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InterPro: IPR011991 Winged helix repressor DNA-binding

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UniProtKB
Matches:
146465 proteins
AccessionHelp
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IPR011991 Wing_hlx_DNA_bd
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Domain
SignaturesHelp
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InterPro RelationshipsHelp
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Children IPR000232 Heat shock factor (HSF)-type, DNA-binding
IPR000418 Ets
IPR000485 HTH transcriptional regulator, AsnC-type
IPR000524 HTH transcriptional regulator, GntR
IPR000591 DEP domain
IPR000607 Double-stranded RNA-specific adenosine deaminase (DRADA)
IPR000847 HTH transcriptional regulator, LysR
IPR001346 Interferon regulatory factor
IPR001523 Paired box protein, N-terminal
IPR001766 Transcription factor, fork head
IPR003150 DNA-binding RFX
IPR003316 Transcription factor E2F/dimerisation partner (TDP)
IPR004409 Biotin operon repressor, helix-turn-helix region
IPR005561 ANTAR
IPR005818 Histone H1/H5
IPR006199 LexA, DNA-binding domain
IPR006630 RNA-binding protein Lupus La
IPR008823 DNA helicase, Holliday junction RuvB type, C-terminal
IPR009718 Rex DNA-binding, C-terminal
IPR014048 Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
IPR014793 Dissimilatory sulphite reductase D
IPR015191 Translation elongation factor SelB, winged helix, type 3
IPR015198 Transcription factor MotA, activation, bacteriophage
IPR015265 Bacterial purine repressor, N-terminal
IPR016032 Signal transduction response regulator, C-terminal effector
IPR019559 Cullin protein, neddylation domain
IPR020900 Arginine repressor, DNA-binding domain
Found in IPR000525 Initiator Rep protein
IPR000717 Proteasome component (PCI) domain
IPR000835 HTH transcriptional regulator, MarR
IPR000943 RNA polymerase sigma-70 factor
IPR001367 Iron dependent repressor
IPR001669 Arginine repressor
IPR001845 HTH transcriptional regulator, ArsR
IPR002571 Negative regulator of class I heat shock protein
IPR002717 MOZ/SAS-like protein
IPR002831 Transcriptional regulator TrmB
IPR002853 Transcription factor TFIIE, alpha subunit
IPR003166 Transcription factor TFIIE beta subunit, DNA-binding
IPR003196 Transcription initiation factor IIF, beta subunit
IPR003314 Transposase MuA/Repressor CI, DNA-binding
IPR003432 Replication terminator protein
IPR004085 DNA topoisomerase VI, subunit A
IPR004605 DNA helicase, Holliday junction RuvB type
IPR005149 Transcriptional regulator PadR N-terminal-like
IPR005234 Chromosome segregation/condensation protein ScpB, prokaryote
IPR005241 Transcription factor TFllE alpha-related protein
IPR005650 Penicillinase repressor
IPR005819 Histone H5
IPR006200 Peptidase S24, LexA repressor
IPR006291 Signal transduction response regulator, heavy metal response
IPR007394 Putative helix-turn-helix protein, YlxM/p13-like
IPR008851 Transcription initiation factor IIF, alpha subunit
IPR009374 Translation initiation factor 3, subunit 12, eukaryotic
IPR010166 Accessory regulator, Staphylococcus
IPR010906 Phage DNA packaging Nu1
IPR011879 Signal transduction response regulator, phosphate regulon transcriptional regulatory protein phoB
IPR012015 Uncharacterised conserved protein HTH transcriptional regulator, archaea
IPR012712 Homoprotocatechuate degradation transcriptional regulator HpaR
IPR012759 RNA polymerase sigma factor RpoH, proteobacteria
IPR012760 RNA polymerase sigma factor RpoD, C-terminal
IPR012761 RNA polymerase sigma factor RpoS, proteobacteria
IPR012845 RNA polymerase sigma factor, FliA/WhiG
IPR012967 Plant methyltransferase dimerisation
