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

A6W7Q5 (SYE_KINRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Krad_1356
OrganismKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) [Complete proteome] [HAMAP]
Taxonomic identifier266940 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesKineosporiineaeKineosporiaceaeKineococcus

Protein attributes

Sequence length501 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 – 501501Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330977

Regions

Motif21 – 3111"HIGH" region HAMAP-Rule MF_00022
Motif266 – 2705"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2691ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6W7Q5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 70EE9152537C7723

FASTA50154,661
        10         20         30         40         50         60 
MTDIAAPPAP GTSPVRVRFC PSPTGTPHVG LIRTALFNWA HARHTGGTFV FRIEDTDAAR 

        70         80         90        100        110        120 
DSEESYAQIL DALDWLGLDW DEGIGVGGPH EPYRQSLRRP VYDDVVRRLR EAGHLYESFS 

       130        140        150        160        170        180 
TAEEIEARHE AAGRPKVLGY DGFDRDLTPE QVAAFRAEGR EPTLRLRLPE GRDYSFDDVV 

       190        200        210        220        230        240 
RGRIEFKAGS FPDPVLVRAN GDPLYTLVNP VDDALMGITH VLRGEDLLSS TPRQIALHEA 

       250        260        270        280        290        300 
LVDIGVSQAV PLFGHLPYVT GEGSKKLSKR DPESNLFHHR DRGFIREGLL NYLALLGWGI 

       310        320        330        340        350        360 
SEDRDVFSVE EMVAAFDVAD VNASPARFDV AKAEAINAAH LRLLAPEDFR GRLVPYLQAA 

       370        380        390        400        410        420 
GVLPAQPSPE QLERLAAAAP LVQERMTLLG QAPGMLGFLF VADGDVVLEP DATAALRPEA 

       430        440        450        460        470        480 
ADVLDASLAA LEALTGWTTA DLEAALRAAV VEGLGVKPKF AFAPLRTAVT GRRVSPPLFE 

       490        500 
SMEILGRESS LARLRRLRAT L 

« Hide

References

[1]"Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., Fliermans C., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-149 / DSM 14245 / SRS30216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000750 Genomic DNA. Translation: ABS02844.1.
RefSeqYP_001361108.1. NC_009664.2.

3D structure databases

ProteinModelPortalA6W7Q5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266940.Krad_1356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS02844; ABS02844; Krad_1356.
GeneID5335836.
KEGGkra:Krad_1356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAKHYDGDF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycKRAD266940:GI4N-872-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 nameSYE_KINRD
AccessionPrimary (citable) accession number: A6W7Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 54 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