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Conserved domains on  [gi|657228140|ref|WP_029341840|]
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MULTISPECIES: BglG family transcription antiterminator LicT [Exiguobacterium]

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
 1-276 1.37e-69

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 216.50  E-value: 1.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140   1 MIIHQIFNNNVISVFDEAGRERVVMGKGIGFKRNSGQAILASDVEKVFYLDDAGNHERFKLLLQEIPEEIIVLTDDIVTI 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  81 AKLTLGKkLNELVYIALADHLHFALERHEKGLEIKNVLLWEIKRLYQDEFSVGLQALELVEEKFNIILPEDEAAYIALHI 160
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140 161 VNAELNEEMPNIVSMTKVIQEVLNLVKYHFALEWDENALAYHRFVTHLKFFAQRLVSRTEYEGDESALFDLVKMQYPKSY 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 657228140 241 VCTEKIATFIQTKYDYRLTDEEKLYLTVHITRLIKE 276
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-276 1.37e-69

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 216.50  E-value: 1.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140   1 MIIHQIFNNNVISVFDEAGRERVVMGKGIGFKRNSGQAILASDVEKVFYLDDAGNHERFKLLLQEIPEEIIVLTDDIVTI 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  81 AKLTLGKkLNELVYIALADHLHFALERHEKGLEIKNVLLWEIKRLYQDEFSVGLQALELVEEKFNIILPEDEAAYIALHI 160
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140 161 VNAELNEEMPNIVSMTKVIQEVLNLVKYHFALEWDENALAYHRFVTHLKFFAQRLVSRTEYEGDESALFDLVKMQYPKSY 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 657228140 241 VCTEKIATFIQTKYDYRLTDEEKLYLTVHITRLIKE 276
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
61-279 3.16e-43

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 155.40  E-value: 3.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  61 LLLQEIPEEIIVLTDDIVTIAKLTLGKKLNELVYIALADHLHFALERHEKGLEIK--NVLLWEIKRlyQDEFSVGLQALE 138
Cdd:COG3711  169 LLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140 139 LVEEKFNIILPEDEAAYIALHIVNAELNEEMP----NIVSMTKVIQEVLNLVKYHFALEWDENALAYHRFVTHLKFFAQR 214
Cdd:COG3711  247 LIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINR 326

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657228140 215 LVSRTEYEGDesaLFDLVKMQYPKSYVCTEKIATFIQTKYDYRLTDEEKLYLTVHITRLIKEKKK 279
Cdd:COG3711  327 LKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKE 388
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 76-163 1.16e-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: 81.15  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140   76 DIVTIAKLTLGKKL-NELVYIALADHLHFALERHEKGLEIKNVLLWEIKRLYQDEFSVGLQALELVEEKFNIILPEDEAA 154
Cdd:pfam00874   2 EIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 657228140  155 YIALHIVNA 163
Cdd:pfam00874  82 YIALHFLSA 90
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-55 4.01e-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: 75.97  E-value: 4.01e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 657228140     1 MIIHQIFNNNVISVFDEAGRERVVMGKGIGFKRNSGQAILASDVEKVFYLDDAGN 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-276 1.37e-69

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 216.50  E-value: 1.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140   1 MIIHQIFNNNVISVFDEAGRERVVMGKGIGFKRNSGQAILASDVEKVFYLDDAGNHERFKLLLQEIPEEIIVLTDDIVTI 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  81 AKLTLGKkLNELVYIALADHLHFALERHEKGLEIKNVLLWEIKRLYQDEFSVGLQALELVEEKFNIILPEDEAAYIALHI 160
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140 161 VNAELNEEMPNIVSMTKVIQEVLNLVKYHFALEWDENALAYHRFVTHLKFFAQRLVSRTEYEGDESALFDLVKMQYPKSY 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 657228140 241 VCTEKIATFIQTKYDYRLTDEEKLYLTVHITRLIKE 276
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
61-279 3.16e-43

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 155.40  E-value: 3.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  61 LLLQEIPEEIIVLTDDIVTIAKLTLGKKLNELVYIALADHLHFALERHEKGLEIK--NVLLWEIKRlyQDEFSVGLQALE 138
Cdd:COG3711  169 LLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140 139 LVEEKFNIILPEDEAAYIALHIVNAELNEEMP----NIVSMTKVIQEVLNLVKYHFALEWDENALAYHRFVTHLKFFAQR 214
Cdd:COG3711  247 LIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINR 326

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657228140 215 LVSRTEYEGDesaLFDLVKMQYPKSYVCTEKIATFIQTKYDYRLTDEEKLYLTVHITRLIKEKKK 279
Cdd:COG3711  327 LKYGIPIRNP---LLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKE 388
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 76-163 1.16e-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: 81.15  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140   76 DIVTIAKLTLGKKL-NELVYIALADHLHFALERHEKGLEIKNVLLWEIKRLYQDEFSVGLQALELVEEKFNIILPEDEAA 154
Cdd:pfam00874   2 EIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 657228140  155 YIALHIVNA 163
Cdd:pfam00874  82 YIALHFLSA 90
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-55 4.01e-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: 75.97  E-value: 4.01e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 657228140     1 MIIHQIFNNNVISVFDEAGRERVVMGKGIGFKRNSGQAILASDVEKVFYLDDAGN 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-57 5.11e-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 (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: 75.93  E-value: 5.11e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 657228140    2 IIHQIFNNNVISVFDEAGRERVVMGKGIGFKRNSGQAILASDVEKVFYLDDAGNHE 57
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEESE 56
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
43-184 1.27e-16

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 79.78  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  43 DVEKVFYLDDAGNHERFKLLLQEIPEEIIVLTDDIVTIAKLTLGKKLNELVYIALADHLHFALERHEKGLEIKNVLLWEI 122
Cdd:COG3933  430 DVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINPNLNEI 509

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657228140 123 KRLYQDEFSVGLQALELVEEKFNIILPEDEAAYIALHIVNAELNEEMPNIV------------SMTKVIQEVLN 184
Cdd:COG3933  510 KKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKVGvivlahgystasSMAEVANRLLG 583
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 180-273 8.43e-10

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: 54.57  E-value: 8.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  180 QEVLNLVKYHFALEWDENaLAYHRFVTHLKFFAQRLVSRTEYEGDesaLFDLVKMQYPKSYVCTEKIATFIQTKYDYRLT 259
Cdd:pfam00874   1 EEIIELIEKKLGITFDDD-ILYIRLILHLAFAIERIKEGITIENP---LLEEIKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|....
gi 657228140  260 DEEKLYLTVHITRL 273
Cdd:pfam00874  77 EDEIGYIALHFLSA 90
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 37-173 1.64e-09

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: 58.20  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  37 QAILASDVEKVF--YLDDAGNHERFKLLLQEIPEEIIVLTDDIVTIAKLTLGKKLNELVYIALADHLHFALERHEKGLEI 114
Cdd:COG1221  435 NKIISKDIESYFkkLIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKI 514

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 657228140 115 KNVLLWEIKRLYQDEFSVGLQALELVEEKFNIILPEDEAAYIALHIVNAELNEEMPNIV 173
Cdd:COG1221  515 INPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFILLLLIELKEEKSLSENV 573
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
67-156 2.29e-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: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657228140  67 PEEII-VLTDDIVTIAKLtLGKKLNELVYIALADHLHFALER---HEKGLEIKNvlLWEIKRLYQDEFSVGLQALELVEE 142
Cdd:COG3933  820 PEKIInELEDFISRLENL-LGIKLDNDVKIGLILHIACMIERlvtGEEILTYPN--KEEFIQENESEYAVIKEAFSPIEE 896

                         90
                 ....*....|....
gi 657228140 143 KFNIILPEDEAAYI 156
Cdd:COG3933  897 KYNIKIPDSEIAYI 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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