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Conserved domains on  [gi|156564357|ref|NP_000895|]
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ribosyldihydronicotinamide dehydrogenase [quinone] isoform 1 [Homo sapiens]

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 6.12e-74

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 222.41  E-value: 6.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNlepratdkditgtlsnpevFNYGVETHEAYKQRSLASD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEG-------------------FDPVLSAADFYRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  85 ITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGD 164
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156564357 165 SRYFlwpLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIW 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 6.12e-74

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 222.41  E-value: 6.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNlepratdkditgtlsnpevFNYGVETHEAYKQRSLASD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEG-------------------FDPVLSAADFYRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  85 ITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGD 164
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156564357 165 SRYFlwpLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIW 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 1.22e-62

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: 193.70  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357    4 KKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLePRATDKDITGtLSNPEVfnygvetheaykqrslAS 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYALFL-PVLDAEDLAD-LTYPQG----------------AA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   84 DITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIP-GFYDSGLLQGKLALLSVTTGGTAEMYTKTGVN 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156564357  163 GDS-RYFLWPLqHGTLHFCGFKVLAPQISF-APEIASEEERKGMVAAWSQRL 212
Cdd:pfam02525 143 GFSlDELLPYL-RGILGFCGITDLPPFAVEgTAGPEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 5-222 2.86e-25

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 97.77  E-value: 2.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSfngSLKNVAVDELSRQGCTVTVSDLYAmnlepratdkditgtlSNPEVFnygvetheaykqrslaSD 84
Cdd:PRK04930   7 KVLLLYAHPESQD---SVANRVLLKPAQQLEHVTVHDLYA----------------HYPDFF----------------ID 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  85 ITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGfydsGLLQGKLALLSVTTGGTAEMYTKTGVNgd 164
Cdd:PRK04930  52 IPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDGYN-- 125

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564357 165 sRY----FLWPLQHgTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQrlqtiWKEEPIP 222
Cdd:PRK04930 126 -RYpmsdILRPFEL-TAAMCRMHWLSPIIIYWARRQSPEELASHARAYGD-----WLANPLS 180
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-216 6.12e-74

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 222.41  E-value: 6.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNlepratdkditgtlsnpevFNYGVETHEAYKQRSLASD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEG-------------------FDPVLSAADFYRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  85 ITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGD 164
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156564357 165 SRYFlwpLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIW 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 1.22e-62

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: 193.70  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357    4 KKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLePRATDKDITGtLSNPEVfnygvetheaykqrslAS 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYALFL-PVLDAEDLAD-LTYPQG----------------AA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   84 DITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIP-GFYDSGLLQGKLALLSVTTGGTAEMYTKTGVN 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156564357  163 GDS-RYFLWPLqHGTLHFCGFKVLAPQISF-APEIASEEERKGMVAAWSQRL 212
Cdd:pfam02525 143 GFSlDELLPYL-RGILGFCGITDLPPFAVEgTAGPEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 5-222 2.86e-25

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 97.77  E-value: 2.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSfngSLKNVAVDELSRQGCTVTVSDLYAmnlepratdkditgtlSNPEVFnygvetheaykqrslaSD 84
Cdd:PRK04930   7 KVLLLYAHPESQD---SVANRVLLKPAQQLEHVTVHDLYA----------------HYPDFF----------------ID 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  85 ITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGfydsGLLQGKLALLSVTTGGTAEMYTKTGVNgd 164
Cdd:PRK04930  52 IPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDGYN-- 125

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156564357 165 sRY----FLWPLQHgTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQrlqtiWKEEPIP 222
Cdd:PRK04930 126 -RYpmsdILRPFEL-TAAMCRMHWLSPIIIYWARRQSPEELASHARAYGD-----WLANPLS 180
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-127 5.07e-17

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 76.28  E-value: 5.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   1 MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDitgtlsNPEVFNygveTHEAYkqrs 80
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPED------EPDWKN----PDKRY---- 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 156564357  81 lASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAF 127
Cdd:PRK09739  67 -SPEVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
84-218 2.13e-16

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 74.05  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  84 DITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGfydsGLLQGKLALLSVTTGGtAEMYTKTGVNG 163
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGG----TALHGKHLLWAVTTGG-GESHFEIGAHP 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156564357 164 DSRYFLWPLQhGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTiWKE 218
Cdd:PRK00871 120 GFDVLSQPLQ-ATALYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLE-WQE 172
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
4-152 3.09e-11

