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Conserved domains on  [gi|767224359|gb|AJT02947|]
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Aif1p [Saccharomyces cerevisiae YJM244]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 1903257)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant, similar to Homo sapiens ferroptosis suppressor protein and Saccharomyces cerevisiae apoptosis-inducing factor

CATH:  3.50.50.100
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  31810296

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Ndh super family cl43367
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
5-363 2.93e-25

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


The actual alignment was detected with superfamily member COG1252:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 105.60  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   5 TKNIVVvgagvfgvsvANHLYRELGGTYAIKLVTASNYVYFLPS----AV-RLTVSKDytksILPLKNVL-DSGIEVIKD 78
Cdd:COG1252    1 MKRIVIvgggfagleaARRLRKKLGGDAEVTLIDPNPYHLFQPLlpevAAgTLSPDDI----AIPLRELLrRAGVRFIQG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  79 TAASFD--DKEVVLGSDRAIKFDILVLATGSKWAD--------------PIGSTYTFGDNYKEYFEReASRISDAdHILF 142
Cdd:COG1252   77 EVTGIDpeARTVTLADGRTLSYDYLVIATGSVTNFfgipglaehalplkTLEDALALRERLLAAFER-AERRRLL-TIVV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 143 LGGGFVNCELAGEL--LFKYL---EEIRSGKKRISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGASLDt 217
Cdd:COG1252  155 VGGGPTGVELAGELaeLLRKLlryPGIDPDKVRITLVEAGPRILPG---LGEKLSEAAEKELEKRGVEVHTGTRVTEVD- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 218 sPKRIFLGEGSSkyIDADLIYRGVGISPNvPVNSISDL-CDKKGFIQVEKNFRVKAVEagNVFAIGDVTNFRYHGlvkrD 296
Cdd:COG1252  231 -ADGVTLEDGEE--IPADTVIWAAGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPD----G 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 297 NWV-----------DVLTRNVISSLQEGTEASLV--DADCLetghapsgVSLGPNAGFGQfplplLGTINIPSFLISRAK 363
Cdd:COG1252  301 KPVpktaqaavqqaKVLAKNIAALLRGKPLKPFRyrDKGCL--------ASLGRGAAVAD-----VGGLKLSGFLAWLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
5-363 2.93e-25

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 105.60  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   5 TKNIVVvgagvfgvsvANHLYRELGGTYAIKLVTASNYVYFLPS----AV-RLTVSKDytksILPLKNVL-DSGIEVIKD 78
Cdd:COG1252    1 MKRIVIvgggfagleaARRLRKKLGGDAEVTLIDPNPYHLFQPLlpevAAgTLSPDDI----AIPLRELLrRAGVRFIQG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  79 TAASFD--DKEVVLGSDRAIKFDILVLATGSKWAD--------------PIGSTYTFGDNYKEYFEReASRISDAdHILF 142
Cdd:COG1252   77 EVTGIDpeARTVTLADGRTLSYDYLVIATGSVTNFfgipglaehalplkTLEDALALRERLLAAFER-AERRRLL-TIVV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 143 LGGGFVNCELAGEL--LFKYL---EEIRSGKKRISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGASLDt 217
Cdd:COG1252  155 VGGGPTGVELAGELaeLLRKLlryPGIDPDKVRITLVEAGPRILPG---LGEKLSEAAEKELEKRGVEVHTGTRVTEVD- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 218 sPKRIFLGEGSSkyIDADLIYRGVGISPNvPVNSISDL-CDKKGFIQVEKNFRVKAVEagNVFAIGDVTNFRYHGlvkrD 296
Cdd:COG1252  231 -ADGVTLEDGEE--IPADTVIWAAGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPD----G 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 297 NWV-----------DVLTRNVISSLQEGTEASLV--DADCLetghapsgVSLGPNAGFGQfplplLGTINIPSFLISRAK 363
Cdd:COG1252  301 KPVpktaqaavqqaKVLAKNIAALLRGKPLKPFRyrDKGCL--------ASLGRGAAVAD-----VGGLKLSGFLAWLLK 367
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 71-285 4.29e-21

