|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
183-416 |
4.60e-152 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 432.29 E-value: 4.60e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 183 KKPRLKTFEIYRWKP--GDQPQTQTYEVDLEQCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVS 260
Cdd:PLN00129 39 KPSNLKEFQIYRWNPdnPGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 261 SIDQNESKCCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDlKREAGTAQYLQSVDDRLVLDGLYECILCACCQT 340
Cdd:PLN00129 119 KIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKK-PPEDGQKEHLQSKEDRAKLDGMYECILCACCST 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665392308 341 SCPSYWWNSNKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLKQLL 416
Cdd:PLN00129 198 SCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLL 273
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
189-417 |
2.00e-112 |
|
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: 329.40 E-value: 2.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKP--GDQPQTQTYEVDLEqCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQNE 266
Cdd:COG0479 4 TLKIWRQDPetDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 267 SKCcRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDlkrEAGTAQYLQSVDDRLVLDGLYECILCACCQTSCPSYW 346
Cdd:COG0479 83 DTI-TIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG---PAPDNERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665392308 347 WNSnKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLKQLLV 417
Cdd:COG0479 159 ANP-DFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
192-413 |
1.31e-101 |
|
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: 301.66 E-value: 1.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 192 IYRWKP--GDQPQTQTYEVDLEQCgAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQNESKC 269
Cdd:TIGR00384 1 VLRFNPdvDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 270 CRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDLKREAGTaqYLQSVDDRLVLDGLYECILCACCQTSCPSYWWNS 349
Cdd:TIGR00384 80 MKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGE--FLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665392308 350 NkYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLK 413
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 ... |
189-293 |
7.91e-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: 153.93 E-value: 7.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKP---GDQPQTQTYEVDLEqCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQN 265
Cdd:pfam13085 1 TLRVFRYDPrvdRDEPYYQEYEVPYE-EGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 665392308 266 ESKCCRIYPLPHLYVVRDLVPDMSQFYD 293
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
201-251 |
2.77e-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: 36.60 E-value: 2.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 665392308 201 PQTQTYEVDleqCGAMVLDALIKIKnemdptLTFRRSCREGICGSCAMNIN 251
Cdd:cd00207 7 GSGVEVEVP---EGETLLDAAREAG------IDIPYSCRAGACGTCKVEVV 48
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
183-416 |
4.60e-152 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 432.29 E-value: 4.60e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 183 KKPRLKTFEIYRWKP--GDQPQTQTYEVDLEQCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVS 260
Cdd:PLN00129 39 KPSNLKEFQIYRWNPdnPGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 261 SIDQNESKCCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDlKREAGTAQYLQSVDDRLVLDGLYECILCACCQT 340
Cdd:PLN00129 119 KIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKK-PPEDGQKEHLQSKEDRAKLDGMYECILCACCST 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665392308 341 SCPSYWWNSNKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLKQLL 416
Cdd:PLN00129 198 SCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLL 273
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
189-417 |
3.10e-146 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 415.73 E-value: 3.10e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKP--GDQPQTQTYEVDLEQCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQNE 266
Cdd:PRK05950 1 TFKIYRYNPdvDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 267 SKCCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDlkrEAGTAQYLQSVDDRLVLDGLYECILCACCQTSCPSYW 346
Cdd:PRK05950 81 KGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT---PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665392308 347 WNSNKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLKQLLV 417
Cdd:PRK05950 158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLL 228
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
189-417 |
2.00e-112 |
|
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: 329.40 E-value: 2.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKP--GDQPQTQTYEVDLEqCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQNE 266
Cdd:COG0479 4 TLKIWRQDPetDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 267 SKCcRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDlkrEAGTAQYLQSVDDRLVLDGLYECILCACCQTSCPSYW 346
Cdd:COG0479 83 DTI-TIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG---PAPDNERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665392308 347 WNSnKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLKQLLV 417
Cdd:COG0479 159 ANP-DFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
192-413 |
1.31e-101 |
|
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: 301.66 E-value: 1.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 192 IYRWKP--GDQPQTQTYEVDLEQCgAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQNESKC 269
Cdd:TIGR00384 1 VLRFNPdvDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 270 CRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDLKREAGTaqYLQSVDDRLVLDGLYECILCACCQTSCPSYWWNS 349
Cdd:TIGR00384 80 MKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGE--FLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665392308 350 NkYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLK 413
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
188-417 |
1.03e-91 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 277.22 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 188 KTFEIYRWKPGD--QPQTQTYEVDLEQCGAMVLDALIKIKNEmDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIdQN 265
Cdd:PRK12575 5 RILHIYRYDPDDdaAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNM-QA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 266 ESKCCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDLKREAgtaQYLQSVDDRLVLDGLYECILCACCQTSCPSY 345
Cdd:PRK12575 83 LPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPPER---ERLQTPQEREQLDGLYECILCACCSTACPSY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665392308 346 WWNSNKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLKQLLV 417
Cdd:PRK12575 160 WWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
189-422 |
6.66e-60 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 196.89 E-value: 6.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKPGDQPQTQTYEVDLEQcGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLAC---VSSIDQN 265
Cdd:PRK12576 10 IFKVKRYDPEKGSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACktlVLDVAKK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 266 ESKCCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDlKREAGTAQYLQSVDDRLVLDGLYECILCACCQTSCPSY 345
Cdd:PRK12576 89 YNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAK-EVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACPVV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665392308 346 WWNSNkYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDpwKLYRCHSIMNCTNTCPKHLNPARAIIQLKQlLVGLKKK 422
Cdd:PRK12576 168 AIDPE-FLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS-FTRVYKP 240
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
189-420 |
3.76e-52 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 177.96 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKPGDQPQTQTYEVDLEQcGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQNESK 268
Cdd:PRK12577 4 LFKILRQKQNSAPYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 269 CCR----------IYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQ---RKDLKREagtaqYLQSVDDRLVLDGLYECILC 335
Cdd:PRK12577 83 LSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVStaaRQVPERE-----FLQTPEERSKLDQTGNCILC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 336 ACCQTSCPSYWWNSNkYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDP----WKLYRCHsimNCTNTCPKHLNPARAIIQ 411
Cdd:PRK12577 158 GACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNQGtagvWGCTRCY---YCNSVCPMEVAPLDQITK 233
|
....*....
gi 665392308 412 LKQLLVGLK 420
Cdd:PRK12577 234 IKQEILARK 242
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
189-293 |
7.91e-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: 153.93 E-value: 7.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWKP---GDQPQTQTYEVDLEqCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSIDQN 265
Cdd:pfam13085 1 TLRVFRYDPrvdRDEPYYQEYEVPYE-EGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 665392308 266 ESKCCRIYPLPHLYVVRDLVPDMSQFYD 293
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
186-413 |
6.75e-45 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 156.40 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 186 RLKTFEIYRWKP--GDQPQTQTYEVDLEQCGAmVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSId 263
Cdd:PRK12385 5 KNLKIEVLRYNPevDTEPHSQTYEVPYDETTS-LLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 264 QNESKCCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDLKREAGTaqYLQSVDDRLVLDGLYECILCACCQTSCP 343
Cdd:PRK12385 83 RDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGP--NKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 344 SYWWNSnKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPARAIIQLK 413
Cdd:PRK12385 161 QFGLNP-EFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
187-415 |
2.08e-35 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 136.67 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 187 LKTFEIY--RWKPG-DQPQTQTYEVDLEQcGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVSSID 263
Cdd:PRK06259 1 MKMITITvkRFDPEkDEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 264 QNESkccrIYPLpHLYVVRDLVPDMSQFYDQYRSIQPWLQRKdlKREAGTAQYLQSVDDrlvldgLYECILCACCQTSCP 343
Cdd:PRK06259 80 DGMI----IEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRK--NEKITYPEDIEDIKK------LRGCIECLSCVSTCP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665392308 344 SYwwNSNKYLGPAVLMQAYRWVIDSRDEATEQRLDFLKDpwkLYRCHSIMNCTNTCPKHLN-PARAIIQLKQL 415
Cdd:PRK06259 147 AR--KVSDYPGPTFMRQLARFAFDPRDEGDREKEAFDEG---LYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL 214
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
184-403 |
1.17e-33 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 126.22 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 184 KPRLKTFEIYRWKP---GDQPQTQTYEVDlEQCGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLACVS 260
Cdd:PRK13552 1 MGRTLTFNIFRYNPqdpGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 261 SIDQNESKCCRIYPLPHLYVVRDLVPDMSQFYDQ-YRSIQPWLQRK---DLKReagtaqyLQSVDDRLVLDGLYE---CI 333
Cdd:PRK13552 80 LTSDYPDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDkefDIHR-------LEERMEPEEADEIYEldrCI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665392308 334 LCACCQTSCPSYWWNSNkYLGPAVLMQAYRWVIDSRDEAT-EQRLDFLKDPWKLYRCHSIMNCTNTCPKHL 403
Cdd:PRK13552 153 ECGCCVAACGTKQMRED-FVGAVGLNRIARFELDPRDERTdEDFYELIGNDDGVFGCMSLLGCEDNCPKDL 222
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
189-420 |
4.58e-21 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 92.07 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRwkpGDQP--QTQTYEVDLEQcGAMVLDALIKIKNEMDPTLTFRRSCREGICGSCAMNINGTNTLAC---VSSID 263
Cdd:PRK12386 6 KFRVWR---GDASggELQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCmtrMSTFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 264 QNESkcCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQRKDLKreagTAQY-LQSVDdrlvLDGLYE---CILCACCQ 339
Cdd:PRK12386 82 EDET--VTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDLQ----PGEYrMQQVD----VERSQEfrkCIECFLCQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 340 TSC---PSYWWNSNKYLGPAVLMQAYRWVIDSRDEATeqRLDFLKDPWKLYRCHSIMNCTNTCPKHLNPA-RAIIQLKQL 415
Cdd:PRK12386 152 NVChvvRDHEENKPAFAGPRFLMRIAELEMHPLDTAD--RRAEAQEEHGLGYCNITKCCTEVCPEHIKITdNALIPMKER 229
|
....*
gi 665392308 416 LVGLK 420
Cdd:PRK12386 230 VVDRK 234
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
184-401 |
1.04e-16 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 79.26 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 184 KPRLKTFEIYRWK-PGDQPQTQTYEVDLEQcGAMVLDALIKI-KN-------EMDPtLTFRRSCREGICGSCAMNINGTN 254
Cdd:PRK08640 2 SEKTVRLIIKRQDgPDSKPYWEEFEIPYRP-NMNVISALMEIrRNpvnakgeKTTP-VVWDMNCLEEVCGACSMVINGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 255 TLACVSSIDQNESKcCRIYPLPHLYVVRDLVPDMSQFYDQYRSIQPWLQrKDLKREAGTAQYLqSVDDRLVLDGLYECIL 334
Cdd:PRK08640 80 RQACTALIDQLEQP-IRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIP-IDGTYDLGPGPRM-PEEKRQWAYELSKCMT 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665392308 335 CACCQTSCPSYwwNS-NKYLGPAVLMQAyrwvidsR--------DEATEQRLDFLKDPWKLYRCHSIMNCTNTCPK 401
Cdd:PRK08640 157 CGCCLEACPNV--NEkSDFIGPAAISQV-------RlfnahptgEMHKEERLRALMGDGGIADCGNAQNCVRVCPK 223
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
331-404 |
2.54e-06 |
|
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: 44.76 E-value: 2.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665392308 331 ECILCACCQTSCPSYWWNSNKylgPAVLMQAYRWvidsrdeateQRLDFLKDPWKLYRCHSIMNCTNTCPKHLN 404
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
332-403 |
4.76e-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: 43.84 E-value: 4.76e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665392308 332 CILCACCQTSCPSYwwnsnkylgpavLMQAYRWVIDSRDEATEQRLDFLKDPWK---LYRCHSIMNCTNTCPKHL 403
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRLEALEGLaegLWLCTLCGACTEVCPVGI 64
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
189-258 |
4.97e-05 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 44.44 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 189 TFEIYRWK-PGDQPQTQTYEVD--------LEqcgamVLDALikikNEM------DPtLTFRRSCREGICGSCAMNING- 252
Cdd:PRK07570 4 TLKIWRQKgPDDKGKFETYEVDdispdmsfLE-----MLDVL----NEQliekgeEP-VAFDHDCREGICGMCGLVINGr 73
|
90
....*....|.
gi 665392308 253 -----TNTLAC 258
Cdd:PRK07570 74 phgpdRGTTTC 84
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
328-417 |
2.68e-04 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 39.50 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 328 GLYECILCACCQTSCPSYWWNSnkyLGPAVLMQAYRWviDSRDEateqrldFLKDPwKLYRCHSIMNCTNTCPKHLNPAR 407
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL--GLKEE-------VLKSD-SIWLCVSCYTCTERCPRGIDIAD 67
|
90
....*....|
gi 665392308 408 AIIQLKQLLV 417
Cdd:COG1150 68 VMDALRNLAI 77
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
300-425 |
5.65e-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: 41.99 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392308 300 PWLQRKDLKREAGTAQYLQSVDDRLVLDGLYECILCACCQTSCPSYWWNSNKYLGPAVLMQAYRWVIDSRDEateqrLDF 379
Cdd:COG0247 48 LNPGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELP-----LDL 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 665392308 380 LKDPWK-LYRCHSIMNCTNTCPKHLNPARAIIQLKQLLVglKKKGKP 425
Cdd:COG0247 123 SEEVYEvLDLCLTCKACETACPSGVDIADLIAEARAQLV--ERGGRP 167
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
201-251 |
2.77e-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: 36.60 E-value: 2.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 665392308 201 PQTQTYEVDleqCGAMVLDALIKIKnemdptLTFRRSCREGICGSCAMNIN 251
Cdd:cd00207 7 GSGVEVEVP---EGETLLDAAREAG------IDIPYSCRAGACGTCKVEVV 48
|
|
| |
