ID   PP2C4_PARTE             Reviewed;         301 AA.
AC   A0DTY1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Probable protein phosphatase 2C 4;
DE            Short=PP2C 4;
DE            EC=3.1.3.16;
GN   ORFNames=GSPATT00020181001;
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=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 {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; CT868574; CAK86498.1; -; Genomic_DNA.
DR   RefSeq; XP_001453895.1; XM_001453858.1.
DR   AlphaFoldDB; A0DTY1; -.
DR   SMR; A0DTY1; -.
DR   STRING; 5888.CAK86498; -.
DR   EnsemblProtists; CAK86498; CAK86498; GSPATT00020181001.
DR   GeneID; 5039680; -.
DR   KEGG; ptm:GSPATT00020181001; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_4_1_1; -.
DR   InParanoid; A0DTY1; -.
DR   OMA; SMQGYRM; -.
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   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 2.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 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..301
FT                   /note="Probable protein phosphatase 2C 4"
FT                   /id="PRO_0000307831"
FT   DOMAIN          23..298
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   301 AA;  33666 MW;  C63A00AB18150686 CRC64;
     MGPYLSQPNK NKTTTSGEGK SIIFAASEMQ GWRNTMEDAH IHVCDLQQDL SIFGVFDGHG
     GKEVAQFVEK HFIEELQKNK NFKDQKFEDA LRETFLKMDE LLLTPEGQKE IIQIKGGDDE
     ASYAGCTANV ALFHKNVLYV ANAGDSRSVL CRNNTNYDMS VDHKPDNYEE KSRIERAGGF
     VSDGRVNGNL NLSRALGDLE YKRDSKLRSN EQLIIALPDI KKVELNQTDK FLLMGCDGVF
     ETLDHQDLLK FINQKLGNQQ ITPQLLGRVA EDLLDNLIAP DTSAGTGCDN MTTLIIYLKG
     K