ID PTP_NPVAC Reviewed; 168 AA. AC P24656; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 27-MAR-2024, entry version 107. DE RecName: Full=Tyrosine-protein phosphatase; DE EC=3.1.3.48; DE AltName: Full=BVP; GN Name=PTP; ORFNames=ORF1; OS Autographa californica nuclear polyhedrosis virus (AcMNPV). OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus; OC Alphabaculovirus aucalifornicae. OX NCBI_TaxID=46015; OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1993873; DOI=10.1099/0022-1317-72-2-285; RA Tilakaratne N., Hardin S.E., Weaver R.F.; RT "Nucleotide sequence and transcript mapping of the HindIII F region of the RT Autographa californica nuclear polyhedrosis virus genome."; RL J. Gen. Virol. 72:285-291(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C6; RX PubMed=1926775; DOI=10.1016/0042-6822(91)90770-c; RA Possee R.D., Sun T.P., Howard S.C., Ayres M.D., Hill-Perkins M., RA Gearing K.L.; RT "Nucleotide sequence of the Autographa californica nuclear polyhedrosis 9.4 RT kbp EcoRI-I and -R (polyhedrin gene) region."; RL Virology 185:229-241(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C6; RX PubMed=8030224; DOI=10.1006/viro.1994.1380; RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.; RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis RT virus."; RL Virology 202:586-605(1994). RN [4] RP CHARACTERIZATION. RX PubMed=8444848; DOI=10.1016/s0021-9258(18)53457-8; RA Sheng Z., Charbonneau H.; RT "The baculovirus Autographa californica encodes a protein tyrosine RT phosphatase."; RL J. Biol. Chem. 268:4728-4733(1993). RN [5] RP FUNCTION, AND MUTAGENESIS OF CYS-119. RX PubMed=9707557; DOI=10.1073/pnas.95.17.9808; RA Takagi T., Taylor G.S., Kusakabe T., Charbonneau H., Buratowski S.; RT "A protein tyrosine phosphatase-like protein from baculovirus has RNA 5'- RT triphosphatase and diphosphatase activities."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9808-9812(1998). RN [6] RP FUNCTION. RX PubMed=18385232; DOI=10.1128/jvi.00058-08; RA Li Y., Guarino L.A.; RT "Roles of LEF-4 and PTP/BVP RNA triphosphatases in processing of RT baculovirus late mRNAs."; RL J. Virol. 82:5573-5583(2008). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), AND MUTAGENESIS OF ASN-124. RX PubMed=15713658; DOI=10.1074/jbc.m500885200; RA Changela A., Martins A., Shuman S., Mondragon A.; RT "Crystal structure of baculovirus RNA triphosphatase complexed with RT phosphate."; RL J. Biol. Chem. 280:17848-17856(2005). CC -!- FUNCTION: Plays a role in the regulation and processing of late viral CC mRNAs by displaying RNA 5'-triphosphatase and diphosphatase activities. CC {ECO:0000269|PubMed:18385232, ECO:0000269|PubMed:9707557}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- MISCELLANEOUS: Probably expressed late in infection. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class CDC14 subfamily. {ECO:0000305}. 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; L22858; AAA66631.1; -; Genomic_DNA. DR EMBL; M96763; AAA46753.1; -; Genomic_DNA. DR EMBL; M75679; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A40781; A40781. DR RefSeq; NP_054030.1; NC_001623.1. DR PDB; 1YN9; X-ray; 1.50 A; A/B/C=1-168. DR PDBsum; 1YN9; -. DR SMR; P24656; -. DR GeneID; 1403833; -. DR KEGG; vg:1403833; -. DR OrthoDB; 10871at10239; -. DR EvolutionaryTrace; P24656; -. DR Proteomes; UP000008292; Genome. 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:0016311; P:dephosphorylation; IEA:InterPro. DR CDD; cd17665; DSP_DUSP11; 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; PTHR10367; MRNA-CAPPING ENZYME; 1. DR PANTHER; PTHR10367:SF9; RNA_RNP COMPLEX-1-INTERACTING PHOSPHATASE; 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Late protein; Protein phosphatase; KW Reference proteome. FT CHAIN 1..168 FT /note="Tyrosine-protein phosphatase" FT /id="PRO_0000094881" FT DOMAIN 24..168 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 119 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT SITE 124 FT /note="Essential for RNA triphosphatase activity" FT /evidence="ECO:0000269|PubMed:15713658" FT MUTAGEN 119 FT /note="C->S: Loss of activity." FT /evidence="ECO:0000269|PubMed:9707557" FT MUTAGEN 124 FT /note="N->A: Abolishes triphosphatase activity." FT /evidence="ECO:0000269|PubMed:15713658" FT MUTAGEN 124 FT /note="N->D: Abolishes triphosphatase activity." FT /evidence="ECO:0000269|PubMed:15713658" FT MUTAGEN 124 FT /note="N->Q: Abolishes triphosphatase activity." FT /evidence="ECO:0000269|PubMed:15713658" FT CONFLICT 49 FT /note="V -> I (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 167..168 FT /note="LI -> F (in Ref. 1)" FT /evidence="ECO:0000305" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:1YN9" FT STRAND 19..24 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 30..33 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 45..51 FT /evidence="ECO:0007829|PDB:1YN9" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:1YN9" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:1YN9" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 93..109 FT /evidence="ECO:0007829|PDB:1YN9" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:1YN9" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 124..138 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 142..153 FT /evidence="ECO:0007829|PDB:1YN9" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:1YN9" SQ SEQUENCE 168 AA; 19288 MW; 2D4D85F11C52AB09 CRC64; MFPARWHNYL QCGQVIKDSN LICFKTPLRP ELFAYVTSEE DVWTAEQIVK QNPSIGAIID LTNTSKYYDG VHFLRAGLLY KKIQVPGQTL PPESIVQEFI DTVKEFTEKC PGMLVGVHCT HGINRTGYMV CRYLMHTLGI APQEAIDRFE KARGHKIERQ NYVQDLLI //