IPR014071 Copper transport repressor CopY/TcrY
IPR014075 SUF system FeS cluster assembly, SufR regulator, cyanobacteria
IPR014091 Transcriptional repressor poly-beta-hydroxybutyrate-responsive
IPR014200 RNA polymerase sigma-E type
IPR014209 RNA polymerase sigma-K type
IPR014212 RNA polymerase sigma-G type
IPR014218 RNA polymerase sigma-H type
IPR014236 RNA polymerase sigma-F type
IPR014277 Cell division control protein 6 related, archaea
IPR014284 RNA polymerase sigma-70
IPR014288 RNA polymerase sigma-B type
IPR014322 RNA polymerase sigma-B/F/G type
IPR014646 Replication protein A, subunit RPA32
IPR014892 Replication protein A, C-terminal
IPR015210 Restriction endonuclease, type II, NaeI, C-terminal
IPR016262 RNA polymerase sigma factor, SigB/SigC/SigD, plastid
IPR016263 RNA polymerase sporulation-specific sigma factor, SigK/SigE
IPR016371 RNA polymerase sigma-H factor
IPR016461 O-methyltransferase, COMT, eukaryota
IPR016481 Transcription factor TFE, archaea
IPR016640 Transcription initiation factor IIF, beta subunit, subgroup
IPR016656 Transcription initiation factor TFIIE, beta subunit
IPR016723 Transcriptional regulator, ArsR, predicted
IPR016943 Uncharacterised conserved protein UCP030050, HTH transcriptional regulator, BH1869
IPR016998 HTH transcriptional regulator, Rot
IPR017206 Signal transduction histidine kinase, hybrid-type, BC3207, predicted
IPR017799 Transcriptional regulator, PadR, acidobacterial-type
IPR017848 RNA polymerase sigma factor, RpoD-like, cyanobacteria
IPR019888 Transcription regulator, AsnC-type
IPR019941 Transcription regulator LuxR, chaperone HchA-associated
IPR020890 HTH-type transcriptional regulator HdfR
Contains IPR001497 Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
IPR001808 HTH transcriptional regulator, Crp
IPR001867 Signal transduction response regulator, C-terminal
IPR007624 RNA polymerase sigma-70 region 3
IPR007630 RNA polymerase sigma-70 region 4
IPR013196 Helix-turn-helix, type 11
IPR013324 RNA polymerase sigma factor, region 3/4
IPR014786 Anaphase promoting complex subunit 2
IPR015189 Translation elongation factor SelB, winged helix, type 1
IPR016157 Cullin, conserved site
IPR017919 Transcription factor TFE/TFIIEalpha, HTH domain
IPR018122 Transcription factor, fork head, conserved site
IPR018334 Transcription regulator ArsR, conserved site
IPR018335 Transcription regulator Crp-type HTH, conserved site
IPR019817 Interferon regulatory factor, conserved site
IPR019885 HTH transcriptional regulator, AsnC-type, conserved site
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif, where the "wings", or loops, are small beta-sheets. The winged helix motif consists of two wings (W1, W2), three alpha helices (H1, H2, H3) and three beta-sheets (S1, S2, S3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 [1]. The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA, while the wings make different DNA contacts, often with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.

Many different proteins with diverse biological functions contain a winged helix DNA-binding domain, including transcriptional repressors such as biotin repressor, LexA repressor and the arginine repressor [2]; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell differentiation, heat-shock transcription factor, and the general transcription factors TFIIE and TFIIF [3, 4]; helicases such as RuvB that promotes branch migration at the Holliday junction, and CDC6 in the pre-replication complex [5, 6]; endonucleases such as FokI and TnsA [7]; histones; and Mu transposase, where the flexible wing of the enhancer-binding domain is essential for efficient transposition [8].
