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Q18GA5 (SYE_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:HQ_2888A
OrganismHaloquadratum walsbyi (strain DSM 16790 / HBSQ001) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum

Protein attributes

Sequence length586 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

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367800

Regions

Motif119 – 12911"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q18GA5 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 8C08E0AC6BEEE65B

FASTA58665,819
        10         20         30         40         50         60 
MTIDDELRDR IKRSAKKHAL LNAVKHKSDA EVGAIMGPLM GENPEFRPHG DAIPGIVSGV 

        70         80         90        100        110        120 
VSQINDLSVD ERRSRLETIA PEALTDIESE DTTDTYDLPS LPGVSDDEPT QSVRMRAAPN 

       130        140        150        160        170        180 
PNGPWHIGHA RMPAVIGTYS NRYDGSFIIR FDDTDPETKR PDLDAYDDIL EDVAYLGFEP 

       190        200        210        220        230        240 
DDVIRASDRL ELYYARAREL IDAGGAYTCS CSGEHFSKLK NAGEACPHRE KSVNQTQTEF 

       250        260        270        280        290        300 
EAMIHGEYSA GEMVLRVRTD IEHKNPALRD WVAFRLIDTP HPRPQAADYR CWPMLDFQSG 

       310        320        330        340        350        360 
IDDHETGVTH IIRGIDLQDS AKRQRFVYDY FDWEYPEVVH WGHINVDEYD VSLSTSTLIE 

       370        380        390        400        410        420 
KIETGELDGW DDPRAPTLQS LRRRGIKGDA IVEAMINLGT STTNVELSMS SIYSNNRQHI 

       430        440        450        460        470        480 
DAKADRYFFV RNGETFTLET ASEDTIAGHP PLHPDNPERG ERVVPVTDGI TIEPADVPAD 

       490        500        510        520        530        540 
GDRVWLKGYA CVRRDDNHFR TTNDGIEVVR EGDVDVIHWA PAPESSASIS VRMRTPDGDI 

       550        560        570        580 
TGIAEPDLTD AEIDDIVQFE RVGFARIDTK DEQSLDTDMT VYWTHP 

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790 / HBSQ001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180088 Genomic DNA. Translation: CAJ52995.1.
RefSeqYP_658596.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18GA5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362976.HQ2888A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ52995; CAJ52995; HQ_2888A.
GeneID4194047.
KEGGhwa:HQ2888A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAYLGWDDP.

Enzyme and pathway databases

BioCycHWAL362976:GJSR-1995-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYE_HALWD
AccessionPrimary (citable) accession number: Q18GA5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 60 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