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Conserved domains on  [gi|257696596|emb|CBC48638|]
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unnamed protein product [Arabidopsis thaliana]

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 257696596   1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPM 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI-QDEASETTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129  75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIdRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 257696596 240 EAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQLQR 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 257696596   1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPM 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI-QDEASETTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129  75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIdRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 257696596 240 EAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
51-276 8.83e-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: 344.42  E-value: 8.83e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNPGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:COG0479    4 TLKIWRQDPETDSKPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 131 SETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWN 210
Cdd:COG0479   83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPA--PDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257696596 211 PEsYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQ 276
Cdd:COG0479  161 PD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKR 225
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
54-275 9.97e-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: 313.60  E-value: 9.97e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596   54 IYRWNPDNPGKPELQNYQIDLKDCgPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEASET 133
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  134 -TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTpASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPE 212
Cdd:TIGR00384  80 mKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKS-QPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257696596  213 sYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIK 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 2.02e-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: 156.24  E-value: 2.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596   51 TFQIYRWNPDNP-GKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQD- 128
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDl 79
                          90       100
                  ....*....|....*....|....*...
gi 257696596  129 EASETTITPLPHMFVIKDLVVDMTNFYN 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 257696596   1 MASGLIGRLVGTKPSKLAtaarliPARWTSTGAEAETKASSGGGRGSNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPM 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLA------PAAAASAAASAETKASSKGSKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  81 VLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI-QDEASETTITPLPHMFVIKDLVVDMTNFYNQYK 159
Cdd:PLN00129  75 VLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIdRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 160 SIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYLGPAALLHANRWISDSRDEYTKERL 239
Cdd:PLN00129 155 SIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERL 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 257696596 240 EAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQLQR 279
Cdd:PLN00129 235 EALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
51-277 6.78e-156

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 433.45  E-value: 6.78e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNPGKPELQNYQIDLKDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 131 SET-TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWW 209
Cdd:PRK05950  81 KGKiVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPP--PARERLQSPEDREKLDGLYECILCACCSTSCPSFWW 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257696596 210 NPESYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQL 277
Cdd:PRK05950 159 NPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRM 226
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
51-276 8.83e-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: 344.42  E-value: 8.83e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNPGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:COG0479    4 TLKIWRQDPETDSKPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 131 SETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWN 210
Cdd:COG0479   83 DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPA--PDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257696596 211 PEsYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQ 276
Cdd:COG0479  161 PD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKR 225
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
54-275 9.97e-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: 313.60  E-value: 9.97e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596   54 IYRWNPDNPGKPELQNYQIDLKDCgPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEASET 133
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  134 -TITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTpASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPE 212
Cdd:TIGR00384  80 mKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKS-QPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257696596  213 sYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIK 275
Cdd:TIGR00384 159 -FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
47-277 2.48e-103

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 300.72  E-value: 2.48e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  47 SNLKTFQIYRWNPDNPGKPELQNYQIDLKDCGPMVLDALIKIKNEmDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKI 126
Cdd:PRK12575   2 ADTRILHIYRYDPDDDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 127 QDEASETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPAsvPAKEILQSKKDRAKLDGMYECILCACCSTSCPS 206
Cdd:PRK12575  81 QALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVP--PERERLQTPQEREQLDGLYECILCACCSTACPS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257696596 207 YWWNPESYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIKQL 277
Cdd:PRK12575 159 YWWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTM 229
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
51-276 1.59e-64

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 204.93  E-value: 1.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNPgkPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLAC-------L 123
Cdd:PRK12577   4 LFKILRQKQNSA--PYVQTYTLEV-EPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvgseL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 124 TKIQDEAS----ETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPaSVPAKEILQSKKDRAKLDGMYECILCAC 199
Cdd:PRK12577  81 ARLSDSNSgaipEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAAR-QVPEREFLQTPEERSKLDQTGNCILCGA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257696596 200 CSTSCPSYWWNPEsYLGPAALLHANRWISDSRDEYTKERLEAID-DEFKLYRCHTILNCARACPKGLNPGKQITHIKQ 276
Cdd:PRK12577 160 CYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQ 236
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
51-279 3.34e-56

