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Conserved domains on  [gi|912774235|ref|WP_050267878|]
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MULTISPECIES: MerR family transcriptional regulator [Bacilli]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_MerR-SF super family cl02600
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 13-73 1.02e-10

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.


The actual alignment was detected with superfamily member cd04764:

Pssm-ID: 470628  Cd Length: 67  Bit Score: 55.03  E-value: 1.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912774235  13 VADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQaQKWSYDQVRSW 73
Cdd:cd04764    6 VSEIIGVKPHTLRYYEKEFNLYIPRTENGRRYYTDEDIELLKKIKTLLE-KGLSIKEIKEI 65
racA super family cl26654
chromosome-anchoring protein RacA;
11-185 1.79e-03

chromosome-anchoring protein RacA;


The actual alignment was detected with superfamily member PRK13182:

Pssm-ID: 237292 [Multi-domain]  Cd Length: 175  Bit Score: 37.34  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912774235  11 KIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQAQKWSYDQVRSWRNGELDLFVSKEEKSEL 90
Cdd:PRK13182   4 PFVAKKLGVSPKTVQRWVKQLNLPCEKNEYGHYIFTEEDLQLLEYVKSQIEEGQNMQDTQKPSSNDVEETQVNTIVQNIS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912774235  91 EKKLNEVLENQQLQNQFNQALVQKLQEITNELVTTK--EHLANTEKKLTEVEGKNSELEvFIEKKLEKRDQLLLENirdm 168
Cdd:PRK13182  84 SVDFEQLEAQLNTITRRLDELERQLQQKADDVVSYQllQHRREMEEMLERLQKLEARLK-KLEPIYITPDTEPTYE---- 158

                        170
                 ....*....|....*..
gi 912774235 169 qAQNQKQKRKGFFGLFK 185
Cdd:PRK13182 159 -REKKPKRRKMIFSIFG 174
 
Name Accession Description Interval E-value
HTH_MlrA-like_sg1 cd04764
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ...
 13-73 1.02e-10

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: 55.03  E-value: 1.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912774235  13 VADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQaQKWSYDQVRSW 73
Cdd:cd04764    6 VSEIIGVKPHTLRYYEKEFNLYIPRTENGRRYYTDEDIELLKKIKTLLE-KGLSIKEIKEI 65
MerR_1 pfam13411
MerR HTH family regulatory protein;
13-58 1.39e-08

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 49.48  E-value: 1.39e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 912774235   13 VADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKE 58
Cdd:pfam13411   6 LARLLGVTPRTLRYWEREGLLPPPRTERGRRYYTDEDVERLRLIKA 51
COG2452 COG2452
Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];
9-69 2.88e-05

Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];


Pssm-ID: 441988 [Multi-domain]  Cd Length: 178  Bit Score: 42.67  E-value: 2.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912774235   9 TPKIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAiKEKIQAQKWSYDQ 69
Cdd:COG2452    2 TPGEAAELLGVSPKTLRRWEKEGKLPAIRTPGGHRRYPESEVERLER-RTVIYARVSSADQ 61
HTH_BldC NF033787
BldC family transcriptional regulator; BldC, a helix-turn-helix transcription factor with ...
 9-53 1.36e-04

BldC family transcriptional regulator; BldC, a helix-turn-helix transcription factor with homology to the mercury resistance transcriptional regulator MerR, is a DNA-binding protein. It is considered the founding member of a subfamily of regulators with an asymmetric head-to-tail oligomerization for cooperative DNA binding, rather than classic dimerization.


Pssm-ID: 411367  Cd Length: 49  Bit Score: 38.00  E-value: 1.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 912774235   9 TPKIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEEL 53
Cdd:NF033787   4 TPAEVAALFRVDPKTVTRWAKAGKLTSIRTLGGHRRYRESEVRAL 48
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
9-57 1.48e-03

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 35.96  E-value: 1.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 912774235     9 TPKIVADLLGITPDLLKVWSNEFNIQ-TERSQGGHRRYSKENIEELKAIK 57
Cdd:smart00422   2 TIGEVAKLAGVSVRTLRYYERIGLLPpPIRTEGGYRLYSDEDLERLRFIK 51
racA PRK13182
chromosome-anchoring protein RacA;
11-185 1.79e-03

chromosome-anchoring protein RacA;


