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Conserved domains on  [gi|16128868|ref|NP_415421|]
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putative oxidoreductase YcaK [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

NADPH-dependent FMN reductase family protein( domain architecture ID 10013330)

NADPH-dependent FMN reductase family protein contains a flavodoxin-like fold, which is characterized by an open twisted/alpha beta structure consisting of five parallel beta-sheets connected by alpha-helices which surround the sheet

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-196 1.51e-124

NAD(P)H oxidoreductase;


:

Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 349.39  E-value: 1.51e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    1 MQSERIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRRNFNPVMTPEDEPDWKNMDKRYSPEVHQLYSELLEH 80
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKRYSPEVHQLYSELLEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   81 DTLVVVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGDKESFVQMGWEKNISDYLK-NMCSYLGIE 159
Cdd:PRK09739  81 DALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGSKESFVKRGWEKNMSDYLNvGMASYLGIE 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 16128868  160 DADVTFLCNTVVFDGEELHASYYQSLLSQVRDMVDAL 196
Cdd:PRK09739 161 DSDVTFLYNTLVFDGEELHASHYQSLLSQAREMVDAL 197
 
Name Accession Description Interval E-value
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-196 1.51e-124

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 349.39  E-value: 1.51e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    1 MQSERIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRRNFNPVMTPEDEPDWKNMDKRYSPEVHQLYSELLEH 80
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKRYSPEVHQLYSELLEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   81 DTLVVVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGDKESFVQMGWEKNISDYLK-NMCSYLGIE 159
Cdd:PRK09739  81 DALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGSKESFVKRGWEKNMSDYLNvGMASYLGIE 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 16128868  160 DADVTFLCNTVVFDGEELHASYYQSLLSQVRDMVDAL 196
Cdd:PRK09739 161 DSDVTFLYNTLVFDGEELHASHYQSLLSQAREMVDAL 197
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-196 1.23e-51

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 164.24  E-value: 1.23e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   5 RIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRRNFNPVMTPEDEPDwknmDKRYSPEVHQLYSELLEHDTLV 84
Cdd:COG2249   1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYR----DGPLPIDVAAEQELLLWADHLV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  85 VVFPLWWYSFPAMLKGYIDRVWNNGLAYG-----DGHKLPFNKVRWVALVGGDKESFVQMGWEKNISDYLKN-MCSYLGI 158
Cdd:COG2249  77 FQFPLWWYSMPALLKGWIDRVLTPGFAYGygggyPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEELLFRgTLGYCGM 156

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 16128868 159 EDADVTFLCNTVVFDGEELhasyyQSLLSQVRDMVDAL 196
Cdd:COG2249 157 KVLPPFVLYGVDRSSDEER-----AAWLERVRELLAAL 189
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 5-189 4.41e-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: 147.87  E-value: 4.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868     5 RIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRrNFNPVMTPEDEPDWKNMDKRYspEVHQLYSELLEHDTLV 84
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYA-LFLPVLDAEDLADLTYPQGAA--DVESEQEELLAADVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    85 VVFPLWWYSFPAMLKGYIDRVWNNGLAY------GDGHKLPFNKVRWVALVGGDKESFVQMGWEKNISD----YLKNMCS 154
Cdd:pfam02525  79 FQFPLYWFSVPALLKGWIDRVLRAGFAFkyeeggPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDellpYLRGILG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16128868   155 YLGIEDADVTFLCNTVVFDGEELHASYYQSLLSQV 189
Cdd:pfam02525 159 FCGITDLPPFAVEGTAGPEDEAALAEALERYEERL 193
 
Name Accession Description Interval E-value
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-196 1.51e-124

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 349.39  E-value: 1.51e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    1 MQSERIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRRNFNPVMTPEDEPDWKNMDKRYSPEVHQLYSELLEH 80
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKRYSPEVHQLYSELLEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   81 DTLVVVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGDKESFVQMGWEKNISDYLK-NMCSYLGIE 159
Cdd:PRK09739  81 DALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGSKESFVKRGWEKNMSDYLNvGMASYLGIE 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 16128868  160 DADVTFLCNTVVFDGEELHASYYQSLLSQVRDMVDAL 196
Cdd:PRK09739 161 DSDVTFLYNTLVFDGEELHASHYQSLLSQAREMVDAL 197
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-196 1.23e-51

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 164.24  E-value: 1.23e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   5 RIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRRNFNPVMTPEDEPDwknmDKRYSPEVHQLYSELLEHDTLV 84
Cdd:COG2249   1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADFYR----DGPLPIDVAAEQELLLWADHLV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  85 VVFPLWWYSFPAMLKGYIDRVWNNGLAYG-----DGHKLPFNKVRWVALVGGDKESFVQMGWEKNISDYLKN-MCSYLGI 158
Cdd:COG2249  77 FQFPLWWYSMPALLKGWIDRVLTPGFAYGygggyPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEELLFRgTLGYCGM 156

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 16128868 159 EDADVTFLCNTVVFDGEELhasyyQSLLSQVRDMVDAL 196
Cdd:COG2249 157 KVLPPFVLYGVDRSSDEER-----AAWLERVRELLAAL 189
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 5-189 4.41e-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: 147.87  E-value: 4.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868     5 RIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRrNFNPVMTPEDEPDWKNMDKRYspEVHQLYSELLEHDTLV 84
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYA-LFLPVLDAEDLADLTYPQGAA--DVESEQEELLAADVIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    85 VVFPLWWYSFPAMLKGYIDRVWNNGLAY------GDGHKLPFNKVRWVALVGGDKESFVQMGWEKNISD----YLKNMCS 154
Cdd:pfam02525  79 FQFPLYWFSVPALLKGWIDRVLRAGFAFkyeeggPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDellpYLRGILG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16128868   155 YLGIEDADVTFLCNTVVFDGEELHASYYQSLLSQV 189
Cdd:pfam02525 159 FCGITDLPPFAVEGTAGPEDEAALAEALERYEERL 193
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 5-180 1.23e-11

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 60.33  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   5 RIYLVWAHPRHDSLTAHIADAIHQRAMERKIQVTELDLYRRNFNPVMTPEDEPDWKNMDkryspEVHQLYSELLEHDTLV 84
Cdd:COG0655   1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCGGTGKCVIKD-----DMNAIYEKLLEADGII 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  85 VVFPLWWYSFPAMLKGYIDR---VWNNGlaygdghKLPFNKVRWVALVGGDkesfvqmGWEKNISDYLKNMCSYLGIEDA 161
Cdd:COG0655  76 FGSPTYFGNMSAQLKAFIDRlyaLWAKG-------KLLKGKVGAVFTTGGH-------GGAEATLLSLNTFLLHHGMIVV 141

                       170
                ....*....|....*....
gi 16128868 162 DVTFLCNTVVFDGEELHAS 180
Cdd:COG0655 142 GLPPYGAVGGGGPGDVLDE 160
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
11-166 2.85e-11

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 59.76  E-value: 2.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  11 AHPRHD-----SLTAHIADAIHQRAMErkIQVTELDLYR------------RNFNPV--MTPEDEPDWKNMDkryspevh 71
Cdd:COG1182   9 SSPRGEgsvsrRLADAFVAALRAAHPD--DEVTYRDLAAeplphldgawlaAFFTPAegRTPEQQAALALSD-------- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  72 QLYSELLEHDTLVVVFPLWWYSFPAMLKGYIDRVWNNGL--AYGDGHKLPFNKVRWVALV---GGDKESFVQMGWEkNIS 146
Cdd:COG1182  79 ELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRtfRYTENGPVGLLTGKKAVVItarGGVYSGGPAAGMD-FQT 157

                       170       180
                ....*....|....*....|
gi 16128868 147 DYLKNMCSYLGIEdaDVTFL 166
Cdd:COG1182 158 PYLRTVLGFIGIT--DVEFV 175
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 2-143 2.86e-10

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 56.94  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    2 QSERIYLVWAHPR-HDSltahiadaIHQRAMERKIQ----VTELDLYRRnfnpvmtpedEPDWkNMDKRYSpevHQLyse 76
Cdd:PRK04930   4 QPPKVLLLYAHPEsQDS--------VANRVLLKPAQqlehVTVHDLYAH----------YPDF-FIDIPHE---QAL--- 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128868   77 LLEHDTLVVVFPLWWYSFPAMLKGYIDRVWNNGLAYG-DGHKLPFNKVRWVALVGGDKESFVQMGWEK 143
Cdd:PRK04930  59 LREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGpGGNALAGKYWRSVITTGEPESAYRYDGYNR 126
PRK00170 PRK00170
azoreductase; Reviewed
 36-165 3.04e-08

