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Conserved domains on  [gi|15600168|ref|NP_253662|]
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NAD(P)H quinone oxidoreductase [Pseudomonas aeruginosa PAO1]

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 ...
 2-211 3.61e-77

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 230.88  E-value: 3.61e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   2 NVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMNWNPVASAADFAERadpdylvyaleqresvkrQSLAADI 81
Cdd:COG2249   1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYRD------------------GPLPIDV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168  82 QAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGGKRFYDQGGLAGKKALVSLTLGGRQHMFGEGAIHGPL 161
Cdd:COG2249  63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15600168 162 EDMLrpiLRGTLAYVGMQVLEPFVAWHVPYISEEARGNFLRAYRARLENL 211
Cdd:COG2249 143 EELL---FRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAAL 189
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-211 3.61e-77

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 230.88  E-value: 3.61e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   2 NVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMNWNPVASAADFAERadpdylvyaleqresvkrQSLAADI 81
Cdd:COG2249   1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYRD------------------GPLPIDV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168  82 QAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGGKRFYDQGGLAGKKALVSLTLGGRQHMFGEGAIHGPL 161
Cdd:COG2249  63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15600168 162 EDMLrpiLRGTLAYVGMQVLEPFVAWHVPYISEEARGNFLRAYRARLENL 211
Cdd:COG2249 143 EELL---FRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAAL 189
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-208 3.81e-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: 187.54  E-value: 3.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168     1 MNVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMnWNPVASAADFAERADPDYlvyaleqresvkrqslAAD 80
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLADLTYPQG----------------AAD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYG-GKRFYDQGGLAGKKALVSLTLGGRQHMFGEGAIHG 159
Cdd:pfam02525  64 VESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKyEEGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNG 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15600168   160 -PLEDMLRPiLRGTLAYVGMQVLEPFVAWHVPYIS-EEARGNFLRAYRARL 208
Cdd:pfam02525 144 fSLDELLPY-LRGILGFCGITDLPPFAVEGTAGPEdEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-151 3.33e-21

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 87.45  E-value: 3.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    1 MNVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMNWNPVASAADFAERADPDylvyaleqresvKRQSlaAD 80
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPD------------KRYS--PE 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600168   81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGGKRfydqgGLAGKKAL-VSLTLGGRQHM 151
Cdd:PRK09739  70 VHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGH-----KLPFNKVRwVALVGGSKESF 136
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-211 3.61e-77

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 230.88  E-value: 3.61e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   2 NVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMNWNPVASAADFAERadpdylvyaleqresvkrQSLAADI 81
Cdd:COG2249   1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYRD------------------GPLPIDV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168  82 QAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGGKRFYDQGGLAGKKALVSLTLGGRQHMFGEGAIHGPL 161
Cdd:COG2249  63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15600168 162 EDMLrpiLRGTLAYVGMQVLEPFVAWHVPYISEEARGNFLRAYRARLENL 211
Cdd:COG2249 143 EELL---FRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAAL 189
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-208 3.81e-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: 187.54  E-value: 3.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168     1 MNVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMnWNPVASAADFAERADPDYlvyaleqresvkrqslAAD 80
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLADLTYPQG----------------AAD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYG-GKRFYDQGGLAGKKALVSLTLGGRQHMFGEGAIHG 159
Cdd:pfam02525  64 VESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKyEEGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNG 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15600168   160 -PLEDMLRPiLRGTLAYVGMQVLEPFVAWHVPYIS-EEARGNFLRAYRARL 208
Cdd:pfam02525 144 fSLDELLPY-LRGILGFCGITDLPPFAVEGTAGPEdEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-151 3.33e-21

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 87.45  E-value: 3.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    1 MNVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMNWNPVASAADFAERADPDylvyaleqresvKRQSlaAD 80
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPD------------KRYS--PE 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600168   81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGGKRfydqgGLAGKKAL-VSLTLGGRQHM 151
Cdd:PRK09739  70 VHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGH-----KLPFNKVRwVALVGGSKESF 136
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 2-210 1.26e-17

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 77.35  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    2 NVLIVHAHNEPQ-SFTRALCDQACETLagqGHaVQVSDLYAmnwnpvasaadfaerADPDYLVyaleqresvkrqslaaD 80
Cdd:PRK04930   7 KVLLLYAHPESQdSVANRVLLKPAQQL---EH-VTVHDLYA---------------HYPDFFI----------------D 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGgkrfYDQGGLAGKKALVSLTLGGRQHMFGEGAI-HG 159
Cdd:PRK04930  52 IPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASG----PGGNALAGKYWRSVITTGEPESAYRYDGYnRY 127

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15600168  160 PLEDMLRPIlRGTLAYVGMQVLEPFVAWHVPYISEEARGNFLRAYRARLEN 210
Cdd:PRK04930 128 PMSDILRPF-ELTAAMCRMHWLSPIIIYWARRQSPEELASHARAYGDWLAN 177
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-211 6.57e-17

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 75.94  E-value: 6.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   1 MNVLIVHAH-NEPQSFTRALCDQACETL--AGQGHAVQVSDLYAMNWnPVASAADFAERADPDylvyalEQRESVKRQSL 77
Cdd:COG1182   2 MKLLHIDSSpRGEGSVSRRLADAFVAALraAHPDDEVTYRDLAAEPL-PHLDGAWLAAFFTPA------EGRTPEQQAAL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168  78 AAdIQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGgkrfYDQGG----LAGKKALVSLTLGGrqhMFG 153
Cdd:COG1182  75 AL-SDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFR----YTENGpvglLTGKKAVVITARGG---VYS 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168 154 EGAIHGPleDMLRPILRGTLAYVGMQVLEpFVawHVPYIS--EEARGNFLRAYRARLENL 211
Cdd:COG1182 147 GGPAAGM--DFQTPYLRTVLGFIGITDVE-FV--RAEGTAagPEAAEAALAAARAAIAEL 201
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
80-208 1.59e-16

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 74.44  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   80 DIQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYGgkrfydQGGLA--GKKALVSLTLGGRQHMFGEGAI 157
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYG------HGGTAlhGKHLLWAVTTGGGESHFEIGAH 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600168  158 hgPLEDMLRPILRGTLAYVGMQVLEPFvAWHVPYI-SEEARGNFLRAYRARL 208
Cdd:PRK00871 119 --PGFDVLSQPLQATALYCGLNWLPPF-AMHCTFIcDDETLEGQARHYKQRL 167
PRK00170 PRK00170
azoreductase; Reviewed
 1-178 1.30e-14

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 69.92  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    1 MNVLIVHAH-NEPQSFTRALCDQACETL--AGQGHAVQVSDLYAmNWNPVASAADFAERADPDYlvyALEQREsvkrQSL 77
Cdd:PRK00170   2 SKVLVIKSSiLGDYSQSMQLGDAFIEAYkeAHPDDEVTVRDLAA-EPIPVLDGEVVGALGKSAE---TLTPRQ----QEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   78 AADIQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSGVCYggkRFYDQG--GLA-GKKALVSLTLGGrqhmfge 154
Cdd:PRK00170  74 VALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTF---RYTENGpvGLVtGKKALLITSRGG------- 143

                        170       180
                 ....*....|....*....|....*.
gi 15600168  155 gaIH--GPlEDMLRPILRGTLAYVGM 178
Cdd:PRK00170 144 --IHkdGP-TDMGVPYLKTFLGFIGI 166
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-188 1.61e-11

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 60.33  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168     1 MNVLIVHAHNEPQSFTRALCDQACETLAgQGHAVQVSDLYAMNwNPVASAADFAERADPDylvyaleqresvkrqslaaD 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLE-EGAEVELIDLADLI-LPLCDEDLEEEQGDPD-------------------D 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168    81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVlvsgvcyggKRFYDQGGLAGKKALVSLTLGGRQHMFGegaihgp 160
Cdd:pfam03358  60 VQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDWL---------SRLRGGKELRGKPVAIVSTGGGRSGGLR------- 123

                         170       180
                  ....*....|....*....|....*....
gi 15600168   161 LEDMLRPIlrgtLAYVGMQVL-EPFVAWH 188
Cdd:pfam03358 124 AVEQLRQV----LAELGAIVVpSGQVAVG 148
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 2-180 1.39e-10

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 58.40  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   2 NVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLYAMNWNPVASAADFAERADPDylvyaleqresvkrqslaaDI 81
Cdd:COG0655   1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCGGTGKCVIKD-------------------DM 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168  82 QAELDKLLWADLLILNFPIYWFSVPAILKGWFDRvlvsgvCYGgkRFYDQGGLAGKKALVsLTLGGrqhmfgegaiHGPL 161
Cdd:COG0655  62 NAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDR------LYA--LWAKGKLLKGKVGAV-FTTGG----------HGGA 122

                       170
                ....*....|....*....
gi 15600168 162 EDMLRPILRgTLAYVGMQV 180
Cdd:COG0655 123 EATLLSLNT-FLLHHGMIV 140
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-186 1.65e-09

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 54.78  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   1 MNVLIVHAHNEPQSFTRALCDQACETLAGQGHAVQVSDLyamnwnpvasaadfAERADPDYLvyaleqrESVKRQSLAAD 80
Cdd:COG0431   1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDL--------------RDLDLPLYD-------EDLEADGAPPA 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168  81 IQAELDKLLWADLLILNFPIYWFSVPAILKGWFDrvlvsgvcyggkrFYDQGGLAGKKALVSLTLGGRQHMFGegaihgp 160
Cdd:COG0431  60 VKALREAIAAADGVVIVTPEYNGSYPGVLKNALD-------------WLSRSELAGKPVALVSTSGGARGGLR------- 119

                       170       180
                ....*....|....*....|....*.
gi 15600168 161 LEDMLRPILRgtlaYVGMQVLEPFVA 186
Cdd:COG0431 120 ALEHLRPVLS----ELGAVVLPPQVS 141
PRK01355 PRK01355
azoreductase; Reviewed
 85-118 1.35e-03

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 38.53  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15600168   85 LDKLLWADLLILNFPIYWFSVPAILKGWFDRVLV 118
Cdd:PRK01355  72 INQLKSVDKVVISCPMTNFNVPATLKNYLDHIAV 105
PRK06934 PRK06934
flavodoxin; Provisional
 67-130 3.12e-03

flavodoxin; Provisional


Pssm-ID: 180760 [Multi-domain]  Cd Length: 221  Bit Score: 37.58  E-value: 3.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600168   67 EQRESVKrqslaADIQAELDKLLWADLLILNFPIYWFSVPAILKGWFDRVLVSG------VCYGGKRFYD 130
Cdd:PRK06934 111 EVKEGGR-----PEMREKIQNLADYDQIFIGYPIWWYKMPMVMYSFFEQHDFSGktlipfTTHGGSRFSD 175
 
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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