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Conserved domains on  [gi|1307845990|gb|AUD69671|]
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Transcription antiterminator BglG family [Bifidobacterium breve]

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
 1-277 2.53e-35

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 128.67  E-value: 2.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990   1 MEILRVFNNNVVLA-KDRGREVILTGRGLGFKAKPGMTVDDAKVARVFVPAQGRDPDHMAQLLGDIPPEII----RLISE 75
Cdd:PRK09772    3 MQITKILNNNVVVViDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMatcdRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990  76 TMDEVGlsseaAQSSTLVMALADHVCGALRRAKNGIPpVPYPLNSEIRSLYKREYQQGCALLAALNRRLDDALdPSESVA 155
Cdd:PRK09772   83 AQERLG-----KLQDSIYISLTDHCQFAIKRFQQNVL-LPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQL-PKDEVG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 156 F-ALHFVNAGFStGDLSPTYMMTGVIQQLLAVIESTYNIKLDEHSVNVGRFITHLRYLFVRIHQHEQLSREPDAIVSSIM 234
Cdd:PRK09772  156 FiAMHLVSAQMS-GNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1307845990 235 SSYAKASKCARLIASLIELRLDTTLTEDEVAYLTLHVARVTDQ 277
Cdd:PRK09772  235 QNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-277 2.53e-35

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 128.67  E-value: 2.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990   1 MEILRVFNNNVVLA-KDRGREVILTGRGLGFKAKPGMTVDDAKVARVFVPAQGRDPDHMAQLLGDIPPEII----RLISE 75
Cdd:PRK09772    3 MQITKILNNNVVVViDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMatcdRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990  76 TMDEVGlsseaAQSSTLVMALADHVCGALRRAKNGIPpVPYPLNSEIRSLYKREYQQGCALLAALNRRLDDALdPSESVA 155
Cdd:PRK09772   83 AQERLG-----KLQDSIYISLTDHCQFAIKRFQQNVL-LPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQL-PKDEVG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 156 F-ALHFVNAGFStGDLSPTYMMTGVIQQLLAVIESTYNIKLDEHSVNVGRFITHLRYLFVRIHQHEQLSREPDAIVSSIM 234
Cdd:PRK09772  156 FiAMHLVSAQMS-GNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1307845990 235 SSYAKASKCARLIASLIELRLDTTLTEDEVAYLTLHVARVTDQ 277
Cdd:PRK09772  235 QNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
61-283 2.37e-33

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 128.44  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990  61 LLGDIPPEIIRLISETMDEVGLSSEAAQSSTLVMALADHVCGALRRAKNGIP-PVPYPLNSEIRSlyKREYQQGCALLAA 139
Cdd:COG3711   170 LLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYiKLDNPLLWEIKK--PKEYEIAKEILKL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 140 LNRRLDDALDPSESVAFALHFVNAGFSTGDLSP---TYMMTGVIQQLLAVIESTYNIKLDEHSVNVGRFITHLRYLFVRI 216
Cdd:COG3711   248 IEERLGISLPEDEIGYIALHLLGARLNNDNELSeiiTLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRL 327

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307845990 217 HQHEQLsREPdaIVSSIMSSYAKASKCARLIASLIELRLDTTLTEDEVAYLTLHVARVTDQTNQNRS 283
Cdd:COG3711   328 KYGIPI-RNP--LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESKK 391
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 7.51e-20

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: 80.98  E-value: 7.51e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307845990    1 MEILRVFNNNVVLAKDR-GREVILTGRGLGFKAKPGMTVDDAKVARVFVPAQGRD 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDEnGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-49 2.29e-18

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: 77.08  E-value: 2.29e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1307845990   2 EILRVFNNNVVLAKD-RGREVILTGRGLGFKAKPGMTVDDAKVARVFVP 49
Cdd:pfam03123   1 KIKKVLNNNVVLAKDdNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVL 49
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-277 2.53e-35

