PP2C1_PARTE
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 03-AUG-2022, entry version 117.
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}.
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; 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.CAK59272; -.
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; IEFTCEN; -.
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; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
