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Q2GGL8 (SYE2_EHRCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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
Synonyms:gltX-2
Ordered Locus Names:ECH_0605
OrganismEhrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas) [Complete proteome] [HAMAP]
Taxonomic identifier205920 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length469 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 – 469469Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000237363

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
Q2GGL8 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: FC59CCB762FB49A0

FASTA46954,319
        10         20         30         40         50         60 
MSHNVITRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDKKR SSKELIDSII 

        70         80         90        100        110        120 
NAMSWLKIPY DGEIVLQSKN ISRHIEIANQ LILNNKAYYC YCSEEEINKE KEEFSKKGLY 

       130        140        150        160        170        180 
YKHNCIWKNK NFTIDNLTRV IRLRSPTEGV TSFDDKVYGN ITVSNTQLDD MVLLRSDNTP 

       190        200        210        220        230        240 
TYLLSVVVDD HDMNITHIIR GTDHLTNTAR QLLIYNALEW NPPKFAHIPL IHDEDGNKLS 

       250        260        270        280        290        300 
KRHQAIGIHE YKNLGILPEA ISNYLLRMGW SHEDDEIISM DQAIKWFSIK NIGQSPARLD 

       310        320        330        340        350        360 
NKKLEFLNNH YISLTEDEVI LNMIIPIIEK KIGYMLNEVK KGYLLKGLYE LKKRTKNLVN 

       370        380        390        400        410        420 
LANESLFYVE DVPISIDQEA SAIIKDYKHV FSILYNNLSR ISEKEWNNSI LTSTIKNISQ 

       430        440        450        460 
NLDIKISNIY HCLRASIVGR MNAPSIIEIM INLQQEECLK RIKYAQNIE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000236 Genomic DNA. Translation: ABD45013.1.
RefSeqYP_507415.1. NC_007799.1.

3D structure databases

ProteinModelPortalQ2GGL8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205920.ECH_0605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD45013; ABD45013; ECH_0605.
GeneID3927900.
KEGGech:ECH_0605.
PATRIC20576662. VBIEhrCha103583_0523.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycECHA205920:GJNR-607-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_EHRCR
AccessionPrimary (citable) accession number: Q2GGL8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 21, 2006
Last modified: May 14, 2014
This is version 55 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