ID A0A075CH78_9POXV Unreviewed; 171 AA. AC A0A075CH78; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-APR-2021, entry version 17. DE SubName: Full=Protein phosphatase {ECO:0000313|EMBL:AGZ95387.1}; GN Name=GTPV068 {ECO:0000313|EMBL:AGZ95387.1}; OS Goatpox virus FZ. OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Capripoxvirus. OX NCBI_TaxID=1416740 {ECO:0000313|EMBL:AGZ95387.1, ECO:0000313|Proteomes:UP000134642}; RN [1] {ECO:0000313|EMBL:AGZ95387.1, ECO:0000313|Proteomes:UP000134642} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FZ {ECO:0000313|EMBL:AGZ95387.1}; RX PubMed=25113672; DOI=10.1016/j.vetmic.2014.07.013; RA Zeng X., Chi X., Li W., Hao W., Li M., Huang X., Huang Y., Rock D.L., RA Luo S., Wang S.; RT "Complete genome sequence analysis of goatpox virus isolated from China RT shows high variation."; RL Vet. Microbiol. 173:38-49(2014). 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:0000256|ARBA:ARBA00001119}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. 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; KC951854; AGZ95387.1; -; Genomic_DNA. DR Proteomes; UP000134642; Genome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:0039563; P:suppression by virus of host 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; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. 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 4: Predicted; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961}; KW Late protein {ECO:0000256|ARBA:ARBA00022921}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}. FT DOMAIN 26..165 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000259|PROSITE:PS50054" FT DOMAIN 86..161 FT /note="TYR_PHOSPHATASE_2" FT /evidence="ECO:0000259|PROSITE:PS50056" SQ SEQUENCE 171 AA; 19951 MW; BBA141421FD3137B CRC64; MDKKSLYENV LLKSTGSLPK AKAPSKMMRV TDYVYLGNYD DAINAISSNV NFKYILNLTT EKYCFNDSRI NIIHMPLIDD EKTNLNDHFD YVTKFLSKCD EEHYPVLVHC VAGVNRSGAM IMAYLMSKRS KDIPAFIYFL YIYHSMREKR GAFIENPSFR KQLIDKYIIN E //