Methionine--tRNA ligase, cytoplasmic - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P00958 (SYMC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 137. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	751 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 85000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	methionyl-tRNA aminoacylation Inferred from direct assay PubMed 3312199. Source: SGD
Cellular_component	methionyl glutamyl tRNA synthetase complex Inferred from direct assay PubMed 11069915. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW methionine-tRNA ligase activity Inferred from direct assay PubMed 3312199. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRP40	P33203	1	EBI-18762,EBI-701

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 751

750

Methionine--tRNA ligase, cytoplasmic

PRO_0000139269

Regions

Motif

205 – 215

"HIGH" region

Motif

408 – 412

"KMSKS" region

Sites

Binding site

411

ATP By similarity

Amino acid modifications

Modified residue

N-acetylserine Ref.3

Modified residue

373

Phosphoserine Ref.10

Experimental info

Mutagenesis

584

N → D or Q: Abolishes aminoacylation activity. Ref.8

Mutagenesis

588

R → A, K or Q: Abolishes aminoacylation activity. Ref.8

Sequence conflict

122

T → A Ref.1

Sequence conflict

122

T → A Ref.3

Secondary structure

751

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00958 [UniParc].

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

FASTA

751

85,678

        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' referencesShow '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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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].
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, MASS SPECTROMETRY.
+	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.

PIR

SYBYMT. S64597.

RefSeq

NP_011780.3. NM_001181393.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HSN	X-ray	2.20	A	2-159	[»]

ProteinModelPortal

P00958.

SMR

P00958. Positions 1-160, 199-739.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2211N.

IntAct

P00958. 12 interactions.

MINT

MINT-648422.

STRING

4932.YGR264C.

Proteomic databases

PaxDb

P00958.

PeptideAtlas

P00958.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR264C; YGR264C; YGR264C.

GeneID

853181.

KEGG

sce:YGR264C.

Organism-specific databases

SGD

S000003496. MES1.

Phylogenomic databases

eggNOG

COG0143.

GeneTree

ENSGT00550000075017.

HOGENOM

HOG000200402.

K01874.

OMA

HISTTEY.

OrthoDB

EOG4X0R1H.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30933-MONOMER.

BRENDA

6.1.1.10. 984.

Gene expression databases

Genevestigator

P00958.

GermOnline

YGR264C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.50.620. 2 hits.

InterPro

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.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]

Pfam

PF09635. MetRS-N. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]

PRINTS

PR01041. TRNASYNTHMET.

SUPFAM

SSF47323. tRNAsyn_1a_bind. 1 hit.

TIGRFAMs

TIGR00398. metG. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00958.

NextBio

973317.

Entry information

Entry name

SYMC_YEAST

Accession

Primary (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:	May 29, 2013
This is version 137 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents