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Conserved domains on  [gi|17533915|ref|NP_495992|]
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Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial [Caenorhabditis elegans]

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

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List of domain hits

 Name Accession Description Interval E-value
PLN00129 super family cl33415
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-284 5.68e-156

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: 436.53  E-value: 5.68e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    1 MLARSARLLHSAELAANAIRAASGapataaaaeaSFPSTDDVAAKTKKTGNRIKTFEIYRFNPEAPGaKPTVQKFDVDLD 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLAPAAAAS----------AAASAETKASSKGSKPSNLKEFQIYRWNPDNPG-KPHLQSYKVDLN 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   81 QCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSDTSKSTKIYPLPHMFVVKDLVPDMNLF 160
Cdd:PLN00129  70 DCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  161 YAQYASIQPWIQKKTPLTLGEKQMHQSVAERDRLDGLYECILCACCSTSCPSYWWNADKYLGPAVLMQAYRWVIDSRDDY 240
Cdd:PLN00129 150 YQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEY 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 17533915  241 ATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLL 284
Cdd:PLN00129 230 TKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLL 273
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-284 5.68e-156

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 436.53  E-value: 5.68e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    1 MLARSARLLHSAELAANAIRAASGapataaaaeaSFPSTDDVAAKTKKTGNRIKTFEIYRFNPEAPGaKPTVQKFDVDLD 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLAPAAAAS----------AAASAETKASSKGSKPSNLKEFQIYRWNPDNPG-KPHLQSYKVDLN 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   81 QCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSDTSKSTKIYPLPHMFVVKDLVPDMNLF 160
Cdd:PLN00129  70 DCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  161 YAQYASIQPWIQKKTPLTLGEKQMHQSVAERDRLDGLYECILCACCSTSCPSYWWNADKYLGPAVLMQAYRWVIDSRDDY 240
Cdd:PLN00129 150 YQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEY 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 17533915  241 ATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLL 284
Cdd:PLN00129 230 TKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLL 273
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 55-285 6.33e-108

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: 312.84  E-value: 6.33e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  55 TFEIYRFNPEApGAKPTVQKFDVDLDqCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDsD 134
Cdd:COG0479   4 TLKIWRQDPET-DSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915 135 TSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPltLGEKQMHQSVAERDRLDGLYECILCACCSTSCPSYW 214
Cdd:COG0479  81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGP--APDNERLQSPEDREKADDLAECILCGACVAACPNVW 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533915 215 WNADkYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLLT 285
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 58-281 7.45e-104

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: 302.04  E-value: 7.45e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    58 IYRFNPEApGAKPTVQKFDVDLDQCgTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSDTSK 137
Cdd:TIGR00384   1 VLRFNPDV-DEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   138 STKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTLGEKQMhQSVAERDRLDGLYECILCACCSTSCPSYWWNA 217
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFL-QTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533915   218 DkYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIK 281
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 55-162 1.12e-45

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: 149.69  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    55 TFEIYRFNPEAPGAKPTVQKFDVDLDqCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSD 134
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVPYE-EGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 17533915   135 TSKSTKIYPLPHMFVVKDLVPDMNLFYA 162
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 73-134 7.16e-04

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: 37.76  E-value: 7.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  73 QKFDVDldqCGTMILDALIKIKnevdptLTFRRSCREGICGSCAMNI------------------GGQNTLACICKIDSD 134
Cdd:cd00207  10 VEVEVP---EGETLLDAAREAG------IDIPYSCRAGACGTCKVEVvegevdqsdpslldeeeaEGGYVLACQTRVTDG 80
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 1-284 5.68e-156

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 436.53  E-value: 5.68e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    1 MLARSARLLHSAELAANAIRAASGapataaaaeaSFPSTDDVAAKTKKTGNRIKTFEIYRFNPEAPGaKPTVQKFDVDLD 80
Cdd:PLN00129   1 MAAGLLRRLAGAKAGLLAPAAAAS----------AAASAETKASSKGSKPSNLKEFQIYRWNPDNPG-KPHLQSYKVDLN 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   81 QCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSDTSKSTKIYPLPHMFVVKDLVPDMNLF 160
Cdd:PLN00129  70 DCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTITPLPHMFVIKDLVVDMTNF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  161 YAQYASIQPWIQKKTPLTLGEKQMHQSVAERDRLDGLYECILCACCSTSCPSYWWNADKYLGPAVLMQAYRWVIDSRDDY 240
Cdd:PLN00129 150 YQQYKSIEPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEY 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 17533915  241 ATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLL 284
Cdd:PLN00129 230 TKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLL 273
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 55-284 5.19e-145

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 406.87  E-value: 5.19e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   55 TFEIYRFNPEApGAKPTVQKFDVDLDQCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSD 134
Cdd:PRK05950   1 TFKIYRYNPDV-DANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  135 TSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTLGEKQmhQSVAERDRLDGLYECILCACCSTSCPSYW 214
Cdd:PRK05950  80 KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPARERL--QSPEDREKLDGLYECILCACCSTSCPSFW 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  215 WNADKYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLL 284
Cdd:PRK05950 158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRML 227
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 55-285 6.33e-108

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: 312.84  E-value: 6.33e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  55 TFEIYRFNPEApGAKPTVQKFDVDLDqCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDsD 134
Cdd:COG0479   4 TLKIWRQDPET-DSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVR-D 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915 135 TSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPltLGEKQMHQSVAERDRLDGLYECILCACCSTSCPSYW 214
Cdd:COG0479  81 LKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGP--APDNERLQSPEDREKADDLAECILCGACVAACPNVW 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533915 215 WNADkYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLLT 285
Cdd:COG0479 159 ANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREAL 228
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 58-281 7.45e-104

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: 302.04  E-value: 7.45e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    58 IYRFNPEApGAKPTVQKFDVDLDQCgTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSDTSK 137
Cdd:TIGR00384   1 VLRFNPDV-DEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   138 STKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTLGEKQMhQSVAERDRLDGLYECILCACCSTSCPSYWWNA 217
Cdd:TIGR00384  79 VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFL-QTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533915   218 DkYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIK 281
Cdd:TIGR00384 158 E-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
54-285 4.67e-96

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 283.00  E-value: 4.67e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   54 KTFEIYRFNPEaPGAKPTVQKFDVDLDQCGTMILDALIKIKNEvDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDS 133
Cdd:PRK12575   5 RILHIYRYDPD-DDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-DETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  134 dTSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTlgEKQMHQSVAERDRLDGLYECILCACCSTSCPSY 213
Cdd:PRK12575  83 -LPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPP--ERERLQTPQEREQLDGLYECILCACCSTACPSY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17533915  214 WWNADKYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKSLLT 285
Cdd:PRK12575 160 WWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLA 231
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
55-296 6.62e-51

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 170.65  E-value: 6.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   55 TFEIYRFNPEAPgakPTVQKFDVDLDQcGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSD 134
Cdd:PRK12577   4 LFKILRQKQNSA---PYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  135 TSKSTK----------IYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPlTLGEKQMHQSVAERDRLDGLYECILCA 204
Cdd:PRK12577  80 LARLSDsnsgaipeitIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAAR-QVPEREFLQTPEERSKLDQTGNCILCG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  205 CCSTSCPSYWWNADkYLGPAVLMQAYRWVIDSRDDYATERLHRMH-DSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIKS- 282
Cdd:PRK12577 159 ACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQe 237

                        250
                 ....*....|....
gi 17533915  283 LLTgftsKPAAEPS 296
Cdd:PRK12577 238 ILA----RKDAQDS 247
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
55-282 1.17e-50