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PDB - click here
1a04 , 1al3 , 1aoy , 1awc , 1b1b , 1b4a , 1b9m , 1b9n , 1bby , 1bc7 , 1bc8 , 1bi0 , 1bi1 , 1bi2 , 1bi3 , 1bia , 1bib , 1bja , 1bm9 , 1c0w , 1cf7 , 1cgp , 1d3y , 1d5v , 1d8j , 1d8k , 1ddn , 1dp7 , 1dpr , 1dpu , 1dux , 1e17 , 1e2x , 1eh6 , 1eh7 , 1eh8 , 1ev7 , 1f1z , 1f4k , 1f5t , 1f9n , 1fbq , 1fbs , 1fbu , 1fc3 , 1fli , 1fnn , 1fok , 1fp1 , 1fp2 , 1fpq , 1fpx , 1fse , 1fsh , 1ft9 , 1fwz , 1fx7 , 1fy7 , 1fyk , 1fyl , 1fym , 1fzp , 1g3s , 1g3t , 1g3w , 1g3y , 1g4d , 1g6n , 1ghc , 1gvj , 1gxp , 1gxq , 1h0m , 1h9g , 1h9t , 1hbx , 1hkq , 1hks , 1hkt , 1hqc , 1hst , 1hw1 , 1hw2 , 1hw5 , 1hxd , 1i1g , 1i1s , 1i27 , 1i5z , 1i6x , 1iaw , 1if1 , 1in4 , 1in5 , 1in6 , 1in7 , 1in8 , 1irf , 1irg , 1iuy , 1iw7 , 1ixc , 1ixr , 1ixs , 1iz1 , 1j0r , 1j2x , 1j59 , 1j5y , 1j75 , 1j7k , 1j9i , 1je8 , 1jgs , 1jhc , 1jhe , 1jhf , 1jhh , 1k6o , 1k78 , 1k79 , 1k7a , 1ka8 , 1kq8 , 1ku2 , 1ku3 , 1ku7 , 1ku9 , 1l0o , 1l3l , 1l9u , 1l9z , 1lb2 , 1ldd , 1ldj , 1ldk , 1lea , 1leb , 1lj9 , 1lnw , 1lq1 , 1lva , 1md0 , 1mdm , 1mgt , 1mj9 , 1mja , 1mjb , 1mkm , 1nha , 1o3q , 1o3r , 1o3s , 1o3t , 1o57 , 1o7f , 1o7l , 1odd , 1okr , 1omi , 1on1 , 1on2 , 1onv , 1opc , 1oyi , 1p2f , 1p4a , 1p4w , 1p4x , 1p6r , 1p92 , 1pdn , 1pp7 , 1pp8 , 1pue , 1q1h , 1qbj , 1qgp , 1qnt , 1qo0 , 1qpm , 1qqi , 1r1t , 1r1u , 1r1v , 1r22 , 1r23 , 1r36 , 1r7j , 1rep , 1ri7 , 1rio , 1rnl , 1rp3 , 1run , 1ruo , 1rz4 , 1s29 , 1s3j , 1s7a , 1s7o , 1s8n , 1sax , 1sc5 , 1sd4 , 1sd5 , 1sd6 , 1sd7 , 1sfe , 1sfu , 1sfx , 1smt , 1smy , 1stz , 1t0f , 1t2k , 1t38 , 1t39 , 1t6s , 1tbx , 1tlh , 1tns , 1tnt , 1tty , 1u2w , 1u6g , 1u8r , 1ub9 , 1ucr , 1ufm , 1uhm , 1uhw , 1uly , 1uss , 1ust , 1v3f , 1v4r , 1w4m , 1w5s , 1w5t , 1wsu , 1wwx , 1xcb , 1xcv , 1xma , 1xmk , 1xsd , 1xsv , 1xsx , 1yfh , 1yg2 , 1yo5 , 1yqa , 1ys6 , 1ys7 , 1yty , 1z1d , 1z91 , 1z9c , 1zg1 , 1zg3 , 1zg5 , 1zga , 1zgj , 1zh5 , 1zhf , 1zlj , 1zlk , 1zrc , 1zrd , 1zre , 1zrf , 1zyr , 2a07 , 2a61 , 2a68 , 2a69 , 2a6e , 2a6h , 2acj , 2as5 , 2bby , 2be5 , 2beo , 2bgc , 2bv6 , 2cfx , 2cg4 , 2cgp , 2cqk , 2cso , 2cw0 , 2cwe , 2cyy , 2d45 , 2dbb , 2dll , 2dpd , 2dpu , 2dqr , 2dt5 , 2dtr , 2e1c , 2e7w , 2e7x , 2efn , 2efo , 2efp , 2efq , 2efw , 2esh , 2esn , 2eth , 2ev0 , 2ev5 , 2ev6 , 2ewn , 2f5c , 2f5d , 2f5e , 2f5f , 2fbh , 2fbi , 2fbk , 2fez , 