ID A6W427_KINRD Unreviewed; 463 AA. AC A6W427; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Krad_0075 {ECO:0000313|EMBL:ABS01566.1}; OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216). OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae; OC Kineococcus. OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS01566.1, ECO:0000313|Proteomes:UP000001116}; RN [1] {ECO:0000313|Proteomes:UP000001116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216 RC {ECO:0000313|Proteomes:UP000001116}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., RA Fliermans C., Richardson P.; RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."; RL Submitted (JUL-2007) 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; CP000750; ABS01566.1; -; Genomic_DNA. DR RefSeq; WP_012085614.1; NC_009664.2. DR AlphaFoldDB; A6W427; -. DR STRING; 266940.Krad_0075; -. DR KEGG; kra:Krad_0075; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_025431_1_1_11; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000001116; 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:UP000001116}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 310..331 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 6..238 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT REGION 261..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 412..463 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 418..438 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 439..455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 463 AA; 48131 MW; 071618871FFA9FA9 CRC64; MAIALNFAAR SDVGLGRSSN QDSGYAGPHL LVVADGMGGH AGGDVASSLA VGELSILDGE SHGSDDAAQH LHDALEAANA QLRRRVGDEP DLAGMGTTVT AILRAGSRLV LAHIGDSRGY LLREGRLTQL TKDHSYVQSL LDEGRISPEE AERHPQRSVI MRVLTGRDDD EADVSVREAK PGDRYLLCSD GLSGVVSHET LAETLAAGMD PDTTCQRLVE LALRGGGPDN ISCVVADVVE LGGGPPPSTT PQVVGAAAFH RPRRSSAAGT PAARAAALRA AQDESGDDSE DDDAQPRLSE RERRRRRRRW IAGPVLLLLV LVAGGFGGWR WSQQQYFVGA DGSNVAVYRG LTQDIGPLGT SHVVESTGIS LSDLPTTWAD KVRARIASQD LAGARRTVSD LEDIASACRA ATAPTTPAVP VVPAPAAASP PASTPAPTSE PTSEPTSTPS STPLTVEDCG GVG //