HTH_XREHelix-turn-helix XRE-family like proteins |
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| SMART accession number: | SM00530 |
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| Description: | |
| Interpro abstract (IPR001387): | This is large family of DNA binding helix-turn helix proteins that include a bacterial plasmid copy control protein, bacterial methylases, various bacteriophage transcription control proteins and a vegetative specific protein from Dictyostelium discoideum (Slime mould). |
| GO function: | sequence-specific DNA binding (GO:0043565) |
| Family alignment: |
There are 9313 HTH_XRE domains in 9188 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae - Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Wood HE, Devine KM, McConnell DJ
- Characterisation of a repressor gene (xre) and a temperature-sensitive allele from the Bacillus subtilis prophage, PBSX.
- Gene. 1990; 96: 83-8
- Display abstract
The defective prophage of Bacillus subtilis 168, PBSX, is a chromosomally based element which encodes a non-infectious phage-like particle with bactericidal activity. PBSX is induced by agents which elicit the SOS response. In a PBSX thermoinducible strain which carries the xhi1479 mutation, PBSX is induced by raising the growth temperature from 37 degrees C to 48 degrees C. A 1.2-kb fragment has been cloned which complements the xhi1479 mutation. The nucleotide sequence of this fragment contains an open reading frame (ORF) which encodes a protein of 113 amino acids (aa). This aa sequence resembles that of other bacteriophage repressors and suggests that the N-terminal region forms a helix-turn-helix motif, typical of the DNA-binding domain of many bacterial regulatory proteins. The ORF is preceded by four 15-bp direct repeats, each of which contains an internal palindromic sequence, and by sequences resembling a SigA-dependent promoter. The nt sequence of an equivalent fragment from the PBSX thermoinducible strain has also been determined. There are three aa differences within the ORF compared to the wild type, one of which lies within the helix-turn-helix segment. This ORF encodes a repressor protein of PBSX.
- Mondragon A, Subbiah S, Almo SC, Drottar M, Harrison SC
- Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution.
- J Mol Biol. 1989; 205: 189-200
- Display abstract
The crystal structure of the amino-terminal domain of phage 434 repressor has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 A resolution. The protein comprises five short alpha-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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Click the image to view the interactive version of the map in iPath% proteins involved KEGG pathway ID Description 25.00
map00760Nicotinate and nicotinamide metabolism 17.50
map00400Phenylalanine, tyrosine and tryptophan biosynthesis 5.00
map00251Glutamate metabolism 5.00
map00230Purine metabolism 3.75
map00350Tyrosine metabolism 3.75
map00910Nitrogen metabolism 3.75
map00252Alanine and aspartate metabolism 3.75
map00530Aminosugars metabolism 3.75
map00360Phenylalanine metabolism 3.75 map00401 Novobiocin biosynthesis 3.75
map00710Carbon fixation 3.75
map00330Arginine and proline metabolism 3.75
map00950Alkaloid biosynthesis I 3.75
map00272Cysteine metabolism 1.25 map03020 RNA polymerase 1.25
map00562Inositol phosphate metabolism 1.25 map00903 Limonene and pinene degradation 1.25
map00240Pyrimidine metabolism 1.25
map00361gamma-Hexachlorocyclohexane degradation 1.25
map00626Naphthalene and anthracene degradation 1.25
map00632Benzoate degradation via CoA ligation 1.25
map00271Methionine metabolism This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with HTH_XRE domain which could be assigned to a KEGG orthologous group, and not all proteins containing HTH_XRE domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of HTH_XRE domains in PDB
PDB code Main view Title 1adr 
Determination of the nuclear magnetic resonance structure of the dna-binding domain of the p22 c2 repressor (1-76) in solution and comparison with the dna-binding domain of the 434 repressor 1b0n 
Sinr protein/sini protein complex 1lli 
The crystal structure of a mutant protein with altered but improved hydrophobic core packing 1lmb 
Refined 1.8 angstrom crystal structure of the lambda repressor-operator complex 1lrp 
Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda 1per 
The complex between phage 434 repression dna-binding domain and operator site or3: structural differences between consensus and non-consensus half-sites 1pra 
Determination of the nuclear magnetic resonance solution structure of the dna-binding domain (residues 1 to 69) of the 434 repressor and comparison with the x-ray crystal structure 1r63 
Structural role of a buried salt bridge in the 434 repressor dna-binding domain, nmr, 20 structures 1r69 
Structure of the amino-terminal domain of phage 434 repressor at 2.0 angstroms resolution 1rio 
Structure of bacteriophage lambda ci-ntd in complex with sigma-region4 of thermus aquaticus bound to dna 1rpe 
The phage 434 or2/r1-69 complex at 2.5 angstroms resolution 1sq8 
A variant 434 repressor dna binding domain devoid of hydroxyl groups, nmr, 20 structures 1utx 
Regulation of cytolysin expression by enterococcus faecalis: role of cylr2 1x57 
Solution structures of the hth domain of human edf-1 protein 1y7y 
High-resolution crystal structure of the restriction- modification controller protein c.ahdi from aeromonas hydrophila 1y9q 
Crystal structure of hth_3 family transcriptional regulator from vibrio cholerae 1zug 
Structure of phage 434 cro protein, nmr, 20 structures 1zz6 
Crystal structure of apo-hppe 1zz7 
Crystal structure of feii hppe in complex with substrate form 1 1zz8 
Crystal structure of feii hppe in complex with substrate form 2 1zz9 
Crystal structure of feii hppe 1zzb 
Crystal structure of coii hppe in complex with substrate 1zzc 
Crystal structure of coii hppe in complex with tris buffer 2a6c 
Crystal structure of (np_841403.1) from nitrosomonas europaea at 1.90 a resolution 2aw6 
Structure of a bacterial peptide pheromone/receptor complex and its mechanism of gene regulation 2awi 
Structure of prgx y153c mutant 2axu 
Structure of prgx 2axv 
Structure of prgx y153c mutant 2axz 
Crystal structure of prgx/ccf10 complex 2b5a 
C.bcli, control element of the bcli restriction- modification system 2bnm 
Structure of a zn enzyme 2bnn 
Structure of a zn enzyme 2bno 
Structure of a zn enzyme 2cro 
Structure of phage 434 cro protein at 2.35 angstroms resolution 2eby 
Crystal structure of a hypothetical protein from e. coli 2ef8 
Crystal structure of c.ecot38is 2ewt 
Crystal structure of the dna-binding domain of bldd 2grl 
Crystal structure of dct/icf10 complex 2grm 
Crystal structure of prgx/icf10 complex 2gzu 
High-resolution structure determination of the cylr2 homodimer using intermonomer distances from paramagnetic relaxation enhancement and nmr dipolar couplings 2icp 
Crystal structure of the bacterial antitoxin higa from escherichia coli at ph 4.0. northeast structural genomics consortium target er390. 2ict 
Crystal structure of the bacterial antitoxin higa from escherichia coli at ph 8.5. northeast structural genomics target er390. 2jvl 
2k9q 
2kpj 
2o38 
Putative xre family transcriptional regulator 2ofy 
Crystal structure of putative xre-family transcriptional regulator from rhodococcus sp. 2or1 
Recognition of a dna operator by the repressor of phage 434. a view at high resolution 2p5t 
Molecular and structural characterization of the pezat chromosomal toxin-antitoxin system of the human pathogen streptococcus pneumoniae 2ppx 
Crystal structure of a hth xre-family like protein from agrobacterium tumefaciens 2qfc 
Crystal structure of bacillus thuringiensis plcr complexed with papr 2r1j 
Crystal structure of the p22 c2 repressor protein in complex with the synthetic operator 9t 2r63 
Structural role of a buried salt bridge in the 434 repressor dna-binding domain, nmr, 20 structures 2wiu 
3b7h 
Crystal structure of the prophage lp1 protein 11 3bdn 
Crystal structure of the lambda repressor 3bs3 
Crystal structure of a putative dna-binding protein from bacteroides fragilis 3cec 
Crystal structure of putative antidote protein of plasmid maintenance system (zp_00107635.1) from nostoc punctiforme pcc 73102 at 1.60 a resolution 3clc 
Crystal structure of the restriction-modification controller protein c.esp1396i tetramer in complex with its natural 35 base-pair operator 3cro 
The phage 434 cro/or1 complex at 2.5 angstroms resolution 3dnv 
3eus 
3f51 
3f52 
3f6w 
3fya 
3g5g 
3g7d 
3gbf 
3hzi 
3ivp 
- Links (links to other resources describing this domain)
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PFAM HTH_3 INTERPRO IPR001387






