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Conserved domains on  [gi|1461657093|ref|WP_116486322|]
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PRD domain-containing protein [Streptococcus parauberis]

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
 3-276 1.62e-28

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 110.18  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093   3 RVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTESQENFMTLLKDVPLDfITVTYDVIETL 82
Cdd:PRK09772    4 QITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLE-VMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  83 SSKYSYPVQEYLYVTLTDHIHCAYKAVlednYQESKLPN-----ISQEYGIEYVIAKEALAMFRQKLLNDLPDDEIGRIA 157
Cdd:PRK09772   83 AQERLGKLQDSIYISLTDHCQFAIKRF----QQNVLLPNpllwdIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 158 LHFINAKGVMAVEKSPKV-DLTRSVLSKVQEELERlgikRTKENSNFYDRLMIHLTYFLQYLDRSPNDNGPLMDMGKHIQ 236
Cdd:PRK09772  159 MHLVSAQMSGNMEDVAGVtQLMREMLQLIKFQFSL----NYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1461657093 237 IAYPEAYDVGEKIYQIIASETGVAIHESEKFYIVLHVQRL 276
Cdd:PRK09772  235 QNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 3-276 1.62e-28

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 110.18  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093   3 RVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTESQENFMTLLKDVPLDfITVTYDVIETL 82
Cdd:PRK09772    4 QITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLE-VMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  83 SSKYSYPVQEYLYVTLTDHIHCAYKAVlednYQESKLPN-----ISQEYGIEYVIAKEALAMFRQKLLNDLPDDEIGRIA 157
Cdd:PRK09772   83 AQERLGKLQDSIYISLTDHCQFAIKRF----QQNVLLPNpllwdIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 158 LHFINAKGVMAVEKSPKV-DLTRSVLSKVQEELERlgikRTKENSNFYDRLMIHLTYFLQYLDRSPNDNGPLMDMGKHIQ 236
Cdd:PRK09772  159 MHLVSAQMSGNMEDVAGVtQLMREMLQLIKFQFSL----NYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1461657093 237 IAYPEAYDVGEKIYQIIASETGVAIHESEKFYIVLHVQRL 276
Cdd:PRK09772  235 QNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
41-277 2.65e-26

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 107.64  E-value: 2.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  41 IADKIEKVFSLKSTESQENFMTLLKDVPLDFITVTYDVIETLSSKYSYPVQEYLYVTLTDHIHCAYKAVLEDNYQESKLP 120
Cdd:COG3711   148 IRKALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 121 NISQ-EYGIEYVIAKEALAMFRQKLLNDLPDDEIGRIALHFINAKGVMAVEKSPKVD-----LTRSVLSKVQEELErlgi 194
Cdd:COG3711   228 LLWEiKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITleitkLIKEIINIIEEELG---- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 195 KRTKENSNFYDRLMIHLTYFLQYLDRSPNDNGPLMDMgkhIQIAYPEAYDVGEKIYQIIASETGVAIHESEKFYIVLHVQ 274
Cdd:COG3711   304 IDLDEDSLLYERLITHLKPAINRLKYGIPIRNPLLEE---IKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFG 380


                  ...
gi 1461657093 275 RLL 277
Cdd:COG3711   381 AAL 383
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 3-58 2.64e-21

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: 84.40  E-value: 2.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1461657093   3 RVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTESQE 58
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 1.22e-19

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: 80.21  E-value: 1.22e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1461657093    2 YRVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTE 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 3-276 1.62e-28

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 110.18  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093   3 RVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTESQENFMTLLKDVPLDfITVTYDVIETL 82
Cdd:PRK09772    4 QITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLE-VMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  83 SSKYSYPVQEYLYVTLTDHIHCAYKAVlednYQESKLPN-----ISQEYGIEYVIAKEALAMFRQKLLNDLPDDEIGRIA 157
Cdd:PRK09772   83 AQERLGKLQDSIYISLTDHCQFAIKRF----QQNVLLPNpllwdIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 158 LHFINAKGVMAVEKSPKV-DLTRSVLSKVQEELERlgikRTKENSNFYDRLMIHLTYFLQYLDRSPNDNGPLMDMGKHIQ 236
Cdd:PRK09772  159 MHLVSAQMSGNMEDVAGVtQLMREMLQLIKFQFSL----NYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1461657093 237 IAYPEAYDVGEKIYQIIASETGVAIHESEKFYIVLHVQRL 276
Cdd:PRK09772  235 QNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
41-277 2.65e-26

