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Conserved domains on  [gi|550995569|ref|WP_022740334|]
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MULTISPECIES: succinate dehydrogenase/fumarate reductase iron-sulfur subunit [Adlercreutzia]

Protein Classification

succinate dehydrogenase/fumarate reductase iron-sulfur subunit( domain architecture ID 11422279)

succinate dehydrogenase/fumarate reductase iron-sulfur subunit similar to the iron-sulfur subunit of Wolinella succinogenes 8-methylmenaquinol:fumarate reductase, which catalyzes the reduction of fumarate using 8-methylmenaquinol-6 as the electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-224 6.88e-69

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


:

Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 210.76  E-value: 6.88e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDNAPYETTYEVPHDdEYMTLLQALVYIHEN-EEPLAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD- 78
Cdd:COG0479    3 VTLKIWRQDPETDSKPRFQTYEVPVS-PGMTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  79 -GSHTVEPLAGLPVVKDLVVDKSQVQEKIAETYKRVRVAPLTEEDLQTYNMEDADELFGINYCARCQVCTAGCPARAINP 157
Cdd:COG0479   82 kDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWANP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569 158 DYIGPSHMLAVAFRHFDPYDQA--DRIVE-AVQGGLWDCTMCGTCTAHCNQlEIDHLAIWQKLRDAATER 224
Cdd:COG0479  162 DFLGPAALAQAYRFALDPRDEEteERLEAlEDEEGVWRCTTCGNCTEVCPK-GIPPTKAIAKLKREALKR 230
 
Name Accession Description Interval E-value
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-224 6.88e-69

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 210.76  E-value: 6.88e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDNAPYETTYEVPHDdEYMTLLQALVYIHEN-EEPLAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD- 78
Cdd:COG0479    3 VTLKIWRQDPETDSKPRFQTYEVPVS-PGMTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  79 -GSHTVEPLAGLPVVKDLVVDKSQVQEKIAETYKRVRVAPLTEEDLQTYNMEDADELFGINYCARCQVCTAGCPARAINP 157
Cdd:COG0479   82 kDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWANP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569 158 DYIGPSHMLAVAFRHFDPYDQA--DRIVE-AVQGGLWDCTMCGTCTAHCNQlEIDHLAIWQKLRDAATER 224
Cdd:COG0479  162 DFLGPAALAQAYRFALDPRDEEteERLEAlEDEEGVWRCTTCGNCTEVCPK-GIPPTKAIAKLKREALKR 230
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 1-226 1.89e-53

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 178.66  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDnAPYETTYEVPHDDEyMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPDG 79
Cdd:PRK06259   4 ITITVKRFDPEKD-EPHFESYEVPVKEG-MTVLDALEYINKTYDAnIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  80 ShTVEPLAgLPVVKDLVVDKSQVQEKIA--ETY-KRVRVAPLTEEDLqtynmEDADELFGinyCARCQVCTAGCPARAIN 156
Cdd:PRK06259  82 M-IIEPLD-FPVIKDLIVDREPYYKKLKslRNYlQRKNEKITYPEDI-----EDIKKLRG---CIECLSCVSTCPARKVS 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550995569 157 pDYIGPSHMLAVAFRHFDPYDQADRIVEAVQGGLWDCTMCGTCTAHC-NQLEIDHLAIwQKLRDAATERGL 226
Cdd:PRK06259 152 -DYPGPTFMRQLARFAFDPRDEGDREKEAFDEGLYNCTTCGKCVEVCpKEIDIPGKAI-EKLRALAFKKGL 220
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 5-218 1.29e-51

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 166.45  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569    5 VKRYDPSKDNAPYETTYEVPHDDEyMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD-GSH- 81
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPsLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDlGQPv 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   82 -TVEPLAGLPVVKDLVVDKSQVQEKiaetYKRVR-------VAPLTEEDLQTynMEDADELFGINYCARCQVCTAGCPAR 153
Cdd:TIGR00384  80 mKIEPLPNLPVIKDLVVDMGPFYAK----LEAIKpylirksQPEPEGEFLQT--PEQREKLDQLSGCILCGCCYSSCPAF 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550995569  154 AINPDYIGPSHMLAVAFRHFDPYDQA--DRIVEAV-QGGLWDCTMCGTCTAHCNQlEID-HLAIwQKLR 218
Cdd:TIGR00384 154 WWNPEFLGPAALTAAYRFLIDSRDHAtkDRLEGLNdKNGVWRCTTCMNCSEVCPK-GVNpARAI-EKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 2-104 1.55e-36

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 124.27  E-value: 1.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569    2 KITVKRYDPSKD-NAPYETTYEVPHDDEyMTLLQALVYIHEN-EEPLAFDFSCRGRMCGRCAMMLDGEPVLAC---VEPL 76
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPYEEG-MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACktlIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 550995569   77 PDGSHTVEPLAGLPVVKDLVVDKSQVQE 104
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-224 6.88e-69

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 210.76  E-value: 6.88e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDNAPYETTYEVPHDdEYMTLLQALVYIHEN-EEPLAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD- 78
Cdd:COG0479    3 VTLKIWRQDPETDSKPRFQTYEVPVS-PGMTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  79 -GSHTVEPLAGLPVVKDLVVDKSQVQEKIAETYKRVRVAPLTEEDLQTYNMEDADELFGINYCARCQVCTAGCPARAINP 157
Cdd:COG0479   82 kDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWANP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569 158 DYIGPSHMLAVAFRHFDPYDQA--DRIVE-AVQGGLWDCTMCGTCTAHCNQlEIDHLAIWQKLRDAATER 224
Cdd:COG0479  162 DFLGPAALAQAYRFALDPRDEEteERLEAlEDEEGVWRCTTCGNCTEVCPK-GIPPTKAIAKLKREALKR 230
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 1-226 1.89e-53

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 178.66  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDnAPYETTYEVPHDDEyMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPDG 79
Cdd:PRK06259   4 ITITVKRFDPEKD-EPHFESYEVPVKEG-MTVLDALEYINKTYDAnIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  80 ShTVEPLAgLPVVKDLVVDKSQVQEKIA--ETY-KRVRVAPLTEEDLqtynmEDADELFGinyCARCQVCTAGCPARAIN 156
Cdd:PRK06259  82 M-IIEPLD-FPVIKDLIVDREPYYKKLKslRNYlQRKNEKITYPEDI-----EDIKKLRG---CIECLSCVSTCPARKVS 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550995569 157 pDYIGPSHMLAVAFRHFDPYDQADRIVEAVQGGLWDCTMCGTCTAHC-NQLEIDHLAIwQKLRDAATERGL 226
Cdd:PRK06259 152 -DYPGPTFMRQLARFAFDPRDEGDREKEAFDEGLYNCTTCGKCVEVCpKEIDIPGKAI-EKLRALAFKKGL 220
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 5-218 1.29e-51

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 166.45  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569    5 VKRYDPSKDNAPYETTYEVPHDDEyMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD-GSH- 81
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPsLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDlGQPv 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   82 -TVEPLAGLPVVKDLVVDKSQVQEKiaetYKRVR-------VAPLTEEDLQTynMEDADELFGINYCARCQVCTAGCPAR 153
Cdd:TIGR00384  80 mKIEPLPNLPVIKDLVVDMGPFYAK----LEAIKpylirksQPEPEGEFLQT--PEQREKLDQLSGCILCGCCYSSCPAF 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550995569  154 AINPDYIGPSHMLAVAFRHFDPYDQA--DRIVEAV-QGGLWDCTMCGTCTAHCNQlEID-HLAIwQKLR 218
Cdd:TIGR00384 154 WWNPEFLGPAALTAAYRFLIDSRDHAtkDRLEGLNdKNGVWRCTTCMNCSEVCPK-GVNpARAI-EKLK 220
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 2-203 7.38e-46

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 152.26  E-value: 7.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   2 KITVKRYDPSKDNAPYETTYEVPHDDEYMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEP---LP 77
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPtLTFRRSCREGVCGSDAMNINGKNGLACITPisdLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  78 DGSHTVEPLAGLPVVKDLVVDKSQVQEKiaetYKRVR------VAPLTEEDLQTYnmEDADELFGINYCARCQVCTAGCP 151
Cdd:PRK05950  81 KGKIVIRPLPGLPVIKDLVVDMTQFYAQ----YRSIKpylindTPPPARERLQSP--EDREKLDGLYECILCACCSTSCP 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 550995569 152 ARAINPD-YIGPSHMLAvAFRH-FDPYDQADR----IVEAVQgGLWDCTMCGTCTAHC 203
Cdd:PRK05950 155 SFWWNPDkFLGPAALLQ-AYRFiADSRDEATGerldILDDPF-GVFRCHTIMNCVEVC 210
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-203 5.54e-43

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 145.23  E-value: 5.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDNAPYETTYEVPHDDEyMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD- 78
Cdd:PRK12385   7 LKIEVLRYNPEVDTEPHSQTYEVPYDET-TSLLDALGYIKDNLAPdLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDy 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  79 -GSHTVEPLAGLPVVKDLVVDKSQVQEKIAETYKRVRVAPLTEED---LQT-YNMEDADELFGinyCARCQVCTAGCPAR 153
Cdd:PRK12385  86 tGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDgpnKQTpAQMAKYHQFSG---CINCGLCYAACPQF 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 550995569 154 AINPDYIGPShMLAVAFRH-FDPYD--QADRI-VEAVQGGLWDCTMCGTCTAHC 203
Cdd:PRK12385 163 GLNPEFIGPA-AITLAHRYnLDSRDhgKKERMkQLNGQNGVWSCTFVGYCSEVC 215
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 2-104 1.55e-36

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 124.27  E-value: 1.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569    2 KITVKRYDPSKD-NAPYETTYEVPHDDEyMTLLQALVYIHEN-EEPLAFDFSCRGRMCGRCAMMLDGEPVLAC---VEPL 76
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPYEEG-MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACktlIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 550995569   77 PDGSHTVEPLAGLPVVKDLVVDKSQVQE 104
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
2-218 6.38e-36

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 127.94  E-value: 6.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   2 KITVKRYDPSKdnAPYETTYEVpHDDEYMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPLPD-- 78
Cdd:PRK12576  10 IFKVKRYDPEK--GSWWQEYKV-KVDRFTQVTEALRRIKEEQDPtLSYRASCHMAVCGSCGMKINGEPRLACKTLVLDva 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  79 ----GSHTVEPLAGLPVVKDLVVDKSQVQEKIAETYKRVRVAPLTEEDLQTYNM--EDADELFGINYCARCQVCTAGCPA 152
Cdd:PRK12576  87 kkynSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLkpEDQKELWKFAQCIWCGLCVSACPV 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550995569 153 RAINPDYIGPsHMLAVAFRHF-DPYDQ-ADRIVEAVQGGLWDCTMCGTCTAHCNQlEIDHLAIWQKLR 218
Cdd:PRK12576 167 VAIDPEFLGP-AAHAKGYRFLaDPRDTiTEERMKILIDSSWRCTYCYSCSNVCPR-DIEPVTAIKKTR 232
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 1-178 1.03e-29

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 110.81  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDP-SKDNAPYETTYEVPHDDEyMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLAC---VEP 75
Cdd:PRK13552   5 LTFNIFRYNPqDPGSKPHMVTYQLEETPG-MTLFIALNRIREEQDPsLQFDFVCRAGICGSCAMVINGRPTLACrtlTSD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  76 LPDGSHTVEPLAGLPVVKDLVVDKSqvqEKIAETYKRVRVAPLTEEDLQTYNMED------ADELFGINYCARCQVCTAG 149
Cdd:PRK13552  84 YPDGVITLMPLPVFKLIGDLSVNTG---KWFREMSERVESWIHTDKEFDIHRLEErmepeeADEIYELDRCIECGCCVAA 160

                        170       180
                 ....*....|....*....|....*....
gi 550995569 150 CPARAINPDYIGPSHMLAVAFRHFDPYDQ 178
Cdd:PRK13552 161 CGTKQMREDFVGAVGLNRIARFELDPRDE 189
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 5-203 1.00e-26

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 103.72  E-value: 1.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   5 VKRYDPSKDNAPYETTYEVPHDDEYMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLAC---VEPLPDGS 80
Cdd:PLN00129  48 IYRWNPDNPGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPsLTFRRSCREGICGSCAMNIDGKNTLACltkIDRDESGP 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  81 HTVEPLAGLPVVKDLVVDKSQV--QEKIAETYKRVRVAPL--TEEDLQTynMEDADELFGINYCARCQVCTAGCPARAIN 156
Cdd:PLN00129 128 TTITPLPHMFVIKDLVVDMTNFyqQYKSIEPWLKTKKPPEdgQKEHLQS--KEDRAKLDGMYECILCACCSTSCPSYWWN 205

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550995569 157 PD-YIGPSHMLAvAFRHF-DPYDQ-ADRIVEAVQGG--LWDCTMCGTCTAHC 203
Cdd:PLN00129 206 PEkFLGPAALLH-AYRWIsDSRDEyTKERLEALDDEfkLYRCHTIRNCSNAC 256
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
5-179 6.57e-26

