GenomeNet

Database: UniProt
Entry: B7QH32_IXOSC
LinkDB: B7QH32_IXOSC
Original site: B7QH32_IXOSC 
ID   B7QH32_IXOSC            Unreviewed;       155 AA.
AC   B7QH32;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   10-APR-2019, entry version 62.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=8041155 {ECO:0000313|VectorBase:ISCW015027-PA};
GN   ORFNames=IscW_ISCW015027 {ECO:0000313|EMBL:EEC18154.1};
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:EEC18154.1, ECO:0000313|Proteomes:UP000001555, ECO:0000313|VectorBase:ISCW015027-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555,
RC   ECO:0000313|VectorBase:ISCW015027-PA}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC18154.1};
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:ISCW015027-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|VectorBase:ISCW015027-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:
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; ABJB010846394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS936254; EEC18154.1; -; Genomic_DNA.
DR   RefSeq; XP_002414489.1; XM_002414444.1.
DR   UniGene; Isc.25358; -.
DR   ProteinModelPortal; B7QH32; -.
DR   EnsemblMetazoa; ISCW015027-RA; ISCW015027-PA; ISCW015027.
DR   GeneID; 8041155; -.
DR   KEGG; isc:IscW_ISCW015027; -.
DR   VectorBase; ISCW015027-RA; ISCW015027-PA; ISCW015027.
DR   CTD; 8041155; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; B7QH32; -.
DR   KO; K04565; -.
DR   OMA; IVIHANE; -.
DR   OrthoDB; 1574423at2759; -.
DR   PhylomeDB; B7QH32; -.
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:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; 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:EEC18154.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       15    151       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   155 AA;  16025 MW;  2121BE414D0B34A0 CRC64;
     MGAQAQSVIC VLNAGEIRGI VQFAQLNASH VRVSFNGSGI PEGVHGFHVH QYGDISTGCA
     AAGGHFNPDS VNHGGPDSPV RHVGDLGNVE ADLHGVVTFS RDDSYLQLSG DRSILGRAIV
     LHADPDDLGL GGYPDSLTTG HAGARIACCV IVYAK
//
DBGET integrated database retrieval system