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Conserved domains on  [gi|499176343|ref|WP_010873930|]
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MULTISPECIES: precorrin-8X methylmutase [unclassified Synechocystis]

Protein Classification

helix-turn-helix domain-containing protein; MerR family transcriptional regulator( domain architecture ID 11269464)

helix-turn-helix (HTH) domain-containing protein with a MerR family HTH domain may bind DNA and function as a transcriptional regulator; MerR family transcriptional regulator containing a MerR family helix-turn-helix (HTH) DNA-binding domain and a class I SAM-dependent methyltransferase as its effector domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CobH COG2082
Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]; Precorrin-8X ...
 157-355 1.82e-81

Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]; Precorrin-8X methylmutase CbiC/CobH is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 441685  Cd Length: 203  Bit Score: 247.26  E-value: 1.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 157 TTTHPEAFQESLKHLLP--DLSAYSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALD 234
Cdd:COG2082    3 IRDPAEIERESFAIIRAelDLSRFSEDEEPVVVRLIHATGDFDLADLLRFSPGAVEAGRAALRAGAPIVTDVEMVAAGIN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 235 QTRLAHLGCTVKTLIDDPHITGLREAEQAFWHHDHWQQRLQQIPqGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPI 314
Cdd:COG2082   83 KRRLPALGNEVICLISDPRVAELAKAEGITRSAAAMRLAAERLE-GAIVAIGNAPTALFELLELIEEGAPRPALIIGVPV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499176343 315 GFSHAPGAKRRLMTSPIPHITIQGSLGGGLLAAVTLNALVE 355
Cdd:COG2082  162 GFVGAAESKEALMASGVPYITVRGRKGGSAIAAAAVNALLY 202
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
6-75 6.73e-24

helix_turn_helix, mercury resistance;


:

Pssm-ID: 197716  Cd Length: 70  Bit Score: 93.35  E-value: 6.73e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343     6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:smart00422   1 YTIGEVAKLAG--VSVRTLRYYERIGLLPPPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELLE 68
 
Name Accession Description Interval E-value
CobH COG2082
Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]; Precorrin-8X ...
 157-355 1.82e-81

Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]; Precorrin-8X methylmutase CbiC/CobH is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441685  Cd Length: 203  Bit Score: 247.26  E-value: 1.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 157 TTTHPEAFQESLKHLLP--DLSAYSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALD 234
Cdd:COG2082    3 IRDPAEIERESFAIIRAelDLSRFSEDEEPVVVRLIHATGDFDLADLLRFSPGAVEAGRAALRAGAPIVTDVEMVAAGIN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 235 QTRLAHLGCTVKTLIDDPHITGLREAEQAFWHHDHWQQRLQQIPqGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPI 314
Cdd:COG2082   83 KRRLPALGNEVICLISDPRVAELAKAEGITRSAAAMRLAAERLE-GAIVAIGNAPTALFELLELIEEGAPRPALIIGVPV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499176343 315 GFSHAPGAKRRLMTSPIPHITIQGSLGGGLLAAVTLNALVE 355
Cdd:COG2082  162 GFVGAAESKEALMASGVPYITVRGRKGGSAIAAAAVNALLY 202
CbiC pfam02570
Precorrin-8X methylmutase; This is a family Precorrin-8X methylmutases also known as Precorrin ...
 174-355 7.31e-66

Precorrin-8X methylmutase; This is a family Precorrin-8X methylmutases also known as Precorrin isomerase, CbiC/CobH, EC:5.4.1.2. This enzyme catalyzes the reaction: Precorrin-8X <=> hydrogenobyrinate. This enzyme is part of the Cobalamin (vitamin B12) biosynthetic pathway and catalyzes a methyl rearrangement.


Pssm-ID: 426840  Cd Length: 195  Bit Score: 206.85  E-value: 7.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  174 DLSAYSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRLAHLGCTVKTLIDDPH 253
Cdd:pfam02570  14 GLHRFSPAEYEIVRRVIHATGDFEYADLLRFSPGAVEAGRAALKAGAPIVTDVNMVAAGINKRRLATFGNPVYCFLDDPE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  254 ITGLREaEQAFWHHDHWQQRLQQIPQGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGAKRRLMTSPIPH 333
Cdd:pfam02570  94 VAELAK-ERGITRSAAAMELAAERLPGAIVVIGNAPTALFELLELIEEGKIRPALVIGVPVGFVGAAESKEALAASGVPY 172

                         170       180
                  ....*....|....*....|..
gi 499176343  334 ITIQGSLGGGLLAAVTLNALVE 355
Cdd:pfam02570 173 ITVRGRKGGSAVAAAIVNALLY 194
cobH PRK08285
precorrin-8X methylmutase; Reviewed
 174-353 2.74e-25

precorrin-8X methylmutase; Reviewed


Pssm-ID: 181352  Cd Length: 208  Bit Score: 101.50  E-value: 2.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 174 DLSAYSE----ITIHLLHqlvlACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRLAHlGCTVKTLI 249
Cdd:PRK08285  24 DLSRFPAdlekVAVRMIH----ACGMVDVADDLAFSPGAVAAARAALAAGAPILCDARMVAEGITRARLPA-DNEVICTL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 250 DDPHITGL-------REAEQAfwhhDHWQQRLQqipqGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGA 322
Cdd:PRK08285  99 RDPRVPELaaelgntRSAAAL----ELWRPRLA----GSVVAIGNAPTALFRLLEMLDAGAPRPAAILGFPVGFVGAAES 170

                        170       180       190
                 ....*....|....*....|....*....|...
gi 499176343 323 KRRLMTSP--IPHITIQGSLGGGLLAAVTLNAL 353
Cdd:PRK08285 171 KDALAADSrgVPYLIVRGRRGGSAMAAAAVNAL 203
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
6-75 6.73e-24

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 93.35  E-value: 6.73e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343     6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:smart00422   1 YTIGEVAKLAG--VSVRTLRYYERIGLLPPPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELLE 68
HTH_MerR-like cd00592
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ...
 6-108 1.07e-23

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.