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: 92.38  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   71 SGIEVIKDtAASFDDKEVVLGSDRAIKFDILVLATGSKWADP--IGSTYTFGDNYKEYfeREASRISDAD---HILFLGG 145
Cdd:pfam07992  84 EVVSIDPG-AKKVVLEELVDGDGETITYDRLVIATGARPRLPpiPGVELNVGFLVRTL--DSAEALRLKLlpkRVVVVGG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  146 GFVNCELAGELlfkyleeiRSGKKRISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNT--VGASLDTSPKRIF 223
Cdd:pfam07992 161 GYIGVELAAAL--------AKLGKEVTLIEALDRLLR---AFDEEISAALEKALEKNGVEVRLGTsvKEIIGDGDGVEVI 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767224359  224 LGEGssKYIDADLIYRGVGISPNVPVNSISDL-CDKKGFIQVEKNFRVKaveAGNVFAIGDVT 285
Cdd:pfam07992 230 LKDG--TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTS---VPGIYAAGDCR 287
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
85-283 5.03e-12

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 66.48  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  85 DKEVVLGSDRAIKFDILVLATGSK-WADPI---GSTYTFgDNYKEYFEREAsRISDADHILFLGGGFVNCELAGELlfky 160
Cdd:PRK04965  87 EAQVVKSQGNQWQYDKLVLATGASaFVPPIpgrELMLTL-NSQQEYRAAET-QLRDAQRVLVVGGGLIGTELAMDL---- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 161 leeIRSGkKRISIIHNSDKLLPdsGLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYIDADLIYRG 240
Cdd:PRK04965 161 ---CRAG-KAVTLVDNAASLLA--SLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAA 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767224359 241 VGISPNVPVNSISDLCDKKGfIQVEKNFRVKAVeagNVFAIGD 283
Cdd:PRK04965 235 AGLRPNTALARRAGLAVNRG-IVVDSYLQTSAP---DIYALGD 273
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 25-286 2.11e-08

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 55.75  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   25 YRELGGT------YAIKL-VTASNYVYFLPSAV-------RLTVSKDYtKSILPLKNVLDSGIE-----VIKDTAA---- 81
Cdd:TIGR01423  44 YAALGGTcvnvgcVPKKLmVTGAQYMDTLRESAgfgwefdRSSVKANW-KALIAAKNKAVLDINksyegMFADTEGltff 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   82 ----SFDDKEVVLGSDRA---------IKFDILVLATGSkWADPI---GSTYTFGDNYKEYFEREASRIsdadhiLFLGG 145
Cdd:TIGR01423 123 lgwgALEDKNVVLVRESAdpksavkerLQAEHILLATGS-WPQMLgipGIEHCISSNEAFYLDEPPRRV------LTVGG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  146 GFVNCELAGelLFKYLEEiRSGKkrISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGA--SLDTSPKRIF 223
Cdd:TIGR01423 196 GFISVEFAG--IFNAYKP-RGGK--VTLCYRNNMILRG---FDSTLRKELTKQLRANGINIMTNENPAkvTLNADGSKHV 267

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767224359  224 LGEgSSKYIDADLIYRGVGISP---NVPVNSISDLCDKKGFIQVEKNFRVKaveAGNVFAIGDVTN 286
Cdd:TIGR01423 268 TFE-SGKTLDVDVVMMAIGRVPrtqTLQLDKVGVELTKKGAIQVDEFSRTN---VPNIYAIGDVTD 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
5-363 2.93e-25

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 105.60  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   5 TKNIVVvgagvfgvsvANHLYRELGGTYAIKLVTASNYVYFLPS----AV-RLTVSKDytksILPLKNVL-DSGIEVIKD 78
Cdd:COG1252    1 MKRIVIvgggfagleaARRLRKKLGGDAEVTLIDPNPYHLFQPLlpevAAgTLSPDDI----AIPLRELLrRAGVRFIQG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  79 TAASFD--DKEVVLGSDRAIKFDILVLATGSKWAD--------------PIGSTYTFGDNYKEYFEReASRISDAdHILF 142
Cdd:COG1252   77 EVTGIDpeARTVTLADGRTLSYDYLVIATGSVTNFfgipglaehalplkTLEDALALRERLLAAFER-AERRRLL-TIVV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 143 LGGGFVNCELAGEL--LFKYL---EEIRSGKKRISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGASLDt 217
Cdd:COG1252  155 VGGGPTGVELAGELaeLLRKLlryPGIDPDKVRITLVEAGPRILPG---LGEKLSEAAEKELEKRGVEVHTGTRVTEVD- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 218 sPKRIFLGEGSSkyIDADLIYRGVGISPNvPVNSISDL-CDKKGFIQVEKNFRVKAVEagNVFAIGDVTNFRYHGlvkrD 296
Cdd:COG1252  231 -ADGVTLEDGEE--IPADTVIWAAGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPD----G 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 297 NWV-----------DVLTRNVISSLQEGTEASLV--DADCLetghapsgVSLGPNAGFGQfplplLGTINIPSFLISRAK 363
Cdd:COG1252  301 KPVpktaqaavqqaKVLAKNIAALLRGKPLKPFRyrDKGCL--------ASLGRGAAVAD-----VGGLKLSGFLAWLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 27-299 2.26e-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: 96.42  E-value: 2.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  27 ELGGTYAIKLVTASNYVYF----LPSAVRLTVSKDYTKSILPLKNVLDSGIEVI-KDTAASFD--DKEVVLGSDRAIKFD 99
Cdd:COG0446    1 RLGPDAEITVIEKGPHHSYqpcgLPYYVGGGIKDPEDLLVRTPESFERKGIDVRtGTEVTAIDpeAKTVTLRDGETLSYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 100 ILVLATGSK--WaDPI-GST----YTFGdNYKEYFE-REASRISDADHILFLGGGFVNCELAgellfkylEEIRSGKKRI 171
Cdd:COG0446   81 KLVLATGARprP-PPIpGLDlpgvFTLR-TLDDADAlREALKEFKGKRAVVIGGGPIGLELA--------EALRKRGLKV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 172 SIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPK-RIFLGEGSSkyIDADLIYRGVGISPNVPVN 250
Cdd:COG0446  151 TLVERAPRLLG---VLDPEMAALLEEELREHGVELRLGETVVAIDGDDKvAVTLTDGEE--IPADLVVVAPGVRPNTELA 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767224359 251 SISDL-CDKKGFIQVEKNFRVKaveAGNVFAIGDVTNFrYHGLVKRDNWV 299
Cdd:COG0446  226 KDAGLaLGERGWIKVDETLQTS---DPDVYAAGDCAEV-PHPVTGKTVYI 271
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 71-285 4.29e-21

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: 92.38  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   71 SGIEVIKDtAASFDDKEVVLGSDRAIKFDILVLATGSKWADP--IGSTYTFGDNYKEYfeREASRISDAD---HILFLGG 145
Cdd:pfam07992  84 EVVSIDPG-AKKVVLEELVDGDGETITYDRLVIATGARPRLPpiPGVELNVGFLVRTL--DSAEALRLKLlpkRVVVVGG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  146 GFVNCELAGELlfkyleeiRSGKKRISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNT--VGASLDTSPKRIF 223
Cdd:pfam07992 161 GYIGVELAAAL--------AKLGKEVTLIEALDRLLR---AFDEEISAALEKALEKNGVEVRLGTsvKEIIGDGDGVEVI 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767224359  224 LGEGssKYIDADLIYRGVGISPNVPVNSISDL-CDKKGFIQVEKNFRVKaveAGNVFAIGDVT 285
Cdd:pfam07992 230 LKDG--TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTS---VPGIYAAGDCR 287
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 72-286 2.04e-16

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: 80.13  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  72 GIEVIKDTAaSF-DDKEVVLGSDRAIKFDILVLATGSKWADPigstytfgdnykEYFEREASRISDAD----------HI 140
Cdd:COG1249  105 GVDVIRGRA-RFvDPHTVEVTGGETLTADHIVIATGSRPRVP------------PIPGLDEVRVLTSDealeleelpkSL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 141 LFLGGGFVNCELAGelLFKYLeeirsGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNT--VGASLDTS 218
Cdd:COG1249  172 VVIGGGYIGLEFAQ--IFARL-----GSE-VTLVERGDRLLP---GEDPEISEALEKALEKEGIDILTGAkvTSVEKTGD 240

