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Conserved domains on  [gi|2361072643|emb|CAI4760155|]
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ATM_1a_G0048230.mRNA.1.CDS.1 [Saccharomyces cerevisiae]

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 1.83e-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: 105.98  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643   5 TKNIVVvgagvfgvsvANHLYRELGGTYAIKLVTASNYVYFLPS----AV-RLTVSKDytksILPLKNVL-DSGIEVIKD 78
Cdd:COG1252     1 MKRIVIvgggfagleaARRLRKKLGGDAEVTLIDPNPYHLFQPLlpevAAgTLSPDDI----AIPLRELLrRAGVRFIQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  79 TAASFD--DKEVVLGSDRAIKFDILVLATGSKWAD--------------PIGSTYTFGDNYREYFEReASRISDAdHILF 142
Cdd:COG1252    77 EVTGIDpeARTVTLADGRTLSYDYLVIATGSVTNFfgipglaehalplkTLEDALALRERLLAAFER-AERRRLL-TIVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 143 LGGGFVNCELAGEL--LFKYL---EEIRSGKKRISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGASLDt 217
Cdd:COG1252   155 VGGGPTGVELAGELaeLLRKLlryPGIDPDKVRITLVEAGPRILPG---LGEKLSEAAEKELEKRGVEVHTGTRVTEVD- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 218 sPKRIFLGEGSSkyIDADLIYRGVGISPNvPVNSISDL-CDKKGFIQVEKNFRVKAVEagNVFAIGDVTNFRYHGlvkrD 296
Cdd:COG1252   231 -ADGVTLEDGEE--IPADTVIWAAGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPD----G 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 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 1.83e-25

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 105.98  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643   5 TKNIVVvgagvfgvsvANHLYRELGGTYAIKLVTASNYVYFLPS----AV-RLTVSKDytksILPLKNVL-DSGIEVIKD 78
Cdd:COG1252     1 MKRIVIvgggfagleaARRLRKKLGGDAEVTLIDPNPYHLFQPLlpevAAgTLSPDDI----AIPLRELLrRAGVRFIQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  79 TAASFD--DKEVVLGSDRAIKFDILVLATGSKWAD--------------PIGSTYTFGDNYREYFEReASRISDAdHILF 142
Cdd:COG1252    77 EVTGIDpeARTVTLADGRTLSYDYLVIATGSVTNFfgipglaehalplkTLEDALALRERLLAAFER-AERRRLL-TIVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 143 LGGGFVNCELAGEL--LFKYL---EEIRSGKKRISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGASLDt 217
Cdd:COG1252   155 VGGGPTGVELAGELaeLLRKLlryPGIDPDKVRITLVEAGPRILPG---LGEKLSEAAEKELEKRGVEVHTGTRVTEVD- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 218 sPKRIFLGEGSSkyIDADLIYRGVGISPNvPVNSISDL-CDKKGFIQVEKNFRVKAVEagNVFAIGDVTNFRYHGlvkrD 296
Cdd:COG1252   231 -ADGVTLEDGEE--IPADTVIWAAGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPD----G 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 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 1.09e-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: 93.92  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  71 SGIEVIKDtAASFDDKEVVLGSDRAIKFDILVLATGSKWADP--IGSTYTFGDNYREYfeREASRISDAD---HILFLGG 145
Cdd:pfam07992  84 EVVSIDPG-AKKVVLEELVDGDGETITYDRLVIATGARPRLPpiPGVELNVGFLVRTL--DSAEALRLKLlpkRVVVVGG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 146 GFVNCELAGELlfkyleeiRSGKKRISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNT--VGASLDTSPKRIF 223
Cdd:pfam07992 161 GYIGVELAAAL--------AKLGKEVTLIEALDRLLR---AFDEEISAALEKALEKNGVEVRLGTsvKEIIGDGDGVEVI 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2361072643 224 LGEGssKYIDADLIYRGVGISPNVPVNSISDL-CDKKGFIQVEKNFRVKaveAGNVFAIGDVT 285
Cdd:pfam07992 230 LKDG--TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTS---VPGIYAAGDCR 287
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
85-283 6.79e-12

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 66.09  E-value: 6.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  85 DKEVVLGSDRAIKFDILVLATGSK-WADPI-GSTYTFGDNYREYFEREASRISDADHILFLGGGFVNCELAGELlfkyle 162
Cdd:PRK04965   87 EAQVVKSQGNQWQYDKLVLATGASaFVPPIpGRELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDL------ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 163 eIRSGkKRISIIHNSDKLLPdsGLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYIDADLIYRGVG 242
Cdd:PRK04965  161 -CRAG-KAVTLVDNAASLLA--SLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAG 236

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2361072643 243 ISPNVPVNSISDLCDKKGfIQVEKNFRVKAVeagNVFAIGD 283
Cdd:PRK04965  237 LRPNTALARRAGLAVNRG-IVVDSYLQTSAP---DIYALGD 273
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 25-286 2.63e-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: 55.36  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  25 YRELGGT------YAIKL-VTASNYVYFLPSAV-------RLTVSKDYtKSILPLKNVLDSGIE-----VIKDTAA---- 81
Cdd:TIGR01423  44 YAALGGTcvnvgcVPKKLmVTGAQYMDTLRESAgfgwefdRSSVKANW-KALIAAKNKAVLDINksyegMFADTEGltff 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  82 ----SFDDKEVVLGSDRA---------IKFDILVLATGSkWADPI---GSTYTFGDNYREYFEREASRIsdadhiLFLGG 145
Cdd:TIGR01423 123 lgwgALEDKNVVLVRESAdpksavkerLQAEHILLATGS-WPQMLgipGIEHCISSNEAFYLDEPPRRV------LTVGG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 146 GFVNCELAGelLFKYLEEiRSGKkrISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGA--SLDTSPKRIF 223
Cdd:TIGR01423 196 GFISVEFAG--IFNAYKP-RGGK--VTLCYRNNMILRG---FDSTLRKELTKQLRANGINIMTNENPAkvTLNADGSKHV 267

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2361072643 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 1.83e-25

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 105.98  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643   5 TKNIVVvgagvfgvsvANHLYRELGGTYAIKLVTASNYVYFLPS----AV-RLTVSKDytksILPLKNVL-DSGIEVIKD 78
Cdd:COG1252     1 MKRIVIvgggfagleaARRLRKKLGGDAEVTLIDPNPYHLFQPLlpevAAgTLSPDDI----AIPLRELLrRAGVRFIQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  79 TAASFD--DKEVVLGSDRAIKFDILVLATGSKWAD--------------PIGSTYTFGDNYREYFEReASRISDAdHILF 142
Cdd:COG1252    77 EVTGIDpeARTVTLADGRTLSYDYLVIATGSVTNFfgipglaehalplkTLEDALALRERLLAAFER-AERRRLL-TIVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 143 LGGGFVNCELAGEL--LFKYL---EEIRSGKKRISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGASLDt 217
Cdd:COG1252   155 VGGGPTGVELAGELaeLLRKLlryPGIDPDKVRITLVEAGPRILPG---LGEKLSEAAEKELEKRGVEVHTGTRVTEVD- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 218 sPKRIFLGEGSSkyIDADLIYRGVGISPNvPVNSISDL-CDKKGFIQVEKNFRVKAVEagNVFAIGDVTNFRYHGlvkrD 296
Cdd:COG1252   231 -ADGVTLEDGEE--IPADTVIWAAGVKAP-PLLADLGLpTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPD----G 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 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 2.09e-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: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  27 ELGGTYAIKLVTASNYVYF----LPSAVRLTVSKDYTKSILPLKNVLDSGIEVI-KDTAASFD--DKEVVLGSDRAIKFD 99
Cdd:COG0446     1 RLGPDAEITVIEKGPHHSYqpcgLPYYVGGGIKDPEDLLVRTPESFERKGIDVRtGTEVTAIDpeAKTVTLRDGETLSYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 100 ILVLATGSK--WaDPI-GST----YTFGdNYREYFE-REASRISDADHILFLGGGFVNCELAgellfkylEEIRSGKKRI 171
Cdd:COG0446    81 KLVLATGARprP-PPIpGLDlpgvFTLR-TLDDADAlREALKEFKGKRAVVIGGGPIGLELA--------EALRKRGLKV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 172 SIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPK-RIFLGEGSSkyIDADLIYRGVGISPNVPVN 250
Cdd:COG0446   151 TLVERAPRLLG---VLDPEMAALLEEELREHGVELRLGETVVAIDGDDKvAVTLTDGEE--IPADLVVVAPGVRPNTELA 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2361072643 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 1.09e-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: 93.92  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  71 SGIEVIKDtAASFDDKEVVLGSDRAIKFDILVLATGSKWADP--IGSTYTFGDNYREYfeREASRISDAD---HILFLGG 145
Cdd:pfam07992  84 EVVSIDPG-AKKVVLEELVDGDGETITYDRLVIATGARPRLPpiPGVELNVGFLVRTL--DSAEALRLKLlpkRVVVVGG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 146 GFVNCELAGELlfkyleeiRSGKKRISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNT--VGASLDTSPKRIF 223
Cdd:pfam07992 161 GYIGVELAAAL--------AKLGKEVTLIEALDRLLR---AFDEEISAALEKALEKNGVEVRLGTsvKEIIGDGDGVEVI 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2361072643 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 2.18e-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: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  72 GIEVIKDTAaSF-DDKEVVLGSDRAIKFDILVLATGSKWADPigstytfgdnyrEYFEREASRISDAD----------HI 140
Cdd:COG1249   105 GVDVIRGRA-RFvDPHTVEVTGGETLTADHIVIATGSRPRVP------------PIPGLDEVRVLTSDealeleelpkSL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 141 LFLGGGFVNCELAGelLFKYLeeirsGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNT--VGASLDTS 218
Cdd:COG1249   172 VVIGGGYIGLEFAQ--IFARL-----GSE-VTLVERGDRLLP---GEDPEISEALEKALEKEGIDILTGAkvTSVEKTGD 240

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2361072643 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 3.12e-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: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  70 DSGIEVIKDTAAS---FDDKEVVLGSDRAIKFDILVLATGSK-WADPI-GST----YTFGDnyREYFEREASRISDADHI 140
Cdd:COG1251    68 ENGIDLRLGTRVTaidRAARTVTLADGETLPYDKLVLATGSRpRVPPIpGADlpgvFTLRT--LDDADALRAALAPGKRV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 141 LFLGGGFVNCELAGELlfkyleeiRSGKKRISIIHNSDKLLPD------SGLYNDTLRknvtdylsKNGITLYLNTVGAS 214
Cdd:COG1251   146 VVIGGGLIGLEAAAAL--------RKRGLEVTVVERAPRLLPRqldeeaGALLQRLLE--------ALGVEVRLGTGVTE 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2361072643 215 L--DTSPKRIFLGEGSSkyIDADLIYRGVGISPNVpvnsisDLCDKKGfIQVEKNFRVKA---VEAGNVFAIGDVTNFR 288
Cdd:COG1251   210 IegDDRVTGVRLADGEE--LPADLVVVAIGVRPNT------ELARAAG-LAVDRGIVVDDylrTSDPDIYAAGDCAEHP 279
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
85-283 6.79e-12

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 66.09  E-value: 6.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  85 DKEVVLGSDRAIKFDILVLATGSK-WADPI-GSTYTFGDNYREYFEREASRISDADHILFLGGGFVNCELAGELlfkyle 162
Cdd:PRK04965   87 EAQVVKSQGNQWQYDKLVLATGASaFVPPIpGRELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDL------ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 163 eIRSGkKRISIIHNSDKLLPdsGLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYIDADLIYRGVG 242
Cdd:PRK04965  161 -CRAG-KAVTLVDNAASLLA--SLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAG 236

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2361072643 243 ISPNVPVNSISDLCDKKGfIQVEKNFRVKAVeagNVFAIGD 283
Cdd:PRK04965  237 LRPNTALARRAGLAVNRG-IVVDSYLQTSAP---DIYALGD 273
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 53-288 5.51e-10

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 60.58  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  53 TVSKDYTKSILplKNVLD-SGIEVIKDTAASFDDKEVVLGSDRaIKFDILVLATGSKWAdPI-GSTYTFGDNYreYFERE 130
Cdd:PRK06292   88 RERDRFVGGVV--EGLEKkPKIDKIKGTARFVDPNTVEVNGER-IEAKNIVIATGSRVP-PIpGVWLILGDRL--LTSDD 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 131 ASRISDA-DHILFLGGGFVNCELAgellfKYLEeiRSGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNgITLYLN 209
Cdd:PRK06292  162 AFELDKLpKSLAVIGGGVIGLELG-----QALS--RLGVK-VTVFERGDRILP---LEDPEVSKQAQKILSKE-FKIKLG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 210 T----VGASlDTSPKRIFLGEGSSKYIDADLIYRGVGISPNVPVNSISDL---CDKKGFIQVEKNFRvKAVEagNVFAIG 282
Cdd:PRK06292  230 AkvtsVEKS-GDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTgieLDERGRPVVDEHTQ-TSVP--GIYAAG 305


                  ....*.
gi 2361072643 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 2.75e-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: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 139 HILFLGGGFVNCELAGELLfkyleeiRSGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTS 218
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALA-------RLGSK-VTVVERRDRLLP---GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGN 69


                  ..
gi 2361072643 219 PK 220
Cdd:pfam00070  70 GD 71
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 25-286 2.63e-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: 55.36  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  25 YRELGGT------YAIKL-VTASNYVYFLPSAV-------RLTVSKDYtKSILPLKNVLDSGIE-----VIKDTAA---- 81
Cdd:TIGR01423  44 YAALGGTcvnvgcVPKKLmVTGAQYMDTLRESAgfgwefdRSSVKANW-KALIAAKNKAVLDINksyegMFADTEGltff 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  82 ----SFDDKEVVLGSDRA---------IKFDILVLATGSkWADPI---GSTYTFGDNYREYFEREASRIsdadhiLFLGG 145
Cdd:TIGR01423 123 lgwgALEDKNVVLVRESAdpksavkerLQAEHILLATGS-WPQMLgipGIEHCISSNEAFYLDEPPRRV------LTVGG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 146 GFVNCELAGelLFKYLEEiRSGKkrISIIHNSDKLLPDsglYNDTLRKNVTDYLSKNGITLYLNTVGA--SLDTSPKRIF 223
Cdd:TIGR01423 196 GFISVEFAG--IFNAYKP-RGGK--VTLCYRNNMILRG---FDSTLRKELTKQLRANGINIMTNENPAkvTLNADGSKHV 267

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2361072643 224 LGEgSSKYIDADLIYRGVGISP---NVPVNSISDLCDKKGFIQVEKNFRVKaveAGNVFAIGDVTN 286
Cdd:TIGR01423 268 TFE-SGKTLDVDVVMMAIGRVPrtqTLQLDKVGVELTKKGAIQVDEFSRTN---VPNIYAIGDVTD 329
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 136-290 5.25e-07

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 51.32  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 136 DADHILFLGGGFVNCELAGELLFKYLEeirsgkkrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASL 215
Cdd:PRK13512  147 QVDKALVVGAGYISLEVLENLYERGLH--------PTLIHRSDKINK---LMDADMNQPILDELDKREIPYRLNEEIDAI 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2361072643 216 DTSPKRIflgeGSSKYIDADLIYRGVGISPNVP-VNSISDLCDKKGFIQVEKNFRVKaveAGNVFAIGDV-TNFRYH 290
Cdd:PRK13512  216 NGNEVTF----KSGKVEHYDMIIEGVGTHPNSKfIESSNIKLDDKGFIPVNDKFETN---VPNIYAIGDIiTSHYRH 285
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 97-283 4.34e-06

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 48.50  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  97 KFDILVLATGSKWADP------IGSTYTFGDNYREYFEREASRISDADHILFLGGGFVNCELAgellfkylEEIRSGKKR 170
Cdd:PRK09564  103 TYDKLMIATGARPIIPpikninLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGFIGLEAV--------EAAKHLGKN 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 171 ISIIHNSDKLLPDSglYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYiDADLIYRGVGISPNVPVN 250
Cdd:PRK09564  175 VRIIQLEDRILPDS--FDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEY-EADVVIVATGVKPNTEFL 251

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2361072643 251 SISDL-CDKKGFIQVEknfRVKAVEAGNVFAIGD 283
Cdd:PRK09564  252 EDTGLkTLKNGAIIVD---EYGETSIENIYAAGD 282
PRK06370 PRK06370
FAD-containing oxidoreductase;
138-289 4.52e-06

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 48.27  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 138 DHILFLGGGFVNCELAGelLFKyleeiRSGkKRISIIHNSDKLLP--DSglynDTlRKNVTDYLSKNGITLYLNT--VGA 213
Cdd:PRK06370  172 EHLVIIGGGYIGLEFAQ--MFR-----RFG-SEVTVIERGPRLLPreDE----DV-AAAVREILEREGIDVRLNAecIRV 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 214 SLDTSPKRI-FLGEGSSKYIDADLIYRGVGISPNVpvnsiSDL--------CDKKGFIQVEKNFRVKaveAGNVFAIGDV 284
Cdd:PRK06370  239 ERDGDGIAVgLDCNGGAPEITGSHILVAVGRVPNT-----DDLgleaagveTDARGYIKVDDQLRTT---NPGIYAAGDC 310


                  ....*
gi 2361072643 285 tNFRY 289
Cdd:PRK06370  311 -NGRG 314
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 72-285 1.41e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 46.68  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  72 GIEVIKDTAaSFDDKEVV----LGSDRAIKFDILVLATGSKWADPIGstytfgdnyreyFEREASRISDADHILFL---- 143
Cdd:PRK06416  106 KVDIIRGEA-KLVDPNTVrvmtEDGEQTYTAKNIILATGSRPRELPG------------IEIDGRVIWTSDEALNLdevp 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 144 ------GGGFVNCELAGelLFKYLeeirsGKKrISIIHNSDKLLPdsgLYNDTLRKNVTDYLSKNGITLYLNTVGASLDT 217
Cdd:PRK06416  173 kslvviGGGYIGVEFAS--AYASL-----GAE-VTIVEALPRILP---GEDKEISKLAERALKKRGIKIKTGAKAKKVEQ 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 218 SPKRIFL---GEGSSKYIDADLIYRGVGISPN----------VPVNsisdlcdkKGFIQVEKNFRvKAVEagNVFAIGDV 284
Cdd:PRK06416  242 TDDGVTVtleDGGKEETLEADYVLVAVGRRPNtenlgleelgVKTD--------RGFIEVDEQLR-TNVP--NIYAIGDI 310


                  .
gi 2361072643 285 T 285
Cdd:PRK06416  311 V 311
PRK07846 PRK07846
mycothione reductase; Reviewed
 73-286 1.81e-05

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 46.49  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  73 IEVIKDTAASFDDKEVVLGSDRAIKFDILVLATGSK-WADPI----GSTYTFGDnyreyferEASRISD-ADHILFLGGG 146
Cdd:PRK07846  104 IDVYRGHARFIGPKTLRTGDGEEITADQVVIAAGSRpVIPPViadsGVRYHTSD--------TIMRLPElPESLVIVGGG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 147 FVNCELAGelLFKYLeeirsgKKRISIIHNSDKLLpdsGLYNDTLRKNVTDYLSKN-GITLYLNTVGASLDTSPKRIFLG 225
Cdd:PRK07846  176 FIAAEFAH--VFSAL------GVRVTVVNRSGRLL---RHLDDDISERFTELASKRwDVRLGRNVVGVSQDGSGVTLRLD 244

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2361072643 226 EGSSkyIDADLIYRGVGISPNvpvnsiSDLCD-KKGFIQVEKNFRVKAVE-----AGNVFAIGDVTN 286
Cdd:PRK07846  245 DGST--VEADVLLVATGRVPN------GDLLDaAAAGVDVDEDGRVVVDEyqrtsAEGVFALGDVSS 303
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
72-287 2.25e-05

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 46.30  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643  72 GIEVIKDTAaSFDDKEVVL-----GSDRAIKFDILVLATGSKWADPigSTYTFgdnyreyferEASRISDADHILFL--- 143
Cdd:PRK05249  108 RVDLIQGRA-RFVDPHTVEvecpdGEVETLTADKIVIATGSRPYRP--PDVDF----------DHPRIYDSDSILSLdhl 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 144 -------GGGFVNCELAGelLFKYLeeirsGKKrISIIHNSDKLLpdsglynDTLRKNVTDYLS----KNGITLYLNTVG 212
Cdd:PRK05249  175 prsliiyGAGVIGCEYAS--IFAAL-----GVK-VTLINTRDRLL-------SFLDDEISDALSyhlrDSGVTIRHNEEV 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2361072643 213 ASLDTSPKRIFLGEGSSKYIDADLIYRGVGISPNVpvnsiSDLC--------DKKGFIQVEKNFRVkAVEagNVFAIGDV 284
Cdd:PRK05249  240 EKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNT-----DGLNlenagleaDSRGQLKVNENYQT-AVP--HIYAVGDV 311


                  ...
gi 2361072643 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 2361072643  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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