|
Name |
Accession |
Description |
Interval |
E-value |
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
19-266 |
0e+00 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 541.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 19 KQKTVKLIIKRQDTSDSKPYEETFEIPYRENLNVIACLMEIRRNPVNIKGEKTTPVVWDMNCLEEVCGACSMVINGRARQ 98
Cdd:PRK08640 2 SEKTVRLIIKRQDGPDSKPYWEEFEIPYRPNMNVISALMEIRRNPVNAKGEKTTPVVWDMNCLEEVCGACSMVINGKPRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 99 SCSAIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGTYDLGPGPRMPEKKRQTAYELSKCMTCGVCL 178
Cdd:PRK08640 82 ACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGTYDLGPGPRMPEEKRQWAYELSKCMTCGCCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 179 EVCPNVTENNKFVGAQAISQVRLFNLHPTGSMTKDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAMNRETTFH 258
Cdd:PRK08640 162 EACPNVNEKSDFIGPAAISQVRLFNAHPTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAAMNRETTKQ 241
|
....*...
gi 577530840 259 MFKSFFGS 266
Cdd:PRK08640 242 SFKSFFGS 249
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
21-258 |
9.48e-101 |
|
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: 293.58 E-value: 9.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 21 KTVKLIIKRQD-TSDSKPYEETFEIPYRENLNVIACLMEIrrnpvniKGEKTTPVVWDMNCLEEVCGACSMVINGRARQS 99
Cdd:COG0479 1 MTVTLKIWRQDpETDSKPRFQTYEVPVSPGMTVLDALDYI-------KEEQDPTLAFRRSCREGICGSCAMVINGRPRLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 100 CSAIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGTYDlGPGPRMPEKKRQTAYELSKCMTCGVCLE 179
Cdd:COG0479 74 CQTHVRDLKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP-DNERLQSPEDREKADDLAECILCGACVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577530840 180 VCPNVTENNKFVGAQAISQVRLFNLHPTGSMTkDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAMNRETTFH 258
Cdd:COG0479 153 ACPNVWANPDFLGPAALAQAYRFALDPRDEET-EERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
27-251 |
4.93e-43 |
|
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: 146.04 E-value: 4.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 27 IKRQDTS-DSKPYEETFEIPYRENLNVIACLMEIrrnpvniKGEKTTPVVWDMNCLEEVCGACSMVINGRARQSCSAIVD 105
Cdd:TIGR00384 1 VLRFNPDvDEKPHLQSYEVPADEGMTVLDALNYI-------KDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 106 QLEQP-IRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDG-TYDLGPGPRMPEkKRQTAYELSKCMTCGVCLEVCPN 183
Cdd:TIGR00384 74 DLGQPvMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSqPEPEGEFLQTPE-QREKLDQLSGCILCGCCYSSCPA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577530840 184 VTENNKFVGAQAISQVRLFNLHPTgSMTKDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAM 251
Cdd:TIGR00384 153 FWWNPEFLGPAALTAAYRFLIDSR-DHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKL 219
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
24-134 |
2.85e-38 |
|
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: 130.05 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 24 KLIIKRQDTSDSK--PYEETFEIPYRENLNVIACLMEIRRNPVnikgektTPVVWDMNCLEEVCGACSMVINGRARQSCS 101
Cdd:pfam13085 1 TLRVFRYDPRVDRdePYYQEYEVPYEEGMTVLDALNKIKEEQD-------PTLAFRRSCREGICGSCAMNINGKPRLACK 73
|
90 100 110
....*....|....*....|....*....|....
gi 577530840 102 AIVDQ-LEQPIRLEPMNTFPVIRDLQVDRSRMFD 134
Cdd:pfam13085 74 TLIDDlLGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
19-266 |
0e+00 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 541.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 19 KQKTVKLIIKRQDTSDSKPYEETFEIPYRENLNVIACLMEIRRNPVNIKGEKTTPVVWDMNCLEEVCGACSMVINGRARQ 98
Cdd:PRK08640 2 SEKTVRLIIKRQDGPDSKPYWEEFEIPYRPNMNVISALMEIRRNPVNAKGEKTTPVVWDMNCLEEVCGACSMVINGKPRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 99 SCSAIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGTYDLGPGPRMPEKKRQTAYELSKCMTCGVCL 178
Cdd:PRK08640 82 ACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGTYDLGPGPRMPEEKRQWAYELSKCMTCGCCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 179 EVCPNVTENNKFVGAQAISQVRLFNLHPTGSMTKDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAMNRETTFH 258
Cdd:PRK08640 162 EACPNVNEKSDFIGPAAISQVRLFNAHPTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAAMNRETTKQ 241
|
....*...
