InterPro : IPR010982

Name  Lambda repressor-like, DNA-binding domain Short Name  Lambda_DNA-bd_dom
Type  Domain Description  Bacteriophage lambdaC1 repressor controls the expression of viral genes as part of the lysogeny/lytic growth switch. C1 is essential for maintaining lysogeny, where the phage replicates non-disruptively along with the host. If the host cell is threatened, then lytic growth is induced. The Lambda C1 repressor consists of two domains connected by a linker: an N-terminal DNA-binding domain that also mediates interactions with RNA polymerase, and a C-terminal dimerisation domain []. The DNA-binding domain consists of four helices in a closed folded leaf motif. Several different phage repressors from different helix-turn-helix families contain DNA-binding domains that adopt a similar topology. These include the Lambda Cro repressor, Bacteriophage 434C1 and Cro repressors, P22 C2 repressor, and Bacteriophage MuNer protein.The DNA-binding domain of Bacillus subtilisspore inhibition repressor SinR is identical to that of phage repressors []. SinR represses sporulation, which only occurs in response to adverse conditions. This provides a possible evolutionary link between the two adaptive responses of bacterial sporulation and prophage induction.Other DNA-binding domains also display similar structural folds to that of Lambda C1. These include bacterial regulators such as the purine repressor (PurR), the lactose repressor (Lacr) and the fructose repressor (FruR), each of which has an N-terminal DNA-binding domain that exhibits a fold similar to that of lambda C1, except that they lack the first helix [, , ]. POU-specific domains found in transcription factors such as in Oct-1, Pit-1 and Hepatocyte nuclear factor 1a (LFB1/HNF1) display four-helical fold DNA-binding domains similar to that of Lambda C1 [, , ]. The N-terminal domain of cyanase has an alpha-helix bundle motif similar to Lambda C1, but it probably does not bind DNA. Cyanase is an enzyme found in bacteria and plants that catalyses the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide in response to extracellular cyanate [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

3 Child Features

Id Name Short Name Type
IPR001387 Cro/C1-type helix-turn-helix domain Cro/C1-type_HTH Domain
IPR000843 Transcription regulator HTH, LacI Tscrpt_reg_HTH_LacI Domain
IPR027910 YdiL-like domain YdiL-like Domain

0 Contains

13 Found In

Id Name Short Name Type
IPR000327 POU-specific POU_specific Domain
IPR015584 POU domain-containing protein, class 4-related POU4-related Family
IPR015586 Pituitary-specific positive transcription factor 1 Pit_1 Family
IPR006899 Hepatocyte nuclear factor 1, N-terminal HNF-1_N Domain
IPR015585 POU domain-containing protein, class 5 POU_dom_5 Family
IPR016362 Transcription factor, homeobox/POU Transcription_factor_POU Family
IPR004451 Conserved hypothetical protein CHP00270 CHP00270 Family
IPR000972 Octamer-binding transcription factor TF_octamer Family
IPR022452 Zinc finger/helix-turn-helix protein, YgiT Znf/HTH_YgiT Family
IPR010744 Bacteriophage CI repressor Phage_CI_repr Family
IPR008076 Cyanate hydratase Cyanase Family
IPR015060 Protein of unknown functionDUF1870 DUF1870 Family
IPR020886 Transcription regulator HTH, Cro/C1-type DNA-binding Tscrpt_reg_HTH_Cro/C1 Family

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Jacobson EM Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility. 1997 Genes Dev 11 198-212
Walsh MA Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. 2000 Structure 8 505-14
Lewis RJ An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex. 1998 J Mol Biol 283 907-12
Bell CE Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. 2000 Cell 101 801-11
Schumacher MA Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices. 1994 Science 266 763-70
Bell CE A closer view of the conformation of the Lac repressor bound to operator. 2000 Nat Struct Biol 7 209-14
Penin F Three-dimensional structure of the DNA-binding domain of the fructose repressor from Escherichia coli by 1H and 15N NMR. 1997 J Mol Biol 270 496-510
Reményi A Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping. 2001 Mol Cell 8 569-80
Chi YI Diabetes mutations delineate an atypical POU domain in HNF-1alpha. 2002 Mol Cell 10 1129-37



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)