Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEqtTQISQWEVW 83
Cdd:cd00592     1 YTIGEVAKLLGVSVRTLRYYEEKGLLPPERSENGYRLYSEEDLERLRLIRRLRELGLSLKEIRELLDAR--DEELSLAAL 78

                          90       100
                  ....*....|....*....|...
gi 1355085000  84 QEQLLATLEKtsLEKGRALLLKM 106
Cdd:cd00592    79 LALLDEKLAE--LEEKIARLEAL 99

DNA-binding transcriptional regulator, MerR family [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   6 IEMLSDQCGVSMPNLRAWQRSGLLQPV-RDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEQTTQisqwEVWQ 84
Cdd:COG0789     1 IGEVARLTGVSVRTLRYYERIGLLPPPeRTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDDGE----EEVR 76

                          90       100
                  ....*....|....*....|....*.
gi 1355085000  85 EQLLATLEKtsLEKGRALLLKMGREL 110
Cdd:COG0789    77 ELLEEHLAE--LEAQIAELQALRAEL 100

Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEqtTQISQWEVW 83
Cdd:cd00592     1 YTIGEVAKLLGVSVRTLRYYEEKGLLPPERSENGYRLYSEEDLERLRLIRRLRELGLSLKEIRELLDAR--DEELSLAAL 78

                          90       100
                  ....*....|....*....|...
gi 1355085000  84 QEQLLATLEKtsLEKGRALLLKM 106
Cdd:cd00592    79 LALLDEKLAE--LEEKIARLEAL 99

DNA-binding transcriptional regulator, MerR family [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   6 IEMLSDQCGVSMPNLRAWQRSGLLQPV-RDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEQTTQisqwEVWQ 84
Cdd:COG0789     1 IGEVARLTGVSVRTLRYYERIGLLPPPeRTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDDGE----EEVR 76

                          90       100
                  ....*....|....*....|....*.
gi 1355085000  85 EQLLATLEKtsLEKGRALLLKMGREL 110
Cdd:COG0789    77 ELLEEHLAE--LEAQIAELQALRAEL 100

Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVRDDSGRRYFDYSHLMRIHAI 52
Cdd:cd04761     1 YTIGELAKLTGVSPSTLRYYERIGLLSPARTEGGYRLYSDADLERLRLI 49

Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix (HTH) transcription regulator GlnR and related proteins, N-terminal domain. The GlnR and TnrA (also known as ScgR) proteins have been shown to regulate expression of glutamine synthetase as well as several genes involved in nitrogen metabolism. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVR-DDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEQT 74
Cdd:cd01105     2 IGIGEVSKLTGVSPRQLRYWEEKGLIKSIRsDGGGQRKYSLADVDRLLVIKELLDEGFTLAAAVEKLRRRRV 73

Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A) and related proteins, N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRS-GLLQPVRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILK 70
Cdd:cd04763     1 YTIGEVALLTGIKPHVLRAWEREfGLLKPQRSDGGHRLFNDADIDRILEIKRWIDNGVQVSKVKKLLS 68

Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA; Helix-turn-helix (HTH) TipAL, Mta, and SkgA transcription regulators, and related proteins, N-terminal domain. TipAL regulates resistance to and activation by numerous cyclic thiopeptide antibiotics, such as thiostrepton. Mta is a global transcriptional regulator; the N-terminal DNA-binding domain of Mta interacts directly with the promoters of mta, bmr, blt, and ydfK, and induces transcription of these multidrug-efflux transport genes. SkgA has been shown to control stationary-phase expression of catalase-peroxidase in Caulobacter crescentus. These proteins are comprised of distinct domains that harbor an N-terminal active (DNA-binding) site and a regulatory (effector-binding) site. The conserved N-terminal domain of these transcription regulators contains winged HTH motifs that mediate DNA binding. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Unique to this family, is a TipAL-like, lineage specific Bacilli subgroup, which has five conserved cysteines in the C-terminus of the protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVR-DDSGRRYFDYSHLMRIHAIL--KWLdrGLPLNEIARILKGEQTTQI--- 77
Cdd:cd01106     1 YTVGEVAKLTGVSVRTLHYYDEIGLLKPSRrTENGYRLYTEEDLERLQQILflKEL--GFSLKEIKELLKDPSEDLLeal 78

