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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  12 VLPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNH-RTYSLNDVDELLEIRSQMADGFTLADVKRLKHPRHRedsDAEV 90
Cdd:cd01105    1 VIGIGEVSKLTGVSPRQLRYWEEKGLIKSIRSDGGGqRKYSLADVDRLLVIKELLDEGFTLAAAVEKLRRRRV---QAEV 77

                         90
                 ....*....|.
gi 491944177  91 RKVLRDELLNQ 101
Cdd:cd01105   78 RRRLMKDGLQG 88

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  12 VLPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNH-RTYSLNDVDELLEIRSQMADGFTLADVKRLKHPRHRedsDAEV 90
Cdd:cd01105    1 VIGIGEVSKLTGVSPRQLRYWEEKGLIKSIRSDGGGqRKYSLADVDRLLVIKELLDEGFTLAAAVEKLRRRRV---QAEV 77

                         90
                 ....*....|.
gi 491944177  91 RKVLRDELLNQ 101
Cdd:cd01105   78 RRRLMKDGLQG 88

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKP-QRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRLKhpRHREDSDAEVRKV 93
Cdd:COG0789    1 IGEVARLTGVSVRTLRYYERIGLLPPpERTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELL--DLLDDGEEEVREL 78

                 ....*
gi 491944177  94 LRDEL 98
Cdd:COG0789   79 LEEHL 83

HTH-type transcriptional regulator MlrA;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491944177  15 IGTVMLLTDLTARQIRYYETQ-GLVKPQRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRL 77
Cdd:PRK15043   6 IGEVALLCDINPVTLRAWQRRyGLLKPQRTDGGHRLFNDADIDRIREIKRWIDNGVQVSKVKML 69

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  12 VLPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNH-RTYSLNDVDELLEIRSQMADGFTLADVKRLKHPRHRedsDAEV 90
Cdd:cd01105    1 VIGIGEVSKLTGVSPRQLRYWEEKGLIKSIRSDGGGqRKYSLADVDRLLVIKELLDEGFTLAAAVEKLRRRRV---QAEV 77

                         90
                 ....*....|.
gi 491944177  91 RKVLRDELLNQ 101
Cdd:cd01105   78 RRRLMKDGLQG 88

helix_turn_helix, mercury resistance;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491944177    13 LPIGTVMLLTDLTARQIRYYETQGLVKPQ-RNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRL 77
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPPPiRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKEL 66

MerR HTH family regulatory protein;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491944177   15 IGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRL 77
Cdd:pfam13411   3 ISELARLLGVTPRTLRYWEREGLLPPPRTERGRRYYTDEDVERLRLIKALLERGLSLKEIKEL 65

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 491944177  13 LPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEI 61
Cdd:cd04761    1 YTIGELAKLTGVSPSTLRYYERIGLLSPARTEGGYRLYSDADLERLRLI 49

Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins 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 winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKP-QRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKR---LKHPRHREDSD 87
Cdd:cd01108    3 IGEAAKLTGLSAKMIRYYEEIGLIPPpSRSDNGYRVYNQRDIEELRFIRRARDLGFSLEEIREllaLWRDPSRASAD 79

Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; Helix-turn-helix (HTH) CadR and PbrR transcription regulators including Pseudomonas aeruginosa CadR and Ralstonia metallidurans PbrR that 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 form 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLV-KPQRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRLKHPR-HREDSDAEVRK 92
Cdd:cd04784    3 IGELAKKTGCSVETIRYYEKEGLLpAPARSANNYRLYDEEHLERLLFIRRCRSLDMSLDEIRTLLQLQdDPEASCAEVNA 82

                 ..
gi 491944177  93 VL 94
Cdd:cd04784   83 LI 84

Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) transcription regulator HspR, N-terminal domain. 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEIRSQMAD-GFTLADVKRLKHPRHREDSDAEVRKV 93
Cdd:cd04766    4 ISVAAELSGMHPQTLRLYERLGLLSPSRTDGGTRRYSERDIERLRRIQRLTQElGVNLAGVKRILELEEELAELRAELDE 83

                 ....*
gi 491944177  94 LRDEL 98
Cdd:cd04766   84 LRARL 88

Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) transcription regulator, YfmP, and related proteins; N-terminal domain. YfmP regulates the multidrug efflux protein, YfmO, and indirectly regulates the expression of the Bacillus subtilis copZA operon encoding a metallochaperone, CopZ, and a CPx-type ATPase efflux protein, CopA. 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 winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  13 LPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEIRSQMAD-GFTLADVkrlKHPRHREDSDAEVR 91
Cdd:cd04774    1 YKVDEVAKRLGLTKRTLKYYEEIGLVSPERSEGRYRLYSEEDLKRLERILRLREVlGFSLQEV---THFLERPLEPVDGG 77

                         90
                 ....*....|
gi 491944177  92 KVLRDELLNQ 101
Cdd:cd04774   78 HRYSAESLRE 87

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 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKP-QRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRL 77
Cdd:cd04788    3 IGELARRTGLSVRTLHHYDHIGLLSPsQRTEGGHRLYDRADIRRLHQIIALRRLGFSLREIGRA 66

