Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00958

- SYMC_YEAST

UniProt

P00958 - SYMC_YEAST

Protein

Methionine--tRNA ligase, cytoplasmic

Gene

MES1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the attachment of methionine to tRNA(Met) in a two-step reaction: methionine is first activated by ATP to form Met-AMP and then transferred to the acceptor end of tRNA(Met).1 Publication

    Catalytic activityi

    ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).3 Publications

    Kineticsi

    The presence of ARC1 reduces the KM for tRNA(Met) to less than 0.1 µM and increases the catalytic efficiency more than 500-fold.

    1. KM=6.6 µM for tRNA(Met) (in the absence of ARC1)3 Publications
    2. KM=10 µM for methionine3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei411 – 4111ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. methionine-tRNA ligase activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. methionyl-tRNA aminoacylation Source: SGD

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30933-MONOMER.
    BRENDAi6.1.1.10. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine--tRNA ligase, cytoplasmic (EC:6.1.1.10)
    Alternative name(s):
    Methionyl-tRNA synthetase
    Short name:
    MetRS
    Gene namesi
    Name:MES1
    Ordered Locus Names:YGR264C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    SGDiS000003496. MES1.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Largely excluded from the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. methionyl glutamyl tRNA synthetase complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631A → H: Abolishes interaction with ARC1. 1 Publication
    Mutagenesisi502 – 5021G → D in mes1; renders the protein unstable in vitro, elevates the KM for methionine in vivo. 1 Publication
    Mutagenesisi584 – 5841N → D or Q: Abolishes aminoacylation activity. 1 Publication
    Mutagenesisi588 – 5881R → A, K or Q: Abolishes aminoacylation activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 751750Methionine--tRNA ligase, cytoplasmicPRO_0000139269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP00958.
    PaxDbiP00958.
    PeptideAtlasiP00958.

    Expressioni

    Gene expression databases

    GenevestigatoriP00958.

    Interactioni

    Subunit structurei

    Component of a yeast aminoacyl-tRNA synthase (aaRS) complex formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex. Interacts (via N-ter) with ARC1 (via N-ter). Can also form a stable binary complex with ARC1 that is functional in terms of aminoacylation. ARC1 increases the affinity for cognate tRNAs due to the presence of a tRNA binding domain in the middle and C-terminal part of ARC1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARC1P466727EBI-18762,EBI-7224

    Protein-protein interaction databases

    BioGridi33515. 37 interactions.
    DIPiDIP-2211N.
    IntActiP00958. 10 interactions.
    MINTiMINT-648422.
    STRINGi4932.YGR264C.

    Structurei

    Secondary structure

    1
    751
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi10 – 123
    Helixi15 – 3117
    Beta strandi49 – 513
    Helixi61 – 688
    Turni73 – 764
    Helixi78 – 869
    Turni87 – 893
    Helixi90 – 923
    Beta strandi93 – 953
    Helixi98 – 11114
    Helixi122 – 14221
    Helixi148 – 15710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HSNX-ray2.20A2-160[»]
    ProteinModelPortaliP00958.
    SMRiP00958. Positions 1-160, 199-739.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00958.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni36 – 9257Interaction with ARC1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi205 – 21511"HIGH" regionAdd
    BLAST
    Motifi525 – 5295"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0143.
    GeneTreeiENSGT00550000075017.
    HOGENOMiHOG000200402.
    KOiK01874.
    OMAiWVEEASE.
    OrthoDBiEOG7CG77Z.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    2.20.28.20. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00098. Met_tRNA_synth_type1.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR018285. Met-tRNA-synth_N.
    IPR023458. Met-tRNA_ligase_1.
    IPR014758. Met-tRNA_synth.
    IPR015413. Methionyl/Leucyl_tRNA_Synth.
    IPR029038. MetRS_Zn.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PfamiPF09635. MetRS-N. 1 hit.
    PF09334. tRNA-synt_1g. 1 hit.
    [Graphical view]
    PRINTSiPR01041. TRNASYNTHMET.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF57770. SSF57770. 1 hit.
    TIGRFAMsiTIGR00398. metG. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00958-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFLISFDKS KKHPAHLQLA NNLKIALALE YASKNLKPEV DNDNAAMELR    50
    NTKEPFLLFD ANAILRYVMD DFEGQTSDKY QFALASLQNL LYHKELPQQH 100
    VEVLTNKAIE NYLVELKEPL TTTDLILFAN VYALNSSLVH SKFPELPSKV 150
    HNAVALAKKH VPRDSSSFKN IGAVKIQADL TVKPKDSEIL PKPNERNILI 200
    TSALPYVNNV PHLGNIIGSV LSADIFARYC KGRNYNALFI CGTDEYGTAT 250
    ETKALEEGVT PRQLCDKYHK IHSDVYKWFQ IGFDYFGRTT TDKQTEIAQH 300
    IFTKLNSNGY LEEQSMKQLY CPVHNSYLAD RYVEGECPKC HYDDARGDQC 350
    DKCGALLDPF ELINPRCKLD DASPEPKYSD HIFLSLDKLE SQISEWVEKA 400
    SEEGNWSKNS KTITQSWLKD GLKPRCITRD LVWGTPVPLE KYKDKVLYVW 450
    FDATIGYVSI TSNYTKEWKQ WWNNPEHVSL YQFMGKDNVP FHTVVFPGSQ 500
    LGTEENWTML HHLNTTEYLQ YENGKFSKSR GVGVFGNNAQ DSGISPSVWR 550
    YYLASVRPES SDSHFSWDDF VARNNSELLA NLGNFVNRLI KFVNAKYNGV 600
    VPKFDPKKVS NYDGLVKDIN EILSNYVKEM ELGHERRGLE IAMSLSARGN 650
    QFLQENKLDN TLFSQSPEKS DAVVAVGLNI IYAVSSIITP YMPEIGEKIN 700
    KMLNAPALKI DDRFHLAILE GHNINKAEYL FQRIDEKKID EWRAKYGGQQ 750
    V 751
    Length:751
    Mass (Da):85,678
    Last modified:January 23, 2007 - v4
    Checksum:i11679C1AB8BB5E39
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221T → A in CAA24627. (PubMed:6341994)Curated
    Sequence conflicti122 – 1221T → A(PubMed:3905796)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01316 Genomic DNA. Translation: CAA24627.1.
    Y07777 Genomic DNA. Translation: CAA69086.1.
    Z73049 Genomic DNA. Translation: CAA97293.1.
    BK006941 Genomic DNA. Translation: DAA08354.1.
    PIRiS64597. SYBYMT.
    RefSeqiNP_011780.3. NM_001181393.3.

