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Conserved domains on  [gi|1265152516|gb|PGQ78611|]
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levansucrase [Priestia megaterium]

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
 1-273 2.22e-49

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 164.49  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516   1 MKILKVLNNNAVV-FKEGGVEKIAMGPGIAFQKGKNDLINAAKVEKVFVMK--EEQEKFQELLKNLPEEHIQVAEEIISY 77
Cdd:PRK09772    3 MQITKILNNNVVVvIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSshELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  78 AEQQLsATLSHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLYQPEYAIGVWALQHIKKRLDITMPVDEAGYIALHI 157
Cdd:PRK09772   83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 158 HTAKLnSPGMKQLMMNTTIINEMVTIIKKELNTEIDENSMSYQRLLTHLRFALNRLAQNEPFHEMDEEMLDVLKVKYKKS 237
Cdd:PRK09772  162 VSAQM-SGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1265152516 238 YQCAETIKQFVKDEYEINFPEAELGYITLHICRIEQ 273
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRK 276
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-273 2.22e-49

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 164.49  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516   1 MKILKVLNNNAVV-FKEGGVEKIAMGPGIAFQKGKNDLINAAKVEKVFVMK--EEQEKFQELLKNLPEEHIQVAEEIISY 77
Cdd:PRK09772    3 MQITKILNNNVVVvIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSshELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  78 AEQQLsATLSHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLYQPEYAIGVWALQHIKKRLDITMPVDEAGYIALHI 157
Cdd:PRK09772   83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 158 HTAKLnSPGMKQLMMNTTIINEMVTIIKKELNTEIDENSMSYQRLLTHLRFALNRLAQNEPFHEMDEEMLDVLKVKYKKS 237
Cdd:PRK09772  162 VSAQM-SGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1265152516 238 YQCAETIKQFVKDEYEINFPEAELGYITLHICRIEQ 273
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRK 276
BglG COG3711
Transcriptional antiterminator [Transcription];
49-275 1.25e-47

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 167.34  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  49 MKEEQEKFQELLKNLPEEHIQVAEEIISYAEQQLSATLSHHVHIALSDHLSFAVERIARGISIQ--NKLLNEIKSlyQPE 126
Cdd:COG3711   160 LSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 127 YAIGVWALQHIKKRLDITMPVDEAGYIALHIHTAKLNSPGMKQLMMN---TTIINEMVTIIKKELNTEIDENSMSYQRLL 203
Cdd:COG3711   238 YEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITleiTKLIKEIINIIEEELGIDLDEDSLLYERLI 317

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265152516 204 THLRFALNRLAQNEPfheMDEEMLDVLKVKYKKSYQCAETIKQFVKDEYEINFPEAELGYITLHICRIEQRI 275
Cdd:COG3711   318 THLKPAINRLKYGIP---IRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQ 386
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 72-160 2.14e-19

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: 80.37  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  72 EEIISYAEQQLSATL-SHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLYQPEYAIGVWALQHIKKRLDITMPVDEA 150
Cdd:pfam00874   1 EEIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80

                          90
                  ....*....|
gi 1265152516 151 GYIALHIHTA 160
Cdd:pfam00874  81 GYIALHFLSA 90
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 2.20e-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 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: 76.74  E-value: 2.20e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1265152516    1 MKILKVLNNNAV-VFKEGGVEKIAMGPGIAFQKGKNDLINAAKVEKVFVMKEEQE 54
Cdd:smart01061   1 MRIKKVLNNNVVlAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-273 2.22e-49

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 164.49  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516   1 MKILKVLNNNAVV-FKEGGVEKIAMGPGIAFQKGKNDLINAAKVEKVFVMK--EEQEKFQELLKNLPEEHIQVAEEIISY 77
Cdd:PRK09772    3 MQITKILNNNVVVvIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSshELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  78 AEQQLsATLSHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLYQPEYAIGVWALQHIKKRLDITMPVDEAGYIALHI 157
Cdd:PRK09772   83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 158 HTAKLnSPGMKQLMMNTTIINEMVTIIKKELNTEIDENSMSYQRLLTHLRFALNRLAQNEPFHEMDEEMLDVLKVKYKKS 237
Cdd:PRK09772  162 VSAQM-SGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1265152516 238 YQCAETIKQFVKDEYEINFPEAELGYITLHICRIEQ 273
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRK 276
BglG COG3711
Transcriptional antiterminator [Transcription];
49-275 1.25e-47

