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Q14JD8 (SYE_FRAT1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:FTF0307
OrganismFrancisella tularensis subsp. tularensis (strain FSC 198) [Complete proteome] [HAMAP]
Taxonomic identifier393115 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length468 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001900

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding971Zinc By similarity
Metal binding991Zinc By similarity
Metal binding1241Zinc By similarity
Metal binding1261Zinc By similarity
Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q14JD8 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: B5D3AC570C11C4A2

FASTA46852,953
        10         20         30         40         50         60 
MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ EAVDAILDGM 

        70         80         90        100        110        120 
SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS KERLEELREY QQANNLKTGY 

       130        140        150        160        170        180 
DGKCRDANYI PQQGESYVVR FKNPQDGVVS WDDAVKGRIS ISNHELDDMI IQRADGSPTY 

       190        200        210        220        230        240 
NFCVVVDDID MAITHIIRGD DHVNNTPKQI NIYKALNANV PIFAHVPMIL GPDGAKLSKR 

       250        260        270        280        290        300 
HGAVNVMQYR EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE 

       310        320        330        340        350        360 
KLKWLNKHYI KESKFDDIQT EVEYHFAKTG LDISNGPDLK ELVAVMAEKV DTLVELAEKS 

       370        380        390        400        410        420 
SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ QWQDPDVLHN IVSTTAEQCQ 

       430        440        450        460 
VGMGKVGMPL RVAITGSGQS PDIGITLKLL GKNKVVARLT KALEELCK 

« Hide

References

[1]"Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FSC 198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286280 Genomic DNA. Translation: CAL08323.1.
RefSeqYP_666488.1. NC_008245.1.

3D structure databases

ProteinModelPortalQ14JD8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393115.FTF0307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL08323; CAL08323; FTF0307.
GeneID4199800.
KEGGftf:FTF0307.
PATRIC17959315. VBIFraTul133500_0342.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycFTUL393115:GJUT-314-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_FRAT1
AccessionPrimary (citable) accession number: Q14JD8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 59 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