|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-244 |
0e+00 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 566.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 1 MAEMKNLKVEVVRYNPEVDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKT 80
Cdd:PRK12385 1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 81 FLRDYTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385 81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 161 QFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIAT 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240
|
....
gi 1738963693 241 LKPR 244
Cdd:PRK12385 241 LKPR 244
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
11-229 |
5.62e-137 |
|
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: 383.70 E-value: 5.62e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 11 VVRYNPEVDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDYT-KGI 89
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGqPVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 90 KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384 81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 170 GPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
5-235 |
2.85e-117 |
|
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: 334.02 E-value: 2.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 5 KNLKVEVVRYNPEVDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRD 84
Cdd:COG0479 1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 85 YTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPnKQTPAQMAKYHQFSGCINCGLCYAACPQFGL 164
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNER-LQSPEDREKADDLAECILCGACVAACPNVWA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1738963693 165 NPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGKVESSKD 235
Cdd:COG0479 160 NPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
8-112 |
1.70e-43 |
|
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: 142.38 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 8 KVEVVRYNPEVD-TAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDY- 85
Cdd:pfam13085 1 TLRVFRYDPRVDrDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLl 80
|
90 100
....*....|....*....|....*..
gi 1738963693 86 TKGIKVEALANFPIERDLVVDMTHFIE 112
Cdd:pfam13085 81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
148-219 |
2.23e-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: 36.99 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963693 148 GCINCGLCYAACPQFGLnpEFIGPAAITLAHRYNEDSrdhgkkermaqlngqngvwtCTFVGYCSEVCPKHV 219
Cdd:cd10549 7 KCIGCGICVKACPTDAI--ELGPNGAIARGPEIDEDK--------------------CVFCGACVEVCPTGA 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-244 |
0e+00 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 566.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 1 MAEMKNLKVEVVRYNPEVDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKT 80
Cdd:PRK12385 1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 81 FLRDYTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385 81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 161 QFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIAT 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240
|
....
gi 1738963693 241 LKPR 244
Cdd:PRK12385 241 LKPR 244
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
11-229 |
5.62e-137 |
|
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: 383.70 E-value: 5.62e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 11 VVRYNPEVDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDYT-KGI 89
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGqPVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 90 KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384 81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 170 GPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
5-235 |
2.85e-117 |
|
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: 334.02 E-value: 2.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 5 KNLKVEVVRYNPEVDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRD 84
Cdd:COG0479 1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 85 YTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPnKQTPAQMAKYHQFSGCINCGLCYAACPQFGL 164
Cdd:COG0479 81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNER-LQSPEDREKADDLAECILCGACVAACPNVWA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1738963693 165 NPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGKVESSKD 235
Cdd:COG0479 160 NPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
8-226 |
7.36e-92 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 269.74 E-value: 7.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 8 KVEVVRYNPEVDTAPHSAFYDVPYDEQT-SLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDYT 86
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 87 KG-IKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDqGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLN 165
