LCMT1_CANAL
ID LCMT1_CANAL Reviewed; 367 AA.
AC Q5A387; A0A1D8PTQ1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=CAALFM_CR08170CA;
GN ORFNames=CaO19.13734, CaO19.6377;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017630; AOW31501.1; -; Genomic_DNA.
DR RefSeq; XP_716217.1; XM_711124.1.
DR AlphaFoldDB; Q5A387; -.
DR SMR; Q5A387; -.
DR STRING; 237561.Q5A387; -.
DR PRIDE; Q5A387; -.
DR GeneID; 3642073; -.
DR KEGG; cal:CAALFM_CR08170CA; -.
DR CGD; CAL0000196930; orf19.13734.
DR VEuPathDB; FungiDB:CR_08170C_A; -.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_031312_1_1_1; -.
DR InParanoid; Q5A387; -.
DR OMA; IIYEPIR; -.
DR OrthoDB; 1094856at2759; -.
DR PRO; PR:Q5A387; -.
DR Proteomes; UP000000559; Chromosome R.
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..367
FT /note="Leucine carboxyl methyltransferase 1"
FT /id="PRO_0000226124"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 42896 MW; 807A33E30586DE90 CRC64;
MLSPQDRQDK LVRATDLDAL SCKYSINRNL YLNPPDEFVK DLVESYQRYL QYCVGYTGLS
SSRALKGLFQ EKKMPIINRG SYLRTRAIDQ VVNKFIGEFK DRCQIVSLGS GSDTRAFQIF
KSHANVIYHE IDFPESAKVK KLAILQNPVI RELVGTNETS PLINNKEQFE SYSSELHTEK
YHLHGIDLRT LKKPDSQIKG FQPEVPTLVI SECVLCYLSP DEYQRTMNYW TEIADQNYMG
FLIYEPMSLN DQFGETMTLN LQSRGLNLQT FSKYPDLISR KKFLEESCHL KNLRLTDMSY
IGGYKVRQDG REWIDHKEMG RINKLEMIDE IEEIRLLLEH YCLIYGEYTE EKTLNFKGID
TWSWILS
