ID   O18483_ONCVO            Unreviewed;       201 AA.
AC   O18483;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=OvSOD2 {ECO:0000313|EMBL:AAB64227.1};
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282 {ECO:0000313|EMBL:AAB64227.1};
RN   [1] {ECO:0000313|EMBL:AAB64227.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tawe W., Eschbach M.-L., Walter R.D., Henkle-Duehrsen K.J.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000024404}
RP   NUCLEOTIDE SEQUENCE.
RA   Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA   Berriman M.;
RT   "Genome sequencing of Onchocerca volvulus.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:OVOC11516.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) 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. {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. {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; CMVM020000375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF009621; AAB64227.1; -; Genomic_DNA.
DR   AlphaFoldDB; O18483; -.
DR   STRING; 6282.O18483; -.
DR   EnsemblMetazoa; OVOC11516.1; OVOC11516.1; WBGene00248325.
DR   EnsemblMetazoa; OVOC11516.2; OVOC11516.2; WBGene00248325.
DR   HOGENOM; CLU_056632_4_2_1; -.
DR   OMA; CGIILET; -.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000024404};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          57..195
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   201 AA;  21148 MW;  9BD9E833C71AEE5C CRC64;
     MINSFIVIFL SFLIFINYAN LVYVEATHVY GRRSHSNGMH GNGARRAVAV LRGDAGVSGI
     IYFQQDSGGS ITTISGSVSG LTPGLHGFHV HQYGDQTNGC TSAGGHYNPY GKTHGDPNDR
     IKHIGDLGNI VAGANGVAEV YINSYHIKLR GPLSVIGRSL VVHENPDDLG QGTGNMREES
     LKTGNAGSRL ACAVIGIAAV S
//