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Conserved domains on  [gi|502766287|ref|WP_013001271|]
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MULTISPECIES: succinate dehydrogenase iron-sulfur subunit [Streptomyces]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 11481909)

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

EC:  1.3.5.1
Gene Ontology:  GO:0008177|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 22-253 1.37e-147

succinate dehydrogenase iron-sulfur subunit; Reviewed


:

Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 411.49  E-value: 1.37e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  22 TFRVRRFNPEVAAEASWQDFVLEIDPKE-RVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDIN 100
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 101 PeKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITkDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFW- 179
Cdd:PRK05950  81 K-GKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLIN-DTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWw 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITRRF 253
Cdd:PRK05950 159 NPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 22-253 1.37e-147

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 411.49  E-value: 1.37e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  22 TFRVRRFNPEVAAEASWQDFVLEIDPKE-RVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDIN 100
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 101 PeKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITkDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFW- 179
Cdd:PRK05950  81 K-GKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLIN-DTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWw 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITRRF 253
Cdd:PRK05950 159 NPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 20-251 1.11e-122

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 348.27  E-value: 1.11e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNPEVAAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDI 99
Cdd:COG0479    2 TVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 100 npEKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTnEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFW 179
Cdd:COG0479   82 --KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGP-APDNERLQSPEDREKADDLAECILCGACVAACPNVW 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITR 251
Cdd:COG0479  159 ANPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 25-245 3.62e-97

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: 283.55  E-value: 3.62e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287   25 VRRFNPEVAAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDINpEKP 104
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLG-QPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  105 ITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFWNDGQY 184
Cdd:TIGR00384  80 MKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEF 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502766287  185 FGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVK 245
Cdd:TIGR00384 160 LGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 22-128 5.56e-48

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 154.32  E-value: 5.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287   22 TFRVRRFNPEV-AAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDIN 100
Cdd:pfam13085   1 TLRVFRYDPRVdRDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*...
gi 502766287  101 pEKPITIEPIKGLTVLKDLVVDMEPFFQ 128
Cdd:pfam13085  81 -GQDITLEPLPGFPVIRDLVVDRSAFFE 107
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 38-98 2.95e-03

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: 35.83  E-value: 2.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502766287  38 WQDFVLEIDPKERVLDGLHKIKwdedgtLTFRRSCAHGICGS------------------DAMRINGKNRLACKTLIKD 98
Cdd:cd00207    7 GSGVEVEVPEGETLLDAAREAG------IDIPYSCRAGACGTckvevvegevdqsdpsllDEEEAEGGYVLACQTRVTD 79
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 22-253 1.37e-147

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 411.49  E-value: 1.37e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  22 TFRVRRFNPEVAAEASWQDFVLEIDPKE-RVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDIN 100
Cdd:PRK05950   1 TFKIYRYNPDVDANPRMQTYEVDVDECGpMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 101 PeKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITkDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFW- 179
Cdd:PRK05950  81 K-GKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLIN-DTPPPARERLQSPEDREKLDGLYECILCACCSTSCPSFWw 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITRRF 253
Cdd:PRK05950 159 NPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 20-251 1.11e-122

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 348.27  E-value: 1.11e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNPEVAAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDI 99
Cdd:COG0479    2 TVTLKIWRQDPETDSKPRFQTYEVPVSPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHVRDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 100 npEKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTnEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFW 179
Cdd:COG0479   82 --KDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGP-APDNERLQSPEDREKADDLAECILCGACVAACPNVW 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITR 251
Cdd:COG0479  159 ANPDFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 25-245 3.62e-97

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: 283.55  E-value: 3.62e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287   25 VRRFNPEVAAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDINpEKP 104
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEGMTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLG-QPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  105 ITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFWNDGQY 184
Cdd:TIGR00384  80 MKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEF 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502766287  185 FGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVK 245
Cdd:TIGR00384 160 LGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 8-245 1.09e-81

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 246.24  E-value: 1.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287   8 KVEAESAASPYITvTFRVRRFNPEVAAEASWQDFvlEIDPKE---RVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRI 84
Cdd:PLN00129  32 KASSKGSKPSNLK-EFQIYRWNPDNPGKPHLQSY--KVDLNDcgpMVLDVLIKIKNEQDPSLTFRRSCREGICGSCAMNI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  85 NGKNRLACKTLIkDINPEKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTNE-PTRERFQTAEDRERFDDTT 163
Cdd:PLN00129 109 DGKNTLACLTKI-DRDESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLKTKKPPEdGQKEHLQSKEDRAKLDGMY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 164 KCILCAACTSSCPVFW-NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQ 242
Cdd:PLN00129 188 ECILCACCSTSCPSYWwNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIA 267


                 ...
gi 502766287 243 EVK 245
Cdd:PLN00129 268 KIK 270
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
20-252 1.03e-75

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 229.46  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNPEVAAEASWQDFVLEIDPKER-VLDGLHKIKwDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKD 98
Cdd:PRK12575   4 TRILHIYRYDPDDDAAPRMQRYEIAPRAEDRmLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  99 INPEkpITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITkDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVF 178
Cdd:PRK12575  83 LPRE--IVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLIN-DTVPPERERLQTPQEREQLDGLYECILCACCSTACPSY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766287 179 W-NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVkRALITRR 252
Cdd:PRK12575 160 WwNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQI-RTMLARR 233
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
19-252 1.28e-69

