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Q1IZL1 (GLUQ_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamyl-Q tRNA(Asp) synthetase
Short name=Glu-Q-RSs
EC=6.1.1.-
Gene names
Name:gluQ
Ordered Locus Names:Dgeo_1023
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon By similarity. HAMAP MF_01428

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01428

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Glutamyl-Q tRNA(Asp) synthetase HAMAP MF_01428
PRO_1000024354

Regions

Region9 – 135Glutamate binding By similarity
Motif12 – 2211"HIGH" region HAMAP MF_01428
Motif240 – 2445"KMSKS" region HAMAP MF_01428

Sites

Metal binding1001Zinc By similarity
Metal binding1021Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1291Zinc By similarity
Binding site451Glutamate By similarity
Binding site1841Glutamate By similarity
Binding site2021Glutamate By similarity
Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IZL1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 72C0BC1B26CD2F21

FASTA30333,082
        10         20         30         40         50         60 
MNVLPVVGRF APSPTGAMHL GNARTALLAW LHSRALGGLH LLRFEDLDTG RVRSWAYDTT 

        70         80         90        100        110        120 
RRDLEWLGLD WDAEFRQSER LPVYADAVSR LTAAGETYPC TCTRREIRQA IEDSAGAPHG 

       130        140        150        160        170        180 
HEPVYPGTCR LHGAMPGRPA ALRWHVPDGT VCVTDALTCA TLCQNLPAEV GDFVLRRNDG 

       190        200        210        220        230        240 
VYAYHLAVVV DDALMGVTDV VRGADLWTAT PRQVALGRAL GSAPPRYLHV PLMTDFRGER 

       250        260        270        280        290        300 
LAKRGGAPPL RALREGGEEA GRVLSALARS LGWAVPERVS AAELLPLWRA QLTRAGFFIN 


PQS

« 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: ABF45323.1.
RefSeqYP_604492.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IZL1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1IZL1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4057984.
GenomeReviewsGene locus Dgeo_1023 in contig CP000359_GR.
KEGGdge:Dgeo_1023.
NMPDRfig|68909.1.peg.500.
PATRIC21623933. VBIDeiGeo41128_1603.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADAPSSYH.
PhylomeDBQ1IZL1.
ProtClustDBPRK05710.

Enzyme and pathway databases

BioCycDGEO319795:DGEO_1023-MONOMER.

Family and domain databases

HAMAPMF_01428. Glu_Q_tRNA_synth.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR022380. Glu-Q_TRNA(Asp)_Synthase.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR03838. Queuosine_YadB. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLUQ_DEIGD
AccessionPrimary (citable) accession number: Q1IZL1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: January 25, 2012
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

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