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 60.53  E-value: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   4 KKVLIVYAH-QEPKSFNGSLKNVAVDELSRQ--GCTVTVSDLYAMNLEPraTDKDITGTLSNPEvfnygvETHEAYKQRS 80
Cdd:COG1182    2 MKLLHIDSSpRGEGSVSRRLADAFVAALRAAhpDDEVTYRDLAAEPLPH--LDGAWLAAFFTPA------EGRTPEQQAA 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156564357  81 LA-SD-ITDEqkkVREADLVIFQFPLYWFSVPAILKGWMDRVLCQG--FAFDIPGFydSGLLQGKLALLSVTTGGT 152
Cdd:COG1182   74 LAlSDeLIDE---LLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGrtFRYTENGP--VGLLTGKKAVVITARGGV 144
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-153 1.02e-08

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 52.63  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357    5 KVLIVYAHQEPKSFNGSLKNVAVDELsRQGCTVTVSDLYAMNLEPRatDKDITGTLSNPEvfnygvetheaykqrslasD 84
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELL-EEGAEVELIDLADLILPLC--DEDLEEEQGDPD-------------------D 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156564357   85 ITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVlcqgfafdiPGFYDSGLLQGKLALLsVTTGGTA 153
Cdd:pfam03358  60 VQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDWL---------SRLRGGKELRGKPVAI-VSTGGGR 118
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 5-152 5.68e-07

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 48.00  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAhqEPKSfNGS---LKNVAVDELSRQGCTVTVSDLYAMNLEPratdkdITGTLSNPEVFnygvetheaykqrsL 81
Cdd:COG0655    1 KILVING--SPRK-NGNtaaLAEAVAEGAEEAGAEVELIRLADLDIKP------CIGCGGTGKCV--------------I 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156564357  82 ASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRvlCQGFAFDIpgfydsGLLQGKLALLsVTTGGT 152
Cdd:COG0655   58 KDDMNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDR--LYALWAKG------KLLKGKVGAV-FTTGGH 119
PRK00170 PRK00170
azoreductase; Reviewed
 36-151 6.96e-07

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.97  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  36 TVTVSDLYAMNLePrATDKDITGTLSNPEvfnygvETHEAYKQRSLA-SDITDEQKKvrEADLVIFQFPLYWFSVPAILK 114
Cdd:PRK00170  37 EVTVRDLAAEPI-P-VLDGEVVGALGKSA------ETLTPRQQEAVAlSDELLEEFL--AADKIVIAAPMYNFSIPTQLK 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 156564357 115 GWMDRVLCQGFAFDipgfYDS----GLLQGKLALLSVTTGG 151
Cdd:PRK00170 107 AYIDLIARAGKTFR----YTEngpvGLVTGKKALLITSRGG 143
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-192 9.87e-05

NAD(P)H-dependent FMN reductase [Energy production and conversion];


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 41.29  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   4 KKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPraTDKDITGTLSNPEVfnygvetheaykqRSLAs 83
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPL--YDEDLEADGAPPAV-------------KALR- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357  84 ditdeqKKVREADLVIFQFPLYWFSVPAILKGwmdrvlcqgfAFDipgFYDSGLLQGKLALLsVTTGGTAemytktgvng 163
Cdd:COG0431   65 ------EAIAAADGVVIVTPEYNGSYPGVLKN----------ALD---WLSRSELAGKPVAL-VSTSGGA---------- 114

                        170       180       190
                 ....*....|....*....|....*....|.
gi 156564357 164 dsRYFLWPLQH--GTLHFCGFKVLAPQISFA 192
Cdd:COG0431  115 --RGGLRALEHlrPVLSELGAVVLPPQVSIP 143
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
5-154 1.00e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 42.06  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSFNGSLKN----VAVDELSRQGCTVTVSDLYAMNLePRATDKDITGTLSNPEvfnyGVE-THEAYKQR 79
Cdd:PRK13556   3 KVLFVKANNRPAEQAVSVKLyeafLASYKEAHPNDTVVELDLYKEEL-PYVGVDMINGTFKAGK----GFElTEEEAKAV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156564357  80 SLASDITDEqkkVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQG-KLALLSVTTGGTAE 154
Cdd:PRK13556  78 AVADKYLNQ---FLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDkKVALLNARGGVYSE 150
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
5-141 5.78e-03

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 36.64  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564357   5 KVLIVYAHQEPKSFNGSLKN----VAVDELSRQGCTVTVSDLYAMNLePRATDKDITGTLSNPEVFNYGVETHEAykqrs 80
Cdd:PRK13555   3 KVLFVKANDRPAEQAVSSKMyetfVSTYKEANPNTEITELDLFALDL-PYYGNIAISGGYKRSQGMELTAEEEKA----- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156564357  81 lASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGK 141
Cdd:PRK13555  77 -VATVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGK 136
 
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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