ID   PP2C3_PARTE             Reviewed;         300 AA.
AC   A0BQL0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=Probable protein phosphatase 2C 3;
DE            Short=PP2C 3;
DE            EC=3.1.3.16;
GN   ORFNames=GSPATT00031056001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
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. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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 {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; CT868009; CAK60827.1; -; Genomic_DNA.
DR   RefSeq; XP_001428225.1; XM_001428188.2.
DR   AlphaFoldDB; A0BQL0; -.
DR   SMR; A0BQL0; -.
DR   FunCoup; A0BQL0; 1470.
DR   STRING; 5888.A0BQL0; -.
DR   EnsemblProtists; CAK60827; CAK60827; GSPATT00031056001.
DR   GeneID; 5014009; -.
DR   KEGG; ptm:GSPATT00031056001; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_4_1_1; -.
DR   InParanoid; A0BQL0; -.
DR   OMA; FYCANIG; -.
DR   OrthoDB; 10264738at2759; -.
DR   Proteomes; UP000000600; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   FunFam; 3.60.40.10:FF:000064; Protein phosphatase 2C 1; 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:SF803; PROTEIN PHOSPHATASE 1G; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 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   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Probable protein phosphatase 2C 3"
FT                   /id="PRO_0000307830"
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"
SQ   SEQUENCE   300 AA;  33462 MW;  6143F9FE79355637 CRC64;
     MGPYLSQPKR EKVTTSGEGK SVIFAASEMQ GWRNTMEDAH IHRPDIVQDV SVFGVFDGHG
     GREVAQFVEK HFIDELLKNK NFKEQKFEDA LKETFLKMDE LLMTPEGAKE LNNYKATDTD
     ESYAGCTANV ALIHKNTLYV ANAGDSRSVL CRNNTNFDMS VDHKPDNNEE KSRIERAGGF
     VSDGRVNGNL NLSRALGDLE YKSDSKLRPN EQLIIAFPDV KKTELTPQDK FILMGCDGVF
     ETLNHQELLK HVNTTLGNSP VTENLLSKAA EDLLDQLLAP DTSQGTGCDN MTTILVYLKK
//