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InterPro: IPR000738 WHEP-TRS

Protein matches Help

UniProtKB

Matches:

246 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

IPR000738 WHEP-TRS

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00458	WHEP-TRS	216
PROSITE pattern	PS00762	WHEP_TRS_1	130
PROSITE profile	PS51185	WHEP_TRS_2	236
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009068 S15/NS1, RNA-binding

GO Term annotation Help

Process

GO:0006418 tRNA aminoacylation for protein translation

Function

GO:0004812 aminoacyl-tRNA ligase activity
GO:0005524 ATP binding

InterPro annotation

Entry Details in BioMart

Abstract

A conserved domain of 46 amino acids, called WHEP-TRS has been shown [1] to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases. This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases [2]. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.

Structural links Help

PDB - click here

SCOP: a.16.1.3 , c.26.1.1

CATH: 1.10.287.10

Database links Help

PDBe-motif: PS00762

Enzyme: EC:6.1.1

PROSITE doc: PDOC00614

PANDIT: PF00458

Blocks: IPB000738

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000738

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O23627 Glycyl-tRNA synthetase 1, mitochondrial

P07814 Bifunctional aminoacyl-tRNA synthetase

P28668 Bifunctional aminoacyl-tRNA synthetase

P32921 Tryptophanyl-tRNA synthetase, cytoplasmic

Q10039 Glycyl-tRNA synthetase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017449	Prolyl-tRNA synthetase, class II
IPR020056	Ribosomal protein L25/Gln-tRNA synthetase, beta-barrel domain
IPR010987	Glutathione S-transferase, C-terminal-like
IPR018160	Glycyl-tRNA synthetase, alpha2 dimer, C-terminal
IPR004499	Prolyl-tRNA synthetase, class IIa, prokaryotic-type
IPR002305	Aminoacyl-tRNA synthetase, class Ib
IPR002306	Tryptophanyl-tRNA synthetase, class Ib
IPR000738	WHEP-TRS
IPR016061	Prolyl-tRNA synthetase, class II, C-terminal
IPR011035	Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain
IPR000924	Glutamyl/glutaminyl-tRNA synthetase, class Ic
IPR020059	Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain
IPR020058	Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain
IPR009068	S15/NS1, RNA-binding
IPR020060	Glutamyl/glutaminyl-tRNA synthetase, class Ic, N-terminal
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR004526	Glutamyl-tRNA synthetase, class Ic, archaeal/eukaryotic cytosolic
IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
IPR002315	Glycyl-tRNA synthetase, alpha2 dimer
IPR020061	Glutamyl/glutaminyl-tRNA synthetase, class Ic, alpha-bundle domain
IPR004154	Anticodon-binding
IPR002314	Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region
IPR006195	Aminoacyl-tRNA synthetase, class II, conserved region
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M. A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 10 4267-77 1991 [PubMed: 1756734] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1756734&action=stream&blobtype=pdf
2.	Nada S, Chang PK, Dignam JD. Primary structure of the gene for glycyl-tRNA synthetase from Bombyx mori. J. Biol. Chem. 268 7660-7 1993 [PubMed: 8463296] http://intl.jbc.org/cgi/reprint/268/11/7660.pdf

Additional Reading Open in usermanual
	Shen N, Zhou M, Yang B, Yu Y, Dong X, Ding J. Catalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states. Nucleic Acids Res. 36 2008 1288-99 [PubMed: 18180246] http://dx.doi.org/10.1093/nar/gkm1153
	Yang XL, Otero FJ, Ewalt KL, Liu J, Swairjo MA, Kohrer C, RajBhandary UL, Skene RJ, McRee DE, Schimmel P. Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis. EMBO J. 25 2006 2919-29 [PubMed: 16724112] http://dx.doi.org/10.1038/sj.emboj.7601154
	Rho SB, Lee JS, Jeong EJ, Kim KS, Kim YG, Kim S. A multifunctional repeated motif is present in human bifunctional tRNA synthetase. J. Biol. Chem. 273 1998 11267-73 [PubMed: 9556618] http://dx.doi.org/10.1074/jbc.273.18.11267
	Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J. Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity. J. Biol. Chem. 279 2004 8378-88 [PubMed: 14660560] http://dx.doi.org/10.1074/jbc.M311284200
	Shen N, Guo L, Yang B, Jin Y, Ding J. Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity. Nucleic Acids Res. 34 2006 3246-58 [PubMed: 16798914] http://dx.doi.org/10.1093/nar/gkl441
	Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS. Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry 39 2000 15775-82 [PubMed: 11123902] http://dx.doi.org/10.1021/bi001393h
	Yang XL, Guo M, Kapoor M, Ewalt KL, Otero FJ, Skene RJ, McRee DE, Schimmel P. Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase. Structure 15 2007 793-805 [PubMed: 17637340] http://dx.doi.org/10.1016/j.str.2007.05.009

InterPro 23.1