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B3CLF5 (SYE2_WOLPP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:WP0615
OrganismWolbachia pipientis subsp. Culex pipiens (strain wPip) [Complete proteome] [HAMAP]
Taxonomic identifier570417 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length450 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 – 450450Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367795

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif232 – 2365"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3CLF5 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 11C4B6AB9A6A3AAE

FASTA45051,202
        10         20         30         40         50         60 
MPGIVTRFAP SPTGFLHIGG ARTALFNWLY AQRHGGQFLL RIEDTDRKRS TQEAIDAIID 

        70         80         90        100        110        120 
GLKWLGISYD GEIVYQSKRI DRHIEVANLL VEKGRAYHCY CPENEVAEKK IRAREEGKIY 

       130        140        150        160        170        180 
KHKCTHSTSN AEPVVRFKVP DSEDIVVDDK IYGQVTISSD QLDDIVILRS DNTPTYIFAV 

       190        200        210        220        230        240 
VVDDHDAGIT DIIRGSDHLT NTFKQLLIYQ ALDFDVPRFA HVPLIHGEDG NKLSKRHGAT 

       250        260        270        280        290        300 
SVCDYEKMGI LPQAMRNYLL RLGWSHGNDE IISDEQAIEW FNLESIGRSP ARLDFKKLEH 

       310        320        330        340        350        360 
LNNHYISNMS NEDILTLMLR ENTLTDKKKG YLLQGLTELK KRANYLTELL DLAKFYIQVD 

       370        380        390        400        410        420 
LSEEAQQIVK SNLNVIKLLA SFLSSVGSED WNKNFLSSQI KEFSKLHNIK MSDIYHSLRA 

       430        440        450 
PITGIMDAPG IIDIMVILGK DECIKRLQAI 

« 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: CAQ54723.1.
RefSeqYP_001975381.1. NC_010981.1.

3D structure databases

ProteinModelPortalB3CLF5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING570417.WPa_0615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ54723; CAQ54723; WP0615.
GeneID6385357.
KEGGwpi:WPa_0615.
PATRIC24026860. VBIWolEnd95846_0677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycWEND570417:GHSW-623-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_WOLPP
AccessionPrimary (citable) accession number: B3CLF5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: May 14, 2014
This is version 46 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