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 168.39  E-value: 1.17e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   55 TFEIYRFNPEApgaKPTVQKFDVDLDQcGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLAC---ICKI 131
Cdd:PRK12576  10 IFKVKRYDPEK---GSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACktlVLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  132 DSDTSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTLGEKQMHQSVAERDRLDGLYECILCACCSTSCP 211
Cdd:PRK12576  86 AKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACP 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533915  212 SYWWNaDKYLGPAVLMQAYRWVIDSRDDYATERLHRMHDsfSAFKCHTIMNCTKTCPKHLNPAKAIGEIKS 282
Cdd:PRK12576 166 VVAID-PEFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
49-281 3.08e-46

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 156.01  E-value: 3.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   49 TGNRIKTFEIYRFNPEApGAKPTVQKFDVDLDQcGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACI 128
Cdd:PRK12385   2 AEMKNLKIEVLRYNPEV-DTEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  129 CKIdSDTSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKtPLTLGEKQMHQSVAERDRLDGLYECILCACCST 208
Cdd:PRK12385  80 TFL-RDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGN-DRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533915  209 SCPSYWWNADkYLGPAVLMQAYRWVIDSRDDYATERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAKAIGEIK 281
Cdd:PRK12385 158 ACPQFGLNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 55-162 1.12e-45

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: 149.69  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915    55 TFEIYRFNPEAPGAKPTVQKFDVDLDqCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDSD 134
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVPYE-EGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 17533915   135 TSKSTKIYPLPHMFVVKDLVPDMNLFYA 162
Cdd:pfam13085  80 LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 52-271 4.28e-38

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 134.69  E-value: 4.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   52 RIKTFEIYRFNPEAPGAKPTVQKFDVDlDQCGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKI 131
Cdd:PRK13552   3 RTLTFNIFRYNPQDPGSKPHMVTYQLE-ETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  132 DSDTSKSTKIYPLPHMFVVKDLVPDM-NLFYAQYASIQPWI--QKKTPLTLGEKQMHQSVAERdrldgLYE---CILCAC 205
Cdd:PRK13552  82 SDYPDGVITLMPLPVFKLIGDLSVNTgKWFREMSERVESWIhtDKEFDIHRLEERMEPEEADE-----IYEldrCIECGC 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17533915  206 CSTSCPSYWWNADkYLGPAVLMQAYRWVIDSRDDYATERL-HRMHDSFSAFKCHTIMNCTKTCPKHL 271
Cdd:PRK13552 157 CVAACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDL 222
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 55-277 1.53e-32

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 125.12  E-value: 1.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   55 TFEIYRFNPEAPgaKPTVQKFDVDLDQcGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKI-DS 133
Cdd:PRK06259   5 TITVKRFDPEKD--EPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVeDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  134 DTskstkIYPLpHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTlgekqmhQSVAERDRLDGLYECILCACCSTSCPSY 213
Cdd:PRK06259  82 MI-----IEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKI-------TYPEDIEDIKKLRGCIECLSCVSTCPAR 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533915  214 wwNADKYLGPAVLMQAYRWVIDSRDDyaTERLHRMHDSfSAFKCHTIMNCTKTCPKHLN-PAKAI 277
Cdd:PRK06259 149 --KVSDYPGPTFMRQLARFAFDPRDE--GDREKEAFDE-GLYNCTTCGKCVEVCPKEIDiPGKAI 208
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 73-271 4.86e-16

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 75.89  E-value: 4.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   73 QKFDVDLDQcGTMILDALIKIKNEVDPTLTFRRSCREGICGSCAMNIGGQNTLACICKIDS-DTSKSTKIYPLPHMFVVK 151
Cdd:PRK12386  20 QDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTfDEDETVTVTPMRTFPVIR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  152 DLVPDMNLFYAQYASIQPWIQKKtPLTLGEKQMHQsvAERDRLDGLYECILCACCSTSC---PSYWWNADKYLGPAVLMQ 228
Cdd:PRK12386  99 DLVTDVSFNYEKAREIPSFTPPK-DLQPGEYRMQQ--VDVERSQEFRKCIECFLCQNVChvvRDHEENKPAFAGPRFLMR 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17533915  229 AYRWVIDSRDdyATERLHRMHDSFSAFKCHTIMNCTKTCPKHL 271
Cdd:PRK12386 176 IAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 51-269 7.17e-12

