|
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 15830003 4 EFSIYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 83 nqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950 80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830003 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 15830003 7 IYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQP 85
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 86 gkKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384 79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830003 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 15830003 1 MRLEFSIYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:COG0479 1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 80 SALNQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479 79 RDLKDT---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830003 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 15830003 5 FSIYRYNPDVD-DAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:pfam13085 2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100 110
....*....|....*....|....*....|
gi 15830003 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 15830003 4 EFSIYRYNPDVDDAPRMQDYTLEAEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 83 nqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950 80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830003 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 15830003 7 IYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQP 85
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 86 gkKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384 79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830003 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 15830003 1 MRLEFSIYRYNPDVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:COG0479 1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 80 SALNQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479 79 RDLKDT---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830003 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 15830003 7 IYRYNPDVDDAPRMQDYTLEAEEGrDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNqpg 86
Cdd:PRK12575 9 IYRYDPDDDAAPRMQRYEIAPRAE-DRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 87 KKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQnPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNP 166
Cdd:PRK12575 85 REIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTV-PPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 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 15830003 4 EFSIYRYNPDVDDAPRMQDYTLEAEEGRDMMLlDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAl 82
Cdd:PLN00129 45 EFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVL-DVLIKIKnEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDR- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 83 nQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYL-LNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PLN00129 123 -DESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLkTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPS 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830003 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 15830003 1 MRLEFSIYRYNPDvdDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLAC---- 75
Cdd:PRK12577 1 MEVLFKILRQKQN--SAPYVQTYTLEVEPG--NTILDCLNRIKwEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 76 ---ITPISALNQPG-KKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECIL 151
Cdd:PRK12577 77 gseLARLSDSNSGAiPEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 152 CACCSTSCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLDGLS-DAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:PRK12577 157 CGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235
|
....*.
gi 15830003 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 15830003 1 MRLEFSIYRYNPDvdDAPRMQDYTLEAEegRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACIT-P 78
Cdd:PRK12576 7 KEVIFKVKRYDPE--KGSWWQEYKVKVD--RFTQVTEALRRIKeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTlV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 79 ISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLL-NNGQNPPAREHLQMPEQREKLDGLYECILCACCST 157
Cdd:PRK12576 83 LDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYrAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830003 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 15830003 3 LEFSIYRYNPDVDDAPRMQDYTLEAEEgrDMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITpisA 81
Cdd:PRK12385 7 LKIEVLRYNPEVDTEPHSQTYEVPYDE--TTSLLDALGYIKDNlAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT---F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 82 LNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PRK12385 82 LRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830003 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 15830003 2 RLEFSIYRYNP-DVDDAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:PRK13552 4 TLTFNIFRYNPqDPGSKPHMVTYQLEETPG--MTLFIALNRIREEqDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 80 SALnqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQ-YEKIKPYLLNNGQNPPAREHLQM-PEQREKLDGLYECILCACCST 157
Cdd:PRK13552 82 SDY--PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRLEERMePEEADEIYELDRCIECGCCVA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830003 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 15830003 5 FSIYRYNPDVD-DAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:pfam13085 2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100 110
....*....|....*....|....*....|
gi 15830003 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 15830003 7 IYRYNPDVDdAPRMQDYTLEAEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPIsalnQP 85
Cdd:PRK06259 8 VKRFDPEKD-EPHFESYEVPVKEG--MTVLDALEYINKTyDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV----ED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 86 GkkIVIRPLpGLPVIRDLVVDMGQFYAQYEKIKPYLLnngqnpPAREHLQMPEQREKLDGLYECILCACCSTSCPSFwwN 165
Cdd:PRK06259 81 G--MIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQ------RKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--K 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830003 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 15830003 15 DDAPRMQDYTLEAEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNqPGKKIVIRP 93
Cdd:PRK12386 14 ASGGELQDYTVEVNEG--EVVLDVIHRLQaTQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTFD-EDETVTVTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 94 LPGLPVIRDLVVDMGQFYAQYEKIKPYllnngqNPPAR----EHLQMPEQREKLDGLYECILCACCSTSC---PSFWWNP 166
Cdd:PRK12386 91 MRTFPVIRDLVTDVSFNYEKAREIPSF------TPPKDlqpgEYRMQQVDVERSQEFRKCIECFLCQNVChvvRDHEENK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830003 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 15830003 55 CREGVCGSDGLNMNGKNGLACITPISALNQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKP-------YLLNNGQN 127
Cdd:PRK08640 63 CLEEVCGACSMVINGKPRQACTALIDQLEQP---IRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAwipidgtYDLGPGPR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 128 PParehlqmPEQREKLDGLYECILCACCSTSCPSFwwNPD-KFIGPAGLLAAYRF-LIDSRDTETDSRLDGLSDAFSVFR 205
Cdd:PRK08640 140 MP-------EEKRQWAYELSKCMTCGCCLEACPNV--NEKsDFIGPAAISQVRLFnAHPTGEMHKEERLRALMGDGGIAD 210
|
170 180
....*....|....*....|....
gi 15830003 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 15830003 1 MRLEFSIYRyNPDVDDAPRMQDYTLE-AEEgrDMMLLDALIQLKE------KDPsLSFRRSCREGVCGSDGLNMNG---- 69
Cdd:PRK07570 1 MKLTLKIWR-QKGPDDKGKFETYEVDdISP--DMSFLEMLDVLNEqliekgEEP-VAFDHDCREGICGMCGLVINGrphg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830003 70 --KNGLACITPISALNQpGKKIVIRPL--PGLPVIRDLVVDMGQFyaqyEKI----KPYLLNNGQNPPAREHLQMPEQRE 141
Cdd:PRK07570 77 pdRGTTTCQLHMRSFKD-GDTITIEPWraAAFPVIKDLVVDRSAL----DRIiqagGYVSVNTGGAPDANAIPVPKEDAD 151
|
170
....*....|....*....
gi 15830003 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 15830003 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 15830003 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 15830003 145 GLYECILCACCSTSCPSFWW---NPDKFIgpagllaaYRFLIDSRDTETDSRldglsdafSVFRCHSIMNCVSVCPKGLN 221
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAmdyNPRKII--------RLAQLGLKEEVLKSD--------SIWLCVSCYTCTERCPRGID 64
|
90
....*....|....*
gi 15830003 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 15830003 119 PYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRldglS 198
Cdd:COG0247 50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLSE----E 125
|
90 100 110
....*....|....*....|....*....|....*..
gi 15830003 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 15830003 149 CILCACCSTSCPSFWWnpdkfigpagllaayrflidsRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCP 217
Cdd:pfam13237 9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| |
