B5RF43 (SYI_SALG2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase
EC=6.1.1.5

Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	SG0049

Organism

Salmonella gallinarum (strain 287/91 / NCTC 13346) [Complete proteome] [HAMAP]

Taxonomic identifier

550538 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella gallinarum

Protein attributes

Sequence length	944 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02002
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02002
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	isoleucyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP regulation of translational fidelity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding 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 – 944	944	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000189192
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	604 – 608	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	907	1	Zinc By similarity
	Metal binding	910	1	Zinc By similarity
	Metal binding	927	1	Zinc By similarity
	Metal binding	930	1	Zinc By similarity
	Binding site	563	1	Aminoacyl-adenylate By similarity
	Binding site	607	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B5RF43 [UniParc]. Last modified November 4, 2008. Version 1. Checksum: BF7EB1417D6D7744	FASTA	944	105,642
	10 20 30 40 50 60 MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT FILHDGPPYA 70 80 90 100 110 120 NGSIHIGHSV NKILKDIIVK SKGLSGFDSP YVPGWDCHGL PIELKVEQEF GKPGEKFTAA 130 140 150 160 170 180 EFRAKCREYA ATQVDGQRKD FIRLGVLGDW SHPYLTMDFK TEANIIRALG RIIKNGHLHK 190 200 210 220 230 240 GAKPVHWCVD CRSALAEAEV EYYDKTSPSI DVAFRAVDQD AVKAKFGLPG VSGPVSLVIW 250 260 270 280 290 300 TTTPWTLPAN RAISLAPDFD YALVQIDGQA VILAKDLVES VMQRIGAAEY TILGTVKGAE 310 320 330 340 350 360 LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG LETANPVGPD 370 380 390 400 410 420 GAYLPGTYPT LDGVNVFKAN DIVIELLKEK GALLHVEKMQ HSYPCCWRHK TPIIFRATPQ 430 440 450 460 470 480 WFVSMDKEGL RQQSLKEIKG VQWIPDWGQA RIESMVANRP DWCISRQRTW GVPMSLFVHK 490 500 510 520 530 540 ETQELLPIER TLAAMEEVAK RVEVDGIQAW WDLDPKEILG EDADQYEKVP DTLDVWFDSG 550 560 570 580 590 600 STSYSVVDAR PEFAGHAADM YLEGSDQHRG WFMSSLMISV AMKGKAPYRQ VLTHGFTVDG 610 620 630 640 650 660 QGRKMSKSIG NTVSPQDVMN KLGADILRLW VASTDYTGEM AVSDEILKRA ADSYRRIRNT 670 680 690 700 710 720 ARFLLANLNG FNPATDMVKP EEMVVLDRWA VGCAKTAQQE ILKAYEAYDF HEVVQRLMRF 730 740 750 760 770 780 CSVEMGSFYL DIIKDRQYTA KADSVARRSC QTALYHIAEA LVRWMAPIMS FTADEIWGYL 790 800 810 820 830 840 PGEREKYVFT GEWYDGLFGL EENEEFNDAF WDDVRYIKDQ VNKELENQKA NGIKSNLEAK 850 860 870 880 890 900 VTLKYADDAN GTIKKLKLLG EEVRFIFITS QFVISEQAGG IDDENIQYNA GNTTVQAVVT 910 920 930 940 RAEGDKCPRC WHYTTDVGKV AEHADICGRC VSNIAGNGEQ RKFA

References

[1]

"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways." Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J. Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 287/91 / NCTC 13346.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM933173 Genomic DNA. Translation: CAR35957.1.
RefSeq	YP_002225190.1. NC_011274.1.
3D structure databases
ProteinModelPortal	B5RF43.
ModBase	Search...
Protein-protein interaction databases
STRING	550538.SG0049.
Proteomic databases
PRIDE	B5RF43.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR35957; CAR35957; SG0049.
GeneID	6924662.
KEGG	seg:SG0049.
PATRIC	18498178. VBISalEnt1629_0052.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0525.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	SENT550538:GJ93-47-MONOMER.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02002. Ile_tRNA_synth_type1.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023585. Ile-tRNA-ligase_type1. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR009008. Val/Leu/Ile-tRNA-synth_edit. IPR010663. Znf_DNA_glyclase/IsotRNA_synth. [Graphical view]
PANTHER	PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF06827. zf-FPG_IleRS. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_SALG2

Accession

Primary (citable) accession number: B5RF43

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	November 4, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program