ID   PTPH3_MDBVW             Reviewed;         320 AA.
AC   Q5I145;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Tyrosine phosphatase H3;
DE            Short=PTP-H3;
DE            EC=3.1.3.48;
GN   Name=H3;
OS   Microplitis demolitor bracovirus (isolate Webb) (MdBV).
OC   Viruses; Polydnaviridae; Bracovirus.
OX   NCBI_TaxID=654919;
OH   NCBI_TaxID=69319; Microplitis demolitor.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16380146; DOI=10.1016/j.virol.2005.11.010;
RA   Webb B.A., Strand M.R., Dickey S.E., Beck M.H., Hilgarth R.S., Barney W.E.,
RA   Kadash K., Kroemer J.A., Lindstrom K.G., Rattanadechakul W., Shelby K.S.,
RA   Thoetkiattikul H., Turnbull M.W., Witherell R.A.;
RT   "Polydnavirus genomes reflect their dual roles as mutualists and
RT   pathogens.";
RL   Virology 347:160-174(2006).
RN   [2]
RP   FUNCTION.
RX   PubMed=17121799; DOI=10.1128/jvi.02189-06;
RA   Pruijssers A.J., Strand M.R.;
RT   "PTP-H2 and PTP-H3 from Microplitis demolitor Bracovirus localize to focal
RT   adhesions and are antiphagocytic in insect immune cells.";
RL   J. Virol. 81:1209-1219(2007).
CC   -!- FUNCTION: Suppresses host immune cell adhesion and phagocytosis.
CC       {ECO:0000269|PubMed:17121799}.
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AY875685; AAW51787.1; -; Genomic_DNA.
DR   RefSeq; YP_239383.1; NC_007035.1.
DR   SMR; Q5I145; -.
DR   GeneID; 5075818; -.
DR   KEGG; vg:5075818; -.
DR   Proteomes; UP000008168; Genome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 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; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus; Protein phosphatase;
KW   Reference proteome; Viral immunoevasion.
FT   CHAIN           1..320
FT                   /note="Tyrosine phosphatase H3"
FT                   /id="PRO_0000405353"
FT   DOMAIN          22..309
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        250
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
SQ   SEQUENCE   320 AA;  37219 MW;  C029D5041E9A9D23 CRC64;
     MPGYCFEIFN VFDFFDKTNK ANFWEFVRLE HAQVMDIPIS GTVNHFLKPE NLRKNRYHDV
     TCWDNSRVVL SSHGSKMYDY GDSDGKKIIV TSQDSDSTYI HASFVNGFKE ANKFICCQGP
     KESTSGDFWK MVSEHNSSVI VSLTETDDED QVCYEYWVKE EDYELAFGRY VVKTLEIIEE
     SSFTRTRLRL TDVSSDTSRE IHHFWYPHWS DYGNPTNPAE ILNLISKVNQ KRKEMKKTAD
     SQPGPIVVHC SAGIGRTGTF CTIDNALSQL RKEQTVCLPQ TVLKIRKQRH SSVFLPEQYA
     FCYKAVRYAL IREIKKKFFY