|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
1-243 |
3.52e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 467.73 E-value: 3.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 1 AQTAAATAPRIKKFAIYRWDPDKtGDKPHMQTYEIDLNNCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGG 80
Cdd:PLN00129 33 ASSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 81 NTLACTRRIDTNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECIL 160
Cdd:PLN00129 112 NTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 161 CACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKK 240
Cdd:PLN00129 192 CACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQ 271
|
...
3AED_B 241 MMA 243
Cdd:PLN00129 272 LLG 274
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
13-243 |
1.04e-118 |
|
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: 338.26 E-value: 1.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDPDkTGDKPHMQTYEIDLNnCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtN 92
Cdd:COG0479 4 TLKIWRQDPE-TDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 93 LDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEEREKLDGLYECILCACCSTSCPSYW 172
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3AED_B 173 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMA 243
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
16-239 |
8.19e-110 |
|
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: 315.52 E-value: 8.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 16 IYRWDPDkTGDKPHMQTYEIDLNNCgPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLDK 95
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 96 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEEREKLDGLYECILCACCSTSCPSYWWNG 175
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3AED_B 176 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIK 239
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
13-120 |
1.20e-49 |
|
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: 158.55 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDPDKTGDKPHMQTYEIDlNNCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN 92
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
3AED_B 93 LDKVSKIYPLPHMYVIKDLVPDLSNFYA 120
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
44-81 |
3.47e-03 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 35.83 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*...
3AED_B 44 VLDALIKIKneidstLTFRRSCREGICGSCAMNINGGN 81
Cdd:cd00207 20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
1-243 |
3.52e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 467.73 E-value: 3.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 1 AQTAAATAPRIKKFAIYRWDPDKtGDKPHMQTYEIDLNNCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGG 80
Cdd:PLN00129 33 ASSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 81 NTLACTRRIDTNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECIL 160
Cdd:PLN00129 112 NTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 161 CACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKK 240
Cdd:PLN00129 192 CACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQ 271
|
...
3AED_B 241 MMA 243
Cdd:PLN00129 272 LLG 274
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
13-244 |
2.73e-160 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 443.47 E-value: 2.73e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDPDKtGDKPHMQTYEIDLNNCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN 92
Cdd:PRK05950 1 TFKIYRYNPDV-DANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 93 LDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDesQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYW 172
Cdd:PRK05950 80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3AED_B 173 WNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMAT 244
Cdd:PRK05950 158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLE 229
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
13-243 |
1.04e-118 |
|
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: 338.26 E-value: 1.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDPDkTGDKPHMQTYEIDLNnCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtN 92
Cdd:COG0479 4 TLKIWRQDPE-TDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 93 LDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEEREKLDGLYECILCACCSTSCPSYW 172
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3AED_B 173 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMA 243
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
16-239 |
8.19e-110 |
|
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: 315.52 E-value: 8.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 16 IYRWDPDkTGDKPHMQTYEIDLNNCgPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLDK 95
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 96 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEEREKLDGLYECILCACCSTSCPSYWWNG 175
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3AED_B 176 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIK 239
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
16-243 |
1.14e-102 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 298.03 E-value: 1.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 16 IYRWDPDKtGDKPHMQTYEIDLNNCGPMVLDALIKIKNEiDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTnLDK 95
Cdd:PRK12575 9 IYRYDPDD-DAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA-LPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 96 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKkkDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNG 175
Cdd:PRK12575 86 EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI--NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3AED_B 176 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMA 243
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
13-252 |
2.09e-60 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 191.89 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDPDKtgdKPHMQTYEIDLNNcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLAC-TRRID- 90
Cdd:PRK12576 10 IFKVKRYDPEK---GSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACkTLVLDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 91 -TNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCP 169
Cdd:PRK12576 86 aKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 170 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDpfSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMATYKEKK 249
Cdd:PRK12576 166 VVAID-PEFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRSFTRVYKPKS 242
|
...
3AED_B 250 ASA 252
Cdd:PRK12576 243 EVA 245
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
14-251 |
4.14e-58 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 187.59 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 14 FAIYRWDPDKTgdkPHMQTYEIDLNNcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNL 93
Cdd:PRK12577 5 FKILRQKQNSA---PYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 94 DKVSK----------IYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkkdeSQEGKQ----QYLQSIEEREKLDGLYECI 159
Cdd:PRK12577 81 ARLSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYV-----STAARQvperEFLQTPEERSKLDQTGNCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 160 LCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL-QDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEI 238
Cdd:PRK12577 156 LCGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKI 234
|
250
....*....|...
3AED_B 239 KKMMATYKEKKAS 251
Cdd:PRK12577 235 KQEILARKDAQDS 247
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
13-120 |
1.20e-49 |
|
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: 158.55 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDPDKTGDKPHMQTYEIDlNNCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN 92
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
3AED_B 93 LDKVSKIYPLPHMYVIKDLVPDLSNFYA 120
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
10-239 |
2.85e-44 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 149.47 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 10 RIKKFAIYRWDPDKTgDKPHMQTYEIDLNNcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRI 89
Cdd:PRK12385 5 KNLKIEVLRYNPEVD-TEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 90 DTNLDKVsKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEgKQQYLQSIEEREKLDGLYECILCACCSTSCP 169
Cdd:PRK12385 83 RDYTGGM-KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPD-DGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 170 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAIAEIK 239
Cdd:PRK12385 161 QFGLN-PEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
16-249 |
7.32e-41 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 146.30 E-value: 7.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 16 IYRWDPDKtgDKPHMQTYEIDLNNcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLdk 95
Cdd:PRK06259 8 VKRFDPEK--DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 96 vsKIYPLpHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsqegKQQYLQSIEEREKLDGlyeCILCACCSTSCPSYwwNG 175
Cdd:PRK06259 83 --IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNE----KITYPEDIEDIKKLRG---CIECLSCVSTCPAR--KV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3AED_B 176 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQdpfSLYRCHTIMNCTGTCPKGLN-PGKAIAEIKKMmaTYKEKK 249
Cdd:PRK06259 151 SDYPGPTFMRQLARFAFDPRDEGDREKEAFDE---GLYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL--AFKKGL 220
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
10-244 |
1.02e-40 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 140.08 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 10 RIKKFAIYRWDPDKTGDKPHMQTYEIDlNNCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRI 89
Cdd:PRK13552 3 RTLTFNIFRYNPQDPGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 90 DTNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQ-YKSIEPYLKKKDESQEGKqqylqsIEER---EKLDGLYE---CILCA 162
Cdd:PRK13552 82 SDYPDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHR------LEERmepEEADEIYEldrCIECG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 163 CCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL---QDpfSLYRCHTIMNCTGTCPKGLNPGKAIAEIK 239
Cdd:PRK13552 156 CCVAACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFYELignDD--GVFGCMSLLGCEDNCPKDLPLQQQIAYLR 232
|
....*
3AED_B 240 KMMAT 244
Cdd:PRK13552 233 RKMAA 237
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
13-229 |
3.76e-21 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 88.99 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 13 KFAIYRWDpDKTGDkphMQTYEIDLNNcGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT- 91
Cdd:PRK12386 6 KFRVWRGD-ASGGE---LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 92 NLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsQEGKQQYLQsiEEREKLDGLYECILCACCSTSC--- 168
Cdd:PRK12386 81 DEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDL-QPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvv 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3AED_B 169 PSYWWNGDKYLGPAVLMQAYRWMIDSRDdfTEERLAKLQDPFSLYRCHTIMNCTGTCPKGL 229
Cdd:PRK12386 158 RDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
7-238 |
1.33e-15 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 73.87 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 7 TAPRIKKFAIYRWD-PDKtgdKPHMQTYEIDLNNcGPMVLDALIKI-KNEID------STLTFRRSCREGICGSCAMNIN 78
Cdd:PRK08640 1 MSEKTVRLIIKRQDgPDS---KPYWEEFEIPYRP-NMNVISALMEIrRNPVNakgektTPVVWDMNCLEEVCGACSMVIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 79 GGNTLACTRRIDtNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYL--KKKDESQEGKQqylQSIEEREKLDGLY 156
Cdd:PRK08640 77 GKPRQACTALID-QLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIpiDGTYDLGPGPR---MPEEKRQWAYELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 157 ECILCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFT-EERLAKLQDPFSLYRCHTIMNCTGTCPKGLNPGKAI 235
Cdd:PRK08640 153 KCMTCGCCLEACPNVNEKSD-FIGPAAISQVRLFNAHPTGEMHkEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSI 231
|
...
3AED_B 236 AEI 238
Cdd:PRK08640 232 AAM 234
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
157-230 |
1.34e-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: 50.15 E-value: 1.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3AED_B 157 ECILCACCSTSCPSYWWNGDKylgPAVLMQAYRWmidsrddfteERLAKLQDPFSLYRCHTIMNCTGTCPKGLN 230
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
143-244 |
2.83e-06 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 47.76 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 143 LQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIdsRDDFTEERLAKLQDpfSLYRCHTIMNCT 222
Cdd:COG0247 65 LKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVL--EGELPLDLSEEVYE--VLDLCLTCKACE 140
|
90 100
....*....|....*....|..
3AED_B 223 GTCPKGLNPGKAIAEIKKMMAT 244
Cdd:COG0247 141 TACPSGVDIADLIAEARAQLVE 162
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
158-229 |
1.92e-05 |
|
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: 41.53 E-value: 1.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3AED_B 158 CILCACCSTSCPSYwwngdkylgpavLMQAYRWMIDSRD---DFTEERLAKLQDPFSLYRCHTIMNCTGTCPKGL 229
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
154-243 |
3.18e-05 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 41.04 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 154 GLYECILCACCSTSCPSYWWNGdkyLGPAVLMQAYRWmiDSRDDFteerlakLQDPfSLYRCHTIMNCTGTCPKGLNPGK 233
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL--GLKEEV-------LKSD-SIWLCVSCYTCTERCPRGIDIAD 67
|
90
....*....|
3AED_B 234 AIAEIKKMMA 243
Cdd:COG1150 68 VMDALRNLAI 77
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
26-118 |
1.28e-04 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 42.13 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3AED_B 26 DKPHMQTYEID--------------LNncgpmvlDALIKIKNEIdstLTFRRSCREGICGSCAMNING------GNTLAC 85
Cdd:PRK07570 15 DKGKFETYEVDdispdmsflemldvLN-------EQLIEKGEEP---VAFDHDCREGICGMCGLVINGrphgpdRGTTTC 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
3AED_B 86 TRRIDTNLD----KV----SKIYPlphmyVIKDLVPDLSNF 118
Cdd:PRK07570 85 QLHMRSFKDgdtiTIepwrAAAFP-----VIKDLVVDRSAL 120
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
44-81 |
3.47e-03 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 35.83 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*...
3AED_B 44 VLDALIKIKneidstLTFRRSCREGICGSCAMNINGGN 81
Cdd:cd00207 20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
