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Conserved domains on  [gi|1081285177|gb|OFU26164|]
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transcriptional antiterminator [Clostridium sp. HMSC19C05]

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 2.27e-50

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 167.19  E-value: 2.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177   1 MNIKKIFNNNVVVSSLEDGTEIIVTGAGVGFKKKVGDLIDENLISKKYFVQDDQRD-KYNQILNKTSIEYFKISEEIIEK 79
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNgRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  80 ANEVLNtQVNDSIILALTSHIEFAVQREKQGIKLPNLILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHI 159
Cdd:PRK09772   83 AQERLG-KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177 160 INGLENSQKDEGINILEFSKQVIQIIEEVHGFKLDVNSLNYTRLITHLKFFVQRILRKETYNDSDiEDMYKLVNKNYNKP 239
Cdd:PRK09772  162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSD-ESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1081285177 240 KVCTEEIAALVLDRFEYKISKEEELYLMIHINKI 273
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-273 2.27e-50

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 167.19  E-value: 2.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177   1 MNIKKIFNNNVVVSSLEDGTEIIVTGAGVGFKKKVGDLIDENLISKKYFVQDDQRD-KYNQILNKTSIEYFKISEEIIEK 79
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNgRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  80 ANEVLNtQVNDSIILALTSHIEFAVQREKQGIKLPNLILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHI 159
Cdd:PRK09772   83 AQERLG-KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177 160 INGLENSQKDEGINILEFSKQVIQIIEEVHGFKLDVNSLNYTRLITHLKFFVQRILRKETYNDSDiEDMYKLVNKNYNKP 239
Cdd:PRK09772  162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSD-ESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1081285177 240 KVCTEEIAALVLDRFEYKISKEEELYLMIHINKI 273
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
42-270 7.14e-31

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 121.12  E-value: 7.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  42 NLISKKYFVQDDQRDKYNQILNKtsiEYFKISEEIIEKANEVLNTQVNDSIILALTSHIEFAVQREKQG--IKLPNLILN 119
Cdd:COG3711   154 ELLSELLSENDLLSLLLLKLIPE---EDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGkyIKLDNPLLW 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177 120 ETKQlyREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHIIN----GLENSQKDEGINILEFSKQVIQIIEEVHGFKLDV 195
Cdd:COG3711   231 EIKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGarlnNDNELSEIITLEITKLIKEIINIIEEELGIDLDE 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081285177 196 NSLNYTRLITHLKFFVQRILRKETYNDsdieDMYKLVNKNYNKPKVCTEEIAALVLDRFEYKISKEEELYLMIHI 270
Cdd:COG3711   309 DSLLYERLITHLKPAINRLKYGIPIRN----PLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHF 379
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 1.09e-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 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: 72.12  E-value: 1.09e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1081285177    1 MNIKKIFNNNVVVSSLEDGTEIIVTGAGVGFKKKVGDLIDENLISKKYFVQDDQ 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 74-161 2.65e-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: 72.29  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  74 EEIIEKANEVLNTQVNDSIIL-ALTSHIEFAVQREKQGIKLPNLILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEA 152
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDILYiRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80


                  ....*....
gi 1081285177 153 GYIAIHIIN 161
Cdd:pfam00874  81 GYIALHFLS 89
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-273 2.27e-50

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 167.19  E-value: 2.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177   1 MNIKKIFNNNVVVSSLEDGTEIIVTGAGVGFKKKVGDLIDENLISKKYFVQDDQRD-KYNQILNKTSIEYFKISEEIIEK 79
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNgRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  80 ANEVLNtQVNDSIILALTSHIEFAVQREKQGIKLPNLILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHI 159
Cdd:PRK09772   83 AQERLG-KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177 160 INGLENSQKDEGINILEFSKQVIQIIEEVHGFKLDVNSLNYTRLITHLKFFVQRILRKETYNDSDiEDMYKLVNKNYNKP 239
Cdd:PRK09772  162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSD-ESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1081285177 240 KVCTEEIAALVLDRFEYKISKEEELYLMIHINKI 273
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
42-270 7.14e-31

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 121.12  E-value: 7.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  42 NLISKKYFVQDDQRDKYNQILNKtsiEYFKISEEIIEKANEVLNTQVNDSIILALTSHIEFAVQREKQG--IKLPNLILN 119
Cdd:COG3711   154 ELLSELLSENDLLSLLLLKLIPE---EDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGkyIKLDNPLLW 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177 120 ETKQlyREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHIIN----GLENSQKDEGINILEFSKQVIQIIEEVHGFKLDV 195
Cdd:COG3711   231 EIKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGarlnNDNELSEIITLEITKLIKEIINIIEEELGIDLDE 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081285177 196 NSLNYTRLITHLKFFVQRILRKETYNDsdieDMYKLVNKNYNKPKVCTEEIAALVLDRFEYKISKEEELYLMIHI 270
Cdd:COG3711   309 DSLLYERLITHLKPAINRLKYGIPIRN----PLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHF 379
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 1.09e-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 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: 72.12  E-value: 1.09e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1081285177    1 MNIKKIFNNNVVVSSLEDGTEIIVTGAGVGFKKKVGDLIDENLISKKYFVQDDQ 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 54
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 74-161 2.65e-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: 72.29  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  74 EEIIEKANEVLNTQVNDSIIL-ALTSHIEFAVQREKQGIKLPNLILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEA 152
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDILYiRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80


                  ....*....
gi 1081285177 153 GYIAIHIIN 161
Cdd:pfam00874  81 GYIALHFLS 89
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 3-54 6.99e-15

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: 67.45  E-value: 6.99e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1081285177   3 IKKIFNNNVVVSSLEDGTEIIVTGAGVGFKKKVGDLIDENLISKKYFVQDDQ 54
Cdd:pfam03123   2 IKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 53
BglG COG3711
Transcriptional antiterminator [Transcription];
54-175 1.36e-14

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 73.36  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  54 QRDKYNQILNKTSIEYFKISEEIIEKANEVLNTQVNDSIILA--LTSHIEFAVQREKQGIKLPNLILNETKQLYREEFKF 131
Cdd:COG3711   272 RLNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYerLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFEL 351

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1081285177 132 GLWAIDEIEKRIGIKLPEDEAGYIAIHIINGLENSQKDEGINIL 175
Cdd:COG3711   352 AKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESKKKRVL 395
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
37-170 9.06e-12

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 65.14  E-value: 9.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  37 DLIDENLISKKYFVQDDQRDKYNQILNKtsiEYFKISEEIIEKANEVLNTQVNDSIILALTSHIEFAVQREKQGIKLPNL 116
Cdd:COG3933   428 DIDVHLLKFIYDDNKNFNKEELAKIVDE---DIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINP 504

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1081285177 117 ILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHIINGLENSQKDE 170
Cdd:COG3933   505 NLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGK 558
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 179-270 2.07e-08

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: 50.71  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177 179 KQVIQIIEEVHGFKLDvNSLNYTRLITHLKFFVQRILRKETYNDSDIEDMYKLVNKNYNkpkvCTEEIAALVLDRFEYKI 258
Cdd:pfam00874   1 EEIIELIEKKLGITFD-DDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFE----IAKKILEILEEELGIEL 75

                          90
                  ....*....|..
gi 1081285177 259 SKEEELYLMIHI 270
Cdd:pfam00874  76 PEDEIGYIALHF 87
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 31-174 2.41e-08

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: 54.73  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081285177  31 FKKKVGDLIDENLisKKYFVQDDQRDKYNQILNKTSIEYFKISEEIIEKANEVLNTQVNDSIILALTSHIEFAVQREKQG 110
Cdd:COG1221   434 INKIISKDIESYF--KKLIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKG 511

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081285177 111 IKLPNLILNETKQLYREEFKFGLWAIDEIEKRIGIKLPEDEAGYIAIHIINGLENSQKDEGINI 174
Cdd:COG1221   512 KKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFILLLLIELKEEKSLSENVIV 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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