ID   PP2C_LEICH              Reviewed;         406 AA.
AC   P36982;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein phosphatase 2C;
DE            Short=PP2C;
DE            EC=3.1.3.16;
OS   Leishmania chagasi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=44271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MHOM/BR/82/BA-2;
RX   PubMed=8394331; DOI=10.1016/s0021-9258(19)85316-4;
RA   Burns J.M. Jr., Parsons M., Rosman D.E., Reed S.G.;
RT   "Molecular cloning and characterization of a 42-kDa protein phosphatase of
RT   Leishmania chagasi.";
RL   J. Biol. Chem. 268:17155-17161(1993).
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Found in infective promastigote and in tissue
CC       amastigote stages.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; L15559; AAA02864.1; -; Unassigned_DNA.
DR   PIR; A47492; A47492.
DR   AlphaFoldDB; P36982; -.
DR   SMR; P36982; -.
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; 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; Protein phosphatase.
FT   CHAIN           1..406
FT                   /note="Protein phosphatase 2C"
FT                   /id="PRO_0000057764"
FT   DOMAIN          23..274
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         55
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  45139 MW;  9B2C6647FE7B93BA CRC64;
     MGIPLPKPVM TQLQERYGNA IFRCGSNCVN GYRETMEDAH LTYLTDSWGF FGVFDGHVND
     QCSQYLERAW RSAIEKESIP MTDERMKELA LRIDQEWMDS GREGGSTGTF FVALKEGNKV
     HLQVGNVGDS RVVACIDGVC VPLTEDHKPN NEGERQRIEN CAGRVENNRV DGSLAVSRAF
     GDREYKLGSG SQLEQKVIAL ADVQHKDFTF DSNDFVLLCC DGVFEGNFPN EEVVAYVKQQ
     LETCNDLAEV AGRVCEEAIE RGSRDNISCM IVQFKDGSDY AAEPHTTVVP GPFSAPRNSG
     FRKAYESMAD KGNTTVGALL ERRYDTLKAA EALTPEETEE LSQFENGPEA KLTGAERQKW
     FSNYFQKLCE AASNGPSDQM ERLQSLQQQA GIPLSILLSL MGEQTQ