Pssm-ID: 133378 [Multi-domain]  Cd Length: 100  Bit Score: 93.85  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESLDPT 85
Cdd:cd00592    1 YTIGEVAKLLG--VSVRTLRYYEEKGLLPP-ERSENGYRLYSEEDLERLRLIRRLRELGLSLKEIRELLDARDEELSLAA 77

                         90       100
                 ....*....|....*....|...
gi 499176343  86 LMVQLQQQYQAVIQQITRLRQTA 108
Cdd:cd00592   78 LLALLDEKLAELEEKIARLEALL 100
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
8-111 1.19e-22

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


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 91.12  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   8 IKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEEslDPTLM 87
Cdd:COG0789    1 IGEVARLTG--VSVRTLRYYERIGLLPPPERTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDDG--EEEVR 76

                         90       100
                 ....*....|....*....|....
gi 499176343  88 VQLQQQYQAVIQQITRLRQTASAL 111
Cdd:COG0789   77 ELLEEHLAELEAQIAELQALRAEL 100
MerR_1 pfam13411
MerR HTH family regulatory protein;
7-74 2.06e-15

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 70.28  E-value: 2.06e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343    7 TIKELTDAVGggVTPRMVRHYHTLGLLPPVqRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:pfam13411   2 TISELARLLG--VTPRTLRYWEREGLLPPP-RTERGRRYYTDEDVERLRLIKALLERGLSLKEIKELL 66
zntR PRK09514
Zn(2+)-responsive transcriptional regulator;
18-75 5.83e-13

Zn(2+)-responsive transcriptional regulator;


Pssm-ID: 181924 [Multi-domain]  Cd Length: 140  Bit Score: 65.37  E-value: 5.83e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:PRK09514  12 EVTPDTLRFYEKQGLMDPEVRTEGGYRLYTEQDLQRLRFIRRAKQLGFTLEEIRELLS 69
CueR TIGR02044
Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and ...
 18-74 2.57e-11

Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and gold- (I) responsive transcriptional activator of the gamma proteobacterial copper efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This family also lacks a conserved cysteine at the N-terminal end of the dimerization helix which is required for the binding of divalent metals such as zinc; here it is replaced by a serine residue. [Regulatory functions, DNA interactions]


Pssm-ID: 131099 [Multi-domain]  Cd Length: 127  Bit Score: 60.54  E-value: 2.57e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343   18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:TIGR02044  11 GLSSKMIRYYEEKGLIPPPLRSEGGYRTYTQQHLDELRLISRARQVGFSLEECKELL 67
 
Name Accession Description Interval E-value
CobH COG2082
Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]; Precorrin-8X ...
 157-355 1.82e-81

Precorrin-8X methylmutase CbiC/CobH [Coenzyme transport and metabolism]; Precorrin-8X methylmutase CbiC/CobH is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441685  Cd Length: 203  Bit Score: 247.26  E-value: 1.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 157 TTTHPEAFQESLKHLLP--DLSAYSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALD 234
Cdd:COG2082    3 IRDPAEIERESFAIIRAelDLSRFSEDEEPVVVRLIHATGDFDLADLLRFSPGAVEAGRAALRAGAPIVTDVEMVAAGIN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 235 QTRLAHLGCTVKTLIDDPHITGLREAEQAFWHHDHWQQRLQQIPqGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPI 314
Cdd:COG2082   83 KRRLPALGNEVICLISDPRVAELAKAEGITRSAAAMRLAAERLE-GAIVAIGNAPTALFELLELIEEGAPRPALIIGVPV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499176343 315 GFSHAPGAKRRLMTSPIPHITIQGSLGGGLLAAVTLNALVE 355
Cdd:COG2082  162 GFVGAAESKEALMASGVPYITVRGRKGGSAIAAAAVNALLY 202
CbiC pfam02570
Precorrin-8X methylmutase; This is a family Precorrin-8X methylmutases also known as Precorrin ...
 174-355 7.31e-66

Precorrin-8X methylmutase; This is a family Precorrin-8X methylmutases also known as Precorrin isomerase, CbiC/CobH, EC:5.4.1.2. This enzyme catalyzes the reaction: Precorrin-8X <=> hydrogenobyrinate. This enzyme is part of the Cobalamin (vitamin B12) biosynthetic pathway and catalyzes a methyl rearrangement.


Pssm-ID: 426840  Cd Length: 195  Bit Score: 206.85  E-value: 7.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  174 DLSAYSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRLAHLGCTVKTLIDDPH 253
Cdd:pfam02570  14 GLHRFSPAEYEIVRRVIHATGDFEYADLLRFSPGAVEAGRAALKAGAPIVTDVNMVAAGINKRRLATFGNPVYCFLDDPE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  254 ITGLREaEQAFWHHDHWQQRLQQIPQGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGAKRRLMTSPIPH 333
Cdd:pfam02570  94 VAELAK-ERGITRSAAAMELAAERLPGAIVVIGNAPTALFELLELIEEGKIRPALVIGVPVGFVGAAESKEALAASGVPY 172

