Q9RTR9 (GLUQ_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamyl-Q tRNA(Asp) synthetase
Short name=Glu-Q-RSs
EC=6.1.1.-

Gene names

Name:	gluQ
Ordered Locus Names:	DR_1687

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro tRNA modification Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacyl-tRNA ligase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 295	295	Glutamyl-Q tRNA(Asp) synthetase HAMAP MF_01428		PRO_0000208297
Regions
	Region	6 – 10	5	Glutamate binding By similarity
	Motif	9 – 19	11	"HIGH" region HAMAP MF_01428
	Motif	233 – 237	5	"KMSKS" region HAMAP MF_01428
Sites
	Metal binding	93	1	Zinc By similarity
	Metal binding	95	1	Zinc By similarity
	Metal binding	118	1	Zinc By similarity
	Metal binding	122	1	Zinc By similarity
	Binding site	42	1	Glutamate By similarity
	Binding site	177	1	Glutamate By similarity
	Binding site	195	1	Glutamate By similarity
	Binding site	236	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RTR9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: DB4114EB4FE6E709	FASTA	295	32,461
	10 20 30 40 50 60 MTVTGRFAPS PTGAMHLGNA RTALLAWLHS RALGGRHLLR FEDLDTGRVR GWAYDLTRRD 70 80 90 100 110 120 LEWLGLDWDE EFRQSERLDL YAAALAGLDT YPCTCTRKEV LAAIADSAGA PHGEEAVYPG 130 140 150 160 170 180 TCRPGSVHPE RPAARRWRVP EAESCVTDAL SGDTLCQWLP RDVGDFVLQR NDGVYAYHLA 190 200 210 220 230 240 VVVDDALMGV TDVLRGADLW TASPRQAALH RALGFTPPRF LHVPLLSNYR GERLAKRGGA 250 260 270 280 290 PPLSEWREHG EAPGRVLADL AHTLPWPGFQ AVPEEVTAPE LLPLWGDVLA ERPGT

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF11243.1.
PIR	E75366.
RefSeq	NP_295410.1. NC_001263.1.
3D structure databases
ProteinModelPortal	Q9RTR9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1800363.
GenomeReviews	Gene locus DR_1687 in contig AE000513_GR.
KEGG	dra:DR_1687.
NMPDR	fig|243230.1.peg.1869.
PATRIC	21631002. VBIDeiRad64572_1896.
TIGR	DR_1687.
Phylogenomic databases
HOGENOM	HBG628189.
OMA	DAPSSYH.
PhylomeDB	Q9RTR9.
ProtClustDB	PRK05710.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1687-MONOMER.
Family and domain databases
HAMAP	MF_01428. Glu_Q_tRNA_synth. [Tree]
InterPro	IPR001412. 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]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
TIGRFAMs	TIGR03838. Queuosine_YadB. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLUQ_DEIRA

Accession

Primary (citable) accession number: Q9RTR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program