Q3YR29 (SYE2_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 2
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2

Gene names

Name:	gltX2
Ordered Locus Names:	Ecaj_0795

Organism

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

Taxonomic identifier

269484 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	443 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_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm HAMAP MF_00022_B.
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 443	443	Glutamate--tRNA ligase 2 HAMAP MF_00022_B		PRO_0000237361
Regions
	Motif	7 – 17	11	"HIGH" region HAMAP MF_00022_B
	Motif	236 – 240	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3YR29 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: 3508EE2D6663FD3D	FASTA	443	51,549
	10 20 30 40 50 60 MITRFAPSPT GYLHVGNVRT ALICWLYVRK QKGKFLLRFD DTDTQRSQEE YIKEIENDLK 70 80 90 100 110 120 WLNMNWDASF RQSSRFDRYE DVFQYLLKEG FLYPCYESKE ELEFKRKMKL KSGLPPIYDR 130 140 150 160 170 180 SALNLTQAEK DKYFGRAPYF RFKINQDQLI NWDDEIRGKV SFNPKNISDP IIRRVDGTYT 190 200 210 220 230 240 YMLPSVIDDM DFNVTHVIRG EDHISNTAVQ IQMLDALKAK VPMFAHLSLL YSDDNKISKR 250 260 270 280 290 300 VGGSSVKDMQ LYELEPMAIN SYFAKIGTSH PIDVHINMLG LINSFDITAF SQAPTKFNID 310 320 330 340 350 360 DILKLNPKIL HNMSFDDVKD RLKELKIDKP AFWDFVCGNI EKFSDIEEWI KICSRDMVPV 370 380 390 400 410 420 VKQDDKDFIT LALNMFPQGE VHDSTWNTWV SNIKQQTDRR GKNLFAPLRL ALTGLAAGPE 430 440 LAKLLPLIGR EEIVRRLSYS VTQ

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]. Strain: Jake.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000107 Genomic DNA. Translation: AAZ68826.1.
RefSeq	YP_303424.1. NC_007354.1.
3D structure databases
ProteinModelPortal	Q3YR29.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3YR29.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3617585.
GenomeReviews	Gene locus Ecaj_0795 in contig CP000107_GR.
KEGG	ecn:Ecaj_0795.
PATRIC	20575248. VBIEhrCan118076_0869.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	ARTALIC.
ProtClustDB	PRK12558.
Enzyme and pathway databases
BioCyc	ECAN269484:ECAJ_0795-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_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]
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. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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

SYE2_EHRCJ

Accession

Primary (citable) accession number: Q3YR29

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	September 27, 2005
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program