NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499383188|ref|WP_011070759|]
View 

MULTISPECIES: fumarate reductase iron-sulfur subunit [Shewanella]

Protein Classification

fumarate reductase iron-sulfur subunit( domain architecture ID 11486707)

quinone-dependent fumarate reductase iron-sulfur subunit catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 3-242 0e+00

fumarate reductase iron-sulfur subunit; Provisional


:

Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 506.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   3 QGRQLTFNIFRYDPQEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTL 82
Cdd:PRK13552   1 MGRTLTFNIFRYNPQDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  83 TAKYPKGEITLMPLPGFELIGDLSVNTGKFMRELAERLKLWLHPKAnDISIHRLEEPMAPEEAARLYELERCVECGVCVS 162
Cdd:PRK13552  81 TSDYPDGVITLMPLPVFKLIGDLSVNTGKWFREMSERVESWIHTDK-EFDIHRLEERMEPEEADEIYELDRCIECGCCVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 163 ACATKQMRETFVGAVGMMKIARFELDSRDARTAEDFYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMAMTL 242
Cdd:PRK13552 160 ACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQIAYLRRKMAATG 239
 
Name Accession Description Interval E-value
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 3-242 0e+00

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 506.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   3 QGRQLTFNIFRYDPQEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTL 82
Cdd:PRK13552   1 MGRTLTFNIFRYNPQDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  83 TAKYPKGEITLMPLPGFELIGDLSVNTGKFMRELAERLKLWLHPKAnDISIHRLEEPMAPEEAARLYELERCVECGVCVS 162
Cdd:PRK13552  81 TSDYPDGVITLMPLPVFKLIGDLSVNTGKWFREMSERVESWIHTDK-EFDIHRLEERMEPEEADEIYELDRCIECGCCVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 163 ACATKQMRETFVGAVGMMKIARFELDSRDARTAEDFYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMAMTL 242
Cdd:PRK13552 160 ACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQIAYLRRKMAATG 239
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 5-240 1.48e-92

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: 271.62  E-value: 1.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   5 RQLTFNIFRYDPqEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTA 84
Cdd:COG0479    1 MTVTLKIWRQDP-ETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  85 KYpKGEITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLHPkanDISIHRLEEPMAPEEAARLYELERCVECGVCVSAC 164
Cdd:COG0479   80 DL-KDTITIEPLRNFPVIKDLVVDRSAFFDKL-KKVKPYLSP---DGPAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499383188 165 ATKQMRETFVGAVGMMKIARFELDSRDARTAEdFYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMAM 240
Cdd:COG0479  155 PNVWANPDFLGPAALAQAYRFALDPRDEETEE-RLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALK 229
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 11-235 8.41e-56

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: 177.62  E-value: 8.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   11 IFRYDPQEPnDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKYPKGE 90
Cdd:TIGR00384   1 VLRFNPDVD-EKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   91 ITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLhpKANDISIHRLEEPMAPEEAARLYELERCVECGVCVSACATKQMR 170
Cdd:TIGR00384  80 MKIEPLPNLPVIKDLVVDMGPFYAKL-EAIKPYL--IRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499383188  171 ETFVGAVGMMKIARFELDSRDARTAEDfYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLR 235
Cdd:TIGR00384 157 PEFLGPAALTAAYRFLIDSRDHATKDR-LEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 8-114 1.52e-39

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: 132.36  E-value: 1.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188    8 TFNIFRYDPQEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKYP 87
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 499383188   88 KGEITLMPLPGFELIGDLSVNTGKFMR 114
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 3-242 0e+00

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 506.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   3 QGRQLTFNIFRYDPQEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTL 82
Cdd:PRK13552   1 MGRTLTFNIFRYNPQDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  83 TAKYPKGEITLMPLPGFELIGDLSVNTGKFMRELAERLKLWLHPKAnDISIHRLEEPMAPEEAARLYELERCVECGVCVS 162
Cdd:PRK13552  81 TSDYPDGVITLMPLPVFKLIGDLSVNTGKWFREMSERVESWIHTDK-EFDIHRLEERMEPEEADEIYELDRCIECGCCVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 163 ACATKQMRETFVGAVGMMKIARFELDSRDARTAEDFYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMAMTL 242
Cdd:PRK13552 160 ACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQIAYLRRKMAATG 239
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 5-240 1.48e-92

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: 271.62  E-value: 1.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   5 RQLTFNIFRYDPqEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTA 84
Cdd:COG0479    1 MTVTLKIWRQDP-ETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  85 KYpKGEITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLHPkanDISIHRLEEPMAPEEAARLYELERCVECGVCVSAC 164
Cdd:COG0479   80 DL-KDTITIEPLRNFPVIKDLVVDRSAFFDKL-KKVKPYLSP---DGPAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499383188 165 ATKQMRETFVGAVGMMKIARFELDSRDARTAEdFYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMAM 240
Cdd:COG0479  155 PNVWANPDFLGPAALAQAYRFALDPRDEETEE-RLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALK 229
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 11-235 8.41e-56

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: 177.62  E-value: 8.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   11 IFRYDPQEPnDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKYPKGE 90
Cdd:TIGR00384   1 VLRFNPDVD-EKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   91 ITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLhpKANDISIHRLEEPMAPEEAARLYELERCVECGVCVSACATKQMR 170
Cdd:TIGR00384  80 MKIEPLPNLPVIKDLVVDMGPFYAKL-EAIKPYL--IRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499383188  171 ETFVGAVGMMKIARFELDSRDARTAEDfYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLR 235
Cdd:TIGR00384 157 PEFLGPAALTAAYRFLIDSRDHATKDR-LEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 8-238 1.21e-51

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 167.66  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   8 TFNIFRYDPqEPNDKPKMVRYQL-TETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKY 86
Cdd:PRK05950   1 TFKIYRYNP-DVDANPRMQTYEVdVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  87 PKGEITLMPLPGFELIGDLSVNTGKFMRELAErLKLWLHPKANDISIHRLEepmAPEEAARLYELERCVECGVCVSACAT 166
Cdd:PRK05950  80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRS-IKPYLINDTPPPARERLQ---SPEDREKLDGLYECILCACCSTSCPS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499383188 167 KQMR-ETFVGAVGMMKIARFELDSRDARTAEDFyHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKM 238
Cdd:PRK05950 156 FWWNpDKFLGPAALLQAYRFIADSRDEATGERL-DILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRML 227
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-236 1.18e-49

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 163.77  E-value: 1.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   1 MSQGRQLTFNIFRYDP------QEpndkpkmvrYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGF 74
Cdd:PRK12576   3 QSPEKEVIFKVKRYDPekgswwQE---------YKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  75 PTLACRTLT---AKYPKGEITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLHPKaNDISIHRLEEPMAPEEAARLYEL 151
Cdd:PRK12576  74 PRLACKTLVldvAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERM-FKVKPRLYRA-KEVLEGKAEHRLKPEDQKELWKF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 152 ERCVECGVCVSACATKQMRETFVGAVGMMKIARFELDSRDARTAEDFYHVIgnqDGVFGCMTLLGCQDNCPKDLPHMQQI 231
Cdd:PRK12576 152 AQCIWCGLCVSACPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKILI---DSSWRCTYCYSCSNVCPRDIEPVTAI 228


                 ....*
gi 499383188 232 AYLRR 236
Cdd:PRK12576 229 KKTRS 233
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 8-239 3.92e-40

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 139.15  E-value: 3.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   8 TFNIFRYDPQEPNdKPKMVRYQL-TETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKY 86
Cdd:PLN00129  45 EFQIYRWNPDNPG-KPHLQSYKVdLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  87 PKGEITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLHPKaNDISIHRLEEPMAPEEAARLYELERCVECGVCVSACAT 166
Cdd:PLN00129 124 ESGPTTITPLPHMFVIKDLVVDMTNFYQQY-KSIEPWLKTK-KPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPS 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499383188 167 KQMR-ETFVGAVGMMKIARFELDSRDARTAEDFYHVIGNQDgVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMA 239
Cdd:PLN00129 202 YWWNpEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFK-LYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 8-114 1.52e-39

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: 132.36  E-value: 1.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188    8 TFNIFRYDPQEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKYP 87
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 499383188   88 KGEITLMPLPGFELIGDLSVNTGKFMR 114
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
6-235 6.30e-39

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 137.52  E-value: 6.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   6 QLTFNIFRydpQEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLAC------ 79
Cdd:PRK12577   2 EVLFKILR---QKQNSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvgs 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  80 --RTLTAKYPKG--EITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLHPKANDISihRLEEPMAPEEAARLYELERCV 155
Cdd:PRK12577  79 elARLSDSNSGAipEITIAPLGNMPVIKDLVVDMSSFWQNL-EAVDPYVSTAARQVP--EREFLQTPEERSKLDQTGNCI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 156 ECGVCVSACATKQMRETFVGAVGMMKIARFELDSRDARTAE--DFYhvigNQD--GVFGCMTLLGCQDNCPKDLPHMQQI 231
Cdd:PRK12577 156 LCGACYSECNAREVNPEFVGPHALAKAQRMVADSRDTATEQrlELY----NQGtaGVWGCTRCYYCNSVCPMEVAPLDQI 231


                 ....
gi 499383188 232 AYLR 235
Cdd:PRK12577 232 TKIK 235
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
8-239 5.23e-38

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 132.77  E-value: 5.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   8 TFNIFRYDPqEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTAKYP 87
Cdd:PRK12575   6 ILHIYRYDP-DDDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  88 KgEITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLhpkANDISIHRLEEPMAPEEAARLYELERCVECGVCVSACATK 167
Cdd:PRK12575  85 R-EIVLRPLPGLPVVRDLIVDMTDFFNQY-HSIRPYL---INDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499383188 168 QMR-ETFVGAVGMMKIARFELDSRDARTA------EDFYHvignqdgVFGCMTLLGCQDNCPKDLPHMQQIAYLRRKMA 239
Cdd:PRK12575 160 WWNpDKFVGPAGLLQAYRFIADSRDDATAarlddlEDPYR-------LFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 5-227 2.82e-37

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 136.29  E-value: 2.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   5 RQLTFNIFRYDPQEpnDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLTa 84
Cdd:PRK06259   2 KMITITVKRFDPEK--DEPHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  85 kypKGEITLMPLpGFELIGDLSVNTGKFMRELAeRLKLWLHPKAndisihrlEEPMAPEEAARLYELERCVECGVCVSAC 164
Cdd:PRK06259  79 ---EDGMIIEPL-DFPVIKDLIVDREPYYKKLK-SLRNYLQRKN--------EKITYPEDIEDIKKLRGCIECLSCVSTC 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499383188 165 ATKQMREtFVGAVGMMKIARFELDSRDA--RTAEDFyhvignQDGVFGCMTLLGCQDNCPK--DLPH 227
Cdd:PRK06259 146 PARKVSD-YPGPTFMRQLARFAFDPRDEgdREKEAF------DEGLYNCTTCGKCVEVCPKeiDIPG 205
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-224 5.99e-36

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 127.51  E-value: 5.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   1 MSQGRQLTFNIFRYDPqEPNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACR 80
Cdd:PRK12385   1 MAEMKNLKIEVLRYNP-EVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  81 TLTAKYPKGeITLMPLPGFELIGDLSVNTGKFMRELaERLKLWLhpKANDISIHRLEEPMAPEEAARLYELERCVECGVC 160
Cdd:PRK12385  80 TFLRDYTGG-MKVEALANFPIERDLVVDMTHFIESL-EAIKPYI--IGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLC 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499383188 161 VSACATKQMRETFVGAVGMMKIARFELDSRDARTAEDFyHVIGNQDGVFGCmTLLG-CQDNCPKD 224
Cdd:PRK12385 156 YAACPQFGLNPEFIGPAAITLAHRYNLDSRDHGKKERM-KQLNGQNGVWSC-TFVGyCSEVCPKH 218
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 2-236 1.42e-27

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 105.84  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   2 SQGRQLTFNIFRYDpqEPNDKPKMVRYQLTETPGMTVFIALNKLRE-------EQDTSLQFDFVCRAGICGSCAMVINGF 74
Cdd:PRK08640   1 MSEKTVRLIIKRQD--GPDSKPYWEEFEIPYRPNMNVISALMEIRRnpvnakgEKTTPVVWDMNCLEEVCGACSMVINGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  75 PTLACRTLTAKYPKgEITLMPLPGFELIGDLSVNTGKfMRELAERLKLWlhpkandISI---HRLEE-P-MAPEEAARLY 149
Cdd:PRK08640  79 PRQACTALIDQLEQ-PIRLEPMSTFPVVRDLQVDRSR-MFDNLKRVKAW-------IPIdgtYDLGPgPrMPEEKRQWAY 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 150 ELERCVECGVCVSACATKQMRETFVGAVGMMKIARFELDSRDARTAEDFYHVIGNQDGVFGCMTLLGCQDNCPKDLPHMQ 229
Cdd:PRK08640 150 ELSKCMTCGCCLEACPNVNEKSDFIGPAAISQVRLFNAHPTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTT 229


                 ....*..
gi 499383188 230 QIAYLRR 236
Cdd:PRK08640 230 SIAAMNR 236
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 4-203 4.61e-19

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 83.21  E-value: 4.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   4 GRQLTFNIFRYDpqepNDKPKMVRYQLTETPGMTVFIALNKLREEQDTSLQFDFVCRAGICGSCAMVINGFPTLACRTLT 83
Cdd:PRK12386   2 GYTAKFRVWRGD----ASGGELQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  84 AKYPKGE-ITLMPLPGFELIGDLsVNTGKFMRELAERLKLWLHPKANDISIHRleepMAPEEAARLYELERCVECGVCVS 162
Cdd:PRK12386  78 STFDEDEtVTVTPMRTFPVIRDL-VTDVSFNYEKAREIPSFTPPKDLQPGEYR----MQQVDVERSQEFRKCIECFLCQN 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 499383188 163 ACAT----KQMRETFVGAVGMMKIARFE---LDSRDARTAEDFYHVIG 203
Cdd:PRK12386 153 VCHVvrdhEENKPAFAGPRFLMRIAELEmhpLDTADRRAEAQEEHGLG 200
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 7-236 2.72e-15

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 72.56  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188   7 LTFNIFRydpQE-PNDKPKMVRYQLTE-TPGMTVFIAL----NKLREEQDTSLQFDFVCRAGICGSCAMVINGFP----- 75
Cdd:PRK07570   3 LTLKIWR---QKgPDDKGKFETYEVDDiSPDMSFLEMLdvlnEQLIEKGEEPVAFDHDCREGICGMCGLVINGRPhgpdr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188  76 -TLACRTLTAKYPKGE-ITLMPL--PGFELIGDL-----------------SVNTGKfmrelaerlklwlHPKANDIsih 134
Cdd:PRK07570  80 gTTTCQLHMRSFKDGDtITIEPWraAAFPVIKDLvvdrsaldriiqaggyvSVNTGG-------------APDANAI--- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 135 rleePMAPEEAARLYELERCVECGVCVSAC--ATKQMretFVGAvgmmKIARF--------ELDSR-----DARTAEDFy 199
Cdd:PRK07570 144 ----PVPKEDADRAFDAAACIGCGACVAACpnGSAML---FTGA----KVSHLallpqgqpERARRvramvAQMDEEGF- 211

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 499383188 200 hviGNqdgvfgCMTLLGCQDNCPKDLPhMQQIAYLRR 236
Cdd:PRK07570 212 ---GN------CTNTGECEAVCPKGIS-LENIARMNR 238
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 153-225 5.18e-05

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: 40.37  E-value: 5.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499383188  153 RCVECGVCVSACAT-KQMRETFVGAVGMMKIARfeldsrdartAEDFYHVIGNQDGVFGCMTLLGCQDNCPKDL 225
Cdd:pfam13183   1 RCIRCGACLAACPVyLVTGGRFPGDPRGGAAAL----------LGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 150-240 2.52e-04

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 41.60  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499383188 150 ELERCVECGVCVSAC-ATKQMRETFVGAVGMMKIARFELDSRDARTAEDFYHvignqDGVFGCMTLLGCQDNCPKDLPHM 228
Cdd:COG0247   76 ALDACVGCGFCRAMCpSYKATGDEKDSPRGRINLLREVLEGELPLDLSEEVY-----EVLDLCLTCKACETACPSGVDIA 150

                         90
                 ....*....|..
gi 499383188 229 QQIAYLRRKMAM 240
Cdd:COG0247  151 DLIAEARAQLVE 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH