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Q73H00 (SYE2_WOLPM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:WD_0778
OrganismWolbachia pipientis wMel [Complete proteome] [HAMAP]
Taxonomic identifier163164 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length440 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 – 440440Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119698

Regions

Motif7 – 1711"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73H00 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 97632692BD08B046

FASTA44050,976
        10         20         30         40         50         60 
MLTRFAPSPT GYLHVGNVRT ALVCWMYTRN QNGKFLLRFD DTDLQRSDVK YINDIIEDLK 

        70         80         90        100        110        120 
WIGIDWDASF KQSERFERYN EVFLQLIKEG HIYACYETRE ELDIKRKLQL KQGFPPVYDR 

       130        140        150        160        170        180 
SALLLTEQEK IRYEQEGRRP HFRFKLDRNE VVKWNDEVKG EINIATSSVS DPVVKREDGI 

       190        200        210        220        230        240 
YTYMLPSVTD DVDFNVTHIV RGEDHVTNTA VQIQMIKALK AKIPTFAHLP LLHFDDSKIS 

       250        260        270        280        290        300 
KRKGGLDIKS IKEDEIEPMA LVSYLVKLGT SNPIEACACM QSLIDSFDIK KFSSASAQFS 

       310        320        330        340        350        360 
LSEMYKLNSK VLQQMLFEMV QDRLNQIGVG SSEFWYFIRN NIERFSEVAK WWKICKSDIE 

       370        380        390        400        410        420 
PVILDKELIK IAFNALPQGD CNENTLSEWV KTIRQTVDIK AKNLFTQLRS ALTGTETGPE 

       430        440 
LAKLLIFIGK ENIIARLKEK 

« Hide

References

[1]"Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements."
Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F., Nelson W.C. expand/collapse author list , Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.
PLoS Biol. 2:327-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017196 Genomic DNA. Translation: AAS14466.1.
RefSeqNP_966532.1. NC_002978.6.

3D structure databases

ProteinModelPortalQ73H00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING163164.WD0778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS14466; AAS14466; WD_0778.
GeneID2738237.
KEGGwol:WD0778.
PATRIC24030147. VBIWolEnd21207_0775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAGHIYACY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycWEND163164:GJ8W-762-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_WOLPM
AccessionPrimary (citable) accession number: Q73H00
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 75 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