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Conserved domains on  [gi|1490217497|gb|RKY90018|]
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succinate dehydrogenase iron-sulfur subunit [candidate division KSB1 bacterium]

Protein Classification

succinate dehydrogenase/fumarate reductase iron-sulfur subunit( domain architecture ID 11422279)

succinate dehydrogenase/fumarate reductase iron-sulfur subunit similar to the iron-sulfur subunit of Wolinella succinogenes 8-methylmenaquinol:fumarate reductase, which catalyzes the reduction of fumarate using 8-methylmenaquinol-6 as the electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 2-230 1.47e-122

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: 347.50  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   2 EKVIFKVFRFNPERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINR 81
Cdd:COG0479     1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  82 LKsKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDT 161
Cdd:COG0479    81 LK-DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490217497 162 EKNYLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAI 230
Cdd:COG0479   160 NPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
 
Name Accession Description Interval E-value
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 2-230 1.47e-122

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: 347.50  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   2 EKVIFKVFRFNPERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINR 81
Cdd:COG0479     1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  82 LKsKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDT 161
Cdd:COG0479    81 LK-DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490217497 162 EKNYLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAI 230
Cdd:COG0479   160 NPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 6-230 1.39e-119

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 339.85  E-value: 1.39e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   6 FKVFRFNPERDKKPRFDKYEVPIRN-GMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLKS 84
Cdd:PRK05950    2 FKIYRYNPDVDANPRMQTYEVDVDEcGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  85 KKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDTEKN 164
Cdd:PRK05950   82 GKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWNPD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490217497 165 -YLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAI 230
Cdd:PRK05950  162 kFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLL 228
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 8-226 8.50e-102

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: 294.34  E-value: 8.50e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   8 VFRFNPERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLKSKKI 87
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  88 TIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIA-GAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDTEKNYL 166
Cdd:TIGR00384  81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRkSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497 167 GPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLK 226
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-110 4.37e-51

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: 161.64  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   5 IFKVFRFNPERDKK-PRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLK 83
Cdd:pfam13085   1 TLRVFRYDPRVDRDePYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 1490217497  84 SKKITIKPLGHLPVIKDLVVDMTDFWE 110
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 22-77 6.73e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 43.15  E-value: 6.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490217497  22 DKYEVPIRNGMTVLDALyyiqgyLDGSLAFRSSCREGVCGSCGMHIN------------------GKYRLACET 77
Cdd:cd00207     8 SGVEVEVPEGETLLDAA------REAGIDIPYSCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQT 75
 
Name Accession Description Interval E-value
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 2-230 1.47e-122

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: 347.50  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   2 EKVIFKVFRFNPERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINR 81
Cdd:COG0479     1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  82 LKsKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDT 161
Cdd:COG0479    81 LK-DTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490217497 162 EKNYLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAI 230
Cdd:COG0479   160 NPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 6-230 1.39e-119

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 339.85  E-value: 1.39e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   6 FKVFRFNPERDKKPRFDKYEVPIRN-GMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLKS 84
Cdd:PRK05950    2 FKIYRYNPDVDANPRMQTYEVDVDEcGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  85 KKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDTEKN 164
Cdd:PRK05950   82 GKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWNPD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490217497 165 -YLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAI 230
Cdd:PRK05950  162 kFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLL 228
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 8-226 8.50e-102

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: 294.34  E-value: 8.50e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   8 VFRFNPERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLKSKKI 87
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQPVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  88 TIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIA-GAPPEENERIQTQDDRNKLDGLIDCILCACCYAACTITDTEKNYL 166
Cdd:TIGR00384  81 KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRkSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497 167 GPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLK 226
Cdd:TIGR00384 161 GPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 6-228 6.07e-89

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 263.96  E-value: 6.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   6 FKVFRFNPERDKKPRFDKYEVPIRN-GMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLKS 84
Cdd:PLN00129   46 FQIYRWNPDNPGKPHLQSYKVDLNDcGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDES 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  85 KKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEEN--ERIQTQDDRNKLDGLIDCILCACCYAACTIT--D 160
Cdd:PLN00129  126 GPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDGqkEHLQSKEDRAKLDGMYECILCACCSTSCPSYwwN 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490217497 161 TEKnYLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRM 228
Cdd:PLN00129  206 PEK-FLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQL 272
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-226 4.84e-77

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 232.67  E-value: 4.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   1 MEKVIFKVFRFNPERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQIn 80
Cdd:PRK12385    4 MKNLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFL- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  81 RLKSKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAG-APPEENERIQTQDDRNKLDGLIDCILCACCYAACTIT 159
Cdd:PRK12385   83 RDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNdRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQF 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490217497 160 DTEKNYLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLK 226
Cdd:PRK12385  163 GLNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
5-234 5.15e-76

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 229.85  E-value: 5.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   5 IFKVFRFNPERDKKPRFDKYEVPIRNG-MTVLDALYYIQgYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLk 83
Cdd:PRK12575    6 ILHIYRYDPDDDAAPRMQRYEIAPRAEdRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQAL- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  84 SKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEENERIQTQDDRNKLDGLIDCILCACCYAAC-TITDTE 162
Cdd:PRK12575   84 PREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPPERERLQTPQEREQLDGLYECILCACCSTACpSYWWNP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490217497 163 KNYLGPAALLKVDRFVEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAISNTL 234
Cdd:PRK12575  164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLARRAV 235
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-227 9.30e-71

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 217.69  E-value: 9.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   1 MEKVIFKVFRFNPErdKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQIN 80
Cdd:PRK12576    6 EKEVIFKVKRYDPE--KGSWWQEYKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  81 RLKSKK---ITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIAGAPPEEN--ERIQTQDDRNKLDGLIDCILCACCYAA 155
Cdd:PRK12576   84 DVAKKYnsvITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGkaEHRLKPEDQKELWKFAQCIWCGLCVSA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490217497 156 CTITDTEKNYLGPAALLKVDRFVEDSRDNNKKERLLTVsgDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKR 227
Cdd:PRK12576  164 CPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-226 3.67e-69

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 215.33  E-value: 3.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   1 MEkVIFKVFRFNPerDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLAC----E 76
Cdd:PRK12577    1 ME-VLFKILRQKQ--NSAPYVQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  77 TQINRLKSK------KITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYL-IAGAPPEENERIQTQDDRNKLDGLIDCILC 149
Cdd:PRK12577   78 SELARLSDSnsgaipEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVsTAARQVPEREFLQTPEERSKLDQTGNCILC 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490217497 150 ACCYAACTITDTEKNYLGPAALLKVDRFVEDSRDNNKKERL-LTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARLK 226
Cdd:PRK12577  158 GACYSECNAREVNPEFVGPHALAKAQRMVADSRDTATEQRLeLYNQGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 1-229 4.11e-56

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 185.98  E-value: 4.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   1 MEKVIFKVFRFNPERDKkPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQIN 80
Cdd:PRK06259    1 MKMITITVKRFDPEKDE-PHFESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  81 rlksKKITIKPLgHLPVIKDLVVDMTDFWEKYSYIKPYLIAgappeENERIQTQDDRNKLDGLIDCILCACCYAACTITd 160
Cdd:PRK06259   80 ----DGMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQR-----KNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497 161 TEKNYLGPAALLKVDRFVEDSRDNNKKERlltVSGDSGIFRCHTLFNCQEVCPKNLD-PTGAIARLKRMA 229
Cdd:PRK06259  149 KVSDYPGPTFMRQLARFAFDPRDEGDREK---EAFDEGLYNCTTCGKCVEVCPKEIDiPGKAIEKLRALA 215
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-110 4.37e-51

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: 161.64  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   5 IFKVFRFNPERDKK-PRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINRLK 83
Cdd:pfam13085   1 TLRVFRYDPRVDRDePYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 1490217497  84 SKKITIKPLGHLPVIKDLVVDMTDFWE 110
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 3-230 1.67e-49

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 162.04  E-value: 1.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   3 KVIFKVFRFNP-ERDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQINR 81
Cdd:PRK13552    4 TLTFNIFRYNPqDPGSKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  82 LKSKKITIKPLGHLPVIKDLVVD----MTDFWEKY-SYIKP-------YLIAGAPPEENERIqTQDDRnkldglidCILC 149
Cdd:PRK13552   84 YPDGVITLMPLPVFKLIGDLSVNtgkwFREMSERVeSWIHTdkefdihRLEERMEPEEADEI-YELDR--------CIEC 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497 150 ACCYAACTITDTEKNYLGPAALLKVDRFVEDSRDNNKKERLLTVSG-DSGIFRCHTLFNCQEVCPKNLDPTGAIARLKR- 227
Cdd:PRK13552  155 GCCVAACGTKQMREDFVGAVGLNRIARFELDPRDERTDEDFYELIGnDDGVFGCMSLLGCEDNCPKDLPLQQQIAYLRRk 234


                  ...
gi 1490217497 228 MAI 230
Cdd:PRK13552  235 MAA 237
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 1-227 1.28e-35

