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Conserved domains on  [gi|6320118|ref|NP_010198|]
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NADH-ubiquinone reductase (H(+)-translocating) NDE2 [Saccharomyces cerevisiae S288C]

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
 95-544 9.89e-113

NADH dehydrogenase-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00318:

Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 341.36  E-value: 9.89e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    95 LKKKELVILGTGWGAISLLKKLDTSLYNVTVVSPRSFFLFTPLLPSTPVGTIEMKSIVEPVRSIARRTPGevHYIEAEAL 174
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPN--RYLRAVVY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   175 DVDPKAKKVMVQSVSEDEYFVS---SLSYDYLVVSVGAKTTTFNIPGVYGNANFLKEIEDAQNIRMKLMKTIEQASsFPV 251
Cdd:PTZ00318  86 DVDFEEKRVKCGVVSKSNNANVntfSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERAS-LPT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   252 NDPE-RKRLLTFVVVGGGPTGVEFAAELQDYINQDLRKWMPDLSKEMKVILIEALPNILNMFDKTLIKYAEDLFARDEID 330
Cdd:PTZ00318 165 TSVEeRKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   331 LQVNTAVKVVEPTYIrTLQNGQTntdIEYGMLVWATGNEPIDFSKTLMSripEQTNRRGLLINDKLELLGSENsIYAIGD 410
Cdd:PTZ00318 245 IRTKTAVKEVLDKEV-VLKDGEV---IPTGLVVWSTGVGPGPLTKQLKV---DKTSRGRISVDDHLRVKPIPN-VFALGD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   411 CTA--HTGFFPTAQVAHQEGEYLAKILDKKLQIEQLewdmlnstdetevsrlqkevnlrkSKldKFNYKHMGALAYIGSE 488
Cdd:PTZ00318 317 CAAneERPLPTLAQVASQQGVYLAKEFNNELKGKPM------------------------SK--PFVYRSLGSLAYLGNY 370

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320118   489 TAIADLHMGDSSyqlkGMFAFLFWKSAYLAMCLSIRNRILIAMDWTKVYFLGRDSS 544
Cdd:PTZ00318 371 SAIVQLGAFDLS----GFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDIT 422
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 95-544 9.89e-113

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 341.36  E-value: 9.89e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    95 LKKKELVILGTGWGAISLLKKLDTSLYNVTVVSPRSFFLFTPLLPSTPVGTIEMKSIVEPVRSIARRTPGevHYIEAEAL 174
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPN--RYLRAVVY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   175 DVDPKAKKVMVQSVSEDEYFVS---SLSYDYLVVSVGAKTTTFNIPGVYGNANFLKEIEDAQNIRMKLMKTIEQASsFPV 251
Cdd:PTZ00318  86 DVDFEEKRVKCGVVSKSNNANVntfSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERAS-LPT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   252 NDPE-RKRLLTFVVVGGGPTGVEFAAELQDYINQDLRKWMPDLSKEMKVILIEALPNILNMFDKTLIKYAEDLFARDEID 330
Cdd:PTZ00318 165 TSVEeRKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   331 LQVNTAVKVVEPTYIrTLQNGQTntdIEYGMLVWATGNEPIDFSKTLMSripEQTNRRGLLINDKLELLGSENsIYAIGD 410
Cdd:PTZ00318 245 IRTKTAVKEVLDKEV-VLKDGEV---IPTGLVVWSTGVGPGPLTKQLKV---DKTSRGRISVDDHLRVKPIPN-VFALGD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   411 CTA--HTGFFPTAQVAHQEGEYLAKILDKKLQIEQLewdmlnstdetevsrlqkevnlrkSKldKFNYKHMGALAYIGSE 488
Cdd:PTZ00318 317 CAAneERPLPTLAQVASQQGVYLAKEFNNELKGKPM------------------------SK--PFVYRSLGSLAYLGNY 370

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320118   489 TAIADLHMGDSSyqlkGMFAFLFWKSAYLAMCLSIRNRILIAMDWTKVYFLGRDSS 544
Cdd:PTZ00318 371 SAIVQLGAFDLS----GFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDIT 422
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
97-531 1.93e-76

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 246.20  E-value: 1.93e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   97 KKELVILGTGWGAISLLKKLDTSL---YNVTVVSPRSFFLFTPLLPSTPVGTIEMKSIVEPVRSIARRTpgEVHYIEAEA 173
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKKLggdAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRA--GVRFIQGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  174 LDVDPKAKKVMVQSVSEdeyfvssLSYDYLVVSVGAKTTTFNIPGVYGNANFLKEIEDAQNIRMKLMKTIEQAssfpvnd 253
Cdd:COG1252  79 TGIDPEARTVTLADGRT-------LSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  254 pERKRLLTFvvvgggptgV---------EFAAELQDYINQDLRKWMPDLSKeMKVILIEALPNILNMFDKTLIKYAEDLF 324
Cdd:COG1252 145 -ERRRLLTI---------VvvgggptgvELAGELAELLRKLLRYPGIDPDK-VRITLVEAGPRILPGLGEKLSEAAEKEL 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  325 ARDEIDLQVNTAVKVVEPTYIrTLQNGQTntdIEYGMLVWATGNEPIDFSKTLmsriPEQTNRRG-LLINDKLELLGSEN 403
Cdd:COG1252 214 EKRGVEVHTGTRVTEVDADGV-TLEDGEE---IPADTVIWAAGVKAPPLLADL----GLPTDRRGrVLVDPTLQVPGHPN 285

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  404 sIYAIGDCTAHTGFF-----PTAQVAHQEGEYLAKILdkklqieqlewdmlnstdeteVSRLQKEvnlrksKLDKFNYKH 478
Cdd:COG1252 286 -VFAIGDCAAVPDPDgkpvpKTAQAAVQQAKVLAKNI---------------------AALLRGK------PLKPFRYRD 337

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6320118  479 MGALAYIGSETAIADLhMGdssYQLKGMFAFLFWKSAYLAMCLSIRNRILIAM 531
Cdd:COG1252 338 KGCLASLGRGAAVADV-GG---LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 98-428 2.35e-30

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: 120.50  E-value: 2.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118     98 KELVILGTGWGAISLLKKLDTSLYNVTVVS-PRSFFLFTPLLPSTPVGTIEMKSI-------VEPVRSIARRTPGEVH-Y 168
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIaslwadlYKRKEEVVKKLNNGIEvL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    169 IEAEALDVDPKAKKVMVQSVSEDEYFvsSLSYDYLVVSVGAKTTTFNIPGVYGNANFL-KEIEDAQNIRMKLMktieqas 247
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEELVDGDGE--TITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLL------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    248 sfpvndpeRKRLL------TfvvvgggptGVEFAAELQDYInqdlrkwmpdlskeMKVILIEALPNILNMFDKTLIKYAE 321
Cdd:pfam07992 152 --------PKRVVvvgggyI---------GVELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAALE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    322 DLFARDEIDLQVNTAVKVVEP---TYIRTLQNGQTntdIEYGMLVWATGNEPidfSKTLMSRIP-EQTNRRGLLINDKLE 397
Cdd:pfam07992 201 KALEKNGVEVRLGTSVKEIIGdgdGVEVILKDGTE---IDADLVVVAIGRRP---NTELLEAAGlELDERGGIVVDEYLR 274

                         330       340       350
                  ....*....|....*....|....*....|.
gi 6320118    398 LlgSENSIYAIGDCTAHTgfFPTAQVAHQEG 428
Cdd:pfam07992 275 T--SVPGIYAAGDCRVGG--PELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 271-442 1.26e-07

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 54.19  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    271 GVEFAAELQDYinqdlrkwmpdlskEMKVILIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVE--PTYIRTL 348
Cdd:TIGR01350 182 GIEFASIFASL--------------GSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEknDDQVTYE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    349 QNGQTNTDIEYGMLVWATGNEP----IDFSKTLMsripEQTNRRGLLINDKLELlgSENSIYAIGDCtahTGFFPTAQVA 424
Cdd:TIGR01350 248 NKGGETETLTGEKVLVAVGRKPntegLGLEKLGV----ELDERGRIVVDEYMRT--NVPGIYAIGDV---IGGPMLAHVA 318

                         170
                  ....*....|....*...
gi 6320118    425 HQEGEYLAKILDKKLQIE 442
Cdd:TIGR01350 319 SHEGIVAAENIAGKEPAH 336
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 95-544 9.89e-113

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 341.36  E-value: 9.89e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    95 LKKKELVILGTGWGAISLLKKLDTSLYNVTVVSPRSFFLFTPLLPSTPVGTIEMKSIVEPVRSIARRTPGevHYIEAEAL 174
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPN--RYLRAVVY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   175 DVDPKAKKVMVQSVSEDEYFVS---SLSYDYLVVSVGAKTTTFNIPGVYGNANFLKEIEDAQNIRMKLMKTIEQASsFPV 251
Cdd:PTZ00318  86 DVDFEEKRVKCGVVSKSNNANVntfSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERAS-LPT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   252 NDPE-RKRLLTFVVVGGGPTGVEFAAELQDYINQDLRKWMPDLSKEMKVILIEALPNILNMFDKTLIKYAEDLFARDEID 330
Cdd:PTZ00318 165 TSVEeRKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   331 LQVNTAVKVVEPTYIrTLQNGQTntdIEYGMLVWATGNEPIDFSKTLMSripEQTNRRGLLINDKLELLGSENsIYAIGD 410
Cdd:PTZ00318 245 IRTKTAVKEVLDKEV-VLKDGEV---IPTGLVVWSTGVGPGPLTKQLKV---DKTSRGRISVDDHLRVKPIPN-VFALGD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   411 CTA--HTGFFPTAQVAHQEGEYLAKILDKKLQIEQLewdmlnstdetevsrlqkevnlrkSKldKFNYKHMGALAYIGSE 488
Cdd:PTZ00318 317 CAAneERPLPTLAQVASQQGVYLAKEFNNELKGKPM------------------------SK--PFVYRSLGSLAYLGNY 370

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320118   489 TAIADLHMGDSSyqlkGMFAFLFWKSAYLAMCLSIRNRILIAMDWTKVYFLGRDSS 544
Cdd:PTZ00318 371 SAIVQLGAFDLS----GFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDIT 422
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
97-531 1.93e-76

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 246.20  E-value: 1.93e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   97 KKELVILGTGWGAISLLKKLDTSL---YNVTVVSPRSFFLFTPLLPSTPVGTIEMKSIVEPVRSIARRTpgEVHYIEAEA 173
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKKLggdAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRA--GVRFIQGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  174 LDVDPKAKKVMVQSVSEdeyfvssLSYDYLVVSVGAKTTTFNIPGVYGNANFLKEIEDAQNIRMKLMKTIEQAssfpvnd 253
Cdd:COG1252  79 TGIDPEARTVTLADGRT-------LSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  254 pERKRLLTFvvvgggptgV---------EFAAELQDYINQDLRKWMPDLSKeMKVILIEALPNILNMFDKTLIKYAEDLF 324
Cdd:COG1252 145 -ERRRLLTI---------VvvgggptgvELAGELAELLRKLLRYPGIDPDK-VRITLVEAGPRILPGLGEKLSEAAEKEL 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  325 ARDEIDLQVNTAVKVVEPTYIrTLQNGQTntdIEYGMLVWATGNEPIDFSKTLmsriPEQTNRRG-LLINDKLELLGSEN 403
Cdd:COG1252 214 EKRGVEVHTGTRVTEVDADGV-TLEDGEE---IPADTVIWAAGVKAPPLLADL----GLPTDRRGrVLVDPTLQVPGHPN 285

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  404 sIYAIGDCTAHTGFF-----PTAQVAHQEGEYLAKILdkklqieqlewdmlnstdeteVSRLQKEvnlrksKLDKFNYKH 478
Cdd:COG1252 286 -VFAIGDCAAVPDPDgkpvpKTAQAAVQQAKVLAKNI---------------------AALLRGK------PLKPFRYRD 337

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6320118  479 MGALAYIGSETAIADLhMGdssYQLKGMFAFLFWKSAYLAMCLSIRNRILIAM 531
Cdd:COG1252 338 KGCLASLGRGAAVADV-GG---LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 98-428 2.35e-30

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: 120.50  E-value: 2.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118     98 KELVILGTGWGAISLLKKLDTSLYNVTVVS-PRSFFLFTPLLPSTPVGTIEMKSI-------VEPVRSIARRTPGEVH-Y 168
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIaslwadlYKRKEEVVKKLNNGIEvL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    169 IEAEALDVDPKAKKVMVQSVSEDEYFvsSLSYDYLVVSVGAKTTTFNIPGVYGNANFL-KEIEDAQNIRMKLMktieqas 247
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEELVDGDGE--TITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLL------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    248 sfpvndpeRKRLL------TfvvvgggptGVEFAAELQDYInqdlrkwmpdlskeMKVILIEALPNILNMFDKTLIKYAE 321
Cdd:pfam07992 152 --------PKRVVvvgggyI---------GVELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAALE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    322 DLFARDEIDLQVNTAVKVVEP---TYIRTLQNGQTntdIEYGMLVWATGNEPidfSKTLMSRIP-EQTNRRGLLINDKLE 397
Cdd:pfam07992 201 KALEKNGVEVRLGTSVKEIIGdgdGVEVILKDGTE---IDADLVVVAIGRRP---NTELLEAAGlELDERGGIVVDEYLR 274

