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Conserved domains on  [gi|446207872|ref|WP_000285727|]
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PRD domain-containing protein [Streptococcus pneumoniae]

Protein Classification

BglG family transcription antiterminator( domain architecture ID 13930989)

BglG family transcription antiterminator similar to Bacillus subtilis transcriptional regulator MtlR that positively regulates the expression of the mtlAFD operon, which is involved in the uptake and catabolism of mannitol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BglG super family cl34661
Transcriptional antiterminator [Transcription];
43-277 1.80e-26

Transcriptional antiterminator [Transcription];


The actual alignment was detected with superfamily member COG3711:

Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 108.41  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872  43 NQVEKIFRMKTEESRENFMALLKDVPLDFITVTYEIIDKLSKKYHYPIQEYLYVTLTDHIYCSYQALTQGRYKDSNLPDI 122
Cdd:COG3711  150 KALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 123 SA-KYPVAFQIANEAFEIYRQKLADHFPEDEIIRIAYHFINAEGENEVELVESIDKR-----KEILRNVEEVLtDYAIQr 196
Cdd:COG3711  230 WEiKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITLEitkliKEIINIIEEEL-GIDLD- 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 197 tkKNNHFYDRFMIHLNYFLDyldRSRDDNQSLLDMEDHIKQSYPKAFEIGSKIYDVITQHTGLDLYKSERVYLVLHIQRL 276
Cdd:COG3711  308 --EDSLLYERLITHLKPAIN---RLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAA 382


                 .
gi 446207872 277 L 277
Cdd:COG3711  383 L 383
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 6.81e-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: 85.99  E-value: 6.81e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446207872     2 YRILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEE 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
43-277 1.80e-26

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 108.41  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872  43 NQVEKIFRMKTEESRENFMALLKDVPLDFITVTYEIIDKLSKKYHYPIQEYLYVTLTDHIYCSYQALTQGRYKDSNLPDI 122
Cdd:COG3711  150 KALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 123 SA-KYPVAFQIANEAFEIYRQKLADHFPEDEIIRIAYHFINAEGENEVELVESIDKR-----KEILRNVEEVLtDYAIQr 196
Cdd:COG3711  230 WEiKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITLEitkliKEIINIIEEEL-GIDLD- 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 197 tkKNNHFYDRFMIHLNYFLDyldRSRDDNQSLLDMEDHIKQSYPKAFEIGSKIYDVITQHTGLDLYKSERVYLVLHIQRL 276
Cdd:COG3711  308 --EDSLLYERLITHLKPAIN---RLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAA 382


                 .
gi 446207872 277 L 277
Cdd:COG3711  383 L 383
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 3-276 2.39e-25

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 101.71  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872   3 RILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEESRENFMALLKDVPLDFITVTYEIIdKL 82
Cdd:PRK09772   4 QITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRII-SL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872  83 SKKYHYPIQEYLYVTLTDHIYCSYQALTQG-RYKDSNLPDISAKYPVAFQIANEAFEIYRQKLADHFPEDEIIRIAYHFI 161
Cdd:PRK09772  83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNvLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 162 NAEGENEVELVESIdkrKEILRNVEEVLTDYAIQRTKKNNHFYDRFMIHLNYFLDYLDRSRDDNQSLLDMEDHIKQSYPK 241
Cdd:PRK09772 163 SAQMSGNMEDVAGV---TQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQ 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446207872 242 AFEIGSKIYDVITQHTGLDLYKSERVYLVLHIQRL 276
Cdd:PRK09772 240 AWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 6.81e-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: 85.99  E-value: 6.81e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446207872     2 YRILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEE 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 3-58 7.59e-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: 83.25  E-value: 7.59e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446207872    3 RILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEESRE 58
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 77-163 4.53e-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: 60.73  E-value: 4.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872   77 EIIDKLSKKYHYPIQ-EYLYVTLTDHIYCSYQALTQG-RYKDSNLPDISAKYPVAFQIANEAFEIYRQKLADHFPEDEII 154
Cdd:pfam00874   2 EIIELIEKKLGITFDdDILYIRLILHLAFAIERIKEGiTIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 446207872  155 RIAYHFINA 163
Cdd:pfam00874  82 YIALHFLSA 90
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
43-277 1.80e-26

