ID A0A158R9M8_TAEAS Unreviewed; 932 AA.
AC A0A158R9M8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=TASK_LOCUS7495 {ECO:0000313|EMBL:VDK38478.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000749401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000749401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK38478.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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DR EMBL; UYRS01018626; VDK38478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158R9M8; -.
DR STRING; 60517.A0A158R9M8; -.
DR WBParaSite; TASK_0000749401-mRNA-1; TASK_0000749401-mRNA-1; TASK_0000749401.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
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; PTHR23339:SF27; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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 Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT DOMAIN 168..325
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 250..312
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 382..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 103380 MW; CC13A78A548FB489 CRC64;
MYLSTKSLSI DFIFNLFYLL RFYDDFGPFN LAQVYKYCRK VNKKLKASAL SNNRIVHCTS
TEITKRTNAA FLVGCYQIIY LNRSADEAYK HLLLEKYRTF APYRDASSGP SYYDLDLSDC
LRAVQKAVRF GFLDFDNFDL EDYEYNEPTN LLSHSSIIIP LQKVENGDLS WIVPNKFIAF
SGPHTRTMID NGYPMHAPEF YLPYFRKNNV TNVIRLNQKM YESHRFTRAG IAHHELFFPD
GTVPTKAITL QFLDICETAP GAIAVHCKAG LGRTGTLIGC YLMKHYHFTA PEAIAWIRIC
RPGSIIGQQQ NWLEEQQTWC WEEGRRERRE KSPSPLPSRR RKDLIDADVA ANHLSRPIGK
VIYINTDPLK LPTQLRDDPV LRFAGLDNDG DTSQTPLSTT SSTNDQVEVL ISSRPRVYHH
KVQIAGRSQS PPAYGTGGEE SNESNEPRYS PGPSREINGA RMGLGMASSR SMDLSQKPST
YKATFTQGDQ LNRIKVIRKR NKQRKDGTGK DVNIPSTTQH LASSYPRAAL SGSVGEESGS
ALDFREIYNL HDEVTEDGST TVESSDVEAY NRFRYGSGGS QLPSMFYHNV TSSPPNDSKD
RVGIPNGDSI DIQPSMTATL SSRDSLRSSY PRTLTPVNLA PAAVTARTPS ESNVRALRGR
GITTRGRENQ CETKGGVTGG AGISRSNIGM GLPRTGITTT LPISASCVSH QNSRMPTVTR
APPQKVSANR DGHALLCVNY PEVPESSSPS SITTPTTAAV AAGVAARKRV EFAPPPPPPP
PPPPPPLPIL LTSNSLPTSK IRSTADTFYQ RLYHTNNNGR NSNADSNVTN NEVDEKGYYL
RPYRNLRNHN NGDFTVIKYN STNAHTINGR NNGSRGPSPS PLLNSNQIGR HHVRSSSLKP
HAPPISISPV VYADIQTNSP PEFDYRPRAS VR
//
