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Conserved domains on  [gi|1326035869|ref|WP_101894241|]
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FMN-dependent NADH-azoreductase [Ketobacter alkanivorans]

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

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List of domain hits

 Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-207 3.92e-65

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


:

Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 199.59  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPRKQNSLTTDMALRLIERLQSVD-TWEVDRLDLWNTDLPDMNGVTMDAKYAVFSGtpMTGEQADHWQRLN 79
Cdd:COG1182     1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHpDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG--RTPEQQAALALSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  80 RFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTpEDGYIPVLPPRDVVVVTSSGGDYTPGsGLEHEDFA 159
Cdd:COG1182    79 ELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYT-ENGPVGLLTGKKAVVITARGGVYSGG-PAAGMDFQ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1326035869 160 YRYLQQWLQYCMGCNVEFVHLTMTATGPEGVANAMKNAEFKIETMIEQ 207
Cdd:COG1182   157 TPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAA 204
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-207 3.92e-65

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 199.59  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPRKQNSLTTDMALRLIERLQSVD-TWEVDRLDLWNTDLPDMNGVTMDAKYAVFSGtpMTGEQADHWQRLN 79
Cdd:COG1182     1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHpDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG--RTPEQQAALALSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  80 RFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTpEDGYIPVLPPRDVVVVTSSGGDYTPGsGLEHEDFA 159
Cdd:COG1182    79 ELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYT-ENGPVGLLTGKKAVVITARGGVYSGG-PAAGMDFQ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1326035869 160 YRYLQQWLQYCMGCNVEFVHLTMTATGPEGVANAMKNAEFKIETMIEQ 207
Cdd:COG1182   157 TPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAA 204
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 2-209 6.98e-28

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: 103.95  E-value: 6.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   2 KKLLLIESSPRKQnSLTTDMALRLIERLQSVDtWEVDRLDLWNTDLPdmngvTMDAKYAVFSGTPMTGEQADHWQRlnrf 81
Cdd:pfam02525   1 MKILIINAHPRPG-SFSSRLADALVEALKAAG-HEVTVRDLYALFLP-----VLDAEDLADLTYPQGAADVESEQE---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  82 vtQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTPEDGYIPVLPPRDVVVVTSSGGD---YTPGSGLEHE-D 157
Cdd:pfam02525  70 --ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGGGLLGKKVLVIVTTGGPeyaYGKGGYNGFSlD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1326035869 158 FAYRYLQQWLQYCmGC-NVEFVHLtmtatgpEGVANAmkNAEFKIETMIEQYA 209
Cdd:pfam02525 148 ELLPYLRGILGFC-GItDLPPFAV-------EGTAGP--EDEAALAEALERYE 190
PRK00170 PRK00170
azoreductase; Reviewed
 1-202 3.54e-25

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 97.27  E-value: 3.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPRKQNSLTTDMALRLIERLQSVDTW-EVDRLDLWNTDLPDMNGVTMDAKYAvfSGTPMTGEQADHWQRLN 79
Cdd:PRK00170    1 MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDdEVTVRDLAAEPIPVLDGEVVGALGK--SAETLTPRQQEAVALSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  80 RFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTpEDGYIPVLPPRDVVVVTSSGGDYTPGSglehEDFA 159
Cdd:PRK00170   79 ELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYT-ENGPVGLVTGKKALLITSRGGIHKDGP----TDMG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1326035869 160 YRYLQQWLQYCMGCNVEFVHLTMTATGPEGVANAMKNAEFKIE 202
Cdd:PRK00170  154 VPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAAD 196
 
Name Accession Description Interval E-value
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-207 3.92e-65

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 199.59  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPRKQNSLTTDMALRLIERLQSVD-TWEVDRLDLWNTDLPDMNGVTMDAKYAVFSGtpMTGEQADHWQRLN 79
Cdd:COG1182     1 MMKLLHIDSSPRGEGSVSRRLADAFVAALRAAHpDDEVTYRDLAAEPLPHLDGAWLAAFFTPAEG--RTPEQQAALALSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  80 RFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTpEDGYIPVLPPRDVVVVTSSGGDYTPGsGLEHEDFA 159
Cdd:COG1182    79 ELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFRYT-ENGPVGLLTGKKAVVITARGGVYSGG-PAAGMDFQ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1326035869 160 YRYLQQWLQYCMGCNVEFVHLTMTATGPEGVANAMKNAEFKIETMIEQ 207
Cdd:COG1182   157 TPYLRTVLGFIGITDVEFVRAEGTAAGPEAAEAALAAARAAIAELAAA 204
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 2-209 6.98e-28