2ff4 , 2fnp , 2fok , 2frh , 2fxa , 2g9w , 2giv , 2gxb , 2gzw , 2hdc , 2heo , 2hfh , 2hr3 , 2hs5 , 2hts , 2hye , 2hyf , 2hyg , 2ia0 , 2irf , 2isy , 2isz , 2it0 , 2jpb , 2jpc , 2nnn , 2nny , 2nra , 2nyx , 2o6g , 2oqg , 2oz6 , 2ozu , 2p4w , 2p5k , 2p5l , 2p7c , 2p7v , 2pi0 , 2ply , 2pmh , 2pn6 , 2ra5 , 2rc4 , 2rnj , 2stt , 2stw , 2tdx , 2uwm , 2v9v , 2vod , 2von , 2voo , 2vop , 2yx4 , 2yx7 , 2z33 , 2z9o , 3bpy , 3bro , 3bwg , 3deu , 3hsf , 3hts , 6pax
SCOP: a.118.1.18 , a.118.8.3 , a.4.1.5 , a.4.13.1 , a.4.13.2 , a.4.13.3 , a.4.2.1 , a.4.5.1 , a.4.5.10 , a.4.5.11 , a.4.5.12 , a.4.5.13 , a.4.5.14 , a.4.5.15 , a.4.5.16 , a.4.5.17 , a.4.5.18 , a.4.5.19 , a.4.5.2 , a.4.5.20 , a.4.5.21 , a.4.5.22 , a.4.5.23 , a.4.5.24 , a.4.5.27 , a.4.5.28 , a.4.5.29 , a.4.5.3 , a.4.5.30 , a.4.5.31 , a.4.5.32 , a.4.5.33 , a.4.5.34 , a.4.5.35 , a.4.5.36 , a.4.5.37 , a.4.5.38 , a.4.5.39 , a.4.5.4 , a.4.5.40 , a.4.5.41 , a.4.5.44 , a.4.5.45 , a.4.5.46 , a.4.5.47 , a.4.5.48 , a.4.5.49 , a.4.5.5 , a.4.5.50 , a.4.5.51 , a.4.5.53 , a.4.5.58 , a.4.5.6 , a.4.5.60 , a.4.5.61 , a.4.5.64 , a.4.5.7 , a.4.5.8 , a.4.5.9 , a.4.6.1 , a.4.6.2 , a.4.6.3 , a.6.1.5 , a.6.1.7 , a.76.1.1 , b.82.3.2 , b.87.1.1 , c.23.1.1 , c.23.1.3 , c.52.1.12 , c.52.1.9 , c.94.1.1 , d.104.1.2 , d.108.1.1 , d.190.1.2 , e.12.1.1 , e.40.1.1 , i.8.1.1

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR011991 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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O01833 Histone H1.5

O02193 Males-absent on the first protein

O14641 Segment polarity protein dishevelled homolog DVL-2

O54828 Regulator of G-protein signaling 9

P53551 Histone H1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR016137 Regulator of G protein signalling superfamily
IPR000953 Chromo domain
IPR000591 DEP domain
IPR011991 Winged helix repressor DNA-binding
IPR001158 DIX
IPR008339 Dishevelled region
IPR016181 Acyl-CoA N-acyltransferase
IPR015506 Dishevelled related protein
IPR008341 Dishevelled-2 region
IPR015898 G-protein, gamma-like subunit
IPR001478 PDZ/DHR/GLGF
IPR005818 Histone H1/H5
IPR000342 Regulator of G protein signalling
IPR005819 Histone H5
IPR003351 Dishevelled protein
IPR002717 MOZ/SAS-like protein
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
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1. Gajiwala KS, Burley SK.
