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Conserved domains on  [gi|503935176|ref|WP_014169170|]
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MULTISPECIES: succinate dehydrogenase iron-sulfur subunit SdhB [Enterobacteriaceae]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 11481909)

quinone-dependent succinate dehydrogenase iron-sulfur subunit is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q)

EC:  1.3.5.1
Gene Ontology:  GO:0008177|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-238 6.80e-172

succinate dehydrogenase iron-sulfur subunit; Reviewed


:

Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 471.97  E-value: 6.80e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   4 EFSVYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  83 QraGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950  80 K--KGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503935176 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-238 6.80e-172

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 471.97  E-value: 6.80e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   4 EFSVYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  83 QraGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950  80 K--KGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503935176 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-236 1.82e-130

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: 367.15  E-value: 1.82e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   1 MKLEFSVYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:COG0479    1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  80 SALqraGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479   79 RDL---KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503935176 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479  155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 7-230 2.46e-128

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: 361.75  E-value: 2.46e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176    7 VYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISALQRa 85
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQ- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   86 gQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384  78 -PVMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503935176  166 PDkFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-112 1.60e-46

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: 150.08  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176    5 FSVYRYNPDVD-DAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 503935176   83 qrAGQKIVIRPLPGLPVVRDLVVDMGQFYA 112
Cdd:pfam13085  80 --LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-238 6.80e-172

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 471.97  E-value: 6.80e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   4 EFSVYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  83 QraGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950  80 K--KGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503935176 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-236 1.82e-130

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: 367.15  E-value: 1.82e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   1 MKLEFSVYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:COG0479    1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  80 SALqraGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479   79 RDL---KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503935176 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479  155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 7-230 2.46e-128

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: 361.75  E-value: 2.46e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176    7 VYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISALQRa 85
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQ- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   86 gQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384  78 -PVMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503935176  166 PDkFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
7-237 1.16e-127

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 360.43  E-value: 1.16e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   7 VYRYNPDVDDAPRMQDYTLEAEEGrDMMLLDALIQLKEKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISALQRag 86
Cdd:PRK12575   9 IYRYDPDDDAAPRMQRYEIAPRAE-DRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALPR-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  87 qKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQnPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWNP 166
Cdd:PRK12575  86 -EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTV-PPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503935176 167 DKFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRS 237
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLARRA 234
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 4-234 7.94e-123

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 349.86  E-value: 7.94e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   4 EFSVYRYNPDVDDAPRMQDYTLEAEEGRDMMLlDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAl 82
Cdd:PLN00129  45 EFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVL-DVLIKIKnEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDR- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  83 qRAGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYL-LNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PLN00129 123 -DESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLkTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPS 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503935176 162 FWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLL 234
Cdd:PLN00129 202 YWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-238 3.31e-67

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 210.32  E-value: 3.31e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   1 MKLEFSVYRYNPDvdDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:PRK12577   1 MEVLFKILRQKQN--SAPYVQTYTLEVEPG--NTILDCLNRIKwEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  80 -SALQRAGQ-------KIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECIL 151
Cdd:PRK12577  77 gSELARLSDsnsgaipEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176 152 CACCSTSCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGLS-DAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:PRK12577 157 CGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235


                 ....*...
gi 503935176 231 SMLLQRSA 238
Cdd:PRK12577 236 QEILARKD 243
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-231 6.38e-61

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 192.66  E-value: 6.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   1 MKLEFSVYRYNPDvdDAPRMQDYTLEAEegRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACIT-P 78
Cdd:PRK12576   7 KEVIFKVKRYDPE--KGSWWQEYKVKVD--RFTQVTEALRRIKeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTlV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  79 ISALQRAGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLL-NNGQNPPAREHLQSPEQREKLDGLYECILCACCST 157
Cdd:PRK12576  83 LDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYrAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVS 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503935176 158 SCPSFWWNPdKFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDafSVFRCHSIMNCVSVCPKGLNPTRAIGHIKS 231
Cdd:PRK12576 163 ACPVVAIDP-EFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-226 1.12e-56

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 180.67  E-value: 1.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   1 MKLEfsVYRYNPDVDDAPRMQDYTLEAEEgrDMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITpi 79
Cdd:PRK12385   7 LKIE--VLRYNPEVDTEPHSQTYEVPYDE--TTSLLDALGYIKDNlAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  80 sALQRAGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSC 159
Cdd:PRK12385  81 -FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503935176 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAI 226
Cdd:PRK12385 160 PQFGLNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAI 225
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 2-220 9.06e-48

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 157.80  E-value: 9.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   2 KLEFSVYRYNP-DVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:PRK13552   4 TLTFNIFRYNPqDPGSKPHMVTYQLEETPG--MTLFIALNRIREEqDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  80 SALQRAgqKIVIRPLPGLPVVRDLVVDMGQFYAQ-YEKIKPYLLNNGQNPPAR-EHLQSPEQREKLDGLYECILCACCST 157
Cdd:PRK13552  82 SDYPDG--VITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRlEERMEPEEADEIYELDRCIECGCCVA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503935176 158 SCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRL-EGLSDAFSVFRCHSIMNCVSVCPKGL 220
Cdd:PRK13552 160 ACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDL 222
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-112 1.60e-46

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: 150.08  E-value: 1.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176    5 FSVYRYNPDVD-DAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 503935176   83 qrAGQKIVIRPLPGLPVVRDLVVDMGQFYA 112
Cdd:pfam13085  80 --LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 7-226 5.11e-37

