ID   PTPN1_MDBVW             Reviewed;         318 AA.
AC   Q5I128;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Probable tyrosine phosphatase protein N1;
DE            Short=PTP-N1;
DE            EC=3.1.3.48;
GN   Name=N3;
OS   Microplitis demolitor bracovirus (isolate Webb) (MdBV).
OC   Viruses; Polydnaviriformidae; Bracoviriform;
OC   Microplitis demolitor bracovirus.
OX   NCBI_TaxID=654919;
OH   NCBI_TaxID=69319; Microplitis demolitor (Parasitoid wasp).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16061795; DOI=10.1073/pnas.0505240102;
RA   Thoetkiattikul H., Beck M.H., Strand M.R.;
RT   "Inhibitor kappaB-like proteins from a polydnavirus inhibit NF-kappaB
RT   activation and suppress the insect immune response.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11426-11431(2005).
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AY875689; AAW51807.1; -; Genomic_DNA.
DR   RefSeq; YP_239400.1; NC_007039.1.
DR   SMR; Q5I128; -.
DR   GeneID; 5075833; -.
DR   KEGG; vg:5075833; -.
DR   Proteomes; UP000008168; Genome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134:SF544; LD27988P; 1.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Probable tyrosine phosphatase protein N1"
FT                   /id="PRO_0000405373"
FT   DOMAIN          26..292
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        233
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   318 AA;  37071 MW;  0B1B9C6FECC4C9C0 CRC64;
     MVVNCFETCR AIDFWNRRNQ LNFPGIVRLE HHQVILKPFN GTWENSEKPE NQRKNRYNIR
     CWDHNRVILK SGSGSTSNYI HANYVDGFED DKKFIITQGP MEETCNDFWK AVWQNNCSII
     VMLTPTKGTN GEELCYQYWS LNEDSNIITE DFVIETVNTS VRPTYILTTL RITDKISNDS
     RRISHYQYTE WPVDETPTNH VDFIKFIKII NINRKKSGSN YQQQLLSPIV VHCSDGVKKT
     GIFCAVDISL NQLVLRKTVS LAKTAEKIRQ QRHSTISTPD DYLILQPGYY VLLYLLYKIL
     AIIKIKNCGE KKSRRKST
//