|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
1-279 |
0e+00 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 555.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPM 80
Cdd:PLN00129 1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI-QDEASETTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129 75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIdRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1901086808 240 EAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
51-276 |
8.83e-121 |
|
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: 344.42 E-value: 8.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNPGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:COG0479 4 TLKIWRQDPETDSKPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 131 SETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWN 210
Cdd:COG0479 83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPA--PDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901086808 211 PEsYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQ 276
Cdd:COG0479 161 PD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKR 225
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
54-275 |
9.97e-109 |
|
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: 313.60 E-value: 9.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 54 IYRWNPDNPGKPELQNYQIDLKDCgPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEASET 133
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 134 -TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTpASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPE 212
Cdd:TIGR00384 80 mKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKS-QPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901086808 213 sYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIK 275
Cdd:TIGR00384 159 -FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
51-156 |
2.02e-48 |
|
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: 156.24 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNP-GKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQD- 128
Cdd:pfam13085 1 TLRVFRYDPRVDrDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDl 79
|
90 100
....*....|....*....|....*...
gi 1901086808 129 EASETTITPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
1-279 |
0e+00 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 555.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPM 80
Cdd:PLN00129 1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI-QDEASETTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129 75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIdRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1901086808 240 EAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
51-277 |
6.78e-156 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 433.45 E-value: 6.78e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNPGKPELQNYQIDLKDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 131 SET-TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWW 209
Cdd:PRK05950 81 KGKiVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPP--PARERLQSPEDREKLDGLYECILCACCSTSCPSFWW 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086808 210 NPESYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQL 277
Cdd:PRK05950 159 NPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRM 226
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
51-276 |
8.83e-121 |
|
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: 344.42 E-value: 8.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNPGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:COG0479 4 TLKIWRQDPETDSKPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 131 SETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWN 210
Cdd:COG0479 83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPA--PDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1901086808 211 PEsYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQ 276
Cdd:COG0479 161 PD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKR 225
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
54-275 |
9.97e-109 |
|
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: 313.60 E-value: 9.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 54 IYRWNPDNPGKPELQNYQIDLKDCgPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEASET 133
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 134 -TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTpASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPE 212
Cdd:TIGR00384 80 mKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKS-QPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901086808 213 sYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIK 275
Cdd:TIGR00384 159 -FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
47-277 |
2.48e-103 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 300.72 E-value: 2.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 47 SNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPMVLDALIKIKNEmDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI 126
Cdd:PRK12575 2 ADTRILHIYRYDPDDDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 127 QDEASETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPS 206
Cdd:PRK12575 81 QALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVP--PERERLQTPQEREQLDGLYECILCACCSTACPS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1901086808 207 YWWNPESYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQL 277
Cdd:PRK12575 159 YWWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTM 229
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
51-276 |
1.59e-64 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 204.93 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNPgkPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLAC-------L 123
Cdd:PRK12577 4 LFKILRQKQNSA--PYVQTYTLEV-EPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvgseL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 124 TKIQDEAS----ETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPaSVPAKEILQSKKDRAKLDGMYECILCAC 199
Cdd:PRK12577 81 ARLSDSNSgaipEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAAR-QVPEREFLQTPEERSKLDQTGNCILCGA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086808 200 CSTSCPSYWWNPEsYLGPAALLHANRWISDSRDEYTKERLEAID-DEFKLYRCHTILNCARACPKGLNPGKQITHIKQ 276
Cdd:PRK12577 160 CYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQ 236
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
51-279 |
3.34e-56 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 182.26 E-value: 3.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDnpGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK12576 10 IFKVKRYDPE--KGSWWQEYKVKV-DRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVLDVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 131 SE----TTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPS 206
Cdd:PRK12576 87 KKynsvITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACPV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901086808 207 YWWNPEsYLGPAALLHANRWISDSRDEYTKERLEAIDDefKLYRCHTILNCARACPKGLNPGkqiTHIKQLQR 279
Cdd:PRK12576 167 VAIDPE-FLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPV---TAIKKTRS 233
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
51-156 |
2.02e-48 |
|
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: 156.24 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNP-GKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQD- 128
Cdd:pfam13085 1 TLRVFRYDPRVDrDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDl 79
|
90 100
....*....|....*....|....*...
gi 1901086808 129 EASETTITPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
51-275 |
5.76e-48 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 159.87 E-value: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNPGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK12385 8 KIEVLRYNPEVDTEPHSQTYEVPY-DETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 131 SETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWL--KRKTPASVPAKeilQSKKDRAKLDGMYECILCACCSTSCPSYW 208
Cdd:PRK12385 87 GGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIigNDRTPDDGPNK---QTPAQMAKYHQFSGCINCGLCYAACPQFG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901086808 209 WNPEsYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIK 275
Cdd:PRK12385 164 LNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
51-271 |
1.40e-41 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 143.17 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNPG-KPELQNYQIDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQD- 128
Cdd:PRK13552 6 TFNIFRYNPQDPGsKPHMVTYQLEETP-GMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSDy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 129 EASETTITPLPHMFVIKDLVVDMTNFYNQ-YKSIEPWLKRKTPASVPAKEilqSKKDRAKLDGMYE---CILCACCSTSC 204
Cdd:PRK13552 85 PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRLE---ERMEPEEADEIYEldrCIECGCCVAAC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086808 205 PSYWWNPeSYLGPAALLHANRWISDSRDEYTKERL-EAIDDEFKLYRCHTILNCARACPKGLNPGKQI 271
Cdd:PRK13552 162 GTKQMRE-DFVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQI 228
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
51-271 |
1.14e-38 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 141.30 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNPDNpGKPELQNYQIDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK06259 5 TITVKRFDPEK-DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 131 setTITPLpHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPASVPAKEILQSKKDRakldgmyECILCACCSTSCPSYwwN 210
Cdd:PRK06259 83 ---IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKITYPEDIEDIKKLR-------GCIECLSCVSTCPAR--K 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1901086808 211 PESYLGPAALLHANRWISDSRDEYTKERlEAIDDefKLYRCHTILNCARACPKGLN-PGKQI 271
Cdd:PRK06259 150 VSDYPGPTFMRQLARFAFDPRDEGDREK-EAFDE--GLYNCTTCGKCVEVCPKEIDiPGKAI 208
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
51-265 |
1.98e-18 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 82.05 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 51 TFQIYRWNpDNPGkpELQNYQIDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQ--D 128
Cdd:PRK12386 6 KFRVWRGD-ASGG--ELQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMStfD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 129 EASETTITPLPHMFVIKDLVVDMTnfYNQYKSiepwlkRKTPASVPAK-----EILQSKKDRAKLDGMYECILCACCSTS 203
Cdd:PRK12386 82 EDETVTVTPMRTFPVIRDLVTDVS--FNYEKA------REIPSFTPPKdlqpgEYRMQQVDVERSQEFRKCIECFLCQNV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901086808 204 C---PSYWWNPESYLGPAALLHANRWISDSRDeyTKERLEAIDDEFKLYRCHTILNCARACPKGL 265
Cdd:PRK12386 154 ChvvRDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
102-265 |
1.42e-17 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 79.65 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 102 CREGICGSCAMNIDGCNGLACLTKIQDEASETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLK-RKTPASVPAKEILQ 180
Cdd:PRK08640 63 CLEEVCGACSMVINGKPRQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPiDGTYDLGPGPRMPE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 181 SKKDRakldgMYE---CILCACCSTSCPSYwwNPES-YLGPAAllhanrwISDSR--------DEYTKERLEAIDDEFKL 248
Cdd:PRK08640 143 EKRQW-----AYElskCMTCGCCLEACPNV--NEKSdFIGPAA-------ISQVRlfnahptgEMHKEERLRALMGDGGI 208
|
170
....*....|....*..
gi 1901086808 249 YRCHTILNCARACPKGL 265
Cdd:PRK08640 209 ADCGNAQNCVRVCPKGI 225
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
193-266 |
5.67e-07 |
|
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: 45.92 E-value: 5.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1901086808 193 ECILCACCSTSCPSYWWNPESylgPAALlhANRWISdsrdeytkERLEAIDDEFKLYRCHTILNCARACPKGLN 266
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDE---PKKL--MRAAYL--------GDLEELQANKVANLCSECGLCEYACPMGLD 61
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
102-279 |
2.19e-06 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 47.90 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 102 CREGICGSCAMNIDGC------NGLAC---LTKIQDeASETTITP-----LPhmfVIKDLVVDMTNF-----YNQYKSIe 162
Cdd:PRK07570 58 CREGICGMCGLVINGRphgpdrGTTTCqlhMRSFKD-GDTITIEPwraaaFP---VIKDLVVDRSALdriiqAGGYVSV- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 163 pwlkrKTPASVPAKEILQSKK--DRAkLDGMyECILCACCSTSCPsywwNPESYLGPAA------LLHANRwisDSRDEY 234
Cdd:PRK07570 133 -----NTGGAPDANAIPVPKEdaDRA-FDAA-ACIGCGACVAACP----NGSAMLFTGAkvshlaLLPQGQ---PERARR 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1901086808 235 TKERLEAIDDE-FKlyRCHTILNCARACPKGLNpgkqITHIKQLQR 279
Cdd:PRK07570 199 VRAMVAQMDEEgFG--NCTNTGECEAVCPKGIS----LENIARMNR 238
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
194-265 |
2.62e-06 |
|
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: 44.22 E-value: 2.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901086808 194 CILCACCSTSCPSYwwnpesylgpaaLLHANRWISDSRDEYTKERLEA---IDDEFKLYRCHTILNCARACPKGL 265
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRLealEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
194-262 |
1.55e-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: 38.77 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901086808 194 CILCACCSTSCPSYWWnpesylgpaallhanrwisdsRDEYTKERLEAIDDEFKLYRCHTILNCARACP 262
Cdd:pfam13237 9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
137-269 |
7.90e-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: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086808 137 PLPHMFVIKDLVVDMTNFYNQYKSIEPW-LKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYL 215
Cdd:COG0247 22 FLELELGKIKYAFDPDNKLNPGKIGLLNpGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKD 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1901086808 216 GP---AALLhanrwisdsRDEYTKERLEAIDDEFK--LYRCHTILNCARACPKGLNPGK 269
Cdd:COG0247 102 SPrgrINLL---------REVLEGELPLDLSEEVYevLDLCLTCKACETACPSGVDIAD 151
|
|
| |
