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Database: UniProt
Entry: A0A251NK08_PRUPE
LinkDB: A0A251NK08_PRUPE
Original site: A0A251NK08_PRUPE 
ID   A0A251NK08_PRUPE        Unreviewed;       236 AA.
AC   A0A251NK08;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-DEC-2018, entry version 7.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PRUPE_6G042300 {ECO:0000313|EMBL:ONH99666.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Rosales; Rosaceae; Amygdaloideae;
OC   Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH99666.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONH99666.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G.,
RA   Dondini L., Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C.,
RA   Aramini V., Copetti D., Gonzalez S., Horner D.S., Falchi R., Lucas S.,
RA   Mica E., Maldonado J., Lazzari B., Bielenberg D., Pirona R.,
RA   Miculan M., Barakat A., Testolin R., Stella A., Tartarini S.,
RA   Tonutti P., Arus P., Orellana A., Wells C., Main D., Vizzotto G.,
RA   Silva H., Salamini F., Schmutz J., Morgante M., Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies
RT   unique patterns of genetic diversity, domestication and genome
RT   evolution.";
RL   Nat. Genet. 45:487-494(2013).
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; CM007656; ONH99666.1; -; Genomic_DNA.
DR   EnsemblPlants; ONH99666; ONH99666; PRUPE_6G042300.
DR   Gramene; ONH99666; ONH99666; PRUPE_6G042300.
DR   Proteomes; UP000006882; Chromosome g6.
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:UP000006882};
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:UP000006882}.
FT   DOMAIN       35    115       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      126    228       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        60     60       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       108    108       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       197    197       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       201    201       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   236 AA;  26262 MW;  76EF171F4F4A8B6A CRC64;
     MALGAVSRRG LAGLSRNSGG LGLGLGLVTV RGLKTFTLPD LSYDYGELEP YISGEIMQLH
     HQKHHQTYVT NFNKALEHLD QAMAKGHSPT IVKLQSAIKF NGGGHINHSV FWKNLTPVRE
     GGGEPPKDSL ARAVENQFGS LDSLIQKVNV EGAALQGSGW VWLALDKDQK RLSIETTFNQ
     DPLVAKGSSY VPLLGIDVWE HAYYLQYKNV RPDYLKNIWK VINWKYASDV YEKECP
//
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