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Conserved domains on  [gi|2090013040|gb|QZX97911|]
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transcriptional antiterminator BglG (plasmid) [Pantoea alfalfae]

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
 1-275 7.26e-102

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 298.54  E-value: 7.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040   1 MKIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSDLLVRRLEELLHQIPPEVMTTSNCIIDL 80
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  81 AIQRLGKLQESLYITLTDHCFFAIERQKKGLAIKNVLLWDIKRLYPKEFELGQEARAIISRRLNVELPEDEAGFIALHLV 160
Cdd:PRK09772   83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040 161 TAQLNNEMPEVMHVTRVMQEILQLVKYQLRLEYNESSLSYQRFVTHLKFFAQRMLTRTVVDDDDVSLHTAVKDNYPKAWK 240
Cdd:PRK09772  163 SAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2090013040 241 CAVKIAQHLQQSYQRELTAEEIMFLAIHIERVRKE 275
Cdd:PRK09772  243 CAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-275 7.26e-102

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 298.54  E-value: 7.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040   1 MKIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSDLLVRRLEELLHQIPPEVMTTSNCIIDL 80
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  81 AIQRLGKLQESLYITLTDHCFFAIERQKKGLAIKNVLLWDIKRLYPKEFELGQEARAIISRRLNVELPEDEAGFIALHLV 160
Cdd:PRK09772   83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040 161 TAQLNNEMPEVMHVTRVMQEILQLVKYQLRLEYNESSLSYQRFVTHLKFFAQRMLTRTVVDDDDVSLHTAVKDNYPKAWK 240
Cdd:PRK09772  163 SAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2090013040 241 CAVKIAQHLQQSYQRELTAEEIMFLAIHIERVRKE 275
Cdd:PRK09772  243 CAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
44-275 4.10e-49

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 171.58  E-value: 4.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  44 IEKVFAPQSDLLVRRLEELLHQIPPEVMTTSNCIIDLAIQRLG-KLQESLYITLTDHCFFAIERQKKGLAIK--NVLLWD 120
Cdd:COG3711   152 LAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGiKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWE 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040 121 IKRlyPKEFELGQEARAIISRRLNVELPEDEAGFIALHLVTAQLNNEMP----EVMHVTRVMQEILQLVKYQLRLEYNES 196
Cdd:COG3711   232 IKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDED 309

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2090013040 197 SLSYQRFVTHLKFFAQRMLTRTVVDDDdvsLHTAVKDNYPKAWKCAVKIAQHLQQSYQRELTAEEIMFLAIHIERVRKE 275
Cdd:COG3711   310 SLLYERLITHLKPAINRLKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALER 385
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-53 2.73e-22

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: 87.14  E-value: 2.73e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2090013040    1 MKIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSD 53
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDE 53
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-53 2.77e-22

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: 87.10  E-value: 2.77e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2090013040   2 KIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSD 53
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDE 52
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-275 7.26e-102

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 298.54  E-value: 7.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040   1 MKIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSDLLVRRLEELLHQIPPEVMTTSNCIIDL 80
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  81 AIQRLGKLQESLYITLTDHCFFAIERQKKGLAIKNVLLWDIKRLYPKEFELGQEARAIISRRLNVELPEDEAGFIALHLV 160
Cdd:PRK09772   83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040 161 TAQLNNEMPEVMHVTRVMQEILQLVKYQLRLEYNESSLSYQRFVTHLKFFAQRMLTRTVVDDDDVSLHTAVKDNYPKAWK 240
Cdd:PRK09772  163 SAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2090013040 241 CAVKIAQHLQQSYQRELTAEEIMFLAIHIERVRKE 275
Cdd:PRK09772  243 CAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
44-275 4.10e-49

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 171.58  E-value: 4.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  44 IEKVFAPQSDLLVRRLEELLHQIPPEVMTTSNCIIDLAIQRLG-KLQESLYITLTDHCFFAIERQKKGLAIK--NVLLWD 120
Cdd:COG3711   152 LAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGiKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWE 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040 121 IKRlyPKEFELGQEARAIISRRLNVELPEDEAGFIALHLVTAQLNNEMP----EVMHVTRVMQEILQLVKYQLRLEYNES 196
Cdd:COG3711   232 IKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDED 309

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2090013040 197 SLSYQRFVTHLKFFAQRMLTRTVVDDDdvsLHTAVKDNYPKAWKCAVKIAQHLQQSYQRELTAEEIMFLAIHIERVRKE 275
Cdd:COG3711   310 SLLYERLITHLKPAINRLKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALER 385
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-53 2.73e-22

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: 87.14  E-value: 2.73e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2090013040    1 MKIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSD 53
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDE 53
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-53 2.77e-22

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: 87.10  E-value: 2.77e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2090013040   2 KIAKILNNNVVMVQDEQGREQVVMGRGLAFQKRVGDSLNDAQIEKVFAPQSD 53
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDE 52
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 77-162 2.72e-21

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: 85.38  E-value: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  77 IIDLAIQRLGK--LQESLYITLTDHCFFAIERQKKGLAIKNVLLWDIKRLYPKEFELGQEARAIISRRLNVELPEDEAGF 154
Cdd:pfam00874   3 IIELIEKKLGItfDDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGY 82


                  ....*...
gi 2090013040 155 IALHLVTA 162
Cdd:pfam00874  83 IALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 179-271 7.27e-16

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: 71.13  E-value: 7.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040 179 QEILQLVKYQLRLEYNESSLsYQRFVTHLKFFAQRMLTRTVVDDDDVSLhtaVKDNYPKAWKCAVKIAQHLQQSYQRELT 258
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIL-YIRLILHLAFAIERIKEGITIENPLLEE---IKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|...
gi 2090013040 259 AEEIMFLAIHIER 271
Cdd:pfam00874  77 EDEIGYIALHFLS 89
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
38-173 1.33e-13

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 70.53  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  38 SLNDAQIEKVFAPQSDLLVRRLEELLHQIPPEVMTTSNCIIDLAIQRLG-KLQESLYITLTDHCFFAIERQKKGLAIKNV 116
Cdd:COG3933   425 IEIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGrKFSENFIYALSLHLSSFIERIKEGKEIINP 504

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090013040 117 LLWDIKRLYPKEFELGQEARAIISRRLNVELPEDEAGFIALHLVTAQLNNEMPEV-----MH 173
Cdd:COG3933   505 NLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKVgvivlAH 566
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 77-174 7.77e-05

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: 43.94  E-value: 7.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090013040  77 IIDLAIQRLGKLQESLYITLTDHCFFAIERQKKGLAIKNVLLWDIKRLYPKEFELGQEARAIISRRLNVELPEDEAGFIA 156
Cdd:COG1221   478 FEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFIL 557

                          90
                  ....*....|....*...
gi 2090013040 157 LHLVTAQLNNEMPEVMHV 174
Cdd:COG1221   558 LLLIELKEEKSLSENVIV 575
 
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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