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Q9HQI1 (SYE_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:VNG_1153G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

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
Reference 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_0000119715

Regions

Motif114 – 12411"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q9HQI1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E844ED37F8F46776

FASTA58665,312
        10         20         30         40         50         60 
MDDELRERVR RAAERAALFN ALKHGSDAQV GAIMGPMMGE HPDFRAHGDE IPGVIAPVIE 

        70         80         90        100        110        120 
DVNGMSDDEQ RARLAELAPE DVEELDSEDE GDDHALPALP NAEAYDEVRM RCAPNPNGPW 

       130        140        150        160        170        180 
HVGHARMPSV IGTYKQRYDG SFVVRFDDTD PETKRPDLDA YDQILEDLSY LGFEADEVLT 

       190        200        210        220        230        240 
ASDRVETYYE HARRLIGMGG AYTCSCPGAE FSDLKNSGEA CPHRDKDPET VADEFEAMVD 

       250        260        270        280        290        300 
GEYNSGEMVL RVKTDITHKN PALRDWVAFR MVDTPHPRDA ASGYRCWPML DFQSGVDDHR 

       310        320        330        340        350        360 
TGVTHIIRGI DLQDSAKRQR FLYEYFGWEY PEVVHWGHVQ LDAYDVAMST STIKERIAAG 

       370        380        390        400        410        420 
ELEGWDDPRA PTMQSIRRRG IRGAAVVDAM VELGTSSSDV ELAMSAVYAN NRDLVDDTAP 

       430        440        450        460        470        480 
RQFLVRDGFE ARGEGPEESH EAVEVPVDDG PDEATPQVHP EHPDRGDREI PVGERVLVEA 

       490        500        510        520        530        540 
TDLPAAGDRV WLKGYGPVRY DGERFAFLDA DIDIVREEGV DVVQWVPAEH NVDVRLRTMD 

       550        560        570        580 
GDVTGYAEPG FADRDADEIV QFVRVGFARV DAHRDGGASV AYFTHP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004437 Genomic DNA. Translation: AAG19534.1.
PIRB84271.
RefSeqNP_280054.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HQI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64091.VNG1153G.

Proteomic databases

PaxDbQ9HQI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG19534; AAG19534; VNG_1153G.
GeneID1447835.
KEGGhal:VNG1153G.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAAFRIIDT.
PhylomeDBQ9HQI1.

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_HALSA
AccessionPrimary (citable) accession number: Q9HQI1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 76 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