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Q3YR29 (SYE2_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Ecaj_0795
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length443 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 – 443443Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000237361

Regions

Motif7 – 1711"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YR29 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 3508EE2D6663FD3D

FASTA44351,549
        10         20         30         40         50         60 
MITRFAPSPT GYLHVGNVRT ALICWLYVRK QKGKFLLRFD DTDTQRSQEE YIKEIENDLK 

        70         80         90        100        110        120 
WLNMNWDASF RQSSRFDRYE DVFQYLLKEG FLYPCYESKE ELEFKRKMKL KSGLPPIYDR 

       130        140        150        160        170        180 
SALNLTQAEK DKYFGRAPYF RFKINQDQLI NWDDEIRGKV SFNPKNISDP IIRRVDGTYT 

       190        200        210        220        230        240 
YMLPSVIDDM DFNVTHVIRG EDHISNTAVQ IQMLDALKAK VPMFAHLSLL YSDDNKISKR 

       250        260        270        280        290        300 
VGGSSVKDMQ LYELEPMAIN SYFAKIGTSH PIDVHINMLG LINSFDITAF SQAPTKFNID 

       310        320        330        340        350        360 
DILKLNPKIL HNMSFDDVKD RLKELKIDKP AFWDFVCGNI EKFSDIEEWI KICSRDMVPV 

       370        380        390        400        410        420 
VKQDDKDFIT LALNMFPQGE VHDSTWNTWV SNIKQQTDRR GKNLFAPLRL ALTGLAAGPE 

       430        440 
LAKLLPLIGR EEIVRRLSYS VTQ 

« Hide

References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Jake.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000107 Genomic DNA. Translation: AAZ68826.1.
RefSeqYP_303424.1. NC_007354.1.

3D structure databases

ProteinModelPortalQ3YR29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269484.Ecaj_0795.

Proteomic databases

PRIDEQ3YR29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ68826; AAZ68826; Ecaj_0795.
GeneID3617585.
KEGGecn:Ecaj_0795.
PATRIC20575248. VBIEhrCan118076_0869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECAN269484:GI02-832-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_EHRCJ
AccessionPrimary (citable) accession number: Q3YR29
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 27, 2005
Last modified: February 19, 2014
This is version 60 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