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: 103.95  E-value: 6.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   2 KKLLLIESSPRKQnSLTTDMALRLIERLQSVDtWEVDRLDLWNTDLPdmngvTMDAKYAVFSGTPMTGEQADHWQRlnrf 81
Cdd:pfam02525   1 MKILIINAHPRPG-SFSSRLADALVEALKAAG-HEVTVRDLYALFLP-----VLDAEDLADLTYPQGAADVESEQE---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  82 vtQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTPEDGYIPVLPPRDVVVVTSSGGD---YTPGSGLEHE-D 157
Cdd:pfam02525  70 --ELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGGGLLGKKVLVIVTTGGPeyaYGKGGYNGFSlD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1326035869 158 FAYRYLQQWLQYCmGC-NVEFVHLtmtatgpEGVANAmkNAEFKIETMIEQYA 209
Cdd:pfam02525 148 ELLPYLRGILGFC-GItDLPPFAV-------EGTAGP--EDEAALAEALERYE 190
PRK00170 PRK00170
azoreductase; Reviewed
 1-202 3.54e-25

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 97.27  E-value: 3.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPRKQNSLTTDMALRLIERLQSVDTW-EVDRLDLWNTDLPDMNGVTMDAKYAvfSGTPMTGEQADHWQRLN 79
Cdd:PRK00170    1 MSKVLVIKSSILGDYSQSMQLGDAFIEAYKEAHPDdEVTVRDLAAEPIPVLDGEVVGALGK--SAETLTPRQQEAVALSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  80 RFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTpEDGYIPVLPPRDVVVVTSSGGDYTPGSglehEDFA 159
Cdd:PRK00170   79 ELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYT-ENGPVGLVTGKKALLITSRGGIHKDGP----TDMG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1326035869 160 YRYLQQWLQYCMGCNVEFVHLTMTATGPEGVANAMKNAEFKIE 202
Cdd:PRK00170  154 VPYLKTFLGFIGITDVEFVFAEGHNYGPEKAAKIISAAKAAAD 196
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
1-150 8.23e-17

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 75.57  E-value: 8.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPR-KQNSLTTDMALRLIERL-QSVDTWEVDRLDLWNTDLPDMNGVTMDAKYAVFSGTPMTGEQADHWQRL 78
Cdd:PRK13556    1 MSKVLFVKANNRpAEQAVSVKLYEAFLASYkEAHPNDTVVELDLYKEELPYVGVDMINGTFKAGKGFELTEEEAKAVAVA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1326035869  79 NRFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTPEdGYIPVLPPRDVVVVTSSGGDYTPG 150
Cdd:PRK13556   81 DKYLNQFLEADKVVFAFPLWNFTIPAVLHTYIDYLNRAGKTFKYTPE-GPVGLIGDKKVALLNARGGVYSEG 151
PRK13555 PRK13555
FMN-dependent NADH-azoreductase;
1-148 1.86e-13

FMN-dependent NADH-azoreductase;


Pssm-ID: 184139 [Multi-domain]  Cd Length: 208  Bit Score: 66.30  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPR-KQNSLTTDMALRLIERLQSVD-TWEVDRLDLWNTDLPDMNGVTMDAKYAVFSGTPMTGEQADHWQRL 78
Cdd:PRK13555    1 MSKVLFVKANDRpAEQAVSSKMYETFVSTYKEANpNTEITELDLFALDLPYYGNIAISGGYKRSQGMELTAEEEKAVATV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  79 NRFVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFNWTpEDGYIPVLPPRDVVVVTSSGGDYT 148
Cdd:PRK13555   81 DQYLNQFLEADKVVFAFPLWNFTVPAPLITYISYLSQAGKTFKYT-ANGPEGLAGGKKVVVLGARGSDYS 149
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
2-155 2.42e-08

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 51.31  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   2 KKLLLIESSPRKqNSLTTDMALRLIERLQSVDtWEVDRLDLWNTDLPdmngvtmdakyaVFSGTPMTGEQADHWQRLNRf 81
Cdd:COG0431     1 MKILVISGSLRP-GSFNRKLARAAAELAPAAG-AEVELIDLRDLDLP------------LYDEDLEADGAPPAVKALRE- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1326035869  82 vtQFAQADMVVLCAPMWNWGIPYRLKHYVDVItqPQLTFNWTPedgyipvlpprdVVVVTSSGGDYTPGSGLEH 155
Cdd:COG0431    66 --AIAAADGVVIVTPEYNGSYPGVLKNALDWL--SRSELAGKP------------VALVSTSGGARGGLRALEH 123
PRK01355 PRK01355
azoreductase; Reviewed
 1-151 2.97e-07

