Q0I1V8 (SYI_HAES1) 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:	HS_0186

Organism

Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]

Taxonomic identifier

205914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus › Haemophilus somnus

Protein attributes

Sequence length	937 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 – 937	937	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000022074
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	602 – 606	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	900	1	Zinc By similarity
	Metal binding	903	1	Zinc By similarity
	Metal binding	920	1	Zinc By similarity
	Metal binding	923	1	Zinc By similarity
	Binding site	561	1	Aminoacyl-adenylate By similarity
	Binding site	605	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0I1V8 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: C0E8BBD52F459F68	FASTA	937	105,861
	10 20 30 40 50 60 MTDYKNTLNL PETGFPMRGD LAKREPDMLK NWYDKNLYQK VREASKGKKT FILHDGPPYA 70 80 90 100 110 120 NGTLHLGHAV NKILKDIIMK SKTALGFDTP YVPGWDCHGL PIELKVEGLV GKPNEKISAA 130 140 150 160 170 180 EFRQACRDYA KEQVEGQKAD FIRMGVLGDW DNPYLTMNFE TEAEIIRTLG KVIQNGHLYK 190 200 210 220 230 240 GSKPVHWCLD CASSLAEAEV EYEDKVSPSI YVRFAAVSAA EVEEKFNALG KGQGALSAVI 250 260 270 280 290 300 WTTTPWTLPS NRAIAVNAEL EYQLVQLGNE RVILATELVQ TVQNALGIEQ IQILGSAKGG 310 320 330 340 350 360 DLELIRFNHP FYDFSVPMIL GDHVTVDGGT GLVHTAPDHG QDDFVVSKKY GLEMAGLVAN 370 380 390 400 410 420 DGKFISSTPF FAGKGVFEAN DLVLEKLKET GALLKLERIK HSYPHCWRHK TPIIFRATPQ 430 440 450 460 470 480 WFIGMETQDL RIKALSEIKS VRWIPSWGEA RIDKMVANRP DWCISRQRTW GVPMTMFVHN 490 500 510 520 530 540 ETEELHPRTL ELLEDIAKRV EKAGIQAWWD LDPAELLGEE AKTYHKVPDT LDVWFDSGST 550 560 570 580 590 600 YASVVEQRPE FNGKSTDMYL EGSDQHRGWF MSSLMLSTAT NNKAPYKQVL THGFTVDEKG 610 620 630 640 650 660 RKMSKSLGNV IVPSEVWNKN GADILRLWVA STDYTGEIAV SHKILNSAGD TYRRIRNTAR 670 680 690 700 710 720 FLLANLNGFD PKNDLVNPEE MISLDRWAVS CALEAQNEIK EAYDNYQFHT VVQRLMRFCS 730 740 750 760 770 780 IEMGSFYLDI IKDRQYTTKA DSLARRSCQT ALWHISEALV RWIAPILSFT ADEIWGYLPK 790 800 810 820 830 840 LDNRAEFVFT EEFYDGLFGL DESDKLDDTY WQQLLKVRAE VNRVLEQARN DKLIGAGLEA 850 860 870 880 890 900 KVTVYASEEI RPLLEQLGNE LRFVLITSQV VVKPLSKADV AESELTGLAV KVERADGEKC 910 920 930 PRCWHFATDI GSNKEHSHIC GRCIENVEGN GEQRQFA

References

[1]

"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd." Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J. J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129Pt.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000436 Genomic DNA. Translation: ABI24464.1.
RefSeq	YP_718393.1. NC_008309.1.
3D structure databases
ProteinModelPortal	Q0I1V8.
ModBase	Search...
Protein-protein interaction databases
STRING	205914.HS_0186.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABI24464; ABI24464; HS_0186.
GeneID	4239697.
KEGG	hso:HS_0186.
PATRIC	20280280. VBIHaeSom53361_0198.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	HSOM205914:GJ7V-192-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_HAES1

Accession

Primary (citable) accession number: Q0I1V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program