ID PTPH_MIMIV Reviewed; 212 AA.
AC Q5UR74;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Putative tyrosine-protein phosphatase R622;
DE EC=3.1.3.48;
GN OrderedLocusNames=MIMI_R622;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC Mimivirus bradfordmassiliense.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
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. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AY653733; AAV50883.1; -; Genomic_DNA.
DR RefSeq; YP_003987139.1; NC_014649.1.
DR SMR; Q5UR74; -.
DR GeneID; 9925263; -.
DR KEGG; vg:9925263; -.
DR OrthoDB; 12612at10239; -.
DR Proteomes; UP000001134; Genome.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14498; DSP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45948; DUAL SPECIFICITY PROTEIN PHOSPHATASE DDB_G0269404-RELATED; 1.
DR PANTHER; PTHR45948:SF2; DUAL SPECIFICITY PROTEIN PHOSPHATASE DDB_G0269404-RELATED; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..212
FT /note="Putative tyrosine-protein phosphatase R622"
FT /id="PRO_0000253995"
FT DOMAIN 9..191
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 135
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 212 AA; 24840 MW; BD8CC7E8DEF67BD8 CRC64;
MNFHPELSKI SQVTNNIFLS GVFPMEQDPT VIKKLNIKYI LACLDRQYVS DAHNAVLIDN
PECTILYLPY DDDVSQNLWC KNKNTINLVK YTRTMEEYNC LYKQFQMYQN KPMIEIGYHF
INNAVESGNN ILIHCMAGIS RSVSTLTYYL MKKYNIPYSQ AIKYVKDRRS IVNPNDSFKL
QLQGYQSKKE NFIESDGKKV TDFFKYGQSR LK
//
