ID   PPM1K_XENLA             Reviewed;         373 AA.
AC   Q6ING9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Protein phosphatase 1K, mitochondrial;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform kappa;
DE            Short=PP2C-kappa;
DE   Flags: Precursor;
GN   Name=ppm1k;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; BC072312; AAH72312.1; -; mRNA.
DR   RefSeq; NP_001085111.1; NM_001091642.1.
DR   RefSeq; XP_018091803.1; XM_018236314.1.
DR   RefSeq; XP_018091812.1; XM_018236323.1.
DR   AlphaFoldDB; Q6ING9; -.
DR   SMR; Q6ING9; -.
DR   DNASU; 432182; -.
DR   GeneID; 432182; -.
DR   KEGG; xla:432182; -.
DR   CTD; 432182; -.
DR   Xenbase; XB-GENE-956548; ppm1k.S.
DR   OMA; TSTRHCF; -.
DR   OrthoDB; 1044139at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 432182; Expressed in heart and 19 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; -; 1.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
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   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   Protein phosphatase; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           ?..373
FT                   /note="Protein phosphatase 1K, mitochondrial"
FT                   /id="PRO_0000278211"
FT   DOMAIN          95..347
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  41536 MW;  58713D1A52099BB7 CRC64;
     MSTAILVSLL RNGRCQVNRG ALTLCFQKEH SCTTSTRHCF SANRRCFSSR FDLDGSGRPA
     TWDSFGIWDN RIDEPIQLPP SIKYGKLIPH INLSKVGCST QLGKRKENED RFKLARLTPD
     ILYFAVYDGH GGASAAEFCD RFMEDYIKEF LVEEHDMEKV LVKAFLEINK AFARHAHLSV
     DASLLTCGTT ATVALLRDGI ELVVASVGDS RALLCRRGKP FKLTIDHTPE RKEEKLRIKK
     SGGFVTWNSL GQPNVNGRLA MTRSIGDLDL KSMGVIAEPE TKRVKLQHTD DGFLVLTTDG
     INFIVNSQEI CDIINQCHDP KEAAQVLTEQ AIQYGTEDNS TAIVVPFGAW GKHKSSEVSF
     SFSRGFASSG RWD