Pssm-ID: 237292 [Multi-domain]  Cd Length: 175  Bit Score: 37.34  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912774235  11 KIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQAQKWSYDQVRSWRNGELDLFVSKEEKSEL 90
Cdd:PRK13182   4 PFVAKKLGVSPKTVQRWVKQLNLPCEKNEYGHYIFTEEDLQLLEYVKSQIEEGQNMQDTQKPSSNDVEETQVNTIVQNIS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912774235  91 EKKLNEVLENQQLQNQFNQALVQKLQEITNELVTTK--EHLANTEKKLTEVEGKNSELEvFIEKKLEKRDQLLLENirdm 168
Cdd:PRK13182  84 SVDFEQLEAQLNTITRRLDELERQLQQKADDVVSYQllQHRREMEEMLERLQKLEARLK-KLEPIYITPDTEPTYE---- 158

                        170
                 ....*....|....*..
gi 912774235 169 qAQNQKQKRKGFFGLFK 185
Cdd:PRK13182 159 -REKKPKRRKMIFSIFG 174
 
Name Accession Description Interval E-value
HTH_MlrA-like_sg1 cd04764
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ...
 13-73 1.02e-10

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: 55.03  E-value: 1.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912774235  13 VADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQaQKWSYDQVRSW 73
Cdd:cd04764    6 VSEIIGVKPHTLRYYEKEFNLYIPRTENGRRYYTDEDIELLKKIKTLLE-KGLSIKEIKEI 65
HTH_MlrA-CarA cd01104
Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; ...
 11-62 4.68e-10

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: 53.40  E-value: 4.68e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 912774235  11 KIVADLLGITPDLLKVWSNEFNI-QTERSQGGHRRYSKENIEELKAIKEKIQA 62
Cdd:cd01104    4 GAVARLTGVSPDTLRAWERRYGLpAPQRTDGGHRLYSEADVARLRLIRRLTSE 56
HTH_MerR-trunc cd04762
Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family ...
 9-56 1.16e-09

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: 51.82  E-value: 1.16e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 912774235   9 TPKIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAI 56
Cdd:cd04762    2 TTKEAAELLGVSPSTLRRWVKEGKLKAIRTPGGHRRFPEEDLERLLGI 49
HTH_MerR-SF cd04761
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
 9-56 1.99e-09

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: 51.05  E-value: 1.99e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 912774235   9 TPKIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAI 56
Cdd:cd04761    2 TIGELAKLTGVSPSTLRYYERIGLLSPARTEGGYRLYSDADLERLRLI 49
MerR_1 pfam13411
MerR HTH family regulatory protein;
13-58 1.39e-08

MerR HTH family regulatory protein;


Pssm-ID: 463870  Cd Length: 66  Bit Score: 49.48  E-value: 1.39e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 912774235   13 VADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKE 58
Cdd:pfam13411   6 LARLLGVTPRTLRYWEREGLLPPPRTERGRRYYTDEDVERLRLIKA 51
HTH_HspR-like cd01279
Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix ...
 12-63 8.14e-06

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: 42.58  E-value: 8.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 912774235  12 IVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQAQ 63
Cdd:cd01279    6 VAAELLGIHPQTLRVYDRLGLVSPARTNGGGRRYSNNDLELLRQVQRLSQDE 57
COG2452 COG2452
Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];
9-69 2.88e-05

Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];


Pssm-ID: 441988 [Multi-domain]  Cd Length: 178  Bit Score: 42.67  E-value: 2.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 912774235   9 TPKIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAiKEKIQAQKWSYDQ 69
Cdd:COG2452    2 TPGEAAELLGVSPKTLRRWEKEGKLPAIRTPGGHRRYPESEVERLER-RTVIYARVSSADQ 61
SoxR COG0789
DNA-binding transcriptional regulator, MerR family [Transcription];
13-57 7.54e-05

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


Pssm-ID: 440552 [Multi-domain]  Cd Length: 100  Bit Score: 39.89  E-value: 7.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 912774235  13 VADLLGITPDLLKVWSNEFNIQ-TERSQGGHRRYSKENIEELKAIK 57
Cdd:COG0789    4 VARLTGVSVRTLRYYERIGLLPpPERTEGGYRLYSEEDVERLRFIR 49
HTH_MlrA-like_sg2 cd04765
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ...
 13-58 7.80e-05

Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.


