ID Q384T3_TRYB2 Unreviewed; 414 AA.
AC Q384T3;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Phopshatase, putative {ECO:0000313|EMBL:EAN79698.1};
GN ORFNames=Tb11.02.5220 {ECO:0000313|EMBL:EAN79698.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN79698.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:EAN79698.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN79698.1,
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., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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DR EMBL; CH464491; EAN79698.1; -; Genomic_DNA.
DR RefSeq; XP_828810.1; XM_823717.1.
DR AlphaFoldDB; Q384T3; -.
DR STRING; 185431.Q384T3; -.
DR PaxDb; 5691-EAN79698; -.
DR GeneID; 3665557; -.
DR KEGG; tbr:Tb11.02.5220; -.
DR VEuPathDB; TriTrypDB:Tb11.v5.0251; -.
DR VEuPathDB; TriTrypDB:Tb927.11.7320; -.
DR eggNOG; KOG1717; Eukaryota.
DR InParanoid; Q384T3; -.
DR OrthoDB; 3035478at2759; -.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0005929; C:cilium; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISM:GeneDB.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISM:GeneDB.
DR CDD; cd14498; DSP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF532; PUTATIVE-RELATED; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 268..409
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 329..389
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 414 AA; 46629 MW; 2392F67CC11346E5 CRC64;
MSRLLSPSVA LSVENGFADI GEFCASSPDT SSSVSESLAS AELPQLHQQH KLGGVDLNEV
ADELEEELVL CLSTGYCNLS QMGFVTTPAN IPYESLVTLL LSGNQIKEIS ESLFTNGNFQ
FLCKLDLSSN CLESVPKSLF KLMKLEVLLL DHNNITRLPV SVDEQIGSQL LPALQRIGLE
FNDLSRFPIE LFKHCPSLEA VYLSQNLRML NEPVSVKQLL QAAAVESSKE NHRVLLKVDN
KPVFVQQMYD EKWDEVLPWL DVELHKIYPD KVLSFLYLGS LRTAQTPLVY RDLDIGFILS
AGRNMTVHVE SGMRHLVLPI DDHPGEKLRP IFDMAFNFID DAREEGKGVL LHCFAGLSRS
VTIAVAYLMS RYNYKRDEAI EMIRRVRPSS QPNSGFMDIL AQYEQELNNQ KHHM
//