                         170       180
                  ....*....|....*....|..
gi 499176343  334 ITIQGSLGGGLLAAVTLNALVE 355
Cdd:pfam02570 173 ITVRGRKGGSAVAAAIVNALLY 194
cobH PRK08285
precorrin-8X methylmutase; Reviewed
 174-353 2.74e-25

precorrin-8X methylmutase; Reviewed


Pssm-ID: 181352  Cd Length: 208  Bit Score: 101.50  E-value: 2.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 174 DLSAYSE----ITIHLLHqlvlACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRLAHlGCTVKTLI 249
Cdd:PRK08285  24 DLSRFPAdlekVAVRMIH----ACGMVDVADDLAFSPGAVAAARAALAAGAPILCDARMVAEGITRARLPA-DNEVICTL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 250 DDPHITGL-------REAEQAfwhhDHWQQRLQqipqGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGA 322
Cdd:PRK08285  99 RDPRVPELaaelgntRSAAAL----ELWRPRLA----GSVVAIGNAPTALFRLLEMLDAGAPRPAAILGFPVGFVGAAES 170

                        170       180       190
                 ....*....|....*....|....*....|...
gi 499176343 323 KRRLMTSP--IPHITIQGSLGGGLLAAVTLNAL 353
Cdd:PRK08285 171 KDALAADSrgVPYLIVRGRRGGSAMAAAAVNAL 203
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
6-75 6.73e-24

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 93.35  E-value: 6.73e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343     6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:smart00422   1 YTIGEVAKLAG--VSVRTLRYYERIGLLPPPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELLE 68
HTH_MerR-like cd00592
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ...
 6-108 1.07e-23

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.


Pssm-ID: 133378 [Multi-domain]  Cd Length: 100  Bit Score: 93.85  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESLDPT 85
Cdd:cd00592    1 YTIGEVAKLLG--VSVRTLRYYEEKGLLPP-ERSENGYRLYSEEDLERLRLIRRLRELGLSLKEIRELLDARDEELSLAA 77

                         90       100
                 ....*....|....*....|...
gi 499176343  86 LMVQLQQQYQAVIQQITRLRQTA 108
Cdd:cd00592   78 LLALLDEKLAELEEKIARLEALL 100
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
8-111 1.19e-22

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


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 91.12  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   8 IKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEEslDPTLM 87
Cdd:COG0789    1 IGEVARLTG--VSVRTLRYYERIGLLPPPERTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDDG--EEEVR 76

                         90       100
                 ....*....|....*....|....
gi 499176343  88 VQLQQQYQAVIQQITRLRQTASAL 111
Cdd:COG0789   77 ELLEEHLAELEAQIAELQALRAEL 100
PRK05953 PRK05953
Precorrin-8X methylmutase;
185-355 1.32e-20

Precorrin-8X methylmutase;


Pssm-ID: 180325  Cd Length: 208  Bit Score: 88.62  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 185 LLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVV----AAALDQTRLAHLGCTVKTlIDDPHitglREA 260
Cdd:PRK05953  30 IVRRVIYATADFEYLSLIRFSERALQAGAAALAARTTIVVDVPMVqvgiAPTLQNTFANPVYCSTET-ITRPQ----KEK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 261 EQAFWHHDHWQQRLqqiPQGcVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGAKRRLMTSPIPHITIQGSL 340
Cdd:PRK05953 105 TRTAWGIETLARRY---PEA-IFVIGQSQTALTALVELVEAEEIRPALVIATPAGFIDADDAKERLQDSLVPHITIDGRK 180

                        170
                 ....*....|....*
gi 499176343 341 GGGLLAAVTLNALVE 355
Cdd:PRK05953 181 GGAVVAVAIIDGLVD 195
HTH_TipAL-Mta cd01106
Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA; ...
 6-89 6.64e-20

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.


Pssm-ID: 133381 [Multi-domain]  Cd Length: 103  Bit Score: 83.69  E-value: 6.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDShSEESLDPT 85
Cdd:cd01106    1 YTVGEVAKLTG--VSVRTLHYYDEIGLLKPSRRTENGYRLYTEEDLERLQQILFLKELGFSLKEIKELLKD-PSEDLLEA 77


                 ....
gi 499176343  86 LMVQ 89
Cdd:cd01106   78 LREQ 81
HTH_HMRTR cd04770
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ...
 6-127 1.44e-17

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.


Pssm-ID: 133398 [Multi-domain]  Cd Length: 123  Bit Score: 77.99  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESLDPT 85
Cdd:cd04770    1 MKIGELAKAAG--VSPDTIRYYERIGLLPPPQRSENGYRLYGEADLARLRFIRRAQALGFSLAEIRELLSLRDDGAAPCA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499176343  86 LMVQLQQQ-YQAVIQQITRLRQTASALEGLLGRdqsCQITQAE 127
Cdd:cd04770   79 EVRALLEEkLAEVEAKIAELQALRAELAGLLSA---CDGDESV 118
HTH_NolA-AlbR cd04788
Helix-Turn-Helix DNA binding domain of the transcription regulators NolA and AlbR; ...
 8-90 2.45e-17

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.


Pssm-ID: 133415 [Multi-domain]  Cd Length: 96  Bit Score: 76.26  E-value: 2.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   8 IKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDshsEESLDPTLM 87
Cdd:cd04788    3 IGELARRTG--LSVRTLHHYDHIGLLSPSQRTEGGHRLYDRADIRRLHQIIALRRLGFSLREIGRALD---GPDFDPLEL 77


                 ...
gi 499176343  88 VQL 90
Cdd:cd04788   78 LRR 80
cbiC PRK08286
cobalt-precorrin-8 methylmutase;
203-357 3.73e-16

cobalt-precorrin-8 methylmutase;


Pssm-ID: 181353  Cd Length: 214  Bit Score: 76.64  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 203 RLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRLAHLGCTVKTLIDDPHITGLREAEQ------AFwhhdhwqQRLQQ 276
Cdd:PRK08286  57 WFSPDALEKIIDALRNPCTIYTDTTMALSGINKRLLDTLGCEYRCYISDPRVVELAKEQGitrsmaAV-------DIAAA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 277 IPQGCVLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGAKRRLMTSPIPHITIQGSLGGGLLAAVTLNALVET 356
Cdd:PRK08286 130 EEGPKLFVFGNAPTALFRLLEMVEHGQLQVDAVVGVPVGFVGAAESKEALTESDLPAIAALGRKGGSNVAAAIVNAILYH 209


                 .
gi 499176343 357 L 357
Cdd:PRK08286 210 L 210
PRK05782 PRK05782
bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase; Validated
 155-354 3.87e-16

bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase; Validated


Pssm-ID: 235605 [Multi-domain]  Cd Length: 335  Bit Score: 78.31  E-value: 3.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 155 AETTTHPEAFQES-----LKHLLPDLSAYSEITIhlLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVV 229
Cdd:PRK05782 138 LEYTEDPEEIEERsmnyiLENLGLDVKDWREKRV--IARAVYASGNLELAKYVKISNDLLDAGIEAIRAESEIVADVKMV 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 230 AAALDQTRlahlgctVKTLIDDPHITGLREA---EQAFWHHDHWQQRlqqipQGCVLAIGYAPSVLLTACKLIEQQhIQP 306
Cdd:PRK05782 216 SAGIRWKK-------VTCMIDAERTKELAKElgiTRAAAAMRLSLGQ-----GGKVVVIGNAPTALIETLKLVKEG-VDI 282

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499176343 307 ALVIGMPIGFSHAPGAKRRLMTSPIPHITIQGSLGGGLLAAVTLNALV 354
Cdd:PRK05782 283 PFIVATPPGFTNAKEVKEALIESGIPSVVLRGTYGGSGIAVAIINELI 330
cbiC PRK06264
cobalt-precorrin-8 methylmutase;
162-354 4.92e-16

cobalt-precorrin-8 methylmutase;


Pssm-ID: 235759  Cd Length: 210  Bit Score: 75.90  E-value: 4.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 162 EAFQESLKHLLPD-LSAYSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRlah 240
Cdd:PRK06264  17 EIVKNKIKEVLGDkIKLYSEEEMGIIERVVHATADPEYAKLVVFSNDPIEEGLDAIKDKKPIIVDINMVKAGIRYNN--- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 241 lgctVKTLIDDPHITGLREAEQAFWHHDHWQQRLQQIPQGCVlAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAP 320
Cdd:PRK06264  94 ----VYCFISEPEVFELAKKEQITRAVASMRLAKELIDGGIV-VIGNAPTALFEVIRLVKEEGIKPKLVVGVPVGFVKAA 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 499176343 321 GAKRRLMTSPIPHITIQGSLGGGLLAAVTLNALV 354
Cdd:PRK06264 169 ESKEALRNTNIPSISTIGPKGGTPVAVSIINGII 202
MerR_1 pfam13411
MerR HTH family regulatory protein;
7-74 2.06e-15

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 70.28  E-value: 2.06e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343    7 TIKELTDAVGggVTPRMVRHYHTLGLLPPVqRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:pfam13411   2 TISELARLLG--VTPRTLRYWEREGLLPPP-RTERGRRYYTDEDVERLRLIKALLERGLSLKEIKELL 66
cbiC PRK05575
precorrin-8X methylmutase; Validated
 178-354 4.89e-15

precorrin-8X methylmutase; Validated


Pssm-ID: 180140  Cd Length: 204  Bit Score: 72.90  E-value: 4.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 178 YSEITIHLLHQLVLACGDVSLVNAVRLSQGAIASARDALKAGCPVVTDVPVVAAALDQTRLAHLGCTVKTLIDDPHITGL 257
Cdd:PRK05575  27 FSEEELKIVKRVIHTTADFEYKDLIYIREGAIEAAKEILKKGTKIYTDTNMALSGINKKALKKLNSTVQCYVSREEVAKI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343 258 REAEQAfwhhdhwQQRLQQIPQGC-----VLAIGYAPSVLLTACKLIEQQHIQPALVIGMPIGFSHAPGAKRRLMTSPIP 332
Cdd:PRK05575 107 AKERGI-------TRSMAAVEKAAeegveFFVFGNAPTALYKLKELIKEGKANPKFIIAVPVGFVGAAESKEELEKLDIP 179

                        170       180
                 ....*....|....*....|..
gi 499176343 333 HITIQGSLGGGLLAAVTLNALV 354
Cdd:PRK05575 180 YITVRGRKGGSTVAAAIVNALM 201
HTH_CueR cd01108
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ...
 18-75 3.30e-14

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.


Pssm-ID: 133383 [Multi-domain]  Cd Length: 127  Bit Score: 68.74  E-value: 3.30e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:cd01108   11 GLSAKMIRYYEEIGLIPPPSRSDNGYRVYNQRDIEELRFIRRARDLGFSLEEIRELLA 68
HTH_YfmP cd04774
Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) ...
 6-83 1.30e-13

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.


Pssm-ID: 133401 [Multi-domain]  Cd Length: 96  Bit Score: 66.00  E-value: 1.30e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQ-GFQLSHIRQLLDShSEESLD 83
Cdd:cd04774    1 YKVDEVAKRLG--LTKRTLKYYEEIGLVSP-ERSEGRYRLYSEEDLKRLERILRLREVlGFSLQEVTHFLER-PLEPVD 75
HTH_MerR2 cd04769
Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix ...
 18-122 2.44e-13

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.


