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Database: UniProt
Entry: E5SDW9_TRISP
LinkDB: E5SDW9_TRISP
Original site: E5SDW9_TRISP 
ID   E5SDW9_TRISP            Unreviewed;       258 AA.
AC   E5SDW9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 36.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Tsp_01933 {ECO:0000313|EMBL:EFV57014.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV57014.1, ECO:0000313|Proteomes:UP000006823};
RN   [1] {ECO:0000313|EMBL:EFV57014.1, ECO:0000313|Proteomes:UP000006823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS 195 {ECO:0000313|EMBL:EFV57014.1,
RC   ECO:0000313|Proteomes:UP000006823};
RX   PubMed=21336279; DOI=10.1038/ng.769;
RA   Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S.,
RA   Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P.,
RA   Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K.,
RA   Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.;
RT   "The draft genome of the parasitic nematode Trichinella spiralis.";
RL   Nat. Genet. 43:228-235(2011).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFV57014.1}.
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DR   EMBL; ABIR02000866; EFV57014.1; -; Genomic_DNA.
DR   RefSeq; XP_003377741.1; XM_003377693.1.
DR   ProteinModelPortal; E5SDW9; -.
DR   EnsemblMetazoa; EFV57014; EFV57014; EFV57014.
DR   GeneID; 10907148; -.
DR   KEGG; tsp:Tsp_01933; -.
DR   CTD; 10907148; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   InParanoid; E5SDW9; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000006823; 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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006823};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006823}.
FT   DOMAIN       20     94       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      101    204       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        45     45       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        93     93       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       171    171       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       175    175       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   258 AA;  28706 MW;  68DB5486CF3E4473 CRC64;
     MVSFFLKSVP ASCLRCLRKK HTLPDLPYDF GALEPYISAE IMRLHHQKHH ATYVNNLNIA
     EEKHKEALAK KDTTAAIALQ PALRFNAGGH INHTPKSGGM PVGKLAQAIT NNFGSFDIFK
     ANLTAACIGV QGSGWAWLGY DANMKRLQIA TCANQDPLQA TTGLIPLLGI DVWEHAYYLQ
     YKNVRGDYVK AIWEVINWND VQQRFADAVG SALFHEKVKQ TDIAQLYTMR FCKTFDCKNK
     KKGERSSCST AALTLCGT
//
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