|
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: 582.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 1 MTDMKLLKMEVMRYNPERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKT 80
Cdd:PRK12385 1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 81 FLREYTGGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385 81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 161 QFGLNPEFIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFMIAM 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240
|
....
gi 685191068 241 LKPQ 244
Cdd:PRK12385 241 LKPR 244
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
11-229 |
2.52e-135 |
|
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: 379.47 E-value: 2.52e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 11 VMRYNPERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREYTG-GM 89
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQpVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 90 KVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384 81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 170 GPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
7-235 |
3.74e-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: 341.34 E-value: 3.74e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 7 LKMEVMRYNPERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREYT 86
Cdd:COG0479 3 VTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 87 GGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPkDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNP 166
Cdd:COG0479 83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP-DNERLQSPEDREKADDLAECILCGACVAACPNVWANP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 167 EFIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKD 235
Cdd:COG0479 162 DFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
8-112 |
7.30e-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: 145.84 E-value: 7.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 8 KMEVMRYNPERD-SEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREY- 85
Cdd:pfam13085 1 TLRVFRYDPRVDrDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLl 80
|
90 100
....*....|....*....|....*..
gi 685191068 86 TGGMKVEALGNFPIERDLVVDMTHFIE 112
Cdd:pfam13085 81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
148-219 |
1.67e-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: 37.38 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685191068 148 GCINCGLCYAACPQFglnpefigpaAITLAhrynldnrDHGKKERMPQLNGKngvwSCTFVGYCSEVCPKHV 219
Cdd:cd10549 7 KCIGCGICVKACPTD----------AIELG--------PNGAIARGPEIDED----KCVFCGACVEVCPTGA 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: 582.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 1 MTDMKLLKMEVMRYNPERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKT 80
Cdd:PRK12385 1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 81 FLREYTGGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385 81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 161 QFGLNPEFIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFMIAM 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240
|
....
gi 685191068 241 LKPQ 244
Cdd:PRK12385 241 LKPR 244
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
11-229 |
2.52e-135 |
|
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: 379.47 E-value: 2.52e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 11 VMRYNPERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREYTG-GM 89
Cdd:TIGR00384 1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQpVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 90 KVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384 81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 170 GPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
7-235 |
3.74e-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: 341.34 E-value: 3.74e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 7 LKMEVMRYNPERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREYT 86
Cdd:COG0479 3 VTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 87 GGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPkDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLNP 166
Cdd:COG0479 83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAP-DNERLQSPEDREKADDLAECILCGACVAACPNVWANP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 167 EFIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKD 235
Cdd:COG0479 162 DFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
8-226 |
2.48e-94 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 276.29 E-value: 2.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 8 KMEVMRYNPERDSEPHFETFEVPYDEQT-SLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREYT 86
Cdd:PRK05950 1 TFKIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 87 GG-MKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIgNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFGLN 165
Cdd:PRK05950 81 KGkIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLI-NDTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685191068 166 PE-FIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQ 226
Cdd:PRK05950 160 PDkFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIG 221
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-227 |
9.66e-75 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 228.09 E-value: 9.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 1 MTDMKLLKMEVMRYNPERDSepHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKT 80
Cdd:PRK12576 3 QSPEKEVIFKVKRYDPEKGS--WWQEYKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 81 FL----REYTGGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPK-DGPNKQTPAQMAKYHQFSGCINCGLC 155
Cdd:PRK12576 81 LVldvaKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEgKAEHRLKPEDQKELWKFAQCIWCGLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685191068 156 YAACPQFGLNPEFIGPAAITLAHRYNLDNRDHGKKERMPQLngKNGVWSCTFVGYCSEVCPKHVDPAAAIQQ 227
Cdd:PRK12576 161 VSACPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAIKK 230
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
9-231 |
5.73e-56 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 181.82 E-value: 5.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 9 MEV----MRYNPerDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACK----- 79
Cdd:PRK12577 1 MEVlfkiLRQKQ--NSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKenvgs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 80 ---TFLREYTGG---MKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPKDGPNKQTPAQMAKYHQFSGCINCG 153
Cdd:PRK12577 79 elaRLSDSNSGAipeITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCILCG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 154 LCYAACPQFGLNPEFIGPAAITLAHRYNLDNRDHGKKERMPQLN-GKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVE 231
Cdd:PRK12577 159 ACYSECNAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQE 237
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
4-227 |
1.80e-53 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 179.43 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 4 MKLLKMEVMRYNPERDsEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLR 83
Cdd:PRK06259 1 MKMITITVKRFDPEKD-EPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 84 EytgGMKVEALgNFPIERDLVVDMTHFIESLEAIKPYIIGNDRKPkdgpnkQTPAQMAKYHQFSGCINCGLCYAACPQFG 163
Cdd:PRK06259 80 D---GMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKI------TYPEDIEDIKKLRGCIECLSCVSTCPARK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685191068 164 LNpEFIGPAAITLAHRYNLDNRDHGKKERMPQlngKNGVWSCTFVGYCSEVCPKHVD-PAAAIQQ 227
Cdd:PRK06259 150 VS-DYPGPTFMRQLARFAFDPRDEGDREKEAF---DEGLYNCTTCGKCVEVCPKEIDiPGKAIEK 210
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
1-227 |
8.25e-52 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 168.21 E-value: 8.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 1 MTDMKLLkmEVMRYNPERDSEPHFETFEV-PYDEQTSLLDALGYIKdNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACK 79
Cdd:PRK12575 1 MADTRIL--HIYRYDPDDDAAPRMQRYEIaPRAEDRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 80 TFLREYTGGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIIgNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159
Cdd:PRK12575 78 TNMQALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI-NDTVPPERERLQTPQEREQLDGLYECILCACCSTAC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 160 PQFGLNPE-FIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQ 227
Cdd:PRK12575 157 PSYWWNPDkFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQ 225
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
11-229 |
8.25e-52 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 169.58 E-value: 8.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 11 VMRYNPERDSEPHFETFEVPYDE-QTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFL-REYTGG 88
Cdd:PLN00129 48 IYRWNPDNPGKPHLQSYKVDLNDcGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIdRDESGP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 89 MKVEALGNFPIERDLVVDMTHFIESLEAIKPYIigNDRKPKDGPNK---QTPAQMAKYHQFSGCINCGLCYAACPQFGLN 165
Cdd:PLN00129 128 TTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWL--KTKKPPEDGQKehlQSKEDRAKLDGMYECILCACCSTSCPSYWWN 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685191068 166 PE-FIGPAAITLAHRYNLDNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:PLN00129 206 PEkFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
8-112 |
7.30e-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: 145.84 E-value: 7.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 8 KMEVMRYNPERD-SEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREY- 85
Cdd:pfam13085 1 TLRVFRYDPRVDrDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLl 80
|
90 100
....*....|....*....|....*..
gi 685191068 86 TGGMKVEALGNFPIERDLVVDMTHFIE 112
Cdd:pfam13085 81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
7-218 |
2.32e-38 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 133.54 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 7 LKMEVMRYNP-ERDSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREY 85
Cdd:PRK13552 5 LTFNIFRYNPqDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 86 TGG-MKVEALGNFPIERDLVVD----MTHFIESLEA-IKPyiiGNDRKPKDGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159
Cdd:PRK13552 85 PDGvITLMPLPVFKLIGDLSVNtgkwFREMSERVESwIHT---DKEFDIHRLEERMEPEEADEIYELDRCIECGCCVAAC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685191068 160 PQFGLNPEFIGPAAITLAHRYNLDNRDHGKKERMPQLNG-KNGVWSC-TFVGyCSEVCPKH 218
Cdd:PRK13552 162 GTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGnDDGVFGCmSLLG-CEDNCPKD 221
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
4-217 |
1.38e-32 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 118.94 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 4 MKLLKMEVMRYNPErDSEPHFETFEVPYDEQTSLLDALGYIKDN--------LAPdLSYRWSCRMAICGSCGMMVNKVPK 75
Cdd:PRK08640 3 EKTVRLIIKRQDGP-DSKPYWEEFEIPYRPNMNVISALMEIRRNpvnakgekTTP-VVWDMNCLEEVCGACSMVINGKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 76 LACKTFLREYTGGMKVEALGNFPIERDLVVDMTHFIESLEAIKPYIigndrkPKDGPNKQTPA-QMAKYHQ-----FSGC 149
Cdd:PRK08640 81 QACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWI------PIDGTYDLGPGpRMPEEKRqwayeLSKC 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 150 INCGLCYAACPQFGLNPEFIGPAAITLAHRYNLD-NRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCPK 217
Cdd:PRK08640 155 MTCGCCLEACPNVNEKSDFIGPAAISQVRLFNAHpTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPK 223
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
19-219 |
1.03e-25 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 100.93 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 19 DSEPHFETFEVPYDEQTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNKVPKLACKTFLREYTGG--MKVEALGN 96
Cdd:PRK12386 14 ASGGELQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTFDEDetVTVTPMRT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 97 FPIERDLVVDMTHFIESLEAIKPYIIGNDRKPkdGPNKQTPAQMAKYHQFSGCINCGLCYAAC----PQFGLNPEFIGP- 171
Cdd:PRK12386 94 FPVIRDLVTDVSFNYEKAREIPSFTPPKDLQP--GEYRMQQVDVERSQEFRKCIECFLCQNVChvvrDHEENKPAFAGPr 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685191068 172 -----AAITLahrYNLDNRDhgkkeRMPQLNGKNGVWSCTFVGYCSEVCPKHV 219
Cdd:PRK12386 172 flmriAELEM---HPLDTAD-----RRAEAQEEHGLGYCNITKCCTEVCPEHI 216
|
|
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
4-242 |
1.20e-16 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 76.41 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 4 MKLlKMEVMRyNPERDSEPHFETFEVP-YDEQTSLLDAL-----GYIKDNLAPdLSYRWSCRMAICGSCGMMVNKVP--- 74
Cdd:PRK07570 1 MKL-TLKIWR-QKGPDDKGKFETYEVDdISPDMSFLEMLdvlneQLIEKGEEP-VAFDHDCREGICGMCGLVINGRPhgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 75 ---KLACKTFLREYTGG--MKVEAL--GNFPIERDLVVDMTHFIESLEAIKpYIIGNDRKPKDGPNKQTPAQMAKYH-QF 146
Cdd:PRK07570 78 drgTTTCQLHMRSFKDGdtITIEPWraAAFPVIKDLVVDRSALDRIIQAGG-YVSVNTGGAPDANAIPVPKEDADRAfDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 147 SGCINCGLCYAACP-------------QFGLNPEfigpaaitlahrynldnrdhGKKER------MPQLNGKNGVWSCTF 207
Cdd:PRK07570 157 AACIGCGACVAACPngsamlftgakvsHLALLPQ--------------------GQPERarrvraMVAQMDEEGFGNCTN 216
|
250 260 270
....*....|....*....|....*....|....*
gi 685191068 208 VGYCSEVCPKHVdPAAAIQQgkveSAKDFMIAMLK 242
Cdd:PRK07570 217 TGECEAVCPKGI-SLENIAR----MNREYLRASFR 246
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
141-216 |
8.80e-07 |
|
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: 44.93 E-value: 8.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685191068 141 AKYHQFSGCINCGLCYAACPQFGlnpefigpaaitlahrynldNRDHGKKERMPQLNGKNGVWSCTFVGYCSEVCP 216
Cdd:pfam13237 1 KVVIDPDKCIGCGRCTAACPAGL--------------------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
146-226 |
3.23e-06 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 44.12 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 146 FSGCINCGLCYAACPqfglnpefigpaaitLAHRYNLDNRD------HGKKERmpqLNGKNGVWSCTFVGYCSEVCPKHV 219
Cdd:COG1150 2 LKKCYQCGTCTASCP---------------VARAMDYNPRKiirlaqLGLKEE---VLKSDSIWLCVSCYTCTERCPRGI 63
|
....*..
gi 685191068 220 DPAAAIQ 226
Cdd:COG1150 64 DIADVMD 70
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
149-219 |
7.67e-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: 42.68 E-value: 7.67e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685191068 149 CINCGLCYAACPQF-GLNPEFIGPAAITLAHRYNLDNRDHGKKErmpqlngknGVWSCTFVGYCSEVCPKHV 219
Cdd:pfam13183 2 CIRCGACLAACPVYlVTGGRFPGDPRGGAAALLGRLEALEGLAE---------GLWLCTLCGACTEVCPVGI 64
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
149-229 |
9.92e-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: 42.76 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 149 CINCGLCYAACPQFGLNPEFIGPAA--ITLAHRYNLDNRDHGKKERMpqlngKNGVWSCTFVGYCSEVCPKHVDPAAAIQ 226
Cdd:COG0247 80 CVGCGFCRAMCPSYKATGDEKDSPRgrINLLREVLEGELPLDLSEEV-----YEVLDLCLTCKACETACPSGVDIADLIA 154
|
...
gi 685191068 227 QGK 229
Cdd:COG0247 155 EAR 157
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
149-220 |
1.39e-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: 38.98 E-value: 1.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685191068 149 CINCGLCYAACPQFGLNPEFigPAAItlahRYNLDNRDHGKKERMPQLNgkngvwSCTFVGYCSEVCPKHVD 220
Cdd:pfam13534 2 CIQCGCCVDECPRYLLNGDE--PKKL----MRAAYLGDLEELQANKVAN------LCSECGLCEYACPMGLD 61
|
|
| PRK12387 |
PRK12387 |
formate hydrogenlyase complex iron-sulfur subunit; Provisional |
144-216 |
1.69e-04 |
|
formate hydrogenlyase complex iron-sulfur subunit; Provisional
Pssm-ID: 183492 [Multi-domain] Cd Length: 180 Bit Score: 41.17 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685191068 144 HQFSGCINCGLCYAACPqfglnpefigPAAITLahRYNLDnrdhgKKERMPQLN-GKngvwsCTFVGYCSEVCP 216
Cdd:PRK12387 35 YNPQQCIGCAACVNACP----------SNALTV--ETDLA-----TGELAWEFNlGR-----CIFCGRCEEVCP 86
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
149-231 |
6.15e-04 |
|
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: 37.42 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 149 CINCGLCYAACPqfglnpefigPAAITLahrynldnrDHGKKERMPQLNGKNgvwsCTFVGYCSEVCPKHvdpaaAIQQG 228
Cdd:COG1143 4 CIGCGLCVRVCP----------VDAITI---------EDGEPGKVYVIDPDK----CIGCGLCVEVCPTG-----AISMT 55
|
...
gi 685191068 229 KVE 231
Cdd:COG1143 56 PFE 58
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
149-216 |
7.08e-04 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 39.09 E-value: 7.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 149 CINCGLCYAACPQfglnpefigpAAITLahrYNLDNRDHGKKERMPQLN-GKngvwsCTFVGYCSEVCP 216
Cdd:PRK05888 60 CIACKLCAAICPA----------DAITI---EAAEREDGRRRTTRYDINfGR-----CIFCGFCEEACP 110
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
148-219 |
1.67e-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: 37.38 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685191068 148 GCINCGLCYAACPQFglnpefigpaAITLAhrynldnrDHGKKERMPQLNGKngvwSCTFVGYCSEVCPKHV 219
Cdd:cd10549 7 KCIGCGICVKACPTD----------AIELG--------PNGAIARGPEIDED----KCVFCGACVEVCPTGA 56
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
21-66 |
2.19e-03 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 36.36 E-value: 2.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 685191068 21 EPHFETFEVPYDEqtSLLDALgyikdnLAPDLSYRWSCRMAICGSC 66
Cdd:COG0633 7 IPEGHTVEVPAGE--SLLEAA------LRAGIDLPYSCRSGACGTC 44
|
|
| RnfC |
COG4656 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ... |
149-231 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 149 CINCGLCYAACPQfGLNPEFIGPAAitlahrynlDNRDHGKKERMpqlngknGVWSCTFVGYCSEVCPKHVDPAAAIQQG 228
Cdd:COG4656 366 CIRCGRCVDACPM-GLLPQQLYWYA---------RAGDFDKAEEY-------NLMDCIECGCCSYVCPSKIPLVQYIRLA 428
|
...
gi 685191068 229 KVE 231
Cdd:COG4656 429 KAE 431
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
21-92 |
4.18e-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: 35.45 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 21 EPHFETFEVPYDEQTSLLDALgyikdnLAPDLSYRWSCRMAICGSCGMMVNKV------------------PKLACKTFL 82
Cdd:cd00207 4 NVPGSGVEVEVPEGETLLDAA------REAGIDIPYSCRAGACGTCKVEVVEGevdqsdpslldeeeaeggYVLACQTRV 77
|
90
....*....|
gi 685191068 83 reyTGGMKVE 92
Cdd:cd00207 78 ---TDGLVIE 84
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
25-84 |
6.33e-03 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 34.81 E-value: 6.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685191068 25 ETFEVPyDEQTSLLDALgyikDNLAPDLSYrwSCRMAICGSCGMMVNKVPKLACKTFLRE 84
Cdd:pfam00111 8 VTIEVP-DGETTLLDAA----EEAGIDIPY--SCRGGGCGTCAVKVLEGEDQSDQSFLED 60
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
149-217 |
6.55e-03 |
|
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: 463724 [Multi-domain] Cd Length: 51 Bit Score: 34.04 E-value: 6.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685191068 149 CINCGLCYAACPQfglnpefigpAAITLahrynldnRDHGKKERMPQLNGKNgvWSCTFVGYCSEVCPK 217
Cdd:pfam12838 1 CIGCGACVAACPV----------GAITL--------DEVGEKKGTKTVVIDP--ERCVGCGACVAVCPT 49
|
|
| |
