ID   LCMT1_CAEBR             Reviewed;         331 AA.
AC   Q60YU0; A8XT04;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable leucine carboxyl methyltransferase 1;
DE            EC=2.1.1.233;
DE   AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
GN   ORFNames=CBG18087;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE600963; CAP35607.1; -; Genomic_DNA.
DR   RefSeq; XP_002642139.1; XM_002642093.1.
DR   AlphaFoldDB; Q60YU0; -.
DR   SMR; Q60YU0; -.
DR   STRING; 6238.CBG18087; -.
DR   EnsemblMetazoa; CBG18087.1; CBG18087.1; WBGene00037577.
DR   GeneID; 8584134; -.
DR   KEGG; cbr:CBG_18087; -.
DR   CTD; 8584134; -.
DR   WormBase; CBG18087; CBP04345; WBGene00037577; -.
DR   eggNOG; KOG2918; Eukaryota.
DR   HOGENOM; CLU_031312_0_0_1; -.
DR   InParanoid; Q60YU0; -.
DR   OMA; IIYEPIR; -.
DR   OrthoDB; 1094856at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
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..331
FT                   /note="Probable leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000226152"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
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         179..180
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   331 AA;  37629 MW;  F29F3B3D0005437A CRC64;
     MDSEAISSDS HVAAAIATRR RSNSVSDDYS VQRTNDDATQ CKYFAIQKGY WKDDFIGRFA
     NSSANVAEAR RFPEISMGYW ARTAAIEKYV RGFLEEFDGN AQVVSFGCGF DTLFWRLVSS
     DAKLAKYVEV DFSSVTSKKI RHILKPGGSV DLKKSFESEA VVSHHADLHA GNYHLIGADL
     RQTSELEQKL ATCQLDHDIP TIFIAECVLV YMSSNTSSSL LKNLVSQFRH PAFVNYEQFR
     TSDAFTRVME QNLGERGIQL HGLEMCESAE KQEERFRNAG FKSVKVMDMN QIFNQFLDQD
     EVARIRQIEM LDEMELLEQL LAHYCVVFAR V