ID Q4CXG5_TRYCC Unreviewed; 820 AA.
AC Q4CXG5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Dual specificity protein phosphatase, putative {ECO:0000313|EMBL:EAN84969.1};
GN ORFNames=Tc00.1047053504175.40 {ECO:0000313|EMBL:EAN84969.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN84969.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN84969.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN84969.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAN84969.1}.
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DR EMBL; AAHK01001538; EAN84969.1; -; Genomic_DNA.
DR RefSeq; XP_806820.1; XM_801727.1.
DR AlphaFoldDB; Q4CXG5; -.
DR STRING; 353153.Q4CXG5; -.
DR PaxDb; 353153-Q4CXG5; -.
DR EnsemblProtists; EAN84969; EAN84969; Tc00.1047053504175.40.
DR GeneID; 3536938; -.
DR KEGG; tcr:504175.40; -.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; Q4CXG5; -.
DR OrthoDB; 132836at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14498; DSP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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:SF538; SPECIFICITY PROTEIN PHOSPHATASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
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};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296}.
FT DOMAIN 562..748
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 666..700
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 88441 MW; EE63A5DA43901DCF CRC64;
MSLMPADGGE GVGPPGDGNQ QQQQQPPRPQ QQRCCNKQKN REEEGENCEE EETCPLEAFG
SAPASNTSTD VSGAQGLTAC KEEGSGDMTA TTTTTTKTAA VVKVVDTNAG RSQQNGIVVP
ARSGVTEYTC SGRSSSSSVG SSAHVSPSRF VVGSTRHISL TTKPPAPGNG ARVSSGSLSN
SQMQAVIKFV SCRASGDKKQ NATQTSVPVG QSPLQTPGND TSANTERASV DVTPMPTLSL
PLQGQSSKGQ MASLSAIDLP LPHVSLRQCT STPLVPNTVG TQPHSCYEKE EERDYFLQKV
TPQLHRMLPL WRKNFGNEMV TEEGMTVTTT TTTTTTEAET EAECQQEQWQ EKILSENDVS
DRRLRQRLPE ASSRLHIRLP ASPMCNAANS AYNPGSSDFD VSVSSSSSSS RTLSTLQASS
HHFVRSVCHV LTGTPTFSSC NVGPEENETE KTFGTSKAQT TTTTTTTTTT TTKATTMTID
GGGGSNSSNS RSDGFVLTSH EQNDCICGVQ AIGIDAPVEF VQENSTRQFL TKNGNRSGVF
TPSPLPPLPP LSHGACSSYS LDAAMVLPGL FLGSYSDALK IDALAAHGIS LVINVAEECV
MMETMIYNDY DIKFIKFPLK DHSDENITRY FGPITRIIHR QLHRRERALR SSRKAATGNI
RSYDDEEVMS ISSKSVGGGV LVHCRMGVSR SAAIILAYLM IYGETLWVDD NCSIQNQHIE
EESFTPIFTP PNVSPISTLL LDGSDVEKEN HSTNGKCCEC CCCLAIQNPH ITCNTDGVYK
PSVVKSYRDA FEFLKKRKKD INPNIGFVLA LRELDDREGK
//
