PTP_NPVAC
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 03-AUG-2022, entry version 102.
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.
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}.
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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 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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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