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 135.52  E-value: 5.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   7 VYRYNPDVDdAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITpisalqRA 85
Cdd:PRK06259   8 VKRFDPEKD-EPHFESYEVPVKEG--MTVLDALEYINKTyDANIAFRSSCRAGQCGSCAVTINGEPVLACKT------EV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  86 GQKIVIRPLpGLPVVRDLVVDMGQFYAQYEKIKPYLLnngqnpPAREHLQSPEQREKLDGLYECILCACCSTSCPSFwwN 165
Cdd:PRK06259  79 EDGMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQ------RKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--K 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503935176 166 PDKFIGPAGLLAAYRFLIDSRDtETDSRLEGLSDafSVFRCHSIMNCVSVCPKGLN-PTRAI 226
Cdd:PRK06259 150 VSDYPGPTFMRQLARFAFDPRD-EGDREKEAFDE--GLYNCTTCGKCVEVCPKEIDiPGKAI 208
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 2-223 1.39e-21

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 89.76  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   2 KLEFSVYRYNpdvDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPIS 80
Cdd:PRK12386   4 TAKFRVWRGD---ASGGELQDYTVEVNEG--EVVLDVIHRLQaTQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  81 ALQRaGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYllnngqNPPAR----EHLQSPEQREKLDGLYECILCACCS 156
Cdd:PRK12386  79 TFDE-DETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSF------TPPKDlqpgEYRMQQVDVERSQEFRKCIECFLCQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503935176 157 TSC---PSFWWNPDKFIGPagllaayRFLI-----DSRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPT 223
Cdd:PRK12386 152 NVChvvRDHEENKPAFAGP-------RFLMriaelEMHPLDTADRRAEAQEEHGLGYCNITKCCTEVCPEHIKIT 219
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 55-229 3.17e-21

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 88.89  E-value: 3.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  55 CREGVCGSDGVNMNGKNGLACITPISALQragQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNG---QNPPAR 131
Cdd:PRK08640  63 CLEEVCGACSMVINGKPRQACTALIDQLE---QPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGtydLGPGPR 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176 132 ehlQSPEQREKLDGLYECILCACCSTSCPSFwwNPD-KFIGPAGLLAAYRF-LIDSRDTETDSRLEGLSDAFSVFRCHSI 209
Cdd:PRK08640 140 ---MPEEKRQWAYELSKCMTCGCCLEACPNV--NEKsDFIGPAAISQVRLFnAHPTGEMHKEERLRALMGDGGIADCGNA 214

                        170       180
                 ....*....|....*....|
gi 503935176 210 MNCVSVCPKGLNPTRAIGHI 229
Cdd:PRK08640 215 QNCVRVCPKGIPLTTSIAAM 234
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 1-160 1.01e-10

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 59.85  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176   1 MKLEFSVYRyNPDVDDAPRMQDYTLE-AEEgrDMMLLDALIQLKE------KDPtLSFRRSCREGVCGSDGVNMNGK-NG 72
Cdd:PRK07570   1 MKLTLKIWR-QKGPDDKGKFETYEVDdISP--DMSFLEMLDVLNEqliekgEEP-VAFDHDCREGICGMCGLVINGRpHG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176  73 LACITPISALQ----RAGQKIVIRPL--PGLPVVRDLVVDMGQFyaqyEKI----KPYLLNNGQNPPAREHLQSPEQREK 142
Cdd:PRK07570  77 PDRGTTTCQLHmrsfKDGDTITIEPWraAAFPVIKDLVVDRSAL----DRIiqagGYVSVNTGGAPDANAIPVPKEDADR 152

                        170
                 ....*....|....*...
gi 503935176 143 LDGLYECILCACCSTSCP 160
Cdd:PRK07570 153 AFDAAACIGCGACVAACP 170
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 148-221 1.55e-08

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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 49.77  E-value: 1.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503935176  148 ECILCACCSTSCPSFWWNPDKfigPAGLLAAYRFlidsrdtetdSRLEGLSDAFSVFRCHSIMNCVSVCPKGLN 221
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 149-220 3.96e-07

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: 46.15  E-value: 3.96e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503935176  149 CILCACCSTSCPSFwwnpdkfigpagLLAAYRFLIDSRDTETDSRLE---GLSDAFSVFRCHSIMNCVSVCPKGL 220
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRleaLEGLAEGLWLCTLCGACTEVCPVGI 64
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
145-236 4.14e-05

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 40.65  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176 145 GLYECILCACCSTSCPSFWW---NPDKFIgpagllaaYRFLIDSRDTETDSRleglsdafSVFRCHSIMNCVSVCPKGLN 221
Cdd:COG1150    1 NLKKCYQCGTCTASCPVARAmdyNPRKII--------RLAQLGLKEEVLKSD--------SIWLCVSCYTCTERCPRGID 64

                         90
                 ....*....|....*
gi 503935176 222 PTRAIGHIKSMLLQR 236
Cdd:COG1150   65 IADVMDALRNLAIRE 79
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 119-235 9.49e-05

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 42.76  E-value: 9.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503935176 119 PYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSrlEGLS 198
Cdd:COG0247   50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLS--EEVY 127

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503935176 199 DAFsvFRCHSIMNCVSVCPKGLNptraIGHIKSMLLQ 235
Cdd:COG0247  128 EVL--DLCLTCKACETACPSGVD----IADLIAEARA 158
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 21-90 1.85e-04

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 40.46  E-value: 1.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503935176  21 QDYTLEAEEgrDMMLLDAL---IQLKekdptlSFRRSCREGVCGSDGVNMNGKNGLACITPISALqrAGQKIV 90
Cdd:COG2080   11 KPVEVDVDP--DTPLLDVLrddLGLT------GTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQA--DGKEIT 73
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 149-217 1.28e-03

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: 36.07  E-value: 1.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503935176  149 CILCACCSTSCPSFWWnpdkfigpagllaayrflidsRDTETDSRLEGLSDAFSVFRCHSIMNCVSVCP 217
Cdd:pfam13237   9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
 
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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