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Conserved domains on  [gi|565650238|ref|WP_023897666|]
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BglG family transcription antiterminator LicT [Cronobacter malonaticus]

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 2.86e-113

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 327.43  E-value: 2.86e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238   1 MKIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDELVRRLGELLGQIPLEVMTTCDRIIAL 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  81 AAERLGRLQESLYVTLTDHCHYAIERQKKGLAIKNVLLWEIKRLYPKEYALGQEARAIIARRLSVELPEDEAGFIALHLV 160
Cdd:PRK09772  83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 161 TAQLNSEMPEVMHVTRVMQEILQLVKYQLQLEYDEESLSYQRFVTHLKFFAQRMLTRTVVADDDLSLHSAVKDNYPQAWR 240
Cdd:PRK09772 163 SAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 565650238 241 CAEKISGYLSKSYQRELTAEEMMFLAIHIERVRKE 275
Cdd:PRK09772 243 CAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
1-275 2.86e-113

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 327.43  E-value: 2.86e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238   1 MKIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDELVRRLGELLGQIPLEVMTTCDRIIAL 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  81 AAERLGRLQESLYVTLTDHCHYAIERQKKGLAIKNVLLWEIKRLYPKEYALGQEARAIIARRLSVELPEDEAGFIALHLV 160
Cdd:PRK09772  83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 161 TAQLNSEMPEVMHVTRVMQEILQLVKYQLQLEYDEESLSYQRFVTHLKFFAQRMLTRTVVADDDLSLHSAVKDNYPQAWR 240
Cdd:PRK09772 163 SAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 565650238 241 CAEKISGYLSKSYQRELTAEEMMFLAIHIERVRKE 275
Cdd:PRK09772 243 CAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
35-275 1.53e-49

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 172.74  E-value: 1.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  35 TGDELDATR-IEKVFALQSDELVRRLGELLGQIPLEVMTTCDRIIALAAERLG-RLQESLYVTLTDHCHYAIERQKKGLA 112
Cdd:COG3711  142 EGSELDIRKaLAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGiKLSDSIYINLTDHIAIAIKRIKKGKY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 113 IK--NVLLWEIKRlyPKEYALGQEARAIIARRLSVELPEDEAGFIALHLVTAQLNSEMP----EVMHVTRVMQEILQLVK 186
Cdd:COG3711  222 IKldNPLLWEIKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIE 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 187 YQLQLEYDEESLSYQRFVTHLKFFAQRMLTRTVVADDdlsLHSAVKDNYPQAWRCAEKISGYLSKSYQRELTAEEMMFLA 266
Cdd:COG3711  300 EELGIDLDEDSLLYERLITHLKPAINRLKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLT 376

                 ....*....
gi 565650238 267 IHIERVRKE 275
Cdd:COG3711  377 LHFGAALER 385
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
1-54 4.78e-24

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: 91.77  E-value: 4.78e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 565650238     1 MKIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDE 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
2-54 5.93e-24

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: 91.34  E-value: 5.93e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 565650238    2 KIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDE 54
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 53
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
1-275 2.86e-113

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 327.43  E-value: 2.86e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238   1 MKIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDELVRRLGELLGQIPLEVMTTCDRIIAL 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  81 AAERLGRLQESLYVTLTDHCHYAIERQKKGLAIKNVLLWEIKRLYPKEYALGQEARAIIARRLSVELPEDEAGFIALHLV 160
Cdd:PRK09772  83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 161 TAQLNSEMPEVMHVTRVMQEILQLVKYQLQLEYDEESLSYQRFVTHLKFFAQRMLTRTVVADDDLSLHSAVKDNYPQAWR 240
Cdd:PRK09772 163 SAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQ 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 565650238 241 CAEKISGYLSKSYQRELTAEEMMFLAIHIERVRKE 275
Cdd:PRK09772 243 CAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
35-275 1.53e-49

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 172.74  E-value: 1.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  35 TGDELDATR-IEKVFALQSDELVRRLGELLGQIPLEVMTTCDRIIALAAERLG-RLQESLYVTLTDHCHYAIERQKKGLA 112
Cdd:COG3711  142 EGSELDIRKaLAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGiKLSDSIYINLTDHIAIAIKRIKKGKY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 113 IK--NVLLWEIKRlyPKEYALGQEARAIIARRLSVELPEDEAGFIALHLVTAQLNSEMP----EVMHVTRVMQEILQLVK 186
Cdd:COG3711  222 IKldNPLLWEIKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIE 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238 187 YQLQLEYDEESLSYQRFVTHLKFFAQRMLTRTVVADDdlsLHSAVKDNYPQAWRCAEKISGYLSKSYQRELTAEEMMFLA 266
Cdd:COG3711  300 EELGIDLDEDSLLYERLITHLKPAINRLKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLT 376

                 ....*....
gi 565650238 267 IHIERVRKE 275
Cdd:COG3711  377 LHFGAALER 385
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
1-54 4.78e-24

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: 91.77  E-value: 4.78e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 565650238     1 MKIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDE 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
2-54 5.93e-24

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: 91.34  E-value: 5.93e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 565650238    2 KIAKILNNNAVFVLDAQGREQVVMGRGLAFQKRTGDELDATRIEKVFALQSDE 54
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 53
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
76-162 2.97e-20

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: 82.69  E-value: 2.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238   76 RIIALAAERLGR--LQESLYVTLTDHCHYAIERQKKGLAIKNVLLWEIKRLYPKEYALGQEARAIIARRLSVELPEDEAG 153
Cdd:pfam00874   2 EIIELIEKKLGItfDDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81

                  ....*....
gi 565650238  154 FIALHLVTA 162
Cdd:pfam00874  82 YIALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
179-271 2.07e-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: 67.28  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  179 QEILQLVKYQLQLEYDEESLsYQRFVTHLKFFAQRMLTRTVVADDDLSLhsaVKDNYPQAWRCAEKISGYLSKSYQRELT 258
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIL-YIRLILHLAFAIERIKEGITIENPLLEE---IKEKYPKEFEIAKKILEILEEELGIELP 76
                          90
                  ....*....|...
gi 565650238  259 AEEMMFLAIHIER 271
Cdd:pfam00874  77 EDEIGYIALHFLS 89
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
61-173 4.53e-14

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 72.07  E-value: 4.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  61 ELLGQIPLEVMTTCDRIIALAAERLGR-LQESLYVTLTDHCHYAIERQKKGLAIKNVLLWEIKRLYPKEYALGQEARAII 139
Cdd:COG3933  448 ELAKIVDEDIINVVEEILELAEKKLGRkFSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELI 527
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 565650238 140 ARRLSVELPEDEAGFIALHLVTAQLNSEMPEV-----MH 173
Cdd:COG3933  528 EQELDIEIPEDEVGFLTLFLVSLNENNESGKVgvivlAH 566
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
65-174 1.71e-06

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: 48.95  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565650238  65 QIPLEVMTTCDRIIALAAERLGRLQESLYVTLTDHCHYAIERQKKGLAIKNVLLWEIKRLYPKEYALGQEARAIIARRLS 144
Cdd:COG1221  466 VVDEVIVNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELK 545
                         90       100       110
                 ....*....|....*....|....*....|
gi 565650238 145 VELPEDEAGFIALHLVTAQLNSEMPEVMHV 174
Cdd:COG1221  546 ILIPDEEEGFILLLLIELKEEKSLSENVIV 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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