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InterPro: IPR001387 Helix-turn-helix type 3

Protein matchesHelp
UniProtKB
Matches:
27064 proteins
AccessionHelp IPR001387 HTH_3
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR010982 Lambda repressor-like, DNA-binding
Found in IPR013430 Addiction module antidote protein, HigA
IPR013435 Mobile mystery protein A
IPR016429 Bifunctional transcriptional regulator NadR
IPR016472 Transcriptional regulator, MJ0621, predicted
IPR016759 RapGH repressor
IPR017158 Transcriptional regulator, CBS domain-containing, predicted
IPR017271 HTH transcriptional regulator, MJ1545, predicted
IPR017507 Transcriptional regulator, HipB-like
IPR020886 HTH transcriptional regulator, cro/C1-type DNA-binding domain-containing
GO Term annotationHelp
Function GO:0043565 sequence-specific DNA binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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).

Structural linksHelp
CATH: 1.10.260.40
Database linksHelp
PROSITE doc: PDOC50943
PANDIT: PF01381
Blocks: IPB001387
Pfam Clan: CL0123.14

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001387 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14467 Multiprotein-bridging factor 1

O60869 Endothelial differentiation-related factor 1

P06533 HTH-type transcriptional regulator sinR

Q9JMG1 Endothelial differentiation-related factor 1

Q9LV58 Multiprotein-bridging factor 1c

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR010981 SinR repressor/SinI anti-repressor, dimerisation
IPR001387 Helix-turn-helix type 3
IPR010982 Lambda repressor-like, DNA-binding
IPR013729 Multiprotein bridging factor 1, N-terminal
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Watkins D, Hsiao C, Woods KK, Koudelka GB, Williams LD.
P22 c2 repressor-operator complex: mechanisms of direct and indirect readout.
Biochemistry 47 2008 2325-38 [PubMed: 18237194]
http://dx.doi.org/10.1021/bi701826f
McGeehan JE, Streeter SD, Papapanagiotou I, Fox GC, Kneale GG.
High-resolution crystal structure of the restriction-modification controller protein C.AhdI from Aeromonas hydrophila.
J. Mol. Biol. 346 2005 689-701 [PubMed: 15713456]
http://dx.doi.org/10.1016/j.jmb.2004.12.025
Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL.
Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme.
Nature 437 2005 838-44 [PubMed: 16015285]
http://dx.doi.org/10.1038/nature03924
Kabe Y, Goto M, Shima D, Imai T, Wada T, Morohashi K, Shirakawa M, Hirose S, Handa H.
The role of human MBF1 as a transcriptional coactivator.
J. Biol. Chem. 274 1999 34196-202 [PubMed: 10567391]
http://dx.doi.org/10.1074/jbc.274.48.34196
Steinmetzer K, Behlke J, Brantl S, Lorenz M.
CopR binds and bends its target DNA: a footprinting and fluorescence resonance energy transfer study.
Nucleic Acids Res. 30 2002 2052-60 [PubMed: 11972345]
http://dx.doi.org/10.1093/nar/30.9.2052
Shi K, Brown CK, Gu ZY, Kozlowicz BK, Dunny GM, Ohlendorf DH, Earhart CA.
Structure of peptide sex pheromone receptor PrgX and PrgX/pheromone complexes and regulation of conjugation in Enterococcus faecalis.
Proc. Natl. Acad. Sci. U.S.A. 102 2005 18596-601 [PubMed: 16339309]
http://dx.doi.org/10.1073/pnas.0506163102
Takemaru K, Li FQ, Ueda H, Hirose S.
Multiprotein bridging factor 1 (MBF1) is an evolutionarily conserved transcriptional coactivator that connects a regulatory factor and TATA element-binding protein.
Proc. Natl. Acad. Sci. U.S.A. 94 1997 7251-6 [PubMed: 9207077]
http://dx.doi.org/10.1073/pnas.94.14.7251
Rumpel S, Becker S, Zweckstetter M.
High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment.
J. Biomol. NMR 40 2008 1-13 [PubMed: 18026911]
http://dx.doi.org/10.1007/s10858-007-9204-4
Aggarwal AK, Rodgers DW, Drottar M, Ptashne M, Harrison SC.
Recognition of a DNA operator by the repressor of phage 434: a view at high resolution.
Science 242 1988 899-907 [PubMed: 3187531]
http://www.sciencemag.org/cgi/content/abstract/242/4880/899
Lewis RJ, Brannigan JA, Offen WA, Smith I, Wilkinson AJ.
An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex.
J. Mol. Biol. 283 1998 907-12 [PubMed: 9799632]
http://dx.doi.org/10.1006/jmbi.1998.2163
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InterPro 23.1