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Q1RJC6 (SYE2_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:RBE_0457
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length464 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 – 464464Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000277972

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RJC6 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 3287F4E1269D22A0

FASTA46452,642
        10         20         30         40         50         60 
MTNNVITRFA PSPTGFLHIG SARTALFNYL FAKHNNGKFL LRIEDTDKER STEAAVEAIF 

        70         80         90        100        110        120 
SGLKWLGLNW DDEVVFQSKR NDLYKEAALK LLAEGKAYYC FTPQEEIEKQ RQEALENKQH 

       130        140        150        160        170        180 
FIFNSKWRDK TSDTYPKDIK PVIRLKTPSS GSITIHDTLQ GDVVIENCHI DDMVLLRSDG 

       190        200        210        220        230        240 
TATYMLAVVV DDHDMGITHI IRGDDHLTNA ARQIAIYNAF GYHVPIMTHI PLIHGADGAK 

       250        260        270        280        290        300 
LSKRHGALGV EAYKDMGYLP ESLCNYLLRL GWSHGDDEII QMDQAIEWFN LDSLGKSPAR 

       310        320        330        340        350        360 
LDFTKMNSLN SHYLRMLDED SLITKILEIL NRNYKVSEQE VNYIRRGLQG LLVRSETLLD 

       370        380        390        400        410        420 
LAKLAKIYLV NIPVAYESEA KEIIANCDKN LINNVVQGLE KLERFDKESV QDEFKKIAAA 

       430        440        450        460 
NSLKLNEVMK PVRALITGMV GSPSVFEIAE ILGKENILKR LEIK 

« 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: ABE04538.1.
RefSeqYP_537627.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RJC6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04538; ABE04538; RBE_0457.
GeneID3996031.
KEGGrbe:RBE_0457.
PATRIC17882293. VBIRicBel102610_0520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAIQECIND.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-470-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE2_RICBR
AccessionPrimary (citable) accession number: Q1RJC6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 58 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