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Database: UniProt
Entry: A0A183K4G5_9TREM
LinkDB: A0A183K4G5_9TREM
Original site: A0A183K4G5_9TREM 
ID   A0A183K4G5_9TREM        Unreviewed;       111 AA.
AC   A0A183K4G5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   10-APR-2019, entry version 8.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=SCUD_LOCUS9885 {ECO:0000313|EMBL:VDP37518.1};
OS   Schistosoma curassoni.
OC   Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000988501-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000988501-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SCUD_0000988501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDP37518.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Dakar {ECO:0000313|EMBL:VDP37518.1};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAK01033468; VDP37518.1; -; Genomic_DNA.
DR   WBParaSite; SCUD_0000988501-mRNA-1; SCUD_0000988501-mRNA-1; SCUD_0000988501.
DR   Proteomes; UP000050789; Genome assembly.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   Complete proteome {ECO:0000313|Proteomes:UP000050789};
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       22    106       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   111 AA;  12358 MW;  01E8A9268B50D1B0 CRC64;
     MSSNKRFNLV TNFLREKFKN NHFIDVRHGG RHGYPRHAGD LGNIRVGHNS VMIFDLYVSL
     KGLEPYDGFI GRSLVIHANM DDLGRNADEG SRTTGNSGPR LACATIGYRA P
//
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