NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1896924440|ref|WP_186869133|]
View 

MULTISPECIES: BglG family transcription antiterminator LicT [Ornithinibacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09772 super family cl31605
transcriptional antiterminator BglG; Provisional
 1-275 5.96e-61

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 194.54  E-value: 5.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440   1 MKITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQNTGISEKLDQLLKHTSEKYLDIAYEILQY 80
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  81 AQSKLPyKLDEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIGLKAIDFIEEETKIRLDEDEAASIALHL 160
Cdd:PRK09772   83 AQERLG-KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 161 VNSEISGeNMETAILVTEMVNNILNIVKYTYQMELDEDSINYERFLTHLRYFSIRFIRKEKTEDTvDDFFVEQIRQKYVK 240
Cdd:PRK09772  162 VSAQMSG-NMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDS-DESLQQAVKQNYPQ 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1896924440 241 AYQCTRKIATYLQSEFNWEISKDEEMYLTVHIHRV 275
Cdd:PRK09772  240 AWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-275 5.96e-61

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 194.54  E-value: 5.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440   1 MKITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQNTGISEKLDQLLKHTSEKYLDIAYEILQY 80
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  81 AQSKLPyKLDEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIGLKAIDFIEEETKIRLDEDEAASIALHL 160
Cdd:PRK09772   83 AQERLG-KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 161 VNSEISGeNMETAILVTEMVNNILNIVKYTYQMELDEDSINYERFLTHLRYFSIRFIRKEKTEDTvDDFFVEQIRQKYVK 240
Cdd:PRK09772  162 VSAQMSG-NMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDS-DESLQQAVKQNYPQ 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1896924440 241 AYQCTRKIATYLQSEFNWEISKDEEMYLTVHIHRV 275
Cdd:PRK09772  240 AWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
67-281 3.79e-43

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 155.40  E-value: 3.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  67 SEKYLDIAYEILQYAQSKLPYKLDEYLYVALTDHISFAISRHNQG--IRLKNALLYEIRKnyKQEYEIGLKAIDFIEEET 144
Cdd:COG3711   175 PEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGkyIKLDNPLLWEIKK--PKEYEIAKEILKLIEERL 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 145 KIRLDEDEAASIALHLVNSEISGENMETAIL---VTEMVNNILNIVKYTYQMELDEDSINYERFLTHLRYFSIRFIRKEk 221
Cdd:COG3711   253 GISLPEDEIGYIALHLLGARLNNDNELSEIItleITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRLKYGI- 331

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 222 tedTVDDFFVEQIRQKYVKAYQCTRKIATYLQSEFNWEISKDEEMYLTVHIHRVTYRQKN 281
Cdd:COG3711   332 ---PIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKE 388
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-52 1.20e-23

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: 90.61  E-value: 1.20e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1896924440    1 MKITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQN 52
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKD 52
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-57 2.09e-23

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: 90.18  E-value: 2.09e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924440   2 KITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQNTGISE 57
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-275 5.96e-61

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 194.54  E-value: 5.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440   1 MKITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQNTGISEKLDQLLKHTSEKYLDIAYEILQY 80
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  81 AQSKLPyKLDEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIGLKAIDFIEEETKIRLDEDEAASIALHL 160
Cdd:PRK09772   83 AQERLG-KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 161 VNSEISGeNMETAILVTEMVNNILNIVKYTYQMELDEDSINYERFLTHLRYFSIRFIRKEKTEDTvDDFFVEQIRQKYVK 240
Cdd:PRK09772  162 VSAQMSG-NMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDS-DESLQQAVKQNYPQ 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1896924440 241 AYQCTRKIATYLQSEFNWEISKDEEMYLTVHIHRV 275
Cdd:PRK09772  240 AWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
67-281 3.79e-43

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 155.40  E-value: 3.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  67 SEKYLDIAYEILQYAQSKLPYKLDEYLYVALTDHISFAISRHNQG--IRLKNALLYEIRKnyKQEYEIGLKAIDFIEEET 144
Cdd:COG3711   175 PEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGkyIKLDNPLLWEIKK--PKEYEIAKEILKLIEERL 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 145 KIRLDEDEAASIALHLVNSEISGENMETAIL---VTEMVNNILNIVKYTYQMELDEDSINYERFLTHLRYFSIRFIRKEk 221
Cdd:COG3711   253 GISLPEDEIGYIALHLLGARLNNDNELSEIItleITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRLKYGI- 331

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 222 tedTVDDFFVEQIRQKYVKAYQCTRKIATYLQSEFNWEISKDEEMYLTVHIHRVTYRQKN 281
Cdd:COG3711   332 ---PIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKE 388
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-52 1.20e-23

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: 90.61  E-value: 1.20e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1896924440    1 MKITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQN 52
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKD 52
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-57 2.09e-23

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: 90.18  E-value: 2.09e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896924440   2 KITKVLNNNVVITENDQKEELVVMGKGLAFQKKVGQSIDPSKVEKTFVLQNTGISE 57
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 76-163 4.11e-17

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: 74.60  E-value: 4.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  76 EILQYAQSKLPYKL-DEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIGLKAIDFIEEETKIRLDEDEAA 154
Cdd:pfam00874   2 EIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 1896924440 155 SIALHLVNS 163
Cdd:pfam00874  82 YIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
54-176 8.30e-14

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 71.30  E-value: 8.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  54 GISEKLDQLLKHTSEKYLDIAYEILQYAQSKLPYKLDEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIG 133
Cdd:COG3933   441 NKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVA 520

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1896924440 134 LKAIDFIEEETKIRLDEDEAASIALHLVNSEISGENMETAILV 176
Cdd:COG3933   521 KEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKVGVIV 563
BglG COG3711
Transcriptional antiterminator [Transcription];
60-160 1.49e-13

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 70.27  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  60 DQLLKHTSEKYLDIAYEILQYAQSKLPYKL--DEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIGLKAI 137
Cdd:COG3711   277 NELSEIITLEITKLIKEIINIIEEELGIDLdeDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIA 356

                          90       100
                  ....*....|....*....|...
gi 1896924440 138 DFIEEETKIRLDEDEAASIALHL 160
Cdd:COG3711   357 KYLEKELGIEIPEDEIGYLTLHF 379
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 181-274 3.63e-13

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: 63.81  E-value: 3.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 181 NNILNIVKYTYQMELDEDSInYERFLTHLRYFSIRFIRKEktedTVDDFFVEQIRQKYVKAYQCTRKIATYLQSEFNWEI 260
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIL-YIRLILHLAFAIERIKEGI----TIENPLLEEIKEKYPKEFEIAKKILEILEEELGIEL 75

                          90
                  ....*....|....
gi 1896924440 261 SKDEEMYLTVHIHR 274
Cdd:pfam00874  76 PEDEIGYIALHFLS 89
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 76-176 7.10e-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: 43.94  E-value: 7.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  76 EILQYAQSKLPYKLDEYLYVALTDHISFAISRHNQGIRLKNALLYEIRKNYKQEYEIGLKAIDFIEEETKIRLDEDEAAS 155
Cdd:COG1221   476 EIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGF 555

                          90       100
                  ....*....|....*....|.
gi 1896924440 156 IALHLVNSEISGENMETAILV 176
Cdd:COG1221   556 ILLLLIELKEEKSLSENVIVV 576
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
65-273 7.43e-03

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 37.79  E-value: 7.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440  65 HTSEKYLDIAYEILQYAQSKLPYKLDEYLYVALTDHISFAISRHNQGIRLKNALLYEIrkNYKQEYEIGLKAIDFIEEET 144
Cdd:COG3933   347 LRLLSKLLKLLLLLLLNERLLLLELKILIEPLDIFFDSSASSDESDESEEDENLYEII--EIKKKLLLELGIDEEEINII 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924440 145 KIRLDEDEAASIALHlVNSEISGENMETAI--LVTEMVNNILNIVKYTYQMELDEdsinyeRFLTHLRYFSIRFIRKEKT 222
Cdd:COG3933   425 IEIDIDVHLLKFIYD-DNKNFNKEELAKIVdeDIINVVEEILELAEKKLGRKFSE------NFIYALSLHLSSFIERIKE 497

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1896924440 223 EDTVDDFFVEQIRQKYVKAYQCTRKIATYLQSEFNWEISKDEEMYLTVHIH 273
Cdd:COG3933   498 GKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLV 548
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH