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O29979 (SYE_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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:AF_0260
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length551 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 – 551551Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119713

Regions

Motif100 – 11011"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
O29979 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A985A300C6B68F2E

FASTA55164,402
        10         20         30         40         50         60 
MKEVIMKYVV QNAAKYGKAS EKAVMGKVMA ENPELRKKAK EVLELVKECI TEFEALSEEV 

        70         80         90        100        110        120 
RKELIKKYSM DSEAKRELET KKLPELEGAE KGKVVMRFAP NPNGPPTLGS ARGIIVNGEY 

       130        140        150        160        170        180 
AKMYEGKYII RFDDTDPRTK RPMIEAYEWY LEDIEWLGYK PDEVIYASRR IPIYYDYARK 

       190        200        210        220        230        240 
LIEMGKAYTC FCSQEEFKKF RDSGEECPHR NISVEDTLEV WERMLEGDYE EGEVVLRIKT 

       250        260        270        280        290        300 
DMRHKDPAIR DWVAFRIIKE SHPLVGDKYV VYPTLDFESA IEDHLLGITH IIRGKDLIDS 

       310        320        330        340        350        360 
ERRQRYIYEY FGWIYPITKH WGRVKIFEFG KLSTSSIKKD IERGKYEGWD DPRLPTLRAF 

       370        380        390        400        410        420 
RRRGFEPEAI KSFFLSLGVG ENDVSVSLKN LYAENRKIID RKANRYFFIW GPVKIEIVNL 

       430        440        450        460        470        480 
PEKKEVELPL NPHTGEKRRL KGERTIYVTK DDFERLKGQV VRLKDFCNVL LDEKAEFMGF 

       490        500        510        520        530        540 
ELEGVKKGKN IIHWLPESEA IKGKVIGERE AEGLVERNAV RDVGKVVQFE RFAFCKVESA 

       550 
DEELVAVYTH P 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB90966.1.
PIRD69282.
RefSeqNP_069098.1. NC_000917.1.

3D structure databases

ProteinModelPortalO29979.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF0260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90966; AAB90966; AF_0260.
GeneID1483474.
KEGGafu:AF0260.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-267-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 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.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
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_ARCFU
AccessionPrimary (citable) accession number: O29979
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 88 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