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Database: UniProt
Entry: M3B5A0_PSEFD
LinkDB: M3B5A0_PSEFD
Original site: M3B5A0_PSEFD 
ID   M3B5A0_PSEFD            Unreviewed;       154 AA.
AC   M3B5A0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|ARBA:ARBA00020928, ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=MYCFIDRAFT_210905 {ECO:0000313|EMBL:EME84543.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME84543.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME84543.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME84543.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917, 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. {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. {ECO:0000256|RuleBase:RU000393};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; KB446557; EME84543.1; -; Genomic_DNA.
DR   RefSeq; XP_007925167.1; XM_007926976.1.
DR   AlphaFoldDB; M3B5A0; -.
DR   STRING; 383855.M3B5A0; -.
DR   GeneID; 19337240; -.
DR   KEGG; pfj:MYCFIDRAFT_210905; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   OrthoDB; 3470597at2759; -.
DR   Proteomes; UP000016932; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          14..150
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          125..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  15859 MW;  AF8F5C8098D3DA41 CRC64;
     MVKAVAVLRG DSNVKGTVTF EQDAESSPTT VSWDITGHDA NAERGMHVHA FGDNTNGCTS
     AGPHFNPHNK THGAPEDTER HVGDLGNFKT DGQGNAKGSV QDKLIKLIGP ESVLGRTIVV
     HAGTDDLGKG GHEDSKKTGN AGGRPACGVI GIAA
//
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