Q47QV9 (SYI_THEFY) 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:	Tfu_1120

Organism

Thermobifida fusca (strain YX) [Complete proteome] [HAMAP]

Taxonomic identifier

269800 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Nocardiopsaceae › Thermobifida › Thermomonospora fusca

Protein attributes

Sequence length	1060 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_02003
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003
Cofactor	Zinc 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_02003
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 1060	1060	Isoleucine--tRNA ligase HAMAP-Rule MF_02003		PRO_0000098565
Regions
	Motif	55 – 65	11	"HIGH" region HAMAP-Rule MF_02003
	Motif	608 – 612	5	"KMSKS" region HAMAP-Rule MF_02003
Sites
	Binding site	611	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q47QV9 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 3DA876E2028CE987	FASTA	1,060	118,881
	10 20 30 40 50 60 MSKESTRPFP TLPAQIDLPA MEHEVLRRWE EHKIFERSLE QTQGGPTWVF YEGPPTANGT 70 80 90 100 110 120 PGVHHVEARV FKDVFPRFKT MKGFYVERKA GWDCHGLPVE VAVEKELGIS GKKDIEAFGI 130 140 150 160 170 180 AEFNARCRES VLRNVDAFTE MTRRMGYWVN MDEAYRTMDR EYVESVWWAI KQIWDKGLLV 190 200 210 220 230 240 QDYRISPYCP RCGTTLSDHE LAQGYETVTD PSVYVRFPLT SGPLAGQAAL LVWTTTPWTL 250 260 270 280 290 300 VSNTAVAVHP EVDYVVATDG SEQLVVAEPL VGAALGDGWT LTGQRFKGAE LERWTYQRPF 310 320 330 340 350 360 ELVEFDSPAH FVVLGDYVTV EDGTGLVHQA PAFGADDMQV CRAYGLPVVN PVRNDGTFEE 370 380 390 400 410 420 HLDLVGDEFF KTADAALVAD LKDRGLLFKH LDYEHSYPHC WRCHTPLMYY AVPSWYIKTT 430 440 450 460 470 480 AIKDQLLAEN AKTNWVPANV KDGRYGEWLR NNVDWALSRS RYWGTPLPIW EFPDGRRICV 490 500 510 520 530 540 GSLKELSELS GQDLSDLDPH RPYVDDIVIP DPDADPSLPL EQRVARRVPE VIDVWFDSGA 550 560 570 580 590 600 MPFAQWGAPH RNQEKFEANF PAQYICEAID QTRGWFYSLM AVSTLVFGRS SYENVVCLGH 610 620 630 640 650 660 ILAEDGRKMS KHLGNILEPI PVMDRHGADA LRWFMAASGS PWMPRRVGHT VLEEIVRKVL 670 680 690 700 710 720 LTYYNSASFF TLYAGAGDGW SHEQLADAPA PQDRPLLDRW ILSELHSLIK TVDDALERFD 730 740 750 760 770 780 TALAGRALTT FIDDLSNWYV RRSRRRFWAG AGTPEGAAAF ATLFECLETL TLLMAPIVPF 790 800 810 820 830 840 ITDHVWQALR RPDAPESVHL ASWPKADESL IDPALSEQMA LVRRLVELGR AARVDSGQRV 850 860 870 880 890 900 RQPLARALVG APGFAELPEQ LRAQIAEELN VVQLDPLSVV GGDLVDYSVK PNFRALGKRF 910 920 930 940 950 960 GKTTPRVAQA IREADAKTLV ERLRADNAAT VDVDGEQVVL SADEVVVTEQ PREGWTVASE 970 980 990 1000 1010 1020 AGETVALDLE LTPELRRAGV AREVIRLVQD ARKSSGLNIS DRIHLWWSAT DEMTAQAMAE 1030 1040 1050 1060 HAEAISSEVL AVSFTEGTGD ADAYEVVSEE FGITLRLRKA

References

[1]

"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX." Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N. J. Bacteriol. 189:2477-2486(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YX.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000088 Genomic DNA. Translation: AAZ55158.1.
RefSeq	YP_289181.1. NC_007333.1.
3D structure databases
ProteinModelPortal	Q47QV9.
ModBase	Search...
Protein-protein interaction databases
STRING	269800.Tfu_1120.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAZ55158; AAZ55158; Tfu_1120.
GeneID	3579322.
KEGG	tfu:Tfu_1120.
PATRIC	23902736. VBITheFus33945_1168.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246403.
KO	K01870.
OMA	SRSRYWG.
ProtClustDB	PRK06039.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02003. Ile_tRNA_synth_type2.
InterPro	IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023586. Ile-tRNA-ligase_type2. 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. [Graphical view]
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_THEFY

Accession

Primary (citable) accession number: Q47QV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	September 13, 2005
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