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Reviewed, UniProtKB/Swiss-Prot Q1RIM2 (SYE1_RICBR)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 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 lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsia

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000277971

Regions

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

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RIM2-1 [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: 16703114] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000087 Genomic DNA. Translation: ABE04792.1.
RefSeqYP_537881.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3995311.
GenomeReviewsGene locus RBE_0711 in contig CP000087_GR.
KEGGrbe:RBE_0711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1RIM2.
OMAQ1RIM2. LRLDDTD.

Enzyme and pathway databases

BioCycRBEL336407:RBE_0711-MON.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 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: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Rickettsia bellii strain RML369-C

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents