ID A0A1H2ABB4_9ACTN Unreviewed; 292 AA.
AC A0A1H2ABB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=SAMN04489812_5806 {ECO:0000313|EMBL:SDT43177.1};
OS Microlunatus soli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=630515 {ECO:0000313|EMBL:SDT43177.1, ECO:0000313|Proteomes:UP000199103};
RN [1] {ECO:0000313|EMBL:SDT43177.1, ECO:0000313|Proteomes:UP000199103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21800 {ECO:0000313|EMBL:SDT43177.1,
RC ECO:0000313|Proteomes:UP000199103};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; LT629772; SDT43177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2ABB4; -.
DR STRING; 630515.SAMN04489812_5806; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000199103; Chromosome i.
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 Reference proteome {ECO:0000313|Proteomes:UP000199103}.
FT DOMAIN 5..234
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 292 AA; 30705 MW; C78A8494AA5E0F41 CRC64;
MLRFRCAAAS HVGLVRTNNE DSGYAGAYLL LVADGVGGAA AGEVASASTT YVTSSVSMIS
DDDPLAVLAQ AVEFAHHHVR DGVEADPQRD GMSTTLTAVL GNGERFGLVH VGDSRGYLWR
DGALTPITRD HSLMQMLLDS GELRPEDAED FPYRSVIARS INQIEDPEPD LVLLDLRCGD
RILLASDGLT DIVPDDLLGP TVAMPDLDAA VDELVSLALA AGGRDNVTCI LGEVVEGDLI
HPRGRMIGAA ADPHNLIDPA AVRIDRVGGR RTAKLQAVST GADPWGHTGA TA
//