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Conserved domains on  [gi|313768526|ref|YP_004062201|]
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SdhB (mitochondrion) [Gracilariopsis andersonii]

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
 15-250 1.17e-144

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: 406.10  E-value: 1.17e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  15 SNKTTQKYLRIYRWNPSLYNKPWFNIYPISLNNCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACL 94
Cdd:PLN00129  38 SKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  95 KSLNTKEMFIT-IYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPV--KEYLQSTSDRHELNGLYECILCACCSA 171
Cdd:PLN00129 118 TKIDRDESGPTtITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDgqKEHLQSKEDRAKLDGMYECILCACCST 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313768526 172 SCPSYWWNHDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIKYKISKG 250
Cdd:PLN00129 198 SCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 15-250 1.17e-144

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 406.10  E-value: 1.17e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  15 SNKTTQKYLRIYRWNPSLYNKPWFNIYPISLNNCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACL 94
Cdd:PLN00129  38 SKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  95 KSLNTKEMFIT-IYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPV--KEYLQSTSDRHELNGLYECILCACCSA 171
Cdd:PLN00129 118 TKIDRDESGPTtITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDgqKEHLQSKEDRAKLDGMYECILCACCST 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313768526 172 SCPSYWWNHDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIKYKISKG 250
Cdd:PLN00129 198 SCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 23-244 4.01e-111

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: 319.38  E-value: 4.01e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNPSLYNKPWFNIYPISLNnCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAC---LKSLNT 99
Cdd:COG0479    5 LKIWRQDPETDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACqthVRDLKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 100 KemfITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPVKEYLQSTSDRHELNGLYECILCACCSASCPSYWWN 179
Cdd:COG0479   84 T---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526 180 hDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIK 244
Cdd:COG0479  161 -PDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLK 224
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 25-244 9.10e-99

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: 287.79  E-value: 9.10e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526   25 IYRWNPSLYNKPWFNIYPISLNNCgPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAC---LKSLNTKE 101
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACktkVEDLGQPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  102 MfiTIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINlKNIPVK--EYLQSTSDRHELNGLYECILCACCSASCPSYWWN 179
Cdd:TIGR00384  80 M--KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIR-KSQPEPegEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526  180 HDkYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIK 244
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 23-127 3.41e-43

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: 142.38  E-value: 3.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526   23 LRIYRWNPSLY-NKPWFNIYPISlNNCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACLKSLNT-K 100
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDlL 80

                          90       100
                  ....*....|....*....|....*..
gi 313768526  101 EMFITIYPLPHMYVIKDLIPDLTHFYA 127
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 15-250 1.17e-144

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 406.10  E-value: 1.17e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  15 SNKTTQKYLRIYRWNPSLYNKPWFNIYPISLNNCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACL 94
Cdd:PLN00129  38 SKPSNLKEFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  95 KSLNTKEMFIT-IYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPV--KEYLQSTSDRHELNGLYECILCACCSA 171
Cdd:PLN00129 118 TKIDRDESGPTtITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEDgqKEHLQSKEDRAKLDGMYECILCACCST 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313768526 172 SCPSYWWNHDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIKYKISKG 250
Cdd:PLN00129 198 SCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 23-244 1.46e-144

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 403.79  E-value: 1.46e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNPSLYNKPWFNIYPISLNNCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAC---LKSLNT 99
Cdd:PRK05950   2 FKIYRYNPDVDANPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACitpISDLKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 100 KEmfITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPVKEYLQSTSDRHELNGLYECILCACCSASCPSYWWN 179
Cdd:PRK05950  82 GK--IVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWWN 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526 180 HDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIK 244
Cdd:PRK05950 160 PDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIK 224
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 23-244 4.01e-111

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: 319.38  E-value: 4.01e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNPSLYNKPWFNIYPISLNnCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAC---LKSLNT 99
Cdd:COG0479    5 LKIWRQDPETDSKPRFQTYEVPVS-PGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACqthVRDLKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 100 KemfITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPVKEYLQSTSDRHELNGLYECILCACCSASCPSYWWN 179
Cdd:COG0479   84 T---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPDNERLQSPEDREKADDLAECILCGACVAACPNVWAN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526 180 hDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIK 244
Cdd:COG0479  161 -PDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLK 224
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 25-244 9.10e-99

