ID Q1J1V2_DEIGD Unreviewed; 348 AA. AC Q1J1V2; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Dgeo_0229 {ECO:0000313|EMBL:ABF44532.1}; OS Deinococcus geothermalis (strain DSM 11300 / AG-3a). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF44532.1, ECO:0000313|Proteomes:UP000002431}; RN [1] {ECO:0000313|Proteomes:UP000002431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.; RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001512}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001482}; 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; CP000359; ABF44532.1; -; Genomic_DNA. DR RefSeq; WP_011529379.1; NC_008025.1. DR AlphaFoldDB; Q1J1V2; -. DR STRING; 319795.Dgeo_0229; -. DR KEGG; dge:Dgeo_0229; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_0_2_0; -. DR Proteomes; UP000002431; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002431}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276..294 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 300..319 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 9..241 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT REGION 323..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 348 AA; 37403 MW; F3ED3C006F60E38F CRC64; MCAAPPLLSA GLLTDVGRQR RLNQDAVLAL DLPQGGLYAV ADGMGGHAAG ELAANLALDA LSQHYLEGRG SPPERLAEAV QAANLAVLQH AVGEYVGMGT TLLALLIDRG AALLAHVGDS RAYLLRAGKL QRLTEDHSWV AEQVRLGNLT EAEAQNHHWR SVISNGLGAE KNVRLELFGL PLRAGDRLLL CSDGLSGVVG ESTLLELLAR SLPPERTVRE LINAANEAGG PDNITAVVVD ILRDQRLPHY PLPVRRSDGP MDVQTLLRAQ RRSRPLTYVL LILAYFTLLG VMLIPEHRTL VALLGTLLLI GVTITQRLAR ARLRRSAPPR SPGRAASPPD RDPRETPG //