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Conserved domains on  [gi|332364907|gb|EGJ42675|]
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quinone family NAD(P)H dehydrogenase [Streptococcus sanguinis SK355]

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 ...
 2-188 1.14e-72

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 217.40  E-value: 1.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   2 KTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLYAENFDPILRFdqEHRRRDLHKDPEMAKYRDLITWADHLIFI 80
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAgHEVTVHDLYAEGFDPVLSA--ADFYRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  81 FPIWWSGMPAILKGFIDRVFTADFAYSYKKVGLQGHLQGKSSWIIVSHNTPGFALP--FVQDYG-KVLKNQILKLCGISP 157
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSrlGYGGPIeELLFRGTLGYCGMKV 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332364907 158 VKLTELNGVERKTDQQRQEMLKKIGQLASQI 188
Cdd:COG2249  159 LPPFVLYGVDRSSDEERAAWLERVRELLAAL 189
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-188 1.14e-72

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 217.40  E-value: 1.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   2 KTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLYAENFDPILRFdqEHRRRDLHKDPEMAKYRDLITWADHLIFI 80
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAgHEVTVHDLYAEGFDPVLSA--ADFYRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  81 FPIWWSGMPAILKGFIDRVFTADFAYSYKKVGLQGHLQGKSSWIIVSHNTPGFALP--FVQDYG-KVLKNQILKLCGISP 157
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSrlGYGGPIeELLFRGTLGYCGMKV 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332364907 158 VKLTELNGVERKTDQQRQEMLKKIGQLASQI 188
Cdd:COG2249  159 LPPFVLYGVDRSSDEERAAWLERVRELLAAL 189
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-185 1.36e-45

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: 148.64  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907    1 MKTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLYAEnFDPILRFDQEHRRRDLHKDPEMAKYRDLITWADHLIF 79
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAgHEVTVRDLYAL-FLPVLDAEDLADLTYPQGAADVESEQEELLAADVIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   80 IFPIWWSGMPAILKGFIDRVFTADFAYSY-KKVGLQGHLQGKSSWIIVSHNTPGFA----LPFVQDYGKVLKN--QILKL 152
Cdd:pfam02525  80 QFPLYWFSVPALLKGWIDRVLRAGFAFKYeEGGPGGGGLLGKKVLVIVTTGGPEYAygkgGYNGFSLDELLPYlrGILGF 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 332364907  153 CGISPVKLTELNG-VERKTDQQRQEMLKKIGQLA 185
Cdd:pfam02525 160 CGITDLPPFAVEGtAGPEDEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-106 3.60e-26

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 99.01  E-value: 3.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   1 MKTLIIYTHPSPTGFNAAILKEVQNNLSK-KHEVKTLDLYAENFDPILRFDQEHRRRDLHK--DPEMAKYRDLITWADHL 77
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQErGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKrySPEVHQLYSELLEHDAL 83

                         90       100
                 ....*....|....*....|....*....
gi 332364907  78 IFIFPIWWSGMPAILKGFIDRVFTADFAY 106
Cdd:PRK09739  84 VFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-188 1.14e-72

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 217.40  E-value: 1.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   2 KTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLYAENFDPILRFdqEHRRRDLHKDPEMAKYRDLITWADHLIFI 80
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAgHEVTVHDLYAEGFDPVLSA--ADFYRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  81 FPIWWSGMPAILKGFIDRVFTADFAYSYKKVGLQGHLQGKSSWIIVSHNTPGFALP--FVQDYG-KVLKNQILKLCGISP 157
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSrlGYGGPIeELLFRGTLGYCGMKV 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332364907 158 VKLTELNGVERKTDQQRQEMLKKIGQLASQI 188
Cdd:COG2249  159 LPPFVLYGVDRSSDEERAAWLERVRELLAAL 189
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-185 1.36e-45

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: 148.64  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907    1 MKTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLYAEnFDPILRFDQEHRRRDLHKDPEMAKYRDLITWADHLIF 79
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAgHEVTVRDLYAL-FLPVLDAEDLADLTYPQGAADVESEQEELLAADVIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   80 IFPIWWSGMPAILKGFIDRVFTADFAYSY-KKVGLQGHLQGKSSWIIVSHNTPGFA----LPFVQDYGKVLKN--QILKL 152
Cdd:pfam02525  80 QFPLYWFSVPALLKGWIDRVLRAGFAFKYeEGGPGGGGLLGKKVLVIVTTGGPEYAygkgGYNGFSLDELLPYlrGILGF 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 332364907  153 CGISPVKLTELNG-VERKTDQQRQEMLKKIGQLA 185
Cdd:pfam02525 160 CGITDLPPFAVEGtAGPEDEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-106 3.60e-26

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 99.01  E-value: 3.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   1 MKTLIIYTHPSPTGFNAAILKEVQNNLSK-KHEVKTLDLYAENFDPILRFDQEHRRRDLHK--DPEMAKYRDLITWADHL 77
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQErGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKrySPEVHQLYSELLEHDAL 83

                         90       100
                 ....*....|....*....|....*....
gi 332364907  78 IFIFPIWWSGMPAILKGFIDRVFTADFAY 106
Cdd:PRK09739  84 VFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-113 1.70e-16

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 72.66  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907    1 MKTLIIYTHPSPTGFNAAILKEVQNNLSKKHEVKTLDLyAENFDPILRFDQEHRrrdLHKDPEMAKYRDLITWADHLIFI 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDL-ADLILPLCDEDLEEE---QGDPDDVQELREKIAAADAIIIV 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 332364907   81 FPIWWSGMPAILKGFIDRVFTADF--AYSYKKVGL 113
Cdd:pfam03358  77 TPEYNGSVSGLLKNAIDWLSRLRGgkELRGKPVAI 111
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 2-132 2.63e-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: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   2 KTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLYAENFDPILrfDQEHRRRDLHKDpEMAKYRDLITWADHLIFI 80
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEEAgAEVELIRLADLDIKPCI--GCGGTGKCVIKD-DMNAIYEKLLEADGIIFG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332364907  81 FPIWWSGMPAILKGFIDRvftadfaySYKKVGLQGHLQGKSSWIIVSHNTPG 132
Cdd:COG0655   78 SPTYFGNMSAQLKAFIDR--------LYALWAKGKLLKGKVGAVFTTGGHGG 121
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-187 1.55e-10

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 57.83  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   1 MKTLIIYTHPSPTG-FNAAILKEVQNNLSKKH---EVKTLDLYAenfDPILRFDQEH----RRRDLHKDPEMAKYRDLIT 72
Cdd:COG1182    2 MKLLHIDSSPRGEGsVSRRLADAFVAALRAAHpddEVTYRDLAA---EPLPHLDGAWlaafFTPAEGRTPEQQAALALSD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  73 -------WADHLIFIFPIWWSGMPAILKGFIDRVFTADFAYSYKKVGLQGHLQGKSSWIIVS-----HNTPGFALPFVQD 140
Cdd:COG1182   79 elidellAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITArggvySGGPAAGMDFQTP 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332364907 141 YgkvLKnQILKLCGISPVKLTELNGVERKTDQQRQEM---LKKIGQLASQ 187
Cdd:COG1182  159 Y---LR-TVLGFIGITDVEFVRAEGTAAGPEAAEAALaaaRAAIAELAAA 204
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-113 7.12e-10

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 55.16  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   1 MKTLIIYTHPSPTGFNAAILKEVQNNLSKK-HEVKTLDLyAENFDPIlrFDQEHRRRDLHkdPEMAKYRDLITWADHLIF 79
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAgAEVELIDL-RDLDLPL--YDEDLEADGAP--PAVKALREAIAAADGVVI 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332364907  80 IFPIWWSGMPAILKGFIDRVFTAdfAYSYKKVGL 113
Cdd:COG0431   76 VTPEYNGSYPGVLKNALDWLSRS--ELAGKPVAL 107
PRK01355 PRK01355
azoreductase; Reviewed
 2-185 5.29e-08

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 50.47  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   2 KTLIIYTHPSPT--GFNAAILKEVQNNLSKKH---EVKTLDLyaENFDPILRFDQEHRRRDLHKDPEMAKYRDLITWADH 76
Cdd:PRK01355   3 KVLVIKGSMVAKekSFSSALTDKFVEEYKKVNpndEIIILDL--NETKVGSVTLTSENFKTFFKEEVSDKYINQLKSVDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  77 LIFIFPIWWSGMPAILKGFIDRVFTAD--FAYSYKK----VGLQGHLqgkSSWIIVSHNTPGFALPFvQDYGKVLKNqIL 150
Cdd:PRK01355  81 VVISCPMTNFNVPATLKNYLDHIAVANktFSYKYSKkgdaIGLLDHL---KVQILTTQGAPLGWYPW-GSHTNYLEG-TW 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 332364907 151 KLCGISPVKLTELNG--VERKTDQQRQEMLKKIGQLA 185
Cdd:PRK01355 156 EFLGAKVVDSILLAGtkVEPLSNKTPKEIVEEFDKEI 192
PRK00170 PRK00170
azoreductase; Reviewed
 1-127 2.53e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 42.96  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   1 MKTLIIYTHP-SPTGFNAAILKEVQNNLSKKH---EVKTLDLYAENFdPIL---------RFDQEHRRRDLHKDPEMAKY 67
Cdd:PRK00170   2 SKVLVIKSSIlGDYSQSMQLGDAFIEAYKEAHpddEVTVRDLAAEPI-PVLdgevvgalgKSAETLTPRQQEAVALSDEL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  68 RDLITWADHLIFIFPIWWSGMPAILKGFIDRVFTADFAYSYKKVGLQGHLQGKSSWIIVS 127
Cdd:PRK00170  81 LEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITS 140
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 2-120 4.07e-05

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 42.30  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   2 KTLIIYTHPSP--TGFNAAILKEVQnnlSKKHeVKTLDLYAENFDPILrfdqehrrrDLHKDPEMAKYRDLItwadhlIF 79
Cdd:PRK04930   7 KVLLLYAHPESqdSVANRVLLKPAQ---QLEH-VTVHDLYAHYPDFFI---------DIPHEQALLREHDVI------VF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 332364907  80 IFPIWWSGMPAILKGFIDRVFTADFAYsykkvGLQGH-LQGK 120
Cdd:PRK04930  68 QHPLYTYSCPALLKEWLDRVLSRGFAS-----GPGGNaLAGK 104
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
4-134 5.71e-05

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 41.69  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   4 LIIYTHPSP--TGFNAAILKEVQNNlsKKHEVKTL-DLYAEnFDPILRFDQEHRRRdlhkdpemakyRDLITWaDHlifi 80
Cdd:PRK00871   3 LIIYAHPYPhhSHANKRMLEQARTL--EGVEIRSLyQLYPD-FNIDIAAEQEALSR-----------ADLIVW-QH---- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332364907  81 fPIWWSGMPAILKGFIDRVFTADFAYSYKKVGLQG-HL-------QGKSSWIIVSHntPGFA 134
Cdd:PRK00871  64 -PMQWYSIPPLLKLWIDKVLSHGWAYGHGGTALHGkHLlwavttgGGESHFEIGAH--PGFD 122
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
32-115 1.74e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 40.51  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  32 EVKTLDLYAENFdPILRFD------QEHRRRDLHKDPEMA-----KYRDLITWADHLIFIFPIWWSGMPAILKGFIDRVF 100
Cdd:PRK13556  38 TVVELDLYKEEL-PYVGVDmingtfKAGKGFELTEEEAKAvavadKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLN 116

                         90
                 ....*....|....*...
gi 332364907 101 TADFAYSYKK---VGLQG 115
Cdd:PRK13556 117 RAGKTFKYTPegpVGLIG 134
PRK06934 PRK06934
flavodoxin; Provisional
 14-99 3.28e-04

flavodoxin; Provisional


Pssm-ID: 180760 [Multi-domain]  Cd Length: 221  Bit Score: 39.89  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  14 GFNAAILKEVQNNLSKK-HEVKTLDLYAENFDPILRFDQEHRRRDLHkdPEM-AKYRDLITWaDHLIFIFPIWWSGMPAI 91
Cdd:PRK06934  71 GSTQYVAQIIQEETGGDlFRIETVKPYPRQHDPLLKYAEQEVKEGGR--PEMrEKIQNLADY-DQIFIGYPIWWYKMPMV 147


                 ....*...
gi 332364907  92 LKGFIDRV 99
Cdd:PRK06934 148 MYSFFEQH 155
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 3-188 6.93e-03

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 35.26  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907   3 TLIIYThpSPTGfNA-----AILKEVQNNLSKKHEVKTLDLyaenfdpilrfdqehrrrdlhkdPEMAKYrdlitwaDHL 77
Cdd:COG0716    1 ILIVYG--STTG-NTekvaeAIAEALGAAGVDLFEIEDADL-----------------------DDLEDY-------DLL 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332364907  78 IFIFPIWWSGMPAILKGFIDRvftadfaysykkvgLQGHLQGKSSWIIVSHNTpgfalpfvQDYGKVLKN--QILKLCGI 155
Cdd:COG0716   48 ILGTPTWAGELPDDWEDFLEE--------------LKEDLSGKKVALFGTGDS--------SGYGDALGElkELLEEKGA 105

                        170       180       190
                 ....*....|....*....|....*....|...
gi 332364907 156 SPVKLTELNGverKTDQQRQEMLKKIGQLASQI 188
Cdd:COG0716  106 KVVGGYDFEG---SKAPDAEDTEERAEEWLKQL 135
 
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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