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Q04081

- LCMT1_YEAST

UniProt

Q04081 - LCMT1_YEAST

Protein

Leucine carboxyl methyltransferase 1

Gene

PPM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 90 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