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A8F197 (SYE1_RICM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:RMA_0462
OrganismRickettsia massiliae (strain Mtu5) [Complete proteome] [HAMAP]
Taxonomic identifier416276 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length447 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 – 447447Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367758

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
A8F197 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: DA93A01CFFEF542F

FASTA44751,768
        10         20         30         40         50         60 
MTKVITRFAP SPTGMLHVGN IRAALLNWLY AKKHNGQFIL RFDDTDLERS KQEYKDAIEE 

        70         80         90        100        110        120 
DLKFLNINWD QTFNQLSRLS RYDEIKNLLL DKKRLYACYE TPEELELKRK FQLSKGLPPI 

       130        140        150        160        170        180 
YDRASLNLTE EQAKKYIEQG RKPHYRFLVN HELINWHDMI KGEVKYDGKA LSDPIVIRAD 

       190        200        210        220        230        240 
GSMTYMLCSV IDDIDYDITH IIRGEDHVSN TAIQIQMFEA LNTTPPTFGH LSLIINKDEK 

       250        260        270        280        290        300 
ISKRVGGFEI ATLRKEVGIE AMAIASFFSL LGSSAQILPY KSMEKLANQF EISSFSKSPT 

       310        320        330        340        350        360 
IYQPEDLERL NHKLLISLDF DTVKERLKEI NAEYIDENFW LSVSPNLQKL RDVKDWWEIC 

       370        380        390        400        410        420 
HQTPNVENLN LDKEYLKQAA ELLPKGEITK DSWSIWTKEI TNITGRKGKE LFLPLRLALT 

       430        440 
ARESGPEITG VLPLIDREEI IKRLTSA 

« Hide

References

[1]"Lateral gene transfer between obligate intracellular bacteria: evidence from the Rickettsia massiliae genome."
Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.
Genome Res. 17:1657-1664(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mtu5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000683 Genomic DNA. Translation: ABV84683.1.
RefSeqYP_001499230.1. NC_009900.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416276.RMA_0462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV84683; ABV84683; RMA_0462.
GeneID5665154.
KEGGrms:RMA_0462.
PATRIC17895183. VBIRicMas83254_0578.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAAGRLYPC.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycRMAS416276:GJD3-467-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_RICM5
AccessionPrimary (citable) accession number: A8F197
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 42 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