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A8GX08 (SYE2_RICB8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:A1I_05405
OrganismRickettsia bellii (strain OSU 85-389) [Complete proteome] [HAMAP]
Taxonomic identifier391896 [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.

Sequence caution

The sequence ABV79408.1 differs from that shown. Reason: Erroneous initiation.

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_0000367755

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
A8GX08 [UniParc].

Last modified March 24, 2009. Version 2.
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]"Complete genome sequencing of Rickettsia bellii."
Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU 85-389.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000849 Genomic DNA. Translation: ABV79408.1. Different initiation.
RefSeqYP_001496445.1. NC_009883.1.

3D structure databases

ProteinModelPortalA8GX08.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391896.A1I_05405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV79408; ABV79408; A1I_05405.
GeneID5645911.
KEGGrbo:A1I_05405.
PATRIC17880139. VBIRicBel35792_1126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRBEL391896:GH75-1018-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_RICB8
AccessionPrimary (citable) accession number: A8GX08
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 43 of the entry and version 2 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