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Q8Y065 (SYE_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:RSc1179
ORF Names:RS04541
OrganismRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier267608 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length465 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 CAD14881.1 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 – 465465Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119630

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y065 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 772FB42CAE37EB9C

FASTA46552,199
        10         20         30         40         50         60 
MTQRVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGDFI LRIEDTDVER STQEAVDVIL 

        70         80         90        100        110        120 
EAMDWLGLDI DEGPFYQMQR MDRYREVIAQ MVAQDLAYPC YMSTEELDAL REAQRVRGEK 

       130        140        150        160        170        180 
PRYDGTWRPE PGKVLPTPPA GVQPVIRFKN PIGGSVVWDD AVKGRIEISN DELDDLVIAR 

       190        200        210        220        230        240 
PDGTPTYNFC VVVDDMDMRI THVIRGDDHV NNTPRQINIL RALGGTPPIY AHLPTVLNEQ 

       250        260        270        280        290        300 
GEKMSKRHGA MSVTGYRDAG YLPEAVVNYL ARLGWAHGDA EIFSREQFVE WFDLEHLGKS 

       310        320        330        340        350        360 
PAQYNPEKLA WLNNHYIKQA DNARLAELVK PFIEALGGRV EGGPQLADVM ALVKDRANTL 

       370        380        390        400        410        420 
QEVAQTALLF YRTEISVAPE LAAQHLTDEV RPGIMALADK LGTLPEWKRE AIGAAFKEVL 

       430        440        450        460 
GAHGWKMPKL AMPVRLLVAG QLQTPSIDAV LELFGREVVL RRLAG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646052 Genomic DNA. Translation: CAD14881.1. Different initiation.
RefSeqNP_519300.1. NC_003295.1.

3D structure databases

ProteinModelPortalQ8Y065.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267608.RSc1179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD14881; CAD14881; RSc1179.
GeneID1219995.
KEGGrso:RSc1179.
PATRIC20260951. VBIRalSol70888_1198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRSOL267608:GCVU-1193-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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 nameSYE_RALSO
AccessionPrimary (citable) accession number: Q8Y065
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: May 14, 2014
This is version 73 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