    Genome annotation databases

    EnsemblFungiiYGR264C; YGR264C; YGR264C.
    GeneIDi853181.
    KEGGisce:YGR264C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01316 Genomic DNA. Translation: CAA24627.1 .
    Y07777 Genomic DNA. Translation: CAA69086.1 .
    Z73049 Genomic DNA. Translation: CAA97293.1 .
    BK006941 Genomic DNA. Translation: DAA08354.1 .
    PIRi S64597. SYBYMT.
    RefSeqi NP_011780.3. NM_001181393.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HSN X-ray 2.20 A 2-160 [» ]
    ProteinModelPortali P00958.
    SMRi P00958. Positions 1-160, 199-739.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33515. 37 interactions.
    DIPi DIP-2211N.
    IntActi P00958. 10 interactions.
    MINTi MINT-648422.
    STRINGi 4932.YGR264C.

    Proteomic databases

    MaxQBi P00958.
    PaxDbi P00958.
    PeptideAtlasi P00958.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR264C ; YGR264C ; YGR264C .
    GeneIDi 853181.
    KEGGi sce:YGR264C.

    Organism-specific databases

    SGDi S000003496. MES1.

    Phylogenomic databases

    eggNOGi COG0143.
    GeneTreei ENSGT00550000075017.
    HOGENOMi HOG000200402.
    KOi K01874.
    OMAi WVEEASE.
    OrthoDBi EOG7CG77Z.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30933-MONOMER.
    BRENDAi 6.1.1.10. 984.

    Miscellaneous databases

    EvolutionaryTracei P00958.
    NextBioi 973317.
    PROi P00958.

    Gene expression databases

    Genevestigatori P00958.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    2.20.28.20. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_00098. Met_tRNA_synth_type1.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR018285. Met-tRNA-synth_N.
    IPR023458. Met-tRNA_ligase_1.
    IPR014758. Met-tRNA_synth.
    IPR015413. Methionyl/Leucyl_tRNA_Synth.
    IPR029038. MetRS_Zn.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    Pfami PF09635. MetRS-N. 1 hit.
    PF09334. tRNA-synt_1g. 1 hit.
    [Graphical view ]
    PRINTSi PR01041. TRNASYNTHMET.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF57770. SSF57770. 1 hit.
    TIGRFAMsi TIGR00398. metG. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase."
      Walter P., Gangloff J., Bonnet J., Boulanger Y., Ebel J.-P., Fasiolo F.
      Proc. Natl. Acad. Sci. U.S.A. 80:2437-2441(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Fasiolo F.
      Submitted (SEP-1983) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Cytoplasmic methionyl-tRNA synthetase from Bakers' yeast. A monomer with a post-translationally modified N-terminus."
      Fasiolo F., Gibson B.W., Walter P., Chatton B., Biemann K., Boulanger Y.
      J. Biol. Chem. 260:15571-15576(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    4. "Analysis of an 11.6 kb region from the right arm of chromosome VII of Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the presence of three new genes."
      Clemente M.L., Sartori G., Cardazzo B., Carignani G.
      Yeast 13:287-290(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Strategy for the mass spectrometric verification and correction of the primary structures of proteins deduced from their DNA sequences."
      Gibson B.W., Biemann K.
      Proc. Natl. Acad. Sci. U.S.A. 81:1956-1960(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 10-90, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    8. "Cloning and characterization of the yeast methionyl-tRNA synthetase mutation mes1."
      Chatton B., Winsor B., Boulanger Y., Fasiolo F.
      J. Biol. Chem. 262:15094-15097(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-502.
    9. "Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase."
      Despons L., Walter P., Senger B., Ebel J.-P., Fasiolo F.
      FEBS Lett. 289:217-220(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-584 AND ARG-588.
    10. "The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases."
      Simos G., Segref A., Fasiolo F., Hellmuth K., Shevshenko A., Mann M., Hurt E.C.
      EMBO J. 15:5437-5448(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH ARC1.
    11. "A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases."
      Simos G., Sauer A., Fasiolo F., Hurt E.C.
      Mol. Cell 1:235-242(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH ARC1.
    12. "The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p."
      Galani K., Grosshans H., Deinert K., Hurt E.C., Simos G.
      EMBO J. 20:6889-6898(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH ARC1, SUBCELLULAR LOCATION.
    13. "Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs."
      Deinert K., Fasiolo F., Hurt E.C., Simos G.
      J. Biol. Chem. 276:6000-6008(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    15. "Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes."
      Simader H., Hothorn M., Koehler C., Basquin J., Simos G., Suck D.
      Nucleic Acids Res. 34:3968-3979(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-160 IN COMPLEX WITH ARC1, MUTAGENESIS OF ALA-63.

    Entry informationi

    Entry nameiSYMC_YEAST
    AccessioniPrimary (citable) accession number: P00958
    Secondary accession number(s): D6VV43
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 85000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3