Reviewed, UniProtKB/Swiss-Prot P00958 (SYMC_YEAST)

Names and origin

Protein names

Recommended name:
    Methionyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.10
Alternative name(s):
    Methionine--tRNA ligase
      Short name=MetRS

Gene names

Name:	MES1
Ordered Locus Names:	YGR264C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [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. Ref.8
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
Gene Ontology (GO)
Biological process	methionyl-tRNA aminoacylation Inferred from direct assay. Source: SGD
Cellular component	methionyl glutamyl tRNA synthetase complex Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW methionine-tRNA ligase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
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

1

1

Removed Ref.3

Chain

2 – 751

750

Methionyl-tRNA synthetase, cytoplasmic

PRO_0000139269

Regions

Motif

205 – 215

11

"HIGH" region

Motif

408 – 412

5

"KMSKS" region

Sites

Binding site

411

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.3

Modified residue

373

1

Phosphoserine Ref.9

Experimental info

Mutagenesis

584

1

N → D or Q: Abolishes aminoacylation activity. Ref.7

Mutagenesis

588

1

R → A, K or Q: Abolishes aminoacylation activity. Ref.7

Sequence conflict

122

1

T → A Ref.1

Sequence conflict

122

1

T → A Ref.3

Secondary structure

1

.

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.

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.

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751

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

10 – 12

3

Helix

15 – 31

17

Beta strand

49 – 51

3

Beta strand

56 – 58

3

Helix

61 – 68

8

Turn

73 – 76

4

Helix

78 – 86

9

Turn

87 – 89

3

Helix

90 – 92

3

Beta strand

93 – 95

3

Helix

98 – 111

14

Helix

122 – 142

21

Helix

148 – 157

10

Sequences

	Sequence		Length	Mass (Da)
	P00958-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 11679C1AB8BB5E39	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

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: 6341994] [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: 3905796] [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: 9090059] [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: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	"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: 6371805] [Abstract] Cited for: PROTEIN SEQUENCE OF 10-90.
[7]	"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: 1915850] [Abstract] Cited for: MUTAGENESIS OF ASN-584 AND ARG-588.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V01316 Genomic DNA. Translation: CAA24627.1.
Y07777 Genomic DNA. Translation: CAA69086.1.
Z73049 Genomic DNA. Translation: CAA97293.1.

PIR

SYBYMT. S64597.

RefSeq

NP_011780.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2211N.

IntAct

P00958. 12 interactions.

Proteomic databases

PeptideAtlas

P00958.

Genome annotation databases

Ensembl

YGR264C. Saccharomyces cerevisiae. [Contig view]

GeneID

853181.

GenomeReviews

Gene locus YGR264C in contig Y13135_GR.

KEGG

sce:YGR264C.

NMPDR

fig|4932.3.peg.2909.

Organism-specific databases

CYGD

YGR264c.

SGD

S000003496. MES1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P00958.

OMA

P00958. YINGIKH.

Enzyme and pathway databases

BRENDA

6.1.1.10. 250.

Gene expression databases

ArrayExpress

P00958.

GermOnline

YGR264C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR002304. Met-tRNA-synth_Ia.
IPR018285. Met-tRNA-synth_N.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

Pfam

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

PRINTS

PR01041. TRNASYNTHMET.

TIGRFAMs

TIGR00398. metG. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

973317.

Entry information

Entry name

SYMC_YEAST

Accession

Primary (citable) accession number: P00958

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 98 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)