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

Q1IY50 (SYE_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:Dgeo_1539
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length480 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 – 480480Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330967

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IY50 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: F7944E6653C2C491

FASTA48054,347
        10         20         30         40         50         60 
MSVVTRIAPS PTGDPHVGTA YIGLFNHTLA QQARARGEEG KFILRIEDTD RNRYVPDSER 

        70         80         90        100        110        120 
RIFQMMAWLG LTPDESPLQG GPNGPYRQSE RTAIYGEYAR KLVEAGHAYY AFETPEELAA 

       130        140        150        160        170        180 
LREAAQQEGR VIAVPSRDLD PAEAQRRVDA GESAVIRLKV PREGETVVND ALRKPIAFQN 

       190        200        210        220        230        240 
REIDDKVLLK ADGYPTYHLA NVVDDHLMGV THVIRAEEWI TSTPIHVLLY RAFGWAEPIF 

       250        260        270        280        290        300 
AHMPLLRNAD KSKISKRKNP TSVEWYMAQG FLPEAMLNFL ATMGWTHPEG KEIFDLAEFQ 

       310        320        330        340        350        360 
RVFRLEDVTL GGPVFSLDKL RWMNGKYLRE VLSEEEVAER LHAYLASQKH DLPDDDYFRA 

       370        380        390        400        410        420 
VVRMMIPRMD VFSEFLEKTP YFWSEDYPVS EKAQHLIEEG RPFLPELAAR LKNLPSFDPA 

       430        440        450        460        470        480 
TTEAALRAFA EERGLKPGKV MQPLRAAIAG TSESPGMFEL LEVLGQERVV ARVERAARGG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000359 Genomic DNA. Translation: ABF45834.1.
RefSeqYP_605003.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IY50.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319795.Dgeo_1539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF45834; ABF45834; Dgeo_1539.
GeneID4057425.
KEGGdge:Dgeo_1539.
PATRIC21625007. VBIDeiGeo41128_2133.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycDGEO319795:GHMU-1567-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 nameSYE_DEIGD
AccessionPrimary (citable) accession number: Q1IY50
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 64 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