ID A0A365ND57_GIBIN Unreviewed; 154 AA.
AC A0A365ND57;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BFJ72_g12463 {ECO:0000313|EMBL:RKL28365.1}, FPRO05_10294
GN {ECO:0000313|EMBL:RBA18646.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA18646.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA18646.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA18646.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RKL28365.1, ECO:0000313|Proteomes:UP000283569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fp_A8 {ECO:0000313|EMBL:RKL28365.1,
RC ECO:0000313|Proteomes:UP000283569};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|RuleBase:RU000393}.
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:RBA18646.1}.
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DR EMBL; PKMI01000013; RBA18646.1; -; Genomic_DNA.
DR EMBL; MRDB01000064; RKL28365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365ND57; -.
DR VEuPathDB; FungiDB:FPRN_09385; -.
DR Proteomes; UP000251714; Unassembled WGS sequence.
DR Proteomes; UP000283569; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF103; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
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 68..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 154 AA; 15963 MW; 2E253762F0BAD5ED CRC64;
MVKAVSVLRG DSKVSGTVIF EQESESAPTT ITWDITGNDP NAKRGFHIHT FGDNTNGCTS
AGPHFNPHNK THGAPSDETR HVGDLGNLET DGQGNAKGSV TDSLVKLIGP HSIIGRTVVI
HAGTDDLGKG DNEESLKTGN AGPRPACGVI GISN
//