                         330       340       350
                  ....*....|....*....|....*....|.
gi 6320118    398 LlgSENSIYAIGDCTAHTgfFPTAQVAHQEG 428
Cdd:pfam07992 275 T--SVPGIYAAGDCRVGG--PELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 152-446 1.34e-17

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: 83.71  E-value: 1.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  152 VEPVRSIARRTPGEV------HYIEAEALDVDPKAKKVMVQSVSEdeyfvssLSYDYLVVSVGAKTTTFNIPGV-YGNAN 224
Cdd:COG0446  32 IKDPEDLLVRTPESFerkgidVRTGTEVTAIDPEAKTVTLRDGET-------LSYDKLVLATGARPRPPPIPGLdLPGVF 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  225 FLKEIEDAQNIRMKLmktieqassfpvNDPERKRLLtfvvvgggptgveF------AAELQDYinqdLRKWmpdlskEMK 298
Cdd:COG0446 105 TLRTLDDADALREAL------------KEFKGKRAV-------------VigggpiGLELAEA----LRKR------GLK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  299 VILIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVEPT--YIRTLQNGQTntdIEYGMLVWATGNEP-IDFSK 375
Cdd:COG0446 150 VTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDdkVAVTLTDGEE---IPADLVVVAPGVRPnTELAK 226

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320118  376 TlmSRIpEQTNRRGLLINDKLELlgSENSIYAIGDCTAH-------TGFFPTAQVAHQEGEYLAK-ILDKKLQIEQLEW 446
Cdd:COG0446 227 D--AGL-ALGERGWIKVDETLQT--SDPDVYAAGDCAEVphpvtgkTVYIPLASAANKQGRVAAEnILGGPAPFPGLGT 300
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 271-438 6.55e-09

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: 58.17  E-value: 6.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  271 GVEFA---AELQdyinqdlrkwmpdlskeMKVILIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVEPT---Y 344
Cdd:COG1249 180 GLEFAqifARLG-----------------SEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTgdgV 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  345 IRTLQNGQTNTDIEYGMLVWATGnepidfsktlmsRIP------------EQTNRRGLLINDKLELlgSENSIYAIGDCt 412
Cdd:COG1249 243 TVTLEDGGGEEAVEADKVLVATG------------RRPntdglgleaagvELDERGGIKVDEYLRT--SVPGIYAIGDV- 307

                       170       180
                ....*....|....*....|....*..
gi 6320118  413 ahTGFFPTAQVAHQEGEYLAK-ILDKK 438
Cdd:COG1249 308 --TGGPQLAHVASAEGRVAAEnILGKK 332
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 271-442 1.26e-07

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 54.19  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    271 GVEFAAELQDYinqdlrkwmpdlskEMKVILIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVE--PTYIRTL 348
Cdd:TIGR01350 182 GIEFASIFASL--------------GSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEknDDQVTYE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    349 QNGQTNTDIEYGMLVWATGNEP----IDFSKTLMsripEQTNRRGLLINDKLELlgSENSIYAIGDCtahTGFFPTAQVA 424
Cdd:TIGR01350 248 NKGGETETLTGEKVLVAVGRKPntegLGLEKLGV----ELDERGRIVVDEYMRT--NVPGIYAIGDV---IGGPMLAHVA 318

                         170
                  ....*....|....*...
gi 6320118    425 HQEGEYLAKILDKKLQIE 442
Cdd:TIGR01350 319 SHEGIVAAENIAGKEPAH 336
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 298-418 1.93e-07

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 53.61  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   298 KVILIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVEPT---YIRTLQNGQTNTDIEYGMLVWATGnepidfs 374
Cdd:PRK06416 197 EVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTddgVTVTLEDGGKEETLEADYVLVAVG------- 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   375 ktlmsRIP-------EQ----TNRRGLLINDKLElLGSENsIYAIGDCT-----AHTGFF 418
Cdd:PRK06416 270 -----RRPntenlglEElgvkTDRGFIEVDEQLR-TNVPN-IYAIGDIVggpmlAHKASA 322
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 153-411 2.07e-07

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 53.51  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   153 EPVRSIARrTPGEVH------YIEAEALDVDPKAKKVMVQSVSEDEYFvsSLSYDYLVVSVGAKTTTFNIPGV-YGNANF 225
Cdd:PRK09564  54 DPNTMIAR-TPEEFIksgidvKTEHEVVKVDAKNKTITVKNLKTGSIF--NDTYDKLMIATGARPIIPPIKNInLENVYT 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   226 LKEIEDAQNIRmKLMKtieqassfpvnDPERKRLLTFVVvgggptgvefaaelqDYINQDLRKWMPDLSKEMKVILIEAl 305
Cdd:PRK09564 131 LKSMEDGLALK-ELLK-----------DEEIKNIVIIGA---------------GFIGLEAVEAAKHLGKNVRIIQLED- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   306 pNILN-MFDKTLIKYAEDLFARDEIDLQVNTAVKVVEP----TYIRTlQNGQTNTDIeygmLVWATGNEP-IDFSKTlmS 379
Cdd:PRK09564 183 -RILPdSFDKEITDVMEEELRENGVELHLNEFVKSLIGedkvEGVVT-DKGEYEADV----VIVATGVKPnTEFLED--T 254

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6320118   380 RIPEQTNrrGLLINDKLELLGSENsIYAIGDC 411
Cdd:PRK09564 255 GLKTLKN--GAIIVDEYGETSIEN-IYAAGDC 283
PRK06116 PRK06116
glutathione reductase; Validated
 308-435 4.15e-06

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 49.38  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   308 ILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVEPT----YIRTLQNGQTntdIEYGMLVWATGNEP----IDFSKTLMs 379
Cdd:PRK06116 202 PLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNadgsLTLTLEDGET---LTVDCLIWAIGREPntdgLGLENAGV- 277

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320118   380 ripeQTNRRGLLINDKLELLgSENSIYAIGDCTAHTGFFPtaqVAHQEGEYLAKIL 435
Cdd:PRK06116 278 ----KLNEKGYIIVDEYQNT-NVPGIYAVGDVTGRVELTP---VAIAAGRRLSERL 325
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
97-435 2.52e-05

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 46.67  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   97 KKELVILGTGWGAISL---LKKLDTSlYNVTVVS-------PRsfflftPLLPSTPVGTIEMKSIVEPVRSIARRTPGEV 166
Cdd:COG1251   1 KMRIVIIGAGMAGVRAaeeLRKLDPD-GEITVIGaephppyNR------PPLSKVLAGETDEEDLLLRPADFYEENGIDL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  167 HYiEAEALDVDPKAKKVmvqsVSEDEyfvSSLSYDYLVVSVGAKTTTFNIPGVYGNANF-LKEIEDAQNIRmklmktiEQ 245
Cdd:COG1251  74 RL-GTRVTAIDRAARTV----TLADG---ETLPYDKLVLATGSRPRVPPIPGADLPGVFtLRTLDDADALR-------AA 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  246 AssfpvndPERKRLLtfvvvgggPTGVEFAAelqdyinqDLRKwmpdlsKEMKVILIEALPNILN-MFDKTLIKYAEDLF 324
Cdd:COG1251 139 L-------APGKRVVvig---ggLIGLEAAA--------ALRK------RGLEVTVVERAPRLLPrQLDEEAGALLQRLL 194

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118  325 ARDEIDLQVNTAVKVVEPT---YIRTLQNGQTntdIEYGMLVWATGNEP-IDFSKTlmSRIPeqTNrRGLLINDKLELlg 400
Cdd:COG1251 195 EALGVEVRLGTGVTEIEGDdrvTGVRLADGEE---LPADLVVVAIGVRPnTELARA--AGLA--VD-RGIVVDDYLRT-- 264

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 6320118  401 SENSIYAIGDCTAHTGFF------PTAQVAHQEGEYLAKIL 435
Cdd:COG1251 265 SDPDIYAAGDCAEHPGPVygrrvlELVAPAYEQARVAAANL 305
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 298-428 1.24e-03

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 41.25  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118    298 KVILIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVE---PTYIRTLQNGQTNTDIEYGMLVWATGNEPIDFS 374
Cdd:TIGR02053 191 EVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSvrgGGKIITVEKPGGQGEVEADELLVATGRRPNTDG 270

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6320118    375 KTLMSRIPEQTNRRGLLINDKLELlgSENSIYAIGDCTAHTGFFPtaqVAHQEG 428
Cdd:TIGR02053 271 LGLEKAGVKLDERGGILVDETLRT--SNPGIYAAGDVTGGLQLEY---VAAKEG 319
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
329-411 4.99e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 39.51  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320118   329 IDLQVNTAVKVVEPT---YIRTLQNGQTntdIEYGMLVWATGNEPidfsKTLMSRIPEQTNRRGLLINDKLELlgSENSI 405
Cdd:PRK04965 198 VHLLLKSQLQGLEKTdsgIRATLDSGRS---IEVDAVIAAAGLRP----NTALARRAGLAVNRGIVVDSYLQT--SAPDI 268


                 ....*.
gi 6320118   406 YAIGDC 411
Cdd:PRK04965 269 YALGDC 274
 
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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