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 100.80  E-value: 6.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   5 VKRYDPSKDNAPYETTYEV-PHDDEYMtLLQALVYIHENEEPLAFDFSCRGRMCGRCAMMLDGEPVLACV---EPLPdGS 80
Cdd:PRK12575   9 IYRYDPDDDAAPRMQRYEIaPRAEDRM-LLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLtnmQALP-RE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  81 HTVEPLAGLPVVKDLVVDKSQV--QEKIAETYKRVRVAPLTEEDLQTynMEDADELFGINYCARCQVCTAGCPARAINPD 158
Cdd:PRK12575  87 IVLRPLPGLPVVRDLIVDMTDFfnQYHSIRPYLINDTVPPERERLQT--PQEREQLDGLYECILCACCSTACPSYWWNPD 164

                        170       180
                 ....*....|....*....|...
gi 550995569 159 -YIGPSHMLAvAFRHF-DPYDQA 179
Cdd:PRK12575 165 kFVGPAGLLQ-AYRFIaDSRDDA 186
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-203 3.03e-24

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 98.23  E-value: 3.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVKRYDPSKDNAPYETTYEVpHDDEYMTLLQALVYIH-ENEEPLAFDFSCRGRMCGRCAMMLDGEPVLACVE----- 74
Cdd:PRK12577   1 MEVLFKILRQKQNSAPYVQTYTL-EVEPGNTILDCLNRIKwEQDGSLAFRKNCRNTICGSCAMRINGRSALACKEnvgse 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  75 ------PLPDGSH--TVEPLAGLPVVKDLVVDKSQVQEKIAETYKRVRVA---PLTEEDLQTynMEDADELFGINYCARC 143
Cdd:PRK12577  80 larlsdSNSGAIPeiTIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAarqVPEREFLQT--PEERSKLDQTGNCILC 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550995569 144 QVCTAGCPARAINPDYIGPsHMLAVAFRHF-DPYDQ--ADRIVEAVQG--GLWDCTMCGTCTAHC 203
Cdd:PRK12577 158 GACYSECNAREVNPEFVGP-HALAKAQRMVaDSRDTatEQRLELYNQGtaGVWGCTRCYYCNSVC 221
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 1-151 7.87e-17

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 76.79  E-value: 7.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   1 MKITVK--RYDPSKDNAPYETtYEVPHDDEYMTLLQAL-----VYIHENEEPLAFDFSCRGRMCGRCAMMLDGEP----- 68
Cdd:PRK07570   1 MKLTLKiwRQKGPDDKGKFET-YEVDDISPDMSFLEMLdvlneQLIEKGEEPVAFDHDCREGICGMCGLVINGRPhgpdr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  69 -VLAC---VEPLPDGSH-TVEPL--AGLPVVKDLVVDKSQVQEKIAET-YKRVRVAPLTEEDLQTYNMEDADELFGINYC 140
Cdd:PRK07570  80 gTTTCqlhMRSFKDGDTiTIEPWraAAFPVIKDLVVDRSALDRIIQAGgYVSVNTGGAPDANAIPVPKEDADRAFDAAAC 159

                        170
                 ....*....|.
gi 550995569 141 ARCQVCTAGCP 151
Cdd:PRK07570 160 IGCGACVAACP 170
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 5-203 4.34e-15

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 71.94  E-value: 4.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569   5 VKRYDpSKDNAPYETTYEVPHDdEYMTLLQALVYIHENE--------EPLAFDFSCRGRMCGRCAMMLDGEPVLAC---V 73
Cdd:PRK08640  10 IKRQD-GPDSKPYWEEFEIPYR-PNMNVISALMEIRRNPvnakgektTPVVWDMNCLEEVCGACSMVINGKPRQACtalI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  74 EPLPDgSHTVEPLAGLPVVKDLVVDKSqvqeKIAETYKRVRV-APLTeedlQTYNM--------EDADELFGINYCARCQ 144
Cdd:PRK08640  88 DQLEQ-PIRLEPMSTFPVVRDLQVDRS----RMFDNLKRVKAwIPID----GTYDLgpgprmpeEKRQWAYELSKCMTCG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550995569 145 VCTAGCPARAINPDYIGPSHMLAVafRHFDPYD----QADRIVEAV--QGGLWDCTMCGTCTAHC 203
Cdd:PRK08640 159 CCLEACPNVNEKSDFIGPAAISQV--RLFNAHPtgemHKEERLRALmgDGGIADCGNAQNCVRVC 221
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 21-203 1.87e-12

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 64.72  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  21 YEVPHDdEYMTLLQALVYIHENEEP-LAFDFSCRGRMCGRCAMMLDGEPVLACVEPL----PDGSHTVEPLAGLPVVKDL 95
Cdd:PRK12386  22 YTVEVN-EGEVVLDVIHRLQATQAPdLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMstfdEDETVTVTPMRTFPVIRDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569  96 VVDKSQVQEKIAETYKrvrVAPLTEEDLQTYNM--EDADELFGINYCARCQVCTAGCPA----RAINPDYIGPSHMLAVA 169
Cdd:PRK12386 101 VTDVSFNYEKAREIPS---FTPPKDLQPGEYRMqqVDVERSQEFRKCIECFLCQNVCHVvrdhEENKPAFAGPRFLMRIA 177

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 550995569 170 FRHFDPYDQADRIVEA-VQGGLWDCTMCGTCTAHC 203
Cdd:PRK12386 178 ELEMHPLDTADRRAEAqEEHGLGYCNITKCCTEVC 212
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 114-227 4.22e-08

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 52.77  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569 114 RVAPLTEEDLQTYNMEDADELFgiNYCARCQVCTAGCPARAINPDYIGPSHMLAVAFRHFDPYDQADRIVEAVQGGLWDC 193
Cdd:COG0247   56 GDGDLHDKNLKTLPWKELLDAL--DACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLSEEVYEVLDLC 133

                         90       100       110
                 ....*....|....*....|....*....|....
gi 550995569 194 TMCGTCTAHCnQLEIDHLAIWQKLRDAATERGLV 227
Cdd:COG0247  134 LTCKACETAC-PSGVDIADLIAEARAQLVERGGR 166
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 139-203 1.44e-05

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 41.53  E-value: 1.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550995569  139 YCARCQVCTAGCPA-RAINPDYIGPSHMLAVAFRHFDPYDQADRIveavqgGLWDCTMCGTCTAHC 203
Cdd:pfam13183   1 RCIRCGACLAACPVyLVTGGRFPGDPRGGAAALLGRLEALEGLAE------GLWLCTLCGACTEVC 60
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
100-223 1.63e-05

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 44.81  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550995569 100 SQVQE--KIAETYKrvrvaPLTEEDLQTYNmEDADELFGI--NYCARCQVCTAgCPARaIN-PDYIGpSHMLAVAFRHFD 174
Cdd:COG1453  245 EQLDEnlKTADNLE-----PLTEEELAILE-RLAEELGELlkDFCTGCGYCMP-CPQG-INiPEVFR-LYNLARAYGMRE 315

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 550995569 175 ----PYDQADRIVEAvqgglWDCTMCGTCTAHCNQleidHLAIWQKLRDAATE 223
Cdd:COG1453  316 yakeRYNALGPGAKA-----SACIECGACEERCPQ----GLDIPELLKEAHEL 359
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 138-203 2.01e-04

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 38.39  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550995569  138 NYCARCQVCTAGCPARAINPDYIgpshmlavafrhfdpydQADRIVEAVQGGLWDCTMCGTCTAHC 203
Cdd:pfam13237   7 DKCIGCGRCTAACPAGLTRVGAI-----------------VERLEGEAVRIGVWKCIGCGACVEAC 55
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
136-203 4.21e-04

Heterodisulfide reductase, subunit C [Energy production and conversion];


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 37.96  E-value: 4.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550995569 136 GINYCARCQVCTAGCPARA---INPDYIgpshmlavaFRHFdpydQADRIVEAVQG-GLWDCTMCGTCTAHC 203
Cdd:COG1150    1 NLKKCYQCGTCTASCPVARamdYNPRKI---------IRLA----QLGLKEEVLKSdSIWLCVSCYTCTERC 59
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
140-203 7.49e-04

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 39.85  E-value: 7.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550995569 140 CARCQVCTAGCPARAINPDYIGPSHM--LAVAFRHFDPydqadrivEAVQGGLWDCTMCGTCTAHC 203
Cdd:PRK11168   9 CIKCTVCTTACPVARVNPLYPGPKQAgpDGERLRLKDG--------ALYDESLKYCSNCKRCEVAC 66
Fer4_9 pfam13187
4Fe-4S dicluster domain;
139-205 1.17e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.99  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550995569  139 YCARCQVCTAGCPARAINPDYIGPSHmlavafrhfdpydqadriveAVQGGLWDCTMCGTCTAHCNQ 205
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVGQTI--------------------RGDIAGLACIGCGACVDACPR 47
 
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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