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Q68WB4 (SYE2_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RT0614
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

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_0000119643

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68WB4 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B6EE33BFF5549861

FASTA46953,447
        10         20         30         40         50         60 
MTNIITRFAP SPTGFLHIGS ARTALFNYLF ARHNNGKFFL RIEDTDKKRS TKEAIAAIFS 

        70         80         90        100        110        120 
GLKWLGINWD GEVIFQSKRN SLYKEAALKL LKEGKAYYCF TKQEEIARQR QQALKDKKHF 

       130        140        150        160        170        180 
IFNSEWRDKG PSTYPADIKP VIRLKVPREG SITIHDTLQG DIVIENSHID DMILIRADGT 

       190        200        210        220        230        240 
ATYMLAVIVD DHDMGITHII RGDDHLTNAA RQIAIYHAFG YEVPNMTHIP LIHGADGTKL 

       250        260        270        280        290        300 
SKRHGALGVE AYKDMGYLPE SLCNYLLRLG WSHGDDEIIS MNQAIEWFNL DSLGKSPSKL 

       310        320        330        340        350        360 
DFAKMNSINS HYLRMLDNDS LTSKTVAILK QNYKISEKEV SYIKQAMPSL IVRSATLIDL 

       370        380        390        400        410        420 
AQLAYIYLVD SPMIYNQDAK EVIKNCDKDL IKQIIANLNK LEQFDKECIQ NKFKEIAIYN 

       430        440        450        460 
GLKLNDIMRP VRALITGMTA SPSIFEIAET LGKENILKRL NIIYYNLNF 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU04078.1.
RefSeqYP_067560.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68WB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU04078; AAU04078; RT0614.
GeneID2958998.
KEGGrty:RT0614.
PATRIC17910468. VBIRicTyp34752_0634.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-645-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE2_RICTY
AccessionPrimary (citable) accession number: Q68WB4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries