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Q1QY92 (SYE_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:Csal_1211
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length494 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 – 494494Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001888

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QY92 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 27407965240B2A9E

FASTA49456,182
        10         20         30         40         50         60 
MTVRTRIAPS PTGDPHVGTA YIALFNLCFA RQHGGQFILR IEDTDRVRST AESEQMILDS 

        70         80         90        100        110        120 
LRWLGLEWDE GPDVGGPHGP YRQSERGDIY AQYAQQLLDA GHAFKCYRTS EELDELREAR 

       130        140        150        160        170        180 
KAAGLHLALK PADLALPDDE VARREREQWP YVVRMKVPGE GSCVVSDMLR GEIEVDWAQV 

       190        200        210        220        230        240 
DAQILLKSDG MPTYHLANVV DDHLMGITHV MRGEEWINSA PKHKLLYEYF DWPMPTLCHM 

       250        260        270        280        290        300 
PLLRNPDKSK LSKRKNPTSI NYYRRMGFLP QAVTNYLGRM GWSMPDDREK FTLEEMMANF 

       310        320        330        340        350        360 
DIQRVSLGGP VFDLEKLTWL NGVYIREDLD DAALLQALRE WAFNDAYVNQ ILPQVRPRIS 

       370        380        390        400        410        420 
TLSDVMPLAG HFFSGVPPLE ASSFDGIKLE HETLLKLLQF LTWRLEGVSR WEKDVLLDDV 

       430        440        450        460        470        480 
KALAEAFDMK MKAFLAPVFI AVTGSATSTS VLDAMAILGS DMTRARLRHA IEVLGGVSKK 

       490 
QAKRFEKEYR QLQV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000285 Genomic DNA. Translation: ABE58566.1.
RefSeqYP_573265.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1QY92.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290398.Csal_1211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE58566; ABE58566; Csal_1211.
GeneID4027356.
KEGGcsa:Csal_1211.
PATRIC21446198. VBIChrSal113723_1224.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

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_CHRSD
AccessionPrimary (citable) accession number: Q1QY92
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 62 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