LCMT1_ASHGO
ID LCMT1_ASHGO Reviewed; 325 AA.
AC Q759U5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 96.
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=ADR178W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 86.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52098.2; -; Genomic_DNA.
DR RefSeq; NP_984274.2; NM_209627.2.
DR AlphaFoldDB; Q759U5; -.
DR SMR; Q759U5; -.
DR STRING; 33169.AAS52098; -.
DR EnsemblFungi; AAS52098; AAS52098; AGOS_ADR178W.
DR GeneID; 4620436; -.
DR KEGG; ago:AGOS_ADR178W; -.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_031312_1_0_1; -.
DR InParanoid; Q759U5; -.
DR OMA; IIYEPIR; -.
DR Proteomes; UP000000591; Chromosome IV.
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 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..325
FT /note="Leucine carboxyl methyltransferase 1"
FT /id="PRO_0000226122"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 174..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 37376 MW; E05A914F3168544D CRC64;
MDRTVQQTDY DALSCRMAAI TRGYLPSQKQ IEQCGYEGYT EVHVEYCNVL RRLSRRLYSR
VQKACTTLLP VMNYGSFVRT VSVDVELHKY VAGFGGRAQV VNLGCGSDLR MCMLLERYPE
LHYVDVDFAE TVKMKREVLM QSAELCRRIG ASSTSPQEQD CVLHGPRYRL LAGDLRDTGA
LLELLQKHTD ADLPTVVITE CVLCYLPREA AQALIREVCG FYKSGSWISY DPIGGGQRED
RFGSIMQSNL REFRQLELPT LMEFNSKEKY SARFPAPSNI QTMWEYYMTD ISEDEKRKLK
TLQFLDEVEE LEILLSHYVI LVTSW