Pssm-ID: 133397 [Multi-domain]  Cd Length: 116  Bit Score: 65.85  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSeGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSH--SEESLDPTLMVQLQQQYQ 95
Cdd:cd04769   11 GVTIKAIRLYEEKGLLPSPKRS-GNYRVYDAQHVECLRFIKEARQLGFTLAELKAIFAGHegRAVLPWPHLQQALEDKKQ 89

                         90       100
                 ....*....|....*....|....*..
gi 499176343  96 AVIQQITRLRQTASALEGLLGRDQSCQ 122
Cdd:cd04769   90 EIRAQITELQQLLARLDAFEASLKDAL 116
zntR PRK09514
Zn(2+)-responsive transcriptional regulator;
18-75 5.83e-13

Zn(2+)-responsive transcriptional regulator;


Pssm-ID: 181924 [Multi-domain]  Cd Length: 140  Bit Score: 65.37  E-value: 5.83e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:PRK09514  12 EVTPDTLRFYEKQGLMDPEVRTEGGYRLYTEQDLQRLRFIRRAKQLGFTLEEIRELLS 69
HTH_HMRTR_unk cd04787
Helix-Turn-Helix DNA binding domain of putative Heavy Metal Resistance transcription ...
 6-88 8.67e-13

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.


Pssm-ID: 133414 [Multi-domain]  Cd Length: 133  Bit Score: 65.02  E-value: 8.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLdSHSEESLDPT 85
Cdd:cd04787    1 MKVKELANAAG--VTPDTVRFYTRIGLLRPTRDPVNGYRLYSEKDLSRLRFILSARQLGFSLKDIKEIL-SHADQGESPC 77


                 ...
gi 499176343  86 LMV 88
Cdd:cd04787   78 PMV 80
HTH_BmrR cd01107
Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator; Helix-turn-helix (HTH) ...
 18-115 1.33e-12

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.


Pssm-ID: 133382 [Multi-domain]  Cd Length: 108  Bit Score: 63.69  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGN-YRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESLDPTLMVQLqqqyQA 96
Cdd:cd01107   11 NLSIKALRYYDKIGLLKPAYVDPDTgYRYYSAEQLERLNRIKYLRDLGFPLEEIKEILDADNDDELRKLLREKL----AE 86

                         90
                 ....*....|....*....
gi 499176343  97 VIQQITRLRQTASALEGLL 115
Cdd:cd01107   87 LEAEIEELQRILRLLEDRL 105
HTH_MerR-SF cd04761
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 6-57 4.40e-12

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.


Pssm-ID: 133389 [Multi-domain]  Cd Length: 49  Bit Score: 60.30  E-value: 4.40e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVqRSEGNYRLYTQQDVQRLQRV 57
Cdd:cd04761    1 YTIGELAKLTG--VSPSTLRYYERIGLLSPA-RTEGGYRLYSDADLERLRLI 49
CueR TIGR02044
Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and ...
 18-74 2.57e-11

Cu(I)-responsive transcriptional regulator; This model represents the copper-, silver- and gold- (I) responsive transcriptional activator of the gamma proteobacterial copper efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This family also lacks a conserved cysteine at the N-terminal end of the dimerization helix which is required for the binding of divalent metals such as zinc; here it is replaced by a serine residue. [Regulatory functions, DNA interactions]


Pssm-ID: 131099 [Multi-domain]  Cd Length: 127  Bit Score: 60.54  E-value: 2.57e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343   18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:TIGR02044  11 GLSSKMIRYYEEKGLIPPPLRSEGGYRTYTQQHLDELRLISRARQVGFSLEECKELL 67
MerR pfam00376
MerR family regulatory protein;
7-46 2.95e-11

MerR family regulatory protein;


Pssm-ID: 425647 [Multi-domain]  Cd Length: 38  Bit Score: 57.81  E-value: 2.95e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499176343    7 TIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLY 46
Cdd:pfam00376   1 TIGEVAKLLG--VSPRTLRYYEKIGLLPPPERTEGGYRRY 38
HTH_GnyR cd04776
Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR; Putative helix-turn-helix ...
 6-144 4.43e-11

Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR; Putative helix-turn-helix (HTH) regulatory protein, GnyR, and other related proteins. GnyR belongs to the gnyRDBHAL cluster, which is involved in acyclic isoprenoid degradation in Pseudomonas aeruginosa. 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.


Pssm-ID: 133403  Cd Length: 118  Bit Score: 59.47  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRseGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESLDPT 85
Cdd:cd04776    1 YTISELAREFD--VTPRTLRFYEDKGLLSPERR--GQTRVYSRRDRARLKLILRGKRLGFSLEEIRELLDLYDPPGGNRK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343  86 lmvQLQQQYQAVIQQITRLRQTASALEgllgrdqscqitqaEALAQLKQLDVDVQEGLG 144
Cdd:cd04776   77 ---QLEKMLEKIEKRRAELEQQRRDID--------------AALAELDAAEERCRERLA 118
HTH_Cfa-like_unk cd04790
Helix-Turn-Helix DNA binding domain of putative Cfa-like transcription regulators; Putative ...
 6-116 5.40e-11

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.


Pssm-ID: 133417 [Multi-domain]  Cd Length: 172  Bit Score: 60.91  E-value: 5.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDShSEESLDPT 85
Cdd:cd04790    2 LTISQLARQFG--LSRSTLLYYERIGLLSPSARSESNYRLYGERDLERLEQICAYRSAGVSLEDIRSLLQQ-PGDDATDV 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499176343  86 LMVQLqqqyQAVIQQITRLRQTASALEGLLG 116
Cdd:cd04790   79 LRRRL----AELNREIQRLRQQQRAIATLLK 105
HTH_MerR1 cd04783
Helix-Turn-Helix DNA binding domain of the MerR1 transcription regulator; Helix-turn-helix ...
 6-75 5.84e-11

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.


