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Database: UniProt
Entry: X0BZT7_FUSOX
LinkDB: X0BZT7_FUSOX
Original site: X0BZT7_FUSOX 
ID   X0BZT7_FUSOX            Unreviewed;       258 AA.
AC   X0BZT7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   05-DEC-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=FOQG_09203 {ECO:0000313|EMBL:EXK87396.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK87396.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK87396.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK87396.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) 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; KI979324; EXK87396.1; -; Genomic_DNA.
DR   EnsemblFungi; EXK87396; EXK87396; FOQG_09203.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000030663};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    258       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004938974.
FT   DOMAIN       51    132       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      146    242       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       124    124       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       209    209       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       213    213       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   258 AA;  28324 MW;  2A55A9292B843CC5 CRC64;
     MFFSRIPLLP LFFFVSSSSS SSEPDLASDH NQAYTALPDN IQSFSAMSVG TYSLPALPYA
     YDALEPSISA QIMELHHSKH HQAYVTNLNA ALKNYATATS TNDIAGQIAL QSAIKFNGGG
     HINHSLFWEN LSPSSSADAK PESAPTLSAE ISKTWGSIQA FQEAFKKTLL GLQGSGWGWL
     VKDTHGLRIV TTKDQDPVVG GEVPIFGVDM WEHAYYLQYL NGKAAYVDNI WKVINWKTAE
     ARFTGTREDA FKVLRASI
//
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