ID J9EJI4_WUCBA Unreviewed; 265 AA.
AC J9EJI4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=WBA_LOCUS10266 {ECO:0000313|EMBL:VDM19016.1}, WUBG_06733
GN {ECO:0000313|EMBL:EJW82358.1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW82358.1, ECO:0000313|Proteomes:UP000004810};
RN [1] {ECO:0000313|Proteomes:UP000004810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Wuchereria bancrofti.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EJW82358.1}
RP NUCLEOTIDE SEQUENCE.
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Haas B.,
RA Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Wuchereria bancrofti.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:maker-PairedContig_262-snap-gene-0.14-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_262-snap-gene-0.14-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [4] {ECO:0000313|EMBL:VDM19016.1, ECO:0000313|Proteomes:UP000270924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00002170}.
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|ARBA:ARBA00001605};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714}.
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DR EMBL; ADBV01002935; EJW82358.1; -; Genomic_DNA.
DR EMBL; UYWW01012157; VDM19016.1; -; Genomic_DNA.
DR STRING; 6293.J9EJI4; -.
DR WBParaSite; maker-PairedContig_262-snap-gene-0.14-mRNA-1; maker-PairedContig_262-snap-gene-0.14-mRNA-1; maker-PairedContig_262-snap-gene-0.14.
DR OMA; DSLINWD; -.
DR Proteomes; UP000004810; Unassembled WGS sequence.
DR Proteomes; UP000270924; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000270924}.
FT DOMAIN 67..147
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 158..258
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
SQ SEQUENCE 265 AA; 30606 MW; 8B7A1BD9CFFDD72E CRC64;
MFRWREAIYR DLLQVTDESD YWRHRSLTGQ QKALIEDLYR KFVENENDFE LDGFCVYSYG
LNLRQLKHTL PDLPYDYGAL EPILSAEIMK VHHGKHHVAY VNALNQAEEK VKEALAKGDM
QAVVAATKLM NFNVGGHINH TLFWEGLTTV KDSGEPSFEL MSAIKKDFGS LEMMKDKLSA
KTIAIQGSGW GWLAYDKEMK RLQLACCPNQ DILQSTTGLI PLFCIDVWEH AYYLQYKNVR
PDFVKAIWKI ANWKVISDRY VKAMG
//
