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Database: UniProt
Entry: S3CNA6_OPHP1
LinkDB: S3CNA6_OPHP1
Original site: S3CNA6_OPHP1 
ID   S3CNA6_OPHP1            Unreviewed;       156 AA.
AC   S3CNA6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   10-APR-2019, entry version 22.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=F503_00806 {ECO:0000313|EMBL:EPE08023.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Ophiostomatales; Ophiostomataceae;
OC   Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08023.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE08023.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08023.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S.,
RA   Docking R., Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma
RT   piceae, and a comparison with the bark beetle-associated pine pathogen
RT   Grosmannia clavigera.";
RL   BMC Genomics 14:373-373(2013).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; KE148149; EPE08023.1; -; Genomic_DNA.
DR   STRING; 61273.S3CNA6; -.
DR   EnsemblFungi; EPE08023; EPE08023; F503_00806.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000016923; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:EnsemblFungi.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000016923};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       13    152       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   156 AA;  16022 MW;  1D06373899EA8591 CRC64;
     MASRSTFAVV RGDAKVSGTV TFVQESESAP TTITYDLTGN DANAERGFHI HTFGDNTNGC
     TSAGPHFNPH GKTHGAPTDE ARHVGDLGNI KTDAQGNAKG TIEDKLVKLI GPESVIGRTV
     VVHGGTDDLG KGANEESLKT GNAGPRPACG VIGISN
//
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