Cdd:PRK05950 81 KGkIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPA-RERLQSPEDREKLDGLYECILCACCSTSCPSFWWN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963693 166 PE-FIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQ 226
Cdd:PRK05950 160 PDkFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIG 221
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-227 |
3.53e-74 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 226.55 E-value: 3.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 1 MAEMKNLKVEVVRYNPEVDTAPHSafYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKT 80
Cdd:PRK12576 3 QSPEKEVIFKVKRYDPEKGSWWQE--YKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 81 FL----RDYTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPD-QGPNKQTPAQMAKYHQFSGCINCGLC 155
Cdd:PRK12576 81 LVldvaKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEgKAEHRLKPEDQKELWKFAQCIWCGLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963693 156 YAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLngQNGVWTCTFVGYCSEVCPKHVDPAAAIQQ 227
Cdd:PRK12576 161 VSACPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAIKK 230
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
11-231 |
2.64e-53 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 174.88 E-value: 2.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 11 VVRYNPevDTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACK--------TFL 82
Cdd:PRK12577 7 ILRQKQ--NSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKenvgselaRLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 83 RDYTKG---IKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159
Cdd:PRK12577 85 DSNSGAipeITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCILCGACYSEC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1738963693 160 PQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLN-GQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGKVE 231
Cdd:PRK12577 165 NAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQE 237
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
5-229 |
1.60e-52 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 171.13 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 5 KNLK-VEVVRYNPEVDTAPHSAFYDVPYDE-QTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFL 82
Cdd:PLN00129 41 SNLKeFQIYRWNPDNPGKPHLQSYKVDLNDcGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 83 -RDYTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPDQGPN-KQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PLN00129 121 dRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEhLQSKEDRAKLDGMYECILCACCSTSCP 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 161 QFGLNPE-FIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:PLN00129 201 SYWWNPEkFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
4-227 |
7.62e-52 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 175.19 E-value: 7.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 4 MKNLKVEVVRYNPEVDtAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLR 83
Cdd:PRK06259 1 MKMITITVKRFDPEKD-EPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 84 DytkGIKVEALaNFPIERDLVVDMTHFIESLEAIKPYIIGNNRTPdqgpnkQTPAQMAKYHQFSGCINCGLCYAACPQFG 163
Cdd:PRK06259 80 D---GMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKI------TYPEDIEDIKKLRGCIECLSCVSTCPARK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1738963693 164 LNpEFIGPAAITLAHRYNEDSRDHGKKERMAQlngQNGVWTCTFVGYCSEVCPKHVD-PAAAIQQ 227
Cdd:PRK06259 150 VS-DYPGPTFMRQLARFAFDPRDEGDREKEAF---DEGLYNCTTCGKCVEVCPKEIDiPGKAIEK 210
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
9-227 |
2.23e-50 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 164.36 E-value: 2.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 9 VEVVRYNPEVDTAPHSAFYDV-PYDEQTSLLDALGYIKdNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDYTK 87
Cdd:PRK12575 7 LHIYRYDPDDDAAPRMQRYEIaPRAEDRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 88 GIKVEALANFPIERDLVVDMTHFIESLEAIKPYIIgNNRTPDQGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPE 167
Cdd:PRK12575 86 EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI-NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNPD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1738963693 168 -FIGPAAITLAHRYNEDSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPKHVDPAAAIQQ 227
Cdd:PRK12575 165 kFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQ 225
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
8-112 |
1.70e-43 |
|
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: 142.38 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 8 KVEVVRYNPEVD-TAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDY- 85
Cdd:pfam13085 1 TLRVFRYDPRVDrDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLl 80
|
90 100
....*....|....*....|....*..
gi 1738963693 86 TKGIKVEALANFPIERDLVVDMTHFIE 112
Cdd:pfam13085 81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
5-218 |
2.50e-39 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 136.23 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 5 KNLKVEVVRYNPEV-DTAPHSAFYDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLR 83
Cdd:PRK13552 3 RTLTFNIFRYNPQDpGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 84 DYTKG-IKVEALANFPIERDLVVD----MTHFIESLEAikpyIIGNNRTPDqgPNKQ----TPAQMAKYHQFSGCINCGL 154
Cdd:PRK13552 83 DYPDGvITLMPLPVFKLIGDLSVNtgkwFREMSERVES----WIHTDKEFD--IHRLeermEPEEADEIYELDRCIECGC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738963693 155 CYAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNG-QNGVWTC-TFVGyCSEVCPKH 218
Cdd:PRK13552 157 CVAACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGnDDGVFGCmSLLG-CEDNCPKD 221
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
3-217 |
2.73e-30 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 112.77 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 3 EMKNLKVEVVRYNpEVDTAPHSAFYDVPYDEQTSLLDALGYIKDN--------LAPdLSYRWSCRMAICGSCGMMVNKVP 74
Cdd:PRK08640 2 SEKTVRLIIKRQD-GPDSKPYWEEFEIPYRPNMNVISALMEIRRNpvnakgekTTP-VVWDMNCLEEVCGACSMVINGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 75 KLACKTFLRDYTKGIKVEALANFPIERDLVVDMTHFIESLEAIKPYI-IgnNRTPDQGPN-KQTPAQMAKYHQFSGCINC 152
Cdd:PRK08640 80 RQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIpI--DGTYDLGPGpRMPEEKRQWAYELSKCMTC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738963693 153 GLCYAACPQFGLNPEFIGPAAITLAHRYNED-SRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCPK 217
Cdd:PRK08640 158 GCCLEACPNVNEKSDFIGPAAISQVRLFNAHpTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPK 223
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
27-219 |
9.96e-26 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 100.93 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 27 YDVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLRDYT--KGIKVEALANFPIERDLV 104
Cdd:PRK12386 22 YTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTFDedETVTVTPMRTFPVIRDLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 105 VDMTHFIESLEAIKPYiignNRTPDQGPNKQTPAQM--AKYHQFSGCINCGLCYAAC----PQFGLNPEFIGPAAITlah 178
Cdd:PRK12386 102 TDVSFNYEKAREIPSF----TPPKDLQPGEYRMQQVdvERSQEFRKCIECFLCQNVChvvrDHEENKPAFAGPRFLM--- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1738963693 179 RYNE------DSRDhgkkeRMAQLNGQNGVWTCTFVGYCSEVCPKHV 219
Cdd:PRK12386 175 RIAElemhplDTAD-----RRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
58-244 |
1.66e-15 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 73.33 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 58 CRMAICGSCGMMVNKVP------KLACKTFLRDYTKG--IKVEAL--ANFPIERDLVVDMTHFIESLEAIKpYIIGNNRT 127
Cdd:PRK07570 58 CREGICGMCGLVINGRPhgpdrgTTTCQLHMRSFKDGdtITIEPWraAAFPVIKDLVVDRSALDRIIQAGG-YVSVNTGG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 128 PDQGPNKQTPAQMAKYH-QFSGCINCGLCYAACP-------------QFGLNPEfigpaaitlahrynedsrdhGKKER- 192
Cdd:PRK07570 137 APDANAIPVPKEDADRAfDAAACIGCGACVAACPngsamlftgakvsHLALLPQ--------------------GQPERa 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1738963693 193 -----MAQLNGQNGVWTCTFVGYCSEVCPKHVdPAAAIQQgkveSSKDFLIATLKPR 244
Cdd:PRK07570 197 rrvraMVAQMDEEGFGNCTNTGECEAVCPKGI-SLENIAR----MNREYLRASFRGR 248
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
141-216 |
1.52e-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: 44.16 E-value: 1.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738963693 141 AKYHQFSGCINCGLCYAACPQFGlnpefigpaaitlahrynedSRDHGKKERMAQLNGQNGVWTCTFVGYCSEVCP 216
Cdd:pfam13237 1 KVVIDPDKCIGCGRCTAACPAGL--------------------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
149-219 |
3.79e-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: 3.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963693 149 CINCGLCYAACPQF-GLNPEFIGPAAITLAHRYNEDSRDHGKKErmaqlngqnGVWTCTFVGYCSEVCPKHV 219
Cdd:pfam13183 2 CIRCGACLAACPVYlVTGGRFPGDPRGGAAALLGRLEALEGLAE---------GLWLCTLCGACTEVCPVGI 64
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
149-244 |
2.93e-05 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 44.30 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 149 CINCGLCYAACPQFGLNPEFIGPAA--ITLAHRYNEDSRDHGKKERMAQlngqnGVWTCTFVGYCSEVCPKHVDPA---- 222
Cdd:COG0247 80 CVGCGFCRAMCPSYKATGDEKDSPRgrINLLREVLEGELPLDLSEEVYE-----VLDLCLTCKACETACPSGVDIAdlia 154
|
90 100
....*....|....*....|....*
gi 1738963693 223 ---AAIQQGKVESSKDFLIATLKPR 244
Cdd:COG0247 155 earAQLVERGGRPLRDRLLRTFPDR 179
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
146-226 |
4.56e-05 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 40.65 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 146 FSGCINCGLCYAACP---QFGLNP-EFIgpaaitlahrynedsrdhgkkeRMAQLN------GQNGVWTCTFVGYCSEVC 215
Cdd:COG1150 2 LKKCYQCGTCTASCPvarAMDYNPrKII----------------------RLAQLGlkeevlKSDSIWLCVSCYTCTERC 59
|
90
....*....|.
gi 1738963693 216 PKHVDPAAAIQ 226
Cdd:COG1150 60 PRGIDIADVMD 70
|
|
| PRK12387 |
PRK12387 |
formate hydrogenlyase complex iron-sulfur subunit; Provisional |
144-216 |
2.82e-04 |
|
formate hydrogenlyase complex iron-sulfur subunit; Provisional
Pssm-ID: 183492 [Multi-domain] Cd Length: 180 Bit Score: 40.40 E-value: 2.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738963693 144 HQFSGCINCGLCYAACPqfglnpefigPAAITLahRYNEDsrdhgKKERMAQLN-GQngvwtCTFVGYCSEVCP 216
Cdd:PRK12387 35 YNPQQCIGCAACVNACP----------SNALTV--ETDLA-----TGELAWEFNlGR-----CIFCGRCEEVCP 86
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
149-220 |
2.93e-04 |
|
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: 37.83 E-value: 2.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963693 149 CINCGLCYAACPQFGLNPEFigPAAITLAhRYNEDSRDHGKKERMAQlngqngvwtCTFVGYCSEVCPKHVD 220
Cdd:pfam13534 2 CIQCGCCVDECPRYLLNGDE--PKKLMRA-AYLGDLEELQANKVANL---------CSECGLCEYACPMGLD 61
|
|
| RnfC |
COG4656 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ... |
149-231 |
5.65e-04 |
|
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: 40.51 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 149 CINCGLCYAACPQfGLNPEFIGPAAitlahrynedsrDHGKKERMAQLNGQNgvwtCTFVGYCSEVCPKHVDPAAAIQQG 228
Cdd:COG4656 366 CIRCGRCVDACPM-GLLPQQLYWYA------------RAGDFDKAEEYNLMD----CIECGCCSYVCPSKIPLVQYIRLA 428
|
...
gi 1738963693 229 KVE 231
Cdd:COG4656 429 KAE 431
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
149-216 |
8.24e-04 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 38.71 E-value: 8.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 149 CINCGLCYAACPQfglnpefigpAAITLAHRYNEDSRDHGKKER--MAqlngqngvwTCTFVGYCSEVCP 216
Cdd:PRK05888 60 CIACKLCAAICPA----------DAITIEAAEREDGRRRTTRYDinFG---------RCIFCGFCEEACP 110
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
148-219 |
2.23e-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: 36.99 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738963693 148 GCINCGLCYAACPQFGLnpEFIGPAAITLAHRYNEDSrdhgkkermaqlngqngvwtCTFVGYCSEVCPKHV 219
Cdd:cd10549 7 KCIGCGICVKACPTDAI--ELGPNGAIARGPEIDEDK--------------------CVFCGACVEVCPTGA 56
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
149-231 |
2.78e-03 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 35.49 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738963693 149 CINCGLCYAACPqfglnpefigPAAITLahrynedsrDHGKKERMAQLNGQNgvwtCTFVGYCSEVCPKHvdpaaAIQQG 228
Cdd:COG1143 4 CIGCGLCVRVCP----------VDAITI---------EDGEPGKVYVIDPDK----CIGCGLCVEVCPTG-----AISMT 55
|
...
gi 1738963693 229 KVE 231
Cdd:COG1143 56 PFE 58
|
|
| |
