ID   DUSP_FOWPN              Reviewed;         166 AA.
AC   Q9J592;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable dual specificity protein phosphatase H1 homolog;
DE            EC=3.1.3.-;
DE            EC=3.1.3.48;
GN   OrderedLocusNames=FPV138;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; AF198100; AAF44482.1; -; Genomic_DNA.
DR   RefSeq; NP_039101.1; NC_002188.1.
DR   SMR; Q9J592; -.
DR   GeneID; 1486686; -.
DR   KEGG; vg:1486686; -.
DR   Proteomes; UP000008597; Genome.
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   Reference proteome; Viral immunoevasion; Virion.
FT   CHAIN           1..166
FT                   /note="Probable dual specificity protein phosphatase H1
FT                   homolog"
FT                   /id="PRO_0000094870"
FT   DOMAIN          25..166
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        108
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   166 AA;  19637 MW;  D98A7C95DAB29BD6 CRC64;
     MDEKQLYKHI ITKSTNTCVK FTPRDITKIT DYVYLGNYRN VIELPNKTFF KYIVNVSMLK
     YKLKRTDITV LHFPLEDNDT VSISKHIDAV TYVLKKCESL KIPVLVHCMA GINRSSAMIM
     GYLMEIRDKN IPFVIYFLYI YHELKYIRGA FIENKSFLNQ IIDKYI