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: 287.79  E-value: 9.10e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526   25 IYRWNPSLYNKPWFNIYPISLNNCgPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAC---LKSLNTKE 101
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACktkVEDLGQPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  102 MfiTIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINlKNIPVK--EYLQSTSDRHELNGLYECILCACCSASCPSYWWN 179
Cdd:TIGR00384  80 M--KIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIR-KSQPEPegEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526  180 HDkYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIK 244
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
21-244 1.16e-96

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 283.00  E-value: 1.16e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  21 KYLRIYRWNPSLYNKPWFNIYPISLNNCGPMVLDALIQIKdTQDSTLTFRRSCREGICGSCSMNINGINTLACLKSLNTK 100
Cdd:PRK12575   5 RILHIYRYDPDDDAAPRMQRYEIAPRAEDRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 101 EMFITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNIPVKEYLQSTSDRHELNGLYECILCACCSASCPSYWWNH 180
Cdd:PRK12575  84 PREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313768526 181 DKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIK 244
Cdd:PRK12575 164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIR 227
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
23-240 8.99e-57

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 182.64  E-value: 8.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNPSlyNKPWFNIYPISLNNcGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAC----LKSLN 98
Cdd:PRK12576  11 FKVKRYDPE--KGSWWQEYKVKVDR-FTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACktlvLDVAK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  99 TKEMFITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLINLKNI--PVKEYLQSTSDRHELNGLYECILCACCSASCPSY 176
Cdd:PRK12576  88 KYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVleGKAEHRLKPEDQKELWKFAQCIWCGLCVSACPVV 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313768526 177 WWNhDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKmrLFRCHTIMNCSKTCPKSLNPGKAI 240
Cdd:PRK12576 168 AID-PEFLGPAAHAKGYRFLADPRDTITEERMKILIDS--SWRCTYCYSCSNVCPRDIEPVTAI 228
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
23-247 3.01e-47

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 159.86  E-value: 3.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNPSlyNKPWFNIYPISLNNcGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACLKSLNTK-E 101
Cdd:PRK12577   5 FKILRQKQN--SAPYVQTYTLEVEP-GNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKENVGSElA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 102 MF----------ITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWL-INLKNIPVKEYLQSTSDRHELNGLYECILCACCS 170
Cdd:PRK12577  82 RLsdsnsgaipeITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVsTAARQVPEREFLQTPEERSKLDQTGNCILCGACY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313768526 171 ASCPSYWWNHDkYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMR-LFRCHTIMNCSKTCPKSLNPGKAIALIKYKI 247
Cdd:PRK12577 162 SECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNQGTAgVWGCTRCYYCNSVCPMEVAPLDQITKIKQEI 238
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
15-249 1.10e-45

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 153.32  E-value: 1.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  15 SNKTTQKyLRIYRWNPSLYNKPWFNIYPISLNNcGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACL 94
Cdd:PRK12385   2 AEMKNLK-IEVLRYNPEVDTEPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  95 KSLNTKEMFITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWLI-NLKNIPVKEYLQSTSDRHELNGLYECILCACCSASC 173
Cdd:PRK12385  80 TFLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIgNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313768526 174 PSYWWNhDKYLGPAILLQAYRWIVDSRDAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIKYKISK 249
Cdd:PRK12385 160 PQFGLN-PEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESAK 234
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 23-127 3.41e-43

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: 142.38  E-value: 3.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526   23 LRIYRWNPSLY-NKPWFNIYPISlNNCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACLKSLNT-K 100
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVP-YEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDlL 80

                          90       100
                  ....*....|....*....|....*..
gi 313768526  101 EMFITIYPLPHMYVIKDLIPDLTHFYA 127
Cdd:pfam13085  81 GQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 23-240 3.97e-34

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 128.20  E-value: 3.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNPSLyNKPWFNIYPISLNNcGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACLKSLNTKem 102
Cdd:PRK06259   6 ITVKRFDPEK-DEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVEDG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 103 fITIYPLpHMYVIKDLIPDLTHFYAQYKMIKPWLinlknIPVKEYLQSTSDRHELNGLYECILCACCSASCPSYwwNHDK 182
Cdd:PRK06259  82 -MIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYL-----QRKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--KVSD 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 313768526 183 YLGPAILLQAYRWIVDSRDAFTNNRLNFLNHkmrLFRCHTIMNCSKTCPKSLN-PGKAI 240
Cdd:PRK06259 153 YPGPTFMRQLARFAFDPRDEGDREKEAFDEG---LYNCTTCGKCVEVCPKEIDiPGKAI 208
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 23-249 7.85e-30

