ID   LCMT1_KLULA             Reviewed;         333 AA.
AC   Q6CWW0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=KLLA0B01089g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH01972.1; -; Genomic_DNA.
DR   RefSeq; XP_451579.1; XM_451579.1.
DR   AlphaFoldDB; Q6CWW0; -.
DR   SMR; Q6CWW0; -.
DR   STRING; 28985.XP_451579.1; -.
DR   EnsemblFungi; CAH01972; CAH01972; KLLA0_B01089g.
DR   GeneID; 2897248; -.
DR   KEGG; kla:KLLA0_B01089g; -.
DR   eggNOG; KOG2918; Eukaryota.
DR   HOGENOM; CLU_031312_1_0_1; -.
DR   InParanoid; Q6CWW0; -.
DR   OMA; IIYEPIR; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:EnsemblFungi.
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..333
FT                   /note="Leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000226130"
FT   BINDING         79
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         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  38811 MW;  A84540C1046E764F CRC64;
     MERVIQETDN DAFSCKISAI TKRYLPSSEQ KKIGNYEHYE DIHLEFCKEI KSRSRRKYAN
     ITKACRHSLP VMNYGTYLRT VSIDLKLTQW LKNNLENPAD KVQVINLGCG SDLRMMTFLA
     SFPGVQWLDL DYKDVVTFKS TILRSNAKFR ASLQIEGDLP EEPSSIENVI TDRYQLLPCN
     VTDDEQLIPI LKKYTDFSVP AVILTECVLC YLHESKASQL ISTVTGLYKQ GYWISYDPIG
     GSQTNDRFGS IMQDNLMESR QLSMPTLMVF NSEDKYKERF PGKSEIQTMW DYYQNHLEDS
     ERQRLKTLQF LDEIEELQVI FSHYVICTTN WRI