NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|727169525|ref|WP_033637918|]
View 

MULTISPECIES: redox-sensitive transcriptional activator SoxR [Serratia]

Protein Classification

redox-sensitive transcriptional activator SoxR( domain architecture ID 10100020)

redox-sensitive transcriptional activator SoxR mediates responses to stress including exposure to heavy metals, drugs or oxygen radicals

CATH:  1.10.10.10
Gene Ontology:  GO:0003700|GO:0003677|GO:0006355|GO:0051537|GO:0006979
PubMed:  15808743|12829265|17302809|35130613
SCOP:  3000158

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HTH_SoxR cd01110
Helix-Turn-Helix DNA binding domain of the SoxR transcription regulator; Helix-turn-helix (HTH) ...
 12-148 1.37e-75

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: 221.68  E-value: 1.37e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:cd01110    1 ELSVGEVAKRSGVAVSALHFYEQKGLIASWRNAGNQRRYPRDVLRRIAFIKVAQRLGLSLAEIAEALATLPEDRTPTKAD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAH 148
Cdd:cd01110   81 WERLSRAWRDRLDERIAELQQLRDQLDGCIGCGCLSLKKCPLYNPEDRLGAQGPGAR 137
 
Name Accession Description Interval E-value
HTH_SoxR cd01110
Helix-Turn-Helix DNA binding domain of the SoxR transcription regulator; Helix-turn-helix (HTH) ...
 12-148 1.37e-75

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: 221.68  E-value: 1.37e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:cd01110    1 ELSVGEVAKRSGVAVSALHFYEQKGLIASWRNAGNQRRYPRDVLRRIAFIKVAQRLGLSLAEIAEALATLPEDRTPTKAD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAH 148
Cdd:cd01110   81 WERLSRAWRDRLDERIAELQQLRDQLDGCIGCGCLSLKKCPLYNPEDRLGAQGPGAR 137
SoxR TIGR01950
redox-sensitive transcriptional activator SoxR; SoxR is a MerR-family homodimeric ...
 12-153 2.46e-72

redox-sensitive transcriptional activator SoxR; SoxR is a MerR-family homodimeric transcription factor with a 2Fe-2S cluster in each monomer. The motif CIGCGCxxxxxC is conserved. Oxidation of the iron-sulfur cluster activates SoxR. The physiological role in E. coli is response to oxidative stress. It is activated by superoxide, singlet oxygen, nitric oxide (NO), and hydrogen peroxide. In E. coli, SoxR increases expression of transcription factor SoxS; different downstream targets may exist in other species. [Cellular processes, Detoxification, Regulatory functions, DNA interactions]


Pssm-ID: 131005 [Multi-domain]  Cd Length: 142  Bit Score: 213.50  E-value: 2.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525   12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:TIGR01950   1 ELTVGELAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRRVAVIKAAQRVGIPLATIGEALAVLPEGRTPTADD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727169525   92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAHIFEHP 153
Cdd:TIGR01950  81 WARLSSQWREELDERIDQLNALRDQLDGCIGCGCLSLEDCPLRNPGDRLGEEGAGARLLEDE 142
PRK15002 PRK15002
redox-sensitive transcriptional activator SoxR;
12-151 1.96e-68

redox-sensitive transcriptional activator SoxR;


Pssm-ID: 184964  Cd Length: 154  Bit Score: 204.06  E-value: 1.96e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:PRK15002  11 LLTPGEVAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRYVAIIKIAQRIGIPLATIGEAFGVLPEGHTLSAKE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAHIFE 151
Cdd:PRK15002  91 WKQLSSQWREELDRRIHTLVALRDELDGCIGCGCLSRSDCPLRNPGDRLGEEGTGARLLE 150
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
15-117 1.13e-21

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


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 83.42  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGskltSEQWG 93
Cdd:COG0789    1 IGEVARLTGVSVRTLRYYERIGLLPpPERTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDDG----EEEVR 76

                         90       100
                 ....*....|....*....|....
gi 727169525  94 VLSSAWRKTLDERIQRLTVLRDHL 117
Cdd:COG0789   77 ELLEEHLAELEAQIAELQALRAEL 100
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
13-78 3.17e-18

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 73.71  E-value: 3.17e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727169525    13 LTVGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAAL 78
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPpPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELL 67
MerR-DNA-bind pfam09278
MerR, DNA binding; Members of this family of DNA-binding domains are predominantly found in ...
 55-120 5.10e-12

MerR, DNA binding; Members of this family of DNA-binding domains are predominantly found in the prokaryotic transcriptional regulator MerR. They adopt a structure consisting of a core of three alpha helices, with an architecture that is similar to that of the 'winged helix' fold.


