ID   A0A166NYU5_9HYPO        Unreviewed;       248 AA.
AC   A0A166NYU5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
GN   ORFNames=AAL_05745 {ECO:0000313|EMBL:KZZ93360.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ93360.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:KZZ93360.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ93360.1,
RC   ECO:0000313|Proteomes:UP000078544};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ93360.1}.
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DR   EMBL; AZGY01000013; KZZ93360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166NYU5; -.
DR   STRING; 1081109.A0A166NYU5; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000078544; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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:UP000078544}.
FT   DOMAIN          6..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   248 AA;  26290 MW;  C17A5DCFE35BEBB0 CRC64;
     MTVDNSFQTT FAVPLSCNDC IKAVSDSLYQ LGGISKVQGD LQNQIVSVEG VAAPSAIVQA
     IQATGRDAIL RGSGATDSAA VSILETFSDR GIEESDDADR SVRGLARFVQ VNPGRTLVDL
     TLRGVAPGRY QATIREFGDL KDGAMSTGPV WSGGSSMPLG ILGSLDVDED GRGGAFVDHP
     FKIWEVIGHA MILTKQDEVA GPLTNDENTV VGVIARSAGV WDNDKTVCSC TGKTLWEERK
     DEVRKGML
//