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UniProtKB/Swiss-Prot entry P00958


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYMC_YEAST
Primary accession number P00958
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    December 16, 2008 (Entry version 93)
Name and origin of the protein
Protein name Methionyl-tRNA synthetase, cytoplasmic
Synonyms EC 6.1.1.10
Methionine--tRNA ligase
MetRS
Gene name
Name: MES1
OrderedLocusNames: YGR264C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6341994 [NCBI, ExPASy, EBI, Israel, Japan]
Walter P., Gangloff J., Bonnet J., Boulanger Y., Ebel J.-P., Fasiolo F.;
"Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 80:2437-2441(1983).
[2]
SEQUENCE REVISION.
Fasiolo F.;
Submitted (SEP-1983) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2.
PubMed=3905796 [NCBI, ExPASy, EBI, Israel, Japan]
Fasiolo F., Gibson B.W., Walter P., Chatton B., Biemann K., Boulanger Y.;
"Cytoplasmic methionyl-tRNA synthetase from Bakers' yeast. A monomer with a post-translationally modified N-terminus.";
J. Biol. Chem. 260:15571-15576(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<287::AID-YEA75>3.0.CO;2-5; PubMed=9090059 [NCBI, ExPASy, EBI, Israel, Japan]
Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
"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.";
Yeast 13:287-290(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[6]
PROTEIN SEQUENCE OF 10-90.
PubMed=6371805 [NCBI, ExPASy, EBI, Israel, Japan]
Gibson B.W., Biemann K.;
"Strategy for the mass spectrometric verification and correction of the primary structures of proteins deduced from their DNA sequences.";
Proc. Natl. Acad. Sci. U.S.A. 81:1956-1960(1984).
[7]
MUTAGENESIS OF ASN-584 AND ARG-588.
DOI=10.1016/0014-5793(91)81073-H; PubMed=1915850 [NCBI, ExPASy, EBI, Israel, Japan]
Despons L., Walter P., Senger B., Ebel J.-P., Fasiolo F.;
"Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase.";
FEBS Lett. 289:217-220(1991).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V01316; CAA24627.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y07777; CAA69086.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73049; CAA97293.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64597; SYBYMT.
RefSeq NP_011780.1; -.
3D structure databases
PDB
2HSN; X-ray; 2.20 A; A=1-160.[ExPASy / RCSB / EBI]
PDBsum 2HSN; -.
ModBase P00958.
Protein-protein interaction databases
DIP DIP:2211N; -.
IntAct P00958; 13.
Organism-specific databases
CYGD YGR264c; -.
SGD S000003496; MES1.
Yeast-GFP YGR264C.
Gene expression databases
ArrayExpress P00958; -.
GermOnline YGR264C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0017102; Cellular component: methionyl glutamyl tRNA synthetase complex (inferred from direct assay from SGD).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004825; Molecular function: methionine-tRNA ligase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006431; Biological process: methionyl-tRNA aminoacylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR015413; aa-tRNA-synt_I.
IPR001412; aa-tRNA-synth_I_CS.
IPR002304; Met-tRNA-synth_Ia.
IPR014729; Rossmann-like_a/b/a_fold.
IPR014758; tRNA-synt_met_N.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF09334; tRNA-synt_1g; 1.
Pfam graphical view of domain structure.
PRINTS PR01041; TRNASYNTHMET.
TIGRFAMs TIGR00398; metG; 1.
PROSITE PS00178; AA_TRNA_LIGASE_I; 1.
Proteomic databases
PeptideAtlas P00958; -.
Genome annotation databases
Ensembl YGR264C; Saccharomyces cerevisiae. [Contig view]
GeneID 853181; -.
GenomeReviews Y13135_GR; YGR264C.
KEGG sce:YGR264C; -.
NMPDR fig|4932.3.peg.2909; -.
Phylogenomic databases
HOGENOM P00958; -.
Other
LinkHub P00958; -.
NextBio 973317; -.
ProtoNet P00958.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   751  750     Methionyl-tRNA synthetase, cytoplasmic. PRO_0000139269
MOTIF   205   215  11     "HIGH" region. 
MOTIF   408   412  5     "KMSKS" region. 
BINDING   411   411        ATP (By similarity). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   373   373        Phosphoserine. 
MUTAGEN   584   584        N->D,Q: Abolishes aminoacylation activity. 
MUTAGEN   588   588        R->A,K,Q: Abolishes aminoacylation activity. 
CONFLICT   122   122        T -> A (in Ref. 1 and 3). 
STRAND   3     5  3      
STRAND   10    12  3      
HELIX   15    31  17      
STRAND   49    51  3      
STRAND   56    58  3      
HELIX   61    68  8      
TURN   73    76  4      
HELIX   78    86  9      
TURN   87    89  3      
HELIX   90    92  3      
STRAND   93    95  3      
HELIX   98   111  14      
HELIX   122   142  21      
HELIX   148   157  10      
Sequence information
Length: 751 AA [This is the length of the unprocessed precursor] Molecular weight: 85678 Da [This is the MW of the unprocessed precursor] CRC64: 11679C1AB8BB5E39 [This is a checksum on the sequence]
        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 

P00958 in FASTA format

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