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Conserved domains on  [gi|15225428|ref|NP_179673|]
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NAD(P)H dehydrogenase B4 [Arabidopsis thaliana]

Protein Classification

NAD(P)H-binding domain containing protein( domain architecture ID 1001497)

NAD(P)H-binding domain containing protein similar to the mitochondrial internal alternative NAD(P)H-ubiquinone oxidoreductase A, an NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH, but does not translocate protons across the inner mitochondrial membrane

EC:  1.6.-.-
Gene Ontology:  GO:0003959|GO:0016491
PubMed:  8805537

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00318 super family cl33177
NADH dehydrogenase-like protein; Provisional
 61-582 3.43e-131

NADH dehydrogenase-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00318:

Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 390.28  E-value: 3.43e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   61 IRKKKVVVLGSGWSGYSFLSYLNNPNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVKI 140
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  141 DASNKKIHCRSKEGSSLKGTTEFDMDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERASLPNLTE 220
Cdd:PTZ00318  88 DFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  221 EERKKILHFVVVGGGPTGVEFSAELHDFLVQDVAKIYPKVQEFTKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKT 300
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  301 GSMVVGVTADEISTKereTGKIVsePYGMVVWSTGIGSRPVIKDFmqQIGQGQRRVLATDEWLRVEGCDGVYALGDTATI 380
Cdd:PTZ00318 248 KTAVKEVLDKEVVLK---DGEVI--PTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  381 NQRrvmediaaifnkadkgntgtlkkkdfnsvvkdicqrypqvelylkknklknianllksangedtqvniekfkqalse 460
Cdd:PTZ00318 321 EER----------------------------------------------------------------------------- 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  461 vdsqmkNLPATAQVASQQGKYLAKCFNKMEKCEKKPegplrfrgegrhrfQPFRYRHFGSFAPLGGEQTAAELpGDWVSI 540
Cdd:PTZ00318 324 ------PLPTLAQVASQQGVYLAKEFNNELKGKPMS--------------KPFVYRSLGSLAYLGNYSAIVQL-GAFDLS 382

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 15225428  541 GHSSQWLWYSVYASKLVSWRTRMLVISDWTRRFVFGRDSSSI 582
Cdd:PTZ00318 383 GFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 61-582 3.43e-131

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 390.28  E-value: 3.43e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   61 IRKKKVVVLGSGWSGYSFLSYLNNPNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVKI 140
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  141 DASNKKIHCRSKEGSSLKGTTEFDMDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERASLPNLTE 220
Cdd:PTZ00318  88 DFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  221 EERKKILHFVVVGGGPTGVEFSAELHDFLVQDVAKIYPKVQEFTKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKT 300
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  301 GSMVVGVTADEISTKereTGKIVsePYGMVVWSTGIGSRPVIKDFmqQIGQGQRRVLATDEWLRVEGCDGVYALGDTATI 380
Cdd:PTZ00318 248 KTAVKEVLDKEVVLK---DGEVI--PTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  381 NQRrvmediaaifnkadkgntgtlkkkdfnsvvkdicqrypqvelylkknklknianllksangedtqvniekfkqalse 460
Cdd:PTZ00318 321 EER----------------------------------------------------------------------------- 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  461 vdsqmkNLPATAQVASQQGKYLAKCFNKMEKCEKKPegplrfrgegrhrfQPFRYRHFGSFAPLGGEQTAAELpGDWVSI 540
Cdd:PTZ00318 324 ------PLPTLAQVASQQGVYLAKEFNNELKGKPMS--------------KPFVYRSLGSLAYLGNYSAIVQL-GAFDLS 382

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 15225428  541 GHSSQWLWYSVYASKLVSWRTRMLVISDWTRRFVFGRDSSSI 582
Cdd:PTZ00318 383 GFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
63-566 1.25e-73