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 48.93  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSP-RKQNSLTTDMALRLIERLQSVD-TWEVDRLDLwNTDlpDMNGVTMDAK-YAVFsgtpMTGEQADHWqr 77
Cdd:PRK01355    1 MSKVLVIKGSMvAKEKSFSSALTDKFVEEYKKVNpNDEIIILDL-NET--KVGSVTLTSEnFKTF----FKEEVSDKY-- 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1326035869  78 lnrfVTQFAQADMVVLCAPMWNWGIPYRLKHYVDVITQPQLTFN--WTPEDGYIPVLPPRDVVVVTSSG---GDYTPGS 151
Cdd:PRK01355   72 ----INQLKSVDKVVISCPMTNFNVPATLKNYLDHIAVANKTFSykYSKKGDAIGLLDHLKVQILTTQGaplGWYPWGS 146
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-111 1.04e-06

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 47.39  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   1 MKKLLLIESSPRKqNSLTTDMALRLIERLQSVDtWEVDRLDL---------WNTDLPDMNgvTMDAKYAvfsgtpmtgeq 71
Cdd:PRK09739    3 SMRIYLVWAHPRH-DSLTAKVAEAIHQRAQERG-HQVEELDLyrsgfdpvlTPEDEPDWK--NPDKRYS----------- 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1326035869  72 adhwQRLNRFVTQFAQADMVVLCAPMWNWGIPYRLKHYVD 111
Cdd:PRK09739   68 ----PEVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYID 103
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-111 7.21e-05

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 41.46  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   3 KLLLIESSPRKqNSLTTDMALRLIERLQsvDTWEVDRLDLWNTDLPdmngvtmdakyAVFSGTPMTGEQADHWQRLNRfv 82
Cdd:pfam03358   2 KILAISGSPRK-GSNTRKLARWAAELLE--EGAEVELIDLADLILP-----------LCDEDLEEEQGDPDDVQELRE-- 65

                          90       100
                  ....*....|....*....|....*....
gi 1326035869  83 tQFAQADMVVLCAPMWNWGIPYRLKHYVD 111
Cdd:pfam03358  66 -KIAAADAIIIVTPEYNGSVSGLLKNAID 93
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-206 7.91e-05

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 41.84  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   3 KLLLIESSPRKqNSLTTDMALRLIERLQSVDtWEVDRLDLWNTDLPDMNGVTMDAKYAvfsgtpmtgeQADHWQRLnrfV 82
Cdd:COG0655     1 KILVINGSPRK-NGNTAALAEAVAEGAEEAG-AEVELIRLADLDIKPCIGCGGTGKCV----------IKDDMNAI---Y 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869  83 TQFAQADMVVLCAPMWNWGIPYRLKHYVDvitqpQLTFNWTPEDgyipVLPPRDVVVVTSSGGDytpgsGLEHedfAYRY 162
Cdd:COG0655    66 EKLLEADGIIFGSPTYFGNMSAQLKAFID-----RLYALWAKGK----LLKGKVGAVFTTGGHG-----GAEA---TLLS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1326035869 163 LQQWLQYcMGCNV--EFVHLTMTATGPEGVAN--AMKNAEFKIETMIE 206
Cdd:COG0655   129 LNTFLLH-HGMIVvgLPPYGAVGGGGPGDVLDeeGLATARELGKRLAE 175
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-146 9.91e-05

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 41.36  E-value: 9.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326035869   3 KLLLIESSPRKQnSLTTDMALRLIERLQSVDtWEVDRLDL----WNTDLPDMNGvtmdakyavFSGTPMTGEQADHWQRL 78
Cdd:COG2249     1 KILIIYAHPDPS-SFNAALAEAAAEGLEAAG-HEVTVHDLyaegFDPVLSAADF---------YRDGPLPIDVAAEQELL 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1326035869  79 nrfvtqfAQADMVVLCAPMWNWGIPYRLKHYVDVItqpqLTFNWT--PEDGYI-PVLPPRDVVVVTSSGGD 146
Cdd:COG2249    70 -------LWADHLVFQFPLWWYSMPALLKGWIDRV----LTPGFAygYGGGYPgGLLKGKKALLVVTTGGP 129
 
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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