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Conserved domains on  [gi|253795455|ref|NP_001156714|]
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ribosyldihydronicotinamide dehydrogenase [quinone] isoform 1 [Mus musculus]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10006206)

NAD(P)H-dependent oxidoreductase which catalyzes the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P)+; similar to Escherichia coli NADPH:quinone oxidoreductase MdaB

CATH:  3.40.50.360
EC:  1.6.99.-|1.-.-.-
Gene Ontology:  GO:0008753|GO:0009055|GO:0010181
PubMed:  25372605|24699637|16630630|7568029
SCOP:  3001217

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-216 5.19e-75

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 225.10  E-value: 5.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKSFNGSLKKVAVEELSKQGCTVTVSDLYSMNFEPRATRNDItgapsnpdvfsygietheaYKKKALTSD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455  85 IFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIPGFYDSGFLKGKLALLSLTTGGTAEMYTKDGVSGD 164
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 253795455 165 FRYFlwpLQHGTLHFCGFKVLAPQISFGLDVSSEEERKVMLASWAQRLKSIW 216
Cdd:COG2249  142 IEEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-216 5.19e-75

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 225.10  E-value: 5.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKSFNGSLKKVAVEELSKQGCTVTVSDLYSMNFEPRATRNDItgapsnpdvfsygietheaYKKKALTSD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455  85 IFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIPGFYDSGFLKGKLALLSLTTGGTAEMYTKDGVSGD 164
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 253795455 165 FRYFlwpLQHGTLHFCGFKVLAPQISFGLDVSSEEERKVMLASWAQRLKSIW 216
Cdd:COG2249  142 IEEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 4-212 2.87e-61

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 190.24  E-value: 2.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455    4 KKVLIVYAHQEPKSFNGSLKKVAVEELSKQGCTVTVSDLYSMnFEPRATRNDITGapsnpdvfsygiethEAYKKKALts 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD---------------LTYPQGAA-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   84 DIFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIP-GFYDSGFLKGKLALLSLTTGGTAEMYTKDGVS 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 253795455  163 G-DFRYFLWPLqHGTLHFCGFKVLAPQISFGLDV-SSEEERKVMLASWAQRL 212
Cdd:pfam02525 143 GfSLDELLPYL-RGILGFCGITDLPPFAVEGTAGpEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 5-160 5.40e-23

glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 91.60  E-value: 5.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKS--FNGSLKKvAVEELSKqgctVTVSDLYSmnfepratrnditgapSNPDVFsygIetheaykkkalt 82
Cdd:PRK04930   7 KVLLLYAHPESQDsvANRVLLK-PAQQLEH----VTVHDLYA----------------HYPDFF---I------------ 50

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253795455  83 sDIFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIPGfydsGFLKGKLALLSLTTGGTAEMYTKDG 160
Cdd:PRK04930  51 -DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDG 123
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-216 5.19e-75

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 225.10  E-value: 5.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKSFNGSLKKVAVEELSKQGCTVTVSDLYSMNFEPRATRNDItgapsnpdvfsygietheaYKKKALTSD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455  85 IFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIPGFYDSGFLKGKLALLSLTTGGTAEMYTKDGVSGD 164
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 253795455 165 FRYFlwpLQHGTLHFCGFKVLAPQISFGLDVSSEEERKVMLASWAQRLKSIW 216
Cdd:COG2249  142 IEEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 4-212 2.87e-61

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 190.24  E-value: 2.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455    4 KKVLIVYAHQEPKSFNGSLKKVAVEELSKQGCTVTVSDLYSMnFEPRATRNDITGapsnpdvfsygiethEAYKKKALts 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD---------------LTYPQGAA-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   84 DIFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIP-GFYDSGFLKGKLALLSLTTGGTAEMYTKDGVS 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 253795455  163 G-DFRYFLWPLqHGTLHFCGFKVLAPQISFGLDV-SSEEERKVMLASWAQRL 212
Cdd:pfam02525 143 GfSLDELLPYL-RGILGFCGITDLPPFAVEGTAGpEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 5-160 5.40e-23

glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 91.60  E-value: 5.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKS--FNGSLKKvAVEELSKqgctVTVSDLYSmnfepratrnditgapSNPDVFsygIetheaykkkalt 82
Cdd:PRK04930   7 KVLLLYAHPESQDsvANRVLLK-PAQQLEH----VTVHDLYA----------------HYPDFF---I------------ 50

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253795455  83 sDIFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIPGfydsGFLKGKLALLSLTTGGTAEMYTKDG 160
Cdd:PRK04930  51 -DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDG 123
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-127 1.10e-18

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 80.52  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   1 MAGKKVLIVYAHQEPKSFNGSLKKVAVEELSKQGCTVTVSDLYSMNFEPRATRNDitgAP--SNPDvfsygietheaykk 78
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPED---EPdwKNPD-------------- 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 253795455  79 KALTSDIFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAF 127
Cdd:PRK09739  64 KRYSPEVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
84-218 1.23e-15