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 64.24  E-value: 7.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   51 NRIKTFEIYRFnpEAPGAKPTVQKFDVDLDQcGTMILDALIKI-KN-------EVDPtLTFRRSCREGICGSCAMNIGGQ 122
Cdd:PRK08640   3 EKTVRLIIKRQ--DGPDSKPYWEEFEIPYRP-NMNVISALMEIrRNpvnakgeKTTP-VVWDMNCLEEVCGACSMVINGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  123 NTLACICKIDSdTSKSTKIYPLPHMFVVKDLVPDMNLFYAQYASIQPWIQKKTPLTLGE-KQMHQSvaERDRLDGLYECI 201
Cdd:PRK08640  79 PRQACTALIDQ-LEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPIDGTYDLGPgPRMPEE--KRQWAYELSKCM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  202 LCACCSTSCPSYWWNADkYLGPAVLMQAyrwvidsrddyateRLHRMH---DSFSAFKCHTIM------------NCTKT 266
Cdd:PRK08640 156 TCGCCLEACPNVNEKSD-FIGPAAISQV--------------RLFNAHptgEMHKEERLRALMgdggiadcgnaqNCVRV 220


                 ...
gi 17533915  267 CPK 269
Cdd:PRK08640 221 CPK 223
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 199-272 1.31e-08

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: 50.54  E-value: 1.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533915   199 ECILCACCSTSCPSYWWNADKylgPAVLMQAYRWvidsrddyatERLHRMHDSFSAFKCHTIMNCTKTCPKHLN 272
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 200-271 2.88e-04

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: 38.45  E-value: 2.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533915   200 CILCACCSTSCPSYwwnadkylgpavLMQAYRWVIDSRD---DYATERLHRMHDSFSAFKCHTIMNCTKTCPKHL 271
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGgaaALLGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 55-156 3.18e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 41.36  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915   55 TFEIYR-FNPEAPGAKPTVQKFDVDLDQCGTMILDALIK--IKNEVDPtLTFRRSCREGICGSCAMNIGGQ------NTL 125
Cdd:PRK07570   4 TLKIWRqKGPDDKGKFETYEVDDISPDMSFLEMLDVLNEqlIEKGEEP-VAFDHDCREGICGMCGLVINGRphgpdrGTT 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 17533915  126 ACICKI----DSDTSK----STKIYPlphmfVVKDLVPD 156
Cdd:PRK07570  83 TCQLHMrsfkDGDTITiepwRAAAFP-----VIKDLVVD 116
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 73-134 7.16e-04

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: 37.76  E-value: 7.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915  73 QKFDVDldqCGTMILDALIKIKnevdptLTFRRSCREGICGSCAMNI------------------GGQNTLACICKIDSD 134
Cdd:cd00207  10 VEVEVP---EGETLLDAAREAG------IDIPYSCRAGACGTCKVEVvegevdqsdpslldeeeaEGGYVLACQTRVTDG 80
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 200-268 3.78e-03

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: 34.92  E-value: 3.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17533915   200 CILCACCSTSCPSYWWNADKYLgpavlmqayrwvidsrddyatERLHRMHDSFSAFKCHTIMNCTKTCP 268
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIV---------------------ERLEGEAVRIGVWKCIGCGACVEACP 56
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
196-283 6.84e-03

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 34.88  E-value: 6.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533915 196 GLYECILCACCSTSCPSYWWNAdkyLGPAVLMQAYRWvidsrddyatERLHRMHDSFSAFKCHTIMNCTKTCPKHLNPAK 275
Cdd:COG1150   1 NLKKCYQCGTCTASCPVARAMD---YNPRKIIRLAQL----------GLKEEVLKSDSIWLCVSCYTCTERCPRGIDIAD 67


                ....*...
gi 17533915 276 AIGEIKSL 283
Cdd:COG1150  68 VMDALRNL 75
 
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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