NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1488521179|gb|AYH04733|]
View 

PRD domain-containing protein [Pectobacterium parmentieri]

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
 5-282 1.18e-52

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 172.97  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179   5 IKAIKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKDGTSPREFARLIEHVGEEYVHIVNKIIDD 84
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  85 ANRQLhGRLSEQVFFTLIDHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALNDINQQMTLELPEEEAGNIAFHL 164
Cdd:PRK09772   83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 165 VNAQTDvQNMENTLQSVKMLKDIFNIIQYNFHIVIDKESINYSRFLTHMQFFIQRLLENSLIHSNDDFIFDQVTKEYPDA 244
Cdd:PRK09772  162 VSAQMS-GNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1488521179 245 YKCSRLIKDYIHNLLNIDISNDEMLYLIIHIVRITPEQ 282
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKEH 278
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 5-282 1.18e-52

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 172.97  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179   5 IKAIKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKDGTSPREFARLIEHVGEEYVHIVNKIIDD 84
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  85 ANRQLhGRLSEQVFFTLIDHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALNDINQQMTLELPEEEAGNIAFHL 164
Cdd:PRK09772   83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 165 VNAQTDvQNMENTLQSVKMLKDIFNIIQYNFHIVIDKESINYSRFLTHMQFFIQRLLENSLIHSNDDFIFDQVTKEYPDA 244
Cdd:PRK09772  162 VSAQMS-GNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1488521179 245 YKCSRLIKDYIHNLLNIDISNDEMLYLIIHIVRITPEQ 282
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKEH 278
BglG COG3711
Transcriptional antiterminator [Transcription];
70-282 3.28e-40

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 147.31  E-value: 3.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  70 VGEEYVHIVNKIIDDANRQLHGRLSEQVFFTLIDHISFAIERYRKGISIQ--NRLLYEVKRfyPQEFAIASRALNDINQQ 147
Cdd:COG3711   174 IPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILKLIEER 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 148 MTLELPEEEAGNIAFHLVNAQTDVQNM---ENTLQSVKMLKDIFNIIQYNFHIVIDKESINYSRFLTHMQFFIQRLLENS 224
Cdd:COG3711   252 LGISLPEDEIGYIALHLLGARLNNDNElseIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRLKYGI 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488521179 225 LIHsndDFIFDQVTKEYPDAYKCSRLIKDYIHNLLNIDISNDEMLYLIIHIVRITPEQ 282
Cdd:COG3711   332 PIR---NPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQ 386
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 8-56 1.46e-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 (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: 79.78  E-value: 1.46e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1488521179   8 IKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKD 56
Cdd:pfam03123   3 KKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKD 51
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 6-56 2.53e-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: 79.44  E-value: 2.53e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1488521179    6 KAIKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKD 56
Cdd:smart01061   2 RIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKD 52
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 5-282 1.18e-52

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 172.97  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179   5 IKAIKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKDGTSPREFARLIEHVGEEYVHIVNKIIDD 84
Cdd:PRK09772    3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  85 ANRQLhGRLSEQVFFTLIDHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALNDINQQMTLELPEEEAGNIAFHL 164
Cdd:PRK09772   83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 165 VNAQTDvQNMENTLQSVKMLKDIFNIIQYNFHIVIDKESINYSRFLTHMQFFIQRLLENSLIHSNDDFIFDQVTKEYPDA 244
Cdd:PRK09772  162 VSAQMS-GNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1488521179 245 YKCSRLIKDYIHNLLNIDISNDEMLYLIIHIVRITPEQ 282
Cdd:PRK09772  241 WQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKEH 278
BglG COG3711
Transcriptional antiterminator [Transcription];
70-282 3.28e-40

