ID   LCMT1_DEBHA             Reviewed;         369 AA.
AC   Q6BQD2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Leucine carboxyl methyltransferase 1;
DE            EC=2.1.1.233;
DE   AltName: Full=Protein phosphatase methyltransferase 1;
DE   AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
GN   Name=PPM1; OrderedLocusNames=DEHA2E06094g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine
CC       residue of protein phosphatase 2A catalytic subunits to form alpha-
CC       leucine ester residues. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-
CC         methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl
CC         ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA-
CC         COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517;
CC         EC=2.1.1.233;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC       {ECO:0000305}.
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DR   EMBL; CR382137; CAG87815.2; -; Genomic_DNA.
DR   RefSeq; XP_459588.2; XM_459588.1.
DR   AlphaFoldDB; Q6BQD2; -.
DR   SMR; Q6BQD2; -.
DR   STRING; 4959.XP_459588.2; -.
DR   EnsemblFungi; CAG87815; CAG87815; DEHA2E06094g.
DR   GeneID; 2901885; -.
DR   KEGG; dha:DEHA2E06094g; -.
DR   VEuPathDB; FungiDB:DEHA2E06094g; -.
DR   eggNOG; KOG2918; Eukaryota.
DR   HOGENOM; CLU_031312_1_0_1; -.
DR   InParanoid; Q6BQD2; -.
DR   OMA; IIYEPIR; -.
DR   OrthoDB; 1094856at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016651; PPM1.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13600; PTHR13600; 1.
DR   Pfam; PF04072; LCM; 1.
DR   PIRSF; PIRSF016305; LCM_mtfrase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..369
FT                   /note="Leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000226127"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  42526 MW;  67A1F2B3AE0E40A1 CRC64;
     MISPQEKQDK VIRATDLDAL SCRYSANNKS YFSKPDPFID SLISSYKMHL PLCTGYTNMS
     ANRTLRSVFN EQKLPLINRG TYLRTESIDV ITQEFIKEFK KCQVISLGGG SDTRCFRILE
     EHGEDVRYCE IDFHESVKIK KLAIINDKKL ADIVKYDEES QSITSKEEFA RLESNIHTEN
     YHLIGYDLRE LTGALDSGAI LEYVDTSLPT LILSECVLCY LNPKENERII EFWKNAFASK
     ALLALLIYEP MSLNDAFGTT MTHNLSNRGI NLLTFNEYPN LEARYKFLSE KCQSSNVKLT
     DMSNVGGYDS DNTTKAWINS KDLARINRLE LVDEIEEIRL LLKHYCLCYC EFSHSPSLKT
     INKWKWILE