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InterPro: IPR018353 Isoleucyl-tRNA synthetase

Protein matches Help

UniProtKB

Matches:

2394 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR018353 Isoleucyl-tRNA_synthetase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11946:SF9	Ile-tRNA-synt_Ia	2394
Signatures in BioMart

InterPro Relationships Help

Children

IPR002301 Isoleucyl-tRNA synthetase, class Ia

Contains

IPR001412 Aminoacyl-tRNA synthetase, class I, conserved site
IPR002300 Aminoacyl-tRNA synthetase, class Ia
IPR009008 Valyl/Leucyl/Isoleucyl-tRNA synthetase, class Ia, editing
IPR009080 Aminoacyl-tRNA synthetase, class 1a, anticodon-binding
IPR013155 Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
IPR015905 Isoleucyl-tRNA synthetase, class Ia, N-terminal

GO Term annotation Help

Process

GO:0006412 translation

Function

GO:0004822 isoleucine-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

Isoleucyl-tRNA synthetase (EC:6.1.1.5) is an alpha monomer that belongs to class Ia. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyses only the valylated products [1, 2] as shown from the crystal structures.

Structural links Help

PDB - click here

SCOP: a.27.1.1 , b.51.1.1 , c.26.1.1

CATH: 1.10.730.10 , 3.40.50.620 , 3.90.740.10

Database links Help

Enzyme: EC:6.1.1.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018353

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P09436 Isoleucyl-tRNA synthetase, cytoplasmic

P41252 Isoleucyl-tRNA synthetase, cytoplasmic

P73505 Isoleucyl-tRNA synthetase

Q21926 Isoleucyl-tRNA synthetase, cytoplasmic

Q8BIJ6 Isoleucyl-tRNA synthetase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013155	Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding
IPR002300	Aminoacyl-tRNA synthetase, class Ia
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR002301	Isoleucyl-tRNA synthetase, class Ia
IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
IPR010663	DNA glycosylase/AP lyase/isoleucyl tRNA synthetase, zinc finger domain
IPR018353	Isoleucyl-tRNA synthetase
IPR009080	Aminoacyl-tRNA synthetase, class 1a, anticodon-binding
IPR009008	Valyl/Leucyl/Isoleucyl-tRNA synthetase, class Ia, editing
IPR015905	Isoleucyl-tRNA synthetase, class Ia, N-terminal
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Nureki O, Vassylyev DG, Tateno M, Shimada A, Nakama T, Fukai S, Konno M, Hendrickson TL, Schimmel P, Yokoyama S. Enzyme structure with two catalytic sites for double-sieve selection of substrate. Science 280 578-82 1998 [PubMed: 9554847] http://dx.doi.org/10.1126/science.280.5363.578
2.	Silvian LF, Wang J, Steitz TA. Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. Science 285 1074-7 1999 [PubMed: 10446055] http://dx.doi.org/10.1126/science.285.5430.1074

Additional Reading Open in usermanual
	Fukunaga R, Yokoyama S. Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase. J. Mol. Biol. 359 2006 901-12 [PubMed: 16697013] http://dx.doi.org/10.1016/j.jmb.2006.04.025
	Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S. Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine. J. Biol. Chem. 279 2004 8396-402 [PubMed: 14672940] http://dx.doi.org/10.1074/jbc.M312830200
	Nakama T, Nureki O, Yokoyama S. Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase. J. Biol. Chem. 276 2001 47387-93 [PubMed: 11584022] http://dx.doi.org/10.1074/jbc.M109089200

InterPro 23.1