Pssm-ID: 133410 [Multi-domain]  Cd Length: 126  Bit Score: 59.55  E-value: 5.84e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499176343   6 LTIKELTDAVGGGVtpRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLqRVIALKQQ-GFQLSHIRQLLD 75
Cdd:cd04783    1 LTIGELAKAAGVNV--ETIRYYQRRGLLPEPPRPEGGYRRYPEETVTRL-RFIKRAQElGFTLDEIAELLE 68
HTH_YyaN cd01109
Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; ...
 6-72 2.14e-10

Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. 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.


Pssm-ID: 133384 [Multi-domain]  Cd Length: 113  Bit Score: 57.47  E-value: 2.14e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQ 72
Cdd:cd01109    1 YTIKEVAEKTG--LSADTLRYYEKEGLLPPVKRDENGIRDFTEEDLEWLEFIKCLRNTGMSIKDIKE 65
HTH_MerR-like_sg3 cd01282
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 18-75 2.45e-10

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 3). 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.


Pssm-ID: 133388  Cd Length: 112  Bit Score: 57.23  E-value: 2.45e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343  18 GVTPRMVRHYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:cd01282   11 GVSVRSLRYYEEQGLLVP-ERSANGYRDYDEAAVDRVRQIRRLLAAGLTLEEIREFLP 67
HTH_CadR-PbrR-like cd04785
Helix-Turn-Helix DNA binding domain of the CadR- and PbrR-like transcription regulators; ...
 6-75 2.79e-10

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.


Pssm-ID: 133412 [Multi-domain]  Cd Length: 126  Bit Score: 57.56  E-value: 2.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGGGVTprMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:cd04785    1 LSIGELARRTGVNVE--TIRYYESIGLLPEPARTAGGYRLYGAAHVERLRFIRRARDLGFSLEEIRALLA 68
HTH_CadR-PbrR cd04784
Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; ...
 8-75 4.22e-10

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.


Pssm-ID: 133411  Cd Length: 127  Bit Score: 57.19  E-value: 4.22e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343   8 IKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:cd04784    3 IGELAKKTG--CSVETIRYYEKEGLLPAPARSANNYRLYDEEHLERLLFIRRCRSLDMSLDEIRTLLQ 68
HTH_BmrR-like cd04768
Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators; Helix-turn-helix ...
 6-80 5.80e-09

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.


Pssm-ID: 133396 [Multi-domain]  Cd Length: 96  Bit Score: 52.74  E-value: 5.80e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499176343   6 LTIKELtdAVGGGVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEE 80
Cdd:cd04768    1 LTIGEF--AKLAGVSIRTLRHYDDIGLFKPAKIAENGYRYYSYAQLYQLQFILFLRELGFSLAEIKELLDTEMEE 73
HTH_MlrA-CarA cd01104
Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; ...
 33-75 5.85e-09

Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A), 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- and CarA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins.


Pssm-ID: 133379  Cd Length: 68  Bit Score: 51.86  E-value: 5.85e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499176343  33 LPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:cd01104   26 LPAPQRTDGGHRLYSEADVARLRLIRRLTSEGVRISQAAALAL 68
HTH_Cfa-like cd04775
Helix-Turn-Helix DNA binding domain of Cfa-like transcription regulators; Putative ...
 18-116 1.92e-08

Helix-Turn-Helix DNA binding domain of Cfa-like transcription regulators; Putative helix-turn-helix (HTH) MerR-like transcription regulators; the HTH domain of Cfa, a cyclopropane fatty acid synthase, and other related methyltransferases, as well as, the N-terminal domain of a conserved, uncharacterized ~172 a.a. protein. Based on sequence similarity of the N-terminal domain, 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.


Pssm-ID: 133402 [Multi-domain]  Cd Length: 102  Bit Score: 51.77  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  18 GVTPRMVRHYHTLGLLPPVqRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLdshsEESLDPTLMVQlqqQYQAV 97
Cdd:cd04775   12 GVSRSTLLYYESIGLIPSA-RSEANYRLYSEADLSRLEKIVFLQAGGLPLEEIAGCL----AQPHVQAILEE---RLQSL 83

                         90
                 ....*....|....*....
gi 499176343  98 IQQITRLRQTASALEGLLG 116
Cdd:cd04775   84 NREIQRLRQQQQVLAAILG 102
HTH_MerR-like_sg4 cd04779
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 18-71 2.85e-08

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.


Pssm-ID: 133406 [Multi-domain]  Cd Length: 134  Bit Score: 52.12  E-value: 2.85e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499176343  18 GVTPRMVRHYHTLGLLPPVqRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIR 71
Cdd:cd04779   11 GVSKRTIDYYTNLGLLTPE-RSDSNYRYYDETALDRLQLIEHLKGQRLSLAEIK 63
CadR-PbrR TIGR02047
Cd(II)/Pb(II)-responsive transcriptional regulator; This model represents the cadmium(II) and ...
 6-74 2.93e-08

Cd(II)/Pb(II)-responsive transcriptional regulator; This model represents the cadmium(II) and/or lead(II) responsive transcriptional activator of the proteobacterial metal efflux system. This protein is a member of the MerR family of transcriptional activators (pfam00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(6-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of the dimerization helix. [Regulatory functions, DNA interactions]


Pssm-ID: 131102  Cd Length: 127  Bit Score: 51.73  E-value: 2.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343    6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:TIGR02047   1 MKIGELAQKTG--VSVETIRFYEKQGLLPPPARTDNNYRVYTVGHVERLAFIRNCRTLDMSLAEIRQLL 67
HTH_TioE_rpt2 cd04773
Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ...
 6-75 9.36e-08

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.