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 108.41  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872  43 NQVEKIFRMKTEESRENFMALLKDVPLDFITVTYEIIDKLSKKYHYPIQEYLYVTLTDHIYCSYQALTQGRYKDSNLPDI 122
Cdd:COG3711  150 KALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 123 SA-KYPVAFQIANEAFEIYRQKLADHFPEDEIIRIAYHFINAEGENEVELVESIDKR-----KEILRNVEEVLtDYAIQr 196
Cdd:COG3711  230 WEiKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITLEitkliKEIINIIEEEL-GIDLD- 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 197 tkKNNHFYDRFMIHLNYFLDyldRSRDDNQSLLDMEDHIKQSYPKAFEIGSKIYDVITQHTGLDLYKSERVYLVLHIQRL 276
Cdd:COG3711  308 --EDSLLYERLITHLKPAIN---RLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAA 382


                 .
gi 446207872 277 L 277
Cdd:COG3711  383 L 383
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 3-276 2.39e-25

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 101.71  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872   3 RILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEESRENFMALLKDVPLDFITVTYEIIdKL 82
Cdd:PRK09772   4 QITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRII-SL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872  83 SKKYHYPIQEYLYVTLTDHIYCSYQALTQG-RYKDSNLPDISAKYPVAFQIANEAFEIYRQKLADHFPEDEIIRIAYHFI 161
Cdd:PRK09772  83 AQERLGKLQDSIYISLTDHCQFAIKRFQQNvLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 162 NAEGENEVELVESIdkrKEILRNVEEVLTDYAIQRTKKNNHFYDRFMIHLNYFLDYLDRSRDDNQSLLDMEDHIKQSYPK 241
Cdd:PRK09772 163 SAQMSGNMEDVAGV---TQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQ 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446207872 242 AFEIGSKIYDVITQHTGLDLYKSERVYLVLHIQRL 276
Cdd:PRK09772 240 AWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 6.81e-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: 85.99  E-value: 6.81e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446207872     2 YRILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEE 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 3-58 7.59e-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: 83.25  E-value: 7.59e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446207872    3 RILNPMNHNVSLVRNDKGEEVIVIGKGIAFGKKKGDLIAENQVEKIFRMKTEESRE 58
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 77-163 4.53e-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: 60.73  E-value: 4.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872   77 EIIDKLSKKYHYPIQ-EYLYVTLTDHIYCSYQALTQG-RYKDSNLPDISAKYPVAFQIANEAFEIYRQKLADHFPEDEII 154
Cdd:pfam00874   2 EIIELIEKKLGITFDdDILYIRLILHLAFAIERIKEGiTIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 446207872  155 RIAYHFINA 163
Cdd:pfam00874  82 YIALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 199-276 2.39e-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: 53.41  E-value: 2.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446207872  199 KNNHFYDRFMIHLNYFLDYLDRSRDDNQSLLDmedHIKQSYPKAFEIGSKIYDVITQHTGLDLYKSERVYLVLHIQRL 276
Cdd:pfam00874  16 DDDILYIRLILHLAFAIERIKEGITIENPLLE---EIKEKYPKEFEIAKKILEILEEELGIELPEDEIGYIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
39-168 2.71e-04

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 42.41  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872  39 LIAENQVEKIFRMKTEESRENFMALLKDVPLDFITVTYEIIDKLSKKYHYPIQEYLYVTLTDHIYCSYQALTQGRYK-DS 117
Cdd:COG3933  425 IEIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIiNP 504

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446207872 118 NLPDISAKYPVAFQIANEAFEIYRQKLADHFPEDEIIRIAyHFINAEGENE 168
Cdd:COG3933  505 NLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLT-LFLVSLNENN 554
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
150-271 1.05e-03

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 40.49  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207872 150 EDEIIRIAYHFINAEGENEVELVESIDKR-----KEILRNVEEVLtdyaiqrtkkNNHFYDRFMIHL-NYFLDYLDRSRD 223
Cdd:COG3933  428 DIDVHLLKFIYDDNKNFNKEELAKIVDEDiinvvEEILELAEKKL----------GRKFSENFIYALsLHLSSFIERIKE 497

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446207872 224 DNQSLLDMEDHIKQSYPKAFEIGSKIYDVITQHTGLDLYKSERVYLVL 271
Cdd:COG3933  498 GKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTL 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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