ID   Q2H715_CHAGB            Unreviewed;       262 AA.
AC   Q2H715;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
DE   AltName: Full=Superoxide dismutase copper chaperone {ECO:0000256|ARBA:ARBA00032899};
GN   ORFNames=CHGG_05550 {ECO:0000313|EMBL:EAQ88931.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ88931.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SIMILARITY: Belongs to the CCS1 family.
CC       {ECO:0000256|ARBA:ARBA00010636}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC       dismutase family. {ECO:0000256|ARBA:ARBA00025798}.
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DR   EMBL; CH408031; EAQ88931.1; -; Genomic_DNA.
DR   RefSeq; XP_001221645.1; XM_001221644.1.
DR   AlphaFoldDB; Q2H715; -.
DR   STRING; 306901.Q2H715; -.
DR   GeneID; 4390503; -.
DR   VEuPathDB; FungiDB:CHGG_05550; -.
DR   eggNOG; KOG4656; Eukaryota.
DR   HOGENOM; CLU_056632_0_0_1; -.
DR   InParanoid; Q2H715; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF86; COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          6..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   262 AA;  27610 MW;  62BD7FF62561ADD6 CRC64;
     MAVITPFQTL FAVPMTCEGC AKDISSALHK LPGITKVEAN VKDQLVSIEG TAAPSAIVDA
     IQATGKDAIL RGSGTSNSAA VSILETYHHK PDAEVTPAGV PGESWVNERL VRGLVRMVQV
     SPTETLVDLT VRGVPPGTYR ATIREYGNLK DGASSAGPVW SAQSKEGGPP RGVLGTVEIG
     PNGYGNTFIN HPFQVWEVIG HALVVSPQSS PWGFPRLDRL GYGRIAAVVK VWGGAAGSPR
     LGHAARDDHG IAPTCLFRRY TV
//