Pssm-ID: 133400  Cd Length: 108  Bit Score: 49.67  E-value: 9.36e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:cd04773    1 MTIGELAHLLG--VPPSTLRHWEKEGLLSPDREPETGYRVYDPSDVRDARLIHLLRRGGYLLEQIATVVE 68
HTH_HspR cd04766
Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) ...
 18-75 1.00e-07

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.


Pssm-ID: 133394 [Multi-domain]  Cd Length: 91  Bit Score: 49.19  E-value: 1.00e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343  18 GVTPRMVRHYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQ-QGFQLSHIRQLLD 75
Cdd:cd04766   12 GMHPQTLRLYERLGLLSP-SRTDGGTRRYSERDIERLRRIQRLTQeLGVNLAGVKRILE 69
HTH_BltR cd04782
Helix-Turn-Helix DNA binding domain of the BltR transcription regulator; Helix-turn-helix (HTH) ...
 18-82 1.05e-07

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.


Pssm-ID: 133409 [Multi-domain]  Cd Length: 97  Bit Score: 49.15  E-value: 1.05e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESL 82
Cdd:cd04782   11 GISKQTLFHYDKIGLFKPEIVKENGYRYYTLEQFEQLDIILLLKELGISLKEIKDYLDNRNPDEL 75
HTH_MlrA-like_sg1 cd04764
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ...
 7-74 5.26e-07

Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 1). 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. 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.


Pssm-ID: 133392  Cd Length: 67  Bit Score: 46.55  E-value: 5.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343   7 TIKELTDAVGggVTPRMVRHYHT-LGLLPPvqRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:cd04764    2 TIKEVSEIIG--VKPHTLRYYEKeFNLYIP--RTENGRRYYTDEDIELLKKIKTLLEKGLSIKEIKEIL 66
HTH_GlnR-like cd01105
Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix ...
 6-81 1.33e-06

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.


Pssm-ID: 133380  Cd Length: 88  Bit Score: 46.07  E-value: 1.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343   6 LTIKELTDAVGggVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLqRVIA-LKQQGFQLSHIRQLLDSHSEES 81
Cdd:cd01105    2 IGIGEVSKLTG--VSPRQLRYWEEKGLIKSIRSDGGGQRKYSLADVDRL-LVIKeLLDEGFTLAAAVEKLRRRRVQA 75
PRK10227 PRK10227
HTH-type transcriptional regulator CueR;
18-75 1.80e-06

HTH-type transcriptional regulator CueR;


Pssm-ID: 182320  Cd Length: 135  Bit Score: 46.95  E-value: 1.80e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLD 75
Cdd:PRK10227  11 GLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVN 68
HTH_MerR-like_sg2 cd04778
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 18-76 7.46e-06

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 2). 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.


Pssm-ID: 133405 [Multi-domain]  Cd Length: 219  Bit Score: 46.62  E-value: 7.46e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRsEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDS 76
Cdd:cd04778   12 GTTVRNVRAYQDRGLLPPPRR-RGRVAIYNDSHLARLRLINQLLERGYTLAHIAELLAA 69
HTH_TioE_rpt1 cd04772
First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ...
 18-71 1.38e-05

First 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 contains the N-terminal or first repeat (rpt1) of these tandem MerR-like domain proteins.


Pssm-ID: 133399  Cd Length: 99  Bit Score: 43.54  E-value: 1.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQ-RVIALKQQGFQLS--HIR 71
Cdd:cd04772   11 GLSPQTVRNYESLGLIPPAERTANGYRIYTDKHIAALRaYRALLPGYGYRVAqrIMR 67
HTH_MerR-like_sg7 cd04786
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 18-74 1.42e-05

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.


Pssm-ID: 133413 [Multi-domain]  Cd Length: 131  Bit Score: 44.05  E-value: 1.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343  18 GVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:cd04786   11 GMAASRIRFYEAEGLLSSVERSANGYRDYPPETVWVLEIISSAQQAGFSLDEIRQLL 67
PRK13752 PRK13752
mercuric resistance operon transcriptional regulator MerR;
1-81 1.77e-05

mercuric resistance operon transcriptional regulator MerR;


Pssm-ID: 184302  Cd Length: 144  Bit Score: 44.13  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   1 MKTN--HLTIKELTDAvgGGVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL---- 74
Cdd:PRK13752   1 MENNleNLTIGVFAKA--AGVNVETIRFYQRKGLLPEPDKPYGSIRRYGEADVTRVRFVKSAQRLGFSLDEIAELLrled 78


                 ....*..
gi 499176343  75 DSHSEES 81
Cdd:PRK13752  79 GTHCEEA 85
HTH_MlrA-like cd04763
Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix ...
 18-74 2.64e-05

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.


Pssm-ID: 133391  Cd Length: 68  Bit Score: 41.75  E-value: 2.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499176343  18 GVTPRMVRHYHT-LGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:cd04763   11 GIKPHVLRAWEReFGLLKP-QRSDGGHRLFNDADIDRILEIKRWIDNGVQVSKVKKLL 67
HTH_MerR-like_sg6 cd04781
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 6-112 2.31e-04

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.


Pssm-ID: 133408  Cd Length: 120  Bit Score: 40.34  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   6 LTIKELtdAVGGGVTPRMVRHYHTLGLLPPVQRsEGNYRLYTQQDVQRLQrVIALKQQ-GFQLSHIRQLLDSHSEESLDP 84
Cdd:cd04781    1 LDIAEV--ARQSGLPASTLRYYEEKGLIASIGR-RGLRRQYDPQVLDRLA-LIALGRAaGFSLDEIQAMLSHDGKPPIDR 76

                         90       100
                 ....*....|....*....|....*...
gi 499176343  85 TlmvQLQQQYQAVIQQITRLRQTASALE 112
Cdd:cd04781   77 Q---LLKAKAAELDQQIQRLQAMRELLR 101
HTH_MerR-like_sg1 cd04777
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 19-74 2.88e-04

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 1), N-terminal domain. 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.