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767224359 219 PKRIFL-GEGSSKYIDADLIYRGVGISPNVpvnsiSDL--------CDKKGFIQVEKNFRVKaveAGNVFAIGDVTN 286
Cdd:COG1249  241 GVTVTLeDGGGEEAVEADKVLVATGRRPNT-----DGLgleaagveLDERGGIKVDEYLRTS---VPGIYAIGDVTG 309
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
70-288 3.85e-13

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 70.17  E-value: 3.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  70 DSGIEVIKDTAAS---FDDKEVVLGSDRAIKFDILVLATGSK-WADPI-GST----YTFGDnyKEYFEREASRISDADHI 140
Cdd:COG1251   68 ENGIDLRLGTRVTaidRAARTVTLADGETLPYDKLVLATGSRpRVPPIpGADlpgvFTLRT--LDDADALRAALAPGKRV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 141 LFLGGGFVNCELAGELlfkyleeiRSGKKRISIIHNSDKLLPD------SGLYNDTLRknvtdylsKNGITLYLNTVGAS 214
Cdd:COG1251  146 VVIGGGLIGLEAAAAL--------RKRGLEVTVVERAPRLLPRqldeeaGALLQRLLE--------ALGVEVRLGTGVTE 209

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767224359 215 L--DTSPKRIFLGEGSSkyIDADLIYRGVGISPNVpvnsisDLCDKKGfIQVEKNFRVKA---VEAGNVFAIGDVTNFR 288
Cdd:COG1251  210 IegDDRVTGVRLADGEE--LPADLVVVAIGVRPNT------ELARAAG-LAVDRGIVVDDylrTSDPDIYAAGDCAEHP 279
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
85-283 5.03e-12

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 66.48  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  85 DKEVVLGSDRAIKFDILVLATGSK-WADPI---GSTYTFgDNYKEYFEREAsRISDADHILFLGGGFVNCELAGELlfky 160
Cdd:PRK04965  87 EAQVVKSQGNQWQYDKLVLATGASaFVPPIpgrELMLTL-NSQQEYRAAET-QLRDAQRVLVVGGGLIGTELAMDL---- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 161 leeIRSGkKRISIIHNSDKLLPdsGLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYIDADLIYRG 240
Cdd:PRK04965 161 ---CRAG-KAVTLVDNAASLLA--SLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAA 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767224359 241 VGISPNVPVNSISDLCDKKGfIQVEKNFRVKAVeagNVFAIGD 283
Cdd:PRK04965 235 AGLRPNTALARRAGLAVNRG-IVVDSYLQTSAP---DIYALGD 273
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 53-288 5.46e-10

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 60.58  E-value: 5.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  53 TVSKDYTKSILplKNVLD-SGIEVIKDTAASFDDKEVVLGSDRaIKFDILVLATGSKWAdPI-GSTYTFGDNYkeYFERE 130
Cdd:PRK06292  88 RERDRFVGGVV--EGLEKkPKIDKIKGTARFVDPNTVEVNGER-IEAKNIVIATGSRVP-PIpGVWLILGDRL--LTSDD 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 131 ASRISDA-DHILFLGGGFVNCELAgellfKYLEeiRSGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNgITLYLN 209
Cdd:PRK06292 162 AFELDKLpKSLAVIGGGVIGLELG-----QALS--RLGVK-VTVFERGDRILP---LEDPEVSKQAQKILSKE-FKIKLG 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 210 T----VGASlDTSPKRIFLGEGSSKYIDADLIYRGVGISPNVPVNSISDL---CDKKGFIQVEKNFRvKAVEagNVFAIG 282
Cdd:PRK06292 230 AkvtsVEKS-GDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTgieLDERGRPVVDEHTQ-TSVP--GIYAAG 305


                 ....*.
gi 767224359 283 DVTNFR 288
Cdd:PRK06292 306 DVNGKP 311
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 139-220 2.83e-09

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: 53.36  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  139 HILFLGGGFVNCELAGELLfkyleeiRSGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTS 218
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALA-------RLGSK-VTVVERRDRLLP---GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGN 69


                  ..
gi 767224359  219 PK 220
Cdd:pfam00070  70 GD 71
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 25-286 2.11e-08

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 55.75  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   25 YRELGGT------YAIKL-VTASNYVYFLPSAV-------RLTVSKDYtKSILPLKNVLDSGIE-----VIKDTAA---- 81
Cdd:TIGR01423  44 YAALGGTcvnvgcVPKKLmVTGAQYMDTLRESAgfgwefdRSSVKANW-KALIAAKNKAVLDINksyegMFADTEGltff 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359   82 ----SFDDKEVVLGSDRA---------IKFDILVLATGSkWADPI---GSTYTFGDNYKEYFEREASRIsdadhiLFLGG 145
Cdd:TIGR01423 123 lgwgALEDKNVVLVRESAdpksavkerLQAEHILLATGS-WPQMLgipGIEHCISSNEAFYLDEPPRRV------LTVGG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  146 GFVNCELAGelLFKYLEEiRSGKkrISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGA--SLDTSPKRIF 223
Cdd:TIGR01423 196 GFISVEFAG--IFNAYKP-RGGK--VTLCYRNNMILRG---FDSTLRKELTKQLRANGINIMTNENPAkvTLNADGSKHV 267

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767224359  224 LGEgSSKYIDADLIYRGVGISP---NVPVNSISDLCDKKGFIQVEKNFRVKaveAGNVFAIGDVTN 286
Cdd:TIGR01423 268 TFE-SGKTLDVDVVMMAIGRVPrtqTLQLDKVGVELTKKGAIQVDEFSRTN---VPNIYAIGDVTD 329
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 98-290 5.16e-07

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 51.32  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  98 FDILVLATG-SKWADPIGSTYTF-------GDNYKEYFEReasriSDADHILFLGGGFVNCELAGELLFKYLEeirsgkk 169
Cdd:PRK13512 106 YDKLILSPGaSANSLGFESDITFtlrnledTDAIDQFIKA-----NQVDKALVVGAGYISLEVLENLYERGLH------- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 170 rISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIflgeGSSKYIDADLIYRGVGISPNVP- 248
Cdd:PRK13512 174 -PTLIHRSDKINK---LMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTF----KSGKVEHYDMIIEGVGTHPNSKf 245

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767224359 249 VNSISDLCDKKGFIQVEKNFRVKaveAGNVFAIGDV-TNFRYH 290
Cdd:PRK13512 246 IESSNIKLDDKGFIPVNDKFETN---VPNIYAIGDIiTSHYRH 285
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 97-283 3.45e-06

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 48.88  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  97 KFDILVLATGSKWADP------IGSTYTFGDNYKEYFEREASRISDADHILFLGGGFVNCELAgellfkylEEIRSGKKR 170
Cdd:PRK09564 103 TYDKLMIATGARPIIPpikninLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGFIGLEAV--------EAAKHLGKN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 171 ISIIHNSDKLLPDSglYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYiDADLIYRGVGISPNVPVN 250
Cdd:PRK09564 175 VRIIQLEDRILPDS--FDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEY-EADVVIVATGVKPNTEFL 251

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767224359 251 SISDL-CDKKGFIQVEknfRVKAVEAGNVFAIGD 283
Cdd:PRK09564 252 EDTGLkTLKNGAIIVD---EYGETSIENIYAAGD 282
PRK06370 PRK06370
FAD-containing oxidoreductase;
138-289 4.28e-06

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 48.27  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 138 DHILFLGGGFVNCELAGelLFKyleeiRSGkKRISIIHNSDKLLP--DSglynDTlRKNVTDYLSKNGITLYLNT--VGA 213
Cdd:PRK06370 172 EHLVIIGGGYIGLEFAQ--MFR-----RFG-SEVTVIERGPRLLPreDE----DV-AAAVREILEREGIDVRLNAecIRV 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 214 SLDTSPKRI-FLGEGSSKYIDADLIYRGVGISPNVpvnsiSDL--------CDKKGFIQVEKNFRVKaveAGNVFAIGDV 284
Cdd:PRK06370 239 ERDGDGIAVgLDCNGGAPEITGSHILVAVGRVPNT-----DDLgleaagveTDARGYIKVDDQLRTT---NPGIYAAGDC 310