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 111.96  E-value: 7.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  23 LRIYRWNP-SLYNKPWFNIYpiSLNNCGPMVL-DALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLAClKSLNTK 100
Cdd:PRK13552   7 FNIFRYNPqDPGSKPHMVTY--QLEETPGMTLfIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLAC-RTLTSD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 101 --EMFITIYPLPHMYVIKDLIPDL-THFYAQYKMIKPWLINLKNIPVKEyLQSTSDRHELNGLYE---CILCACCSASCP 174
Cdd:PRK13552  84 ypDGVITLMPLPVFKLIGDLSVNTgKWFREMSERVESWIHTDKEFDIHR-LEERMEPEEADEIYEldrCIECGCCVAACG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313768526 175 SYWWNHDkYLGPAILLQAYRWIVDSRDAFTNNRL-NFLNHKMRLFRCHTIMNCSKTCPKSLNPGKAIALIKYKISK 249
Cdd:PRK13552 163 TKQMRED-FVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDLPLQQQIAYLRRKMAA 237
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 47-231 6.26e-17

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 77.82  E-value: 6.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  47 NCGPMVLDALIQIKDTQDSTLTFRRSCREGICGSCSMNINGINTLACLKSLNT--KEMFITIYPLPHMYVIKDLIPDLTH 124
Cdd:PRK12386  27 NEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTfdEDETVTVTPMRTFPVIRDLVTDVSF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 125 FYAQYKMIKPWlINLKNIPVKEYLQSTSDRHELNGLYECILCACCSASC---PSYWWNHDKYLGPAILLQAYRWIVDSRD 201
Cdd:PRK12386 107 NYEKAREIPSF-TPPKDLQPGEYRMQQVDVERSQEFRKCIECFLCQNVChvvRDHEENKPAFAGPRFLMRIAELEMHPLD 185

                        170       180       190
                 ....*....|....*....|....*....|
gi 313768526 202 afTNNRLNFLNHKMRLFRCHTIMNCSKTCP 231
Cdd:PRK12386 186 --TADRRAEAQEEHGLGYCNITKCCTEVCP 213
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 73-249 2.28e-15

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 73.10  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526  73 CREGICGSCSMNINGINTLACLKSLNTKEMFITIYPLPHMYVIKDLIPDLTHFYAQYKMIKPWlinlknIPVKEYLQ--- 149
Cdd:PRK08640  63 CLEEVCGACSMVINGKPRQACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAW------IPIDGTYDlgp 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768526 150 ----STSDRHELNGLYECILCACCSASCPSYwWNHDKYLGPAILLQAyrwivdsrdaftnnRLnFLNH---KM-RLFRCH 221
Cdd:PRK08640 137 gprmPEEKRQWAYELSKCMTCGCCLEACPNV-NEKSDFIGPAAISQV--------------RL-FNAHptgEMhKEERLR 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 313768526 222 TIM------------NCSKTCPKSLNPGKAIALIKYKISK 249
Cdd:PRK08640 201 ALMgdggiadcgnaqNCVRVCPKGIPLTTSIAAMNRETTK 240
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 73-121 6.85e-07

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 49.06  E-value: 6.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526  73 CREGICGSCSMNINGI------NTLACLKSLNtkeMF-----ITIYP-----LPhmyVIKDLIPD 121
Cdd:PRK07570  58 CREGICGMCGLVINGRphgpdrGTTTCQLHMR---SFkdgdtITIEPwraaaFP---VIKDLVVD 116
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 162-235 2.48e-06

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: 43.99  E-value: 2.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313768526  162 ECILCACCSASCPSYWWNHDKylgPAILLQayrwivdsrdAFTNNRLNFLNHKMRLFRCHTIMNCSKTCPKSLN 235
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKLMR----------AAYLGDLEELQANKVANLCSECGLCEYACPMGLD 61
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 163-234 4.91e-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: 40.37  E-value: 4.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313768526  163 CILCACCSASCPSYwwnhdkylgpaiLLQAYRWIVDSRDAFTNNRLN---FLNHKMRLFRCHTIMNCSKTCPKSL 234
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRleaLEGLAEGLWLCTLCGACTEVCPVGI 64
 
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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