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Q04081 (LCMT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine carboxyl methyltransferase 1

EC=2.1.1.233
Alternative name(s):
Protein phosphatase methyltransferase 1
[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1
Gene names
Name:PPM1
Ordered Locus Names:YDR435C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.4

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.

Sequence similarities

Belongs to the methyltransferase superfamily. LCMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Leucine carboxyl methyltransferase 1
PRO_0000226135

Regions

Region175 – 1773S-adenosyl-L-methionine binding

Sites

Binding site811S-adenosyl-L-methionine
Binding site1051S-adenosyl-L-methionine; via carbonyl oxygen
Binding site1281S-adenosyl-L-methionine
Binding site2011S-adenosyl-L-methionine; via carbonyl oxygen

Secondary structure

....................................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04081 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5FAB5B9F8B04D154

FASTA32837,695
        10         20         30         40         50         60 
MERIIQQTDY DALSCKLAAI SVGYLPSSGL QRLSVDLSKK YTEWHRSYLI TLKKFSRRAF 

        70         80         90        100        110        120 
GKVDKAMRSS FPVMNYGTYL RTVGIDAAIL EFLVANEKVQ VVNLGCGSDL RMLPLLQMFP 

       130        140        150        160        170        180 
HLAYVDIDYN ESVELKNSIL RESEILRISL GLSKEDTAKS PFLIDQGRYK LAACDLNDIT 

       190        200        210        220        230        240 
ETTRLLDVCT KREIPTIVIS ECLLCYMHNN ESQLLINTIM SKFSHGLWIS YDPIGGSQPN 

       250        260        270        280        290        300 
DRFGAIMQSN LKESRNLEMP TLMTYNSKEK YASRWSAAPN VIVNDMWEIF NAQIPESERK 

       310        320 
RLRSLQFLDE LEELKVMQTH YILMKAQW 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo."
Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.
EMBO J. 19:5672-5681(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast."
Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.
Arch. Biochem. Biophys. 395:239-245(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity."
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.
J. Biol. Chem. 279:8351-8358(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33007 Genomic DNA. Translation: AAB64876.1.
BK006938 Genomic DNA. Translation: DAA12272.1.
PIRS69715.
RefSeqNP_010723.1. NM_001180743.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJDX-ray1.80A/B/C1-328[»]
1RJEX-ray2.00A/B/C1-328[»]
1RJFX-ray2.25A/B/C1-328[»]
1RJGX-ray2.61A1-328[»]
2OB1X-ray1.90A/B/C10-328[»]
2OB2X-ray1.92A/B/C2-328[»]
ProteinModelPortalQ04081.
SMRQ04081. Positions 2-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32491. 92 interactions.
DIPDIP-5435N.
MINTMINT-517778.
STRING4932.YDR435C.

Proteomic databases

PaxDbQ04081.
PeptideAtlasQ04081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR435C; YDR435C; YDR435C.
GeneID852045.
KEGGsce:YDR435C.

Organism-specific databases

CYGDYDR435c.
SGDS000002843. PPM1.

Phylogenomic databases

eggNOGNOG329644.
HOGENOMHOG000113293.
OMAHEIDFPE.
OrthoDBEOG70611J.

Enzyme and pathway databases

BioCycYEAST:YDR435C-MONOMER.

Gene expression databases

GenevestigatorQ04081.

Family and domain databases

InterProIPR007213. LCM_MeTrfase.
IPR016651. Leu_CO_MeTrfase_LCMT1.
[Graphical view]
PANTHERPTHR13600. PTHR13600. 1 hit.
PfamPF04072. LCM. 1 hit.
[Graphical view]
PIRSFPIRSF016305. LCM_mtfrase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ04081.
NextBio970296.
PROQ04081.

Entry information

Entry nameLCMT1_YEAST
AccessionPrimary (citable) accession number: Q04081
Secondary accession number(s): D6VT62
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references