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 126.64  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   1 MEKVI-FKVFRFNPErDKKPRFDKYEVPIRNGMTVLDALYYIQ-------GYLDGSLAFRSSCREGVCGSCGMHINGKYR 72
Cdd:PRK08640    2 SEKTVrLIIKRQDGP-DSKPYWEEFEIPYRPNMNVISALMEIRrnpvnakGEKTTPVVWDMNCLEEVCGACSMVINGKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  73 LACETQINRLkSKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYLIA------GAPPEENERiqtqdDRNKLDGLIDC 146
Cdd:PRK08640   81 QACTALIDQL-EQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIdgtydlGPGPRMPEE-----KRQWAYELSKC 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497 147 ILCACCYAACTITDTEKNYLGPAALLKVDRF-VEDSRDNNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNLDPTGAIARL 225
Cdd:PRK08640  155 MTCGCCLEACPNVNEKSDFIGPAAISQVRLFnAHPTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAAM 234


                  ..
gi 1490217497 226 KR 227
Cdd:PRK08640  235 NR 236
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 1-226 1.48e-30

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 113.64  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   1 MEKVIFKVFRFNperDKKPRFDKYEVPIRNGMTVLDALYYIQGYLDGSLAFRSSCREGVCGSCGMHINGKYRLACETQIN 80
Cdd:PRK12386    2 GYTAKFRVWRGD---ASGGELQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  81 RL-KSKKITIKPLGHLPVIKDLVVDMTDFWEKYSYIKPYliagAPPEENE----RIQtQDDRNKLDGLIDCILCACCYAA 155
Cdd:PRK12386   79 TFdEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSF----TPPKDLQpgeyRMQ-QVDVERSQEFRKCIECFLCQNV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490217497 156 C-TITDTEKN---YLGPAALLKV---DRFVEDSRDnnkkeRLLTVSGDSGIFRCHTLFNCQEVCPKNLDPT-GAIARLK 226
Cdd:PRK12386  154 ChVVRDHEENkpaFAGPRFLMRIaelEMHPLDTAD-----RRAEAQEEHGLGYCNITKCCTEVCPEHIKITdNALIPMK 227
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 3-227 1.72e-15

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 73.33  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497   3 KVIFKVFRfNPERDKKPRFDKYEVP-IRNGMTVLDAL------YYIQGylDGSLAFRSSCREGVCGSCGMHING------ 69
Cdd:PRK07570    2 KLTLKIWR-QKGPDDKGKFETYEVDdISPDMSFLEMLdvlneqLIEKG--EEPVAFDHDCREGICGMCGLVINGrphgpd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497  70 KYRLACETQINRLKS-KKITIKPL--GHLPVIKDLVVDMTDF---WEKYSYIKpyLIAGAPPEENERIQTQDDrnkLDGL 143
Cdd:PRK07570   79 RGTTTCQLHMRSFKDgDTITIEPWraAAFPVIKDLVVDRSALdriIQAGGYVS--VNTGGAPDANAIPVPKED---ADRA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490217497 144 ID---CILCACCYAACtitdteKNylGPAALL---KVDRF-------VEdsrdnnKKERLLTVSG--DSGIF-RCHTLFN 207
Cdd:PRK07570  154 FDaaaCIGCGACVAAC------PN--GSAMLFtgaKVSHLallpqgqPE------RARRVRAMVAqmDEEGFgNCTNTGE 219

                         250       260
                  ....*....|....*....|
gi 1490217497 208 CQEVCPKNLdPTGAIARLKR 227
Cdd:PRK07570  220 CEAVCPKGI-SLENIARMNR 238
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
185-230 4.20e-06

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 43.74  E-value: 4.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1490217497 185 NKKERLLTvsgDSGIFRCHTLFNCQEVCPKNLDPTGAIARLKRMAI 230
Cdd:COG1150    35 GLKEEVLK---SDSIWLCVSCYTCTERCPRGIDIADVMDALRNLAI 77
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 22-77 6.73e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 43.15  E-value: 6.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490217497  22 DKYEVPIRNGMTVLDALyyiqgyLDGSLAFRSSCREGVCGSCGMHIN------------------GKYRLACET 77
Cdd:cd00207     8 SGVEVEVPEGETLLDAA------REAGIDIPYSCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQT 75
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 146-216 1.19e-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: 41.91  E-value: 1.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490217497 146 CILCACCYAACtitdteknylgPAALLKVDRFVEDSRD---NNKKERLLTVSGDSGIFRCHTLFNCQEVCPKNL 216
Cdd:pfam13183   2 CIRCGACLAAC-----------PVYLVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
Fdx COG0633
Ferredoxin [Energy production and conversion];
22-63 7.03e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 37.52  E-value: 7.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1490217497  22 DKYEVPIRNGMTVLDALyyiqgyLDGSLAFRSSCREGVCGSC 63
Cdd:COG0633     9 EGHTVEVPAGESLLEAA------LRAGIDLPYSCRSGACGTC 44
 
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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