ID A0A0S7DKJ2_9EURO Unreviewed; 435 AA. AC A0A0S7DKJ2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-OCT-2020, entry version 17. DE RecName: Full=Protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064}; DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064}; GN ORFNames=ALT_0645 {ECO:0000313|EMBL:GAQ03324.1}; OS Aspergillus lentulus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ03324.1, ECO:0000313|Proteomes:UP000051487}; RN [1] {ECO:0000313|EMBL:GAQ03324.1, ECO:0000313|Proteomes:UP000051487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ03324.1, RC ECO:0000313|Proteomes:UP000051487}; RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.; RT "Aspergillus lentulus strain IFM 54703T."; RL Submitted (NOV-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GAQ03324.1}. 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; BCLY01000001; GAQ03324.1; -; Genomic_DNA. DR EnsemblFungi; GAQ03324; GAQ03324; ALT_0645. DR OrthoDB; 1423329at2759; -. DR Proteomes; UP000051487; Unassembled WGS sequence. 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}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}; KW Reference proteome {ECO:0000313|Proteomes:UP000051487}. FT DOMAIN 249..352 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT REGION 20..175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 390..435 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 52..66 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..115 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 123..164 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 390..413 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 435 AA; 48839 MW; DCD201B29716632B CRC64; METMDMSPLP HKPPFIVTTE IELNPPTPGG SPIDSPMMSA APSPLQESPL MGPKEDKQER KRPSFLRPSL ARTKAQSFQL GMARPAPESQ APPFKFQTRG AKTSLSASTS LEDMFGESPQ RERPIVRNNS STLLNNPRLR PPLGSGSNGS HARGNGSPSA ASIRKSSHPL MRPRKQCRRS LSMFEHPEDV IAEKEANYTT NAPLQSITDV DTTPSLQLPH FIPEDSADTL PRIDKTILVD LMDGKYNDRF DHIMVVDCRF EYEYEGGHIN GAVNYNDKEY LAAQLFADPK PRTALVLHCE YSAHRAPIMA KYIRHRDRAV NVDHYPQLTY PDMYILDGGY SAFFAEHRSL CFPQNYVEMN AKEHEFACER GLGKVKQRSK LNRAQTFAFG QHSPQMEDSP TGRCRNNSGE RTRFLDSPFE GTPSSRGPGR RMLSY //