Q1WTA9 (SYI_LACS1) 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:	LSL_1042

Organism

Lactobacillus salivarius (strain UCC118) [Complete proteome] [HAMAP]

Taxonomic identifier

362948 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus salivarius

Protein attributes

Sequence length	931 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 – 931	931	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_1000022085
Regions
	Motif	57 – 67	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	597 – 601	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	891	1	Zinc By similarity
	Metal binding	894	1	Zinc By similarity
	Metal binding	911	1	Zinc By similarity
	Metal binding	914	1	Zinc By similarity
	Binding site	556	1	Aminoacyl-adenylate By similarity
	Binding site	600	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1WTA9 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: 5DC79435C3CACD89	FASTA	931	106,202
	10 20 30 40 50 60 MKVKDTLNLG KTKFPMRGNL PVREVERQNE WEENKVYEQR QKLNEGKPSF VLHDGPPYAN 70 80 90 100 110 120 GNIHMGHAMN KISKDFIVRS KSMMGFRAPY VPGWDTHGLP IEQQLKKAGV DRKALSVAEF 130 140 150 160 170 180 REMCRQYALE QVDKQRKDFK RLGVAGEWDN PYLTLKPEYE AQQIRVFGKM AEKGLIYKGK 190 200 210 220 230 240 KPVFWSWSSE SALAEAEVEY HDVTSPSAFY GEQVVDGKGV LDENTYMVVW TTTPWTIPAS 250 260 270 280 290 300 EGITIDATFD YAVVQHDDDE RKYVLAADLV NADAELFGWN DVKIVKTVKG AELENVLCQH 310 320 330 340 350 360 PFYPERKLVT MLGDFVTTDA GTGLVHTAPG FGEDDFNIGV KYGLDVYVPV DDKGYMTEDT 370 380 390 400 410 420 GEDFAGLFYE DANEVSLKKL EEAGVLLKQM DYEHSYPFDW RTKKPIIFRA TPQWFASVDK 430 440 450 460 470 480 IRDQILGAIN EVQFFPDWGQ KRLYNMIRDR GDWVISRQRV WGVPLPIFYG EDGEAIMTKE 490 500 510 520 530 540 TIEHVAKLVE EHGSNIWFQR EAKDLLPEGF TSEHSPNGKF TKETDIMDVW FDSGSSHQGV 550 560 570 580 590 600 CAERDYLTYP ADLYLEGSDQ YRGWFNSSLI TSVAYSGHAP YKQILSQGFT LDGKGRKMSK 610 620 630 640 650 660 SLGNTIVPSE VIDKMGAEII RLWVLSVDTS ADVRVSMGSF QQIAESYRKF RNTVRFLLAN 670 680 690 700 710 720 TTDFDPAKNA VAFDEMESID KYMTVLVNKF TKEILDAYAN YEFMEIYKKL INFITTDLSA 730 740 750 760 770 780 FYMDVAKDVV YIEAPDSKKR RSMQTVLYDV VVRLTKLMTP ILPHTTEEIW KYLKEDEEYA 790 800 810 820 830 840 QLSEMPEVKH FNNEEKLVDL WNRFMNLRSG VFKALEEARN EKLIGKSFEA HVDLYVSNGV 850 860 870 880 890 900 QADLDALNAN VRQALIVSAL DVHPLSEAPE NALKFNDEYA VVVEHAEGEV CPRCRMIKTD 910 920 930 IGSDADLPTL CASCAEIVRE NYPEALTEGL E

References

[1]

"Multireplicon genome architecture of Lactobacillus salivarius." Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W. Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UCC118.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000233 Genomic DNA. Translation: ABD99850.1.
RefSeq	YP_535933.1. NC_007929.1.
3D structure databases
ProteinModelPortal	Q1WTA9.
SMR	Q1WTA9. Positions 1-920.
ModBase	Search...
Protein-protein interaction databases
STRING	362948.LSL_1042.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD99850; ABD99850; LSL_1042.
GeneID	3976743.
KEGG	lsl:LSL_1042.
PATRIC	22278987. VBILacSal43464_1115.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	LSAL362948:GJDJ-1120-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_LACS1

Accession

Primary (citable) accession number: Q1WTA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 2, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program