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Conserved domains on  [gi|520914460|ref|WP_020333853|]
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PRD domain-containing protein [Vibrio natriegens]

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

CATH:  1.10.1790.10
Gene Ontology:  GO:0045893|GO:0003723

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09772 super family cl31605
transcriptional antiterminator BglG; Provisional
4-274 3.06e-50

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 166.81  E-value: 3.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460   4 IIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLNQGDATSeRLKVLMESLPLEVVEITEFICNEA 83
Cdd:PRK09772   5 ITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNG-RLSELLSHIPLEVMATCDRIISLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  84 EKSLNKkFGNGLFVSLSDHLDFAIKRSKDGLSIPNPFEWEIRSFYDQEFKFAEGIIQKILLNWGVLLERSEACSIALHII 163
Cdd:PRK09772  84 QERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460 164 NADNS-NLNDFKSLTKIVYQILNIVKYVFNVELDENSPNYHRFVTHLKFFAQRIGKKEVITNHDSLLSDLLIKELTKTHQ 242
Cdd:PRK09772 163 SAQMSgNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 520914460 243 CVDTISEFVRKTYDHPMSDSEKLYLVIHIDRV 274
Cdd:PRK09772 243 CAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
4-274 3.06e-50

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 166.81  E-value: 3.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460   4 IIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLNQGDATSeRLKVLMESLPLEVVEITEFICNEA 83
Cdd:PRK09772   5 ITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNG-RLSELLSHIPLEVMATCDRIISLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  84 EKSLNKkFGNGLFVSLSDHLDFAIKRSKDGLSIPNPFEWEIRSFYDQEFKFAEGIIQKILLNWGVLLERSEACSIALHII 163
Cdd:PRK09772  84 QERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460 164 NADNS-NLNDFKSLTKIVYQILNIVKYVFNVELDENSPNYHRFVTHLKFFAQRIGKKEVITNHDSLLSDLLIKELTKTHQ 242
Cdd:PRK09772 163 SAQMSgNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 520914460 243 CVDTISEFVRKTYDHPMSDSEKLYLVIHIDRV 274
Cdd:PRK09772 243 CAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
63-276 1.17e-34

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 131.52  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  63 VLMESLPLEVVEITEFICNEAEKSLNKKFGNGLFVSLSDHLDFAIKRSKDGLSI--PNPFEWEIRSfyDQEFKFAEGIIQ 140
Cdd:COG3711  169 LLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIklDNPLLWEIKK--PKEYEIAKEILK 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460 141 KILLNWGVLLERSEACSIALHIINADNSNLNDFKS-----LTKIVYQILNIVKYVFNVELDENSPNYHRFVTHLKFFAQR 215
Cdd:COG3711  247 LIEERLGISLPEDEIGYIALHLLGARLNNDNELSEiitleITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINR 326
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520914460 216 IGKKEVITNHdslLSDLLIKELTKTHQCVDTISEFVRKTYDHPMSDSEKLYLVIHIDRVLN 276
Cdd:COG3711  327 LKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
3-52 8.56e-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: 72.46  E-value: 8.56e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 520914460    3 TIIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLN 52
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLK 50
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
2-55 7.62e-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: 69.81  E-value: 7.62e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 520914460     2 FTIIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLNQGD 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
4-274 3.06e-50

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 166.81  E-value: 3.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460   4 IIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLNQGDATSeRLKVLMESLPLEVVEITEFICNEA 83
Cdd:PRK09772   5 ITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNG-RLSELLSHIPLEVMATCDRIISLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  84 EKSLNKkFGNGLFVSLSDHLDFAIKRSKDGLSIPNPFEWEIRSFYDQEFKFAEGIIQKILLNWGVLLERSEACSIALHII 163
Cdd:PRK09772  84 QERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460 164 NADNS-NLNDFKSLTKIVYQILNIVKYVFNVELDENSPNYHRFVTHLKFFAQRIGKKEVITNHDSLLSDLLIKELTKTHQ 242
Cdd:PRK09772 163 SAQMSgNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 520914460 243 CVDTISEFVRKTYDHPMSDSEKLYLVIHIDRV 274
Cdd:PRK09772 243 CAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
63-276 1.17e-34

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 131.52  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  63 VLMESLPLEVVEITEFICNEAEKSLNKKFGNGLFVSLSDHLDFAIKRSKDGLSI--PNPFEWEIRSfyDQEFKFAEGIIQ 140
Cdd:COG3711  169 LLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIklDNPLLWEIKK--PKEYEIAKEILK 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460 141 KILLNWGVLLERSEACSIALHIINADNSNLNDFKS-----LTKIVYQILNIVKYVFNVELDENSPNYHRFVTHLKFFAQR 215
Cdd:COG3711  247 LIEERLGISLPEDEIGYIALHLLGARLNNDNELSEiitleITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINR 326
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520914460 216 IGKKEVITNHdslLSDLLIKELTKTHQCVDTISEFVRKTYDHPMSDSEKLYLVIHIDRVLN 276
Cdd:COG3711  327 LKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
3-52 8.56e-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: 72.46  E-value: 8.56e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 520914460    3 TIIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLN 52
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLK 50
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
2-55 7.62e-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: 69.81  E-value: 7.62e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 520914460     2 FTIIQVLNNNVVSAADEKGQELILTGKGLGFKALPGGEIDPSVAEKVFRLNQGD 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
79-165 1.40e-12

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: 62.27  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460   79 ICNEAEKSLNKKFGN-GLFVSLSDHLDFAIKRSKDGLSIPNPFEWEIRSFYDQEFKFAEGIIQKILLNWGVLLERSEACS 157
Cdd:pfam00874   3 IIELIEKKLGITFDDdILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGY 82

                  ....*...
gi 520914460  158 IALHIINA 165
Cdd:pfam00874  83 IALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
182-271 3.08e-10

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: 55.72  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  182 QILNIVKYVFNVELDENSpNYHRFVTHLKFFAQRIgkKEVITNHDSLLSDLlIKELTKTHQCVDTISEFVRKTYDHPMSD 261
Cdd:pfam00874   2 EIIELIEKKLGITFDDDI-LYIRLILHLAFAIERI--KEGITIENPLLEEI-KEKYPKEFEIAKKILEILEEELGIELPE 77
                          90
                  ....*....|
gi 520914460  262 SEKLYLVIHI 271
Cdd:pfam00874  78 DEIGYIALHF 87
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
39-142 2.40e-07

Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 51.66  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520914460  39 EIDPSVAEKVFRLNqgDATSERLKVLMESLPLEVVEITEFICNEAEKSLNKKFGNGLFVSLSDHLDFAIKRSKDGLSIPN 118
Cdd:COG3933  426 EIDIDVHLLKFIYD--DNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIIN 503
                         90       100
                 ....*....|....*....|....
gi 520914460 119 PFEWEIRSFYDQEFKFAEGIIQKI 142
Cdd:COG3933  504 PNLNEIKKKYPKEFKVAKEIKELI 527
 
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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