Q9RX30 (SYE_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	DR_0485

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus radiodurans

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Sequence caution	The sequence AAF10063.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 483	483	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119552
Regions
	Motif	14 – 24	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	253 – 257	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	256	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RX30 [UniParc]. Last modified April 30, 2003. Version 2. Checksum: 7F6F65C0BF3A4567	FASTA	483	54,689
	10 20 30 40 50 60 MSAPSSPRVT RIAPSPTGDP HVGTAYIGLF NHTLARQSGG RFILRVEDTD RNRYVPDSEK 70 80 90 100 110 120 RIFQMMQWLN LTPDESPLQG GPNGPYRQSE RFDLYGDYAR QLVQSGHAYY AFETSDELAA 130 140 150 160 170 180 LREEAQKAGH VIAIPSRDLG AAQAQARVDA GEPAVIRLKV DRDGETVVND LLRDPIHFAN 190 200 210 220 230 240 KEIDDKVLLK ADGFPTYHLA NVVDDRLMQV THVVRAEEWI TSTPIHVLLY RAFGWPEPVF 250 260 270 280 290 300 AHMPLLRNAD KSKISKRKNP TSVEWYQNQG FLPEAMLNFL ATMGWTHPDG QEIFDLAEFE 310 320 330 340 350 360 RVFRLEDVTL GGPVFDLAKL RWYNGKYLRE VLSEDDVARR LHAFLMQNKV TLPSVDGPQD 370 380 390 400 410 420 PYFRAVTHLM IPRLEVFADF MDKTLYFWSE DYPVNEKAQK AIDAGKELLP ELAARLKNLP 430 440 450 460 470 480 TFDAASIKEM FHAYAEEKGL KMGKVMPPIR AAVAGTMESP DLPEMLEALG RERVLARVEK AAR

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] [Europe PMC] [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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF10063.1. Different initiation.
PIR	H75514.
RefSeq	NP_294208.1. NC_001263.1.
3D structure databases
ProteinModelPortal	Q9RX30.
SMR	Q9RX30. Positions 9-482.
ModBase	Search...
Protein-protein interaction databases
STRING	243230.DR_0485.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF10063; AAF10063; DR_0485.
GeneID	1798880.
KEGG	dra:DR_0485.
PATRIC	21628496. VBIDeiRad64572_0664.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	EEWISST.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	DRAD243230:GH46-856-MONOMER.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 1.10.8.70. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
InterPro	IPR008925. 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_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. 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]
PANTHER	PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_DEIRA

Accession

Primary (citable) accession number: Q9RX30

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	April 30, 2003
Last modified:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program