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   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable dual specificity protein phosphatase H1 homolog;
DE            EC=3.1.3.-;
DE            EC=3.1.3.48;
GN   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 STAT1 and blocking
CC       interferon (IFN)-stimulated innate immune responses. {ECO:0000250}.
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   -!- 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;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=Approximately 200 molecules of H1 are packaged
CC       within the virion and are essential for the viability of the virus.
CC       {ECO:0000250}.
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   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0039563; P:suppression 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   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; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 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   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; Late protein; Protein phosphatase;
KW   Viral immunoevasion; Virion.
FT   CHAIN           1..171
FT                   /note="Probable dual specificity protein phosphatase H1
FT                   homolog"
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