|
Name |
Accession |
Description |
Interval |
E-value |
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
4-238 |
1.10e-172 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 474.28 E-value: 1.10e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 4 EFSVYRYNPDVDDAPRMQDYTLEVEEgRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 83 qrPGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950 80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069032964 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
1-236 |
3.29e-131 |
|
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: 369.07 E-value: 3.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 1 MKLEFSVYRYNPDVDDAPRMQDYTLEVEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:COG0479 1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 80 SALqrpGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479 79 RDL---KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069032964 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479 155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
7-230 |
3.46e-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: 361.36 E-value: 3.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 7 VYRYNPDVDDAPRMQDYTLEVEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISALQRP 85
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 86 gqKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384 79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069032964 166 PDkFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 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 |
1.79e-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: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 5 FSVYRYNPDVD-DAPRMQDYTLEVEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:pfam13085 2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100 110
....*....|....*....|....*....|
gi 1069032964 83 qrPGQKIVIRPLPGLPVVRDLVVDMGQFYA 112
Cdd:pfam13085 80 --LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
4-238 |
1.10e-172 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 474.28 E-value: 1.10e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 4 EFSVYRYNPDVDDAPRMQDYTLEVEEgRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 83 qrPGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950 80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069032964 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950 157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
1-236 |
3.29e-131 |
|
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: 369.07 E-value: 3.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 1 MKLEFSVYRYNPDVDDAPRMQDYTLEVEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:COG0479 1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 80 SALqrpGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQSPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479 79 RDL---KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069032964 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479 155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
7-237 |
2.50e-128 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 362.35 E-value: 2.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 7 VYRYNPDVDDAPRMQDYTLEVEEGrDMMLLDALIQLKEKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISALQRpg 86
Cdd:PRK12575 9 IYRYDPDDDAAPRMQRYEIAPRAE-DRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALPR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 87 qKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQnPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWNP 166
Cdd:PRK12575 86 -EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTV-PPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069032964 167 DKFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRS 237
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLARRA 234
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
7-230 |
3.46e-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: 361.36 E-value: 3.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 7 VYRYNPDVDDAPRMQDYTLEVEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISALQRP 85
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 86 gqKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384 79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069032964 166 PDkFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
4-234 |
1.89e-123 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 351.40 E-value: 1.89e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 4 EFSVYRYNPDVDDAPRMQDYTLEVEEGRDMMLlDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAl 82
Cdd:PLN00129 45 EFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVL-DVLIKIKnEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDR- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 83 qRPGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYL-LNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PLN00129 123 -DESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLkTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPS 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069032964 162 FWWNPDKFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLL 234
Cdd:PLN00129 202 YWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-238 |
4.62e-68 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 212.63 E-value: 4.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 1 MKLEFSVYRYNPDvdDAPRMQDYTLEVEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:PRK12577 1 MEVLFKILRQKQN--SAPYVQTYTLEVEPG--NTILDCLNRIKwEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 80 -SALQRPGQ-------KIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECIL 151
Cdd:PRK12577 77 gSELARLSDsnsgaipEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 152 CACCSTSCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETESRLEGLS-DAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:PRK12577 157 CGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235
|
....*...
gi 1069032964 231 SMLLQRSA 238
Cdd:PRK12577 236 QEILARKD 243
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-231 |
8.54e-61 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 192.27 E-value: 8.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 1 MKLEFSVYRYNPDvdDAPRMQDYTLEVEegRDMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACIT-P 78
Cdd:PRK12576 7 KEVIFKVKRYDPE--KGSWWQEYKVKVD--RFTQVTEALRRIKeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTlV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 79 ISALQRPGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLL-NNGQNPPAREHLQSPEQREKLDGLYECILCACCST 157
Cdd:PRK12576 83 LDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYrAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069032964 158 SCPSFWWNPdKFIGPAGLLAAYRFLIDSRDTETESRLEGLSDafSVFRCHSIMNCVSVCPKGLNPTRAIGHIKS 231
Cdd:PRK12576 163 ACPVVAIDP-EFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-226 |
1.56e-57 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 182.98 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 1 MKLEfsVYRYNPDVDDAPRMQDYtlEVEEGRDMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITpi 79
Cdd:PRK12385 7 LKIE--VLRYNPEVDTEPHSQTY--EVPYDETTSLLDALGYIKDNlAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 80 sALQRPGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSC 159
Cdd:PRK12385 81 -FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069032964 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAI 226
Cdd:PRK12385 160 PQFGLNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAI 225
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
2-220 |
2.65e-48 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 158.96 E-value: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 2 KLEFSVYRYNP-DVDDAPRMQDYTLEVEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPI 79
Cdd:PRK13552 4 TLTFNIFRYNPqDPGSKPHMVTYQLEETPG--MTLFIALNRIREEqDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 80 SALqrPGQKIVIRPLPGLPVVRDLVVDMGQFYAQ-YEKIKPYLLNNGQNPPAR-EHLQSPEQREKLDGLYECILCACCST 157
Cdd:PRK13552 82 SDY--PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRlEERMEPEEADEIYELDRCIECGCCVA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069032964 158 SCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTET-ESRLEGLSDAFSVFRCHSIMNCVSVCPKGL 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 |
1.79e-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: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 5 FSVYRYNPDVD-DAPRMQDYTLEVEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPISAL 82
Cdd:pfam13085 2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100 110
....*....|....*....|....*....|
gi 1069032964 83 qrPGQKIVIRPLPGLPVVRDLVVDMGQFYA 112
Cdd:pfam13085 80 --LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
7-226 |
2.03e-37 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 136.29 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 7 VYRYNPDVDdAPRMQDYTLEVEEGrdMMLLDALIQLKEK-DPTLSFRRSCREGVCGSDGVNMNGKNGLACITPIsalqRP 85
Cdd:PRK06259 8 VKRFDPEKD-EPHFESYEVPVKEG--MTVLDALEYINKTyDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV----ED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 86 GqkIVIRPLpGLPVVRDLVVDMGQFYAQYEKIKPYLLnngqnpPAREHLQSPEQREKLDGLYECILCACCSTSCPSFwwN 165
Cdd:PRK06259 81 G--MIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQ------RKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--K 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069032964 166 PDKFIGPAGLLAAYRFLIDSRDTETESRleglsDAF--SVFRCHSIMNCVSVCPKGLN-PTRAI 226
Cdd:PRK06259 150 VSDYPGPTFMRQLARFAFDPRDEGDREK-----EAFdeGLYNCTTCGKCVEVCPKEIDiPGKAI 208
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
2-223 |
5.38e-23 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 93.61 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 2 KLEFSVYRYNpdvDDAPRMQDYTLEVEEGrdMMLLDALIQLK-EKDPTLSFRRSCREGVCGSDGVNMNGKNGLACITPIS 80
Cdd:PRK12386 4 TAKFRVWRGD---ASGGELQDYTVEVNEG--EVVLDVIHRLQaTQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 81 ALQrPGQKIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYllnngqNPPAR----EHLQSPEQREKLDGLYECILCACCS 156
Cdd:PRK12386 79 TFD-EDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSF------TPPKDlqpgEYRMQQVDVERSQEFRKCIECFLCQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069032964 157 TSC---PSFWWNPDKFIGPagllaayRFLI-----DSRDTETESRLEGLSDAFSVFRCHSIMNCVSVCPKGLNPT 223
Cdd:PRK12386 152 NVChvvRDHEENKPAFAGP-------RFLMriaelEMHPLDTADRRAEAQEEHGLGYCNITKCCTEVCPEHIKIT 219
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
55-229 |
2.95e-22 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 91.59 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 55 CREGVCGSDGVNMNGKNGLACITPISALQRPgqkIVIRPLPGLPVVRDLVVDMGQFYAQYEKIKPYLLNNG---QNPPAR 131
Cdd:PRK08640 63 CLEEVCGACSMVINGKPRQACTALIDQLEQP---IRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGtydLGPGPR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 132 ehlQSPEQREKLDGLYECILCACCSTSCPSFwwNPD-KFIGPAGLLAAYRF-LIDSRDTETESRLEGLSDAFSVFRCHSI 209
Cdd:PRK08640 140 ---MPEEKRQWAYELSKCMTCGCCLEACPNV--NEKsDFIGPAAISQVRLFnAHPTGEMHKEERLRALMGDGGIADCGNA 214
|
170 180
....*....|....*....|
gi 1069032964 210 MNCVSVCPKGLNPTRAIGHI 229
Cdd:PRK08640 215 QNCVRVCPKGIPLTTSIAAM 234
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
1-160 |
4.51e-11 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 61.00 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 1 MKLEFSVYRyNPDVDDAPRMQDYTLE-VEEgrDMMLLDALIQLKE------KDPtLSFRRSCREGVCGSDGVNMNGK-NG 72
Cdd:PRK07570 1 MKLTLKIWR-QKGPDDKGKFETYEVDdISP--DMSFLEMLDVLNEqliekgEEP-VAFDHDCREGICGMCGLVINGRpHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 73 LACITPISALQ----RPGQKIVIRPL--PGLPVVRDLVVDMGQFyaqyEKI----KPYLLNNGQNPPAREHLQSPEQREK 142
Cdd:PRK07570 77 PDRGTTTCQLHmrsfKDGDTITIEPWraAAFPVIKDLVVDRSAL----DRIiqagGYVSVNTGGAPDANAIPVPKEDADR 152
|
170
....*....|....*...
gi 1069032964 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 |
1.47e-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: 1.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069032964 148 ECILCACCSTSCPSFWWNPDKfigPAGLLAAYRFlidsrdteteSRLEGLSDAFSVFRCHSIMNCVSVCPKGLN 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 |
3.92e-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: 3.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069032964 149 CILCACCSTSCPSFwwnpdkfigpagLLAAYRFLIDSRDTETESRLE---GLSDAFSVFRCHSIMNCVSVCPKGL 220
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRleaLEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
145-236 |
3.43e-05 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 41.04 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 145 GLYECILCACCSTSCPSFWW---NPDKFIgpagllaaYRFLIDSRDTETESRleglsdafSVFRCHSIMNCVSVCPKGLN 221
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAmdyNPRKII--------RLAQLGLKEEVLKSD--------SIWLCVSCYTCTERCPRGID 64
|
90
....*....|....*
gi 1069032964 222 PTRAIGHIKSMLLQR 236
Cdd:COG1150 65 IADVMDALRNLAIRE 79
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
21-90 |
5.67e-05 |
|
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: 42.00 E-value: 5.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069032964 21 QDYTLEVEEgrDMMLLDAL---IQLKekdptlSFRRSCREGVCGSDGVNMNGKNGLACITPISALQrpGQKIV 90
Cdd:COG2080 11 KPVEVDVDP--DTPLLDVLrddLGLT------GTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQAD--GKEIT 73
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
119-235 |
7.84e-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: 43.14 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069032964 119 PYLLNNGQNPPAREHLQSPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETESrlEGLS 198
Cdd:COG0247 50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLS--EEVY 127
|
90 100 110
....*....|....*....|....*....|....*..
gi 1069032964 199 DAFsvFRCHSIMNCVSVCPKGLNptraIGHIKSMLLQ 235
Cdd:COG0247 128 EVL--DLCLTCKACETACPSGVD----IADLIAEARA 158
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
149-217 |
7.59e-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: 36.84 E-value: 7.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069032964 149 CILCACCSTSCPSFWWnpdkfigpagllaayrflidsRDTETESRLEGLSDAFSVFRCHSIMNCVSVCP 217
Cdd:pfam13237 9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| |
