Reviewed, UniProtKB/Swiss-Prot Q3YS31 (SYE1_EHRCJ)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1

Gene names

Name:	gltX1
Ordered Locus Names:	Ecaj_0432

Organism

Ehrlichia canis (strain Jake) [Complete proteome] [HAMAP]

Taxonomic identifier

269484 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	469 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 MF_00022
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022
Subunit structure	Monomer By similarity. HAMAP MF_00022
Subcellular location	Cytoplasm HAMAP MF_00022.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 469	469	Glutamyl-tRNA synthetase 1 HAMAP MF_00022		PRO_0000237360
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP MF_00022
	Motif	238 – 242	5	"KMSKS" region HAMAP MF_00022
Sites
	Binding site	241	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3YS31-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: F265F659A7DB3D4A	FASTA	469	53,980
	10 20 30 40 50 60 MSHDVITRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDKKR SSQELIDSII 70 80 90 100 110 120 NAMSWLKIHY DGKAVLQSEN ISRHVEIANQ LMLNNKAYYC YCSEEEINKE KEESAKKGLY 130 140 150 160 170 180 YKHNCIWKNK SAPNSNITRV VRLKSPTDGV TSFDDEVYGN ITVNNSQLDD MILLRSDNTP 190 200 210 220 230 240 TYLLSVVVDD HDMNISHIIR GTDHLTNTAR QLLIYNALEW DPPKFAHIPL IHDENGNKLS 250 260 270 280 290 300 KRHQAIGIHE YKNSGILPEA IFNYLLRMGW SHENDEVITI DQAIRWFSIE GIGQSPSRLD 310 320 330 340 350 360 SKKLEFLNNH YINITDNETI LNMIIPIIEE KTGHIITDVK KGYLLKGLSE LKKRTKNLVN 370 380 390 400 410 420 LAKESLFYVE DIPISIDQES ITVIKDYKHI FSILYDNLSK ISEKDWNHNI LMSIIKDISC 430 440 450 460 NLEVKISIVY HCLRASITGR MNAPSIIEIM INLQHKECLQ RIKYALDVI

References

[1]

"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies." Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C. J. Bacteriol. 188:4015-4023(2006) [PubMed: 16707693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000107 Genomic DNA. Translation: AAZ68474.1.
RefSeq	YP_303072.1.
3D structure databases
SMR	Q3YS31. Positions 5-467.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3YS31.
Genome annotation databases
GeneID	3617778.
GenomeReviews	Gene locus Ecaj_0432 in contig CP000107_GR.
KEGG	ecn:Ecaj_0432.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	DLVIQRS.
PhylomeDB	Q3YS31.
Enzyme and pathway databases
BioCyc	ECAN269484:ECAJ_0432-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_Ic_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020060. Glu/Gln-tRNA-synth_Ic_N. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE1_EHRCJ

Accession

Primary (citable) accession number: Q3YS31

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	September 27, 2005
Last modified:	February 9, 2010
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)