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InterPro: IPR004154 Anticodon-binding

Protein matches Help

UniProtKB

Matches:

7536 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

IPR004154 Anticodon_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.50.800	Anticodon_bd	7159
Pfam	PF03129	HGTP_anticodon	7343
SuperFamily	SSF52954	Anticodon_bd	7485
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002315 Glycyl-tRNA synthetase, alpha2 dimer
IPR002320 Threonyl-tRNA synthetase, class IIa
IPR004499 Prolyl-tRNA synthetase, class IIa, prokaryotic-type
IPR004500 Prolyl-tRNA synthetase, class IIa, bacterial
IPR004516 Histidyl-tRNA synthetase, class IIa
IPR015807 Histidyl-tRNA synthetase, class IIa, subgroup
IPR018160 Glycyl-tRNA synthetase, alpha2 dimer, C-terminal

GO Term annotation Help

Process

GO:0006412 translation

Function

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

InterPro annotation

Entry Details in BioMart

Abstract

tRNA synthetases, or tRNA ligases are involved in protein synthesis. This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases [1] it is probably the anticodon binding domain [2].

Structural links Help

PDB - click here

SCOP: c.51.1.1 , d.104.1.1

CATH: 3.30.930.10 , 3.40.50.800

Database links Help

Enzyme: EC:6.1.1

PANDIT: PF03129

Blocks: IPB004154

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004154

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P04801 Threonyl-tRNA synthetase, cytoplasmic

P07814 Bifunctional aminoacyl-tRNA synthetase

P28668 Bifunctional aminoacyl-tRNA synthetase

P34183 Histidyl-tRNA synthetase

Q9QZM2 DNA polymerase subunit gamma-2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017449	Prolyl-tRNA synthetase, class II
IPR004516	Histidyl-tRNA synthetase, class IIa
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
IPR012947	Threonyl/alanyl tRNA synthetase, SAD
IPR000738	WHEP-TRS
IPR018158	Threonyl-tRNA synthetase, class IIa, conserved region
IPR016061	Prolyl-tRNA synthetase, class II, C-terminal
IPR004095	TGS
IPR011035	Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain
IPR000924	Glutamyl/glutaminyl-tRNA synthetase, class Ic
IPR015807	Histidyl-tRNA synthetase, class IIa, subgroup
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
IPR002320	Threonyl-tRNA synthetase, class IIa
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
IPR012676	TGS-like
IPR012675	Beta-grasp fold, ferredoxin-type
IPR006195	Aminoacyl-tRNA synthetase, class II, conserved region
IPR018163	Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Wolf YI, Aravind L, Grishin NV, Koonin EV. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 9 689-710 1999 [PubMed: 10447505] http://www.genome.org/cgi/content/abstract/9/8/689
2.	Aberg A, Yaremchuk A, Tukalo M, Rasmussen B, Cusack S. Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry 36 3084-94 1997 [PubMed: 9115984] http://dx.doi.org/10.1021/bi9618373

Additional Reading Open in usermanual
	Fan L, Kim S, Farr CL, Schaefer KT, Randolph KM, Tainer JA, Kaguni LS. A novel processive mechanism for DNA synthesis revealed by structure, modeling and mutagenesis of the accessory subunit of human mitochondrial DNA polymerase. J. Mol. Biol. 358 2006 1229-43 [PubMed: 16574152] http://dx.doi.org/10.1016/j.jmb.2006.02.073
	Torres-Larios A, Sankaranarayanan R, Rees B, Dock-Bregeon AC, Moras D. Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase. J. Mol. Biol. 331 2003 201-11 [PubMed: 12875846] http://dx.doi.org/10.1016/S0022-2836(03)00719-8
	Carrodeguas JA, Theis K, Bogenhagen DF, Kisker C. Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer. Mol. Cell 7 2001 43-54 [PubMed: 11172710] http://dx.doi.org/10.1016/S1097-2765(01)00153-8
	Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Soll D, Steitz TA. The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases. Proc. Natl. Acad. Sci. U.S.A. 100 2003 1673-8 [PubMed: 12578991] http://dx.doi.org/10.1073/pnas.0437911100
	Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D. Structural basis of translational control by Escherichia coli threonyl tRNA synthetase. Nat. Struct. Biol. 9 2002 343-7 [PubMed: 11953757]

InterPro 23.1