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 51.43  E-value: 3.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   36 QVTELDLYRRNFnPVMTPEDEPDWKNMDKRYSPEVHQ-------LYSELLEHDTLVVVFPLWWYSFPAMLKGYIDRVWNN 108
Cdd:PRK00170  37 EVTVRDLAAEPI-PVLDGEVVGALGKSAETLTPRQQEavalsdeLLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARA 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128868  109 GLAYGDGHKLPfnkvrwVALVGGDKESFVQM--GWEKN-----ISDYLKNMCSYLGIEDADVTF 165
Cdd:PRK00170 116 GKTFRYTENGP------VGLVTGKKALLITSrgGIHKDgptdmGVPYLKTFLGFIGITDVEFVF 173
FMN_red pfam03358
NADPH-dependent FMN reductase;
13-130 3.64e-07

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 47.62  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868    13 PRHDSLTAHIADAIHQRAmERKIQVTELDLyRRNFNPVMTPEDEPDwknmdKRYSPEVHQLYSELLEHDTLVVVFPLWWY 92
Cdd:pfam03358  10 PRKGSNTRKLARWAAELL-EEGAEVELIDL-ADLILPLCDEDLEEE-----QGDPDDVQELREKIAAADAIIIVTPEYNG 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 16128868    93 SFPAMLKGYIDRvwnngLAYGDGHKLPFNKVrwVALVG 130
Cdd:pfam03358  83 SVSGLLKNAIDW-----LSRLRGGKELRGKP--VAIVS 113
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
81-136 1.76e-06

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 46.32  E-value: 1.76e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128868   81 DTLVVVFPLWWYSFPAMLKGYIDRVWNNGLAYG-DGHKLPFNKVRWVALVGGDKESF 136
Cdd:PRK00871  57 DLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGhGGTALHGKHLLWAVTTGGGESHF 113
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
13-130 6.11e-06

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 44.38  E-value: 6.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  13 PRHDSLTAHIADAIHQRAMERKIQVTELDLyrRNFN-PVMTPEDEPDWknmdkrYSPEVHQLYSELLEHDTLVVVFPLWW 91
Cdd:COG0431  10 LRPGSFNRKLARAAAELAPAAGAEVELIDL--RDLDlPLYDEDLEADG------APPAVKALREAIAAADGVVIVTPEYN 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16128868  92 YSFPAMLKGYIDRVWNNGLAygdghklpfNKVrwVALVG 130
Cdd:COG0431  82 GSYPGVLKNALDWLSRSELA---------GKP--VALVS 109
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
36-174 1.83e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 40.90  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868   36 QVTELDLYRRN------------FNPV----MTPEDEPDWKNMDKryspevhqLYSELLEHDTLVVVFPLWWYSFPAMLK 99
Cdd:PRK13556  38 TVVELDLYKEElpyvgvdmingtFKAGkgfeLTEEEAKAVAVADK--------YLNQFLEADKVVFAFPLWNFTIPAVLH 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128868  100 GYIDRVWNNGLAYGDGHKLPfnkvrwVALVGGDKESFVQ----------MGWEKNISDYLKNMCSYLGIEDAdvtflcNT 169
Cdd:PRK13556 110 TYIDYLNRAGKTFKYTPEGP------VGLIGDKKVALLNarggvysegpAAEVEMAVKYVASMMGFFGVTNM------ET 177


                 ....*
gi 16128868  170 VVFDG 174
Cdd:PRK13556 178 VVIEG 182
PRK07116 PRK07116
flavodoxin; Provisional
 58-95 1.30e-03

flavodoxin; Provisional


Pssm-ID: 180850  Cd Length: 160  Bit Score: 37.73  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 16128868   58 DWKNMDKRYS---------PEVHQLYSELLEHDTLVVVFPLWWYSFP 95
Cdd:PRK07116  46 DWNDKKSRSSvemadkssrPAIAKKIENIAEYDVIFLGFPIWWYVAP 92
 
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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