ID PPM1G_CAEEL Reviewed; 491 AA. AC P49595; Q8MNS3; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 164. DE RecName: Full=Protein phosphatase ppm-1.G {ECO:0000305}; DE EC=3.1.3.16; DE AltName: Full=Protein phosphatase 2C isoform gamma homolog {ECO:0000305}; DE Short=PP2C-gamma {ECO:0000305}; DE AltName: Full=Protein phosphatase magnesium-dependent 1 gamma homolog {ECO:0000305}; GN Name=ppm-1.G {ECO:0000312|WormBase:F42G9.1a}; GN ORFNames=F42G9.1 {ECO:0000312|WormBase:F42G9.1a}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a {ECO:0000312|WormBase:F42G9.1a}; CC IsoId=P49595-1; Sequence=Displayed; CC Name=b {ECO:0000312|WormBase:F42G9.1b}; CC IsoId=P49595-2; Sequence=VSP_060334; 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; BX284603; CCD61882.1; -; Genomic_DNA. DR EMBL; BX284603; CCD61883.1; -; Genomic_DNA. DR PIR; T16354; T16354. DR RefSeq; NP_741086.1; NM_171075.4. [P49595-1] DR RefSeq; NP_741087.1; NM_171076.3. DR AlphaFoldDB; P49595; -. DR SMR; P49595; -. DR BioGRID; 40503; 4. DR IntAct; P49595; 2. DR STRING; 6239.F42G9.1a.1; -. DR iPTMnet; P49595; -. DR EPD; P49595; -. DR PaxDb; 6239-F42G9-1a; -. DR PeptideAtlas; P49595; -. DR EnsemblMetazoa; F42G9.1a.1; F42G9.1a.1; WBGene00018362. [P49595-1] DR EnsemblMetazoa; F42G9.1b.1; F42G9.1b.1; WBGene00018362. [P49595-2] DR GeneID; 175233; -. DR KEGG; cel:CELE_F42G9.1; -. DR UCSC; F42G9.1a; c. elegans. DR AGR; WB:WBGene00018362; -. DR WormBase; F42G9.1a; CE07231; WBGene00018362; ppm-1.G. [P49595-1] DR WormBase; F42G9.1b; CE30788; WBGene00018362; ppm-1.G. [P49595-2] DR eggNOG; KOG0699; Eukaryota. DR GeneTree; ENSGT00940000165923; -. DR HOGENOM; CLU_013173_13_1_1; -. DR InParanoid; P49595; -. DR OMA; RYGQNCI; -. DR OrthoDB; 11028at2759; -. DR PhylomeDB; P49595; -. DR PRO; PR:P49595; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00018362; Expressed in adult organism and 5 other cell types or tissues. 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; 2. 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; 2. 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 Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding; KW Protein phosphatase; Reference proteome. FT CHAIN 1..491 FT /note="Protein phosphatase ppm-1.G" FT /id="PRO_0000057762" FT DOMAIN 23..486 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 112..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 112..129 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 173..195 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 196..224 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 259..293 FT /note="Acidic residues" 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 428 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 477 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT VAR_SEQ 1..37 FT /note="MGAYLNKPIIEKEKEEGSGNGLSYACTTMQGWRVNQE -> MDFKNVEYFYL FT KNFQ (in isoform b)" FT /evidence="ECO:0000305" FT /id="VSP_060334" SQ SEQUENCE 491 AA; 53142 MW; F110D12E343953D6 CRC64; MGAYLNKPII EKEKEEGSGN GLSYACTTMQ GWRVNQEDAH NCVVDLHTDW HMFGVYDGHG GTEVSKFTSA KLPDFLKERK FWEADDVAEC LQKAFVDFDD FIRAEESMKE LKDIGDEGKP KKAGGEADSE DEADRIDTIE EASVPLAELL KRYGGAGVGK SLLSAFLAKG DVSDDSEDED EDEEEAEEQD DTEEKKENED ASAEVVIENA EDKEEEEGSP KKKGQKRCQK SPIQSEAKKS KSETDAETAP SSSSGVDGVA TEEEDEDDSD KEFVADEEED DEDAEDEQSD EEMVDGSLAP LLLGSGGAEV PGEDSGTTAC VCLVGKDKVI VANAGDSRAV LCRNGKAVDL SVDHKPEDEV ETNRIHAAGG QIEDGRVNGG LNLSRAFGDH AYKKNQELGL KEQMITALPD VKIEALTPED EFIVVACDGI WNSMESQQVV DFVRDLLAKG SSCAEVCDAL CDACLADSTD GDGTGCDNMT VICTTFDRKS K //