Pssm-ID: 462739  Cd Length: 65  Bit Score: 57.51  E-value: 5.10e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169525   55 LRYIAVIKIAQRAGIPLEEIRAALSrFPIGSKLTSEQWGVLSSAWRKTLDERIQRLTVLRDHLDSC 120
Cdd:pfam09278   1 LRRLAFIRRARRLGFSLEEIRELLA-LYDDPGPPCADVRALLREKLAELEARIAELQALRDELDAL 65
 
Name Accession Description Interval E-value
HTH_SoxR cd01110
Helix-Turn-Helix DNA binding domain of the SoxR transcription regulator; Helix-turn-helix (HTH) ...
 12-148 1.37e-75

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: 221.68  E-value: 1.37e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:cd01110    1 ELSVGEVAKRSGVAVSALHFYEQKGLIASWRNAGNQRRYPRDVLRRIAFIKVAQRLGLSLAEIAEALATLPEDRTPTKAD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAH 148
Cdd:cd01110   81 WERLSRAWRDRLDERIAELQQLRDQLDGCIGCGCLSLKKCPLYNPEDRLGAQGPGAR 137
SoxR TIGR01950
redox-sensitive transcriptional activator SoxR; SoxR is a MerR-family homodimeric ...
 12-153 2.46e-72

redox-sensitive transcriptional activator SoxR; SoxR is a MerR-family homodimeric transcription factor with a 2Fe-2S cluster in each monomer. The motif CIGCGCxxxxxC is conserved. Oxidation of the iron-sulfur cluster activates SoxR. The physiological role in E. coli is response to oxidative stress. It is activated by superoxide, singlet oxygen, nitric oxide (NO), and hydrogen peroxide. In E. coli, SoxR increases expression of transcription factor SoxS; different downstream targets may exist in other species. [Cellular processes, Detoxification, Regulatory functions, DNA interactions]


Pssm-ID: 131005 [Multi-domain]  Cd Length: 142  Bit Score: 213.50  E-value: 2.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525   12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:TIGR01950   1 ELTVGELAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRRVAVIKAAQRVGIPLATIGEALAVLPEGRTPTADD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727169525   92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAHIFEHP 153
Cdd:TIGR01950  81 WARLSSQWREELDERIDQLNALRDQLDGCIGCGCLSLEDCPLRNPGDRLGEEGAGARLLEDE 142
PRK15002 PRK15002
redox-sensitive transcriptional activator SoxR;
12-151 1.96e-68

redox-sensitive transcriptional activator SoxR;


Pssm-ID: 184964  Cd Length: 154  Bit Score: 204.06  E-value: 1.96e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQ 91
Cdd:PRK15002  11 LLTPGEVAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRYVAIIKIAQRIGIPLATIGEAFGVLPEGHTLSAKE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIGCGCLSLADCPLRNPNDILGRQGAGAHIFE 151
Cdd:PRK15002  91 WKQLSSQWREELDRRIHTLVALRDELDGCIGCGCLSRSDCPLRNPGDRLGEEGTGARLLE 150
HTH_MerR-like_sg6 cd04781
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 13-132 9.40e-23

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: 86.95  E-value: 9.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPigskltseqw 92
Cdd:cd04781    1 LDIAEVARQSGLPASTLRYYEEKGLIASIGRRGLRRQYDPQVLDRLALIALGRAAGFSLDEIQAMLSHDG---------- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 727169525  93 gvLSSAWRK-------TLDERIQRLTVLRDHLDSCIGCGCLSLADCP 132
Cdd:cd04781   71 --KPPIDRQllkakaaELDQQIQRLQAMRELLRHVAQCPAPSHLDCP 115
HTH_MerR-like cd00592
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ...
 13-118 8.23e-22

