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Database: UniProt
Entry: A0A0M8N1L7_9HYPO
LinkDB: A0A0M8N1L7_9HYPO
Original site: A0A0M8N1L7_9HYPO 
ID   A0A0M8N1L7_9HYPO        Unreviewed;       268 AA.
AC   A0A0M8N1L7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
GN   ORFNames=ESCO_004402 {ECO:0000313|EMBL:KOS21257.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21257.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS21257.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) 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   -!- 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:KOS21257.1}.
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DR   EMBL; LGSR01000013; KOS21257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N1L7; -.
DR   STRING; 150374.A0A0M8N1L7; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000053831; 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   PANTHER; PTHR10003:SF86; COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00403; HMA; 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:UP000053831}.
FT   DOMAIN          6..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   268 AA;  27867 MW;  D40C51942D272F06 CRC64;
     MAVPHTFQTL FAVPLSCDGC VKSVSDALYR LGGITRVEAN LQDQLISVQG SVAPSAIVQT
     IQETGKDAIL RGSGASNSAA VSILETYAES IAREASADPD RAVRGLARMV QVSPERTLVD
     LTVRGVSPGT YRATIREYGN LAEGAASAGP VWRGTAAAAG AASGPGSGSG SGSGSDFKGC
     LGEVQVAQDG RGSAFADHGF QIWEAIGHAL VLTRQEEREG GRLANDEDTV VGVIARSAGV
     WENDKTVCSC TGKTLWEERR DEVQKGML
//
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