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C4ZSJ8 (SYM_ECOBW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine--tRNA ligase

EC=6.1.1.10
Alternative name(s):
Methionyl-tRNA synthetase
Short name=MetRS
Gene names
Name:metG
Ordered Locus Names:BWG_1900
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation By similarity. HAMAP-Rule MF_00098

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00098

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00098

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00098.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
tRNA-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmethionyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 677677Methionine--tRNA ligase HAMAP-Rule MF_00098
PRO_1000202756

Regions

Domain575 – 677103tRNA-binding
Motif15 – 2511"HIGH" region HAMAP-Rule MF_00098
Motif333 – 3375"KMSKS" region HAMAP-Rule MF_00098

Sites

Metal binding1461Zinc By similarity
Metal binding1491Zinc By similarity
Metal binding1591Zinc By similarity
Metal binding1621Zinc By similarity
Binding site3361ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C4ZSJ8 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 363F3324AFD3202C

FASTA67776,255
        10         20         30         40         50         60 
MTQVAKKILV TCALPYANGS IHLGHMLEHI QADVWVRYQR MRGHEVNFIC ADDAHGTPIM 

        70         80         90        100        110        120 
LKAQQLGITP EQMIGEMSQE HQTDFAGFNI SYDNYHSTHS EENRQLSELI YSRLKENGFI 

       130        140        150        160        170        180 
KNRTISQLYD PEKGMFLPDR FVKGTCPKCK SPDQYGDNCE VCGATYSPTE LIEPKSVVSG 

       190        200        210        220        230        240 
ATPVMRDSEH FFFDLPSFSE MLQAWTRSGA LQEQVANKMQ EWFESGLQQW DISRDAPYFG 

       250        260        270        280        290        300 
FEIPNAPGKY FYVWLDAPIG YMGSFKNLCD KRGDSVSFDE YWKKDSTAEL YHFIGKDIVY 

       310        320        330        340        350        360 
FHSLFWPAML EGSNFRKPSN LFVHGYVTVN GAKMSKSRGT FIKASTWLNH FDADSLRYYY 

       370        380        390        400        410        420 
TAKLSSRIDD IDLNLEDFVQ RVNADIVNKV VNLASRNAGF INKRFDGVLA SELADPQLYK 

       430        440        450        460        470        480 
TFTDAAEVIG EAWESREFGK AVREIMALAD LANRYVDEQA PWVVAKQEGR DADLQAICSM 

       490        500        510        520        530        540 
GINLFRVLMT YLKPVLPKLT ERAEAFLNTE LTWDGIQQPL LGHKVNPFKA LYNRIDMRQV 

       550        560        570        580        590        600 
EALVEASKEE VKAAAAPVTG PLADDPIQET ITFDDFAKVD LRVALIENAE FVEGSDKLLR 

       610        620        630        640        650        660 
LTLDLGGEKR NVFSGIRSAY PDPQALIGRH TIMVANLAPR KMRFGISEGM VMAAGPGGKD 

       670 
IFLLSPDAGA KPGHQVK 

« Hide

References

[1]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001396 Genomic DNA. Translation: ACR63756.1.
RefSeqYP_002927096.1. NC_012759.1.

3D structure databases

ProteinModelPortalC4ZSJ8.
SMRC4ZSJ8. Positions 5-548, 571-676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595496.BWG_1900.

Chemistry

BindingDBC4ZSJ8.

Proteomic databases

PRIDEC4ZSJ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR63756; ACR63756; BWG_1900.
GeneID7952481.
KEGGebw:BWG_1900.
PATRIC18273113. VBIEscCol60876_2082.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200400.
KOK01874.
OMAANEWGNL.
OrthoDBEOG6CVV9B.
ProtClustDBPRK00133.

Enzyme and pathway databases

BioCycECOL595496:GI18-1967-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
2.40.50.140. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00098. Met_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR023458. Met-tRNA_ligase_1.
IPR014758. Met-tRNA_synth.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PfamPF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00398. metG. 1 hit.
TIGR00399. metG_C_term. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYM_ECOBW
AccessionPrimary (citable) accession number: C4ZSJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries