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Conserved domains on  [gi|645251442|ref|XP_008231680|]
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PREDICTED: NADPH:quinone oxidoreductase-like [Prunus mume]

Protein Classification

NADPH-dependent FMN reductase( domain architecture ID 10001414)

NAD(P)H-dependent FMN reductase may carry out reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor, such as catalyzing the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
13-179 6.10e-41

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 136.05  E-value: 6.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  13 IKVAAICGSLREGSYNRGLIRSAIEISKSsiPGVEIEHVEIAE--LPLLNTDLEGEGsFPPVVEAFRQKILEADSILFAS 90
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRDldLPLYDEDLEADG-APPAVKALREAIAAADGVVIVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  91 PEYNYSVSAPLKNALDWASRppNVWGDKaaaii-sasgGSGGSRSQYHLRQIGVFLDLHFINkPEFFLNAFQppAKFDKN 169
Cdd:COG0431   78 PEYNGSYPGVLKNALDWLSR--SELAGKpvalvstsggARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAG--EAFDED 152
                        170
                 ....*....|
gi 645251442 170 SNLIDAKTRE 179
Cdd:COG0431  153 GELTDEELAE 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
13-179 6.10e-41

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 136.05  E-value: 6.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  13 IKVAAICGSLREGSYNRGLIRSAIEISKSsiPGVEIEHVEIAE--LPLLNTDLEGEGsFPPVVEAFRQKILEADSILFAS 90
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRDldLPLYDEDLEADG-APPAVKALREAIAAADGVVIVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  91 PEYNYSVSAPLKNALDWASRppNVWGDKaaaii-sasgGSGGSRSQYHLRQIGVFLDLHFINkPEFFLNAFQppAKFDKN 169
Cdd:COG0431   78 PEYNGSYPGVLKNALDWLSR--SELAGKpvalvstsggARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAG--EAFDED 152
                        170
                 ....*....|
gi 645251442 170 SNLIDAKTRE 179
Cdd:COG0431  153 GELTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
13-160 1.33e-38

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 130.05  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442   13 IKVAAICGSLREGSYNRGLIRSAIEISKssiPGVEIEHVEIAE--LPLLNTDLEGEGSFPPVVEAFRQKILEADSILFAS 90
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLE---EGAEVELIDLADliLPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 645251442   91 PEYNYSVSAPLKNALDWASRPPN--VWGDKAAAIISASGGSG-GSRSQYHLRQIGVFLDLHFINKPEFFLNAF 160
Cdd:pfam03358  78 PEYNGSVSGLLKNAIDWLSRLRGgkELRGKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPSGQVAVGNA 150
PRK00170 PRK00170
azoreductase; Reviewed
14-111 5.75e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 42.19  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  14 KVAAICGSLREG-SYNRGLIRSAIEISKSSIPGVEIEHVEIAE--LPLLNTD-LEGEGSFPPVVEAfRQK---------- 79
Cdd:PRK00170   3 KVLVIKSSILGDySQSMQLGDAFIEAYKEAHPDDEVTVRDLAAepIPVLDGEvVGALGKSAETLTP-RQQeavalsdell 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 645251442  80 --ILEADSILFASPEYNYSVSAPLKNALDWASRP 111
Cdd:PRK00170  82 eeFLAADKIVIAAPMYNFSIPTQLKAYIDLIARA 115
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
13-179 6.10e-41

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 136.05  E-value: 6.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  13 IKVAAICGSLREGSYNRGLIRSAIEISKSsiPGVEIEHVEIAE--LPLLNTDLEGEGsFPPVVEAFRQKILEADSILFAS 90
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRDldLPLYDEDLEADG-APPAVKALREAIAAADGVVIVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  91 PEYNYSVSAPLKNALDWASRppNVWGDKaaaii-sasgGSGGSRSQYHLRQIGVFLDLHFINkPEFFLNAFQppAKFDKN 169
Cdd:COG0431   78 PEYNGSYPGVLKNALDWLSR--SELAGKpvalvstsggARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAG--EAFDED 152
                        170
                 ....*....|
gi 645251442 170 SNLIDAKTRE 179
Cdd:COG0431  153 GELTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
13-160 1.33e-38

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 130.05  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442   13 IKVAAICGSLREGSYNRGLIRSAIEISKssiPGVEIEHVEIAE--LPLLNTDLEGEGSFPPVVEAFRQKILEADSILFAS 90
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLE---EGAEVELIDLADliLPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 645251442   91 PEYNYSVSAPLKNALDWASRPPN--VWGDKAAAIISASGGSG-GSRSQYHLRQIGVFLDLHFINKPEFFLNAF 160
Cdd:pfam03358  78 PEYNGSVSGLLKNAIDWLSRLRGgkELRGKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPSGQVAVGNA 150
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
14-106 3.61e-15

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 69.96  E-value: 3.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  14 KVAAICGSLREGSYNRGLIRSAIEISKSsiPGVEIEHVEIAEL---PLLNTDLEGEGSFPPVVEAFRQKILEADSILFAS 90
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEE--AGAEVELIRLADLdikPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFGS 78
                         90
                 ....*....|....*.
gi 645251442  91 PEYNYSVSAPLKNALD 106
Cdd:COG0655   79 PTYFGNMSAQLKAFID 94
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
14-106 4.68e-10

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: 56.57  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442   14 KVAAICGSLREGSYNRGLIRSAIEISKSSipGVEIEHVEIAE--LPLLNTDLEGEGS---FPPVVEAFRQKILEADSILF 88
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAA--GHEVTVRDLYAlfLPVLDAEDLADLTypqGAADVESEQEELLAADVIVF 79
                          90
                  ....*....|....*...
gi 645251442   89 ASPEYNYSVSAPLKNALD 106
Cdd:pfam02525  80 QFPLYWFSVPALLKGWID 97
PRK00170 PRK00170
azoreductase; Reviewed
14-111 5.75e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 42.19  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  14 KVAAICGSLREG-SYNRGLIRSAIEISKSSIPGVEIEHVEIAE--LPLLNTD-LEGEGSFPPVVEAfRQK---------- 79
Cdd:PRK00170   3 KVLVIKSSILGDySQSMQLGDAFIEAYKEAHPDDEVTVRDLAAepIPVLDGEvVGALGKSAETLTP-RQQeavalsdell 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 645251442  80 --ILEADSILFASPEYNYSVSAPLKNALDWASRP 111
Cdd:PRK00170  82 eeFLAADKIVIAAPMYNFSIPTQLKAYIDLIARA 115
PRK01355 PRK01355
azoreductase; Reviewed
14-106 4.98e-03

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 36.60  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645251442  14 KVAAICGSL--REGSYNRGLIRSAIEISKSSIPGVEIEHVEIAELPLLNTDLEGEgSFPP-----VVEAFRQKILEADSI 86
Cdd:PRK01355   3 KVLVIKGSMvaKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETKVGSVTLTSE-NFKTffkeeVSDKYINQLKSVDKV 81
                         90       100
                 ....*....|....*....|
gi 645251442  87 LFASPEYNYSVSAPLKNALD 106
Cdd:PRK01355  82 VISCPMTNFNVPATLKNYLD 101
 
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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