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Database: UniProt
Entry: D7LXR5_ARALL
LinkDB: D7LXR5_ARALL
Original site: D7LXR5_ARALL 
ID   D7LXR5_ARALL            Unreviewed;       164 AA.
AC   D7LXR5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 54.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=ARALYDRAFT_326224 {ECO:0000313|EMBL:EFH48060.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A.,
RA   Schneeberger K., Spannagl M., Wang X., Yang L., Nasrallah M.E.,
RA   Bergelson J., Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X.,
RA   Van de Peer Y., Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome
RT   size change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; GL348718; EFH48060.1; -; Genomic_DNA.
DR   RefSeq; XP_002871801.1; XM_002871755.1.
DR   ProteinModelPortal; D7LXR5; -.
DR   STRING; 59689.fgenesh1_pm.C_scaffold_6001444; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_6001444; fgenesh1_pm.C_scaffold_6001444; fgenesh1_pm.C_scaffold_6001444.
DR   GeneID; 9307870; -.
DR   Gramene; fgenesh1_pm.C_scaffold_6001444; fgenesh1_pm.C_scaffold_6001444; fgenesh1_pm.C_scaffold_6001444.
DR   KEGG; aly:ARALYDRAFT_326224; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:EnsemblPlants.
DR   GO; GO:0005773; C:vacuole; IEA:EnsemblPlants.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071486; P:cellular response to high light intensity; IEA:EnsemblPlants.
DR   GO; GO:0071457; P:cellular response to ozone; IEA:EnsemblPlants.
DR   GO; GO:0071472; P:cellular response to salt stress; IEA:EnsemblPlants.
DR   GO; GO:0071493; P:cellular response to UV-B; IEA:EnsemblPlants.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008694};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       17    154       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   164 AA;  16956 MW;  0C6262FDFE0ECD5A CRC64;
     MEAPRGNLRA VALIAGDNNV RGCLQFVQDT FGTTHVTGKI SGLSPGFHGF HIHSFGDTTN
     GCNSTGPHFN PLNRVHGPPN EEERHAGDLG NILAGSDGVA EISIKDKQIP LSGQYSILGR
     AVVVHADPDD LGKGGHKLSK STGNAGSRVG CGIIGLQSSA DAKL
//
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