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B3CNK5 (SYE1_WOLPP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:WP0166
OrganismWolbachia pipientis subsp. Culex pipiens (strain wPip) [Complete proteome] [HAMAP]
Taxonomic identifier570417 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length444 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 – 444444Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367794

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
B3CNK5 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 476AD5A7FBF60089

FASTA44451,763
        10         20         30         40         50         60 
MLTRFAPSPT GYLHVGNIRT ALICWMYTRN QNGKFLLRFD DTDLERSDIK YVDNIIEDLK 

        70         80         90        100        110        120 
WIGINWNSSF KQSERFERYN EVFLQLMKEG HIYACYETRE ELDTKRKLQL KQGFPPVYDK 

       130        140        150        160        170        180 
GALLLTEQEK IRYEQEGRKP HFRFKLDRNK TVKWNDEVKG EINIATIHIS DPVVKREDGI 

       190        200        210        220        230        240 
YTYMLPSVID DIDFNVTHVV RGEDHVTNTA VQIQMIQALK AKIPIFAHLP LLHFDDSKIS 

       250        260        270        280        290        300 
KRKGGLDIKS IREDEIESMA LTSYLAKLGT SDPIEAYIDM QSLIDSFDIK KFSSASLQFS 

       310        320        330        340        350        360 
LSEMYKLNSK VLQQMPFEMV QDRLSQIGSE FWYFIRSNIE KFSEVAKWWK ICKFGIEPVV 

       370        380        390        400        410        420 
LNKEFIKIAL STLPQGDCNE NTLSEWVKNI RQTIDIKAKD LFMQLRLALT GTETGPELAK 

       430        440 
LLIFIGRESI IARLEESQRI IQKV 

« Hide

References

[1]"Genome evolution of Wolbachia strain wPip from the Culex pipiens group."
Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A., Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.
Mol. Biol. Evol. 25:1877-1887(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: wPip.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM999887 Genomic DNA. Translation: CAQ54274.1.
RefSeqYP_001974983.1. NC_010981.1.

3D structure databases

ProteinModelPortalB3CNK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING570417.WPa_0166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ54274; CAQ54274; WP0166.
GeneID6385170.
KEGGwpi:WPa_0166.
PATRIC24025860. VBIWolEnd95846_0183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAVARANIT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycWEND570417:GHSW-168-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 nameSYE1_WOLPP
AccessionPrimary (citable) accession number: B3CNK5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 44 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