ID   LCMT1_YARLI             Reviewed;         324 AA.
AC   Q6C997;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=YALI0D12881g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382130; CAG80953.1; -; Genomic_DNA.
DR   RefSeq; XP_502765.1; XM_502765.1.
DR   AlphaFoldDB; Q6C997; -.
DR   SMR; Q6C997; -.
DR   STRING; 4952.CAG80953; -.
DR   EnsemblFungi; CAG80953; CAG80953; YALI0_D12881g.
DR   GeneID; 2911265; -.
DR   KEGG; yli:YALI0D12881g; -.
DR   VEuPathDB; FungiDB:YALI0_D12881g; -.
DR   HOGENOM; CLU_031312_1_0_1; -.
DR   InParanoid; Q6C997; -.
DR   OMA; IIYEPIR; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006481; P:C-terminal protein methylation; IBA:GO_Central.
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..324
FT                   /note="Leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000226134"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         172..173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36463 MW;  8929CEDB915D76A6 CRC64;
     MNLRKDKVVQ STDGDALSSK YSAVQKGYLQ DEFIDLFVAG SKQAAAQQGP GSARKVVAQF
     QPKLPLINRG TFVRHHAIDV LVDRFLAAKK PGQRVQIISL GAGSDTRPFS LWSSKPENRD
     EILYHEIDFA VSVERKRDII MQDSTLRELV GAQEYDKTTG MHTQRYHLHG IDLRSIGPGF
     VLPGSDPSLA TLIISECCLC YLEPDQAKQV IFWITSEFTN STIVMYEPLS GQDQFGQVMI
     ENLASRGISI PSMTKFPSLE SQIERFKAAG YTEVLATSMD VIHDEWLSPE EQQRIHGLEF
     LDEREELLLL LKHYCVVWAS NLTK