NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039033374|gb|ANM77569|]
View 

NADPH-dependent FMN reductase family protein [Serratia marcescens]

Protein Classification

FMN-dependent NADH-azoreductase( domain architecture ID 10003095)

FMN-dependent NADH-azoreductase catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to form the corresponding amines; requires NADH, but not NADPH, as an electron donor

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0009055|GO:0050446|GO:0016491|GO:0050136|GO:0008753|GO:0010181
PubMed:  24915188
SCOP:  3001217

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-198 3.51e-86

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


:

Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 252.74  E-value: 3.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQTNNLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGELFGALRGV-KNISPRAKAAVALSDRL 79
Cdd:COG1182     1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPaEGRTPEQQAALALSDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  80 IAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAG---HPTDAVTPYL 156
Cdd:COG1182    81 IDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGgpaAGMDFQTPYL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039033374 157 RSVLGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELA 198
Cdd:COG1182   161 RTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELA 202
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-198 3.51e-86

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 252.74  E-value: 3.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQTNNLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGELFGALRGV-KNISPRAKAAVALSDRL 79
Cdd:COG1182     1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPaEGRTPEQQAALALSDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  80 IAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAG---HPTDAVTPYL 156
Cdd:COG1182    81 IDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGgpaAGMDFQTPYL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039033374 157 RSVLGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELA 198
Cdd:COG1182   161 RTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELA 202
PRK00170 PRK00170
azoreductase; Reviewed
 1-198 5.04e-81

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 239.41  E-value: 5.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQTNNLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGELFGALR-GVKNISPRAKAAVALSDRL 79
Cdd:PRK00170    1 MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGkSAETLTPRQQEAVALSDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  80 IAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAGHPTDAVTPYLRSV 159
Cdd:PRK00170   81 LEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPTDMGVPYLKTF 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039033374 160 LGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELA 198
Cdd:PRK00170  161 LGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELA 199
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 2-194 1.40e-41

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: 139.01  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   2 KKILVLKSSIMGnDSQTNNLIDRYLAARKAKGHEdrIVEHDLTALDLPVLDGELFGALrgvkniSPRAKAAVALSDRliA 81
Cdd:pfam02525   1 MKILIINAHPRP-GSFSSRLADALVEALKAAGHE--VTVRDLYALFLPVLDAEDLADL------TYPQGAADVESEQ--E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  82 ELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVG-LVEGVNALVFSSRGGMHA--------GHPTDAV 152
Cdd:pfam02525  70 ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGPEYaygkggynGFSLDEL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033374 153 TPYLRSVLGLMGIGDVQFIYAEGLDM--KPHGRDQGLANAHQRI 194
Cdd:pfam02525 150 LPYLRGILGFCGITDLPPFAVEGTAGpeDEAALAEALERYEERL 193
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-198 3.51e-86

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 252.74  E-value: 3.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQTNNLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGELFGALRGV-KNISPRAKAAVALSDRL 79
Cdd:COG1182     1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHPDDEVTYRDLAAEPLPHLDGAWLAAFFTPaEGRTPEQQAALALSDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  80 IAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAG---HPTDAVTPYL 156
Cdd:COG1182    81 IDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYTENGPVGLLTGKKAVVITARGGVYSGgpaAGMDFQTPYL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039033374 157 RSVLGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELA 198
Cdd:COG1182   161 RTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELA 202
PRK00170 PRK00170
azoreductase; Reviewed
 1-198 5.04e-81

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 239.41  E-value: 5.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQTNNLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGELFGALR-GVKNISPRAKAAVALSDRL 79
Cdd:PRK00170    1 MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDDEVTVRDLAAEPIPVLDGEVVGALGkSAETLTPRQQEAVALSDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  80 IAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAGHPTDAVTPYLRSV 159
Cdd:PRK00170   81 LEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGPVGLVTGKKALLITSRGGIHKDGPTDMGVPYLKTF 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039033374 160 LGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELA 198
Cdd:PRK00170  161 LGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAADELA 199
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 2-194 1.40e-41

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: 139.01  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   2 KKILVLKSSIMGnDSQTNNLIDRYLAARKAKGHEdrIVEHDLTALDLPVLDGELFGALrgvkniSPRAKAAVALSDRliA 81
Cdd:pfam02525   1 MKILIINAHPRP-GSFSSRLADALVEALKAAGHE--VTVRDLYALFLPVLDAEDLADL------TYPQGAADVESEQ--E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  82 ELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVG-LVEGVNALVFSSRGGMHA--------GHPTDAV 152
Cdd:pfam02525  70 ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGgGLLGKKVLVIVTTGGPEYaygkggynGFSLDEL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039033374 153 TPYLRSVLGLMGIGDVQFIYAEGLDM--KPHGRDQGLANAHQRI 194
Cdd:pfam02525 150 LPYLRGILGFCGITDLPPFAVEGTAGpeDEAALAEALERYEERL 193
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
1-198 3.62e-26

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 99.84  E-value: 3.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQTN-NLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGEL----FGALRGVKnISPRAKAAVAL 75
Cdd:PRK13556    1 MSKVLFVKANNRPAEQAVSvKLYEAFLASYKEAHPNDTVVELDLYKEELPYVGVDMingtFKAGKGFE-LTEEEAKAVAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  76 SDRLIAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAGHPTDAV--- 152
Cdd:PRK13556   80 ADKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPEGPVGLIGDKKVALLNARGGVYSEGPAAEVema 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039033374 153 TPYLRSVLGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELA 198
Cdd:PRK13556  160 VKYVASMMGFFGVTNMETVVIEGHNQFPDKAEEIITAGLEEAAKVA 205
PRK01355 PRK01355
azoreductase; Reviewed
 1-181 5.57e-19

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 80.51  E-value: 5.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGND-SQTNNLIDRYLAARKAKGHEDRIVEHDLTALDLP--VLDGELFGALRGVKNisprakaavalSD 77
Cdd:PRK01355    1 MSKVLVIKGSMVAKEkSFSSALTDKFVEEYKKVNPNDEIIILDLNETKVGsvTLTSENFKTFFKEEV-----------SD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  78 RLIAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNY---TATYPVGLVEGVNALVFSSRGGMHAGHPTDAVTP 154
Cdd:PRK01355   70 KYINQLKSVDKVVISCPMTNFNVPATLKNYLDHIAVANKTFSYkysKKGDAIGLLDHLKVQILTTQGAPLGWYPWGSHTN 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039033374 155 YLRSVLGLMGIGDVQFIYAEG------LDMKPH 181
Cdd:PRK01355  150 YLEGTWEFLGAKVVDSILLAGtkveplSNKTPK 182
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
1-199 3.85e-16

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 73.23  E-value: 3.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   1 MKKILVLKSSIMGNDSQ-TNNLIDRYLAARKAKGHEDRIVEHDLTALDLPVLDGELFGAlrGVK-----NISPRAKAAVA 74
Cdd:PRK13555    1 MSKVLFVKANDRPAEQAvSSKMYETFVSTYKEANPNTEITELDLFALDLPYYGNIAISG--GYKrsqgmELTAEEEKAVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  75 LSDRLIAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSRGGMHAGH---PTDA 151
Cdd:PRK13555   79 TVDQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYTANGPEGLAGGKKVVVLGARGSDYSSEqmaPMEM 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039033374 152 VTPYLRSVLGLMGIGDVQFIYAEGLDMKPHGRDQGLANAHQRIAELAG 199
Cdd:PRK13555  159 AVNYVTTVLGFWGITNPETVVIEGHNQYPDRSQQIVEEGLENVKKVAA 206
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-198 1.37e-08

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 52.15  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   3 KILVL-----KSSImgndsqTNNLIDRYLAARKAKGHEdrIVEHDLTALDL-PVLDGELFGAlrgvkniSPRAKAAVAls 76
Cdd:COG2249     1 KILIIyahpdPSSF------NAALAEAAAEGLEAAGHE--VTVHDLYAEGFdPVLSAADFYR-------DGPLPIDVA-- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  77 dRLIAELKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATYPVGLVEGVNALVFSSrggmhAGHPTDAVTPY- 155
Cdd:COG2249    64 -AEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVT-----TGGPEEAYSRLg 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039033374 156 ---------LRSVLGLMGIGDVQFIYAEGLD-MKPHGRDQGLANAHQRIAELA 198
Cdd:COG2249   138 yggpieellFRGTLGYCGMKVLPPFVLYGVDrSSDEERAAWLERVRELLAALA 190
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-177 7.12e-08

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 49.54  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374   3 KILVLKSSImGNDSQTNNLIdRYLAARKAKGHEDRIVehDLTALDLPVLDGELFGALrgvkNISPRAKAavalsdrLIAE 82
Cdd:pfam03358   2 KILAISGSP-RKGSNTRKLA-RWAAELLEEGAEVELI--DLADLILPLCDEDLEEEQ----GDPDDVQE-------LREK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  83 LKESDLLLLGAPMYNLNVPTQLKNWFDLVARARMTFNYTATyPVGLVegvnALVFSSRGGMHAghptdavTPYLRSVLGL 162
Cdd:pfam03358  67 IAAADAIIIVTPEYNGSVSGLLKNAIDWLSRLRGGKELRGK-PVAIV----STGGGRSGGLRA-------VEQLRQVLAE 134

                         170
                  ....*....|....*...
gi 1039033374 163 MG---IGDVQFIYAEGLD 177
Cdd:pfam03358 135 LGaivVPSGQVAVGNATD 152
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
24-164 1.47e-06

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 46.30  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039033374  24 RYLAAR-KAKGHEDRIVehDLTALDLPVLDGELFGalrgvKNISPRAKaavalsdRLIAELKESDLLLLGAPMYNLNVPT 102
Cdd:COG0431    21 RAAAELaPAAGAEVELI--DLRDLDLPLYDEDLEA-----DGAPPAVK-------ALREAIAAADGVVIVTPEYNGSYPG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039033374 103 QLKNWFDLVARArmTFNYTatyPVGLVeGVNAlvfSSRGGMHAGHptdavtpYLRSVLGLMG 164
Cdd:COG0431    87 VLKNALDWLSRS--ELAGK---PVALV-STSG---GARGGLRALE-------HLRPVLSELG 132
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 77-109 2.59e-03

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 37.22  E-value: 2.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039033374  77 DRLIAELKESDLLLLGAPMYNLNVPTQLKNWFD 109
Cdd:COG0655    62 NAIYEKLLEADGIIFGSPTYFGNMSAQLKAFID 94
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH