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Conserved domains on  [gi|16131978|ref|NP_418577|]
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fumarate reductase iron-sulfur protein [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

succinate dehydrogenase/fumarate reductase iron-sulfur subunit( domain architecture ID 11485878)

quinone-dependent succinate dehydrogenase/fumarate reductase iron-sulfur subunit such as in fumarate reductase, which catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor

Graphical summary

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List of domain hits

 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: 562.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    1 MAEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
Cdd:PRK12385   1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   81 FLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385  81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  161 QFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIAT 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240


                 ....
gi 16131978  241 LKPR 244
Cdd:PRK12385 241 LKPR 244
 
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: 562.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    1 MAEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
Cdd:PRK12385   1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   81 FLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385  81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  161 QFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIAT 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240


                 ....
gi 16131978  241 LKPR 244
Cdd:PRK12385 241 LKPR 244
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 11-229 1.92e-139

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: 389.87  E-value: 1.92e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    11 VVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTD-GM 89
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQpVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    90 KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384  81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   170 GPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 5-235 3.54e-116

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: 331.33  E-value: 3.54e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   5 KNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRD 84
Cdd:COG0479   1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  85 YTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSrTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGL 164
Cdd:COG0479  81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAACPNVWA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131978 165 NPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKD 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 4.80e-42

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: 138.91  E-value: 4.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978     8 KIEVVRYNPEVD-TAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDY- 85
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLl 80

                          90       100
                  ....*....|....*....|....*..
gi 16131978    86 TDGMKVEALANFPIERDLVVDMTHFIE 112
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 148-219 1.75e-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: 1.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131978 148 GCINCGLCYAACPQFGLnpEFIGPAAITLAHRYNEDsrdhgkkermaqlnsqngvwSCTFVGYCSEVCPKHV 219
Cdd:cd10549   7 KCIGCGICVKACPTDAI--ELGPNGAIARGPEIDED--------------------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: 562.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    1 MAEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
Cdd:PRK12385   1 MAEMKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   81 FLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PRK12385  81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  161 QFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIAT 240
Cdd:PRK12385 161 QFGLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAKDFLIAM 240


                 ....
gi 16131978  241 LKPR 244
Cdd:PRK12385 241 LKPR 244
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 11-229 1.92e-139

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: 389.87  E-value: 1.92e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    11 VVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTD-GM 89
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQpVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    90 KVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFI 169
Cdd:TIGR00384  81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   170 GPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 5-235 3.54e-116

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: 331.33  E-value: 3.54e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   5 KNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRD 84
Cdd:COG0479   1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  85 YTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSrTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGL 164
Cdd:COG0479  81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAACPNVWA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131978 165 NPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKD 235
Cdd:COG0479 160 NPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 8-226 7.54e-91

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 267.43  E-value: 7.54e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    8 KIEVVRYNPEVDTAPHSAFYEVPYDATT-SLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYT 86
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   87 DG-MKVEALANFPIERDLVVDMTHFIESLEAIKPYIIgNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLN 165
Cdd:PRK05950  81 KGkIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLI-NDTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWN 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131978  166 PE-FIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQ 226
Cdd:PRK05950 160 PDkFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIG 221
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-227 1.41e-74

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 227.71  E-value: 1.41e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    1 MAEMKNLKIEVVRYNPEVDTAPHSafYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80
Cdd:PRK12576   3 QSPEKEVIFKVKRYDPEKGSWWQE--YKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   81 FL----RDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIgNSRTADQGTNIQ--TPAQMAKYHQFSGCINCGL 154
Cdd:PRK12576  81 LVldvaKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLY-RAKEVLEGKAEHrlKPEDQKELWKFAQCIWCGL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131978  155 CYAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLnsQNGVWSCTFVGYCSEVCPKHVDPAAAIQQ 227
Cdd:PRK12576 160 CVSACPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAIKK 230
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
9-231 5.20e-54

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 176.81  E-value: 5.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    9 IEVVRYNPevDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACK--------T 80
Cdd:PRK12577   5 FKILRQKQ--NSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKenvgselaR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   81 FLRDYTDG---MKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYA 157
Cdd:PRK12577  83 LSDSNSGAipeITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCILCGACYS 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131978  158 ACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLN-SQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVE 231
Cdd:PRK12577 163 ECNAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQE 237
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 5-229 1.16e-52

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 171.51  E-value: 1.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    5 KNLK-IEVVRYNPEVDTAPHSAFYEVPY-DATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL 82
Cdd:PLN00129  41 SNLKeFQIYRWNPDNPGKPHLQSYKVDLnDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   83 -RDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNI-QTPAQMAKYHQFSGCINCGLCYAACP 160
Cdd:PLN00129 121 dRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGQKEHlQSKEDRAKLDGMYECILCACCSTSCP 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  161 QFGLNPE-FIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Cdd:PLN00129 201 SYWWNPEkFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 4-227 9.81e-52

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 174.81  E-value: 9.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    4 MKNLKIEVVRYNPEVDtAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLR 83
Cdd:PRK06259   1 MKMITITVKRFDPEKD-EPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   84 dytDGMKVEALaNFPIERDLVVDMTHFIESLEAIKPYIIGNSRTadqgtnIQTPAQMAKYHQFSGCINCGLCYAACPQFG 163
Cdd:PRK06259  80 ---DGMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEK------ITYPEDIEDIKKLRGCIECLSCVSTCPARK 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131978  164 LNpEFIGPAAITLAHRYNEDSRDHGKKERMAqlnSQNGVWSCTFVGYCSEVCPKHVD-PAAAIQQ 227
Cdd:PRK06259 150 VS-DYPGPTFMRQLARFAFDPRDEGDREKEA---FDEGLYNCTTCGKCVEVCPKEIDiPGKAIEK 210
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
9-227 6.17e-49

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 160.89  E-value: 6.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    9 IEVVRYNPEVDTAPHSAFYEVPYDATTS-LLDALGYIKdNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTD 87
Cdd:PRK12575   7 LHIYRYDPDDDAAPRMQRYEIAPRAEDRmLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALPR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   88 GMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIgNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPE 167
Cdd:PRK12575  86 EIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLI-NDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNPD 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131978  168 -FIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQ 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 4.80e-42

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: 138.91  E-value: 4.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978     8 KIEVVRYNPEVD-TAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDY- 85
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLl 80

                          90       100
                  ....*....|....*....|....*..
gi 16131978    86 TDGMKVEALANFPIERDLVVDMTHFIE 112
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 5-218 2.32e-37

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 130.84  E-value: 2.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    5 KNLKIEVVRYNPEV-DTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLR 83
Cdd:PRK13552   3 RTLTFNIFRYNPQDpGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   84 DYTDG-MKVEALANFPIERDLVVD----MTHFIESLEAikpyIIGNSRTADQgTNIQT---PAQMAKYHQFSGCINCGLC 155
Cdd:PRK13552  83 DYPDGvITLMPLPVFKLIGDLSVNtgkwFREMSERVES----WIHTDKEFDI-HRLEErmePEEADEIYELDRCIECGCC 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131978  156 YAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQL-NSQNGVWSC-TFVGyCSEVCPKH 218
Cdd:PRK13552 158 VAACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELiGNDDGVFGCmSLLG-CEDNCPKD 221
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 3-217 4.66e-28

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 107.00  E-value: 4.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978    3 EMKNLKIEVVRYNpEVDTAPHSAFYEVPYDATTSLLDALGYIKDN--------LAPdLSYRWSCRMAICGSCGMMVNNVP 74
Cdd:PRK08640   2 SEKTVRLIIKRQD-GPDSKPYWEEFEIPYRPNMNVISALMEIRRNpvnakgekTTP-VVWDMNCLEEVCGACSMVINGKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   75 KLACKTFLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSrTADQGTNIQTPA---QMAkyHQFSGCIN 151
Cdd:PRK08640  80 RQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDG-TYDLGPGPRMPEekrQWA--YELSKCMT 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131978  152 CGLCYAACPQFGLNPEFIGPAAITLAHRYNED-SRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPK 217
Cdd:PRK08640 157 CGCCLEACPNVNEKSDFIGPAAISQVRLFNAHpTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPK 223
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 27-219 5.21e-23

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 93.61  E-value: 5.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   27 YEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTDG--MKVEALANFPIERDLV 104
Cdd:PRK12386  22 YTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTFDEDetVTVTPMRTFPVIRDLV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  105 VDMTHFIESLEAIKPYIigNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAAC----PQFGLNPEFIGPAAITlahRY 180
Cdd:PRK12386 102 TDVSFNYEKAREIPSFT--PPKDLQPGEYRMQQVDVERSQEFRKCIECFLCQNVChvvrDHEENKPAFAGPRFLM---RI 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16131978  181 NE------DSRDhgkkeRMAQLNSQNGVWSCTFVGYCSEVCPKHV 219
Cdd:PRK12386 177 AElemhplDTAD-----RRAEAQEEHGLGYCNITKCCTEVCPEHI 216
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 58-244 2.10e-19

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 84.11  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978   58 CRMAICGSCGMMVNNVP------KLACKTFLRDYTDG--MKVEAL--ANFPIERDLVVDMTHFIESLEAIKpYIIGNSRT 127
Cdd:PRK07570  58 CREGICGMCGLVINGRPhgpdrgTTTCQLHMRSFKDGdtITIEPWraAAFPVIKDLVVDRSALDRIIQAGG-YVSVNTGG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978  128 ADQGTNIQTPAQMAKYH-QFSGCINCGLCYAACP-------------QFGLNPEfigpaaitlahrynedsrdhGKKER- 192
Cdd:PRK07570 137 APDANAIPVPKEDADRAfDAAACIGCGACVAACPngsamlftgakvsHLALLPQ--------------------GQPERa 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131978  193 -----MAQLNSQNGVWSCTFVGYCSEVCPKHVdPAAAIQQgkveSSKDFLIATLKPR 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 1.73e-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: 1.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131978   141 AKYHQFSGCINCGLCYAACPQFGlnpefigpaaitlahrynedSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCP 216
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACPAGL--------------------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 149-219 3.26e-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: 3.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131978   149 CINCGLCYAACPQF-GLNPEFIGPAAITLAHRYNEDSRDHGKKErmaqlnsqnGVWSCTFVGYCSEVCPKHV 219
Cdd:pfam13183   2 CIRCGACLAACPVYlVTGGRFPGDPRGGAAALLGRLEALEGLAE---------GLWLCTLCGACTEVCPVGI 64
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
146-226 1.34e-05

Heterodisulfide reductase, subunit C [Energy production and conversion];


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 42.19  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978 146 FSGCINCGLCYAACP---QFGLNPEFIgpaaITLAHrynedsrdHGKKERMaqLNSqNGVWSCTFVGYCSEVCPKHVDPA 222
Cdd:COG1150   2 LKKCYQCGTCTASCPvarAMDYNPRKI----IRLAQ--------LGLKEEV--LKS-DSIWLCVSCYTCTERCPRGIDIA 66


                ....
gi 16131978 223 AAIQ 226
Cdd:COG1150  67 DVMD 70
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 149-244 2.51e-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: 44.68  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978 149 CINCGLCYAACPQFGLNPEFIGPAA--ITLAHRYNEDSRDHGKKERMAQlnsqnGVWSCTFVGYCSEVCPKHVDPA---- 222
Cdd:COG0247  80 CVGCGFCRAMCPSYKATGDEKDSPRgrINLLREVLEGELPLDLSEEVYE-----VLDLCLTCKACETACPSGVDIAdlia 154

                        90       100
                ....*....|....*....|....*
gi 16131978 223 ---AAIQQGKVESSKDFLIATLKPR 244
Cdd:COG0247 155 earAQLVERGGRPLRDRLLRTFPDR 179
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 149-220 1.80e-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: 38.60  E-value: 1.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131978   149 CINCGLCYAACPQFGLNPEfigPAAITLAHRYNEDSRDHGKKERMAqlnsqngvwSCTFVGYCSEVCPKHVD 220
Cdd:pfam13534   2 CIQCGCCVDECPRYLLNGD---EPKKLMRAAYLGDLEELQANKVAN---------LCSECGLCEYACPMGLD 61
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 144-216 3.57e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 40.02  E-value: 3.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131978  144 HQFSGCINCGLCYAACPqfglnpefigPAAITLahRYNEdsrDHGKKermaqlnsqngVWS-----CTFVGYCSEVCP 216
Cdd:PRK12387  35 YNPQQCIGCAACVNACP----------SNALTV--ETDL---ATGEL-----------AWEfnlgrCIFCGRCEEVCP 86
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 149-231 8.80e-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: 40.12  E-value: 8.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978 149 CINCGLCYAACPQfGLNPEFIGPAAitlahrynedsrDHGKKERMAQLNSQNgvwsCTFVGYCSEVCPKHVDPAAAIQQG 228
Cdd:COG4656 366 CIRCGRCVDACPM-GLLPQQLYWYA------------RAGDFDKAEEYNLMD----CIECGCCSYVCPSKIPLVQYIRLA 428


                ...
gi 16131978 229 KVE 231
Cdd:COG4656 429 KAE 431
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
149-216 9.77e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 38.71  E-value: 9.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131978  149 CINCGLCYAACPQfglnpefigpAAITLAHRYNEDSRDHGKK-----ERmaqlnsqngvwsCTFVGYCSEVCP 216
Cdd:PRK05888  60 CIACKLCAAICPA----------DAITIEAAEREDGRRRTTRydinfGR------------CIFCGFCEEACP 110
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 149-231 1.59e-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: 36.26  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131978 149 CINCGLCYAACPqfglnpefigPAAITLahrynedsrDHGKKERMAQLNSQNgvwsCTFVGYCSEVCPKHvdpaaAIQQG 228
Cdd:COG1143   4 CIGCGLCVRVCP----------VDAITI---------EDGEPGKVYVIDPDK----CIGCGLCVEVCPTG-----AISMT 55


                ...
gi 16131978 229 KVE 231
Cdd:COG1143  56 PFE 58
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 148-219 1.75e-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: 1.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131978 148 GCINCGLCYAACPQFGLnpEFIGPAAITLAHRYNEDsrdhgkkermaqlnsqngvwSCTFVGYCSEVCPKHV 219
Cdd:cd10549   7 KCIGCGICVKACPTDAI--ELGPNGAIARGPEIDED--------------------KCVFCGACVEVCPTGA 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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