ID   PP2C1_PARTE             Reviewed;         300 AA.
AC   P49444; A0BL55;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Protein phosphatase 2C 1;
DE            Short=PP2C 1;
DE            EC=3.1.3.16;
GN   ORFNames=GSPATT00029903001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Stock 51;
RX   PubMed=7806499; DOI=10.1016/s0021-9258(20)30058-2;
RA   Klumpp S., Hanke C., Donella-Deana A., Beyer A., Kellner R., Pinna L.A.,
RA   Schultz J.E.;
RT   "A membrane-bound protein phosphatase type 2C from Paramecium tetraurelia.
RT   Purification, characterization, and cloning.";
RL   J. Biol. Chem. 269:32774-32780(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- FUNCTION: Enzyme with a broad specificity.
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; Z36985; CAA85448.1; -; mRNA.
DR   EMBL; CT868001; CAK59272.1; -; Genomic_DNA.
DR   PIR; A55804; A55804.
DR   RefSeq; XP_001426670.1; XM_001426633.1.
DR   AlphaFoldDB; P49444; -.
DR   SMR; P49444; -.
DR   STRING; 5888.P49444; -.
DR   EnsemblProtists; CAK59272; CAK59272; GSPATT00029903001.
DR   GeneID; 5012454; -.
DR   KEGG; ptm:GSPATT00029903001; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_4_1_1; -.
DR   InParanoid; P49444; -.
DR   OMA; TKRPEYR; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Protein phosphatase; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Protein phosphatase 2C 1"
FT                   /id="PRO_0000057765"
FT   DOMAIN          23..298
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         57
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        44
FT                   /note="P -> H (in Ref. 1; CAA85448)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  33699 MW;  B9EF98B4F78F24EC CRC64;
     MGPYLSQPKR DKTTTTGQGK SVIFAASEMQ GWRNTMEDAH IHRPDIIQDV SVFGVFDGHG
     GREVAQFVEK HFVDELLKNK NFKEQKFEEA LKETFLKMDE LLLTPEGQKE LNQYKATDTD
     ESYAGCTANV ALIYKNTLYV ANAGDSRSVL CRNNTNHDMS VDHKPDNPEE KSRIERAGGF
     VSDGRVNGNL NLSRALGDLE YKRDNKLRSN EQLIIALPDV KKTELTPQDK FILMGCDGVF
     ETLNHQELLK QVNSTIGQAQ VTEELLKKAA EDLLDQLLAP DTSQGTGCDN MTTILVYLRR
//