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Database: UniProt
Entry: A0A0D3CLB6_BRAOL
LinkDB: A0A0D3CLB6_BRAOL
Original site: A0A0D3CLB6_BRAOL 
ID   A0A0D3CLB6_BRAOL        Unreviewed;       231 AA.
AC   A0A0D3CLB6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   05-DEC-2018, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=106292572 {ECO:0000313|EnsemblPlants:Bo5g137020.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae;
OC   Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g137020.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo5g137020.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F.,
RA   Belcram H., Links M.G., Just J., Clarke C., Bender T., Huebert T.,
RA   Mason A.S., Pires J.C., Barker G., Moore J., Walley P.G., Manoli S.,
RA   Batley J., Edwards D., Nelson M.N., Wang X., Paterson A.H., King G.,
RA   Bancroft I., Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome
RT   dominance in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo5g137020.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   RefSeq; XP_013583638.1; XM_013728184.1.
DR   EnsemblPlants; Bo5g137020.1; Bo5g137020.1; Bo5g137020.
DR   GeneID; 106292572; -.
DR   Gramene; Bo5g137020.1; Bo5g137020.1; Bo5g137020.
DR   KEGG; boe:106292572; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000032141; Chromosome C5.
DR   ExpressionAtlas; A0A0D3CLB6; baseline.
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:UP000032141};
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:UP000032141}.
FT   DOMAIN       30    111       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      121    223       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        55     55       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       103    103       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       192    192       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       196    196       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   231 AA;  25433 MW;  1A6A72E995B04A92 CRC64;
     MAIRSVLSTR TLSGLKETSS KLLGFRGIQT FTLPDLPYDY SALEPAISGE IMQIHHQKHH
     QTYVTNYNNA LEQLDQAVNK GDASTVVKLH SAIQFNGGGH VNHSIFWKNL APVNQGGGEP
     PKGALGGAID THFGSLEGLV KKMSAEGAAL QGSGWVWLGL DKELKKLVVD TTANQDPLVT
     KGASLVPLVG IDVWEHAYYL QYKNVRPDYL KNVWKVINWK YASEVYESEC K
//
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