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Conserved domains on  [gi|1958700389|ref|XP_038951418|]
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ribosyldihydronicotinamide dehydrogenase [quinone] isoform X1 [Rattus norvegicus]

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)+

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0009055|GO:0050136|GO:0008753|GO:0010181
PubMed:  25372605|7568029
SCOP:  3001217

Graphical summary

 Zoom to residue level

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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 9.37e-74

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 222.02  E-value: 9.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvtgalsnpevfkygieayeAYKKKALTSD 84
Cdd:COG2249     1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD-------------------FYRDGPLPID 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  85 ILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGD 164
Cdd:COG2249    62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958700389 165 FRYFlwpLQHGTLHFCGFKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIW 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 9.37e-74

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 222.02  E-value: 9.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvtgalsnpevfkygieayeAYKKKALTSD 84
Cdd:COG2249     1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD-------------------FYRDGPLPID 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  85 ILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGD 164
Cdd:COG2249    62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958700389 165 FRYFlwpLQHGTLHFCGFKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIW 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 8.67e-60

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: 186.39  E-value: 8.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   4 KKVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMnFEPRATRNDVTgALSNPEVFKygieayeaykkkalts 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLA-DLTYPQGAA---------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  84 DILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVP-GFYDSGFLKDKLALLSFTTGGTAEMYTKAGVN 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958700389 163 G-DFRYFLWPLqHGTLHFCGFKVLAPQISFG-PEVSSEEQRKVMLASWVQRL 212
Cdd:pfam02525 143 GfSLDELLPYL-RGILGFCGITDLPPFAVEGtAGPEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 5-167 2.42e-21

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 87.37  E-value: 2.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKS--FNGSMKQvAVEELSKqgctVTVSDLYtmnfeprATRndvtgalsnPEVFkygIeayeaykkkalt 82
Cdd:PRK04930    7 KVLLLYAHPESQDsvANRVLLK-PAQQLEH----VTVHDLY-------AHY---------PDFF---I------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  83 sDILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGfydsGFLKDKLALLSFTTGGTAEMYTKAGVN 162
Cdd:PRK04930   51 -DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDGYN 125


                  ....*
gi 1958700389 163 gdfRY 167
Cdd:PRK04930  126 ---RY 127
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-216 9.37e-74

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 222.02  E-value: 9.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvtgalsnpevfkygieayeAYKKKALTSD 84
Cdd:COG2249     1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD-------------------FYRDGPLPID 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  85 ILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGD 164
Cdd:COG2249    62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958700389 165 FRYFlwpLQHGTLHFCGFKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIW 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 8.67e-60

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: 186.39  E-value: 8.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   4 KKVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMnFEPRATRNDVTgALSNPEVFKygieayeaykkkalts 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLA-DLTYPQGAA---------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  84 DILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVP-GFYDSGFLKDKLALLSFTTGGTAEMYTKAGVN 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958700389 163 G-DFRYFLWPLqHGTLHFCGFKVLAPQISFG-PEVSSEEQRKVMLASWVQRL 212
Cdd:pfam02525 143 GfSLDELLPYL-RGILGFCGITDLPPFAVEGtAGPEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 5-167 2.42e-21

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 87.37  E-value: 2.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKS--FNGSMKQvAVEELSKqgctVTVSDLYtmnfeprATRndvtgalsnPEVFkygIeayeaykkkalt 82
Cdd:PRK04930    7 KVLLLYAHPESQDsvANRVLLK-PAQQLEH----VTVHDLY-------AHY---------PDFF---I------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  83 sDILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGfydsGFLKDKLALLSFTTGGTAEMYTKAGVN 162
Cdd:PRK04930   51 -DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDGYN 125


                  ....*
gi 1958700389 163 gdfRY 167
Cdd:PRK04930  126 ---RY 127
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-160 1.16e-19

