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Conserved domains on  [gi|2431519332|ref|YP_010620151|]
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Succinate dehydrogenase subunit 2 (mitochondrion) [Herposiphonia versicolor]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 1001168)

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

CATH:  1.10.1060.10|3.10.20.30
EC:  1.3.5.1
Gene Ontology:  GO:0046872|GO:0009055|GO:0051536|GO:0008177|GO:0048039

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN00129 super family cl33415
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 18-246 4.46e-103

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


The actual alignment was detected with superfamily member PLN00129:

Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 300.55  E-value: 4.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  18 NSNFFYIRIYRWNPYLSLKPWFNIFPLKLQiNSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLN 97
Cdd:PLN00129   40 PSNLKEFQIYRWNPDNPGKPHLQSYKVDLN-DCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLT 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  98 KFSLSNSQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRK---ENFKQEILQSKIDRFELDGLYECILCACCSSS 174
Cdd:PLN00129  119 KIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKkppEDGQKEHLQSKEDRAKLDGMYECILCACCSTS 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2431519332 175 CPSYWWNYQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:PLN00129  199 CPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 18-246 4.46e-103

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 300.55  E-value: 4.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  18 NSNFFYIRIYRWNPYLSLKPWFNIFPLKLQiNSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLN 97
Cdd:PLN00129   40 PSNLKEFQIYRWNPDNPGKPHLQSYKVDLN-DCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLT 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  98 KFSLSNSQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRK---ENFKQEILQSKIDRFELDGLYECILCACCSSS 174
Cdd:PLN00129  119 KIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKkppEDGQKEHLQSKEDRAKLDGMYECILCACCSTS 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2431519332 175 CPSYWWNYQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:PLN00129  199 CPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 24-246 2.19e-79

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: 238.49  E-value: 2.19e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSLKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLAC---LNKFs 100
Cdd:COG0479     5 LKIWRQDPETDSKPRFQTY--EVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACqthVRDL- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 101 lsnSQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKENF-KQEILQSKIDRFELDGLYECILcaccssscpsYW 179
Cdd:COG0479    82 ---KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPApDNERLQSPEDREKADDLAECILcgacvaacpnVW 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2431519332 180 WNyQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:COG0479   159 AN-PDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLK 224
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 26-246 1.41e-77

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: 233.48  E-value: 1.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  26 IYRWNPYLSLKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLSNSQ 105
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSY--EVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 106 FLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKENFKQ--EILQSKIDRFELDGLYECILCACCSSSCPSYWWNyQ 183
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPegEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN-P 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2431519332 184 KYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:TIGR00384 158 EFLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 24-130 1.95e-38

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: 129.66  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLS-LKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLS 102
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEY--EVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 2431519332 103 NSQFLTIYPLPHFSIIKDLVCDLTNFYN 130
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 18-246 4.46e-103

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 300.55  E-value: 4.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  18 NSNFFYIRIYRWNPYLSLKPWFNIFPLKLQiNSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLN 97
Cdd:PLN00129   40 PSNLKEFQIYRWNPDNPGKPHLQSYKVDLN-DCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLT 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  98 KFSLSNSQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRK---ENFKQEILQSKIDRFELDGLYECILCACCSSS 174
Cdd:PLN00129  119 KIDRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKkppEDGQKEHLQSKEDRAKLDGMYECILCACCSTS 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2431519332 175 CPSYWWNYQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:PLN00129  199 CPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIK 270
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 24-246 9.48e-100

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 290.16  E-value: 9.48e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSLKPWFNIFPLKLQINSKfMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLSN 103
Cdd:PRK05950    2 FKIYRYNPDVDANPRMQTYEVDVDECGP-MVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 104 SQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKENFKQ-EILQSKIDRFELDGLYECILCACCSSSCPSYWWNY 182
Cdd:PRK05950   81 KGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPArERLQSPEDREKLDGLYECILCACCSTSCPSFWWNP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2431519332 183 QKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:PRK05950  161 DKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIK 224
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 24-246 2.19e-79

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: 238.49  E-value: 2.19e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSLKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLAC---LNKFs 100
Cdd:COG0479     5 LKIWRQDPETDSKPRFQTY--EVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACqthVRDL- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 101 lsnSQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKENF-KQEILQSKIDRFELDGLYECILcaccssscpsYW 179
Cdd:COG0479    82 ---KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPApDNERLQSPEDREKADDLAECILcgacvaacpnVW 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2431519332 180 WNyQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:COG0479   159 AN-PDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLK 224
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 26-246 1.41e-77

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: 233.48  E-value: 1.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  26 IYRWNPYLSLKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLSNSQ 105
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSY--EVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 106 FLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKENFKQ--EILQSKIDRFELDGLYECILCACCSSSCPSYWWNyQ 183
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPegEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN-P 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2431519332 184 KYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:TIGR00384 158 EFLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
24-242 6.30e-67

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 207.12  E-value: 6.30e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSLKPWFNIFPLKLQINSKfMILDLLFYIKNNfDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLSN 103
Cdd:PRK12575    7 LHIYRYDPDDDAAPRMQRYEIAPRAEDR-MLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 104 SQfLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKENF-KQEILQSKIDRFELDGLYECILCACCSSSCPSYWWNY 182
Cdd:PRK12575   85 RE-IVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPpERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 183 QKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVI 242
Cdd:PRK12575  164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAI 223
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
24-246 8.09e-41

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 140.22  E-value: 8.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSLKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLAClNKFSLSN 103
Cdd:PRK12385    9 IEVLRYNPEVDTEPHSQTY--EVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLAC-KTFLRDY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 104 SQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKEN------FKQEILQ-SKIDRFELdglyeCILCACCSSSCP 176
Cdd:PRK12385   86 TGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRtpddgpNKQTPAQmAKYHQFSG-----CINCGLCYAACP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 177 SYWWNyQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHNITNCSQVCPKKLNPAKVINFLK 246
Cdd:PRK12385  161 QFGLN-PEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 24-130 1.95e-38

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: 129.66  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLS-LKPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLS 102
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEY--EVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 2431519332 103 NSQFLTIYPLPHFSIIKDLVCDLTNFYN 130
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
24-251 1.17e-36

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 130.64  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPylSLKPWFNIFPLKLQinsKFM-ILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLAC----LNK 98
Cdd:PRK12576   11 FKVKRYDP--EKGSWWQEYKVKVD---RFTqVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACktlvLDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  99 FSLSNSQfLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIRKEnfkqEILQSKI-------DRFELDGLYECIlcacc 171
Cdd:PRK12576   86 AKKYNSV-ITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAK----EVLEGKAehrlkpeDQKELWKFAQCI----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 172 ssscpsyWWNY-----------QKYLGPAILLQAYKWLIDSRDFSKFMRIKfLNTKSrITKCHNITNCSQVCPKKLNPAK 240
Cdd:PRK12576  156 -------WCGLcvsacpvvaidPEFLGPAAHAKGYRFLADPRDTITEERMK-ILIDS-SWRCTYCYSCSNVCPRDIEPVT 226

                         250
                  ....*....|.
gi 2431519332 241 VINFLKYFSQF 251
Cdd:PRK12576  227 AIKKTRSFTRV 237
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
24-246 8.22e-33

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 121.73  E-value: 8.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSlkPWFNIFPLklQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLAC-------L 96
Cdd:PRK12577    5 FKILRQKQNSA--PYVQTYTL--EVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvgseL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  97 NKFSLSNS---QFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLIR--KENFKQEILQSKIDRFELDGLYECILCACC 171
Cdd:PRK12577   81 ARLSDSNSgaiPEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTaaRQVPEREFLQTPEERSKLDQTGNCILCGAC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2431519332 172 SSSCPSYWWNyQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSR----ITKCHnitNCSQVCPKKLNPAKVINFLK 246
Cdd:PRK12577  161 YSECNAREVN-PEFVGPHALAKAQRMVADSRDTATEQRLELYNQGTAgvwgCTRCY---YCNSVCPMEVAPLDQITKIK 235
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 24-242 7.98e-27

