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Q0S2G8 (SYE_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:RHA1_ro06493
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length491 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 – 491491Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330993

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif256 – 2605"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2591ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0S2G8 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 949B8EFC6A3BEA60

FASTA49154,212
        10         20         30         40         50         60 
MTTSEVRVRF CPSPTGTPHV GLVRTALFNW AFARHNGGSF VFRIEDTDAA RDSEESYQAI 

        70         80         90        100        110        120 
LDALRWLGLN WDEGPEVGGP YEPYRQSQRR DLHLDVVAKL LAAGEAYESF STPEEVEERH 

       130        140        150        160        170        180 
KAAGRDPKLG YDNFDRDLTP DQRQAFLDEG RKPVVRLRMP DHDLTWDDLV RGETTFKAGT 

       190        200        210        220        230        240 
VPDFALTRGN GIPLYTLVNP VDDALMKITH VLRGEDLLSS TPRQLALYEA MQRIGVADFT 

       250        260        270        280        290        300 
PRFGHLPFVM GQGNKKLSKR DPESNLFIHR DRGFVPEGLL NYLALLGWGI SDDHDVFSLD 

       310        320        330        340        350        360 
EMVAAFDISK VNSNPARFDQ KKADAINAEH IRLLEPADFA ARLRAFLTLH GHLGETVDES 

       370        380        390        400        410        420 
VFATAAELVQ TRIVVLSDAW DLLKFLFVDE ADFAIDPAAA AKNLGADSAP VLDAALASLD 

       430        440        450        460        470        480 
AVEAWDAASL EEALKTALVD ELGLKPRKAF APVRVAVTGS HISPPLYESM ELLGRDVSLS 

       490 
RLRSARAGVA G 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000431 Genomic DNA. Translation: ABG98268.1.
RefSeqYP_706426.1. NC_008268.1.

3D structure databases

ProteinModelPortalQ0S2G8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING101510.RHA1_ro06493.

Proteomic databases

PRIDEQ0S2G8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG98268; ABG98268; RHA1_ro06493.
GeneID4224044.
KEGGrha:RHA1_ro06493.
PATRIC23211949. VBIRhoJos26306_6548.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAITESCRY.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycRJOS101510:GJJ1-6490-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 nameSYE_RHOSR
AccessionPrimary (citable) accession number: Q0S2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 62 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