Pssm-ID: 133404 [Multi-domain]  Cd Length: 107  Bit Score: 39.70  E-value: 2.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499176343  19 VTPRMVRHYHTLGLLPPvQRSEGNYRlYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:cd04777   12 ITIDTVRHYIDLGLLIP-EKKGGQYF-FDEKCQDDLEFILELKGLGFSLIEIQKIF 65
HTH_Cfa cd04789
Helix-Turn-Helix DNA binding domain of the Cfa transcription regulator; Putative ...
 26-116 2.97e-04

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.


Pssm-ID: 133416  Cd Length: 102  Bit Score: 39.78  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343  26 HYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEESldptlmvQLQQQYQAVIQQITRLR 105
Cdd:cd04789   20 YYEKLGLITG-TRNANGYRLYPDSDLQRLLLIQQLQAGGLSLKECLACLQGKLTRS-------LLLERLSSLAEQIARKQ 91

                         90
                 ....*....|.
gi 499176343 106 QTASALEGLLG 116
Cdd:cd04789   92 QARDLLAALLG 102
HTH_MerR-like_sg5 cd04780
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 8-82 2.98e-04

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 5), N-terminal domain. 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.


Pssm-ID: 133407  Cd Length: 95  Bit Score: 39.62  E-value: 2.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499176343   8 IKELTDAVGggvTPRMVRHYHTL-GLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGF-QLSHIRQLLDSHSEESL 82
Cdd:cd04780    3 MSELSKRSG---VSVATIKYYLReGLLPEGRRLAPNQAEYSEAHVERLRLIRALQQEGGlPISQIKEVLDAIADASL 76
HTH_SoxR cd01110
Helix-Turn-Helix DNA binding domain of the SoxR transcription regulator; Helix-turn-helix (HTH) ...
 6-76 4.86e-04

Helix-Turn-Helix DNA binding domain of the SoxR transcription regulator; Helix-turn-helix (HTH) transcriptional regulator SoxR. The global regulator, SoxR, up-regulates gene expression of another transcription activator, SoxS, which directly stimulates the oxidative stress regulon genes in E. coli. The soxRS response renders the bacterial cell resistant to superoxide-generating agents, macrophage-generated nitric oxide, organic solvents, and antibiotics. The SoxR proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the unusually long spacer between the -35 and -10 promoter elements. They also harbor a regulatory C-terminal domain containing an iron-sulfur center.


Pssm-ID: 133385 [Multi-domain]  Cd Length: 139  Bit Score: 39.87  E-value: 4.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499176343   6 LTIKELtdAVGGGVTPRMVRHYHTLGLLPPVqRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDS 76
Cdd:cd01110    2 LSVGEV--AKRSGVAVSALHFYEQKGLIASW-RNAGNQRRYPRDVLRRIAFIKVAQRLGLSLAEIAEALAT 69
PRK13749 PRK13749
HTH-type transcriptional regulator MerD;
4-129 5.45e-04

HTH-type transcriptional regulator MerD;


Pssm-ID: 184299  Cd Length: 121  Bit Score: 39.51  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499176343   4 NHLTIKELtdAVGGGVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLdshseESLD 83
Cdd:PRK13749   2 SAYTVSRL--ALDAGVSVHIVRDYLLRGLLRPVACTTGGYGLFDDAALQRLCFVRAAFEAGIGLDALARLC-----RALD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499176343  84 PTLMVQLQQQYQAVIQQITRLRQTASALEGLLGRDQSCQITQAEAL 129
Cdd:PRK13749  75 AADGDEAAAQLAVLRQLVERRREALADLEVQLATMPTEPAQHAESL 120
HTH_MerD cd01111
Helix-Turn-Helix DNA binding domain of the MerD transcription regulator; Helix-turn-helix (HTH) ...
 6-74 8.45e-04

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.


Pssm-ID: 133386  Cd Length: 107  Bit Score: 38.52  E-value: 8.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343   6 LTIKELtdAVGGGVTPRMVRHYHTLGLLPPVQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLL 74
Cdd:cd01111    1 YSISQL--ALDAGVSVHIVRDYLLRGLLHPVARTEGGYGLFDDCALQRLRFVRAAFEAGIGLDELARLC 67
HTH_HspR-like cd01279
Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix ...
 18-75 1.87e-03

Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix (HTH) transcription regulator HspR and related proteins, 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 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.


Pssm-ID: 133387  Cd Length: 98  Bit Score: 37.19  E-value: 1.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499176343  18 GVTPRMVRHYHTLGLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQ-QGFQLSHIRQLLD 75
Cdd:cd01279   12 GIHPQTLRVYDRLGLVSP-ARTNGGGRRYSNNDLELLRQVQRLSQdEGFNLAGIKRIIE 69
PRK15043 PRK15043
HTH-type transcriptional regulator MlrA;
31-80 2.10e-03

HTH-type transcriptional regulator MlrA;


Pssm-ID: 185003 [Multi-domain]  Cd Length: 243  Bit Score: 39.14  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 499176343  31 GLLPPvQRSEGNYRLYTQQDVQRLQRVIALKQQGFQLSHIRQLLDSHSEE 80
Cdd:PRK15043  28 GLLKP-QRTDGGHRLFNDADIDRIREIKRWIDNGVQVSKVKMLLSNENVD 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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