GenomeNet

Database: UniProt/SWISS-PROT
Entry: SODC_DROWI
LinkDB: SODC_DROWI
Original site: SODC_DROWI 
ID   SODC_DROWI              Reviewed;         153 AA.
AC   P41973; B4N5E2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-JUN-2017, entry version 110.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=Sod; ORFNames=GK20556;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7926818; DOI=10.1016/0378-1119(94)90085-X;
RA   Kwiatowski J., Latorre A., Skarecky D., Ayala F.J.;
RT   "Characterization of a Cu/Zn superoxide dismutase-encoding gene region
RT   in Drosophila willistoni.";
RL   Gene 147:295-296(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; L13281; AAA57250.1; -; Genomic_DNA.
DR   EMBL; CH964101; EDW79581.1; -; Genomic_DNA.
DR   RefSeq; XP_002068595.1; XM_002068559.2.
DR   ProteinModelPortal; P41973; -.
DR   SMR; P41973; -.
DR   STRING; 7260.FBpp0249699; -.
DR   EnsemblMetazoa; FBtr0251207; FBpp0249699; FBgn0013156.
DR   GeneID; 6645808; -.
DR   KEGG; dwi:Dwil_GK20556; -.
DR   FlyBase; FBgn0013156; Dwil\Sod.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; P41973; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   PhylomeDB; P41973; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    153       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164099.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000250}.
SQ   SEQUENCE   153 AA;  15543 MW;  40F798E2285237CE CRC64;
     MVVKAVCVIN GDAKGTVFFE QEDNGAPVKV TGEVTGLGKG LHGFHVHEFG DNTNGCMSSG
     PHFNPHSKEH GAPGDENRHL GDLGNIEASG SGPTAVNITD SKITLVGANS IIGRTVVVHA
     DPDDLGKGGH ELSKTTGNAG ARIGCGVIGI AKI
//
DBGET integrated database retrieval system