LCMT1_YEAST
ID LCMT1_YEAST Reviewed; 328 AA.
AC Q04081; D6VT62;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
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=YDR435C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11060018; DOI=10.1093/emboj/19.21.5672;
RA Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.;
RT "Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic
RT subunit promotes its functional association with regulatory subunits in
RT vivo.";
RL EMBO J. 19:5672-5681(2000).
RN [4]
RP FUNCTION.
RX PubMed=11697862; DOI=10.1006/abbi.2001.2558;
RA Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.;
RT "Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity
RT responsible for modification of the major forms of protein phosphatase 2A
RT in yeast.";
RL Arch. Biochem. Biophys. 395:239-245(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE.
RX PubMed=14660564; DOI=10.1074/jbc.m311484200;
RA Leulliot N., Quevillon-Cheruel S., Sorel I., de La Sierra-Gallay I.L.,
RA Collinet B., Graille M., Blondeau K., Bettache N., Poupon A., Janin J.,
RA van Tilbeurgh H.;
RT "Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine
RT carboxyl methyltransferase involved in the regulation of protein
RT phosphatase 2A activity.";
RL J. Biol. Chem. 279:8351-8358(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. Acts on the two major protein phosphatase 2A
CC catalytic subunits, PPH21 and PPH22. {ECO:0000269|PubMed:11060018,
CC ECO:0000269|PubMed:11697862}.
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 -!- ACTIVITY REGULATION: Inhibited by S-adenosyl-L-homocysteine.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
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DR EMBL; U33007; AAB64876.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12272.1; -; Genomic_DNA.
DR PIR; S69715; S69715.
DR RefSeq; NP_010723.1; NM_001180743.1.
DR PDB; 1RJD; X-ray; 1.80 A; A/B/C=1-328.
DR PDB; 1RJE; X-ray; 2.00 A; A/B/C=1-328.
DR PDB; 1RJF; X-ray; 2.25 A; A/B/C=1-328.
DR PDB; 1RJG; X-ray; 2.61 A; A=1-328.
DR PDB; 2OB1; X-ray; 1.90 A; A/B/C=10-328.
DR PDB; 2OB2; X-ray; 1.92 A; A/B/C=2-328.
DR PDBsum; 1RJD; -.
DR PDBsum; 1RJE; -.
DR PDBsum; 1RJF; -.
DR PDBsum; 1RJG; -.
DR PDBsum; 2OB1; -.
DR PDBsum; 2OB2; -.
DR AlphaFoldDB; Q04081; -.
DR SMR; Q04081; -.
DR BioGRID; 32491; 202.
DR DIP; DIP-5435N; -.
DR STRING; 4932.YDR435C; -.
DR MaxQB; Q04081; -.
DR PaxDb; Q04081; -.
DR PRIDE; Q04081; -.
DR EnsemblFungi; YDR435C_mRNA; YDR435C; YDR435C.
DR GeneID; 852045; -.
DR KEGG; sce:YDR435C; -.
DR SGD; S000002843; PPM1.
DR VEuPathDB; FungiDB:YDR435C; -.
DR eggNOG; KOG2918; Eukaryota.
DR GeneTree; ENSGT00940000156372; -.
DR HOGENOM; CLU_031312_1_0_1; -.
DR InParanoid; Q04081; -.
DR OMA; IIYEPIR; -.
DR BioCyc; YEAST:YDR435C-MON; -.
DR BRENDA; 2.1.1.233; 984.
DR EvolutionaryTrace; Q04081; -.
DR PRO; PR:Q04081; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04081; protein.
DR GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IMP:SGD.
DR GO; GO:0006481; P:C-terminal protein methylation; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:0010506; P:regulation of autophagy; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..328
FT /note="Leucine carboxyl methyltransferase 1"
FT /id="PRO_0000226135"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 175..177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 8..22
FT /evidence="ECO:0007829|PDB:1RJD"
FT TURN 28..32
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 35..55
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 72..95
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1RJG"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1RJE"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 209..222
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1RJD"
FT TURN 260..265
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:1RJD"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:1RJD"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:1RJD"
SQ SEQUENCE 328 AA; 37695 MW; 5FAB5B9F8B04D154 CRC64;
MERIIQQTDY DALSCKLAAI SVGYLPSSGL QRLSVDLSKK YTEWHRSYLI TLKKFSRRAF
GKVDKAMRSS FPVMNYGTYL RTVGIDAAIL EFLVANEKVQ VVNLGCGSDL RMLPLLQMFP
HLAYVDIDYN ESVELKNSIL RESEILRISL GLSKEDTAKS PFLIDQGRYK LAACDLNDIT
ETTRLLDVCT KREIPTIVIS ECLLCYMHNN ESQLLINTIM SKFSHGLWIS YDPIGGSQPN
DRFGAIMQSN LKESRNLEMP TLMTYNSKEK YASRWSAAPN VIVNDMWEIF NAQIPESERK
RLRSLQFLDE LEELKVMQTH YILMKAQW
