mercuric resistence transcriptional repressor protein MerD; This model represents a transcriptional repressor protein of the MerR family (pfam00376) whose expression is regulated by the mercury-sensitive transcriptional activator, MerR. MerD has been shown to repress the transcription of the mer operon. [Cellular processes, Detoxification]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025   1 MSAYTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRALDAADGDG 80
Cdd:TIGR02054   1 MNAYTISRLAEDAGVSVHVVRDYLLRGLLHPVRRTTSGYGIFDDASLQRLRFVRAAFEAGIGLGELARLCRALDAANGDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1393952025  81 ASAQLAVLRQLVERRREALASLEMQLAAMPTEPAQHAESL 120
Cdd:TIGR02054  81 TAACLAVLRQLVEARREALAALEVQLAAMPTAAAQHSESA 120

helix_turn_helix, mercury resistance;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025    4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRAL 73
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPPPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELLELL 70

MerR HTH family regulatory protein;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPvAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLC 70
Cdd:pfam13411   1 YTISELARLLGVTPRTLRYWEREGLLPP-PRTERGRRYYTDEDVERLRLIKALLERGLSLKEIKELL 66

mercuric resistence transcriptional repressor protein MerD; This model represents a transcriptional repressor protein of the MerR family (pfam00376) whose expression is regulated by the mercury-sensitive transcriptional activator, MerR. MerD has been shown to repress the transcription of the mer operon. [Cellular processes, Detoxification]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025   1 MSAYTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRALDAADGDG 80
Cdd:TIGR02054   1 MNAYTISRLAEDAGVSVHVVRDYLLRGLLHPVRRTTSGYGIFDDASLQRLRFVRAAFEAGIGLGELARLCRALDAANGDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1393952025  81 ASAQLAVLRQLVERRREALASLEMQLAAMPTEPAQHAESL 120
Cdd:TIGR02054  81 TAACLAVLRQLVEARREALAALEVQLAAMPTAAAQHSESA 120

helix_turn_helix, mercury resistance;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025    4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRAL 73
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPPPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELLELL 70

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRALDAADGDGASA 83
Cdd:cd04783     1 LTIGELAKAAGVNVETIRYYQRRGLLPEPPRPEGGYRRYPEETVTRLRFIKRAQELGFTLDEIAELLELDDGTDCSEARE 80

                          90       100
                  ....*....|....*....|....*....
gi 1393952025  84 QLAVLRQLVERRREALASLEMQLAAMPTE 112
Cdd:cd04783    81 LAEQKLAEVDEKIADLQRMRASLQELVSQ 109

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        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPvAYTTGGYGLFDDTALQRLRFV 53
Cdd:cd04761     1 YTIGELAKLTGVSPSTLRYYERIGLLSP-ARTEGGYRLYSDADLERLRLI 49

Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; Helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR): MerR1 (mercury), CueR (copper), CadR (cadmium), PbrR (lead), ZntR (zinc), and other related proteins. These transcription regulators 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLcraLDAADGDGASA 83
Cdd:cd04770     1 MKIGELAKAAGVSPDTIRYYERIGLLPPPQRSENGYRLYGEADLARLRFIRRAQALGFSLAEIREL---LSLRDDGAAPC 77

                          90       100
                  ....*....|....*....|....*....
gi 1393952025  84 QLAVLR-----QLVERRREALASLEMQLA 107
Cdd:cd04770    78 AEVRALleeklAEVEAKIAELQALRAELA 106

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 1393952025   5 TVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRalDAADGDGASAQ 84
Cdd:cd04787     2 KVKELANAAGVTPDTVRFYTRIGLLRPTRDPVNGYRLYSEKDLSRLRFILSARQLGFSLKDIKEILS--HADQGESPCPM 79

                          90       100
                  ....*....|....*....|....*
gi 1393952025  85 lavLRQLVERRreaLASLEMQLAAM 109
Cdd:cd04787    80 ---VRRLIEQR---LAETERRIKEL 98

Zn(2+)-responsive transcriptional regulator;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARL 69
Cdd:PRK09514    2 YRIGELAKLAEVTPDTLRFYEKQGLMDPEVRTEGGYRLYTEQDLQRLRFIRRAKQLGFTLEEIREL 67

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 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALarlcRALDAADGDGASA 83
Cdd:cd04790     2 LTISQLARQFGLSRSTLLYYERIGLLSPSARSESNYRLYGERDLERLEQICAYRSAGVSLEDI----RSLLQQPGDDATD 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1393952025  84 QLAVLRQLVERRREALASLEMQLAAMPTEP 113
Cdd:cd04790    78 VLRRRLAELNREIQRLRQQQRAIATLLKQP 107

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 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLcraLDAADGDGASA 83
Cdd:cd01106     1 YTVGEVAKLTGVSVRTLHYYDEIGLLKPSRRTENGYRLYTEEDLERLQQILFLKELGFSLKEIKEL---LKDPSEDLLEA 77

                          90
                  ....*....|....*.
gi 1393952025  84 qLAVLRQLVERRREAL 99
Cdd:cd01106    78 -LREQKELLEEKKERL 92

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025  14 GVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDAlarlCRALDA--ADGDGASAQlavLRQL 91
Cdd:cd01108    11 GLSAKMIRYYEEIGLIPPPSRSDNGYRVYNQRDIEELRFIRRARDLGFSLEE----IRELLAlwRDPSRASAD---VKAL 83

                          90
                  ....*....|....*...
gi 1393952025  92 VERRreaLASLEMQLAAM 109
Cdd:cd01108    84 ALEH---IAELERKIAEL 98

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025   6 VSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIgldALARLCRALDAADGDgasaQL 85
Cdd:cd04788     3 IGELARRTGLSVRTLHHYDHIGLLSPSQRTEGGHRLYDRADIRRLHQIIALRRLGF---SLREIGRALDGPDFD----PL 75

                          90
                  ....*....|....*
gi 1393952025  86 AVLRQLVERRREALA 100
Cdd:cd04788    76 ELLRRQLARLEEQLE 90

HTH-type transcriptional regulator CueR;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393952025   6 VSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFVRAAFEAGIGLDALARLCRALDAADGDGASAQL 85
Cdd:PRK10227    3 ISDVAKITGLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLFNDPQRHSADVKR 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1393952025  86 AVLRQL--VERRREALASLEMQLAAMptepaqhAESLP 121
Cdd:PRK10227   83 RTLEKVaeIERHIEELQSMRDQLLAL-------ANACP 113

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
                  ....*....|....*....|....*....|....*....|....*....|
gi 1393952025   4 YTVSRLALDAGVSVHIVRDYLLRGLLRPVAYTTGGYGLFDDTALQRLRFV 53
Cdd:cd04768     1 LTIGEFAKLAGVSIRTLRHYDDIGLFKPAKIAENGYRYYSYAQLYQLQFI 50