|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
5-271 |
1.79e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 469.65 E-value: 1.79e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 5 VALSLRRRLPATTLGGACLQASRGAQTAAATA-------PRIKKFAIYRWDPDKaGDKPHMQTYEVDLNKCGPMVLDALI 77
Cdd:PLN00129 2 AAGLLRRLAGAKAGLLAPAAAASAAASAETKAsskgskpSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 78 KIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYL 157
Cdd:PLN00129 81 KIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 158 KKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDP 237
Cdd:PLN00129 161 KTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDE 240
|
250 260 270
....*....|....*....|....*....|....
gi 115387094 238 FSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 271
Cdd:PLN00129 241 FKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
41-271 |
4.09e-119 |
|
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: 340.57 E-value: 4.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDPDKaGDKPHMQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtN 120
Cdd:COG0479 4 TLKIWRQDPET-DSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 121 LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEEREKLDGLYECILCACCSTSCPSYW 200
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115387094 201 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 271
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
44-267 |
3.58e-111 |
|
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: 320.15 E-value: 3.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 44 IYRWDPDkAGDKPHMQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNK 123
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 124 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEEREKLDGLYECILCACCSTSCPSYWWNG 203
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115387094 204 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 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 |
8.65e-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: 157.40 E-value: 8.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDPDKAGDKPHMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN 120
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 115387094 121 LNKVSKIYPLPHMYVIKDLVPDLSNFYA 148
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
56-109 |
3.26e-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: 3.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 115387094 56 PHMQTYEVDLNKcGPMVLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 109
Cdd:cd00207 5 VPGSGVEVEVPE-GETLLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
5-271 |
1.79e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 469.65 E-value: 1.79e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 5 VALSLRRRLPATTLGGACLQASRGAQTAAATA-------PRIKKFAIYRWDPDKaGDKPHMQTYEVDLNKCGPMVLDALI 77
Cdd:PLN00129 2 AAGLLRRLAGAKAGLLAPAAAASAAASAETKAsskgskpSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 78 KIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYL 157
Cdd:PLN00129 81 KIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 158 KKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDP 237
Cdd:PLN00129 161 KTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDE 240
|
250 260 270
....*....|....*....|....*....|....
gi 115387094 238 FSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 271
Cdd:PLN00129 241 FKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
41-272 |
6.76e-161 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 446.16 E-value: 6.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDPDKaGDKPHMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN 120
Cdd:PRK05950 1 TFKIYRYNPDV-DANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 121 LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDesQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYW 200
Cdd:PRK05950 80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115387094 201 WNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMAT 272
Cdd:PRK05950 158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLE 229
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
41-271 |
4.09e-119 |
|
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: 340.57 E-value: 4.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDPDKaGDKPHMQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtN 120
Cdd:COG0479 4 TLKIWRQDPET-DSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 121 LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEEREKLDGLYECILCACCSTSCPSYW 200
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115387094 201 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 271
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
44-267 |
3.58e-111 |
|
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: 320.15 E-value: 3.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 44 IYRWDPDkAGDKPHMQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNK 123
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 124 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEEREKLDGLYECILCACCSTSCPSYWWNG 203
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115387094 204 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 267
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
44-271 |
1.64e-101 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 296.10 E-value: 1.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 44 IYRWDPDKaGDKPHMQTYEVDLNKCGPMVLDALIKIKNEvDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTnLNK 123
Cdd:PRK12575 9 IYRYDPDD-DAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA-LPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 124 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKkkDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNG 203
Cdd:PRK12575 86 EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI--NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115387094 204 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMA 271
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
41-276 |
1.31e-61 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 196.12 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDPDKagdKPHMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLAC-TRRID- 118
Cdd:PRK12576 10 IFKVKRYDPEK---GSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACkTLVLDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 119 -TNLNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCP 197
Cdd:PRK12576 86 aKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115387094 198 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDpfSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEK 276
Cdd:PRK12576 166 VVAID-PEFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRSFTRVYKPK 241
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
42-279 |
3.17e-57 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 186.44 E-value: 3.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 42 FAIYRWDPDKAgdkPHMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNL 121
Cdd:PRK12577 5 FKILRQKQNSA---PYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 122 NKVSK----------IYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkkdeSQEGKQ----QYLQSIEEREKLDGLYECI 187
Cdd:PRK12577 81 ARLSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYV-----STAARQvperEFLQTPEERSKLDQTGNCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 188 LCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL-QDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEI 266
Cdd:PRK12577 156 LCGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKI 234
|
250
....*....|...
gi 115387094 267 KKMMATYKEKKAS 279
Cdd:PRK12577 235 KQEILARKDAQDS 247
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
41-148 |
8.65e-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: 157.40 E-value: 8.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDPDKAGDKPHMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN 120
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 115387094 121 LNKVSKIYPLPHMYVIKDLVPDLSNFYA 148
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
38-267 |
8.65e-45 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 151.78 E-value: 8.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 38 RIKKFAIYRWDPDKaGDKPHMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRI 117
Cdd:PRK12385 5 KNLKIEVLRYNPEV-DTEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 118 DTNLNKVsKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEgKQQYLQSIEEREKLDGLYECILCACCSTSCP 197
Cdd:PRK12385 83 RDYTGGM-KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPD-DGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 198 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 267
Cdd:PRK12385 161 QFGLN-PEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
44-277 |
7.73e-41 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 147.08 E-value: 7.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 44 IYRWDPDKagDKPHMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLnk 123
Cdd:PRK06259 8 VKRFDPEK--DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 124 vsKIYPLpHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsqegKQQYLQSIEEREKLDGlyeCILCACCSTSCPSYwwNG 203
Cdd:PRK06259 83 --IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNE----KITYPEDIEDIKKLRG---CIECLSCVSTCPAR--KV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115387094 204 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQdpfSLYRCHTIMNCTRTCPKGLN-PGKAIAEIKKMmaTYKEKK 277
Cdd:PRK06259 151 SDYPGPTFMRQLARFAFDPRDEGDREKEAFDE---GLYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL--AFKKGL 220
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
38-272 |
3.76e-40 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 139.31 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 38 RIKKFAIYRWDPDKAGDKPHMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRI 117
Cdd:PRK13552 3 RTLTFNIFRYNPQDPGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 118 DTNLNKVSKIYPLPHMYVIKDLVPDLSNFYAQ-YKSIEPYLKKKDESQEGKqqylqsIEER---EKLDGLYE---CILCA 190
Cdd:PRK13552 82 SDYPDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHR------LEERmepEEADEIYEldrCIECG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 191 CCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL---QDpfSLYRCHTIMNCTRTCPKGLNPGKAIAEIK 267
Cdd:PRK13552 156 CCVAACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFYELignDD--GVFGCMSLLGCEDNCPKDLPLQQQIAYLR 232
|
....*
gi 115387094 268 KMMAT 272
Cdd:PRK13552 233 RKMAA 237
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
41-257 |
2.92e-21 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 89.76 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 41 KFAIYRWDpDKAGDkphMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT- 119
Cdd:PRK12386 6 KFRVWRGD-ASGGE---LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 120 NLNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsQEGKQQYLQsiEEREKLDGLYECILCACCSTSC--- 196
Cdd:PRK12386 81 DEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDL-QPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvv 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115387094 197 PSYWWNGDKYLGPAVLMQAYRWMIDSRDdfTEERLAKLQDPFSLYRCHTIMNCTRTCPKGL 257
Cdd:PRK12386 158 RDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
35-266 |
3.58e-17 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 78.88 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 35 TAPRIKKFAIYRWD-PDKagdKPHMQTYEVDLNKcGPMVLDALIKI-KNEVD------STLTFRRSCREGICGSCAMNIN 106
Cdd:PRK08640 1 MSEKTVRLIIKRQDgPDS---KPYWEEFEIPYRP-NMNVISALMEIrRNPVNakgektTPVVWDMNCLEEVCGACSMVIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 107 GGNTLACTRRIDtNLNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYL--KKKDESQEGKQqylQSIEEREKLDGLY 184
Cdd:PRK08640 77 GKPRQACTALID-QLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIpiDGTYDLGPGPR---MPEEKRQWAYELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 185 ECILCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFT-EERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAI 263
Cdd:PRK08640 153 KCMTCGCCLEACPNVNEKSD-FIGPAAISQVRLFNAHPTGEMHkEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSI 231
|
...
gi 115387094 264 AEI 266
Cdd:PRK08640 232 AAM 234
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
185-258 |
6.18e-09 |
|
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: 51.31 E-value: 6.18e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115387094 185 ECILCACCSTSCPSYWWNGDKylgPAVLMQAYRWmidsrddfteERLAKLQDPFSLYRCHTIMNCTRTCPKGLN 258
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
171-272 |
2.62e-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: 48.15 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 171 LQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIdsRDDFTEERLAKLQDpfSLYRCHTIMNCT 250
Cdd:COG0247 65 LKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVL--EGELPLDLSEEVYE--VLDLCLTCKACE 140
|
90 100
....*....|....*....|..
gi 115387094 251 RTCPKGLNPGKAIAEIKKMMAT 272
Cdd:COG0247 141 TACPSGVDIADLIAEARAQLVE 162
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
186-257 |
5.04e-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: 43.45 E-value: 5.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115387094 186 CILCACCSTSCPSYwwngdkylgpavLMQAYRWMIDSRD---DFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGL 257
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
182-271 |
1.76e-05 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 42.19 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 182 GLYECILCACCSTSCPSYWWNGdkyLGPAVLMQAYRWmiDSRDDFteerlakLQDPfSLYRCHTIMNCTRTCPKGLNPGK 261
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL--GLKEEV-------LKSD-SIWLCVSCYTCTERCPRGIDIAD 67
|
90
....*....|
gi 115387094 262 AIAEIKKMMA 271
Cdd:COG1150 68 VMDALRNLAI 77
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
47-146 |
4.26e-05 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 43.67 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115387094 47 WDPDKAGDKPHMQTYEVDlNKCGPM----VLDALikikNEvdsTLT--------FRRSCREGICGSCAMNING------G 108
Cdd:PRK07570 8 WRQKGPDDKGKFETYEVD-DISPDMsfleMLDVL----NE---QLIekgeepvaFDHDCREGICGMCGLVINGrphgpdR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 115387094 109 NTLACTRRI----DTNLNKV----SKIYPlphmyVIKDLVPDLSNF 146
Cdd:PRK07570 80 GTTTCQLHMrsfkDGDTITIepwrAAAFP-----VIKDLVVDRSAL 120
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
56-109 |
3.26e-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: 3.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 115387094 56 PHMQTYEVDLNKcGPMVLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 109
Cdd:cd00207 5 VPGSGVEVEVPE-GETLLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
186-254 |
5.63e-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: 34.53 E-value: 5.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115387094 186 CILCACCSTSCPSYWWNGDKYlgpavlmqayrwmidsrddftEERLAKLQDPFSLYRCHTIMNCTRTCP 254
Cdd:pfam13237 9 CIGCGRCTAACPAGLTRVGAI---------------------VERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| |
