|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-243 |
0e+00 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 551.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 1 MSATRIQSVEILRYDPAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKS 80
Cdd:PRK12385 1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 81 FLRDYPNGVKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACP 160
Cdd:PRK12385 81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 161 QFGLNPEFIGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGKVESSKDFVIAM 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240
|
...
gi 769951462 241 IKP 243
Cdd:PRK12385 241 LKP 243
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
11-229 |
7.61e-130 |
|
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: 365.99 E-value: 7.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 11 ILRYDPAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPN-GV 89
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQpVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 90 KIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384 81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 170 GPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
9-235 |
1.92e-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: 342.50 E-value: 1.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 9 VEILRYDPAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPNG 88
Cdd:COG0479 5 LKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLKDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 89 VKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIgNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFGLNPEF 168
Cdd:COG0479 85 ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLS-PDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWANPDF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 769951462 169 IGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGKVESSKD 235
Cdd:COG0479 164 LGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
9-112 |
2.74e-45 |
|
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: 147.00 E-value: 2.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 9 VEILRYDPAKDA-EPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPN 87
Cdd:pfam13085 2 LRVFRYDPRVDRdEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLG 81
|
90 100
....*....|....*....|....*.
gi 769951462 88 G-VKIEPLANFAIEKDLIVDMTPFIE 112
Cdd:pfam13085 82 QdITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
21-92 |
2.04e-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: 36.22 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 21 EPYLEKFEVPFNETMSVLDALgyikdnLDKDLSYRWSCRMAICGSCGMMVN------------------GVPKLACKSFL 82
Cdd:cd00207 4 NVPGSGVEVEVPEGETLLDAA------REAGIDIPYSCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQTRV 77
|
90
....*....|
gi 769951462 83 RDypnGVKIE 92
Cdd:cd00207 78 TD---GLVIE 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-243 |
0e+00 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 551.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 1 MSATRIQSVEILRYDPAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKS 80
Cdd:PRK12385 1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 81 FLRDYPNGVKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACP 160
Cdd:PRK12385 81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 161 QFGLNPEFIGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGKVESSKDFVIAM 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240
|
...
gi 769951462 241 IKP 243
Cdd:PRK12385 241 LKP 243
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
11-229 |
7.61e-130 |
|
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: 365.99 E-value: 7.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 11 ILRYDPAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPN-GV 89
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQpVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 90 KIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384 81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 170 GPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
9-235 |
1.92e-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: 342.50 E-value: 1.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 9 VEILRYDPAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPNG 88
Cdd:COG0479 5 LKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLKDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 89 VKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIgNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFGLNPEF 168
Cdd:COG0479 85 ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLS-PDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWANPDF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 769951462 169 IGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGKVESSKD 235
Cdd:COG0479 164 LGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
9-244 |
1.82e-94 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 276.67 E-value: 1.82e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 9 VEILRYDPAKDAEPYLEKFEVPFNE-TMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPN 87
Cdd:PRK05950 2 FKIYRYNPDVDANPRMQTYEVDVDEcGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 88 G-VKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIgNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFGLNP 166
Cdd:PRK05950 82 GkIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLI-NDTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWNP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 769951462 167 E-FIGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAvnqgkvesskdfvIAMIKPM 244
Cdd:PRK05950 161 DkFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKA-------------IGEIKRM 226
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
9-225 |
1.51e-78 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 238.11 E-value: 1.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 9 VEILRYDPAKDAepYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFL----RD 84
Cdd:PRK12576 11 FKVKRYDPEKGS--WWQEYKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVldvaKK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 85 YPNGVKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPE-DGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFG 163
Cdd:PRK12576 89 YNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEgKAEHRLKPEDQKELWKFAQCIWCGLCVSACPVVA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769951462 164 LNPEFIGPAALTLAHRYNLDSRDNGQHERMELIngENGAWGCTFVGYCSEVCPKHVDPAAAV 225
Cdd:PRK12576 169 IDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAI 228
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
11-231 |
5.41e-62 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 197.22 E-value: 5.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 11 ILRYDPakDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKS--------FL 82
Cdd:PRK12577 7 ILRQKQ--NSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKEnvgselarLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 83 RDYPNG---VKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAAC 159
Cdd:PRK12577 85 DSNSGAipeITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCILCGACYSEC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 769951462 160 PQFGLNPEFIGPAALTLAHRYNLDSRDNGQHERMELIN-GENGAWGCTFVGYCSEVCPKHVDPAAAVNQGKVE 231
Cdd:PRK12577 165 NAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQE 237
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
3-229 |
1.10e-58 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 187.30 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 3 ATRIQSVEILRYDPAKDAEPYLEKFEVPFNET--MsVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLAC-K 79
Cdd:PLN00129 40 PSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCgpM-VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLAClT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 80 SFLRDYPNGVKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTN-LQTPEQMAKYKQFAGCINCGLCYAA 158
Cdd:PLN00129 119 KIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEhLQSKEDRAKLDGMYECILCACCSTS 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769951462 159 CPQFGLNPE-FIGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQGK 229
Cdd:PLN00129 199 CPSYWWNPEkFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-227 |
3.63e-58 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 184.39 E-value: 3.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 1 MSATRIqsVEILRYDPAKDAEPYLEKFEV-PFNETMSVLDALGYIKdNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACK 79
Cdd:PRK12575 1 MADTRI--LHIYRYDPDDDAAPRMQRYEIaPRAEDRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 80 SFLRDYPNGVKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIIgNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAAC 159
Cdd:PRK12575 78 TNMQALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI-NDTVPPERERLQTPQEREQLDGLYECILCACCSTAC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 769951462 160 PQFGLNPE-FIGPAALTLAHRYNLDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHVDPAAAVNQ 227
Cdd:PRK12575 157 PSYWWNPDkFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQ 225
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
8-225 |
1.72e-57 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 189.83 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 8 SVEILRYDPAKDaEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDypn 87
Cdd:PRK06259 5 TITVKRFDPEKD-EPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVED--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 88 GVKIEPLaNFAIEKDLIVDMTPFIERLEAIKPYIIGNDRTPedgtnlQTPEQMAKYKQFAGCINCGLCYAACPQFGLNpE 167
Cdd:PRK06259 81 GMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKI------TYPEDIEDIKKLRGCIECLSCVSTCPARKVS-D 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 769951462 168 FIGPAALTLAHRYNLDSRDNGQHERMELingENGAWGCTFVGYCSEVCPKHVD-PAAAV 225
Cdd:PRK06259 153 YPGPTFMRQLARFAFDPRDEGDREKEAF---DEGLYNCTTCGKCVEVCPKEIDiPGKAI 208
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
5-218 |
4.54e-48 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 158.57 E-value: 4.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 5 RIQSVEILRYDP-AKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLR 83
Cdd:PRK13552 3 RTLTFNIFRYNPqDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 84 DYPNGV-KIEPLANFAIEKDLIVD----MTPFIERLEAikpyIIGNDRTPeDGTNLQT---PEQMAKYKQFAGCINCGLC 155
Cdd:PRK13552 83 DYPDGViTLMPLPVFKLIGDLSVNtgkwFREMSERVES----WIHTDKEF-DIHRLEErmePEEADEIYELDRCIECGCC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 769951462 156 YAACPQFGLNPEFIGPAALTLAHRYNLDSRDNGQHERM-ELINGENGAWGC-TFVGyCSEVCPKH 218
Cdd:PRK13552 158 VAACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCmSLLG-CEDNCPKD 221
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
9-112 |
2.74e-45 |
|
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: 147.00 E-value: 2.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 9 VEILRYDPAKDA-EPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKSFLRDYPN 87
Cdd:pfam13085 2 LRVFRYDPRVDRdEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLLG 81
|
90 100
....*....|....*....|....*.
gi 769951462 88 G-VKIEPLANFAIEKDLIVDMTPFIE 112
Cdd:pfam13085 82 QdITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
11-217 |
9.93e-36 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 127.03 E-value: 9.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 11 ILRYDpAKDAEPYLEKFEVPFNETMSVLDALGYIKDNLDKDLSYR-----W--SCRMAICGSCGMMVNGVPKLACKSFLR 83
Cdd:PRK08640 10 IKRQD-GPDSKPYWEEFEIPYRPNMNVISALMEIRRNPVNAKGEKttpvvWdmNCLEEVCGACSMVINGKPRQACTALID 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 84 DYPNGVKIEPLANFAIEKDLIVDMTPFIERLEAIKPYIigndrtPEDGTNLQTP-EQMAKYKQ-----FAGCINCGLCYA 157
Cdd:PRK08640 89 QLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWI------PIDGTYDLGPgPRMPEEKRqwayeLSKCMTCGCCLE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 769951462 158 ACPQFGLNPEFIGPAALTLAHRYNLD-SRDNGQHERMELINGENGAWGCTFVGYCSEVCPK 217
Cdd:PRK08640 163 ACPNVNEKSDFIGPAAISQVRLFNAHpTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPK 223
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
24-219 |
4.87e-25 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 99.00 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 24 LEKFEVPFNETMSVLDALGYIKDNLDKDLSYRWSCRMAICGSCGMMVNGVPKLACKS----FLRDYPngVKIEPLANFAI 99
Cdd:PRK12386 19 LQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTrmstFDEDET--VTVTPMRTFPV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 100 EKDLIVDMTPFIERLEAIKPYIIGNDRTPEDGTNLQtpEQMAKYKQFAGCINCGLCYAAC----PQFGLNPEFIGP---- 171
Cdd:PRK12386 97 IRDLVTDVSFNYEKAREIPSFTPPKDLQPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvvrDHEENKPAFAGPrflm 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 769951462 172 --AALTLahrYNLDSRDngqheRMELINGENGAWGCTFVGYCSEVCPKHV 219
Cdd:PRK12386 175 riAELEM---HPLDTAD-----RRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
32-217 |
4.50e-21 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 88.35 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 32 NETMSVLDALgyikDNLDKDL--------SYRWSCRMAICGSCGMMVNGVP------KLACKSFLRDYPNG--VKIEPL- 94
Cdd:PRK07570 28 SPDMSFLEML----DVLNEQLiekgeepvAFDHDCREGICGMCGLVINGRPhgpdrgTTTCQLHMRSFKDGdtITIEPWr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 95 -ANFAIEKDLIVDMTPFiERLEAIKPYIIGNDRTPEDGTNLQTPEQMAKYK-QFAGCINCGLCYAACPQfglnpefiGPA 172
Cdd:PRK07570 104 aAAFPVIKDLVVDRSAL-DRIIQAGGYVSVNTGGAPDANAIPVPKEDADRAfDAAACIGCGACVAACPN--------GSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 769951462 173 AL----TLAHrynLDSRDNGQHER----------MElingENGAWGCTFVGYCSEVCPK 217
Cdd:PRK07570 175 MLftgaKVSH---LALLPQGQPERarrvramvaqMD----EEGFGNCTNTGECEAVCPK 226
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
141-216 |
1.07e-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: 404174 [Multi-domain] Cd Length: 56 Bit Score: 44.55 E-value: 1.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 769951462 141 AKYKQFAGCINCGLCYAACPQFGlnpefigpaaltlahrynldSRDNGQHERMELINGENGAWGCTFVGYCSEVCP 216
Cdd:pfam13237 1 KVVIDPDKCIGCGRCTAACPAGL--------------------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
149-219 |
1.97e-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: 44.22 E-value: 1.97e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769951462 149 CINCGLCYAACPQF-GLNPEFIGPAAltlahrynlDSRDNGQHERMELINGENGAWGCTFVGYCSEVCPKHV 219
Cdd:pfam13183 2 CIRCGACLAACPVYlVTGGRFPGDPR---------GGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
149-220 |
4.60e-05 |
|
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: 40.14 E-value: 4.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769951462 149 CINCGLCYAACPQFGLNPEFigPAALtlahRYNLDSRDNGQHERMELINgengawGCTFVGYCSEVCPKHVD 220
Cdd:pfam13534 2 CIQCGCCVDECPRYLLNGDE--PKKL----MRAAYLGDLEELQANKVAN------LCSECGLCEYACPMGLD 61
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
119-229 |
1.08e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 39.68 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 119 PYIIGNDRTPEDGTNLQTPEQMAKYKQFAGCINCGLCYAACPQFGLNPEFIGPA---ALTLAHRYNLDSRDNGQHERMEL 195
Cdd:COG0247 50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPrgrINLLREVLEGELPLDLSEEVYEV 129
|
90 100 110
....*....|....*....|....*....|....
gi 769951462 196 IngengaWGCTFVGYCSEVCPKHVDPAAAVNQGK 229
Cdd:COG0247 130 L------DLCLTCKACETACPSGVDIADLIAEAR 157
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
21-92 |
2.04e-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: 36.22 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 21 EPYLEKFEVPFNETMSVLDALgyikdnLDKDLSYRWSCRMAICGSCGMMVN------------------GVPKLACKSFL 82
Cdd:cd00207 4 NVPGSGVEVEVPEGETLLDAA------REAGIDIPYSCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQTRV 77
|
90
....*....|
gi 769951462 83 RDypnGVKIE 92
Cdd:cd00207 78 TD---GLVIE 84
|
|
| RnfC |
COG4656 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ... |
131-231 |
2.29e-03 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 443694 [Multi-domain] Cd Length: 451 Bit Score: 38.58 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 131 GTN---LQTPEQMAKYKQFAgCINCGLCYAACPQfGLNPEFIGPAALtlahrynldsrdNGQHERMELINGENgawgCTF 207
Cdd:COG4656 346 GTNgilALTKEEVPPPEEQP-CIRCGRCVDACPM-GLLPQQLYWYAR------------AGDFDKAEEYNLMD----CIE 407
|
90 100
....*....|....*....|....
gi 769951462 208 VGYCSEVCPKHVDPAAAVNQGKVE 231
Cdd:COG4656 408 CGCCSYVCPSKIPLVQYIRLAKAE 431
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
149-225 |
4.47e-03 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 35.26 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769951462 149 CINCGLCYAACP---QFGLNP-EFIgpaaltlaHRYNLDSRDngqhermELINGENGaWGCTFVGYCSEVCPKHVDPAAA 224
Cdd:COG1150 5 CYQCGTCTASCPvarAMDYNPrKII--------RLAQLGLKE-------EVLKSDSI-WLCVSCYTCTERCPRGIDIADV 68
|
.
gi 769951462 225 V 225
Cdd:COG1150 69 M 69
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
148-219 |
5.41e-03 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 35.84 E-value: 5.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769951462 148 GCINCGLCYAACPQFglnpefigpaALTLAhrynldsrDNGQHERMELINGEngawGCTFVGYCSEVCPKHV 219
Cdd:cd10549 7 KCIGCGICVKACPTD----------AIELG--------PNGAIARGPEIDED----KCVFCGACVEVCPTGA 56
|
|
| |
