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Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (Protein phosphatase methyltransferase 1) ([Phosphatase 2A protein]-leucine-carboxy methyltransferase 1)

 LCMT1_YEAST             Reviewed;         328 AA.
Q04081; D6VT62;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-APR-2018, entry version 122.
RecName: Full=Leucine carboxyl methyltransferase 1;
EC=2.1.1.233;
AltName: Full=Protein phosphatase methyltransferase 1;
AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
Name=PPM1; OrderedLocusNames=YDR435C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=11060018; DOI=10.1093/emboj/19.21.5672;
Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.;
"Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic
subunit promotes its functional association with regulatory subunits
in vivo.";
EMBO J. 19:5672-5681(2000).
[4]
FUNCTION.
PubMed=11697862; DOI=10.1006/abbi.2001.2558;
Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.;
"Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity
responsible for modification of the major forms of protein phosphatase
2A in yeast.";
Arch. Biochem. Biophys. 395:239-245(2001).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH
S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE.
PubMed=14660564; DOI=10.1074/jbc.M311484200;
Leulliot N., Quevillon-Cheruel S., Sorel I., de La Sierra-Gallay I.L.,
Collinet B., Graille M., Blondeau K., Bettache N., Poupon A.,
Janin J., van Tilbeurgh H.;
"Structure of protein phosphatase methyltransferase 1 (PPM1), a
leucine carboxyl methyltransferase involved in the regulation of
protein phosphatase 2A activity.";
J. Biol. Chem. 279:8351-8358(2004).
-!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine
residue of protein phosphatase 2A catalytic subunits to form
alpha-leucine ester residues. Acts on the two major protein
phosphatase 2A catalytic subunits, PPH21 and PPH22.
{ECO:0000269|PubMed:11060018, ECO:0000269|PubMed:11697862}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [phosphatase 2A
protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A
protein]-leucine methyl ester.
-!- ENZYME REGULATION: Inhibited by S-adenosyl-L-homocysteine.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U33007; AAB64876.1; -; Genomic_DNA.
EMBL; BK006938; DAA12272.1; -; Genomic_DNA.
PIR; S69715; S69715.
RefSeq; NP_010723.1; NM_001180743.1.
PDB; 1RJD; X-ray; 1.80 A; A/B/C=1-328.
PDB; 1RJE; X-ray; 2.00 A; A/B/C=1-328.
PDB; 1RJF; X-ray; 2.25 A; A/B/C=1-328.
PDB; 1RJG; X-ray; 2.61 A; A=1-328.
PDB; 2OB1; X-ray; 1.90 A; A/B/C=10-328.
PDB; 2OB2; X-ray; 1.92 A; A/B/C=2-328.
PDBsum; 1RJD; -.
PDBsum; 1RJE; -.
PDBsum; 1RJF; -.
PDBsum; 1RJG; -.
PDBsum; 2OB1; -.
PDBsum; 2OB2; -.
ProteinModelPortal; Q04081; -.
SMR; Q04081; -.
BioGrid; 32491; 190.
DIP; DIP-5435N; -.
STRING; 4932.YDR435C; -.
MaxQB; Q04081; -.
PaxDb; Q04081; -.
PRIDE; Q04081; -.
EnsemblFungi; YDR435C; YDR435C; YDR435C.
GeneID; 852045; -.
KEGG; sce:YDR435C; -.
EuPathDB; FungiDB:YDR435C; -.
SGD; S000002843; PPM1.
HOGENOM; HOG000113293; -.
InParanoid; Q04081; -.
KO; K18203; -.
OMA; PYIQYFV; -.
OrthoDB; EOG092C4D3U; -.
BioCyc; YEAST:YDR435C-MONOMER; -.
BRENDA; 2.1.1.233; 984.
EvolutionaryTrace; Q04081; -.
PRO; PR:Q04081; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IMP:SGD.
GO; GO:0006481; P:C-terminal protein methylation; IMP:SGD.
GO; GO:0034622; P:cellular protein-containing complex assembly; IMP:SGD.
GO; GO:0010506; P:regulation of autophagy; IMP:SGD.
InterPro; IPR016651; Leu_CO_MeTrfase_LCMT1.
InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF04072; LCM; 1.
PIRSF; PIRSF016305; LCM_mtfrase; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Methyltransferase;
Reference proteome; S-adenosyl-L-methionine; Transferase.
CHAIN 1 328 Leucine carboxyl methyltransferase 1.
/FTId=PRO_0000226135.
REGION 175 177 S-adenosyl-L-methionine binding.
BINDING 81 81 S-adenosyl-L-methionine.
BINDING 105 105 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 128 128 S-adenosyl-L-methionine.
BINDING 201 201 S-adenosyl-L-methionine; via carbonyl
oxygen.
HELIX 3 6 {ECO:0000244|PDB:1RJD}.
HELIX 8 22 {ECO:0000244|PDB:1RJD}.
TURN 28 32 {ECO:0000244|PDB:1RJD}.
HELIX 35 55 {ECO:0000244|PDB:1RJD}.
HELIX 57 68 {ECO:0000244|PDB:1RJD}.
HELIX 72 95 {ECO:0000244|PDB:1RJD}.
STRAND 97 104 {ECO:0000244|PDB:1RJD}.
HELIX 112 118 {ECO:0000244|PDB:1RJD}.
STRAND 122 128 {ECO:0000244|PDB:1RJD}.
HELIX 130 142 {ECO:0000244|PDB:1RJD}.
HELIX 144 150 {ECO:0000244|PDB:1RJD}.
STRAND 162 165 {ECO:0000244|PDB:1RJD}.
STRAND 167 173 {ECO:0000244|PDB:1RJD}.
STRAND 176 178 {ECO:0000244|PDB:1RJG}.
HELIX 179 187 {ECO:0000244|PDB:1RJD}.
STRAND 192 194 {ECO:0000244|PDB:1RJE}.
STRAND 196 202 {ECO:0000244|PDB:1RJD}.
HELIX 204 206 {ECO:0000244|PDB:1RJD}.
HELIX 209 222 {ECO:0000244|PDB:1RJD}.
STRAND 224 233 {ECO:0000244|PDB:1RJD}.
HELIX 243 255 {ECO:0000244|PDB:1RJD}.
TURN 260 265 {ECO:0000244|PDB:1RJD}.
HELIX 268 272 {ECO:0000244|PDB:1RJD}.
HELIX 273 275 {ECO:0000244|PDB:1RJD}.
STRAND 278 285 {ECO:0000244|PDB:1RJD}.
HELIX 286 292 {ECO:0000244|PDB:1RJD}.
HELIX 296 303 {ECO:0000244|PDB:1RJD}.
HELIX 311 318 {ECO:0000244|PDB:1RJD}.
STRAND 321 328 {ECO:0000244|PDB:1RJD}.
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


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