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 107.78  E-value: 7.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSlKPWFNifPLKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFslsn 103
Cdd:PRK06259    6 ITVKRFDPEKD-EPHFE--SYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 104 SQFLTIYPLpHFSIIKDLVCDLTNFYNQLRLIQPWLIRK---ENFKQEILQSKidrfELDGLYECILCACCSSSCPsyww 180
Cdd:PRK06259   79 EDGMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKnekITYPEDIEDIK----KLRGCIECLSCVSTCPARK---- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2431519332 181 nYQKYLGPAILLQAYKWLIDSRDFSKFMRIKFLNTKSRITKCHnitNCSQVCPKKLN-PAKVI 242
Cdd:PRK06259  150 -VSDYPGPTFMRQLARFAFDPRDEGDREKEAFDEGLYNCTTCG---KCVEVCPKEIDiPGKAI 208
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 24-165 1.06e-18

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 81.92  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  24 IRIYRWNPYLSL-KPWFNIFplKLQINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFSLS 102
Cdd:PRK13552    7 FNIFRYNPQDPGsKPHMVTY--QLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSDY 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 103 NSQFLTIYPLPHFSIIKDLVCDLTNFYNQL-RLIQPWLIRKENFKQEILQSKIDR------FELDGLYEC 165
Cdd:PRK13552   85 PDGVITLMPLPVFKLIGDLSVNTGKWFREMsERVESWIHTDKEFDIHRLEERMEPeeadeiYELDRCIEC 154
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 47-233 2.05e-13

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 67.80  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  47 QINSKFMILDLLFYIKNNFDSTLTFRRSCREGICGSCAMNINGLNSLACLNKFS-LSNSQFLTIYPLPHFSIIKDLVCDL 125
Cdd:PRK12386   25 EVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMStFDEDETVTVTPMRTFPVIRDLVTDV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 126 TNFYNQLRLIQPWLIRKENFKQE--ILQSKIDR-FELDGLYECILCACCSSSCPSYWWNYQKYLGPAILLQaYKWL---- 198
Cdd:PRK12386  105 SFNYEKAREIPSFTPPKDLQPGEyrMQQVDVERsQEFRKCIECFLCQNVCHVVRDHEENKPAFAGPRFLMR-IAELemhp 183

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2431519332 199 IDSRDFSKFMRIKFLNTKSRITKChnitnCSQVCP 233
Cdd:PRK12386  184 LDTADRRAEAQEEHGLGYCNITKC-----CTEVCP 213
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 75-236 1.65e-08

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 53.84  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332  75 CREGICGSCAMNINGLNSLAC---LNKFslsnSQFLTIYPLPHFSIIKDLVCDLTNFYNQLRLIQPWLirkenfkqeilq 151
Cdd:PRK08640   63 CLEEVCGACSMVINGKPRQACtalIDQL----EQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWI------------ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2431519332 152 skidrfELDGLYEciLCACCSSSCPSYWWNYQ---------------------KYLGPAILLQAYkwLIDSR---DFSKF 207
Cdd:PRK08640  127 ------PIDGTYD--LGPGPRMPEEKRQWAYElskcmtcgccleacpnvneksDFIGPAAISQVR--LFNAHptgEMHKE 196

                         170       180
                  ....*....|....*....|....*....
gi 2431519332 208 MRIKFLNTKSRITKCHNITNCSQVCPKKL 236
Cdd:PRK08640  197 ERLRALMGDGGIADCGNAQNCVRVCPKGI 225
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 75-136 2.51e-06

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 47.13  E-value: 2.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2431519332  75 CREGICGSCAMNINGL------NSLAC-LNKFSLSNSQFLTIYPL--PHFSIIKDLVCDLTNFYnqlRLIQ 136
Cdd:PRK07570   58 CREGICGMCGLVINGRphgpdrGTTTCqLHMRSFKDGDTITIEPWraAAFPVIKDLVVDRSALD---RIIQ 125
 
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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