ID   C9R7Z0_AMMDK            Unreviewed;       236 AA.
AC   C9R7Z0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Adeg_1312 {ECO:0000313|EMBL:ACX52419.1};
OS   Ammonifex degensii (strain DSM 10501 / KC4).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Ammonifex.
OX   NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52419.1, ECO:0000313|Proteomes:UP000002620};
RN   [1] {ECO:0000313|EMBL:ACX52419.1, ECO:0000313|Proteomes:UP000002620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG   US DOE Joint Genome Institute;
RA   Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA   Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT   "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL   Submitted (OCT-2009) 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; CP001785; ACX52419.1; -; Genomic_DNA.
DR   RefSeq; WP_015739296.1; NC_013385.1.
DR   AlphaFoldDB; C9R7Z0; -.
DR   STRING; 429009.Adeg_1312; -.
DR   KEGG; adg:Adeg_1312; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   Proteomes; UP000002620; Chromosome.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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;
KW   Hydrolase {ECO:0000313|EMBL:ACX52419.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002620}.
FT   DOMAIN          2..234
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   236 AA;  25885 MW;  12441AE10FF20E2A CRC64;
     MEWVAKSDQG LIRPRNEDAY LVLPDKGLFA VADGLGGHQA GEVASQLAVS TVAQFWQEER
     EVSLEKLVAA VKAANEAVYR ASLARPECMG MGTTLTVCLL KEKELLWAHV GDSRGYLLRG
     EEISQFTRDH TLVAELLREG EISPEEVKYH PYRHVLSRAL GIEATVEVDA GSFVLEQGDI
     ILLCTDGLTL HLAPEEILRL VREAESLPAG GEKLLAEALE RGGEDNITLV MVRIDD
//