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Database: UniProt
Entry: S9ULA8_9TRYP
LinkDB: S9ULA8_9TRYP
Original site: S9ULA8_9TRYP 
ID   S9ULA8_9TRYP            Unreviewed;       226 AA.
AC   S9ULA8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=STCU_03105 {ECO:0000313|EMBL:EPY31918.1}, STCU_04482
GN   {ECO:0000313|EMBL:EPY29539.1};
OS   Strigomonas culicis.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY29539.1};
RN   [1] {ECO:0000313|EMBL:EPY29539.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P.,
RA   Brocchi M., Colabardini A.C., de Araujo Lima B., Machado C.R.,
RA   de Almeida Soares C.M., Probst C.M., de Menezes C.B., Thompson C.E.,
RA   Bartholomeu D.C., Gradia D.F., Pavoni D.P., Grisard E.C.,
RA   Fantinatti-Garboggini F., Marchini F.K., Rodrigues-Luiz G.F.,
RA   Wagner G., Goldman G.H., Fietto J.L., Elias M.C., Goldman M.H.,
RA   Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and
RT   Their Respective Endosymbionts Reveals New Aspects of the
RT   Trypanosomatidae Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
RN   [2] {ECO:0000313|EMBL:EPY29539.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Motta M.C.M., Martins A.C.A., Preta C.M.C.C., Silva R., de Souza S.S.,
RA   Klein C.C., de Almeida L.G.P., Cunha O.L., Colabardini A.C.,
RA   Lima B.A., Machado C.R., Soares C.M.A., de Menezes C.B.A.,
RA   Bartolomeu D.C., Grisard E.C., Fantinatti-Garboggini F.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L.R.,
RA   Ciapina L.P., Brocchi M., Elias M.C., Goldman M.H.S., Sagot M.-F.,
RA   Pereira M., Stoco P.H., Teixeira S.M.R., de Mendonca-Neto R.P.,
RA   Maciel T.E.F., Mendes T.A.O., Urmenyi T.P., Teixeira M.M.G.,
RA   de Camargo E.F.P., de Sousa W., Schenkman S., de Vasconcelos A.T.R.;
RL   Submitted (MAR-2013) 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:EPY29539.1}.
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DR   EMBL; ATMH01004482; EPY29539.1; -; Genomic_DNA.
DR   EMBL; ATMH01003105; EPY31918.1; -; Genomic_DNA.
DR   EnsemblProtists; EPY29539; EPY29539; STCU_04482.
DR   EnsemblProtists; EPY31918; EPY31918; STCU_03105.
DR   OrthoDB; 1353361at2759; -.
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       30    111       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      120    219       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        54     54       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       104    104       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       191    191       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   226 AA;  25465 MW;  401E4B51EE480162 CRC64;
     MFRVLSKATA RVAAPAMCFT SLPSLTYPAE LPKLSFDYKD GVAPVFSPRQ IELHYTKHHK
     SYVDKLNTIG AGFEGKTIEE IILATDGKVD KKVMFNQAAQ HFNHSFYWNC ICPGGKAIPK
     ELESAIAKAF GSVEKFKEAF QAAGANNFGS GWTWLCIDPK TNALVIDNTS NAGCPLTANL
     RPILTVDVWE HAYYKDFENR RPDYLNDFWK IVNWEYVAQQ YAHVSK
//
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