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Database: UniProt
Entry: H2KUR6_CLOSI
LinkDB: H2KUR6_CLOSI
Original site: H2KUR6_CLOSI 
ID   H2KUR6_CLOSI            Unreviewed;       233 AA.
AC   H2KUR6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=CLF_109998 {ECO:0000313|EMBL:GAA36079.2};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea;
OC   Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA36079.2};
RN   [1] {ECO:0000313|EMBL:GAA36079.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA36079.2};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L.,
RA   Lv X., Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C.,
RA   Hu X., Xu J., Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(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; DF144161; GAA36079.2; -; Genomic_DNA.
DR   SMR; H2KUR6; -.
DR   InParanoid; H2KUR6; -.
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; 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   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       57    194       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   233 AA;  25378 MW;  BDE4E3D82B186194 CRC64;
     MGAELRLLVN RTKGRVDTFL VKVFSDNHIQ DKEMHSVNAA DSLTSFELSD GIAVFQGNHT
     GRVDFKVTPP RMVNVVGSVD GFEREKMHGV HIHETGDIDN GCLNANAHWN PFNKNHGGVD
     SRERHEGDLG NAMTDVNGVL HINVTVEIGL LDPRLDFIGL ALVVHAQVDD LGRFPDIGSR
     TTGNSGGRLA CAVIGRTSSY KVNKAIGETS PNIVLLFAGI LPIILRQTLY HIL
//
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