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Database: UniProt
Entry: A0A1X2G8S8_9FUNG
LinkDB: A0A1X2G8S8_9FUNG
Original site: A0A1X2G8S8_9FUNG 
ID   A0A1X2G8S8_9FUNG        Unreviewed;       254 AA.
AC   A0A1X2G8S8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   28-JUN-2023, entry version 20.
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=DM01DRAFT_1326578 {ECO:0000313|EMBL:ORX47954.1};
OS   Hesseltinella vesiculosa.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX   NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX47954.1, ECO:0000313|Proteomes:UP000242146};
RN   [1] {ECO:0000313|EMBL:ORX47954.1, ECO:0000313|Proteomes:UP000242146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX47954.1,
RC   ECO:0000313|Proteomes:UP000242146};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORX47954.1}.
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DR   EMBL; MCGT01000031; ORX47954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2G8S8; -.
DR   STRING; 101127.A0A1X2G8S8; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000242146; 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:UP000242146}.
FT   DOMAIN          1..55
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   254 AA;  26969 MW;  5E49B1E07A89920D CRC64;
     MTCQSCVNDI TNILNVFPNV THFDVDLENQ SVVIEGTAPP SQLARALKDT GRTVVVRGQG
     VADDQQGHSG AAVCIFDIYK DNPNQAPPTG TSGLARFVQI DRDTCLIDLT VQGLTPGKHG
     VHIHESGDIS RGWLSTGDHF NPTGVDHGDD CTGHVGDLGN IDVDTNGWGD LVVESERIKV
     WDIIGRSMVI TELADDLGKS SHADAKLTGN SGQGILSGII ARSAGAFENM KKVCACSGAT
     LWEEARVQEQ PKAV
//
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