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Database: UniProt
Entry: A0A0G4EVM8_VITBC
LinkDB: A0A0G4EVM8_VITBC
Original site: A0A0G4EVM8_VITBC 
ID   A0A0G4EVM8_VITBC        Unreviewed;       222 AA.
AC   A0A0G4EVM8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-DEC-2018, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Vbra_1709 {ECO:0000313|EMBL:CEM02146.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Alveolata; Chromerida; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM02146.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM02146.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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; CDMY01000319; CEM02146.1; -; Genomic_DNA.
DR   EnsemblProtists; CEM02146; CEM02146; Vbra_1709.
DR   OMA; YLHSIFW; -.
DR   Proteomes; UP000041254; 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:UP000041254};
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:UP000041254}.
FT   DOMAIN       17     99       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      107    208       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        41     41       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        91     91       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       176    176       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       180    180       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   222 AA;  24654 MW;  9C7BBB26CD7ACBF9 CRC64;
     MSFLSSVPCA MADGDFYKLP DLPYDYGALE PSIDATTMQL HHDKHHATYV KKLNDALKEK
     KPRATNLADL QAEAMKLGST VRNNGGGAYN HALFWRMMAP VGKGGEPSEA LQKAINAVWG
     SKEGFQEAFS KAATAVFGSG WAWLIVKKGG LEITTTPNQD NNLMISGSGI PILGIDVWEH
     AYYLKYNNRR PDYVKEWWKV VNWSEVNNNY ENYALKGIPV PA
//
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