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Database: UniProt
Entry: A0A0M9G869_9TRYP
LinkDB: A0A0M9G869_9TRYP
Original site: A0A0M9G869_9TRYP 
ID   A0A0M9G869_9TRYP        Unreviewed;       208 AA.
AC   A0A0M9G869;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ABB37_01236 {ECO:0000313|EMBL:KPA84740.1};
OS   Leptomonas pyrrhocoris.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=157538 {ECO:0000313|EMBL:KPA84740.1};
RN   [1] {ECO:0000313|EMBL:KPA84740.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H10 {ECO:0000313|EMBL:KPA84740.1};
RA   Flegontov P., Butenko A., Firsov S., Vlcek C., Logacheva M.D.,
RA   Field M., Filatov D., Flegontova O., Gerasimov E., Jackson A.P.,
RA   Kelly S., Opperdoes F., O'Reilly A., Votypka J., Yurchenko V.,
RA   Lukes J.;
RT   "High-quality genome of monoxenous trypanosomatid Leptomonas
RT   pyrrhocoris.";
RL   Submitted (JUL-2015) 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: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:KPA84740.1}.
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DR   EMBL; LGTL01000002; KPA84740.1; -; Genomic_DNA.
DR   RefSeq; XP_015663179.1; XM_015797659.1.
DR   EnsemblProtists; KPA84740; KPA84740; ABB37_01236.
DR   GeneID; 26901531; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23132 MW;  0F8DFEE0BC43271A CRC64;
     MPFAVQPLPW GYDALASKGI SKEQVTFHYD KHHKGYAVKL NAAAEANPDL ASKSLVEIIK
     TVKGPAFNSA AQIFNHDFYW RCMSANGGGE PHGKIANAIT ESFGSFAKFK EEFTAAANGH
     FGSGWAWLVK DTASGKLKVY QSHDANCPLT EENLKPILTC DVWEHAYYID YRNDRAAYVN
     TWWKVVNWDF ANKCYSASSG SSYVNSDL
//
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