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Database: UniProt
Entry: N1RI24_FUSC4
LinkDB: N1RI24_FUSC4
Original site: N1RI24_FUSC4 
ID   N1RI24_FUSC4            Unreviewed;       212 AA.
AC   N1RI24;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   16-JAN-2019, entry version 20.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=FOC4_g10006602 {ECO:0000313|EMBL:EMT66208.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229665 {ECO:0000313|EMBL:EMT66208.1};
RN   [1] {ECO:0000313|EMBL:EMT66208.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Race 4 {ECO:0000313|EMBL:EMT66208.1};
RA   Fang X., Huang J.;
RT   "Genome Sequencing and Comparative Transcriptomics of Race1 and Race4
RT   of Banana pathogen: Fusarium oxysporum f.sp. Cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; KB726988; EMT66208.1; -; Genomic_DNA.
DR   EnsemblFungi; EMT66208; EMT66208; FOC4_g10006602.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        5     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      100    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        30     30       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   212 AA;  23243 MW;  7459C62461867ECB CRC64;
     MSVGTYSLPA LPYAYDALEP SISAQIMELH HSKHHQAYVT NLNAALKNYA TATSTNDIAG
     QIALQSAIKF NGGGHINHSL FWENLSPSSS ADAKPESAPT LSAEISKTWG SIQAFQEAFK
     KTLLGLQGSG WGWLVKDTHG LRIVTTKDQD PVVGGEVPIF GVDMWEHAYY LQYLNGKAAY
     VDNVWNVINW KTAEARFTGT REDAFKVLRA SI
//
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