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 72.13  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455  84 DIFEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDIPGFYdsgfLKGKLALLSLTTGGtAEMYTKDGVSG 163
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGGTA----LHGKHLLWAVTTGG-GESHFEIGAHP 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 253795455 164 DFRYFLWPLQhGTLHFCGFKVLAPQISFGLDVSSEEERKVMLASWAQRLKSiWKE 218
Cdd:PRK00871 120 GFDVLSQPLQ-ATALYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLE-WQE 172
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
4-152 1.20e-09

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 55.91  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   4 KKVLIVYAH-QEPKSFNGSLKKVAVEELSKQ--GCTVTVSDLYSMNFePRATRNDITGAPSNPDVFSygiethEAYKKKA 80
Cdd:COG1182    2 MKLLHIDSSpRGEGSVSRRLADAFVAALRAAhpDDEVTYRDLAAEPL-PHLDGAWLAAFFTPAEGRT------PEQQAAL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253795455  81 LTSD-IFEEqrkVQEADLVIFQFPLYWFSVPAILKGWMDRVLCRG--FAFDIPGFydSGFLKGKLALLSLTTGGT 152
Cdd:COG1182   75 ALSDeLIDE---LLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGrtFRYTENGP--VGLLTGKKAVVITARGGV 144
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 5-213 4.00e-08

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 51.47  E-value: 4.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAhqEPKSfNGS---LKKVAVEELSKQGCTVTVSDLYSMNFEPRatrnditgapsnpdvfsygieTHEAYKKKAL 81
Cdd:COG0655    1 KILVING--SPRK-NGNtaaLAEAVAEGAEEAGAEVELIRLADLDIKPC---------------------IGCGGTGKCV 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455  82 TSDIFEEQR-KVQEADLVIFQFPLYWFSVPAILKGWMDRvlCRGFAFDIpgfydsGFLKGKLALLsLTTGGTAEmytKDG 160
Cdd:COG0655   57 IKDDMNAIYeKLLEADGIIFGSPTYFGNMSAQLKAFIDR--LYALWAKG------KLLKGKVGAV-FTTGGHGG---AEA 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455 161 VSGDFRYFLwpLQHGtLHFCG-FKVLAPQISFGLDVSSEEERKVM------LASWAQRLK 213
Cdd:COG0655  125 TLLSLNTFL--LHHG-MIVVGlPPYGAVGGGGPGDVLDEEGLATArelgkrLAELAKKLK 181
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-153 4.37e-08

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 50.70  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455    5 KVLIVYAHQEPKSFNGSLKKVAVEELsKQGCTVTVSDLYSMNFePRATRNDITGAPSNPDVfsygietheaykkKALTsd 84
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELL-EEGAEVELIDLADLIL-PLCDEDLEEEQGDPDDV-------------QELR-- 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 253795455   85 ifeeqRKVQEADLVIFQFPLYWFSVPAILKGWMDRVlcrgfafdiPGFYDSGFLKGKLALLsLTTGGTA 153
Cdd:pfam03358  65 -----EKIAAADAIIIVTPEYNGSVSGLLKNAIDWL---------SRLRGGKELRGKPVAI-VSTGGGR 118
PRK00170 PRK00170
azoreductase; Reviewed
 87-163 3.26e-06

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 46.04  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455  87 EEQRKV----------QEADLVIFQFPLYWFSVPAILKGWMDRVLCRGFAFDipgfYDS----GFLKGKLALLSLTTGGt 152
Cdd:PRK00170  69 RQQEAValsdelleefLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFR----YTEngpvGLVTGKKALLITSRGG- 143

                         90
                 ....*....|.
gi 253795455 153 aemYTKDGVSG 163
Cdd:PRK00170 144 ---IHKDGPTD 151
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
5-118 1.08e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 42.06  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKSFNGSLKK----VAVEELSKQGCTVTVSDLYSMNFePRATRNDITGapsnpdVF--SYGIETHEAYKK 78
Cdd:PRK13556   3 KVLFVKANNRPAEQAVSVKLyeafLASYKEAHPNDTVVELDLYKEEL-PYVGVDMING------TFkaGKGFELTEEEAK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 253795455  79 KALTSDIFEEQrkVQEADLVIFQFPLYWFSVPAILKGWMD 118
Cdd:PRK13556  76 AVAVADKYLNQ--FLEADKVVFAFPLWNFTIPAVLHTYID 113
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
5-113 6.58e-03

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 36.64  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253795455   5 KVLIVYAHQEPKSFNGSLKK----VAVEELSKQGCTVTVSDLYSMNFePRATRNDITGAPSNpdvfSYGIETHEAYKKKA 80
Cdd:PRK13555   3 KVLFVKANDRPAEQAVSSKMyetfVSTYKEANPNTEITELDLFALDL-PYYGNIAISGGYKR----SQGMELTAEEEKAV 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 253795455  81 LTSDIFEEQrkVQEADLVIFQFPLYWFSVPAIL 113
Cdd:PRK13555  78 ATVDQYLNQ--FLEADKVVFAFPLWNFTVPAPL 108
 
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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