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Database: UniProt
Entry: S9VVK9_9TRYP
LinkDB: S9VVK9_9TRYP
Original site: S9VVK9_9TRYP 
ID   S9VVK9_9TRYP            Unreviewed;       236 AA.
AC   S9VVK9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=STCU_05770 {ECO:0000313|EMBL:EPY27400.1}, STCU_12402
GN   {ECO:0000313|EMBL:EPY14969.1};
OS   Strigomonas culicis.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY27400.1};
RN   [1] {ECO:0000313|EMBL:EPY27400.1}
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:EPY27400.1}
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:EPY27400.1}.
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DR   EMBL; ATMH01012758; EPY14969.1; -; Genomic_DNA.
DR   EMBL; ATMH01005770; EPY27400.1; -; Genomic_DNA.
DR   EnsemblProtists; EPY14969; EPY14969; STCU_12402.
DR   EnsemblProtists; EPY27400; EPY27400; STCU_05770.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    236       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007727273.
FT   DOMAIN       44    124       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      132    234       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        69     69       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       117    117       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       202    202       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       206    206       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   236 AA;  26352 MW;  8B2B9121326E448F CRC64;
     MTRHISSLSL SLSLSLSLSR CFYDLRFVFI SSLPSILTQP TMPFTVDPLP WAYDALAAKG
     ISKEQISFHY DKHHKGYATK LNAAAEQNAE LAAKTIEEII KTVTGPAFNS AAQIFNHNFY
     WKSLCPNGGG APSGKIAEAI AKDFGSFEKF KEEFTAAANG HFGSGWAWLV KDTTSQKLKI
     FQTHDAGCVL TEANLKPIIC CDVWEHAYYI DYKNDRAAYV NTWWNVVNWS HAESQL
//
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