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 147.31  E-value: 3.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  70 VGEEYVHIVNKIIDDANRQLHGRLSEQVFFTLIDHISFAIERYRKGISIQ--NRLLYEVKRfyPQEFAIASRALNDINQQ 147
Cdd:COG3711   174 IPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEIKK--PKEYEIAKEILKLIEER 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 148 MTLELPEEEAGNIAFHLVNAQTDVQNM---ENTLQSVKMLKDIFNIIQYNFHIVIDKESINYSRFLTHMQFFIQRLLENS 224
Cdd:COG3711   252 LGISLPEDEIGYIALHLLGARLNNDNElseIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAINRLKYGI 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488521179 225 LIHsndDFIFDQVTKEYPDAYKCSRLIKDYIHNLLNIDISNDEMLYLIIHIVRITPEQ 282
Cdd:COG3711   332 PIR---NPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQ 386
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 8-56 1.46e-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 (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: 79.78  E-value: 1.46e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1488521179   8 IKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKD 56
Cdd:pfam03123   3 KKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKD 51
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 6-56 2.53e-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: 79.44  E-value: 2.53e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1488521179    6 KAIKILNNSLVLSSDADNNEIIVMGKGIGFNSKTGDILDPAKIEKTFILKD 56
Cdd:smart01061   2 RIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKD 52
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 79-167 3.78e-14

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: 66.51  E-value: 3.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  79 NKIIDDANRQLHGRL-SEQVFFTLIDHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALNDINQQMTLELPEEEA 157
Cdd:pfam00874   1 EEIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80

                          90
                  ....*....|
gi 1488521179 158 GNIAFHLVNA 167
Cdd:pfam00874  81 GYIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
65-175 3.16e-12

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 66.68  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  65 RLIEHVGEEYVHIVNKIIDDANRQLHGRLSEQVFFTLIDHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALNDI 144
Cdd:COG3933   448 ELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELI 527

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1488521179 145 NQQMTLELPEEEAGNIAFHLVNAQTDVQNME 175
Cdd:COG3933   528 EQELDIEIPEDEVGFLTLFLVSLNENNESGK 558
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 185-277 4.46e-11

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: 58.03  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 185 KDIFNIIQYNFHIVIDKESInYSRFLTHMQFFIQRLLENSLIhsnDDFIFDQVTKEYPDAYKCSRLIKDYIHNLLNIDIS 264
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIL-YIRLILHLAFAIERIKEGITI---ENPLLEEIKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|...
gi 1488521179 265 NDEMLYLIIHIVR 277
Cdd:pfam00874  77 EDEIGYIALHFLS 89
BglG COG3711
Transcriptional antiterminator [Transcription];
66-164 2.52e-10

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 60.64  E-value: 2.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179  66 LIEHVGEEYVHIVNKIIDDANRQLHGRLSE--QVFFTLIDHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALND 143
Cdd:COG3711   279 LSEIITLEITKLIKEIINIIEEELGIDLDEdsLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKY 358

                          90       100
                  ....*....|....*....|.
gi 1488521179 144 INQQMTLELPEEEAGNIAFHL 164
Cdd:COG3711   359 LEKELGIEIPEDEIGYLTLHF 379
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
183-276 4.47e-04

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 41.64  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488521179 183 MLKDIFNIIQYNFHIVIDKESINYS-RFLTHMQFFIQRLLE-----NSLIHSNDDFIfdqvTKEYPDAYKCSRLIKDYIH 256
Cdd:COG3933   453 VDEDIINVVEEILELAEKKLGRKFSeNFIYALSLHLSSFIErikegKEIINPNLNEI----KKKYPKEFKVAKEIKELIE 528

                          90       100
                  ....*....|....*....|
gi 1488521179 257 NLLNIDISNDEMLYLIIHIV 276
Cdd:COG3933   529 QELDIEIPEDEVGFLTLFLV 548
PRK11564 PRK11564
stationary phase inducible protein CsiE; Provisional
 93-161 1.68e-03

stationary phase inducible protein CsiE; Provisional


Pssm-ID: 236932 [Multi-domain]  Cd Length: 426  Bit Score: 39.61  E-value: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488521179  93 LSEQVFFtlidHISFAIERYRKGISIQNRLLYEVKRFYPQEFAIASRALNDINQQMTLELPEEEAGNIA 161
Cdd:PRK11564  259 LCDQLYT----HLAQALERSLFAIGIDNTLPEEFARLYPRLLRTTRAALAGFEQEYGVHFSDEEVGLVA 323
 
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