                          90       100
                  ....*....|....*....|....
gi 1355085000  78 -SQWEVWQEQ------LLATLEKT 94
Cdd:cd01106    79 rEQKELLEEKkerldkLIKTIDRT 102

Helix-Turn-Helix DNA binding domain of putative Cfa-like transcription regulators; Putative helix-turn-helix (HTH) MerR-like transcription regulator; conserved, Cfa-like, unknown proteins (~172 a.a.). The N-terminal domain of these proteins appears to be related to the HTH domain of Cfa, a cyclopropane fatty acid synthase. These Cfa-like proteins have a unique C-terminal domain with conserved histidines (motif HXXFX7HXXF). Based on sequence similarity of the N-terminal domains, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQP-VRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILkgeQTTQISQWEV 82
Cdd:cd04790     2 LTISQLARQFGLSRSTLLYYERIGLLSPsARSESNYRLYGERDLERLEQICAYRSAGVSLEDIRSLL---QQPGDDATDV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1355085000  83 WQEQLLA-TLEKTSL-EKGRAL--LLKMGRELPAGMLLDK 118
Cdd:cd04790    79 LRRRLAElNREIQRLrQQQRAIatLLKQPTLLKEQRLVTK 118

Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators; Helix-turn-helix (HTH) BmrR-like transcription regulators (TipAL, Mta, SkgA, BmrR, and BltR), N-terminal domain. These proteins have been shown to regulate expression of specific regulons in response to various toxic substances, antibiotics, or oxygen radicals in Bacillus subtilis, Streptomyces, and Caulobacter crescentus. They are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVR-DDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGE 72
Cdd:cd04768     1 LTIGEFAKLAGVSIRTLRHYDDIGLFKPAKiAENGYRYYSYAQLYQLQFILFLRELGFSLAEIKELLDTE 70

MerR family regulatory protein;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1355085000   5 TIEMLSDQCGVSMPNLRAWQRSGLLQ-PVRDDSGRRYF 41
Cdd:pfam00376   1 TIGEVAKLLGVSPRTLRYYEKIGLLPpPERTEGGYRRY 38

Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family mostly have a truncated helix-turn-helix (HTH) MerR-like domain. They lack a portion of the C-terminal region, called Wing 2 and the long dimerization helix that is typically present in MerR-like proteins. These truncated domains are found in response regulator receiver (REC) domain proteins (i.e., CheY), cytosine-C5 specific DNA methylases, IS607 transposase-like proteins, and RacA, a bacterial protein that anchors chromosomes to cell poles.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVRDDSGRRYFDYSHLMRI 49
Cdd:cd04762     1 LTTKEAAELLGVSPSTLRRWVKEGKLKAIRTPGGHRRFPEEDLERL 46

Helix-Turn-Helix DNA binding domain of the CadR- and PbrR-like transcription regulators; Helix-turn-helix (HTH) CadR- and PbrR-like transcription regulators. CadR and PbrR regulate expression of the cadmium and lead resistance operons, respectively. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines which comprise a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLL-QPVRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEI 65
Cdd:cd04785     1 LSIGELARRTGVNVETIRYYESIGLLpEPARTAGGYRLYGAAHVERLRFIRRARDLGFSLEEI 63

Helix-Turn-Helix DNA binding domain of the MerR1 transcription regulator; Helix-turn-helix (HTH) transcription regulator MerR1. MerR1 transcription regulators, such as Tn21 MerR and Tn501 MerR, mediate response to mercury exposure in eubacteria. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines that define a mercury binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLL-QPVRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARIL 69
Cdd:cd04783     1 LTIGELAKAAGVNVETIRYYQRRGLLpEPPRPEGGYRRYPEETVTRLRFIKRAQELGFTLDEIAELL 67

Helix-Turn-Helix DNA binding domain of the transcription regulators NolA and AlbR; Helix-turn-helix (HTH) transcription regulators NolA and AlbR, N-terminal domain. In Bradyrhizobium (Arachis) sp. NC92, NolA is required for efficient nodulation of host plants. In Xanthomonas albilineans, AlbR regulates the expression of the pathotoxin, albicidin. These proteins are putatively comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. They share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1355085000   9 LSDQCGVSMPNLRAWQRSGLLQPV-RDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGE 72
Cdd:cd04788     6 LARRTGLSVRTLHHYDHIGLLSPSqRTEGGHRLYDRADIRRLHQIIALRRLGFSLREIGRALDGP 70

Helix-Turn-Helix DNA binding domain of the BltR transcription regulator; Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BltR (BmrR-like transporter) of Bacillus subtilis, and related proteins; N-terminal domain. Blt, like Bmr, is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. These regulators are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. They share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQP-VRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEI 65
Cdd:cd04782     1 FTTGEFAKLCGISKQTLFHYDKIGLFKPeIVKENGYRYYTLEQFEQLDIILLLKELGISLKEI 63

Helix-Turn-Helix DNA binding domain of the MerD transcription regulator; Helix-turn-helix (HTH) transcription regulator MerD. The putative secondary regulator of mercury resistance (mer) operons, MerD, has been shown to down-regulate the expression of this operon in gram-negative bacteria. It binds to the same operator DNA as MerR that activates transcription of the operon in the presence of mercury ions. The MerD protein shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily, which promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are conserved and contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPV-RDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEQTTQISQWEV 82
Cdd:cd01111     1 YSISQLALDAGVSVHIVRDYLLRGLLHPVaRTEGGYGLFDDCALQRLRFVRAAFEAGIGLDELARLCRALDAGDGKQPEA 80

                          90
                  ....*....|
gi 1355085000  83 WQEQLLATLE 92
Cdd:cd01111    81 CLAQLRQKIE 90

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 4). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1355085000   6 IEMLSDQCGVSMPNLRAWQRSGLLQPVRDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILKGEQTTQISQWEVWQE 85
Cdd:cd04779     3 IGQLAHLAGVSKRTIDYYTNLGLLTPERSDSNYRYYDETALDRLQLIEHLKGQRLSLAEIKDQLEEVQRSDKEQREVAQE 82

Helix-Turn-Helix DNA binding domain of putative HspR-like transcription regulators; Putative helix-turn-helix (HTH) transcription regulator HspR-like proteins. Unlike the characterized HspR, these proteins have a C-terminal domain with putative metal binding cysteines (MBC). Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1355085000   4 FTIEMLSDQCGVSMPNLRAWQRSGLLQPVRDDsGRRYFDYSHLMRIHAILKWL-DRGLPLNEIARIL 69
Cdd:cd04767     2 YPIGVVAELLNIHPETLRIWERHGLIKPARRN-GQRLYSNNDLKRLRFIKKLInEKGLNIAGVKQIL 67

HTH-type transcriptional regulator MerD;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1355085000   1 MSHFTIEMLSDQCGVSMPNLRAWQRSGLLQPV-RDDSGRRYFDYSHLMRIHAILKWLDRGLPLNEIARILK 70
Cdd:PRK13749    1 MSAYTVSRLALDAGVSVHIVRDYLLRGLLRPVaCTTGGYGLFDDAALQRLCFVRAAFEAGIGLDALARLCR 71

Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD mainly contains the C-terminal or second repeat (rpt2) of these tandem MerR-like domain proteins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1355085000   5 TIEMLSDQCGVSMPNLRAWQRSGLLQPVRDDS-GRRYFDYSHLMRIHAILKWLDRGLPLNEIARIL 69
Cdd:cd04773     2 TIGELAHLLGVPPSTLRHWEKEGLLSPDREPEtGYRVYDPSDVRDARLIHLLRRGGYLLEQIATVV 67