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: 83.83  E-value: 8.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLtseqw 92
Cdd:cd00592    1 YTIGEVAKLLGVSVRTLRYYEEKGLLPPERSENGYRLYSEEDLERLRLIRRLRELGLSLKEIRELLDARDEELSL----- 75

                         90       100
                 ....*....|....*....|....*.
gi 727169525  93 gvlsSAWRKTLDERIQRLTVLRDHLD 118
Cdd:cd00592   76 ----AALLALLDEKLAELEEKIARLE 97
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
15-117 1.13e-21

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


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 83.42  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGskltSEQWG 93
Cdd:COG0789    1 IGEVARLTGVSVRTLRYYERIGLLPpPERTEGGYRLYSEEDVERLRFIRRLRELGFSLAEIRELLDLLDDG----EEEVR 76

                         90       100
                 ....*....|....*....|....
gi 727169525  94 VLSSAWRKTLDERIQRLTVLRDHL 117
Cdd:COG0789   77 ELLEEHLAELEAQIAELQALRAEL 100
HTH_MerR2 cd04769
Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators; Helix-turn-helix ...
 13-132 1.50e-18

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: 75.87  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAAlsrFPIGSKLTSEQW 92
Cdd:cd04769    1 MYIGELAQQTGVTIKAIRLYEEKGLLPSPKRSGNYRVYDAQHVECLRFIKEARQLGFTLAELKAI---FAGHEGRAVLPW 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727169525  93 GVLSSAW---RKTLDERIQRLTVLRDHLDSCIGcgclSLADCP 132
Cdd:cd04769   78 PHLQQALedkKQEIRAQITELQQLLARLDAFEA----SLKDAL 116
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
13-78 3.17e-18

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 73.71  E-value: 3.17e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727169525    13 LTVGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAAL 78
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPpPIRTEGGYRLYSDEDLERLRFIKRLKELGFSLEEIKELL 67
HTH_HMRTR cd04770
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ...
 13-133 1.16e-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: 73.75  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLI-QATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALsRFPIGSKLTSEQ 91
Cdd:cd04770    1 MKIGELAKAAGVSPDTIRYYERIGLLpPPQRSENGYRLYGEADLARLRFIRRAQALGFSLAEIRELL-SLRDDGAAPCAE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIG-CGCLSLADCPL 133
Cdd:cd04770   80 VRALLEEKLAEVEAKIAELQALRAELAGLLSaCDGDESVICPI 122
HTH_MerR1 cd04783
Helix-Turn-Helix DNA binding domain of the MerR1 transcription regulator; Helix-turn-helix ...
 13-133 5.46e-15

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: 66.86  E-value: 5.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLI-QATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSrfpIGSKLTSEQ 91
Cdd:cd04783    1 LTIGELAKAAGVNVETIRYYQRRGLLpEPPRPEGGYRRYPEETVTRLRFIKRAQELGFTLDEIAELLE---LDDGTDCSE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHL----DSCIGCGclSLADCPL 133
Cdd:cd04783   78 ARELAEQKLAEVDEKIADLQRMRASLqelvSQCAATK--NNVSCPI 121
HTH_MerR-like_sg3 cd01282
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 13-118 2.44e-13

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: 62.24  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALS--RFPIGSKLTSE 90
Cdd:cd01282    1 MRIGELAARTGVSVRSLRYYEEQGLLVPERSANGYRDYDEAAVDRVRQIRRLLAAGLTLEEIREFLPclRGGEPTFRPCP 80

                         90       100
                 ....*....|....*....|....*...
gi 727169525  91 QWGVLSSAWRKTLDERIQRLTVLRDHLD 118
Cdd:cd01282   81 DLLAVLRRELARIDRQIADLTRSRDRLD 108
HTH_MerR-like_sg7 cd04786
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 15-78 2.91e-13

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: 62.54  E-value: 2.91e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQAT-RNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAAL 78
Cdd:cd04786    3 IGELAKRSGMAASRIRFYEAEGLLSSVeRSANGYRDYPPETVWVLEIISSAQQAGFSLDEIRQLL 67
HTH_Cfa-like cd04775
Helix-Turn-Helix DNA binding domain of Cfa-like transcription regulators; Putative ...
 12-122 7.55e-13

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: 61.01  E-value: 7.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRfPIGSKLTSEQ 91
Cdd:cd04775    1 MYTIGQMSRKFGVSRSTLLYYESIGLIPSARSEANYRLYSEADLSRLEKIVFLQAGGLPLEEIAGCLAQ-PHVQAILEER 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 727169525  92 wgvLSSawrktLDERIQRLTVLRDHLDSCIG 122
Cdd:cd04775   80 ---LQS-----LNREIQRLRQQQQVLAAILG 102
HTH_YyaN cd01109
Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; ...
 13-118 7.86e-13

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: 60.93  E-value: 7.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLI-QATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIR--AALSRfpIGSKLTS 89
Cdd:cd01109    1 YTIKEVAEKTGLSADTLRYYEKEGLLpPVKRDENGIRDFTEEDLEWLEFIKCLRNTGMSIKDIKeyAELRR--EGDSTIP 78

                         90       100
                 ....*....|....*....|....*....
gi 727169525  90 EQWGVLsSAWRKTLDERIQRLTVLRDHLD 118
Cdd:cd01109   79 ERLELL-EEHREELEEQIAELQETLAYLD 106
HTH_TipAL-Mta cd01106
Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA; ...
 13-118 4.60e-12

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: 58.65  E-value: 4.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPS----VVLRYIAVIKiaqRAGIPLEEIRAALSRfPIGSKLT 88
Cdd:cd01106    1 YTVGEVAKLTGVSVRTLHYYDEIGLLKPSRRTENGYRLYTeedlERLQQILFLK---ELGFSLKEIKELLKD-PSEDLLE 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 727169525  89 S--EQwgvlssawRKTLDERIQRLTVLRDHLD 118
Cdd:cd01106   77 AlrEQ--------KELLEEKKERLDKLIKTID 100
MerR-DNA-bind pfam09278
MerR, DNA binding; Members of this family of DNA-binding domains are predominantly found in ...
 55-120 5.10e-12

MerR, DNA binding; Members of this family of DNA-binding domains are predominantly found in the prokaryotic transcriptional regulator MerR. They adopt a structure consisting of a core of three alpha helices, with an architecture that is similar to that of the 'winged helix' fold.


Pssm-ID: 462739  Cd Length: 65  Bit Score: 57.51  E-value: 5.10e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169525   55 LRYIAVIKIAQRAGIPLEEIRAALSrFPIGSKLTSEQWGVLSSAWRKTLDERIQRLTVLRDHLDSC 120
Cdd:pfam09278   1 LRRLAFIRRARRLGFSLEEIRELLA-LYDDPGPPCADVRALLREKLAELEARIAELQALRDELDAL 65
HTH_CadR-PbrR-like cd04785
Helix-Turn-Helix DNA binding domain of the CadR- and PbrR-like transcription regulators; ...
 13-133 5.23e-12

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: 59.10  E-value: 5.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLI-QATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRA--ALSRFPIGSkltS 89
Cdd:cd04785    1 LSIGELARRTGVNVETIRYYESIGLLpEPARTAGGYRLYGAAHVERLRFIRRARDLGFSLEEIRAllALSDRPDRS---C 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 727169525  90 EQWGVLSSAWRKTLDERIQRLTVLRDHLDSCI-GCGCLSLADCPL 133
Cdd:cd04785   78 AEADAIARAHLADVRARIADLRRLEAELKRMVaACSGGRVADCRI 122
HTH_MerR-SF cd04761
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 13-50 8.17e-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: 56.83  E-value: 8.17e-12
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRY 50
Cdd:cd04761    1 YTIGELAKLTGVSPSTLRYYERIGLLSPARTEGGYRLY 38
MerR_1 pfam13411
MerR HTH family regulatory protein;
14-78 8.40e-12

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 57.18  E-value: 8.40e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169525   14 TVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAAL 78
Cdd:pfam13411   2 TISELARLLGVTPRTLRYWEREGLLPPPRTERGRRYYTDEDVERLRLIKALLERGLSLKEIKELL 66
MerR pfam00376
MerR family regulatory protein;
14-50 1.36e-10

MerR family regulatory protein;


Pssm-ID: 425647 [Multi-domain]  Cd Length: 38  Bit Score: 53.19  E-value: 1.36e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 727169525   14 TVGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRY 50
Cdd:pfam00376   1 TIGEVAKLLGVSPRTLRYYEKIGLLPpPERTEGGYRRY 38
HTH_CueR cd01108
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ...
 13-132 2.56e-10

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: 54.88  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLI-QATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRA--ALSRFPigsKLTS 89
Cdd:cd01108    1 MNIGEAAKLTGLSAKMIRYYEEIGLIpPPSRSDNGYRVYNQRDIEELRFIRRARDLGFSLEEIREllALWRDP---SRAS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 727169525  90 EQWGVLSSAWRKTLDERIQRLTVLRDHL----DSCIGCGClslADCP 132
Cdd:cd01108   78 ADVKALALEHIAELERKIAELQAMRRTLqqlaDSCHGDDR---PDCP 121
HTH_TioE_rpt2 cd04773
Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ...
 13-112 6.51e-10

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: 53.13  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGN-QRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFpigskltsEQ 91
Cdd:cd04773    1 MTIGELAHLLGVPPSTLRHWEKEGLLSPDREPETgYRVYDPSDVRDARLIHLLRRGGYLLEQIATVVEQL--------RH 72

                         90       100
                 ....*....|....*....|.
gi 727169525  92 WGVLSSAwRKTLDERIQRLTV 112
Cdd:cd04773   73 AGGTEAL-AAALEQRRVALTQ 92
HTH_BmrR-like cd04768
Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators; Helix-turn-helix ...
 13-113 9.86e-10

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: 52.35  E-value: 9.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRY-IAVIKIAQRAGIPLEEIRAALS--RFPIGSKLTS 89
Cdd:cd04768    1 LTIGEFAKLAGVSIRTLRHYDDIGLFKPAKIAENGYRYYSYAQLYqLQFILFLRELGFSLAEIKELLDteMEELTAMLLE 80

                         90       100
                 ....*....|....*....|....
gi 727169525  90 EqwgvlssawRKTLDERIQRLTVL 113
Cdd:cd04768   81 K---------KQAIQQKIDRLQQL 95
HTH_Cfa cd04789
Helix-Turn-Helix DNA binding domain of the Cfa transcription regulator; Putative ...
 12-122 5.14e-09

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: 50.95  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSrfpigSKLTSEQ 91
Cdd:cd04789    1 MYTISELAEKAGISRSTLLYYEKLGLITGTRNANGYRLYPDSDLQRLLLIQQLQAGGLSLKECLACLQ-----GKLTRSL 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 727169525  92 WgvlsSAWRKTLDERIQRLTVLRDHLDSCIG 122
Cdd:cd04789   76 L----LERLSSLAEQIARKQQARDLLAALLG 102
HTH_NolA-AlbR cd04788
Helix-Turn-Helix DNA binding domain of the transcription regulators NolA and AlbR; ...
 15-114 5.52e-09

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: 50.45  E-value: 5.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQAT-RNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRfpigsklTSEQWG 93
Cdd:cd04788    3 IGELARRTGLSVRTLHHYDHIGLLSPSqRTEGGHRLYDRADIRRLHQIIALRRLGFSLREIGRALDG-------PDFDPL 75

                         90       100
                 ....*....|....*....|.
gi 727169525  94 VLSSAWRKTLDERIQRLTVLR 114
Cdd:cd04788   76 ELLRRQLARLEEQLELATRLR 96
HTH_BmrR cd01107
Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator; Helix-turn-helix (HTH) ...
 13-110 9.12e-09

