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Database: UniProt/TrEMBL
Entry: B7PUC4_IXOSC
LinkDB: B7PUC4_IXOSC
Original site: B7PUC4_IXOSC 
ID   B7PUC4_IXOSC            Unreviewed;       154 AA.
AC   B7PUC4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   25-OCT-2017, entry version 60.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=8031487 {ECO:0000313|VectorBase:ISCW008219-PA};
GN   ORFNames=IscW_ISCW008219 {ECO:0000313|EMBL:EEC10196.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Acari; Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945 {ECO:0000313|Proteomes:UP000001555};
RN   [1] {ECO:0000313|EMBL:EEC10196.1, ECO:0000313|Proteomes:UP000001555, ECO:0000313|VectorBase:ISCW008219-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555,
RC   ECO:0000313|VectorBase:ISCW008219-PA}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC10196.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M.,
RA   Amedeo P., Galinsky K.J., Schobel S., Inman J., Hostetler J.,
RA   Miller J., Hammond M., Megy K., Lawson D., Kodira C., Sutton G.,
RA   Meyer J., Hill C.A., Birren B., Nene V., Collins F.,
RA   Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:ISCW008219-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|VectorBase:ISCW008219-PA};
RG   VectorBase;
RL   Submitted (FEB-2017) to UniProtKB.
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; ABJB010584638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS791940; EEC10196.1; -; Genomic_DNA.
DR   RefSeq; XP_002405905.1; XM_002405861.1.
DR   UniGene; Isc.683; -.
DR   ProteinModelPortal; B7PUC4; -.
DR   STRING; 6945.ISCW008219-PA; -.
DR   EnsemblMetazoa; ISCW008219-RA; ISCW008219-PA; ISCW008219.
DR   GeneID; 8031487; -.
DR   KEGG; isc:IscW_ISCW008219; -.
DR   VectorBase; ISCW008219-RA; ISCW008219-PA; ISCW008219.
DR   CTD; 8031487; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; B7PUC4; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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; 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:UP000001555};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:EEC10196.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15643 MW;  69FA5372AA3408D2 CRC64;
     MSVKAVCVLK GSEKTTGTVY FTQAGPNQPV VVTGEITGLE QGLHGFHVHE FGDNTNGCTS
     AGPHFNPLGK EHGAPTDTNR HVGDLGNVIA GDDGVAKVAI TDSQISLSGP HSIIGRSVVI
     HADPDDLGKG GHELSKTTGN AGARLACGVV GVTK
//
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