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B5R0E7 (SYM_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 43. 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:SEN2148
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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_1000093727

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
B5R0E7 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 948CC4D95594D4FE

FASTA67776,288
        10         20         30         40         50         60 
MTQVAKKILV TCALPYANGS IHLGHMLEHI QADVWVRYQR MRGHEVNFIC ADDAHGTPIM 

        70         80         90        100        110        120 
LKAQQLGITP EQMIGEMSQE HQTDFAGFNI SYDNYHSTHS DENRELSELI YTRLKENGFI 

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

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

       250        260        270        280        290        300 
FEIPNAPGKY FYVWLDAPIG YMGSFKNLCD KRGDTTSFDE YWKKDSDAEL YHFIGKDIVY 

       310        320        330        340        350        360 
FHSLFWPAML EGSHFRKPTN LFVHGYVTVN GAKMSKSRGT FIKASTWLKH FDADSLRYYY 

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

       430        440        450        460        470        480 
TFTDAAAVIG EAWESREFGK AIREIMALAD VANRYVDEQA PWVVAKQEGR DADLQAICSM 

       490        500        510        520        530        540 
GINLFRVLMT YLKPVLPTLS ERVEAFLNSE LNWDAIEQPL LSHKVNTFKA LYNRIDMKQV 

       550        560        570        580        590        600 
EALVEASKEE VKAAAAPVTG PLADFPIQET ITFDDFAKID LRVALIENAE FVEGSDKLLR 

       610        620        630        640        650        660 
LTLDLGGEKR NVFSGIRSAY PDPQALIGRQ TVMVANLAPR KMRFGVSEGM VMAAGPGGKD 

       670 
IFLLSPDDGA KPGQQVK 

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR33733.1.
RefSeqYP_002244240.1. NC_011294.1.

3D structure databases

ProteinModelPortalB5R0E7.
SMRB5R0E7. Positions 5-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN2148.

Proteomic databases

PRIDEB5R0E7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR33733; CAR33733; SEN2148.
PATRIC32334795. VBISalEnt14964_2172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200400.
OMANQCIYVC.
OrthoDBEOG6CVV9B.

Enzyme and pathway databases

BioCycSENT550537:GJFI-2177-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
2.20.28.20. 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.
IPR029038. MetRS_Zn.
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.
SSF57770. SSF57770. 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_SALEP
AccessionPrimary (citable) accession number: B5R0E7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: June 11, 2014
This is version 43 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