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: 50.21  E-value: 9.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVV-LRYIAVIKIAQRAGIPLEEIRAALSRFPigskltse 90
Cdd:cd01107    1 FTIGEFAKLSNLSIKALRYYDKIGLLKpAYVDPDTGYRYYSAEqLERLNRIKYLRDLGFPLEEIKEILDADN-------- 72

                         90       100
                 ....*....|....*....|
gi 727169525  91 qwgvlSSAWRKTLDERIQRL 110
Cdd:cd01107   73 -----DDELRKLLREKLAEL 87
HTH_Cfa-like_unk cd04790
Helix-Turn-Helix DNA binding domain of putative Cfa-like transcription regulators; Putative ...
 12-110 3.12e-08

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: 50.12  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSE 90
Cdd:cd04790    1 MLTISQLARQFGLSRSTLLYYERIGLLSpSARSESNYRLYGERDLERLEQICAYRSAGVSLEDIRSLLQQPGDDATDVLR 80

                         90       100
                 ....*....|....*....|
gi 727169525  91 QwgVLSSawrktLDERIQRL 110
Cdd:cd04790   81 R--RLAE-----LNREIQRL 93
HTH_CadR-PbrR cd04784
Helix-Turn-Helix DNA binding domain of the CadR and PbrR transcription regulators; ...
 15-79 2.28e-07

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: 46.79  E-value: 2.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQA-TRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALS 79
Cdd:cd04784    3 IGELAKKTGCSVETIRYYEKEGLLPApARSANNYRLYDEEHLERLLFIRRCRSLDMSLDEIRTLLQ 68
PRK13752 PRK13752
mercuric resistance operon transcriptional regulator MerR;
13-133 2.33e-07

mercuric resistance operon transcriptional regulator MerR;


Pssm-ID: 184302  Cd Length: 144  Bit Score: 47.21  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLI-QATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIrAALSRFPIGSKltSEQ 91
Cdd:PRK13752   8 LTIGVFAKAAGVNVETIRFYQRKGLLpEPDKPYGSIRRYGEADVTRVRFVKSAQRLGFSLDEI-AELLRLEDGTH--CEE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 727169525  92 WGVLSSAWRKTLDERIQRLTVLRDHLDSCIgCGCLSL---ADCPL 133
Cdd:PRK13752  85 ASSLAEHKLKDVREKMADLARMEAVLSELV-CACHARkgnVSCPL 128
PRK10227 PRK10227
HTH-type transcriptional regulator CueR;
13-133 2.96e-07

HTH-type transcriptional regulator CueR;


Pssm-ID: 182320  Cd Length: 135  Bit Score: 46.95  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEq 91
Cdd:PRK10227   1 MNISDVAKITGLTSKAIRFYEEKGLVTpPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLFNDPQRHSAD- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727169525  92 wgvlssAWRKTLD-----ER-IQRLTVLRDHL----DSCIGCGClslADCPL 133
Cdd:PRK10227  80 ------VKRRTLEkvaeiERhIEELQSMRDQLlalaNACPGDDS---ADCPI 122
HTH_BltR cd04782
Helix-Turn-Helix DNA binding domain of the BltR transcription regulator; Helix-turn-helix (HTH) ...
 13-110 4.00e-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: 45.68  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSV----VLRYIAVIKiaqRAGIPLEEIRAALsrfpigSKLT 88
Cdd:cd04782    1 FTTGEFAKLCGISKQTLFHYDKIGLFKPEIVKENGYRYYTLeqfeQLDIILLLK---ELGISLKEIKDYL------DNRN 71

                         90       100
                 ....*....|....*....|..
gi 727169525  89 SEQWGVLSSAWRKTLDERIQRL 110
Cdd:cd04782   72 PDELIELLKKQEKEIKEEIEEL 93
zntR PRK09514
Zn(2+)-responsive transcriptional regulator;
15-124 4.13e-07

Zn(2+)-responsive transcriptional regulator;


Pssm-ID: 181924 [Multi-domain]  Cd Length: 140  Bit Score: 46.50  E-value: 4.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQ-ATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALSRFPIGSKLTSEQWG 93
Cdd:PRK09514   4 IGELAKLAEVTPDTLRFYEKQGLMDpEVRTEGGYRLYTEQDLQRLRFIRRAKQLGFTLEEIRELLSIRLDPEHHTCQEVK 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 727169525  94 VLSSAWRKTLDERIQRLTVLRDHL----DSCigCG 124
Cdd:PRK09514  84 GIVDEKLAEVEAKIAELQHMRRSLqrlnDAC--CG 116
HTH_YfmP cd04774
Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) ...
 13-82 5.09e-07

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: 45.20  E-value: 5.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSV-VLRYIAVIKIAQRAGIPLEEIRAALSRFP 82
Cdd:cd04774    1 YKVDEVAKRLGLTKRTLKYYEEIGLVSPERSEGRYRLYSEEdLKRLERILRLREVLGFSLQEVTHFLERPL 71
HTH_MerR-like_sg5 cd04780
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 15-79 7.91e-07

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: 44.63  E-value: 7.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQA-TRNAGNQRRYPSVVLRYIAVIKIAQR-AGIPLEEIRAALS 79
Cdd:cd04780    3 MSELSKRSGVSVATIKYYLREGLLPEgRRLAPNQAEYSEAHVERLRLIRALQQeGGLPISQIKEVLD 69
HTH_MerR-like_sg4 cd04779
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ...
 15-118 7.55e-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 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: 42.88  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169525  15 VGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRAALS-RFPIgskltseqwg 93
Cdd:cd04779    3 IGQLAHLAGVSKRTIDYYTNLGLLTPERSDSNYRYYDETALDRLQLIEHLKGQRLSLAEIKDQLEeVQRS---------- 72

                         90       100
                 ....*....|....*....|....*
gi 727169525  94 vlssawRKTLDERIQRLTVLRDHLD 118
Cdd:cd04779   73 ------DKEQREVAQEVQLVCDQID 91
HTH_MerR-trunc cd04762
Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family ...
 13-51 3.55e-05

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


Pssm-ID: 133390 [Multi-domain]  Cd Length: 49  Bit Score: 39.10  E-value: 3.55e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYP 51
Cdd:cd04762    1 LTTKEAAELLGVSPSTLRRWVKEGKLKAIRTPGGHRRFP 39
HTH_GlnR-like cd01105
Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix ...
 12-75 1.19e-04

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: 38.75  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169525  12 LLTVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRR--YPSVVLRyIAVIKIAQRAGIPLEEIR 75
Cdd:cd01105    1 VIGIGEVSKLTGVSPRQLRYWEEKGLIKSIRSDGGGQRkySLADVDR-LLVIKELLDEGFTLAAAV 65
HTH_MlrA-CarA cd01104
Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; ...
 13-76 1.53e-04

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: 37.99  E-value: 1.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169525  13 LTVGEVAKRSGVAISALHFYESK-GLIQATRNAGNQRRYPSVVLRYIAVIKIAQRAGIPLEEIRA 76
Cdd:cd01104    1 YTIGAVARLTGVSPDTLRAWERRyGLPAPQRTDGGHRLYSEADVARLRLIRRLTSEGVRISQAAA 65
HTH_GnyR cd04776
Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR; Putative helix-turn-helix ...
 13-75 1.63e-04

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: 39.05  E-value: 1.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727169525  13 LTVGEVAKRSGVAISALHFYESKGLIQATRNaGNQRRY-PSVVLRyIAVIKIAQRAGIPLEEIR 75
Cdd:cd04776    1 YTISELAREFDVTPRTLRFYEDKGLLSPERR-GQTRVYsRRDRAR-LKLILRGKRLGFSLEEIR 62
HTH_HspR cd04766
Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) ...
 14-75 7.68e-03

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: 33.78  E-value: 7.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169525  14 TVGEVAKRSGVAISALHFYESKGLIQATRNAGNQRRYPSvvlRYIAVIKIAQR----AGIPLEEIR 75
Cdd:cd04766    3 VISVAAELSGMHPQTLRLYERLGLLSPSRTDGGTRRYSE---RDIERLRRIQRltqeLGVNLAGVK 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH