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Database: UniProt/TrEMBL
Entry: D7KIV8_ARALL
LinkDB: D7KIV8_ARALL
Original site: D7KIV8_ARALL 
ID   D7KIV8_ARALL            Unreviewed;       152 AA.
AC   D7KIV8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   05-JUL-2017, entry version 50.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=ARALYDRAFT_888118 {ECO:0000313|EMBL:EFH65975.1};
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; GL348713; EFH65975.1; -; Genomic_DNA.
DR   RefSeq; XP_002889716.1; XM_002889670.1.
DR   STRING; 59689.scaffold_100912.1; -.
DR   PRIDE; D7KIV8; -.
DR   EnsemblPlants; scaffold_100912.1; scaffold_100912.1; scaffold_100912.1.
DR   GeneID; 9328537; -.
DR   Gramene; scaffold_100912.1; scaffold_100912.1; scaffold_100912.1.
DR   KEGG; aly:ARALYDRAFT_888118; -.
DR   KO; K04565; -.
DR   OrthoDB; EOG09360P4O; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR   GO; GO:0005634; C:nucleus; 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:0071280; P:cellular response to copper ion; IEA:EnsemblPlants.
DR   GO; GO:0071484; P:cellular response to 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:0071329; P:cellular response to sucrose stimulus; IEA:EnsemblPlants.
DR   GO; GO:0071493; P:cellular response to UV-B; IEA:EnsemblPlants.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR   GO; GO:0035195; P:gene silencing by miRNA; IEA:EnsemblPlants.
DR   GO; GO:0010039; P:response to iron ion; IEA:EnsemblPlants.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 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       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15137 MW;  B53DC02FE7F9F6F2 CRC64;
     MAKGVAVLNS SEGVKGTIFF TQEGDGVTTV TGTVSGLKPG LHGFHVHALG DTTNGCMSTG
     PHFNPDGKTH GAPEDANRHA GDLGNITVGD DGTATFTITD TQIPLTGPNS IVGRAVVVHA
     DPDDLGKGGH ELSLATGNAG GRVACGIIGL QG
//
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