Zn(2+)-responsive transcriptional regulator;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKPQ-RNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRL 77
Cdd:PRK09514   4 IGELAKLAEVTPDTLRFYEKQGLMDPEvRTEGGYRLYTEQDLQRLRFIRRAKQLGFTLEEIREL 67

MerR family regulatory protein;

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 491944177   15 IGTVMLLTDLTARQIRYYETQGLVK-PQRNAGNHRTY 50
Cdd:pfam00376   2 IGEVAKLLGVSPRTLRYYEKIGLLPpPERTEGGYRRY 38

Helix-Turn-Helix DNA binding domain of putative Heavy Metal Resistance transcription regulators; Putative helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR), unknown subgroup. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to heavy metal 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. This subgroup lacks one of the conserved, metal-binding cysteines seen in the MerR1 group.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  23 DLTARQIRYYETQGLVKPQRNAGN-HRTYSLNDVDELLEIRSQMADGFTLADVKR-LKHPRHREDSDAEVRKVLRDELLN 100
Cdd:cd04787   11 GVTPDTVRFYTRIGLLRPTRDPVNgYRLYSEKDLSRLRFILSARQLGFSLKDIKEiLSHADQGESPCPMVRRLIEQRLAE 90

                 ...
gi 491944177 101 QSR 103
Cdd:cd04787   91 TER 93

Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), 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. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  15 IGTVMLLTDLTARQIRYYETQ-GLVKPQRNAGNHRTYSLNDVDELLEIRSQMAD-GFTLADVKRL----KHPRHREDSDA 88
Cdd:cd04765    3 IGEVAEILGLPPHVLRYWETEfPQLKPVKRAGGRRYYRPKDVELLLLIKHLLYEkGYTIEGAKQAlkedGAAAIREEEAE 82

                         90
                 ....*....|..
gi 491944177  89 EVRKVLRDELLN 100
Cdd:cd04765   83 ERLPSIRAELLD 94

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 7) with a conserved cysteine present in the C-terminal portion of the protein. 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 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKP-QRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRLKHP-----RHREDSDA 88
Cdd:cd04786    3 IGELAKRSGMAASRIRFYEAEGLLSSvERSANGYRDYPPETVWVLEIISSAQQAGFSLDEIRQLLPAdasnwQHDELLAA 82

                         90
                 ....*....|....*....
gi 491944177  89 EVRKVLRDELLnQSRLNQS 107
Cdd:cd04786   83 LERKVADIEAL-EARLAQN 100

Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MerR2 and related proteins. MerR2 in Bacillus cereus RC607 regulates resistance to organomercurials. 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 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRL 77
Cdd:cd04769    3 IGELAQQTGVTIKAIRLYEEKGLLPSPKRSGNYRVYDAQHVECLRFIKEARQLGFTLAELKAI 65

Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator; Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  13 LPIGTVMLLTDLTARQIRYYETQGLVKPQR--NAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRLKHprhrEDSDAEV 90
Cdd:cd01107    1 FTIGEFAKLSNLSIKALRYYDKIGLLKPAYvdPDTGYRYYSAEQLERLNRIKYLRDLGFPLEEIKEILD----ADNDDEL 76

                 ....*
gi 491944177  91 RKVLR 95
Cdd:cd01107   77 RKLLR 81

Helix-Turn-Helix DNA binding domain of the Cfa transcription regulator; Putative helix-turn-helix (HTH) MerR-like transcription regulator; the N-terminal domain of Cfa, a cyclopropane fatty acid synthase and other related methyltransferases. 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 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 491944177  23 DLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEIRSQMADGFTL 71
Cdd:cd04789   12 GISRSTLLYYEKLGLITGTRNANGYRLYPDSDLQRLLLIQQLQAGGLSL 60

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 6) with at least two conserved cysteines present in the C-terminal portion of the protein. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491944177  13 LPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTYSLNDVDELLEIRSQMADGFTLADVKRLKHP 80
Cdd:cd04781    1 LDIAEVARQSGLPASTLRYYEEKGLIASIGRRGLRRQYDPQVLDRLALIALGRAAGFSLDEIQAMLSH 68

redox-sensitive transcriptional activator SoxR;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491944177   8 RTRSVLPIGTVMLLTDLTARQIRYYETQGLVKPQRNAGNHRTY 50
Cdd:PRK15002   7 RIKALLTPGEVAKRSGVAVSALHFYESKGLITSIRNSGNQRRY 49

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491944177  15 IGTVMLLTDLTARQIRYYETQGLVKPQRNAGN-HRTYSLNDVDELLEIRSQMADGFTLADVKRLKHPRHREDSDAEVRKV 93
Cdd:cd04773    3 IGELAHLLGVPPSTLRHWEKEGLLSPDREPETgYRVYDPSDVRDARLIHLLRRGGYLLEQIATVVEQLRHAGGTEALAAA 82

                 ...
gi 491944177  94 LRD 96
Cdd:cd04773   83 LEQ 85