Reviewed, UniProtKB/Swiss-Prot Q2GDP4 (SYE1_NEOSM)

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:	NSE_0518

Organism

Neorickettsia sennetsu (strain Miyayama) [Complete proteome] [HAMAP]

Taxonomic identifier

222891 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Neorickettsia

Protein attributes

Sequence length	433 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 By similarity 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 – 433	433	Glutamyl-tRNA synthetase 1 HAMAP MF_00022		PRO_0000367718
Regions
	Motif	7 – 17	11	"HIGH" region HAMAP MF_00022
	Motif	230 – 234	5	"KMSKS" region HAMAP MF_00022
Sites
	Binding site	233	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GDP4-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 862FFB1C69E5A119	FASTA	433	49,866
	10 20 30 40 50 60 MITRFAPSPT GLIHLGNART ALIAYFAARS SGGEFILRID DTDVTRIKSE YVNKIFTDLS 70 80 90 100 110 120 WLGIKEDLCI KQSERCELYA NAVVKLKESG RIYPCYETPE ELEIERRSLL ARALPPVYRR 130 140 150 160 170 180 KNRPQHSTRL PYYRFELDPD RVVIWEDKLR GKIVIDLHST SDPIVIRENG TYTYMLPSVV 190 200 210 220 230 240 DDIECRISTI IRGEDHISNT AVQIQMFEAL GCTEIPKFAH MPLLKLQTGK MSKRAGGNEI 250 260 270 280 290 300 QTFRENYIEP EVICLYLLNL GSKSRSTFKN YKDYSNFNLE NYSSSSSVTV LEDEIYSLNA 310 320 330 340 350 360 DFLRLSNYED LARRLGGVSK TFWDAVKNNV KSIPEVNYWW EICTTEAKLY PGIGCNAQLV 370 380 390 400 410 420 RDAISVLPQE EVSRETYRRW VELIVENYRY DKREVHINLR LALTGKVGGP EMAAILPFIS 430 RERILIRLND SLS

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000237 Genomic DNA. Translation: ABD46392.1.
RefSeq	YP_506402.1.
3D structure databases
SMR	Q2GDP4. Positions 1-236, 2-432.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GDP4.
Genome annotation databases
GeneID	3931642.
GenomeReviews	Gene locus NSE_0518 in contig CP000237_GR.
KEGG	nse:NSE_0518.
TIGR	NSE_0518.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	FISRERI.
Enzyme and pathway databases
BioCyc	NSEN222891:NSE_0518-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. 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: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.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE1_NEOSM

Accession

Primary (citable) accession number: Q2GDP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 21, 2006
Last modified:	January 19, 2010
This is version 38 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)