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Conserved domains on  [gi|297322885|gb|EFH53306|]
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succinate dehydrogenase 2-1 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 11476389)

quinone-dependent succinate dehydrogenase iron-sulfur subunit is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-279 0e+00

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


:

Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 555.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELKDYQVDLKDCGPM 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIE-DGSSGTTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129  75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDrDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 297322885 240 EAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-279 0e+00

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 555.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELKDYQVDLKDCGPM 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIE-DGSSGTTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129  75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDrDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 297322885 240 EAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 51-276 4.73e-121

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: 345.19  E-value: 4.73e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNPGKPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIEDGS 130
Cdd:COG0479    4 TLKIWRQDPETDSKPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 131 SGTTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWN 210
Cdd:COG0479   83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPA--PDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297322885 211 PEsYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQ 276
Cdd:COG0479  161 PD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKR 225
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 54-275 1.36e-109

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: 315.91  E-value: 1.36e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   54 IYRWNPDNPGKPELKDYQVDLKDCgPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIED-GSSG 132
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDlGQPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  133 TTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTpASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPE 212
Cdd:TIGR00384  80 MKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKS-QPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297322885  213 sYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIK 275
Cdd:TIGR00384 159 -FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 51-156 7.33e-48

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: 154.70  E-value: 7.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   51 TFQIYRWNPDNP-GKPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIED- 128
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDl 79

                          90       100
                  ....*....|....*....|....*...
gi 297322885  129 GSSGTTITPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-279 0e+00

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 555.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELKDYQVDLKDCGPM 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIE-DGSSGTTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129  75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDrDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 297322885 240 EAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 51-277 2.15e-157

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 437.30  E-value: 2.15e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNPGKPELKDYQVDLKDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIEDGS 130
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 131 SGT-TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWW 209
Cdd:PRK05950  81 KGKiVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPP--PARERLQSPEDREKLDGLYECILCACCSTSCPSFWW 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297322885 210 NPESYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQL 277
Cdd:PRK05950 159 NPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRM 226
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 51-276 4.73e-121

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: 345.19  E-value: 4.73e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNPGKPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIEDGS 130
Cdd:COG0479    4 TLKIWRQDPETDSKPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 131 SGTTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWN 210
Cdd:COG0479   83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPA--PDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297322885 211 PEsYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQ 276
Cdd:COG0479  161 PD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKR 225
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 54-275 1.36e-109

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: 315.91  E-value: 1.36e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   54 IYRWNPDNPGKPELKDYQVDLKDCgPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIED-GSSG 132
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDlGQPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  133 TTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTpASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPE 212
Cdd:TIGR00384  80 MKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKS-QPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297322885  213 sYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIK 275
Cdd:TIGR00384 159 -FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
47-277 2.59e-100

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 293.02  E-value: 2.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  47 SNLKTFQIYRWNPDNPGKPELKDYQVDLKDCGPMVLDALIKIKNEmDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI 126
Cdd:PRK12575   2 ADTRILHIYRYDPDDDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 127 EDGSSGTTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPS 206
Cdd:PRK12575  81 QALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVP--PERERLQTPQEREQLDGLYECILCACCSTACPS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297322885 207 YWWNPESYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIKQL 277
Cdd:PRK12575 159 YWWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTM 229
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
51-276 2.18e-62

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 199.54  E-value: 2.18e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNPgkPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLAC-------L 123
Cdd:PRK12577   4 LFKILRQKQNSA--PYVQTYTLEV-EPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvgseL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 124 TKIEDGSSGT----TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPaSVPAKEILQSKKDRAKLDGMYECILCAC 199
Cdd:PRK12577  81 ARLSDSNSGAipeiTIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAAR-QVPEREFLQTPEERSKLDQTGNCILCGA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297322885 200 CSTSCPSYWWNPEsYLGPAALLHANRWISDSRDEYTKERLEAVD-DEFKLYRCHTILNCARACPKGLNPGKQIAHIKQ 276
Cdd:PRK12577 160 CYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQ 236
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
51-271 1.43e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 180.33  E-value: 1.43e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDnpGKPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTK----I 126
Cdd:PRK12576  10 IFKVKRYDPE--KGSWWQEYKVKV-DRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLvldvA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 127 EDGSSGTTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPS 206
Cdd:PRK12576  87 KKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACPV 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297322885 207 YWWNPEsYLGPAALLHANRWISDSRDEYTKERLEAVDDefKLYRCHTILNCARACPKGLNPGKQI 271
Cdd:PRK12576 167 VAIDPE-FLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAI 228
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
51-271 1.94e-48

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 161.02  E-value: 1.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNPGKPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIEDGS 130
Cdd:PRK12385   8 KIEVLRYNPEVDTEPHSQTYEVPY-DETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 131 SGTTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWL--KRKTPASVPAKeilQSKKDRAKLDGMYECILCACCSTSCPSYW 208
Cdd:PRK12385  87 GGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIigNDRTPDDGPNK---QTPAQMAKYHQFSGCINCGLCYAACPQFG 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297322885 209 WNPEsYLGPAALLHANRWISDSRDEYTKERLEAVDDEFKLYRCHTILNCARACPKGLNPGKQI 271
Cdd:PRK12385 164 LNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAI 225
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 51-156 7.33e-48

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: 154.70  E-value: 7.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885   51 TFQIYRWNPDNP-GKPELKDYQVDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIED- 128
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDl 79

                          90       100
                  ....*....|....*....|....*...
gi 297322885  129 GSSGTTITPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 51-275 9.03e-42

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 143.55  E-value: 9.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNPG-KPELKDYQVDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIEDG 129
Cdd:PRK13552   6 TFNIFRYNPQDPGsKPHMVTYQLEETP-GMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSDY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 130 SSGT-TITPLPHMFVIKDLVVDMTNFYNQ-YKSIEPWLKRKTPASVPAKEilqSKKDRAKLDGMYE---CILCACCSTSC 204
Cdd:PRK13552  85 PDGViTLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRLE---ERMEPEEADEIYEldrCIECGCCVAAC 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297322885 205 PSYWWNPeSYLGPAALLHANRWISDSRDEYTKERL-EAVDDEFKLYRCHTILNCARACPKGLNPGKQIAHIK 275
Cdd:PRK13552 162 GTKQMRE-DFVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQIAYLR 232
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 51-271 9.92e-41

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 146.69  E-value: 9.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNPDNpGKPELKDYQVDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIEDgs 130
Cdd:PRK06259   5 TITVKRFDPEK-DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVED-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 131 sGTTITPLpHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPASVPAKEILQSKKDRakldgmyECILCACCSTSCPSYwwN 210
Cdd:PRK06259  81 -GMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKITYPEDIEDIKKLR-------GCIECLSCVSTCPAR--K 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297322885 211 PESYLGPAALLHANRWISDSRDEYTKERlEAVDDefKLYRCHTILNCARACPKGLN-PGKQI 271
Cdd:PRK06259 150 VSDYPGPTFMRQLARFAFDPRDEGDREK-EAFDE--GLYNCTTCGKCVEVCPKEIDiPGKAI 208
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 51-265 1.47e-19

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 85.14  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRWNpDNPGkpELKDYQVDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIE--D 128
Cdd:PRK12386   6 KFRVWRGD-ASGG--ELQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMStfD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 129 GSSGTTITPLPHMFVIKDLVVDMTnfYNQYKSiepwlkRKTPASVPAK-----EILQSKKDRAKLDGMYECILCACCSTS 203
Cdd:PRK12386  82 EDETVTVTPMRTFPVIRDLVTDVS--FNYEKA------REIPSFTPPKdlqpgEYRMQQVDVERSQEFRKCIECFLCQNV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297322885 204 C---PSYWWNPESYLGPAALLHANRWISDSRDeyTKERLEAVDDEFKLYRCHTILNCARACPKGL 265
Cdd:PRK12386 154 ChvvRDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 102-274 4.57e-17

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 78.49  E-value: 4.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 102 CREGICGSCAMNIDGCNGLACLTKIEDGSSGTTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLK-RKTPASVPAKEILQ 180
Cdd:PRK08640  63 CLEEVCGACSMVINGKPRQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPiDGTYDLGPGPRMPE 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 181 SKKDRakldgMYE---CILCACCSTSCPSYwwNPES-YLGPAAllhanrwISDSR--------DEYTKERLEAVDDEFKL 248
Cdd:PRK08640 143 EKRQW-----AYElskCMTCGCCLEACPNV--NEKSdFIGPAA-------ISQVRlfnahptgEMHKEERLRALMGDGGI 208

                        170       180
                 ....*....|....*....|....*.
gi 297322885 249 YRCHTILNCARACPKGLNPGKQIAHI 274
Cdd:PRK08640 209 ADCGNAQNCVRVCPKGIPLTTSIAAM 234
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 51-279 8.35e-08

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 51.76  E-value: 8.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885  51 TFQIYRW-NPDNPGKpeLKDYQVDlkDCGP-M----VLDALikikNEM------DPsLTFRRSCREGICGSCAMNIDGC- 117
Cdd:PRK07570   4 TLKIWRQkGPDDKGK--FETYEVD--DISPdMsfleMLDVL----NEQliekgeEP-VAFDHDCREGICGMCGLVINGRp 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 118 -----NGLACLTKIEDGSSGTTIT-------PLPhmfVIKDLVVDMTNF-----YNQYKSIepwlkrKTPASVPAKEILQ 180
Cdd:PRK07570  75 hgpdrGTTTCQLHMRSFKDGDTITiepwraaAFP---VIKDLVVDRSALdriiqAGGYVSV------NTGGAPDANAIPV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 181 SKK--DRAkLDGMyECILCACCSTSCPsywwNPESYLGPAA------LLHANRwisDSRDEYTKERLEAVDDE-FKlyRC 251
Cdd:PRK07570 146 PKEdaDRA-FDAA-ACIGCGACVAACP----NGSAMLFTGAkvshlaLLPQGQ---PERARRVRAMVAQMDEEgFG--NC 214

                        250       260
                 ....*....|....*....|....*...
gi 297322885 252 HTILNCARACPKGLNpgkqIAHIKQLQR 279
Cdd:PRK07570 215 TNTGECEAVCPKGIS----LENIARMNR 238
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 193-266 3.82e-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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 46.30  E-value: 3.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297322885  193 ECILCACCSTSCPSYWWNPESylgPAALlhANRWISdsrdeytkERLEAVDDEFKLYRCHTILNCARACPKGLN 266
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKL--MRAAYL--------GDLEELQANKVANLCSECGLCEYACPMGLD 61
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 194-265 2.32e-06

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 44.22  E-value: 2.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297322885  194 CILCACCSTSCPSYwwnpesylgpaaLLHANRWISDSRDEYTKERLEAV---DDEFKLYRCHTILNCARACPKGL 265
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRLEaleGLAEGLWLCTLCGACTEVCPVGI 64
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 194-262 3.92e-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: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 37.62  E-value: 3.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297322885  194 CILCACCSTSCPSYWWnpesylgpaallhanrwisdsRDEYTKERLEAVDDEFKLYRCHTILNCARACP 262
Cdd:pfam13237   9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 137-278 6.55e-03

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 37.75  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297322885 137 PLPHMFVIKDLVVDMTNFYNQYKSIEPW-LKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYL 215
Cdd:COG0247   22 FLELELGKIKYAFDPDNKLNPGKIGLLNpGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKD 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297322885 216 GPAALLHANRWISdsRDEYTKERLEAVDDEfkLYRCHTILNCARACPKGLNPGKQIAHIKQLQ 278
Cdd:COG0247  102 SPRGRINLLREVL--EGELPLDLSEEVYEV--LDLCLTCKACETACPSGVDIADLIAEARAQL 160
 
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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