ID   Q47AP2_DECAR            Unreviewed;       274 AA.
AC   Q47AP2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, 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=Daro_3360 {ECO:0000313|EMBL:AAZ48089.1};
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ48089.1};
RN   [1] {ECO:0000313|EMBL:AAZ48089.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RCB {ECO:0000313|EMBL:AAZ48089.1};
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};
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DR   EMBL; CP000089; AAZ48089.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47AP2; -.
DR   STRING; 159087.Daro_3360; -.
DR   KEGG; dar:Daro_3360; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_4; -.
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   NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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          8..255
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   274 AA;  29700 MW;  1A3F65BF02149C02 CRC64;
     MMLRDALEMV VRTDPGLIRS HNEDAVFAEA GLGIAILADG MGGYNAGEVA SGMAITRLAE
     DLNRVISSCV TQEGSGSCDP SVIERHIVNE VGAANFAIFH ASQSCSQYAG MGTTLVLAWF
     YDNRMSVAHV GDSRLYRLRG QVFELLTRDH SLRQEQVDNG MISPEEARYA ENRNLVTRAL
     GVDPSVDVEV HDFDVQPGDI VLLCSDGLND MLEDEDIALT LSALGGNLPL AADHLIQLAN
     DHGGRDNVSV ILVKVLGDYS APKGWWQRLF GCLK
//