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Q1WSS4 (SYE_LACS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:LSL_1248
OrganismLactobacillus salivarius (strain UCC118) [Complete proteome] [HAMAP]
Taxonomic identifier362948 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-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

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001915

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1WSS4 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 33F567BDDB0A918E

FASTA49557,068
        10         20         30         40         50         60 
MAKNKIRVRY APSPTGHLHI GNARTALFNY LFARHNKGTF VLRIEDTDTK RNIADGEKSQ 

        70         80         90        100        110        120 
MDNLEWLGID WDEGPDKPGK YGPYRQSERK DIYKPLIQEL LDKDLAYESF MTEEELQAQR 

       130        140        150        160        170        180 
EEQKARGEAP RYVYEYEGMS KEEIKKAQDE ARAKGLKPVV RIRVPHNKTY EWDDIVKGKI 

       190        200        210        220        230        240 
SFLSDTIGGD FVIQKRDGMP TYNFAVVVDD HLMEITHVLR GDDHVANTPK QLVVYEAFGW 

       250        260        270        280        290        300 
KAPEFGHMSL IINTETGKKL SKRDETVLQF IEQYRELGYL PDAMFNFITL LGWSPVGESE 

       310        320        330        340        350        360 
IFNKQEFIKM FDAKRLSKSP AAFDGKKLEW INNQYVKAAK EDEIMDSSLR QLIKAGKVQA 

       370        380        390        400        410        420 
DPDAYTIEWA RKLISLYKQQ MSYTGQIVEM ADVFFNEPPV LSEDAKKELA DESAAIVLKE 

       430        440        450        460        470        480 
FAERVKDLPI FDAVEIQNTI RSIQKDTKIK GRKLYMPIRI ATTREMHGPE LAPSIELLGR 

       490 
EKALKHLKQT LEEMN 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000233 Genomic DNA. Translation: ABE00055.1.
RefSeqYP_536138.1. NC_007929.1.

3D structure databases

ProteinModelPortalQ1WSS4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362948.LSL_1248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE00055; ABE00055; LSL_1248.
GeneID3977280.
KEGGlsl:LSL_1248.
PATRIC22279405. VBILacSal43464_1322.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLSAL362948:GJDJ-1329-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_LACS1
AccessionPrimary (citable) accession number: Q1WSS4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 2, 2006
Last modified: February 19, 2014
This is version 61 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