                 ....*
gi 767224359 285 tNFRY 289
Cdd:PRK06370 311 -NGRG 314
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 72-285 1.56e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 46.68  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  72 GIEVIKDTAaSFDDKEVV----LGSDRAIKFDILVLATGSKWADPIGstytfgdnykeyFEREASRISDADHILFL---- 143
Cdd:PRK06416 106 KVDIIRGEA-KLVDPNTVrvmtEDGEQTYTAKNIILATGSRPRELPG------------IEIDGRVIWTSDEALNLdevp 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 144 ------GGGFVNCELAGelLFKYLeeirsGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDT 217
Cdd:PRK06416 173 kslvviGGGYIGVEFAS--AYASL-----GAE-VTIVEALPRILP---GEDKEISKLAERALKKRGIKIKTGAKAKKVEQ 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 218 SPKRIFL---GEGSSKYIDADLIYRGVGISPN----------VPVNsisdlcdkKGFIQVEKNFRvKAVEagNVFAIGDV 284
Cdd:PRK06416 242 TDDGVTVtleDGGKEETLEADYVLVAVGRRPNtenlgleelgVKTD--------RGFIEVDEQLR-TNVP--NIYAIGDI 310


                 .
gi 767224359 285 T 285
Cdd:PRK06416 311 V 311
PRK07846 PRK07846
mycothione reductase; Reviewed
 73-286 1.67e-05

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 46.49  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  73 IEVIKDTAASFDDKEVVLGSDRAIKFDILVLATGSK-WADPIgstytFGDNYKEYFEREA-SRISD-ADHILFLGGGFVN 149
Cdd:PRK07846 104 IDVYRGHARFIGPKTLRTGDGEEITADQVVIAAGSRpVIPPV-----IADSGVRYHTSDTiMRLPElPESLVIVGGGFIA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 150 CELAGelLFKYLeeirsgKKRISIIHNSDKLLpdsGLYNDTLRKNVTDYLSKN-GITLYLNTVGASLDTSPKRIFLGEGS 228
Cdd:PRK07846 179 AEFAH--VFSAL------GVRVTVVNRSGRLL---RHLDDDISERFTELASKRwDVRLGRNVVGVSQDGSGVTLRLDDGS 247

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767224359 229 SkyIDADLIYRGVGISPNvpvnsiSDLCD-KKGFIQVEKNFRVKAVE-----AGNVFAIGDVTN 286
Cdd:PRK07846 248 T--VEADVLLVATGRVPN------GDLLDaAAAGVDVDEDGRVVVDEyqrtsAEGVFALGDVSS 303
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
72-287 2.19e-05

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 46.30  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359  72 GIEVIKDTAaSFDDKEVVL-----GSDRAIKFDILVLATGSKWADPigSTYTFgdnykeyferEASRISDADHILFL--- 143
Cdd:PRK05249 108 RVDLIQGRA-RFVDPHTVEvecpdGEVETLTADKIVIATGSRPYRP--PDVDF----------DHPRIYDSDSILSLdhl 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 144 -------GGGFVNCELAGelLFKYLeeirsGKKrISIIHNSDKLLpdsglynDTLRKNVTDYLS----KNGITLYLNTVG 212
Cdd:PRK05249 175 prsliiyGAGVIGCEYAS--IFAAL-----GVK-VTLINTRDRLL-------SFLDDEISDALSyhlrDSGVTIRHNEEV 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767224359 213 ASLDTSPKRIFLGEGSSKYIDADLIYRGVGISPNVpvnsiSDLC--------DKKGFIQVEKNFRVkAVEagNVFAIGDV 284
Cdd:PRK05249 240 EKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNT-----DGLNlenagleaDSRGQLKVNENYQT-AVP--HIYAVGDV 311


                 ...
gi 767224359 285 TNF 287
Cdd:PRK05249 312 IGF 314
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 51-106 6.28e-03

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 38.31  E-value: 6.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767224359  51 RLTVSKDYtksilpLKNVLDSGIEVIKDTAASFDDKEVVLGSDRAIKFDILVLATG 106
Cdd:COG2072  267 RPLLSTDY------YEALRRGNVELVTGGIERITEDGVVFADGTEHEVDVIVWATG 316
 
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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