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Conserved domains on  [gi|447158007|ref|WP_001235263|]
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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
 4-236 1.44e-170

succinate dehydrogenase iron-sulfur subunit; Reviewed


:

Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 468.89  E-value: 1.44e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   4 EFSIYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  83 nqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950  80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLER 230
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-236 1.44e-170

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 468.89  E-value: 1.44e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   4 EFSIYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  83 nqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950  80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLER 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 7-230 1.89e-129

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: 364.44  E-value: 1.89e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007    7 IYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQP 85
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   86 gkKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384  79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447158007  166 PDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-236 2.29e-129

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: 364.45  E-value: 2.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   1 MRLEFSIYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:COG0479    1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  80 SALNQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479   79 RDLKDT---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447158007 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479  155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-112 3.21e-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: 149.31  E-value: 3.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007    5 FSIYRYNPDVD-DAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 447158007   83 NQPGkkIVIRPLPGLPVIRDLVVDMGQFYA 112
Cdd:pfam13085  80 LGQD--ITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-236 1.44e-170

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 468.89  E-value: 1.44e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   4 EFSIYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  83 nqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950  80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLER 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 7-230 1.89e-129

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: 364.44  E-value: 1.89e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007    7 IYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQP 85
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   86 gkKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384  79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447158007  166 PDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-236 2.29e-129

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: 364.45  E-value: 2.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   1 MRLEFSIYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:COG0479    1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  80 SALNQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479   79 RDLKDT---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447158007 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479  155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
7-236 2.13e-125

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 354.65  E-value: 2.13e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   7 IYRYNPDVDDAPRMQDYTLEAEEGrDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNqpg 86
Cdd:PRK12575   9 IYRYDPDDDAAPRMQRYEIAPRAE-DRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALP--- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  87 KKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQnPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNP 166
Cdd:PRK12575  85 REIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTV-PPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007 167 DKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLARR 233
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 4-234 2.03e-122

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 348.70  E-value: 2.03e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   4 EFSIYRYNPDVDDAPRMQDYTLEAEEGRDMMLlDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAl 82
Cdd:PLN00129  45 EFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVL-DVLIKIKnEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDR- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  83 nQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYL-LNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PLN00129 123 -DESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLkTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPS 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447158007 162 FWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLL 234
Cdd:PLN00129 202 YWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-236 4.07e-67

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 209.94  E-value: 4.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   1 MRLEFSIYRYNPDvdDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLAC---- 75
Cdd:PRK12577   1 MEVLFKILRQKQN--SAPYVQTYTLEVEPG--NTILDCLNRIKwEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  76 ---ITPISALNQPG-KKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECIL 151
Cdd:PRK12577  77 gseLARLSDSNSGAiPEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007 152 CACCSTSCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLS-DAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:PRK12577 157 CGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235


                 ....*.
gi 447158007 231 SMLLQR 236
Cdd:PRK12577 236 QEILAR 241
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-231 5.07e-59

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 187.65  E-value: 5.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   1 MRLEFSIYRYNPDvdDAPRMQDYTLEAEegRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACIT-P 78
Cdd:PRK12576   7 KEVIFKVKRYDPE--KGSWWQEYKVKVD--RFTQVTEALRRIKeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTlV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  79 ISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLL-NNGQNPPAREHLQMPEQREKLDGLYECILCACCST 157
Cdd:PRK12576  83 LDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYrAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVS 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007 158 SCPSFWWNPdKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDafSVFRCHSIMNCVSVCPKGLNPTRAIGHIKS 231
Cdd:PRK12576 163 ACPVVAIDP-EFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
3-226 7.76e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 176.04  E-value: 7.76e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   3 LEFSIYRYNPDVDDAPRMQDYTLEAEEgrDMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITpisA 81
Cdd:PRK12385   7 LKIEVLRYNPEVDTEPHSQTYEVPYDE--TTSLLDALGYIKDNlAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT---F 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  82 LNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PRK12385  82 LRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQ 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447158007 162 FWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAI 226
Cdd:PRK12385 162 FGLNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAI 225
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 2-220 7.32e-50

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 162.81  E-value: 7.32e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   2 RLEFSIYRYNP-DVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:PRK13552   4 TLTFNIFRYNPqDPGSKPHMVTYQLEETPG--MTLFIALNRIREEqDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  80 SALnqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQ-YEKIKPYLLNNGQNPPAREHLQM-PEQREKLDGLYECILCACCST 157
Cdd:PRK13552  82 SDY--PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRLEERMePEEADEIYELDRCIECGCCVA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007 158 SCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRL-DGLSDAFSVFRCHSIMNCVSVCPKGL 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 3.21e-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: 149.31  E-value: 3.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007    5 FSIYRYNPDVD-DAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 447158007   83 NQPGkkIVIRPLPGLPVIRDLVVDMGQFYA 112
Cdd:pfam13085  80 LGQD--ITLEPLPGFPVIRDLVVDRSAFFE 107
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 7-226 1.20e-35

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 131.67  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   7 IYRYNPDVDdAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPIsalnQP 85
Cdd:PRK06259   8 VKRFDPEKD-EPHFESYEVPVKEG--MTVLDALEYINKTyDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV----ED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  86 GkkIVIRPLpGLPVIRDLVVDMGQFYAQYEKIKPYLLnngqnpPAREHLQMPEQREKLDGLYECILCACCSTSCPSFwwN 165
Cdd:PRK06259  81 G--MIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQ------RKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--K 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007 166 PDKFIGPAGLLAAYRFLIDSRDTEtdsrlDGLSDAF--SVFRCHSIMNCVSVCPKGLN-PTRAI 226
Cdd:PRK06259 150 VSDYPGPTFMRQLARFAFDPRDEG-----DREKEAFdeGLYNCTTCGKCVEVCPKEIDiPGKAI 208
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 15-223 1.11e-22

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 92.84  E-value: 1.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  15 DDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNqPGKKIVIRP 93
Cdd:PRK12386  14 ASGGELQDYTVEVNEG--EVVLDVIHRLQaTQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTFD-EDETVTVTP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  94 LPGLPVIRDLVVDMGQFYAQYEKIKPYllnngqNPPAR----EHLQMPEQREKLDGLYECILCACCSTSC---PSFWWNP 166
Cdd:PRK12386  91 MRTFPVIRDLVTDVSFNYEKAREIPSF------TPPKDlqpgEYRMQQVDVERSQEFRKCIECFLCQNVChvvRDHEENK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447158007 167 DKFIGPagllaayRFLI-----DSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPT 223
Cdd:PRK12386 165 PAFAGP-------RFLMriaelEMHPLDTADRRAEAQEEHGLGYCNITKCCTEVCPEHIKIT 219
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 55-229 8.60e-22

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 90.43  E-value: 8.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  55 CREGVCGSDGLNMNGKNGLACITPISALNQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKP-------YLLNNGQN 127
Cdd:PRK08640  63 CLEEVCGACSMVINGKPRQACTALIDQLEQP---IRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAwipidgtYDLGPGPR 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007 128 PParehlqmPEQREKLDGLYECILCACCSTSCPSFwwNPD-KFIGPAGLLAAYRF-LIDSRDTETDSRLDGLSDAFSVFR 205
Cdd:PRK08640 140 MP-------EEKRQWAYELSKCMTCGCCLEACPNV--NEKsDFIGPAAISQVRLFnAHPTGEMHKEERLRALMGDGGIAD 210

                        170       180
                 ....*....|....*....|....
gi 447158007 206 CHSIMNCVSVCPKGLNPTRAIGHI 229
Cdd:PRK08640 211 CGNAQNCVRVCPKGIPLTTSIAAM 234
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 1-160 1.83e-09

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 56.38  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007   1 MRLEFSIYRyNPDVDDAPRMQDYTLE-AEEgrDMMLLDALIQLKE------KDPsLSFRRSCREGVCGSDGLNMNG---- 69
Cdd:PRK07570   1 MKLTLKIWR-QKGPDDKGKFETYEVDdISP--DMSFLEMLDVLNEqliekgEEP-VAFDHDCREGICGMCGLVINGrphg 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007  70 --KNGLACITPISALNQpGKKIVIRPL--PGLPVIRDLVVDMGQFyaqyEKI----KPYLLNNGQNPPAREHLQMPEQRE 141
Cdd:PRK07570  77 pdRGTTTCQLHMRSFKD-GDTITIEPWraAAFPVIKDLVVDRSAL----DRIiqagGYVSVNTGGAPDANAIPVPKEDAD 151

                        170
                 ....*....|....*....
gi 447158007 142 KLDGLYECILCACCSTSCP 160
Cdd:PRK07570 152 RAFDAAACIGCGACVAACP 170
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 148-221 2.39e-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: 49.38  E-value: 2.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447158007  148 ECILCACCSTSCPSFWWNPDKfigPAGLLAAYRFlidsrdtetdSRLDGLSDAFSVFRCHSIMNCVSVCPKGLN 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 4.16e-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: 4.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447158007  149 CILCACCSTSCPSFwwnpdkfigpagLLAAYRFLIDSRDTETDSRLD---GLSDAFSVFRCHSIMNCVSVCPKGL 220
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRleaLEGLAEGLWLCTLCGACTEVCPVGI 64
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
145-236 4.53e-05

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 40.65  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007 145 GLYECILCACCSTSCPSFWW---NPDKFIgpagllaaYRFLIDSRDTETDSRldglsdafSVFRCHSIMNCVSVCPKGLN 221
Cdd:COG1150    1 NLKKCYQCGTCTASCPVARAmdyNPRKII--------RLAQLGLKEEVLKSD--------SIWLCVSCYTCTERCPRGID 64

                         90
                 ....*....|....*
gi 447158007 222 PTRAIGHIKSMLLQR 236
Cdd:COG1150   65 IADVMDALRNLAIRE 79
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 119-235 2.75e-04

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 41.60  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447158007 119 PYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRldglS 198
Cdd:COG0247   50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLSE----E 125

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447158007 199 DAFSVFRCHSIMNCVSVCPKGLNptraIGHIKSMLLQ 235
Cdd:COG0247  126 VYEVLDLCLTCKACETACPSGVD----IADLIAEARA 158
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 149-217 1.79e-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: 35.69  E-value: 1.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447158007  149 CILCACCSTSCPSFWWnpdkfigpagllaayrflidsRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCP 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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