ID   A0A168SPL9_ABSGL        Unreviewed;       271 AA.
AC   A0A168SPL9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 28.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
DE   AltName: Full=Superoxide dismutase copper chaperone {ECO:0000256|ARBA:ARBA00032899};
GN   Name=ABSGL_14405.1 scaffold 14663 {ECO:0000313|EMBL:SAM08739.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM08739.1};
RN   [1] {ECO:0000313|EMBL:SAM08739.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM08739.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT554937; SAM08739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168SPL9; -.
DR   STRING; 4829.A0A168SPL9; -.
DR   InParanoid; A0A168SPL9; -.
DR   OMA; KNVWEER; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000078561; 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; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
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   PRINTS; PR00068; CUZNDISMTASE.
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   Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT   DOMAIN          8..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   271 AA;  29447 MW;  A777A2E780A9B105 CRC64;
     MPASLKKQFK TEFAVEMTCQ SCVDDITTVL QAFPDINHFE VDLSDQRVTI EGTALPSKIS
     RALKDSGRTV IVRGQGVADE TQGHSGAAVC IFDIYGEDPT QQMPKGKSGL ARFVQIDQDT
     CLIDLTVEGL EPGKHGVHIH ECGDVSRGWL STGDHFNPTG VDHGDECTGH LGDLGNLTVD
     NNGWGDLVVE SERIKVWDII GRSMVITKHE DDLGRGLQQQ SKWDGNSGPG ILCGIIARSA
     GAFENMKKIC ACNGNTLWEE ARLVQDNRVS N
//