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Database: UniProt
Entry: W9RZP5_9ROSA
LinkDB: W9RZP5_9ROSA
Original site: W9RZP5_9ROSA 
ID   W9RZP5_9ROSA            Unreviewed;       238 AA.
AC   W9RZP5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=L484_010676 {ECO:0000313|EMBL:EXC19545.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Rosales; Moraceae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC19545.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K.
RT   Schneid.";
RL   Submitted (JAN-2013) 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; KE345873; EXC19545.1; -; Genomic_DNA.
DR   RefSeq; XP_010108483.1; XM_010110181.1.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000030645; 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:UP000030645};
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:UP000030645}.
FT   DOMAIN       31    112       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      122    231       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        56     56       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       104    104       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       193    193       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       197    197       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   238 AA;  26423 MW;  3364A779679472FE CRC64;
     MALGSLRRKA LLDLGGNGGR LGLGLVRGLK TFTLPDLPYD YGALEPVISA EIMLLHHQKH
     HQTYVTNYNK SLEQLDHAID KGDVSTTVKL QSSVKFNGGG HLNHSIFWKN LAPVNEGGGE
     PPKGSLGWAI DTQFGSLESL ILKINTEGAA LQGSGWVWLA LDKEFKKLSI ETTANQDPLV
     TKAATLVPLL GIDVWEHAYY LQNVITMQYK NVKPDYLKNI WKVINWKYVS EVFEKESP
//
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