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 182.26  E-value: 3.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDnpGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK12576  10 IFKVKRYDPE--KGSWWQEYKVKV-DRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVLDVA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 131 SE----TTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPS 206
Cdd:PRK12576  87 KKynsvITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACPV 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257696596 207 YWWNPEsYLGPAALLHANRWISDSRDEYTKERLEAIDDefKLYRCHTILNCARACPKGLNPGkqiTHIKQLQR 279
Cdd:PRK12576 167 VAIDPE-FLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPV---TAIKKTRS 233
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
51-156 2.02e-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: 156.24  E-value: 2.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596   51 TFQIYRWNPDNP-GKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQD- 128
Cdd:pfam13085   1 TLRVFRYDPRVDrDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDl 79
                          90       100
                  ....*....|....*....|....*...
gi 257696596  129 EASETTITPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
51-275 5.76e-48

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 159.87  E-value: 5.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNPGKPELQNYQIDLkDCGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK12385   8 KIEVLRYNPEVDTEPHSQTYEVPY-DETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 131 SETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWL--KRKTPASVPAKeilQSKKDRAKLDGMYECILCACCSTSCPSYW 208
Cdd:PRK12385  87 GGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIigNDRTPDDGPNK---QTPAQMAKYHQFSGCINCGLCYAACPQFG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257696596 209 WNPEsYLGPAALLHANRWISDSRDEYTKERLEAIDDEFKLYRCHTILNCARACPKGLNPGKQITHIK 275
Cdd:PRK12385 164 LNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
51-271 1.40e-41

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 143.17  E-value: 1.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNPG-KPELQNYQIDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQD- 128
Cdd:PRK13552   6 TFNIFRYNPQDPGsKPHMVTYQLEETP-GMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSDy 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 129 EASETTITPLPHMFVIKDLVVDMTNFYNQ-YKSIEPWLKRKTPASVPAKEilqSKKDRAKLDGMYE---CILCACCSTSC 204
Cdd:PRK13552  85 PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRLE---ERMEPEEADEIYEldrCIECGCCVAAC 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257696596 205 PSYWWNPeSYLGPAALLHANRWISDSRDEYTKERL-EAIDDEFKLYRCHTILNCARACPKGLNPGKQI 271
Cdd:PRK13552 162 GTKQMRE-DFVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQI 228
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
51-271 1.14e-38

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 141.30  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNPDNpGKPELQNYQIDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQDEA 130
Cdd:PRK06259   5 TITVKRFDPEK-DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 131 setTITPLpHMFVIKDLVVDMTNFYNQYKSIEPWLKRKTPASVPAKEILQSKKDRakldgmyECILCACCSTSCPSYwwN 210
Cdd:PRK06259  83 ---IIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKITYPEDIEDIKKLR-------GCIECLSCVSTCPAR--K 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257696596 211 PESYLGPAALLHANRWISDSRDEYTKERlEAIDDefKLYRCHTILNCARACPKGLN-PGKQI 271
Cdd:PRK06259 150 VSDYPGPTFMRQLARFAFDPRDEGDREK-EAFDE--GLYNCTTCGKCVEVCPKEIDiPGKAI 208
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
51-265 1.98e-18

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 82.05  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596  51 TFQIYRWNpDNPGkpELQNYQIDLKDcGPMVLDALIKIKNEMDPSLTFRRSCREGICGSCAMNIDGCNGLACLTKIQ--D 128
Cdd:PRK12386   6 KFRVWRGD-ASGG--ELQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMStfD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 129 EASETTITPLPHMFVIKDLVVDMTnfYNQYKSiepwlkRKTPASVPAK-----EILQSKKDRAKLDGMYECILCACCSTS 203
Cdd:PRK12386  82 EDETVTVTPMRTFPVIRDLVTDVS--FNYEKA------REIPSFTPPKdlqpgEYRMQQVDVERSQEFRKCIECFLCQNV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257696596 204 C---PSYWWNPESYLGPAALLHANRWISDSRDeyTKERLEAIDDEFKLYRCHTILNCARACPKGL 265
Cdd:PRK12386 154 ChvvRDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
102-265 1.42e-17

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 79.65  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 102 CREGICGSCAMNIDGCNGLACLTKIQDEASETTITPLPHMFVIKDLVVDMTNFYNQYKSIEPWLK-RKTPASVPAKEILQ 180
Cdd:PRK08640  63 CLEEVCGACSMVINGKPRQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPiDGTYDLGPGPRMPE 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 181 SKKDRakldgMYE---CILCACCSTSCPSYwwNPES-YLGPAAllhanrwISDSR--------DEYTKERLEAIDDEFKL 248
Cdd:PRK08640 143 EKRQW-----AYElskCMTCGCCLEACPNV--NEKSdFIGPAA-------ISQVRlfnahptgEMHKEERLRALMGDGGI 208
                        170
                 ....*....|....*..
gi 257696596 249 YRCHTILNCARACPKGL 265
Cdd:PRK08640 209 ADCGNAQNCVRVCPKGI 225
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
193-266 5.67e-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: 45.92  E-value: 5.67e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257696596  193 ECILCACCSTSCPSYWWNPESylgPAALlhANRWISdsrdeytkERLEAIDDEFKLYRCHTILNCARACPKGLN 266
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKL--MRAAYL--------GDLEELQANKVANLCSECGLCEYACPMGLD 61
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
102-279 2.19e-06

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 47.90  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 102 CREGICGSCAMNIDGC------NGLAC---LTKIQDeASETTITP-----LPhmfVIKDLVVDMTNF-----YNQYKSIe 162
Cdd:PRK07570  58 CREGICGMCGLVINGRphgpdrGTTTCqlhMRSFKD-GDTITIEPwraaaFP---VIKDLVVDRSALdriiqAGGYVSV- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 163 pwlkrKTPASVPAKEILQSKK--DRAkLDGMyECILCACCSTSCPsywwNPESYLGPAA------LLHANRwisDSRDEY 234
Cdd:PRK07570 133 -----NTGGAPDANAIPVPKEdaDRA-FDAA-ACIGCGACVAACP----NGSAMLFTGAkvshlaLLPQGQ---PERARR 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 257696596 235 TKERLEAIDDE-FKlyRCHTILNCARACPKGLNpgkqITHIKQLQR 279
Cdd:PRK07570 199 VRAMVAQMDEEgFG--NCTNTGECEAVCPKGIS----LENIARMNR 238
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
194-265 2.62e-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: 2.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257696596  194 CILCACCSTSCPSYwwnpesylgpaaLLHANRWISDSRDEYTKERLEA---IDDEFKLYRCHTILNCARACPKGL 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 1.55e-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: 38.77  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257696596  194 CILCACCSTSCPSYWWnpesylgpaallhanrwisdsRDEYTKERLEAIDDEFKLYRCHTILNCARACP 262
Cdd:pfam13237   9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
137-269 7.90e-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: 37.36  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257696596 137 PLPHMFVIKDLVVDMTNFYNQYKSIEPW-LKRKTPASVPAKEILQSKKDRAKLDGMYECILCACCSTSCPSYWWNPESYL 215
Cdd:COG0247   22 FLELELGKIKYAFDPDNKLNPGKIGLLNpGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKD 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 257696596 216 GP---AALLhanrwisdsRDEYTKERLEAIDDEFK--LYRCHTILNCARACPKGLNPGK 269
Cdd:COG0247  102 SPrgrINLL---------REVLEGELPLDLSEEVYevLDLCLTCKACETACPSGVDIAD 151
 
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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