|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
31-273 |
4.71e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 468.88 E-value: 4.71e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 31 AQTAAAAAPRIKKFAIYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGG 110
Cdd:PLN00129 33 ASSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 111 NTLACTRRIDTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECIL 190
Cdd:PLN00129 112 NTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 191 CACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKK 270
Cdd:PLN00129 192 CACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQ 271
|
...
gi 51701449 271 MMA 273
Cdd:PLN00129 272 LLG 274
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
43-273 |
2.93e-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: 343.27 E-value: 2.93e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDPDkTGDKPRMQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtD 122
Cdd:COG0479 4 TLKIWRQDPE-TDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 123 LSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEDREKLDGLYECILCACCSTSCPSYW 202
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51701449 203 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 273
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
46-269 |
8.08e-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: 316.68 E-value: 8.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 46 IYRWDPDkTGDKPRMQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSK 125
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 126 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEDREKLDGLYECILCACCSTSCPSYWWNG 205
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51701449 206 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIK 269
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 ... |
43-150 |
3.11e-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: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDPDKTGDKPRMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 51701449 123 LSKVSKIYPLPHMYVIKDLVPDLSNFYA 150
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
58-111 |
5.64e-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: 5.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 51701449 58 PRMQTYEVDLNKcGPMVLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 111
Cdd:cd00207 5 VPGSGVEVEVPE-GETLLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
31-273 |
4.71e-169 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 468.88 E-value: 4.71e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 31 AQTAAAAAPRIKKFAIYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGG 110
Cdd:PLN00129 33 ASSKGSKPSNLKEFQIYRWNPDN-PGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 111 NTLACTRRIDTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECIL 190
Cdd:PLN00129 112 NTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 191 CACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKK 270
Cdd:PLN00129 192 CACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQ 271
|
...
gi 51701449 271 MMA 273
Cdd:PLN00129 272 LLG 274
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
43-274 |
2.50e-161 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 447.32 E-value: 2.50e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:PRK05950 1 TFKIYRYNPDV-DANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 123 LSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDesQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYW 202
Cdd:PRK05950 80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51701449 203 WNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMAT 274
Cdd:PRK05950 158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLE 229
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
43-273 |
2.93e-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: 343.27 E-value: 2.93e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDPDkTGDKPRMQTYEVDLNkCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDtD 122
Cdd:COG0479 4 TLKIWRQDPE-TDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 123 LSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGkqQYLQSIEDREKLDGLYECILCACCSTSCPSYW 202
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDN--ERLQSPEDREKADDLAECILCGACVAACPNVW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51701449 203 WNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 273
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
46-269 |
8.08e-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: 316.68 E-value: 8.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 46 IYRWDPDkTGDKPRMQTYEVDLNKCgPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSK 125
Cdd:TIGR00384 1 VLRFNPD-VDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 126 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQyLQSIEDREKLDGLYECILCACCSTSCPSYWWNG 205
Cdd:TIGR00384 79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEF-LQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51701449 206 DkYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIK 269
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
46-273 |
4.18e-101 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 295.33 E-value: 4.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 46 IYRWDPDKtGDKPRMQTYEVDLNKCGPMVLDALIKIKNEvDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTdLSK 125
Cdd:PRK12575 9 IYRYDPDD-DAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA-LPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 126 VSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKkkDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNG 205
Cdd:PRK12575 86 EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI--NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51701449 206 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMA 273
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
43-282 |
5.05e-61 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 194.58 E-value: 5.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDPDKtgdKPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLAC-TRRID- 120
Cdd:PRK12576 10 IFKVKRYDPEK---GSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACkTLVLDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 121 -TDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCP 199
Cdd:PRK12576 86 aKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 200 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDpfSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMATYKEKR 279
Cdd:PRK12576 166 VVAID-PEFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRSFTRVYKPKS 242
|
...
gi 51701449 280 ALA 282
Cdd:PRK12576 243 EVA 245
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
44-277 |
6.73e-57 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 185.67 E-value: 6.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 44 FAIYRWDPDKTgdkPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDL 123
Cdd:PRK12577 5 FKILRQKQNSA---PYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 124 SKVSK----------IYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLkkkdeSQEGKQ----QYLQSIEDREKLDGLYECI 189
Cdd:PRK12577 81 ARLSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYV-----STAARQvperEFLQTPEERSKLDQTGNCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 190 LCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL-QDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEI 268
Cdd:PRK12577 156 LCGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYnQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKI 234
|
....*....
gi 51701449 269 KKMMATYKE 277
Cdd:PRK12577 235 KQEILARKD 243
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
43-150 |
3.11e-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: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDPDKTGDKPRMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTD 122
Cdd:pfam13085 1 TLRVFRYDPRVDRDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79
|
90 100
....*....|....*....|....*...
gi 51701449 123 LSKVSKIYPLPHMYVIKDLVPDLSNFYA 150
Cdd:pfam13085 80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
40-269 |
4.24e-45 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 152.55 E-value: 4.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 40 RIKKFAIYRWDPDKTgDKPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACtRRI 119
Cdd:PRK12385 5 KNLKIEVLRYNPEVD-TEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLAC-KTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 120 DTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEgKQQYLQSIEDREKLDGLYECILCACCSTSCP 199
Cdd:PRK12385 82 LRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPD-DGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 200 SYWWNgDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIK 269
Cdd:PRK12385 161 QFGLN-PEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
40-274 |
3.59e-39 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 137.00 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 40 RIKKFAIYRWDPDKTGDKPRMQTYEVDlNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACtRRI 119
Cdd:PRK13552 3 RTLTFNIFRYNPQDPGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLAC-RTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 120 DTDLSK-VSKIYPLPHMYVIKDLVPDLSNFYAQ-YKSIEPYLKKKDESQEGKqqylqsIEDR---EKLDGLYE---CILC 191
Cdd:PRK13552 81 TSDYPDgVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHR------LEERmepEEADEIYEldrCIEC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 192 ACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFTEERLAKL---QDpfSVYRCHTIMNCTQTCPKGLNPGKAIAEI 268
Cdd:PRK13552 155 GCCVAACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFYELignDD--GVFGCMSLLGCEDNCPKDLPLQQQIAYL 231
|
....*.
gi 51701449 269 KKMMAT 274
Cdd:PRK13552 232 RRKMAA 237
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
46-281 |
4.68e-39 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 142.45 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 46 IYRWDPDKtgDKPRMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLsk 125
Cdd:PRK06259 8 VKRFDPEK--DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 126 vsKIYPLpHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsqegKQQYLQSIEDREKLDGlyeCILCACCSTSCPSYwwNG 205
Cdd:PRK06259 83 --IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNE----KITYPEDIEDIKKLRG---CIECLSCVSTCPAR--KV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51701449 206 DKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQdpfSVYRCHTIMNCTQTCPKGLN-PGKAIAEIKKMmaTYKEKRAL 281
Cdd:PRK06259 151 SDYPGPTFMRQLARFAFDPRDEGDREKEAFDE---GLYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL--AFKKGLGL 222
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
43-259 |
3.45e-22 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 92.45 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 43 KFAIYRWDpDKTGDkprMQTYEVDLNKcGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDT- 121
Cdd:PRK12386 6 KFRVWRGD-ASGGE---LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 122 DLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDEsQEGKQQYLQsiEDREKLDGLYECILCACCSTSC--- 198
Cdd:PRK12386 81 DEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDL-QPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvv 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51701449 199 PSYWWNGDKYLGPAVLMQAYRWMIDSRDdfTEERLAKLQDPFSVYRCHTIMNCTQTCPKGL 259
Cdd:PRK12386 158 RDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
39-268 |
3.27e-16 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 76.18 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 39 PRIKKFAIYRWD-PDKtgdKPRMQTYEVDLNKcGPMVLDALIKI-KNEVD------STLTFRRSCREGICGSCAMNINGG 110
Cdd:PRK08640 3 EKTVRLIIKRQDgPDS---KPYWEEFEIPYRP-NMNVISALMEIrRNPVNakgektTPVVWDMNCLEEVCGACSMVINGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 111 NTLACTRRIDTdLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYL--KKKDESQEGKQqylQSIEDREKLDGLYEC 188
Cdd:PRK08640 79 PRQACTALIDQ-LEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIpiDGTYDLGPGPR---MPEEKRQWAYELSKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 189 ILCACCSTSCPSYWWNGDkYLGPAVLMQAYRWMIDSRDDFT-EERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAE 267
Cdd:PRK08640 155 MTCGCCLEACPNVNEKSD-FIGPAAISQVRLFNAHPTGEMHkEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAA 233
|
.
gi 51701449 268 I 268
Cdd:PRK08640 234 M 234
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
187-260 |
2.23e-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: 2.23e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51701449 187 ECILCACCSTSCPSYWWNGDKylgPAVLMQAYRWmidsrddfteERLAKLQDPFSVYRCHTIMNCTQTCPKGLN 260
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
173-274 |
3.26e-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: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 173 LQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIdsRDDFTEERLAKLQDpfSVYRCHTIMNCT 252
Cdd:COG0247 65 LKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVL--EGELPLDLSEEVYE--VLDLCLTCKACE 140
|
90 100
....*....|....*....|..
gi 51701449 253 QTCPKGLNPGKAIAEIKKMMAT 274
Cdd:COG0247 141 TACPSGVDIADLIAEARAQLVE 162
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
188-259 |
4.70e-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: 4.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51701449 188 CILCACCSTSCPSYwwngdkylgpavLMQAYRWMIDSRD---DFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGL 259
Cdd:pfam13183 2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
56-148 |
8.88e-06 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 45.98 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 56 DKPRMQTYEVDlNKCGPM----VLDALikikNEvdsTLT--------FRRSCREGICGSCAMNING------GNTLACTR 117
Cdd:PRK07570 15 DKGKFETYEVD-DISPDMsfleMLDVL----NE---QLIekgeepvaFDHDCREGICGMCGLVINGrphgpdRGTTTCQL 86
|
90 100 110
....*....|....*....|....*....|....*....
gi 51701449 118 RI----DTDLSKV----SKIYPlphmyVIKDLVPDLSNF 148
Cdd:PRK07570 87 HMrsfkDGDTITIepwrAAAFP-----VIKDLVVDRSAL 120
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
184-273 |
1.59e-05 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 42.19 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51701449 184 GLYECILCACCSTSCPSYWWNGdkyLGPAVLMQAYRWmiDSRDDFteerlakLQDPfSVYRCHTIMNCTQTCPKGLNPGK 263
Cdd:COG1150 1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL--GLKEEV-------LKSD-SIWLCVSCYTCTERCPRGIDIAD 67
|
90
....*....|
gi 51701449 264 AIAEIKKMMA 273
Cdd:COG1150 68 VMDALRNLAI 77
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
188-256 |
2.24e-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: 35.69 E-value: 2.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51701449 188 CILCACCSTSCPSYWWNGDKYlgpavlmqayrwmidsrddftEERLAKLQDPFSVYRCHTIMNCTQTCP 256
Cdd:pfam13237 9 CIGCGRCTAACPAGLTRVGAI---------------------VERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
58-111 |
5.64e-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: 5.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 51701449 58 PRMQTYEVDLNKcGPMVLDALIKIKnevdstLTFRRSCREGICGSCAMNINGGN 111
Cdd:cd00207 5 VPGSGVEVEVPE-GETLLDAAREAG------IDIPYSCRAGACGTCKVEVVEGE 51
|
|
| |
