Q9K9V0 (SYI_BACHD) 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:	BH2545

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	921 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 MF_02002
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_02002
Subunit structure	Monomer By similarity. HAMAP MF_02002
Subcellular location	Cytoplasm By similarity HAMAP MF_02002.
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 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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 921	921	Isoleucine--tRNA ligase HAMAP MF_02002		PRO_0000098349
Regions
	Motif	57 – 67	11	"HIGH" region HAMAP MF_02002
	Motif	593 – 597	5	"KMSKS" region HAMAP MF_02002
Sites
	Metal binding	887	1	Zinc By similarity
	Metal binding	890	1	Zinc By similarity
	Metal binding	907	1	Zinc By similarity
	Metal binding	910	1	Zinc By similarity
	Binding site	552	1	Aminoacyl-adenylate By similarity
	Binding site	596	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K9V0 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 5D9A17ED5A741B9A	FASTA	921	104,563
	10 20 30 40 50 60 MDFKETLLMP KTDFPMRGNL PNREPQMQEE WKDMNIYEKV QARTKGRPLF VLHDGPPYAN 70 80 90 100 110 120 GDIHMGHALN KVLKDMIVRY KSMAGFHAPY VPGWDTHGLP IEQALTKSGV DRKSMSVAEF 130 140 150 160 170 180 RKLCEEFARK QIDRQREQFM RLGVRGDWWN PYVTLDKGFE AQQVKVFGEM AKKGYIYKGK 190 200 210 220 230 240 KPVYWSPSSE SALAEAEIEY HDKRSPSIYV AFPVKDGKNV LQQDEKIVIW TTTPWTIPAN 250 260 270 280 290 300 LGIAVHPELE YSVVAVKGEK YVVASGLVET LESALEWENP EILRTIKGVD LEYVVAEHPI 310 320 330 340 350 360 YGRDSLVVLG DHVTLDAGTG CVHTAPGHGE EDYIVGQKYG LDVLCPVDDK GYMTAEAPGF 370 380 390 400 410 420 EGLFYDEANK PITQKLDECG ALLKLTFITH SYAHDWRTKK PVIYRATAQW FASIENFRDE 430 440 450 460 470 480 LLRAIQEVKW VPEWGETRLY NMVRDRGDWC ISRQRVWGVP IPIFYGENGE PIITDETINH 490 500 510 520 530 540 VSELFRKHGS NVWFEWETKD LLPEGFTHES SPNGQFTREM DIMDVWFDSG SSHQGVLVER 550 560 570 580 590 600 EELDRPADLY LEGSDQYRGW FNSSLSTSVA ITGKAPYKGV LSHGFTLDGE GKKMSKSLGN 610 620 630 640 650 660 VVIPNDVMKQ LGADILRLWV ASVDYQADVR VSDKILKQVS EVYRKIRNTY RFLLGNLHDF 670 680 690 700 710 720 HPATHRVAID QLNGLDRYML AKLNDVINRV KKAYDEYQFS TVYHELHNFC TIELSSFYMD 730 740 750 760 770 780 IAKDTLYVKH ADHPDRRATQ TVMYDVLVAL AKLLSPIIPH TADEVWKHIP GVEEESVQLT 790 800 810 820 830 840 DMPEPIELGD VSELKQKWDA FINVRDDVLK ALENARNEKV IGKSLTAAIT LYADGDVRQL 850 860 870 880 890 900 LEELGPLDKL FIVSAVKVAG SVADAPKEAE SYDDLAIVVE KAVGETCERC WVVSPTVGTN 910 920 NEHPTLCADC AETVATYYVT K

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB06264.1.
PIR	A83968.
RefSeq	NP_243411.1. NC_002570.2.
3D structure databases
ProteinModelPortal	Q9K9V0.
SMR	Q9K9V0. Positions 2-882.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000050308; EBBACP00000048947; EBBACG00000050299.
GeneID	891516.
GenomeReviews	Gene locus BH2545 in contig BA000004_GR.
KEGG	bha:BH2545.
NMPDR	fig|272558.1.peg.2545.
PATRIC	18942282. VBIBacHal18977_2654.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00070000031886.
HOGENOM	HBG577712.
OMA	KQVLTHG.
PhylomeDB	Q9K9V0.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	BHAL272558:BH2545-MONOMER.
Family and domain databases
HAMAP	MF_02002. Ile_tRNA_synth_type1. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-synt. IPR023585. Ile-tRNA-synt_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]
Gene3D	G3DSA:3.90.740.10. G3DSA:3.90.740.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01870.
PANTHER	PTHR11946:SF9. Ile-tRNA-synt_Ia. 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_BACHD

Accession

Primary (citable) accession number: Q9K9V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program