Winged helix proteins.
Curr. Opin. Struct. Biol. 10 110-6 2000 [PubMed: 10679470]
http://dx.doi.org/10.1016/S0959-440X(99)00057-3
2. Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW.
Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
Proc. Natl. Acad. Sci. U.S.A. 89 9257-61 1992 [PubMed: 1409631]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1409631&action=stream&blobtype=pdf
3. Lai E, Clark KL, Burley SK, Darnell JE Jr.
Hepatocyte nuclear factor 3/fork head or "winged helix" proteins: a family of transcription factors of diverse biologic function.
Proc. Natl. Acad. Sci. U.S.A. 90 10421-3 1993 [PubMed: 8248124]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8248124
4. Cicero MP, Hubl ST, Harrison CJ, Littlefield O, Hardy JA, Nelson HC.
The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity.
Nucleic Acids Res. 29 1715-23 2001 [PubMed: 11292844]
http://dx.doi.org/10.1093/nar/29.8.1715
5. Yamada K, Miyata T, Tsuchiya D, Oyama T, Fujiwara Y, Ohnishi T, Iwasaki H, Shinagawa H, Ariyoshi M, Mayanagi K, Morikawa K.
Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.
Mol. Cell 10 671-81 2002 [PubMed: 12408833]
http://dx.doi.org/10.1016/S1097-2765(02)00641-X
6. Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM.
Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.
Mol. Cell 6 637-48 2000 [PubMed: 11030343]
http://dx.doi.org/10.1016/S1097-2765(00)00062-9
7. Wah DA, Hirsch JA, Dorner LF, Schildkraut I, Aggarwal AK.
Structure of the multimodular endonuclease FokI bound to DNA.
Nature 388 97-100 1997 [PubMed: 9214510]
http://dx.doi.org/10.1038/40446
8. Clubb RT, Mizuuchi M, Huth JR, Omichinski JG, Savilahti H, Mizuuchi K, Clore GM, Gronenborn AM.
The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition.
Proc. Natl. Acad. Sci. U.S.A. 93 1146-50 1996 [PubMed: 8577730]
http://dx.doi.org/10.1073/pnas.93.3.1146

Additional ReadingHelp
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Sala C, Haouz A, Saul FA, Miras I, Rosenkrands I, Alzari PM, Cole ST.
Genome-wide regulon and crystal structure of BlaI (Rv1846c) from Mycobacterium tuberculosis.
Mol. Microbiol. 71 2009 1102-16 [PubMed: 19154333]
http://dx.doi.org/10.1111/j.1365-2958.2008.06583.x
Lamber EP, Vanhille L, Textor LC, Kachalova GS, Sieweke MH, Wilmanns M.
Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization.
EMBO J. 27 2008 2006-17 [PubMed: 18566588]
http://dx.doi.org/10.1038/emboj.2008.117
Garnett JA, Marincs F, Baumberg S, Stockley PG, Phillips SE.
Structure and function of the arginine repressor-operator complex from Bacillus subtilis.
J. Mol. Biol. 379 2008 284-98 [PubMed: 18455186]
http://dx.doi.org/10.1016/j.jmb.2008.03.007
Donaldson LW.
The NMR structure of the Staphylococcus aureus response regulator VraR DNA binding domain reveals a dynamic relationship between it and its associated receiver domain.
Biochemistry 47 2008 3379-88 [PubMed: 18293926]
http://dx.doi.org/10.1021/bi701844q
Itou H, Yao M, Watanabe N, Tanaka I.
Crystal structure of the PH1932 protein, a unique archaeal ArsR type winged-HTH transcription factor from Pyrococcus horikoshii OT3.
Proteins 70 2008 1631-4 [PubMed: 18076033]
http://dx.doi.org/10.1002/prot.21851
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InterPro 23.1