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Q054R6 (SYM_LEPBL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LBL_0593
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]
Taxonomic identifier355276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length704 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.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Contains 1 tRNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 704704Methionine--tRNA ligase HAMAP-Rule MF_00098
PRO_0000331846

Regions

Domain603 – 704102tRNA-binding
Motif17 – 2711"HIGH" region HAMAP-Rule MF_00098
Motif348 – 3525"KMSKS" region HAMAP-Rule MF_00098

Sites

Metal binding1481Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding1611Zinc By similarity
Metal binding1641Zinc By similarity
Binding site3511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q054R6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 2D59CFD57EA68102

FASTA70479,881
        10         20         30         40         50         60 
MNSSSIQRKI LVTSALPYAN GPIHLGHVLE GIQTDIWVRF QKAIGNECYF FCADDTHGTP 

        70         80         90        100        110        120 
VMLAARKEKI TPEQLIERVG QEHYTDLTSF GINYDNYDST HSKANQEISK DIYLKLKEKG 

       130        140        150        160        170        180 
HISKRSIEQA YCEKDRMFLP DRFIKGTCPN CNSKNQYGDN CEVCGATYNP KDLIDSHCTL 

       190        200        210        220        230        240 
CGTPPVVKNS DHIFFKLGNF HKKTEQSNVD FDLQSWIETS EAVSESEGVK KKLKEWFDAG 

       250        260        270        280        290        300 
LQDWDISRDG PYFGFEIPSE KNKYFYVWLD APVGYMASSK NFFEKNFPNE PNKFDSFWKD 

       310        320        330        340        350        360 
KNSEIVHFIG KDILYFHTLF WPAMLEGSGY RSPSKIHVHG FIGVNGEKMS KSRGTFIKAK 

       370        380        390        400        410        420 
TFAKFLDAEH LRFYLAAKLG PGMDDIDLSF DDFVNKVNAD LVGNLINSVS RVSTTILDTL 

       430        440        450        460        470        480 
DRTLGTVSEE GLALLEEILT QPVKTGTRDD SIQNIIKTAY EQRNYAKVMR EITRLGDRVN 

       490        500        510        520        530        540 
RYVNDNAPWK LIKENPEKAR EIVTAVLNAS RFLAIYLYPV VPKISEQIYK LLNLKGSPEF 

       550        560        570        580        590        600 
KDLDKSRILE KTKINPYEMI TKRVDEKAIK VMLEENKQSE HPKKEEIPKS SNKEEGIEIS 

       610        620        630        640        650        660 
IEELSKVELR VGEIVEAKPV EGADKLVNVK VDLGELGIKN VFAGIKIAYQ PENLKGLKVV 

       670        680        690        700 
VVANLKPRKM KFGISEAMLL ASGEGESLSL FVPHKDAKPG DRLK 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L550.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000348 Genomic DNA. Translation: ABJ78179.1.
RefSeqYP_797112.1. NC_008508.1.

3D structure databases

ProteinModelPortalQ054R6.
SMRQ054R6. Positions 141-166.
ModBaseSearch...

Protein-protein interaction databases

STRING355276.LBL_0593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ78179; ABJ78179; LBL_0593.
GeneID4408426.
KEGGlbl:LBL_0593.
PATRIC22364510. VBILepBor75619_0728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200400.
KOK01874.
OMARMHGHEV.
ProtClustDBPRK00133.

Enzyme and pathway databases

BioCycLBOR355276:GHUQ-888-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00098. Met_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
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.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00398. metG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYM_LEPBL
AccessionPrimary (citable) accession number: Q054R6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 14, 2006
Last modified: May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families