ID Q47AU0_DECAR Unreviewed; 265 AA. AC Q47AU0; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Daro_3311 {ECO:0000313|EMBL:AAZ48041.1}; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae; OC Dechloromonas. OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ48041.1}; RN [1] {ECO:0000313|EMBL:AAZ48041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RCB {ECO:0000313|EMBL:AAZ48041.1}; RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.; RT "Complete sequence of Dechloromonas aromatica RCB."; RL Submitted (AUG-2005) 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; CP000089; AAZ48041.1; -; Genomic_DNA. DR AlphaFoldDB; Q47AU0; -. DR STRING; 159087.Daro_3311; -. DR KEGG; dar:Daro_3311; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_5_0_4; -. DR OrthoDB; 9801841at2; -. 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; FT DOMAIN 6..245 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 265 AA; 28526 MW; 84ACD1BC04DA6F32 CRC64; MAIAVDACAA QHQGDRKEQQ DRVAILPHAR ARGVALAVVA DGMGGHTGGA LAAEQVVHTA KTNLDQFSAA DETSQKMLEN SMREAHTMIK ASRFMNEMDP HSTAVMLLLQ PGRVTWGYCG DSRLYHFRGK KLVGRTVDHS YVEHLVATGK ITPEQALTHP NRNVLLASLG GADDPKITLD EVTELSPGDA FVLCSDGLWA YFDDEELGAL VADNSARQAC EILIDKARQR AKGSGDNLSL AIIKLNEAVP KKPTPPAGFV PRLPT //