eggNOG; KOG4656; Eukaryota.
DR HOGENOM; CLU_056632_0_0_1; -.
DR InParanoid; Q75DD6; -.
DR OMA; KGMGSDQ; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0101031; C:chaperone complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
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; IBA:GO_Central.
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..238
FT /note="Superoxide dismutase 1 copper chaperone"
FT /id="PRO_0000239060"
FT DOMAIN 7..70
FT /note="HMA"
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 21
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 218
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 220
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT DISULFID 218
FT /note="Interchain (with C-58 in apo-SOD1)"
FT /evidence="ECO:0000250|UniProtKB:P40202"
SQ SEQUENCE 238 AA; 24068 MW; 8BC3AD7E183AF3FC CRC64;
MIDPSESFEA TYAVPMHCGD CTGEISRALR AVPGVQEVTP DLERQLVAVR GIAPPSSIVQ
ALAATGRDAI LRGSGEPDSA AVAILESASA GGPPVRGLVR AVQVAPNKTL FDITLNGLPG
PAQYYASIRA SGDVSRGAAS TGPAWHVFED AVACERASPL GADLCAGSAL FVAPLAVQAL
IGRGFLVGAD RGHALAGAAA VGVLARSAGA WQNDKVVCAC SGDTLWQERG SARSANIA