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 107.64  E-value: 2.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  41 IADKIEKVFSLKSTESQENFMTLLKDVPLDFITVTYDVIETLSSKYSYPVQEYLYVTLTDHIHCAYKAVLEDNYQESKLP 120
Cdd:COG3711   148 IRKALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 121 NISQ-EYGIEYVIAKEALAMFRQKLLNDLPDDEIGRIALHFINAKGVMAVEKSPKVD-----LTRSVLSKVQEELErlgi 194
Cdd:COG3711   228 LLWEiKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITleitkLIKEIINIIEEELG---- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 195 KRTKENSNFYDRLMIHLTYFLQYLDRSPNDNGPLMDMgkhIQIAYPEAYDVGEKIYQIIASETGVAIHESEKFYIVLHVQ 274
Cdd:COG3711   304 IDLDEDSLLYERLITHLKPAINRLKYGIPIRNPLLEE---IKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFG 380


                  ...
gi 1461657093 275 RLL 277
Cdd:COG3711   381 AAL 383
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 3-58 2.64e-21

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: 84.40  E-value: 2.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1461657093   3 RVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTESQE 58
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 1.22e-19

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: 80.21  E-value: 1.22e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1461657093    2 YRVLQALNNNVALVKDEHDQQFVVMGLGITFQKRKGDLVIADKIEKVFSLKSTE 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 77-163 7.69e-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: 54.57  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  77 DVIETLSSKYSYPVQ-EYLYVTLTDHIHCAYKAVLE-DNYQESKLPNISQEYGIEYVIAKEALAMFRQKLLNDLPDDEIG 154
Cdd:pfam00874   2 EIIELIEKKLGITFDdDILYIRLILHLAFAIERIKEgITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 1461657093 155 RIALHFINA 163
Cdd:pfam00874  82 YIALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 199-276 1.46e-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: 53.80  E-value: 1.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1461657093 199 ENSNFYDRLMIHLTYFLQYLDRSPNDNGPLMDmgkHIQIAYPEAYDVGEKIYQIIASETGVAIHESEKFYIVLHVQRL 276
Cdd:pfam00874  16 DDDILYIRLILHLAFAIERIKEGITIENPLLE---EIKEKYPKEFEIAKKILEILEEELGIELPEDEIGYIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
39-164 3.41e-04

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 42.03  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  39 LVIADKIEKVFSLKSTESQENFMTLLKDVPLDFITVTYDVIETLSSKYSYPVQEYLYVTLTDHIHCAYKAVLEDNYQ-ES 117
Cdd:COG3933   425 IEIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIiNP 504

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1461657093 118 KLPNISQEYGIEYVIAKEALAMFRQKLLNDLPDDEIGRIALHFINAK 164
Cdd:COG3933   505 NLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLN 551
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
32-271 2.53e-03

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 39.33  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093  32 FQKRKGDLVIADKIEKVFSLKSTESQENFMTLLKDVPLDFITVTYDVIETLSSKysyPVQEYLYVTLTDHIHCAYKAVLE 111
Cdd:COG3933   336 LAKAIKEATIILRLLSKLLKLLLLLLLNERLLLLELKILIEPLDIFFDSSASSD---ESDESEEDENLYEIIEIKKKLLL 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 112 DNYQESKLPNISQEYGIEYVIAKealamFRQKLLNDLPDDEIGRIALHFInakgvmavekspkVDLTRSVLSKVQEELER 191
Cdd:COG3933   413 ELGIDEEEINIIIEIDIDVHLLK-----FIYDDNKNFNKEELAKIVDEDI-------------INVVEEILELAEKKLGR 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461657093 192 lgikrtkensNFYDRLMIHLTYFLQY-LDRSPNDNGPLMDMGKHIQIAYPEAYDVGEKIYQIIASETGVAIHESEKFYIV 270
Cdd:COG3933   475 ----------KFSENFIYALSLHLSSfIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLT 544


                  .
gi 1461657093 271 L 271
Cdd:COG3933   545 L 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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