ID DUSP_RACVI Reviewed; 171 AA.
AC P80994;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Probable dual specificity protein phosphatase OPG106;
DE EC=3.1.3.-;
DE EC=3.1.3.48;
GN Name=OPG106; ORFNames=VH1;
OS Raccoon poxvirus (RCN).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=10256;
OH NCBI_TaxID=9654; Procyon lotor (Raccoon).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8387208; DOI=10.1073/pnas.90.9.4017;
RA Hakes D.J., Martell K.J., Zhao W.G., Massung R.F., Esposito J.J.,
RA Dixon J.E.;
RT "A protein phosphatase related to the vaccinia virus VH1 is encoded in the
RT genomes of several orthopoxviruses and a baculovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4017-4021(1993).
CC -!- FUNCTION: Serine/tyrosine phosphatase which down-regulates cellular
CC antiviral response by dephosphorylating activated host STAT1 and
CC blocking interferon (IFN)-stimulated innate immune responses.
CC Dephosphorylates the OPG144 protein. {ECO:0000250|UniProtKB:P07239}.
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;
CC Evidence={ECO:0000250|UniProtKB:P07239};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P07239};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07239}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P07239}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P07239}. Note=Approximately 200
CC molecules of OPG106 are packaged within the virion and are essential
CC for the viability of the virus. {ECO:0000250|UniProtKB:P07239}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; L13165; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B47452; B47452.
DR RefSeq; YP_009143407.1; NC_027213.1.
DR SMR; P80994; -.
DR GeneID; 24528129; -.
DR KEGG; vg:24528129; -.
DR OrthoDB; 12612at10239; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:RHEA.
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 GO; GO:0039563; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
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; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF519; DUAL SPECIFICITY PROTEIN PHOSPHATASE MPK3; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 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 2: Evidence at transcript level;
KW Host cytoplasm; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Interferon antiviral system evasion;
KW Late protein; Protein phosphatase; Viral immunoevasion; Virion.
FT CHAIN 1..171
FT /note="Probable dual specificity protein phosphatase
FT OPG106"
FT /id="PRO_0000094872"
FT DOMAIN 23..171
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 110
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 171 AA; 19741 MW; E03416F4988B3E81 CRC64;
MDKKSLYKYL LLRSTGDIHR AKSPTMMTRV TNNVYLGNYK NAMEAPSSEV KFKYILNLTM
DKYSFTNSNI NIIHVPMVDD TSTDISIYFD DITAFLSKCD QRNEPVLVHC AAGVNRSGAM
ILAYLMSKNK ESSPMLYFLY VYHSMRDLRG AFVENPSFKR QIIEKYVIDK N
//
