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InterPro: IPR006199 LexA, DNA-binding domain

Protein matches Help

UniProtKB

Matches:

1411 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

IPR006199 LexA_DNA-bd_dom

Secondary

IPR002865

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01726	LexA_DNA_bind	1411
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011991 Winged helix repressor DNA-binding

Found in

IPR006200 Peptidase S24, LexA repressor

GO Term annotation Help

Process

GO:0006508 proteolysis

Function

GO:0004252 serine-type endopeptidase activity

InterPro annotation

Entry Details in BioMart

Abstract

This is the DNA binding domain of the LexA SOS regulon repressor which prevents expression of DNA repair proteins in bacteria. The aligned region contains a variant form of the helix-turn-helix DNA binding motif [1]. This domain usually at the N terminus is found associated with IPR006198 the auto-proteolytic domain of LexA EC:3.4.21.88.

Structural links Help

PDB - click here

SCOP: a.4.5.2 , b.87.1.1

CATH: 1.10.10.10

Database links Help

Enzyme: EC:3.4.21.88

PANDIT: PF01726

Blocks: IPB006199

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006199

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A5GWB6 Heat-inducible transcription repressor hrcA

P0A7C2 LexA repressor

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code

Publications Open in usermanual
1.	Fogh RH, Ottleben G, Ruterjans H, Schnarr M, Boelens R, Kaptein R. Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy. EMBO J. 13 3936-44 1994 [PubMed: 8076591] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8076591

Additional Reading Open in usermanual
	Luo Y, Pfuetzner RA, Mosimann S, Paetzel M, Frey EA, Cherney M, Kim B, Little JW, Strynadka NC. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 106 2001 585-94 [PubMed: 11551506] http://dx.doi.org/10.1016/S0092-8674(01)00479-2

InterPro 23.1