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P00958 (SYMC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine--tRNA ligase, cytoplasmic

EC=6.1.1.10
Alternative name(s):
Methionyl-tRNA synthetase
Short name=MetRS
Gene names
Name:MES1
Ordered Locus Names:YGR264C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length751 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP-Rule MF_00098

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00098.

Miscellaneous

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

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARC1P466727EBI-18762,EBI-7224

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 751750Methionine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00098
PRO_0000139269

Regions

Motif205 – 21511"HIGH" region HAMAP-Rule MF_00098
Motif408 – 4125"KMSKS" region HAMAP-Rule MF_00098

Sites

Binding site4111ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.3

Experimental info

Mutagenesis5841N → D or Q: Abolishes aminoacylation activity. Ref.8
Mutagenesis5881R → A, K or Q: Abolishes aminoacylation activity. Ref.8
Sequence conflict1221T → A Ref.1
Sequence conflict1221T → A Ref.3

Secondary structure

........................ 751
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00958 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 11679C1AB8BB5E39

FASTA75185,678
        10         20         30         40         50         60 
MSFLISFDKS KKHPAHLQLA NNLKIALALE YASKNLKPEV DNDNAAMELR NTKEPFLLFD 

        70         80         90        100        110        120 
ANAILRYVMD DFEGQTSDKY QFALASLQNL LYHKELPQQH VEVLTNKAIE NYLVELKEPL 

       130        140        150        160        170        180 
TTTDLILFAN VYALNSSLVH SKFPELPSKV HNAVALAKKH VPRDSSSFKN IGAVKIQADL 

       190        200        210        220        230        240 
TVKPKDSEIL PKPNERNILI TSALPYVNNV PHLGNIIGSV LSADIFARYC KGRNYNALFI 

       250        260        270        280        290        300 
CGTDEYGTAT ETKALEEGVT PRQLCDKYHK IHSDVYKWFQ IGFDYFGRTT TDKQTEIAQH 

       310        320        330        340        350        360 
IFTKLNSNGY LEEQSMKQLY CPVHNSYLAD RYVEGECPKC HYDDARGDQC DKCGALLDPF 

       370        380        390        400        410        420 
ELINPRCKLD DASPEPKYSD HIFLSLDKLE SQISEWVEKA SEEGNWSKNS KTITQSWLKD 

       430        440        450        460        470        480 
GLKPRCITRD LVWGTPVPLE KYKDKVLYVW FDATIGYVSI TSNYTKEWKQ WWNNPEHVSL 

       490        500        510        520        530        540 
YQFMGKDNVP FHTVVFPGSQ LGTEENWTML HHLNTTEYLQ YENGKFSKSR GVGVFGNNAQ 

       550        560        570        580        590        600 
DSGISPSVWR YYLASVRPES SDSHFSWDDF VARNNSELLA NLGNFVNRLI KFVNAKYNGV 

       610        620        630        640        650        660 
VPKFDPKKVS NYDGLVKDIN EILSNYVKEM ELGHERRGLE IAMSLSARGN QFLQENKLDN 

       670        680        690        700        710        720 
TLFSQSPEKS DAVVAVGLNI IYAVSSIITP YMPEIGEKIN KMLNAPALKI DDRFHLAILE 

       730        740        750 
GHNINKAEYL FQRIDEKKID EWRAKYGGQQ V 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
[8]"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.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01316 Genomic DNA. Translation: CAA24627.1.
Y07777 Genomic DNA. Translation: CAA69086.1.
Z73049 Genomic DNA. Translation: CAA97293.1.
BK006941 Genomic DNA. Translation: DAA08354.1.
PIRSYBYMT. S64597.
RefSeqNP_011780.3. NM_001181393.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HSNX-ray2.20A2-160[»]
ProteinModelPortalP00958.
SMRP00958. Positions 1-160, 199-739.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33515. 37 interactions.
DIPDIP-2211N.
IntActP00958. 10 interactions.
MINTMINT-648422.
STRING4932.YGR264C.

Proteomic databases

MaxQBP00958.
PaxDbP00958.
PeptideAtlasP00958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR264C; YGR264C; YGR264C.
GeneID853181.
KEGGsce:YGR264C.

Organism-specific databases

SGDS000003496. MES1.

Phylogenomic databases

eggNOGCOG0143.
GeneTreeENSGT00550000075017.
HOGENOMHOG000200402.
KOK01874.
OMAWVEEASE.
OrthoDBEOG7CG77Z.

Enzyme and pathway databases

BioCycYEAST:G3O-30933-MONOMER.
BRENDA6.1.1.10. 984.

Gene expression databases

GenevestigatorP00958.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
2.20.28.20. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00098. Met_tRNA_synth_type1.
InterProIPR001412. 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]
PfamPF09635. MetRS-N. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF57770. SSF57770. 1 hit.
TIGRFAMsTIGR00398. metG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00958.
NextBio973317.
PROP00958.

Entry information

Entry nameSYMC_YEAST
AccessionPrimary (citable) accession number: P00958
Secondary accession number(s): D6VV43
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries