Q47BK5 (SYI_DECAR) 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:	Daro_3046

Organism

Dechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]

Taxonomic identifier

159087 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Dechloromonas › Dechloromonas aromatica

Protein attributes

Sequence length	932 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 – 932	932	Isoleucine--tRNA ligase HAMAP-Rule MF_02002		PRO_0000098378
Regions
	Motif	58 – 68	11	"HIGH" region HAMAP-Rule MF_02002
	Motif	611 – 615	5	"KMSKS" region HAMAP-Rule MF_02002
Sites
	Metal binding	895	1	Zinc By similarity
	Metal binding	898	1	Zinc By similarity
	Metal binding	915	1	Zinc By similarity
	Metal binding	918	1	Zinc By similarity
	Binding site	570	1	Aminoacyl-adenylate By similarity
	Binding site	614	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q47BK5 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 06C1ECF9BC461869	FASTA	932	104,052
	10 20 30 40 50 60 MADYKDSLNL PDTAFPMRGD LPKREPQWVA QWQEKKLYQR IREICAGRPR FTLHDGPPYA 70 80 90 100 110 120 NGDIHIGHAV NKVLKDIIVR SKTLSGFDAP YVPGWDCHGL PIEHQIEKLH GKAIPADKVR 130 140 150 160 170 180 ELSRAYAAEQ VERQKKDFIR LGVLGDWGNP YLTMNFSAEA GEIRALGKIL EQGYLYQGLK 190 200 210 220 230 240 PVNWCLDCGS ALAEAEVEYE DKNSPAIDVA FEVHENHTAK LAAAFGLTHL RGPAFAVIWT 250 260 270 280 290 300 TTPWTLPANE AVSVHPDLTY DLIETEKGAL ILVRELAEAA LKRYGLEGTV AGSCTGDKLD 310 320 330 340 350 360 QMLLKHPFQN RDVAIICGTH VTTEAGTGLV HTAPAHGVDD YNIGKKYGLP VNNPVGNDGK 370 380 390 400 410 420 FISTTPALSV GELAGKTVWE ANPQVLQELE ARARLLKNER IQHSYPHCWR HKTPIIFRAT 430 440 450 460 470 480 TQWFIGMENK KNEDASTLRW IAERAVDETQ FFPAWGRARL EGMMKTRPDW CVSRQRNWGV 490 500 510 520 530 540 PIPFFLHKET GQPHPRTAEL IEQVALRVEK SGIEAWFSLD AAELLGAEAD QYVKMKDTLD 550 560 570 580 590 600 VWFDSGTTHW HVMRGSHAAD HTYPADLYLE GSDQHRGWFQ SSLLSGCAID GRAPYKGLLT 610 620 630 640 650 660 HGFVVDGKGH KMSKSKGNVI APQQVSDKMG ADILRLWTAS TDYSGELTIS DEILKRVVEG 670 680 690 700 710 720 YRRIRNTLRF LLANVSDFDA ATDMLPIDQW LEIDRYALAL TRELQDGCRA DFDKYEFHRV 730 740 750 760 770 780 VQALQTFCSE DLGGFYLDIL KDRLYTTAPK SVARRSAQSA LWHITQAFVR LLAPITAFTA 790 800 810 820 830 840 EEVWQVLTGK ADDSVMFQVW HDLPALAGEG DLLAKWALIR TARADVTKAL EAQREAGKIG 850 860 870 880 890 900 SALQAAVEIH CGGEKYEALA SLGDDLKFVF ICSSTVAVRD DNEQVIATPL EHAKCERCWH 910 920 930 VREDVGANTE HPTLCGRCVS NLYGEGEVRG CA

References

[1]

"Complete sequence of Dechloromonas aromatica RCB." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RCB.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000089 Genomic DNA. Translation: AAZ47776.1.
RefSeq	YP_286246.1. NC_007298.1.
3D structure databases
ProteinModelPortal	Q47BK5.
ModBase	Search...
Protein-protein interaction databases
STRING	159087.Daro_3046.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAZ47776; AAZ47776; Daro_3046.
GeneID	3568250.
KEGG	dar:Daro_3046.
PATRIC	21604760. VBIDecAro89105_3025.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246402.
KO	K01870.
OMA	KQVLTHG.
ProtClustDB	PRK05743.
Enzyme and pathway databases
BioCyc	DARO159087:GI5B-3125-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_DECAR

Accession

Primary (citable) accession number: Q47BK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program