Pssm-ID: 133393  Cd Length: 99  Bit Score: 39.93  E-value: 7.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 912774235  13 VADLLGITPDLLKVWSNEFN-IQTERSQGGHRRYSKENIEELKAIKE 58
Cdd:cd04765    6 VAEILGLPPHVLRYWETEFPqLKPVKRAGGRRYYRPKDVELLLLIKH 52
HTH_MerR-like cd00592
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ...
 13-57 9.68e-05

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: 39.92  E-value: 9.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 912774235  13 VADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIK 57
Cdd:cd00592    6 VAKLLGVSVRTLRYYEEKGLLPPERSENGYRLYSEEDLERLRLIR 50
HTH_BldC NF033787
BldC family transcriptional regulator; BldC, a helix-turn-helix transcription factor with ...
 9-53 1.36e-04

BldC family transcriptional regulator; BldC, a helix-turn-helix transcription factor with homology to the mercury resistance transcriptional regulator MerR, is a DNA-binding protein. It is considered the founding member of a subfamily of regulators with an asymmetric head-to-tail oligomerization for cooperative DNA binding, rather than classic dimerization.


Pssm-ID: 411367  Cd Length: 49  Bit Score: 38.00  E-value: 1.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 912774235   9 TPKIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEEL 53
Cdd:NF033787   4 TPAEVAALFRVDPKTVTRWAKAGKLTSIRTLGGHRRYRESEVRAL 48
HTH_MlrA-like cd04763
Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix ...
 13-57 1.39e-04

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: 38.67  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 912774235  13 VADLLGITPDLLKVWSNEFN-IQTERSQGGHRRYSKENIEELKAIK 57
Cdd:cd04763    6 VALLTGIKPHVLRAWEREFGlLKPQRSDGGHRLFNDADIDRILEIK 51
HTH_HspR-like_MBC cd04767
Helix-Turn-Helix DNA binding domain of putative HspR-like transcription regulators; Putative ...
 12-57 7.67e-04

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


Pssm-ID: 133395  Cd Length: 120  Bit Score: 37.86  E-value: 7.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 912774235  12 IVADLLGITPDLLKVWSNEFNIQTERsQGGHRRYSKENIEELKAIK 57
Cdd:cd04767    6 VVAELLNIHPETLRIWERHGLIKPAR-RNGQRLYSNNDLKRLRFIK 50
HTH_MERR smart00422
helix_turn_helix, mercury resistance;
9-57 1.48e-03

helix_turn_helix, mercury resistance;


Pssm-ID: 197716  Cd Length: 70  Bit Score: 35.96  E-value: 1.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 912774235     9 TPKIVADLLGITPDLLKVWSNEFNIQ-TERSQGGHRRYSKENIEELKAIK 57
Cdd:smart00422   2 TIGEVAKLAGVSVRTLRYYERIGLLPpPIRTEGGYRLYSDEDLERLRFIK 51
racA PRK13182
chromosome-anchoring protein RacA;
11-185 1.79e-03

chromosome-anchoring protein RacA;


Pssm-ID: 237292 [Multi-domain]  Cd Length: 175  Bit Score: 37.34  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912774235  11 KIVADLLGITPDLLKVWSNEFNIQTERSQGGHRRYSKENIEELKAIKEKIQAQKWSYDQVRSWRNGELDLFVSKEEKSEL 90
Cdd:PRK13182   4 PFVAKKLGVSPKTVQRWVKQLNLPCEKNEYGHYIFTEEDLQLLEYVKSQIEEGQNMQDTQKPSSNDVEETQVNTIVQNIS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 912774235  91 EKKLNEVLENQQLQNQFNQALVQKLQEITNELVTTK--EHLANTEKKLTEVEGKNSELEvFIEKKLEKRDQLLLENirdm 168
Cdd:PRK13182  84 SVDFEQLEAQLNTITRRLDELERQLQQKADDVVSYQllQHRREMEEMLERLQKLEARLK-KLEPIYITPDTEPTYE---- 158

                        170
                 ....*....|....*..
gi 912774235 169 qAQNQKQKRKGFFGLFK 185
Cdd:PRK13182 159 -REKKPKRRKMIFSIFG 174
HTH_GlnR-like cd01105
Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix ...
 11-61 6.30e-03

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: 34.51  E-value: 6.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 912774235  11 KIVADLLGITPDLLKVWSNEFNIQTERS-QGGHRRYSKENIEELKAIKEKIQ 61
Cdd:cd01105    5 GEVSKLTGVSPRQLRYWEEKGLIKSIRSdGGGQRKYSLADVDRLLVIKELLD 56
 
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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