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Q5GSI3 (SYE2_WOLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:Wbm0453
OrganismWolbachia sp. subsp. Brugia malayi (strain TRS) [Complete proteome] [HAMAP]
Taxonomic identifier292805 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length453 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 – 453453Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119702

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif232 – 2365"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5GSI3 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: E5B511D840657C7A

FASTA45351,501
        10         20         30         40         50         60 
MPNIVTRFAP SPTGFLHIGG ARTALFNWLY AKHHGGRFLL RIEDTDRKRS TQEAIDAIIN 

        70         80         90        100        110        120 
GLKWLGVSYD GEIVYQSKRI ERHIEVANLL VEKGKAYCCC CPEDKVAEKK AKAREERKIY 

       130        140        150        160        170        180 
KHKCTSVIPD AKPVVRFNVP DSQEIIVDDK IYGHIKVNSD QLDDMVILRS DNTPTYIFAV 

       190        200        210        220        230        240 
VVDDHDAGIT DIIRGSDHLT NTFKQVLIYQ ALDFDIPRFA HVPLIHGRDG NKLSKRHGAT 

       250        260        270        280        290        300 
SVCDYEKMGI LPKAMRNYLL RLGWSHGNDE IISNEQAVKW FNLESIGRSP ARLNFKKLEH 

       310        320        330        340        350        360 
LNNHYINNMS NEDILTLMLG ESTLTNKKKN YLLQGLTELK KRANYLTELL DLAQFYIKDP 

       370        380        390        400        410        420 
PFDLSEEAEQ VVKSNLDIIK LLASFLSNIG DKNWNKGFLS SQVKEFSKLH SAKISDIYHS 

       430        440        450 
LRAPITGVMD APGIIDIMII LGKDECIRRL QAV 

« Hide

References

[1]"The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode."
Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S. expand/collapse author list , Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., Koonin E., Slatko B.
PLoS Biol. 3:599-614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TRS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017321 Genomic DNA. Translation: AAW71041.1.
RefSeqYP_198283.1. NC_006833.1.

3D structure databases

ProteinModelPortalQ5GSI3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292805.Wbm0453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW71041; AAW71041; Wbm0453.
GeneID3266385.
KEGGwbm:Wbm0453.
PATRIC24032671. VBIWolEnd7741_0709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycWEND292805:GH18-517-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 nameSYE2_WOLTR
AccessionPrimary (citable) accession number: Q5GSI3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2005
Last modified: February 19, 2014
This is version 64 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