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P00958

- SYMC_YEAST

UniProt

P00958 - SYMC_YEAST

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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

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

GO - Biological processi

  1. methionyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

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
Complete GO annotation...

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. 38 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 – 53Combined sources
Beta strandi10 – 123Combined sources
Helixi15 – 3117Combined sources
Beta strandi49 – 513Combined sources
Helixi61 – 688Combined sources
Turni73 – 764Combined sources
Helixi78 – 869Combined sources
Turni87 – 893Combined sources
Helixi90 – 923Combined sources
Beta strandi93 – 953Combined sources
Helixi98 – 11114Combined sources
Helixi122 – 14221Combined sources
Helixi148 – 15710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP00958.
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

        10         20         30         40         50
MSFLISFDKS KKHPAHLQLA NNLKIALALE YASKNLKPEV DNDNAAMELR
60 70 80 90 100
NTKEPFLLFD ANAILRYVMD DFEGQTSDKY QFALASLQNL LYHKELPQQH
110 120 130 140 150
VEVLTNKAIE NYLVELKEPL TTTDLILFAN VYALNSSLVH SKFPELPSKV
160 170 180 190 200
HNAVALAKKH VPRDSSSFKN IGAVKIQADL TVKPKDSEIL PKPNERNILI
210 220 230 240 250
TSALPYVNNV PHLGNIIGSV LSADIFARYC KGRNYNALFI CGTDEYGTAT
260 270 280 290 300
ETKALEEGVT PRQLCDKYHK IHSDVYKWFQ IGFDYFGRTT TDKQTEIAQH
310 320 330 340 350
IFTKLNSNGY LEEQSMKQLY CPVHNSYLAD RYVEGECPKC HYDDARGDQC
360 370 380 390 400
DKCGALLDPF ELINPRCKLD DASPEPKYSD HIFLSLDKLE SQISEWVEKA
410 420 430 440 450
SEEGNWSKNS KTITQSWLKD GLKPRCITRD LVWGTPVPLE KYKDKVLYVW
460 470 480 490 500
FDATIGYVSI TSNYTKEWKQ WWNNPEHVSL YQFMGKDNVP FHTVVFPGSQ
510 520 530 540 550
LGTEENWTML HHLNTTEYLQ YENGKFSKSR GVGVFGNNAQ DSGISPSVWR
560 570 580 590 600
YYLASVRPES SDSHFSWDDF VARNNSELLA NLGNFVNRLI KFVNAKYNGV
610 620 630 640 650
VPKFDPKKVS NYDGLVKDIN EILSNYVKEM ELGHERRGLE IAMSLSARGN
660 670 680 690 700
QFLQENKLDN TLFSQSPEKS DAVVAVGLNI IYAVSSIITP YMPEIGEKIN
710 720 730 740 750
KMLNAPALKI DDRFHLAILE GHNINKAEYL FQRIDEKKID EWRAKYGGQQ

V
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 38 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.
InParanoidi P00958.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 151 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