gi 577530840 259 MFKSFFGS 266
Cdd:PRK08640 242 SFKSFFGS 249
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
21-258 |
9.48e-101 |
|
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: 293.58 E-value: 9.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 21 KTVKLIIKRQD-TSDSKPYEETFEIPYRENLNVIACLMEIrrnpvniKGEKTTPVVWDMNCLEEVCGACSMVINGRARQS 99
Cdd:COG0479 1 MTVTLKIWRQDpETDSKPRFQTYEVPVSPGMTVLDALDYI-------KEEQDPTLAFRRSCREGICGSCAMVINGRPRLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 100 CSAIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGTYDlGPGPRMPEKKRQTAYELSKCMTCGVCLE 179
Cdd:COG0479 74 CQTHVRDLKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP-DNERLQSPEDREKADDLAECILCGACVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577530840 180 VCPNVTENNKFVGAQAISQVRLFNLHPTGSMTkDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAMNRETTFH 258
Cdd:COG0479 153 ACPNVWANPDFLGPAALAQAYRFALDPRDEET-EERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
27-251 |
4.93e-43 |
|
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: 146.04 E-value: 4.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 27 IKRQDTS-DSKPYEETFEIPYRENLNVIACLMEIrrnpvniKGEKTTPVVWDMNCLEEVCGACSMVINGRARQSCSAIVD 105
Cdd:TIGR00384 1 VLRFNPDvDEKPHLQSYEVPADEGMTVLDALNYI-------KDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 106 QLEQP-IRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDG-TYDLGPGPRMPEkKRQTAYELSKCMTCGVCLEVCPN 183
Cdd:TIGR00384 74 DLGQPvMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSqPEPEGEFLQTPE-QREKLDQLSGCILCGCCYSSCPA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577530840 184 VTENNKFVGAQAISQVRLFNLHPTgSMTKDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAM 251
Cdd:TIGR00384 153 FWWNPEFLGPAALTAAYRFLIDSR-DHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKL 219
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
24-134 |
2.85e-38 |
|
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: 130.05 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 24 KLIIKRQDTSDSK--PYEETFEIPYRENLNVIACLMEIRRNPVnikgektTPVVWDMNCLEEVCGACSMVINGRARQSCS 101
Cdd:pfam13085 1 TLRVFRYDPRVDRdePYYQEYEVPYEEGMTVLDALNKIKEEQD-------PTLAFRRSCREGICGSCAMNINGKPRLACK 73
|
90 100 110
....*....|....*....|....*....|....
gi 577530840 102 AIVDQ-LEQPIRLEPMNTFPVIRDLQVDRSRMFD 134
Cdd:pfam13085 74 TLIDDlLGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
24-260 |
2.31e-32 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 118.74 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 24 KLIIKRQDTS-DSKPYEETFEIP-YRENLNVIACLMEIrrnpvniKGEKTTPVVWDMNCLEEVCGACSMVINGRARQSCS 101
Cdd:PRK05950 1 TFKIYRYNPDvDANPRMQTYEVDvDECGPMVLDALIKI-------KNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 102 AIVDQLE-QPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGtydlgPGP-----RMPEKkRQTAYELSKCMTCG 175
Cdd:PRK05950 74 TPISDLKkGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-----PPParerlQSPED-REKLDGLYECILCA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 176 VCLEVCPNVTEN-NKFVGAQAISQVRLFNLHPTGSMTKdERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIAAMNRE 254
Cdd:PRK05950 148 CCSTSCPSFWWNpDKFLGPAALLQAYRFIADSRDEATG-ERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRM 226
|
....*.
gi 577530840 255 TTFHMF 260
Cdd:PRK05950 227 LLERRV 232
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
13-255 |
5.93e-32 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 118.70 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 13 ETQSKPKQKTVKliIKRQDTSDSKPYEEtFEIPYRENLNVIACLmeiRRnpvnIKGEKTTPVVWDMNCLEEVCGACSMVI 92
Cdd:PRK12576 1 MTQSPEKEVIFK--VKRYDPEKGSWWQE-YKVKVDRFTQVTEAL---RR----IKEEQDPTLSYRASCHMAVCGSCGMKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 93 NGRARQSCS----AIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGTYDLGPG-PRM-PEKKRQTaY 166
Cdd:PRK12576 71 NGEPRLACKtlvlDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAeHRLkPEDQKEL-W 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 167 ELSKCMTCGVCLEVCPNVTENNKFVGAQAISQVRLFNLHPTGSMTkDERLNALMgtGGLQQCGNSQNCVNACPKGIPLTT 246
Cdd:PRK12576 150 KFAQCIWCGLCVSACPVVAIDPEFLGPAAHAKGYRFLADPRDTIT-EERMKILI--DSSWRCTYCYSCSNVCPRDIEPVT 226
|
....*....
gi 577530840 247 SIAAMNRET 255
Cdd:PRK12576 227 AIKKTRSFT 235
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
21-253 |
1.17e-30 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 114.28 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 21 KTVKLIIKRQDTSD--SKPYEETFEIPYRENLNVIACLMEIRrnpvnikgEKTTP-VVWDMNCLEEVCGACSMVINGRAR 97
Cdd:PRK13552 3 RTLTFNIFRYNPQDpgSKPHMVTYQLEETPGMTLFIALNRIR--------EEQDPsLQFDFVCRAGICGSCAMVINGRPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 98 QSCSAIVDQLEQP-IRLEPMNTFPVIRDLQVDRSRMFDNL-KRMKAWIPIDGTYDLG-PGPRMPEKKRQTAYELSKCMTC 174
Cdd:PRK13552 75 LACRTLTSDYPDGvITLMPLPVFKLIGDLSVNTGKWFREMsERVESWIHTDKEFDIHrLEERMEPEEADEIYELDRCIEC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 175 GVCLEVCPNVTENNKFVGAQAISQVRLFNLHPtgsmtKDERLNA----LMGTG-GLQQCGNSQNCVNACPKGIPLTTSIA 249
Cdd:PRK13552 155 GCCVAACGTKQMREDFVGAVGLNRIARFELDP-----RDERTDEdfyeLIGNDdGVFGCMSLLGCEDNCPKDLPLQQQIA 229
|
....
gi 577530840 250 AMNR 253
Cdd:PRK13552 230 YLRR 233
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
20-242 |
3.27e-27 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 105.55 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 20 QKTVKLIIKRQD-TSDSKPYEETFEIPYRENLNVIACLMEIRRNPvnikgEKTTPVVWdmNCLEEVCGACSMVINGRARQ 98
Cdd:PRK12385 4 MKNLKIEVLRYNpEVDTEPHSQTYEVPYDETTSLLDALGYIKDNL-----APDLSYRW--SCRMAICGSCGMMVNNVPKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 99 SCSAIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWI------PIDGTYDLGPGpRMpEKKRQtayeLSKCM 172
Cdd:PRK12385 77 ACKTFLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIigndrtPDDGPNKQTPA-QM-AKYHQ----FSGCI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 173 TCGVCLEVCPNVTENNKFVGAQAISQVRLFNLHPTGSmTKDERLNALMGTGGLQQCGNSQNCVNACPKGI 242
Cdd:PRK12385 151 NCGLCYAACPQFGLNPEFIGPAAITLAHRYNLDSRDH-GKKERMKQLNGQNGVWSCTFVGYCSEVCPKHV 219
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
67-254 |
1.21e-24 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 98.75 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 67 KGEKttPVVWDMNCLEEVCGACSMVINGRA------RQSCsaivdQLE-------QPIRLEPM--NTFPVIRDLQVDRSr 131
Cdd:PRK07570 47 KGEE--PVAFDHDCREGICGMCGLVINGRPhgpdrgTTTC-----QLHmrsfkdgDTITIEPWraAAFPVIKDLVVDRS- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 132 MFDNLkrMKAwipidGTY---DLGPGPR-----MPEKKRQTAYELSKCMTCGVCLEVCPNVTEnNKFVGAQaISQvrlFN 203
Cdd:PRK07570 119 ALDRI--IQA-----GGYvsvNTGGAPDanaipVPKEDADRAFDAAACIGCGACVAACPNGSA-MLFTGAK-VSH---LA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577530840 204 LHPTGSMTKDERLNAL---MGTGGLQQCGNSQNCVNACPKGIPLtTSIAAMNRE 254
Cdd:PRK07570 187 LLPQGQPERARRVRAMvaqMDEEGFGNCTNTGECEAVCPKGISL-ENIARMNRE 239
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
21-242 |
1.78e-22 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 96.23 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 21 KTVKLIIKRQDTSDSKPYEETFEIPYRENLNVIACLMEIRRNP-VNIKgekttpvvWDMNCLEEVCGACSMVINGRARQS 99
Cdd:PRK06259 2 KMITITVKRFDPEKDEPHFESYEVPVKEGMTVLDALEYINKTYdANIA--------FRSSCRAGQCGSCAVTINGEPVLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 100 CSAivdQLEQPIRLEPMNtFPVIRDLQVDRSRMFDNLKRMKAWIPIDgtydlGPGPRMPEKKRQTaYELSKCMTCGVCLE 179
Cdd:PRK06259 74 CKT---EVEDGMIIEPLD-FPVIKDLIVDREPYYKKLKSLRNYLQRK-----NEKITYPEDIEDI-KKLRGCIECLSCVS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577530840 180 VCPnVTENNKFVGAQAISQVRLFNLHPtgsmtKDERLNALMG-TGGLQQCGNSQNCVNACPKGI 242
Cdd:PRK06259 144 TCP-ARKVSDYPGPTFMRQLARFAFDP-----RDEGDREKEAfDEGLYNCTTCGKCVEVCPKEI 201
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
74-245 |
2.20e-22 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 92.84 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 74 VVWdmNCLEEVCGACSMVINGRARQSCSAIVDQLEQ--PIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPidgTYDL 151
Cdd:PRK12386 49 VRW--NCKAGKCGSCSAEINGRPRLMCMTRMSTFDEdeTVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTP---PKDL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 152 GPGP-RMPEKKRQTAYELSKCMTCGVCLEVCPNVT--ENNK--FVGAQAISQVRLFNLHPtgsMTKDERLNALMGTGGLQ 226
Cdd:PRK12386 124 QPGEyRMQQVDVERSQEFRKCIECFLCQNVCHVVRdhEENKpaFAGPRFLMRIAELEMHP---LDTADRRAEAQEEHGLG 200
|
170
....*....|....*....
gi 577530840 227 QCGNSQNCVNACPKGIPLT 245
Cdd:PRK12386 201 YCNITKCCTEVCPEHIKIT 219
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
22-244 |
6.27e-22 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 92.84 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 22 TVKLIIKRQdTSDSKPYEETFEIPYRENLNVIACLMEIrrnpvniKGEKTTPVVWDMNCLEEVCGACSMVINGRARQSCS 101
Cdd:PRK12577 2 EVLFKILRQ-KQNSAPYVQTYTLEVEPGNTILDCLNRI-------KWEQDGSLAFRKNCRNTICGSCAMRINGRSALACK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 102 -AIVDQLEQ----------PIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDgtydlgpGPRMPEKK-RQTAYELS 169
Cdd:PRK12577 74 eNVGSELARlsdsnsgaipEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTA-------ARQVPEREfLQTPEERS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 170 K------CMTCGVCLEVCPNVTENNKFVGAQAISQV-RLfnLHPTGSMTKDERLNAL-MGTGGLQQCGNSQNCVNACPKG 241
Cdd:PRK12577 147 KldqtgnCILCGACYSECNAREVNPEFVGPHALAKAqRM--VADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPME 224
|
....
gi 577530840 242 I-PL 244
Cdd:PRK12577 225 VaPL 228
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
25-249 |
7.71e-22 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 90.79 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 25 LIIKRQDTS-DSKPYEETFEIPYREN----LNVIAclmeirrnpvNIKGEKTTpVVWDMNCLEEVCGACSMVINGRARQS 99
Cdd:PRK12575 7 LHIYRYDPDdDAAPRMQRYEIAPRAEdrmlLDVLG----------RVKAQDET-LSYRRSCREGICGSDAMNINGRNGLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 100 CSAIVDQLEQPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDGTYDLGPGPRMPEKKRQTAyELSKCMTCGVCLE 179
Cdd:PRK12575 76 CLTNMQALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPPERERLQTPQEREQLD-GLYECILCACCST 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577530840 180 VCPNVTEN-NKFVGAQAISQVRLFnLHPTGSMTKDERLNALMGTGGLQQCGNSQNCVNACPKGIPLTTSIA 249
Cdd:PRK12575 155 ACPSYWWNpDKFVGPAGLLQAYRF-IADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIG 224
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
12-251 |
9.86e-16 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 74.83 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 12 HETQSKPKQKTVKLI----IKRQD-TSDSKPYEETFEIpyreNLN-----VIACLMEIrrnpvniKGEKTTPVVWDMNCL 81
Cdd:PLN00129 29 AETKASSKGSKPSNLkefqIYRWNpDNPGKPHLQSYKV----DLNdcgpmVLDVLIKI-------KNEQDPSLTFRRSCR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 82 EEVCGACSMVINGRARQSCSAIVDQLE-QPIRLEPMNTFPVIRDLQVDRSRMFDNLKRMKAWIPIDgTYDLGPGPRMPEK 160
Cdd:PLN00129 98 EGICGSCAMNIDGKNTLACLTKIDRDEsGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTK-KPPEDGQKEHLQS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 161 KRQTA-----YElskCMTCGVCLEVCPNVTEN-NKFVGAQAISQVRLFNLHPTGSMTKdERLNALMGTGGLQQCGNSQNC 234
Cdd:PLN00129 177 KEDRAkldgmYE---CILCACCSTSCPSYWWNpEKFLGPAALLHAYRWISDSRDEYTK-ERLEALDDEFKLYRCHTIRNC 252
|
250
....*....|....*..
gi 577530840 235 VNACPKGIPLTTSIAAM 251
Cdd:PLN00129 253 SNACPKGLNPAKAIAKI 269
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
170-242 |
1.82e-04 |
|
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: 38.83 E-value: 1.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577530840 170 KCMTCGVCLEVCPNVTENNkfvgaqaisqVRLFNLHPTGSMTKDERLNALMGTG-GLQQCGNSQNCVNACPKGI 242
Cdd:pfam13183 1 RCIRCGACLAACPVYLVTG----------GRFPGDPRGGAAALLGRLEALEGLAeGLWLCTLCGACTEVCPVGI 64
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
168-253 |
2.37e-03 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 36.03 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 168 LSKCMTCGVCLEVCPNVtennkFVGAQAISQ-VRLFNLhptgsmtkdERLNALMGTGGLQQCGNSQNCVNACPKGIPLTT 246
Cdd:COG1150 2 LKKCYQCGTCTASCPVA-----RAMDYNPRKiIRLAQL---------GLKEEVLKSDSIWLCVSCYTCTERCPRGIDIAD 67
|
....*..
gi 577530840 247 SIAAMNR 253
Cdd:COG1150 68 VMDALRN 74
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
167-254 |
7.54e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 37.36 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530840 167 ELSKCMTCGVCLEVCP--NVTENNKFV---GAQAISQVRLFNLHPTGSMTKDERLNA-LMgtgglqqCGnsqNCVNACPK 240
Cdd:COG0247 76 ALDACVGCGFCRAMCPsyKATGDEKDSprgRINLLREVLEGELPLDLSEEVYEVLDLcLT-------CK---ACETACPS 145
|
90
....*....|....
gi 577530840 241 GIPLTTSIAAMNRE 254
Cdd:COG0247 146 GVDIADLIAEARAQ 159
|
|
| |
