ID   LCMT1_CAEEL             Reviewed;         333 AA.
AC   P46554;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Leucine carboxyl methyltransferase 1 {ECO:0000250|UniProtKB:Q9UIC8};
DE            EC=2.1.1.233 {ECO:0000250|UniProtKB:Q9UIC8};
DE   AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1 {ECO:0000250|UniProtKB:Q9UIC8};
GN   Name=lcmt-1 {ECO:0000312|WormBase:B0285.4};
GN   ORFNames=B0285.4 {ECO:0000312|WormBase:B0285.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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|UniProtKB:Q9UIC8}.
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; Evidence={ECO:0000250|UniProtKB:Q9UIC8};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC       {ECO:0000305}.
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DR   EMBL; BX284603; CAA84295.1; -; Genomic_DNA.
DR   PIR; T18690; T18690.
DR   RefSeq; NP_497875.1; NM_065474.3.
DR   AlphaFoldDB; P46554; -.
DR   SMR; P46554; -.
DR   BioGRID; 40797; 6.
DR   STRING; 6239.B0285.4; -.
DR   iPTMnet; P46554; -.
DR   EPD; P46554; -.
DR   PaxDb; P46554; -.
DR   PeptideAtlas; P46554; -.
DR   EnsemblMetazoa; B0285.4.1; B0285.4.1; WBGene00007137.
DR   GeneID; 175561; -.
DR   KEGG; cel:CELE_B0285.4; -.
DR   UCSC; B0285.4; c. elegans.
DR   CTD; 175561; -.
DR   WormBase; B0285.4; CE00643; WBGene00007137; lcmt-1.
DR   eggNOG; KOG2918; Eukaryota.
DR   GeneTree; ENSGT00940000156372; -.
DR   HOGENOM; CLU_031312_0_0_1; -.
DR   InParanoid; P46554; -.
DR   OMA; IIYEPIR; -.
DR   OrthoDB; 1094856at2759; -.
DR   PhylomeDB; P46554; -.
DR   Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   PRO; PR:P46554; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007137; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..333
FT                   /note="Leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000065058"
FT   BINDING         42
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT   BINDING         107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT   BINDING         181..182
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIC8"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIC8"
SQ   SEQUENCE   333 AA;  37816 MW;  BE2C8F69BE8C4B6C CRC64;
     MDSEAVSSDS HVAAAIATRR RSNSVSDDYS VQRTNDDATQ CKYFATQKGY WKDEFISRFA
     NSSSNVSEAR RFPEISMGYW ARTAAIEKYV RDFLNEFDGN AQVVSLGCGF DTLFWRLVSS
     GAKLVKYVEV DFSSVTSKKI RHILKPIGPN SVDLKKSFES DAVVSHHADL HAGNYHLIGA
     DLRQANELDQ KLATCQLSHD IPTIFIAECV LVYMSADSST ALLKQIVSQF KQPAFVNYEQ
     FRTSDAFTKV MEQNLGDRGI QLHGLEMCES AEKQEERFRN AGFKEVKVMD MNQIFNNFLD
     QKEVSRIREI EMLDEMELLQ QLFAHYCVVS ARI