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 128.67  E-value: 2.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990   1 MEILRVFNNNVVLA-KDRGREVILTGRGLGFKAKPGMTVDDAKVARVFVPAQGRDPDHMAQLLGDIPPEII----RLISE 75
Cdd:PRK09772    3 MQITKILNNNVVVViDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMatcdRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990  76 TMDEVGlsseaAQSSTLVMALADHVCGALRRAKNGIPpVPYPLNSEIRSLYKREYQQGCALLAALNRRLDDALdPSESVA 155
Cdd:PRK09772   83 AQERLG-----KLQDSIYISLTDHCQFAIKRFQQNVL-LPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQL-PKDEVG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 156 F-ALHFVNAGFStGDLSPTYMMTGVIQQLLAVIESTYNIKLDEHSVNVGRFITHLRYLFVRIHQHEQLSREPDAIVSSIM 234
Cdd:PRK09772  156 FiAMHLVSAQMS-GNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1307845990 235 SSYAKASKCARLIASLIELRLDTTLTEDEVAYLTLHVARVTDQ 277
Cdd:PRK09772  235 QNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
61-283 2.37e-33

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 128.44  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990  61 LLGDIPPEIIRLISETMDEVGLSSEAAQSSTLVMALADHVCGALRRAKNGIP-PVPYPLNSEIRSlyKREYQQGCALLAA 139
Cdd:COG3711   170 LLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYiKLDNPLLWEIKK--PKEYEIAKEILKL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 140 LNRRLDDALDPSESVAFALHFVNAGFSTGDLSP---TYMMTGVIQQLLAVIESTYNIKLDEHSVNVGRFITHLRYLFVRI 216
Cdd:COG3711   248 IEERLGISLPEDEIGYIALHLLGARLNNDNELSeiiTLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRL 327

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307845990 217 HQHEQLsREPdaIVSSIMSSYAKASKCARLIASLIELRLDTTLTEDEVAYLTLHVARVTDQTNQNRS 283
Cdd:COG3711   328 KYGIPI-RNP--LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESKK 391
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 7.51e-20

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: 80.98  E-value: 7.51e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307845990    1 MEILRVFNNNVVLAKDR-GREVILTGRGLGFKAKPGMTVDDAKVARVFVPAQGRD 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDEnGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-49 2.29e-18

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: 77.08  E-value: 2.29e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1307845990   2 EILRVFNNNVVLAKD-RGREVILTGRGLGFKAKPGMTVDDAKVARVFVP 49
Cdd:pfam03123   1 KIKKVLNNNVVLAKDdNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVL 49
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 181-273 1.25e-14

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: 68.05  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 181 QQLLAVIESTYNIKLDEHSVnVGRFITHLRYLFVRIHQHEQLSREpdaIVSSIMSSYAKASKCARLIASLIELRLDTTLT 260
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIL-YIRLILHLAFAIERIKEGITIENP---LLEEIKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|...
gi 1307845990 261 EDEVAYLTLHVAR 273
Cdd:pfam00874  77 EDEIGYIALHFLS 89
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 88-163 9.19e-08

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: 48.79  E-value: 9.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1307845990  88 QSSTLVMALADHVCGALRRAKNGIPpVPYPLNSEIRSLYKREYQQGCALLAALNRRLDDALDPSESVAFALHFVNA 163
Cdd:pfam00874  16 DDDILYIRLILHLAFAIERIKEGIT-IENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGYIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
179-269 1.78e-07

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 52.43  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307845990 179 VIQQLLAVIESTYNIKLDEHSVNVgrFITHLRYLFVRIHQHEQLSREpdaIVSSIMSSYAKASKCARLIASLIELRLDTT 258
Cdd:COG3933   460 VVEEILELAEKKLGRKFSENFIYA--LSLHLSSFIERIKEGKEIINP---NLNEIKKKYPKEFKVAKEIKELIEQELDIE 534

                          90
                  ....*....|.
gi 1307845990 259 LTEDEVAYLTL 269
Cdd:COG3933   535 IPEDEVGFLTL 545
 
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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