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Q1RIM2 (SYE1_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:RBE_0711
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length445 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 – 445445Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000277971

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RIM2 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 30EBB08D2FBF8905

FASTA44551,851
        10         20         30         40         50         60 
MTKVITRFAP SPTGMLHVGN IRAALLNWLY AKKHDGQFIL RFDDTDLERS KQEYKDAIRA 

        70         80         90        100        110        120 
DLKFLNLNWD QTFNQLSRLS RYDEIKKLLL DKKRLYACYE TPEELELKRK FQLSKGLPPI 

       130        140        150        160        170        180 
YDRAALNLTE DQIQKYIEQG RKPHYRFLVN HEPITWHDMI KGEVKYEGKA LSDPIVIRAD 

       190        200        210        220        230        240 
GSMTYMLCSV IDDVDYEITH IIRGEDHVSN TAIQIQMFEA LDKYPPTFGH LSLIINKDEK 

       250        260        270        280        290        300 
ISKRVGGFEI ATLREEVGLE AMAIASFFSL LGSSAQIIPH KKMDELVKHF EISSFSKSPT 

       310        320        330        340        350        360 
IYQPEDLERL NHKLLISLEF NEVKDRLKEI DAEYIDENFW LSVRPNLKKL FDAKDWWEIC 

       370        380        390        400        410        420 
HKTPNIQDLN LDKEYLKQAA ELLPEEEITT ETWGIWTKKL AAITNRKGKE LFLPLRLALT 

       430        440 
GKESGPEISK VLPLIKREEI VKRLT 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE04792.1.
RefSeqYP_537881.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RIM2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04792; ABE04792; RBE_0711.
GeneID3995311.
KEGGrbe:RBE_0711.
PATRIC17882902. VBIRicBel102610_0816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMARIALFNW.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-732-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 nameSYE1_RICBR
AccessionPrimary (citable) accession number: Q1RIM2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: May 14, 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

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries