ID Q584E1_TRYB2 Unreviewed; 1286 AA.
AC Q584E1; D6XFI2;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE SubName: Full=Dual specificity protein phosphatase, putative {ECO:0000313|EMBL:AAX79064.1};
DE EC=3.1.3.48 {ECO:0000313|EMBL:AAX79064.1};
GN Name=Tb04.1H19.900 {ECO:0000313|EMBL:AAZ10837.1};
GN ORFNames=Tb927.4.2460 {ECO:0000313|EMBL:AAX79064.1};
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:AAX79064.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:AAX79064.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX79064.1};
RA El-Sayed N.M., Khalak H., Adams M.D.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAZ10837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10837.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [3] {ECO:0000313|EMBL:AAZ10837.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10837.1,
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).
RN [4] {ECO:0000313|EMBL:AAX79064.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX79064.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT ".";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AAZ10837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10837.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT "Sequencing, closure, and annotation of Trypanosoma brucei chromosomes 2
RT through 8.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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; AC079933; AAX79064.1; -; Genomic_DNA.
DR EMBL; CP000067; AAZ10837.1; -; Genomic_DNA.
DR RefSeq; XP_844396.1; XM_839303.1.
DR AlphaFoldDB; Q584E1; -.
DR STRING; 185431.Q584E1; -.
DR PaxDb; 5691-AAZ10837; -.
DR GeneID; 3656773; -.
DR KEGG; tbr:Tb927.4.2460; -.
DR VEuPathDB; TriTrypDB:Tb927.4.2460; -.
DR eggNOG; KOG0201; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; Q584E1; -.
DR OMA; VICIPDF; -.
DR OrthoDB; 168359at2759; -.
DR Proteomes; UP000008524; Chromosome 4.
DR GO; GO:0005929; C:cilium; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0004672; F:protein kinase activity; IEA:InterPro.
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 CDD; cd00180; PKc; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF524; SPECIFICITY PROTEIN PHOSPHATASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 2.
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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAX79064.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 116..399
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 445..712
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1126..1267
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 1188..1256
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 142922 MW; BECC918FEF2C22EC CRC64;
MGACIAALRG KVAGKTNDSH GISDQSLPTA ESTDDSVNNR NGKFNKCIRG EESISSGDMH
GKEGSDLSKS LTSLWGVLSK TEFADFFRAH PELLKSNSAA VMCTGAFRPG ELVGAYCVVK
ELPGGTVGRS FLVKAVDDSG PPTPTVTTPE VEDSGKREFV FKVMTFINRK NLVEPVLDDK
RALMNLTGDG LLRPVHLLLD EGNETVISVT PFLKEGSCAR LAGKLEEDRL LSILRDVASA
LRLLHSHNIY HCNLKLENVL LREDGKACLA DAALWRIFST QSRDCLLFNG ELACMPPEMF
MIDEADNQSK DASKVDIWGF GLFMYRLAYG REPFDIEGKA LEQVCELVSV DRLQFPQRNW
SIASSLEDAI RVCLDDDPER RPTVPGLFSF SLFRNHNFNS VVAGGSVGLP GFRASHNDTG
PSGGRSGSDN YIRWAYPRYH WRKNVSLDEM LGSGGICETY RVHLRRHPSK QFVMKVLKRS
VLKAASQYRI STDDLRHALA VSRLINHPNV LNLLEIVDSR DGCFASQQLA KSRFLYAEFP
PLLNHKNPLF TLKQMLADVL QGLFVLHLNG VPHLRLTPSN IFYELGVGFR VSDFGPLFLA
REEIVESMET DQPLYSVPQW VVDDLKVPIH MSRFSLDVFC VGLLAASALP SVLHEDWYRF
SNSEGCILDV KGVCEKVKNA SLYLKPMLVD FILQALTNPA TTVRDLMNHS YLSDAIDVSR
LDEMKPLNIS PADMEMAVSE RFTTTDESGL WNVLGHDPAA GNGHLWCSMF RNEALPDGCI
RSGIQSVNEV AAARRVPFVK KLVCGLCRCE LPIVLFLCDK CDDYIRCAKC SLVDTHADDH
KLSPHLVHTV GQDGVDGNFF ALLVPTCNIC VAQSLEALEM QANLPHGTLT KDITTQSVTA
ERALRRLTLA KLNPGPKVLP KVSDTEGETW EEEVASCRET RNTELLLHQF ELNTVPKELF
DPPLLHVASI DLSYNKLTSL PDDLALLCNL RSVSVAHNAL TVLPDSMGEL RQLDRLDASH
NKLKDLPLTF VKLRKLSTVT LDFNEFSGLP RVLDDLIVAT ASTPQLSTIY LAENTNITRF
PDYTNLAILP TLKLALDNEP SVYQTYLNEN LAEKLPNIGM LWNKIYPDRI VDNVFCGSLR
TTQSQVVYDK LGIKNLLTVG RDLVPVPPVG GKHLVISLDD IEEADIRCTF DEAVNFIDMS
VEKGEGCLVH CFAGLSRSAT TVIAYFMMKR GMRLGDAYQL TKRGRPSIYP NEGFFRQMIE
LDGELFPDDP PLQLEDIGRE SPNVRV
//