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 240.03  E-value: 1.25e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  63 KKKVVVLGSGWSGYSFLSYLNN---PNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVK 139
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 140 IDASNKKIHCRSkeGSSLkgttefdmDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERAslpnlt 219
Cdd:COG1252  81 IDPEARTVTLAD--GRTL--------SYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 220 eeERKKILHFvvvgggptgV---------EFSAELHDFLvqDVAKIYPKV-QEFTKITLLEAGDHILNMFDKRITAFAEE 289
Cdd:COG1252 145 --ERRRLLTI---------VvvgggptgvELAGELAELL--RKLLRYPGIdPDKVRITLVEAGPRILPGLGEKLSEAAEK 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 290 KFQRDGIDLKTGSMVVGVTADEISTKERETgkivsEPYGMVVWSTGIGSRPVIKDFMQQIGQGQRrvLATDEWLRVEGCD 369
Cdd:COG1252 212 ELEKRGVEVHTGTRVTEVDADGVTLEDGEE-----IPADTVIWAAGVKAPPLLADLGLPTDRRGR--VLVDPTLQVPGHP 284

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 370 GVYALGDTATInqrrvmediaaifnkadkgntgtlkkkdfnsvvkdicqrypqvelylkknklknianllksangedtqv 449
Cdd:COG1252 285 NVFAIGDCAAV--------------------------------------------------------------------- 295

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 450 niekfkqalseVDSQMKNLPATAQVASQQGKYLAKcfNKMEKCEKKPEgplrfrgegrhrfQPFRYRHFGSFAPLGGEQT 529
Cdd:COG1252 296 -----------PDPDGKPVPKTAQAAVQQAKVLAK--NIAALLRGKPL-------------KPFRYRDKGCLASLGRGAA 349

                       490       500       510
                ....*....|....*....|....*....|....*....
gi 15225428 530 AAELPGDWVS--IGHssqWLWYSVYASKLVSWRTRMLVI 566
Cdd:COG1252 350 VADVGGLKLSgfLAW---LLKRAIHLYFLPGFRGRLRVL 385
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 64-376 1.11e-36

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 138.61  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428    64 KKVVVLGSGWSGYSFLSYLNNPNYDVQVVS-PRNFFLFTPLLPSVTNGTVEARSI-------VEPIRGLMRKKGFEYK-- 133
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIaslwadlYKRKEEVVKKLNNGIEvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   134 -EAECVKIDASNKKIHCRSKEGSSlkgttEFDMDYDILILAVGAKPNTFNTPGVEEHAYFL-KEAEDALNIRHsvidcfe 211
Cdd:pfam07992  81 lGTEVVSIDPGAKKVVLEELVDGD-----GETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRL------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   212 raslpnltEEERKKI---------LhfvvvgggptgvEFSAELHDFLVqdvakiypkvqeftKITLLEAGDHILNMFDKR 282
Cdd:pfam07992 149 --------KLLPKRVvvvgggyigV------------ELAAALAKLGK--------------EVTLIEALDRLLRAFDEE 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   283 ITAFAEEKFQRDGIDLKTGSMVVGVTADEIS-TKERETGKIVsePYGMVVWSTGIGSRPVIKDFMqQIGQGQRRVLATDE 361
Cdd:pfam07992 195 ISAALEKALEKNGVEVRLGTSVKEIIGDGDGvEVILKDGTEI--DADLVVVAIGRRPNTELLEAA-GLELDERGGIVVDE 271

                         330
                  ....*....|....*
gi 15225428   362 WLRVEgCDGVYALGD 376
Cdd:pfam07992 272 YLRTS-VPGIYAAGD 285
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 61-582 3.43e-131

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 390.28  E-value: 3.43e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   61 IRKKKVVVLGSGWSGYSFLSYLNNPNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVKI 140
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  141 DASNKKIHCRSKEGSSLKGTTEFDMDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERASLPNLTE 220
Cdd:PTZ00318  88 DFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  221 EERKKILHFVVVGGGPTGVEFSAELHDFLVQDVAKIYPKVQEFTKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKT 300
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  301 GSMVVGVTADEISTKereTGKIVsePYGMVVWSTGIGSRPVIKDFmqQIGQGQRRVLATDEWLRVEGCDGVYALGDTATI 380
Cdd:PTZ00318 248 KTAVKEVLDKEVVLK---DGEVI--PTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  381 NQRrvmediaaifnkadkgntgtlkkkdfnsvvkdicqrypqvelylkknklknianllksangedtqvniekfkqalse 460
Cdd:PTZ00318 321 EER----------------------------------------------------------------------------- 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  461 vdsqmkNLPATAQVASQQGKYLAKCFNKMEKCEKKPegplrfrgegrhrfQPFRYRHFGSFAPLGGEQTAAELpGDWVSI 540
Cdd:PTZ00318 324 ------PLPTLAQVASQQGVYLAKEFNNELKGKPMS--------------KPFVYRSLGSLAYLGNYSAIVQL-GAFDLS 382

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 15225428  541 GHSSQWLWYSVYASKLVSWRTRMLVISDWTRRFVFGRDSSSI 582
Cdd:PTZ00318 383 GFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
63-566 1.25e-73

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 240.03  E-value: 1.25e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  63 KKKVVVLGSGWSGYSFLSYLNN---PNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVK 139
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 140 IDASNKKIHCRSkeGSSLkgttefdmDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERAslpnlt 219
Cdd:COG1252  81 IDPEARTVTLAD--GRTL--------SYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 220 eeERKKILHFvvvgggptgV---------EFSAELHDFLvqDVAKIYPKV-QEFTKITLLEAGDHILNMFDKRITAFAEE 289
Cdd:COG1252 145 --ERRRLLTI---------VvvgggptgvELAGELAELL--RKLLRYPGIdPDKVRITLVEAGPRILPGLGEKLSEAAEK 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 290 KFQRDGIDLKTGSMVVGVTADEISTKERETgkivsEPYGMVVWSTGIGSRPVIKDFMQQIGQGQRrvLATDEWLRVEGCD 369
Cdd:COG1252 212 ELEKRGVEVHTGTRVTEVDADGVTLEDGEE-----IPADTVIWAAGVKAPPLLADLGLPTDRRGR--VLVDPTLQVPGHP 284

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 370 GVYALGDTATInqrrvmediaaifnkadkgntgtlkkkdfnsvvkdicqrypqvelylkknklknianllksangedtqv 449
Cdd:COG1252 285 NVFAIGDCAAV--------------------------------------------------------------------- 295

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 450 niekfkqalseVDSQMKNLPATAQVASQQGKYLAKcfNKMEKCEKKPEgplrfrgegrhrfQPFRYRHFGSFAPLGGEQT 529
Cdd:COG1252 296 -----------PDPDGKPVPKTAQAAVQQAKVLAK--NIAALLRGKPL-------------KPFRYRDKGCLASLGRGAA 349

                       490       500       510
                ....*....|....*....|....*....|....*....
gi 15225428 530 AAELPGDWVS--IGHssqWLWYSVYASKLVSWRTRMLVI 566
Cdd:COG1252 350 VADVGGLKLSgfLAW---LLKRAIHLYFLPGFRGRLRVL 385
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 64-376 1.11e-36

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 138.61  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428    64 KKVVVLGSGWSGYSFLSYLNNPNYDVQVVS-PRNFFLFTPLLPSVTNGTVEARSI-------VEPIRGLMRKKGFEYK-- 133
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIaslwadlYKRKEEVVKKLNNGIEvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   134 -EAECVKIDASNKKIHCRSKEGSSlkgttEFDMDYDILILAVGAKPNTFNTPGVEEHAYFL-KEAEDALNIRHsvidcfe 211
Cdd:pfam07992  81 lGTEVVSIDPGAKKVVLEELVDGD-----GETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRL------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   212 raslpnltEEERKKI---------LhfvvvgggptgvEFSAELHDFLVqdvakiypkvqeftKITLLEAGDHILNMFDKR 282
Cdd:pfam07992 149 --------KLLPKRVvvvgggyigV------------ELAAALAKLGK--------------EVTLIEALDRLLRAFDEE 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   283 ITAFAEEKFQRDGIDLKTGSMVVGVTADEIS-TKERETGKIVsePYGMVVWSTGIGSRPVIKDFMqQIGQGQRRVLATDE 361
Cdd:pfam07992 195 ISAALEKALEKNGVEVRLGTSVKEIIGDGDGvEVILKDGTEI--DADLVVVAIGRRPNTELLEAA-GLELDERGGIVVDE 271

                         330
                  ....*....|....*
gi 15225428   362 WLRVEgCDGVYALGD 376
Cdd:pfam07992 272 YLRTS-VPGIYAAGD 285
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 83-380 5.14e-22

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 97.19  E-value: 5.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  83 NNPNYDVQVVSPRNFFLF--TPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYK-EAECVKIDASNKKIHCRSkegsslkG 159
Cdd:COG0446   2 LGPDAEITVIEKGPHHSYqpCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRD-------G 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 160 TTEfdmDYDILILAVGAKPNTFNTPGVE-EHAYFLKEAEDALNIRHSvidcferaslpnLTEEERKKILhfvvvgggptg 238
Cdd:COG0446  75 ETL---SYDKLVLATGARPRPPPIPGLDlPGVFTLRTLDDADALREA------------LKEFKGKRAV----------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 239 veFS------AELHDFLVQdvAKIypkvqeftKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADEI 312
Cdd:COG0446 129 --VIgggpigLELAEALRK--RGL--------KVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDK 196

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225428 313 STKERETGKIVsePYGMVVwsTGIGSRP---VIKDFmqQIGQGQRRVLATDEWLRVeGCDGVYALGDTATI 380
Cdd:COG0446 197 VAVTLTDGEEI--PADLVV--VAPGVRPnteLAKDA--GLALGERGWIKVDETLQT-SDPDVYAAGDCAEV 260
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 64-383 2.40e-14

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 75.46  E-value: 2.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428   64 KKVVVLGSGWSGYSFLSYL--NNPNYDVQVVSPRNFFLFTPL-LPSVTNG------TVEARSIVEPIrglmrKKGFEYK- 133
Cdd:PRK09564   1 MKIIIIGGTAAGMSAAAKAkrLNKELEITVYEKTDIVSFGACgLPYFVGGffddpnTMIARTPEEFI-----KSGIDVKt 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  134 EAECVKIDASNKKIHCRSkegssLKGTTEFDMDYDILILAVGAKPNTFNTPGVE-EHAYFLKEAEDALNIRHSVIDcfer 212
Cdd:PRK09564  76 EHEVVKVDAKNKTITVKN-----LKTGSIFNDTYDKLMIATGARPIIPPIKNINlENVYTLKSMEDGLALKELLKD---- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  213 aslpnlteEERKKILhfvvvgggptgvEFSAELHDFLVQDVAKIYPKvqeftKITLLEAGDHILN-MFDKRITAFAEEKF 291
Cdd:PRK09564 147 --------EEIKNIV------------IIGAGFIGLEAVEAAKHLGK-----NVRIIQLEDRILPdSFDKEITDVMEEEL 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  292 QRDGIDLKTGSMVVGVTADEISTKER-ETGKIVSEpygMVVWSTGIgsRP---VIKDfmQQIGQGQRRVLATDEWLRVEg 367
Cdd:PRK09564 202 RENGVELHLNEFVKSLIGEDKVEGVVtDKGEYEAD---VVIVATGV--KPnteFLED--TGLKTLKNGAIIVDEYGETS- 273

                        330
                 ....*....|....*.
gi 15225428  368 CDGVYALGDTATINQR 383
Cdd:PRK09564 274 IENIYAAGDCATIYNI 289
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 264-376 1.37e-12

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 70.12  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 264 TKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADE------ISTKERETGKIVSEpygmVVWSTGIg 337
Cdd:COG1249 192 SEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGdgvtvtLEDGGGEEAVEADK----VLVATGR- 266

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15225428 338 sRPVIKDF-MQQIG--QGQRRVLATDEWLRVeGCDGVYALGD 376
Cdd:COG1249 267 -RPNTDGLgLEAAGveLDERGGIKVDEYLRT-SVPGIYAIGD 306
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
63-384 2.75e-12

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 68.63  E-value: 2.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  63 KKKVVVLGSGWSGYSFLSYL--NNPNYDVQVVS-------PRnfflftPLLPSVTNGTVEARSIvepirgLMRKKGFeYK 133
Cdd:COG1251   1 KMRIVIIGAGMAGVRAAEELrkLDPDGEITVIGaephppyNR------PPLSKVLAGETDEEDL------LLRPADF-YE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 134 E--------AECVKIDASNKKIHCRSkeGSSLkgttefdmDYDILILAVGAKPNTFNTPGVE-EHAYFLKEAEDALNIRh 204
Cdd:COG1251  68 EngidlrlgTRVTAIDRAARTVTLAD--GETL--------PYDKLVLATGSRPRVPPIPGADlPGVFTLRTLDDADALR- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 205 svidcfERAslpnlteEERKKI---------LhfvvvgggptgvEFSAELHDflvQDVakiypkvqeftKITLLEAGDHI 275
Cdd:COG1251 137 ------AAL-------APGKRVvvigggligL------------EAAAALRK---RGL-----------EVTVVERAPRL 177

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428 276 LN-MFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADEISTK-ERETGKIVsePYGMVVWSTGIgsRPVIkDFMQQIG-QG 352
Cdd:COG1251 178 LPrQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGvRLADGEEL--PADLVVVAIGV--RPNT-ELARAAGlAV 252

                       330       340       350
                ....*....|....*....|....*....|..
gi 15225428 353 QRRVLaTDEWLRVeGCDGVYALGDTATINQRR 384
Cdd:COG1251 253 DRGIV-VDDYLRT-SDPDIYAAGDCAEHPGPV 282
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 264-376 3.04e-11

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 65.55  E-value: 3.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  264 TKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGV--TADEISTKERETGKIVSEPYGMVVWSTGIgsRPV 341
Cdd:PRK06416 196 AEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVeqTDDGVTVTLEDGGKEETLEADYVLVAVGR--RPN 273

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15225428  342 IKDF-MQQIG-QGQRRVLATDEWLRvEGCDGVYALGD 376
Cdd:PRK06416 274 TENLgLEELGvKTDRGFIEVDEQLR-TNVPNIYAIGD 309
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 265-311 2.20e-05

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 42.96  E-value: 2.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15225428   265 KITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADE 311
Cdd:pfam00070  24 KVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNG 70
PRK06370 PRK06370
FAD-containing oxidoreductase;
265-383 5.94e-04

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 42.50  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  265 KITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADEiSTKERETGKIVSEPYgmVVWS---TGIGSRPV 341
Cdd:PRK06370 196 EVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDG-DGIAVGLDCNGGAPE--ITGShilVAVGRVPN 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15225428  342 IKDF-MQQIG--QGQRRVLATDEWLRVEGcDGVYALGDtatINQR 383
Cdd:PRK06370 273 TDDLgLEAAGveTDARGYIKVDDQLRTTN-PGIYAAGD---CNGR 313
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 64-180 2.74e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 40.18  E-value: 2.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225428  64 KKVVVLGSGWSGYSFLSYLNNPNYDVQVV--SPRnffLFTPLLPSVTngtvearsivEPIRGLMRKKGFEYKEAECVK-I 140
Cdd:COG0446 125 KRAVVIGGGPIGLELAEALRKRGLKVTLVerAPR---LLGVLDPEMA----------ALLEEELREHGVELRLGETVVaI 191

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15225428 141 DASNK-KIHCRSKEgsslkgttefDMDYDILILAVGAKPNT 180
Cdd:COG0446 192 DGDDKvAVTLTDGE----------EIPADLVVVAPGVRPNT 222
 
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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