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Conserved domains on  [gi|499998946|ref|WP_011679664|]
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MULTISPECIES: PRD domain-containing protein [Leuconostoc]

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
 1-281 1.24e-50

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 167.96  E-value: 1.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946   1 MLVKRIFNNNVLLA-ENSEQELVIVGRGVGFKQKIGNTVDSSKIEKTYYPQDENWTRMFNEMADTISSDYVEIASHIIST 79
Cdd:PRK09772   3 MQITKILNNNVVVViDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  80 AEKSLGLSFDGyLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAVAFINEQMGVQLPEDEVGFIALKF 159
Cdd:PRK09772  83 AQERLGKLQDS-IYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946 160 VEKRAGPNFnEKATNMTQLIESALTLIRHDLLPDIDSSNLNYQRLIVHLRFFVDRLLDESHVQKGENSfdnvmsqhLSES 239
Cdd:PRK09772 162 VSAQMSGNM-EDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDES--------LQQA 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499998946 240 LQERYTSSYQCAQRVINYFEKQTKQKTGVNEQVYLTMHLQRI 281
Cdd:PRK09772 233 VKQNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-281 1.24e-50

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 167.96  E-value: 1.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946   1 MLVKRIFNNNVLLA-ENSEQELVIVGRGVGFKQKIGNTVDSSKIEKTYYPQDENWTRMFNEMADTISSDYVEIASHIIST 79
Cdd:PRK09772   3 MQITKILNNNVVVViDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  80 AEKSLGLSFDGyLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAVAFINEQMGVQLPEDEVGFIALKF 159
Cdd:PRK09772  83 AQERLGKLQDS-IYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946 160 VEKRAGPNFnEKATNMTQLIESALTLIRHDLLPDIDSSNLNYQRLIVHLRFFVDRLLDESHVQKGENSfdnvmsqhLSES 239
Cdd:PRK09772 162 VSAQMSGNM-EDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDES--------LQQA 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499998946 240 LQERYTSSYQCAQRVINYFEKQTKQKTGVNEQVYLTMHLQRI 281
Cdd:PRK09772 233 VKQNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
61-283 3.15e-34

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 130.75  E-value: 3.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  61 MADTISSDYVEIASHIISTAEKSLGLSFDGYLLIGLADHIQFAVERLQKNLPIK--NELLWETKHfyPDEYRIGALAVAF 138
Cdd:COG3711  170 LLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILKL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946 139 INEQMGVQLPEDEVGFIALKFVEKRAGPNF---NEKATNMTQLIESALTLIRHDLLPDIDSSNLNYQRLIVHLRFFVDRL 215
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGARLNNDNelsEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRL 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499998946 216 LDESHVqkgENSfdnvmsqhLSESLQERYTSSYQCAQRVINYFEKQTKQKTGVNEQVYLTMHLQRIVD 283
Cdd:COG3711  328 KYGIPI---RNP--------LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 76-160 1.74e-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: 80.76  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946   76 IISTAEKSLGLSF-DGYLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAVAFINEQMGVQLPEDEVGF 154
Cdd:pfam00874   3 IIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGY 82


                  ....*.
gi 499998946  155 IALKFV 160
Cdd:pfam00874  83 IALHFL 88
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 2.99e-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: 79.05  E-value: 2.99e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499998946     1 MLVKRIFNNNVLLAEN-SEQELVIVGRGVGFKQKIGNTVDSSKIEKTYYPQDENW 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDeNGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-281 1.24e-50

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 167.96  E-value: 1.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946   1 MLVKRIFNNNVLLA-ENSEQELVIVGRGVGFKQKIGNTVDSSKIEKTYYPQDENWTRMFNEMADTISSDYVEIASHIIST 79
Cdd:PRK09772   3 MQITKILNNNVVVViDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  80 AEKSLGLSFDGyLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAVAFINEQMGVQLPEDEVGFIALKF 159
Cdd:PRK09772  83 AQERLGKLQDS-IYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946 160 VEKRAGPNFnEKATNMTQLIESALTLIRHDLLPDIDSSNLNYQRLIVHLRFFVDRLLDESHVQKGENSfdnvmsqhLSES 239
Cdd:PRK09772 162 VSAQMSGNM-EDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDES--------LQQA 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499998946 240 LQERYTSSYQCAQRVINYFEKQTKQKTGVNEQVYLTMHLQRI 281
Cdd:PRK09772 233 VKQNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERV 274
BglG COG3711
Transcriptional antiterminator [Transcription];
61-283 3.15e-34

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 130.75  E-value: 3.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  61 MADTISSDYVEIASHIISTAEKSLGLSFDGYLLIGLADHIQFAVERLQKNLPIK--NELLWETKHfyPDEYRIGALAVAF 138
Cdd:COG3711  170 LLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILKL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946 139 INEQMGVQLPEDEVGFIALKFVEKRAGPNF---NEKATNMTQLIESALTLIRHDLLPDIDSSNLNYQRLIVHLRFFVDRL 215
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGARLNNDNelsEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRL 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499998946 216 LDESHVqkgENSfdnvmsqhLSESLQERYTSSYQCAQRVINYFEKQTKQKTGVNEQVYLTMHLQRIVD 283
Cdd:COG3711  328 KYGIPI---RNP--------LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 76-160 1.74e-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: 80.76  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946   76 IISTAEKSLGLSF-DGYLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAVAFINEQMGVQLPEDEVGF 154
Cdd:pfam00874   3 IIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGY 82


                  ....*.
gi 499998946  155 IALKFV 160
Cdd:pfam00874  83 IALHFL 88
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-54 2.99e-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: 79.05  E-value: 2.99e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499998946     1 MLVKRIFNNNVLLAEN-SEQELVIVGRGVGFKQKIGNTVDSSKIEKTYYPQDENW 54
Cdd:smart01061   1 MRIKKVLNNNVVLAEDeNGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 3-53 2.04e-17

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: 74.39  E-value: 2.04e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499998946    3 VKRIFNNNVLLAEN-SEQELVIVGRGVGFKQKIGNTVDSSKIEKTYYPQDEN 53
Cdd:pfam03123   2 IKKVLNNNVVLAKDdNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEE 53
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
59-157 1.05e-16

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 80.16  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  59 NEMADTISSDYVEIASHIISTAEKSLGLSFDGYLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAVAF 138
Cdd:COG3933  447 EELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKEL 526

                         90
                 ....*....|....*....
gi 499998946 139 INEQMGVQLPEDEVGFIAL 157
Cdd:COG3933  527 IEQELDIEIPEDEVGFLTL 545
BglG COG3711
Transcriptional antiterminator [Transcription];
59-157 3.20e-15

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 75.28  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  59 NEMADTISSDYVEIASHIISTAEKSLGLSF--DGYLLIGLADHIQFAVERLQKNLPIKNELLWETKHFYPDEYRIGALAV 136
Cdd:COG3711  277 NELSEIITLEITKLIKEIINIIEEELGIDLdeDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIA 356

                         90       100
                 ....*....|....*....|.
gi 499998946 137 AFINEQMGVQLPEDEVGFIAL 157
Cdd:COG3711  357 KYLEKELGIEIPEDEIGYLTL 377
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 197-280 3.88e-06

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: 44.17  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  197 SNLNYQRLIVHLRFFVDRLldeshvQKGENSFDNVMSQhlsesLQERYTSSYQCAQRVINYFEKQTKQKTGVNEQVYLTM 276
Cdd:pfam00874  17 DDILYIRLILHLAFAIERI------KEGITIENPLLEE-----IKEKYPKEFEIAKKILEILEEELGIELPEDEIGYIAL 85


                  ....
gi 499998946  277 HLQR 280
Cdd:pfam00874  86 HFLS 89
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 30-161 1.52e-03

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: 40.09  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  30 FKQKIGNTVDSskIEKTYYPQDENWTRMFNEMADTISSDYVEIASHIISTAEKSLGLSFDgYLLIGLADHIQFAVERLQK 109
Cdd:COG1221  434 INKIISKDIES--YFKKLIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSS-NLFIALSLHLLSTLLRIKK 510

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499998946 110 NLPIKNELLWETKHFYPDEYRIGALAVAFINEQMGVQLPEDEVGFIALKFVE 161
Cdd:COG1221  511 GKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFILLLLIE 562
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
30-155 3.19e-03

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 38.94  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499998946  30 FKQKIGNTVDSSKIEKtyypqdENWTRMFNEMADTI--------SSDYVEIASHIISTAEKSLGLSFDGYLLIGLADHIQ 101
Cdd:COG3933  782 LQKLLGGELDAEEIEE------INNEIIKNFSLESLiesltilnPEKIINELEDFISRLENLLGIKLDNDVKIGLILHIA 855

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499998946 102 FAVERLQKN---LPIKNELLWETKHfyPDEYRIGALAVAFINEQMGVQLPEDEVGFI 155
Cdd:COG3933  856 CMIERLVTGeeiLTYPNKEEFIQEN--ESEYAVIKEAFSPIEEKYNIKIPDSEIAYI 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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