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InterPro: IPR002547 tRNA-binding domain

Protein matches Help

UniProtKB

Matches:

4127 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

IPR002547 tRNA-bd_dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01588	tRNA_bind	4125
PROSITE profile	PS50886	TRBD	4116
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012340 Nucleic acid-binding, OB-fold

Children

IPR004495 Methionyl-tRNA synthetase, class Ia, beta subunit, C-terminal

Found in

IPR004532 Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial
IPR008231 Secretion chaperone CsaA

GO Term annotation Help

Function

GO:0000049 tRNA binding

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1) [1], human tyrosyl-tRNA synthetase [2], and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases [1]. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme [1]. This domain may perform a common function in tRNA aminoacylation [2].

Structural links Help

PDB - click here

SCOP: b.40.4.4

CATH: 2.40.50.140

Database links Help

Enzyme: EC:6.1.1

PROSITE doc: PDOC50886

PANDIT: PF01588

Blocks: IPB002547

Pfam Clan: CL0021.14

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002547

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P31230 Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1

P46672 GU4 nucleic-binding protein 1

P54577 Tyrosyl-tRNA synthetase, cytoplasmic

Q20970 Methionyl-tRNA synthetase, cytoplasmic

Q9SVN5 Probable methionyl-tRNA synthetase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
IPR002305	Aminoacyl-tRNA synthetase, class Ib
IPR002304	Methionyl-tRNA synthetase, class Ia
IPR002307	Tyrosyl-tRNA synthetase, class Ib, bacterial/mitochondrial
IPR014758	Methionyl-tRNA synthetase, class Ia, N-terminal
IPR016027	Nucleic acid-binding, OB-fold-like
IPR015413	Aminoacyl-tRNA synthetase, class I (M)
IPR012340	Nucleic acid-binding, OB-fold
IPR002547	tRNA-binding domain
IPR009080	Aminoacyl-tRNA synthetase, class 1a, anticodon-binding
IPR015624	Tyrosyl-tRNA synthetase, class Ib, archaeal/eukaryotic cytosolic
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J. 15 5437-48 1996 [PubMed: 8895587] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8895587
2.	Kleeman TA, Wei D, Simpson KL, First EA. Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J. Biol. Chem. 272 14420-5 1997 [PubMed: 9162081] http://dx.doi.org/10.1074/jbc.272.22.14420

Additional Reading Open in usermanual
	Kaminska M, Deniziak M, Kerjan P, Barciszewski J, Mirande M. A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation. EMBO J. 19 2000 6908-17 [PubMed: 11118226] http://dx.doi.org/10.1093/emboj/19.24.6908
	Kawaguchi S, Muller J, Linde D, Kuramitsu S, Shibata T, Inoue Y, Vassylyev DG, Yokoyama S. The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus. EMBO J. 20 2001 562-9 [PubMed: 11157762] http://dx.doi.org/10.1093/emboj/20.3.562
	Shapova YA, Paetzel M. Crystallographic analysis of Bacillus subtilis CsaA. Acta Crystallogr. D Biol. Crystallogr. 63 2007 478-85 [PubMed: 17372352] http://dx.doi.org/10.1107/S0907444907005045
	Galani K, Grosshans H, Deinert K, Hurt EC, Simos G. The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p. EMBO J. 20 2001 6889-98 [PubMed: 11726524] http://dx.doi.org/10.1093/emboj/20.23.6889
	Renault L, Kerjan P, Pasqualato S, Menetrey J, Robinson JC, Kawaguchi S, Vassylyev DG, Yokoyama S, Mirande M, Cherfils J. Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry. EMBO J. 20 2001 570-8 [PubMed: 11157763] http://dx.doi.org/10.1093/emboj/20.3.570
	Kim Y, Shin J, Li R, Cheong C, Kim K, Kim S. A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases. J. Biol. Chem. 275 2000 27062-8 [PubMed: 10852899] http://intl.jbc.org/cgi/content/abstract/275/35/27062
	Kotik-Kogan O, Moor N, Tworowski D, Safro M. Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase. Structure 13 2005 1799-807 [PubMed: 16338408] http://dx.doi.org/10.1016/j.str.2005.08.013
	Moor N, Kotik-Kogan O, Tworowski D, Sukhanova M, Safro M. The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end. Biochemistry 45 2006 10572-83 [PubMed: 16939209] http://dx.doi.org/10.1021/bi060491l
	Crepin T, Schmitt E, Blanquet S, Mechulam Y. Structure and function of the C-terminal domain of methionyl-tRNA synthetase. Biochemistry 41 2002 13003-11 [PubMed: 12390027] http://dx.doi.org/10.1021/bi026343m
	Fishman R, Ankilova V, Moor N, Safro M. Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese. Acta Crystallogr. D Biol. Crystallogr. 57 2001 1534-44 [PubMed: 11679717] http://dx.doi.org/10.1107/S090744490101321X

InterPro 23.1