ID W6JNN3_ATHRO Unreviewed; 494 AA. AC W6JNN3; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 02-JUN-2021, entry version 18. DE RecName: Full=Protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064}; DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064}; GN Name=cdc25 {ECO:0000313|EMBL:BAO51656.1}; OS Athalia rosae (Turnip sawfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Tenthredinoidea; Tenthredinidae; OC Allantinae; Athalia. OX NCBI_TaxID=37344 {ECO:0000313|EMBL:BAO51656.1}; RN [1] {ECO:0000313|EMBL:BAO51656.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Whole body {ECO:0000313|EMBL:BAO51656.1}; RA Sekine K., Hatakeyma M.; RT "The boule gene is required for spermatogenesis in the haploid male of the RT sawfly, Athalia rosae."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000256|ARBA:ARBA00001490}; CC -!- SIMILARITY: Belongs to the MPI phosphatase family. CC {ECO:0000256|ARBA:ARBA00011065}. 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; AB910531; BAO51656.1; -; Genomic_DNA. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro. DR CDD; cd01530; Cdc25; 1. DR Gene3D; 3.40.250.10; -; 1. DR InterPro; IPR000751; MPI_Phosphatase. DR InterPro; IPR001763; Rhodanese-like_dom. DR InterPro; IPR036873; Rhodanese-like_dom_sf. DR Pfam; PF00581; Rhodanese; 1. DR PRINTS; PR00716; MPIPHPHTASE. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:BAO51656.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}. FT DOMAIN 334..447 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT REGION 1..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 87..127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 159..195 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 209..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..43 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 112..126 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..236 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 494 AA; 55587 MW; 9462D396260E859B CRC64; MASRRLSSPE NVLTPSSTDK ENGVVSSPIS FNTSPQKFST LRSMKSRVPL EDCDPNSQDS GYGASYPDKD DVKCQDPFRF AEPLGVAPRR LSVESRSPLR SPLRSPVRSN RPPLFRSLSS GSESMDDGFT ELIDMDTLDD NTQLPSGLSS LLSGQIVSNK SMECEPTTPE TRTKPSFRRS LSLQNENITP QSSRVRSCLF RSPNAISSTS RLSYNDSPRL VSSPVSPPPK SFKRPEPPSD ASPVLVKRCR KSNSLQDICE QTSPKKPTLQ RCFSETEAHA HIKSAIHRST TDADLTGDFS KQCVLPLAEG QHEDLKSISA STLAALIRGE FNDSVRSYKI VDCRYPYEFE GGHVNGALNL FNKDMIEQEL LAPLKNVPEI HSDNEKRDII VFHCEFSWER GPNLSRFLRN IDRQRNKEHY PALHYPEVYL LHGGYQQFYL EEQSLCSPCG YRPMRHPDHE ADLRQFRSKS KSWQGDKSRL NGFTARANLK RLGL //