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 83.21  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   1 MAGKKVLLVYAHQEPKSFNGSMKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvTGALSNPEvfkygieayeaykkKA 80
Cdd:PRK09739    1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPED-EPDWKNPD--------------KR 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  81 LTSDILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDvpgfyDSGFLKDKLALLSFTTGGTAEMYTKAG 160
Cdd:PRK09739   66 YSPEVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYG-----DGHKLPFNKVRWVALVGGSKESFVKRG 140
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
84-218 1.89e-15

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 71.35  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  84 DILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYdsgfLKDKLALLSFTTGGtAEMYTKAGVNG 163
Cdd:PRK00871   45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGGTA----LHGKHLLWAVTTGG-GESHFEIGAHP 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958700389 164 DFRYFLWPLQhGTLHFCGFKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSiWKE 218
Cdd:PRK00871  120 GFDVLSQPLQ-ATALYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLE-WQE 172
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
4-202 2.46e-09

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 55.14  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   4 KKVLLVYAHqePKSFNGSMKQVA---VEELSKQ--GCTVTVSDLYTMNFePRATrNDVTGALSNPEvfkygiEAYEAYKK 78
Cdd:COG1182     2 MKLLHIDSS--PRGEGSVSRRLAdafVAALRAAhpDDEVTYRDLAAEPL-PHLD-GAWLAAFFTPA------EGRTPEQQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389  79 KALT-SDILEEQrkVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQG--FAFDVPGFydSGFLKDKLALLSFTTGGTaem 155
Cdd:COG1182    72 AALAlSDELIDE--LLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGrtFRYTENGP--VGLLTGKKAVVITARGGV--- 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958700389 156 YTKAGVNG-DF--RYflwpLQHgTLHFCGFK----VLAPQISFGPEVSSEEQRK 202
Cdd:COG1182   145 YSGGPAAGmDFqtPY----LRT-VLGFIGITdvefVRAEGTAAGPEAAEAALAA 193
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 5-152 6.27e-08

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 50.70  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAhqEPKSfNGS---MKQVAVEELSKQGCTVTVSDLYTMNFEPratrndvtgalsnpevfkygIEAYEAYKKKAL 81
Cdd:COG0655     1 KILVING--SPRK-NGNtaaLAEAVAEGAEEAGAEVELIRLADLDIKP--------------------CIGCGGTGKCVI 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958700389  82 TSDILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRvlCQGFAFDVpgfydsGFLKDKLALLsFTTGGT 152
Cdd:COG0655    58 KDDMNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDR--LYALWAKG------KLLKGKVGAV-FTTGGH 119
PRK00170 PRK00170
azoreductase; Reviewed
 80-151 1.01e-06

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.58  E-value: 1.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958700389  80 ALTSDILEEqrkVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDvpgfYDS----GFLKDKLALLSFTTGG 151
Cdd:PRK00170   75 ALSDELLEE---FLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFR----YTEngpvGLVTGKKALLITSRGG 143
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-153 7.40e-06

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 44.54  E-value: 7.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKSFNGSMKQVAVEELsKQGCTVTVSDLYTMNFePRATRNDVTGALSNPEVfkygieayeaykkKALTsd 84
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELL-EEGAEVELIDLADLIL-PLCDEDLEEEQGDPDDV-------------QELR-- 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958700389  85 ileeqRKVQEADLVIFQFPLYWFSVPAILKGWMDRvlcqgfafdVPGFYDSGFLKDKLALLsFTTGGTA 153
Cdd:pfam03358  65 -----EKIAAADAIIIVTPEYNGSVSGLLKNAIDW---------LSRLRGGKELRGKPVAI-VSTGGGR 118
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
5-146 2.53e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 40.90  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958700389   5 KVLLVYAHQEPKSFNGSMKQ----VAVEELSKQGCTVTVSDLYTMNFePRATRNDVTGalsnpeVFK--YGIEAYEAYKK 78
Cdd:PRK13556    3 KVLFVKANNRPAEQAVSVKLyeafLASYKEAHPNDTVVELDLYKEEL-PYVGVDMING------TFKagKGFELTEEEAK 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958700389  79 KALTSDILEEQrkVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKD-KLALLS 146
Cdd:PRK13556   76 AVAVADKYLNQ--FLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDkKVALLN 142
 
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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