GenomeNet

Database: UniProt
Entry: Q381T3_TRYB2
LinkDB: Q381T3_TRYB2
Original site: Q381T3_TRYB2 
ID   Q381T3_TRYB2            Unreviewed;       208 AA.
AC   Q381T3;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   05-DEC-2018, entry version 71.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Tb11.01.6660 {ECO:0000313|EMBL:EAN80448.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:EAN80448.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN80448.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B.,
RA   Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L.,
RA   Wickstead B., Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J.,
RA   Bringaud F., Brooks K., Carrington M., Cherevach I.,
RA   Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A.,
RA   Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C.,
RA   Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H.,
RA   Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K.,
RA   Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V.,
RA   Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M.,
RA   Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E.,
RA   Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S.,
RA   Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A.,
RA   Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B.,
RA   White O., Whitehead S., Woodward J., Wortman J., Adams M.D.,
RA   Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H.,
RA   Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M.,
RA   Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CH464491; EAN80448.1; -; Genomic_DNA.
DR   RefSeq; XP_829560.1; XM_824467.1.
DR   ProteinModelPortal; Q381T3; -.
DR   STRING; 5691.EAN80448; -.
DR   PaxDb; Q381T3; -.
DR   GeneDB; Tb927.11.15020:pep; -.
DR   GeneID; 3665380; -.
DR   KEGG; tbr:Tb11.01.6660; -.
DR   EuPathDB; TriTrypDB:Tb927.11.15020; -.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; Q381T3; -.
DR   KO; K04564; -.
DR   Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR   GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR   GO; GO:0046872; F:metal ion binding; ISM:GeneDB.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISM:GeneDB.
DR   GO; GO:0006801; P:superoxide metabolic process; ISM:GeneDB.
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:UP000008524};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:EAN80448.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524}.
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;  23280 MW;  1E3839F08611BC01 CRC64;
     MAFSIPPLPW GYDGLAAKGI SKEQVTFHYD KHHMGYVTKL NAAAKSNPAL AAKSVEEIIR
     TEKGPIFNLA AQIFNHNFYW ESMSPNGGGE PSGKLAEAIR ASFGSFAKFK EEFTNAAVGH
     FGSGWAWLVQ DTTTKKLKVF QTHDAGCPLT EADLKPILAC DVWEHAYYID YKNDRPAYVQ
     TFWNVVNWDH AENQFTRKRN PGAPHSDL
//
DBGET integrated database retrieval system