Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1LBX4 (SYE2_THESQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:TRQ2_1478
OrganismThermotoga sp. (strain RQ2) [Complete proteome] [HAMAP]
Taxonomic identifier126740 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

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_0000367793

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LBX4 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: F42FDD29C3A93EEB

FASTA46954,582
        10         20         30         40         50         60 
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER EYEEKLMESL 

        70         80         90        100        110        120 
RWLGLLWDEG PDVGGDHGPY MQSERVEIYR EHAERLVKEG KAYYVYAYPE EIEEMREKLL 

       130        140        150        160        170        180 
SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI 

       190        200        210        220        230        240 
GDFVIMRSNG LPTYNFACVV DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV 

       250        260        270        280        290        300 
STILGPDGKK LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF 

       310        320        330        340        350        360 
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID EEYFKKVLEI 

       370        380        390        400        410        420 
TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE ELQNVRWTME EITPVFKKVL 

       430        440        450        460 
KQHGVKPKEF YMTLRRVLTG REEGPELVNI IPLLGKEIFL RRIERSLGG 

« Hide

References

[1]"Complete sequence of Thermotoga sp. RQ2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RQ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000969 Genomic DNA. Translation: ACB09822.1.
RefSeqYP_001739505.1. NC_010483.1.

3D structure databases

ProteinModelPortalB1LBX4.
SMRB1LBX4. Positions 1-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING126740.TRQ2_1478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB09822; ACB09822; TRQ2_1478.
GeneID6092924.
KEGGtrq:TRQ2_1478.
PATRIC23949588. VBITheSp108950_1503.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTSP126740:GH49-1525-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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_THESQ
AccessionPrimary (citable) accession number: B1LBX4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 41 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