|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
1-271 |
7.36e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 468.11 E-value: 7.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 1 MAATV---GVSLKRG-FPAAVLGRVGLQACRGAQTAAAAAPRIKKFAIYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDAL 76
Cdd:PLN00129 1 MAAGLlrrLAGAKAGlLAPAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 77 IKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPY 156
Cdd:PLN00129 80 IKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 157 LKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQD 236
Cdd:PLN00129 160 LKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDD 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1243457570 237 PFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 271
Cdd:PLN00129 240 EFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
41-271 |
3.85e-120 |
|
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: 342.88 E-value: 3.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDPDkTGDKPRMQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtD 120
Cdd:COG0479 4 TLKIWRQDPE-TDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 121 LSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEDREKLDGLYECILCACCSTSCPSYW 200
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243457570 201 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 271
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
44-267 |
1.12e-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: 316.29 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 44 IYRWDPDkTGDKPRMQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSK 123
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 124 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEDREKLDGLYECILCACCSTSCPSYWWNG 203
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457570 204 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIK 267
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 ... |
41-148 |
3.22e-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: 158.17 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDPDKTGDKPRMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 120
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 1243457570 121 LSKVSKIYPLPHMYVIKDLVPDLSNFYA 148
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
72-109 |
6.41e-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: 35.06 E-value: 6.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1243457570 72 VLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 109
Cdd:cd00207 20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
1-271 |
7.36e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 468.11 E-value: 7.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 1 MAATV---GVSLKRG-FPAAVLGRVGLQACRGAQTAAAAAPRIKKFAIYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDAL 76
Cdd:PLN00129 1 MAAGLlrrLAGAKAGlLAPAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 77 IKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPY 156
Cdd:PLN00129 80 IKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 157 LKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQD 236
Cdd:PLN00129 160 LKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDD 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1243457570 237 PFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 271
Cdd:PLN00129 240 EFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
41-272 |
3.95e-161 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 446.93 E-value: 3.95e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 120
Cdd:PRK05950 1 TFKIYRYNPDV-DANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 121 LSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDesQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYW 200
Cdd:PRK05950 80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243457570 201 WNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMAT 272
Cdd:PRK05950 158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLE 229
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
41-271 |
3.85e-120 |
|
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: 342.88 E-value: 3.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDPDkTGDKPRMQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtD 120
Cdd:COG0479 4 TLKIWRQDPE-TDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 121 LSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEDREKLDGLYECILCACCSTSCPSYW 200
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243457570 201 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 271
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
44-267 |
1.12e-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: 316.29 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 44 IYRWDPDkTGDKPRMQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSK 123
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 124 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEDREKLDGLYECILCACCSTSCPSYWWNG 203
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457570 204 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIK 267
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
44-271 |
5.56e-101 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 294.94 E-value: 5.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 44 IYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDALIKIKNEvDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTdLSK 123
Cdd:PRK12575 9 IYRYDPDD-DAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA-LPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 124 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKkkDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNG 203
Cdd:PRK12575 86 EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI--NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243457570 204 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 271
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
41-280 |
6.40e-61 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 194.20 E-value: 6.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDPDKtgdKPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLAC-TRRID- 118
Cdd:PRK12576 10 IFKVKRYDPEK---GSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACkTLVLDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 119 -TDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCP 197
Cdd:PRK12576 86 aKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 198 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDpfSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMATYKEKR 277
Cdd:PRK12576 166 VVAID-PEFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRSFTRVYKPKS 242
|
...
gi 1243457570 278 ALA 280
Cdd:PRK12576 243 EVA 245
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
42-275 |
6.24e-57 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 185.67 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 42 FAIYRWDPDKTgdkPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDL 121
Cdd:PRK12577 5 FKILRQKQNSA---PYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 122 SKVSK----------IYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkkdeSQEGKQ----QYLQSIEDREKLDGLYECI 187
Cdd:PRK12577 81 ARLSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYV-----STAARQvperEFLQTPEERSKLDQTGNCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 188 LCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL-QDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEI 266
Cdd:PRK12577 156 LCGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKI 234
|
....*....
gi 1243457570 267 KKMMATYKE 275
Cdd:PRK12577 235 KQEILARKD 243
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
41-148 |
3.22e-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: 158.17 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDPDKTGDKPRMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 120
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 1243457570 121 LSKVSKIYPLPHMYVIKDLVPDLSNFYA 148
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
38-267 |
4.04e-45 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 152.55 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 38 RIKKFAIYRWDPDKTgDKPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACtRRI 117
Cdd:PRK12385 5 KNLKIEVLRYNPEVD-TEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLAC-KTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 118 DTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEgKQQYLQSIEDREKLDGLYECILCACCSTSCP 197
Cdd:PRK12385 82 LRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPD-DGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 198 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIK 267
Cdd:PRK12385 161 QFGLN-PEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
38-272 |
3.43e-39 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 137.00 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 38 RIKKFAIYRWDPDKTGDKPRMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACtRRI 117
Cdd:PRK13552 3 RTLTFNIFRYNPQDPGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLAC-RTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 118 DTDLSK-VSKIYPLPHMYVIKDLVPDLSNFYAQ-YKSIEPYLKKKDESQEGKqqylqsIEDR---EKLDGLYE---CILC 189
Cdd:PRK13552 81 TSDYPDgVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHR------LEERmepEEADEIYEldrCIEC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 190 ACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL---QDpfSVYRCHTIMNCTQTCPKGLNPGKAIAEI 266
Cdd:PRK13552 155 GCCVAACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFYELignDD--GVFGCMSLLGCEDNCPKDLPLQQQIAYL 231
|
....*.
gi 1243457570 267 KKMMAT 272
Cdd:PRK13552 232 RRKMAA 237
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
44-279 |
5.48e-39 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 142.07 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 44 IYRWDPDKtgDKPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLsk 123
Cdd:PRK06259 8 VKRFDPEK--DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 124 vsKIYPLpHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsqegKQQYLQSIEDREKLDGlyeCILCACCSTSCPSYwwNG 203
Cdd:PRK06259 83 --IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNE----KITYPEDIEDIKKLRG---CIECLSCVSTCPAR--KV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243457570 204 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQdpfSVYRCHTIMNCTQTCPKGLN-PGKAIAEIKKMmaTYKEKRAL 279
Cdd:PRK06259 151 SDYPGPTFMRQLARFAFDPRDEGDREKEAFDE---GLYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL--AFKKGLGL 222
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
41-257 |
3.75e-22 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 92.45 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 41 KFAIYRWDpDKTGDkprMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT- 119
Cdd:PRK12386 6 KFRVWRGD-ASGGE---LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 120 DLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsQEGKQQYLQsiEDREKLDGLYECILCACCSTSC--- 196
Cdd:PRK12386 81 DEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDL-QPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvv 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243457570 197 PSYWWNGDKYLGPAVLMQAYRWMIDSRDdfTEERLAKLQDPFSVYRCHTIMNCTQTCPKGL 257
Cdd:PRK12386 158 RDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
37-266 |
3.24e-16 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 76.18 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 37 PRIKKFAIYRWD-PDKtgdKPRMQTYEVDLNKcGPMVLDALIKI-KNEVD------STLTFRRSCREGICGSCAMNINGG 108
Cdd:PRK08640 3 EKTVRLIIKRQDgPDS---KPYWEEFEIPYRP-NMNVISALMEIrRNPVNakgektTPVVWDMNCLEEVCGACSMVINGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 109 NTLACTRRIDTdLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYL--KKKDESQEGKQqylQSIEDREKLDGLYEC 186
Cdd:PRK08640 79 PRQACTALIDQ-LEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIpiDGTYDLGPGPR---MPEEKRQWAYELSKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 187 ILCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFT-EERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAE 265
Cdd:PRK08640 155 MTCGCCLEACPNVNEKSD-FIGPAAISQVRLFNAHPTGEMHkEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAA 233
|
.
gi 1243457570 266 I 266
Cdd:PRK08640 234 M 234
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
185-258 |
2.42e-08 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 49.77 E-value: 2.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457570 185 ECILCACCSTSCPSYWWNGDKylgPAVLMQAYRWmidsrddfteERLAKLQDPFSVYRCHTIMNCTQTCPKGLN 258
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
171-272 |
3.32e-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: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 171 LQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIdsRDDFTEERLAKLQDpfSVYRCHTIMNCT 250
Cdd:COG0247 65 LKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVL--EGELPLDLSEEVYE--VLDLCLTCKACE 140
|
90 100
....*....|....*....|..
gi 1243457570 251 QTCPKGLNPGKAIAEIKKMMAT 272
Cdd:COG0247 141 TACPSGVDIADLIAEARAQLVE 162
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
186-257 |
5.29e-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: 43.07 E-value: 5.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243457570 186 CILCACCSTSCPSYwwngdkylgpavLMQAYRWMIDSRD---DFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGL 257
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
54-146 |
9.42e-06 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 45.98 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 54 DKPRMQTYEVDlNKCGPM----VLDALikikNEvdsTLT--------FRRSCREGICGSCAMNING------GNTLACTR 115
Cdd:PRK07570 15 DKGKFETYEVD-DISPDMsfleMLDVL----NE---QLIekgeepvaFDHDCREGICGMCGLVINGrphgpdRGTTTCQL 86
|
90 100 110
....*....|....*....|....*....|....*....
gi 1243457570 116 RI----DTDLSKV----SKIYPlphmyVIKDLVPDLSNF 146
Cdd:PRK07570 87 HMrsfkDGDTITIepwrAAAFP-----VIKDLVVDRSAL 120
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
182-271 |
1.79e-05 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 42.19 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457570 182 GLYECILCACCSTSCPSYWWNGdkyLGPAVLMQAYRWmiDSRDDFteerlakLQDPfSVYRCHTIMNCTQTCPKGLNPGK 261
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL--GLKEEV-------LKSD-SIWLCVSCYTCTERCPRGIDIAD 67
|
90
....*....|
gi 1243457570 262 AIAEIKKMMA 271
Cdd:COG1150 68 VMDALRNLAI 77
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
186-254 |
2.48e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 35.30 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243457570 186 CILCACCSTSCPSYWWNGDKYlgpavlmqayrwmidsrddftEERLAKLQDPFSVYRCHTIMNCTQTCP 254
Cdd:pfam13237 9 CIGCGRCTAACPAGLTRVGAI---------------------VERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
72-109 |
6.41e-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: 35.06 E-value: 6.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1243457570 72 VLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 109
Cdd:cd00207 20 LLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
