PRD domain-containing protein [Clostridioides difficile]
Protein Classification
Bg1G family transcriptional antiterminator( domain architecture ID 1004078)
Bg1G family transcriptional antiterminator similar to Dickeya chrysanthemi beta-glucoside operon antiterminator that mediates the positive regulation of the beta-glucoside (arb) operon by functioning as a transcriptional antiterminator
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK09772 super family | cl31605 | transcriptional antiterminator BglG; Provisional |
1-277 | 1.57e-45 | |||||
transcriptional antiterminator BglG; Provisional The actual alignment was detected with superfamily member PRK09772: Pssm-ID: 170086 [Multi-domain] Cd Length: 278 Bit Score: 154.86 E-value: 1.57e-45
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| Name | Accession | Description | Interval | E-value | |||||
| PRK09772 | PRK09772 | transcriptional antiterminator BglG; Provisional |
1-277 | 1.57e-45 | |||||
transcriptional antiterminator BglG; Provisional Pssm-ID: 170086 [Multi-domain] Cd Length: 278 Bit Score: 154.86 E-value: 1.57e-45
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| BglG | COG3711 | Transcriptional antiterminator [Transcription]; |
47-282 | 2.61e-32 | |||||
Transcriptional antiterminator [Transcription]; Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 125.36 E-value: 2.61e-32
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| CAT_RBD | pfam03123 | CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ... |
2-56 | 4.21e-17 | |||||
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (pfam00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template. Pssm-ID: 460815 Cd Length: 56 Bit Score: 73.62 E-value: 4.21e-17
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| CAT_RBD | smart01061 | CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ... |
1-54 | 3.23e-16 | |||||
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer.to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template. Pssm-ID: 215004 Cd Length: 55 Bit Score: 70.97 E-value: 3.23e-16
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| Name | Accession | Description | Interval | E-value | |||||
| PRK09772 | PRK09772 | transcriptional antiterminator BglG; Provisional |
1-277 | 1.57e-45 | |||||
transcriptional antiterminator BglG; Provisional Pssm-ID: 170086 [Multi-domain] Cd Length: 278 Bit Score: 154.86 E-value: 1.57e-45
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| BglG | COG3711 | Transcriptional antiterminator [Transcription]; |
47-282 | 2.61e-32 | |||||
Transcriptional antiterminator [Transcription]; Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 125.36 E-value: 2.61e-32
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| CAT_RBD | pfam03123 | CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ... |
2-56 | 4.21e-17 | |||||
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (pfam00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template. Pssm-ID: 460815 Cd Length: 56 Bit Score: 73.62 E-value: 4.21e-17
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| CAT_RBD | smart01061 | CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ... |
1-54 | 3.23e-16 | |||||
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer.to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template. Pssm-ID: 215004 Cd Length: 55 Bit Score: 70.97 E-value: 3.23e-16
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| PRD | pfam00874 | PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
74-161 | 2.13e-11 | |||||
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation. Pssm-ID: 459973 [Multi-domain] Cd Length: 90 Bit Score: 59.19 E-value: 2.13e-11
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| LevR | COG3933 | Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; |
19-174 | 3.43e-10 | |||||
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; Pssm-ID: 443134 [Multi-domain] Cd Length: 916 Bit Score: 60.52 E-value: 3.43e-10
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| PRD | pfam00874 | PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
181-274 | 1.01e-09 | |||||
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation. Pssm-ID: 459973 [Multi-domain] Cd Length: 90 Bit Score: 54.18 E-value: 1.01e-09
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| BglG | COG3711 | Transcriptional antiterminator [Transcription]; |
30-159 | 5.57e-07 | |||||
Transcriptional antiterminator [Transcription]; Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 50.63 E-value: 5.57e-07
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| PspF | COG1221 | Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
38-176 | 2.67e-03 | |||||
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms]; Pssm-ID: 440834 [Multi-domain] Cd Length: 835 Bit Score: 39.32 E-value: 2.67e-03
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| Blast search parameters | ||||
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