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 167.34  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  49 MKEEQEKFQELLKNLPEEHIQVAEEIISYAEQQLSATLSHHVHIALSDHLSFAVERIARGISIQ--NKLLNEIKSlyQPE 126
Cdd:COG3711   160 LSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 127 YAIGVWALQHIKKRLDITMPVDEAGYIALHIHTAKLNSPGMKQLMMN---TTIINEMVTIIKKELNTEIDENSMSYQRLL 203
Cdd:COG3711   238 YEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITleiTKLIKEIINIIEEELGIDLDEDSLLYERLI 317

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265152516 204 THLRFALNRLAQNEPfheMDEEMLDVLKVKYKKSYQCAETIKQFVKDEYEINFPEAELGYITLHICRIEQRI 275
Cdd:COG3711   318 THLKPAINRLKYGIP---IRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQ 386
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 72-160 2.14e-19

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: 80.37  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  72 EEIISYAEQQLSATL-SHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLYQPEYAIGVWALQHIKKRLDITMPVDEA 150
Cdd:pfam00874   1 EEIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80

                          90
                  ....*....|
gi 1265152516 151 GYIALHIHTA 160
Cdd:pfam00874  81 GYIALHFLSA 90
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 2.20e-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 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: 76.74  E-value: 2.20e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1265152516    1 MKILKVLNNNAV-VFKEGGVEKIAMGPGIAFQKGKNDLINAAKVEKVFVMKEEQE 54
Cdd:smart01061   1 MRIKKVLNNNVVlAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 1.08e-16

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: 72.08  E-value: 1.08e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1265152516   2 KILKVLNNNAV-VFKEGGVEKIAMGPGIAFQKGKNDLINAAKVEKVFVMKEEQEK 55
Cdd:pfam03123   1 KIKKVLNNNVVlAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEES 55
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 178-268 3.36e-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: 71.90  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 178 NEMVTIIKKELNTEIDeNSMSYQRLLTHLRFALNRLAQNepfHEMDEEMLDVLKVKYKKSYQCAETIKQFVKDEYEINFP 257
Cdd:pfam00874   1 EEIIELIEKKLGITFD-DDILYIRLILHLAFAIERIKEG---ITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|.
gi 1265152516 258 EAELGYITLHI 268
Cdd:pfam00874  77 EDEIGYIALHF 87
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
44-164 3.95e-13

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 68.99  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  44 EKVFVMKEEQEKFQELLKNLPEEHIQVAEEIISYAEQQLSATLSHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLY 123
Cdd:COG3933   434 LKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKY 513

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1265152516 124 QPEYAIGVWALQHIKKRLDITMPVDEAGYIALHIHTAKLNS 164
Cdd:COG3933   514 PKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENN 554
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
134-266 2.50e-06

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 48.57  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516 134 LQHIKKRLDITMPVDEAGYIALHIHTAKLNSPGMKQLMMNTTI--INEMVTIIKKELNTEIDENsMSYQrLLTHLRFALN 211
Cdd:COG3933   416 IDEEEINIIIEIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIInvVEEILELAEKKLGRKFSEN-FIYA-LSLHLSSFIE 493

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1265152516 212 RLAQNEpfhEMDEEMLDVLKVKYKKSYQCAETIKQFVKDEYEINFPEAELGYITL 266
Cdd:COG3933   494 RIKEGK---EIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTL 545
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 52-164 1.01e-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: 46.64  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  52 EQEKFQELLKNLPEEHIQVAEEIISYAEQQLSATLSHHVHIALSDHLSFAVERIARGISIQNKLLNEIKSLYQPEYAIGV 131
Cdd:COG1221   455 KSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAA 534

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1265152516 132 WALQHIKKRLDITMPVDEAGYIALHIHTAKLNS 164
Cdd:COG1221   535 EAIKIIEEELKILIPDEEEGFILLLLIELKEEK 567
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
54-153 2.42e-05

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 45.49  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265152516  54 EKFQELLKNL-PEEHIQVAEEIISYAEQQLSATLSHHVHIALSDHLSFAVERIARGISIQN-KLLNEIKSLYQPEYAIGV 131
Cdd:COG3933   809 ESLIESLTILnPEKIINELEDFISRLENLLGIKLDNDVKIGLILHIACMIERLVTGEEILTyPNKEEFIQENESEYAVIK 888

                          90       100
                  ....*....|....*....|..
gi 1265152516 132 WALQHIKKRLDITMPVDEAGYI 153
Cdd:COG3933   889 EAFSPIEEKYNIKIPDSEIAYI 910
 
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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