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Database: UniProt
Entry: A0A0D2AMV3_9PEZI
LinkDB: A0A0D2AMV3_9PEZI
Original site: A0A0D2AMV3_9PEZI 
ID   A0A0D2AMV3_9PEZI        Unreviewed;       243 AA.
AC   A0A0D2AMV3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
GN   ORFNames=PV09_00963 {ECO:0000313|EMBL:KIW08018.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08018.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW08018.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08018.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847531; KIW08018.1; -; Genomic_DNA.
DR   RefSeq; XP_016217887.1; XM_016353792.1.
DR   AlphaFoldDB; A0A0D2AMV3; -.
DR   STRING; 253628.A0A0D2AMV3; -.
DR   GeneID; 27308936; -.
DR   VEuPathDB; FungiDB:PV09_00963; -.
DR   HOGENOM; CLU_056632_0_0_1; -.
DR   InParanoid; A0A0D2AMV3; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000053259; 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:UP000053259}.
FT   DOMAIN          8..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   243 AA;  25600 MW;  6A3553BD0889BAF7 CRC64;
     MTVNSIPPFQ TTFAVPLTCE SCVKDVSKSL YALPGIVNVT GDVSSGLVHI TGTAAPSSIV
     SAIQSTGRDA ILRGSGRPDS AAVCILETHT SRSDVGEKVR GLVRMVQVAD ELTIFDVAIR
     GLSEGTYDAT IRNNGNISYG AESTGSIWDA EGKGRGVLGT LSINKGGVGS VFLDKPVAIW
     ELIGRSIVVA KQGKITFNKE DPDELVGVIA RSAGVWENDK TVCSCSGKTV WEERVEQQGR
     GML
//
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