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Q04081

- LCMT1_YEAST

UniProt

Q04081 - LCMT1_YEAST

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Protein

Leucine carboxyl methyltransferase 1

Gene
PPM1, YDR435C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 PPH22.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester.

Enzyme regulationi

Inhibited by S-adenosyl-L-homocysteine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811S-adenosyl-L-methionine
Binding sitei105 – 1051S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei128 – 1281S-adenosyl-L-methionine
Binding sitei201 – 2011S-adenosyl-L-methionine; via carbonyl oxygen

GO - Molecular functioni

  1. protein C-terminal leucine carboxyl O-methyltransferase activity Source: SGD

GO - Biological processi

  1. cellular protein complex assembly Source: SGD
  2. C-terminal protein methylation Source: SGD
  3. regulation of autophagy Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:YDR435C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PPM1
Ordered Locus Names:YDR435C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR435c.
SGDiS000002843. PPM1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Leucine carboxyl methyltransferase 1PRO_0000226135Add
BLAST

Proteomic databases

MaxQBiQ04081.
PaxDbiQ04081.
PeptideAtlasiQ04081.

Expressioni

Gene expression databases

GenevestigatoriQ04081.

Interactioni

Protein-protein interaction databases

BioGridi32491. 93 interactions.
DIPiDIP-5435N.
MINTiMINT-517778.
STRINGi4932.YDR435C.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64
Helixi8 – 2215
Turni28 – 325
Helixi35 – 5521
Helixi57 – 6812
Helixi72 – 9524
Beta strandi97 – 1048
Helixi112 – 1187
Beta strandi122 – 1287
Helixi130 – 14213
Helixi144 – 1507
Beta strandi162 – 1654
Beta strandi167 – 1737
Beta strandi176 – 1783
Helixi179 – 1879
Beta strandi192 – 1943
Beta strandi196 – 2027
Helixi204 – 2063
Helixi209 – 22214
Beta strandi224 – 23310
Helixi243 – 25513
Turni260 – 2656
Helixi268 – 2725
Helixi273 – 2753
Beta strandi278 – 2858
Helixi286 – 2927
Helixi296 – 3038
Helixi311 – 3188
Beta strandi321 – 3288

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ04081.
SMRiQ04081. Positions 2-328.

Miscellaneous databases

EvolutionaryTraceiQ04081.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1773S-adenosyl-L-methionine binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG329644.
HOGENOMiHOG000113293.
KOiK18203.
OMAiIISECVL.
OrthoDBiEOG70611J.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR007213. LCM_MeTrfase.
IPR016651. Leu_CO_MeTrfase_LCMT1.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR13600. PTHR13600. 1 hit.
PfamiPF04072. LCM. 1 hit.
[Graphical view]
PIRSFiPIRSF016305. LCM_mtfrase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q04081-1 [UniParc]FASTAAdd to Basket

« Hide

MERIIQQTDY DALSCKLAAI SVGYLPSSGL QRLSVDLSKK YTEWHRSYLI    50
TLKKFSRRAF GKVDKAMRSS FPVMNYGTYL RTVGIDAAIL EFLVANEKVQ 100
VVNLGCGSDL RMLPLLQMFP HLAYVDIDYN ESVELKNSIL RESEILRISL 150
GLSKEDTAKS PFLIDQGRYK LAACDLNDIT ETTRLLDVCT KREIPTIVIS 200
ECLLCYMHNN ESQLLINTIM SKFSHGLWIS YDPIGGSQPN DRFGAIMQSN 250
LKESRNLEMP TLMTYNSKEK YASRWSAAPN VIVNDMWEIF NAQIPESERK 300
RLRSLQFLDE LEELKVMQTH YILMKAQW 328
Length:328
Mass (Da):37,695
Last modified:November 1, 1996 - v1
Checksum:i5FAB5B9F8B04D154
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33007 Genomic DNA. Translation: AAB64876.1.
BK006938 Genomic DNA. Translation: DAA12272.1.
PIRiS69715.
RefSeqiNP_010723.1. NM_001180743.1.

Genome annotation databases

EnsemblFungiiYDR435C; YDR435C; YDR435C.
GeneIDi852045.
KEGGisce:YDR435C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33007 Genomic DNA. Translation: AAB64876.1 .
BK006938 Genomic DNA. Translation: DAA12272.1 .
PIRi S69715.
RefSeqi NP_010723.1. NM_001180743.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RJD X-ray 1.80 A/B/C 1-328 [» ]
1RJE X-ray 2.00 A/B/C 1-328 [» ]
1RJF X-ray 2.25 A/B/C 1-328 [» ]
1RJG X-ray 2.61 A 1-328 [» ]
2OB1 X-ray 1.90 A/B/C 10-328 [» ]
2OB2 X-ray 1.92 A/B/C 2-328 [» ]
ProteinModelPortali Q04081.
SMRi Q04081. Positions 2-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32491. 93 interactions.
DIPi DIP-5435N.
MINTi MINT-517778.
STRINGi 4932.YDR435C.

Proteomic databases

MaxQBi Q04081.
PaxDbi Q04081.
PeptideAtlasi Q04081.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR435C ; YDR435C ; YDR435C .
GeneIDi 852045.
KEGGi sce:YDR435C.

Organism-specific databases

CYGDi YDR435c.
SGDi S000002843. PPM1.

Phylogenomic databases

eggNOGi NOG329644.
HOGENOMi HOG000113293.
KOi K18203.
OMAi IISECVL.
OrthoDBi EOG70611J.

Enzyme and pathway databases

BioCyci YEAST:YDR435C-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q04081.
NextBioi 970296.
PROi Q04081.

Gene expression databases

Genevestigatori Q04081.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR007213. LCM_MeTrfase.
IPR016651. Leu_CO_MeTrfase_LCMT1.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR13600. PTHR13600. 1 hit.
Pfami PF04072. LCM. 1 hit.
[Graphical view ]
PIRSFi PIRSF016305. LCM_mtfrase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiLCMT1_YEAST
AccessioniPrimary (citable) accession number: Q04081
Secondary accession number(s): D6VT62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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