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Q5HB98 (SYE2_EHRRW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:Erum4310, ERWE_CDS_04490
OrganismEhrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]
Taxonomic identifier254945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length470 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 – 470470Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119561

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HB98 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: ECF29C177C2889AC

FASTA47054,081
        10         20         30         40         50         60 
MLNHVVTRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDSKR SSKELIDSII 

        70         80         90        100        110        120 
NSMIWLNIQH DGDIILQSSR ISRHIEIANQ LILNDKAYYC YCSEEEINLE KEEYTKKGLH 

       130        140        150        160        170        180 
YKHNCIWKNR NPPIGNCSKV IRLHSDTEGI TEFKDKVYGT IAVNNVQLDD MVLLRSNNTP 

       190        200        210        220        230        240 
TYLLSVVVDD YDMGITHIIR GTDHLTNTAR QLLIYNALGW KPPEFAHIPL IHDENGNKLS 

       250        260        270        280        290        300 
KRHHALGIHE YKNAGILPEA LLNYLLRMGW SHGNDEVITI DEAIRWFSID KVGQSPARLD 

       310        320        330        340        350        360 
SKKLEFLNNH YINATNNATI IEMIIPIIEK TIGYKVNTEK IGYLLNGINE LKKRTKNLVN 

       370        380        390        400        410        420 
LANESLFYVE DIPISFDQES LIIIKSNHDI LSILYDNLSK VLNDDWNNST LTSMIKNIVK 

       430        440        450        460        470 
DYNTKIHNIY HCLRASIIGR INAPSIIDIM VNFQREECLN RIKYARDMVK 

« Hide

References

[1]"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number."
Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. expand/collapse author list , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A.
Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.
[2]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR767821 Genomic DNA. Translation: CAH58157.1.
CR925678 Genomic DNA. Translation: CAI26943.1.
RefSeqYP_180296.1. NC_005295.2.
YP_197325.1. NC_006832.1.

3D structure databases

ProteinModelPortalQ5HB98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING254945.Erum4310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH58157; CAH58157; Erum4310.
CAI26943; CAI26943; ERWE_CDS_04490.
GeneID3233341.
3260859.
KEGGeru:Erum4310.
erw:ERWE_CDS_04490.
PATRIC20580721. VBIEhrRum92411_0476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAIQECIND.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycERUM254945:GJ2L-473-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_EHRRW
AccessionPrimary (citable) accession number: Q5HB98
Secondary accession number(s): Q5FEZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 63 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