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 217.25  E-value: 1.28e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  19 ITVTFRVRRFNPEVAAEasWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACK----- 93
Cdd:PRK12577   1 MEVLFKILRQKQNSAPY--VQTYTLEVEPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACKenvgs 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  94 ---TLIKDINPEKP-ITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTNEPTRERFQTAEDRERFDDTTKCILCA 169
Cdd:PRK12577  79 elaRLSDSNSGAIPeITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCILCG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 170 ACTSSCPVFWNDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILN-DRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRAL 248
Cdd:PRK12577 159 ACYSECNAREVNPEFVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIKQEI 238


                 ....
gi 502766287 249 ITRR 252
Cdd:PRK12577 239 LARK 242
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
13-253 3.88e-67

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 209.22  E-value: 3.88e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  13 SAASPYITVTFRVRRFNPEVAAeaSWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLAC 92
Cdd:PRK12576   1 MTQSPEKEVIFKVKRYDPEKGS--WWQEYKVKVDRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLAC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  93 KTLIKDINPEK--PITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKD-TNEPTRERFQTAEDRERFDDTTKCILCA 169
Cdd:PRK12576  79 KTLVLDVAKKYnsVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKeVLEGKAEHRLKPEDQKELWKFAQCIWCG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 170 ACTSSCPVFWNDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILndRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRalI 249
Cdd:PRK12576 159 LCVSACPVVAIDPEFLGPAAHAKGYRFLADPRDTITEERMKIL--IDSSWRCTYCYSCSNVCPRDIEPVTAIKKTRS--F 234


                 ....
gi 502766287 250 TRRF 253
Cdd:PRK12576 235 TRVY 238
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
20-245 1.60e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 178.36  E-value: 1.60e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNPEVAAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDI 99
Cdd:PRK12385   6 NLKIEVLRYNPEVDTEPHSQTYEVPYDETTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 100 nPEKpITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFW 179
Cdd:PRK12385  86 -TGG-MKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAACPQFG 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEVK 245
Cdd:PRK12385 164 LNPEFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 22-128 5.56e-48

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 154.32  E-value: 5.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287   22 TFRVRRFNPEV-AAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDIN 100
Cdd:pfam13085   1 TLRVFRYDPRVdRDEPYYQEYEVPYEEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDLL 80

                          90       100
                  ....*....|....*....|....*...
gi 502766287  101 pEKPITIEPIKGLTVLKDLVVDMEPFFQ 128
Cdd:pfam13085  81 -GQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 20-252 1.97e-39

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 142.45  E-value: 1.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNPEVAAEASwQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDi 99
Cdd:PRK06259   3 MITITVKRFDPEKDEPHF-ESYEVPVKEGMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEVED- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 100 npekPITIEPIKgLTVLKDLVVDMEPFFQAYRDVMPFLITKdtneptRERFQTAEDRERFDDTTKCILCAACTSSCPVFw 179
Cdd:PRK06259  81 ----GMIIEPLD-FPVIKDLIVDREPYYKKLKSLRNYLQRK------NEKITYPEDIEDIKKLRGCIECLSCVSTCPAR- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502766287 180 NDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEIlndRDGVWRCRTTFNCTDACPRGIE-VTKAIQEVkRALITRR 252
Cdd:PRK06259 149 KVSDYPGPTFMRQLARFAFDPRDEGDREKEAF---DEGLYNCTTCGKCVEVCPKEIDiPGKAIEKL-RALAFKK 218
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 20-235 1.66e-32

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 118.51  E-value: 1.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNPEVAA-EASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKD 98
Cdd:PRK13552   4 TLTFNIFRYNPQDPGsKPHMVTYQLEETPGMTLFIALNRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  99 InPEKPITIEPIKGLTVLKDLVVDMEPFFQA-YRDVMPFLITKDTNEPTR--ERFQTAEDRERFdDTTKCILCAACTSSC 175
Cdd:PRK13552  84 Y-PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRleERMEPEEADEIY-ELDRCIECGCCVAAC 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502766287 176 PVFWNDGQYFGPAAIVNAHRFIFDSRDE-AGEQRLEILNDRDGVWRCRTTFNCTDACPRGI 235
Cdd:PRK13552 162 GTKQMREDFVGAVGLNRIARFELDPRDErTDEDFYELIGNDDGVFGCMSLLGCEDNCPKDL 222
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 20-253 1.43e-29

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 111.33  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNpevAAEASWQDFVLEIDPKERVLDGLHKIKWDEDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDI 99
Cdd:PRK12386   4 TAKFRVWRGD---ASGGELQDYTVEVNEGEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMSTF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 100 NPEKPITIEPIKGLTVLKDLVVDMEPFFQAYRDVMPFLITKDTnEPTRERFQTaEDRERFDDTTKCILCAACTSSCPVFW 179
Cdd:PRK12386  81 DEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDL-QPGEYRMQQ-VDVERSQEFRKCIECFLCQNVCHVVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502766287 180 ----NDGQYFGPAAIVNAHRFIFDSRDEAGeqRLEILNDRDGVWRCRTTFNCTDACPRGIEVT-KAIQEVKRALITRRF 253
Cdd:PRK12386 159 dheeNKPAFAGPRFLMRIAELEMHPLDTAD--RRAEAQEEHGLGYCNITKCCTEVCPEHIKITdNALIPMKERVVDRKY 235
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 20-247 2.56e-27

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 105.45  E-value: 2.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  20 TVTFRVRRFNpEVAAEASWQDFVLEIDPKERVLDGLHKI-------KWDEDGTLTFRRSCAHGICGSDAMRINGKNRLAC 92
Cdd:PRK08640   5 TVRLIIKRQD-GPDSKPYWEEFEIPYRPNMNVISALMEIrrnpvnaKGEKTTPVVWDMNCLEEVCGACSMVINGKPRQAC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  93 KTLIKDInpEKPITIEPIKGLTVLKDLVVDMEPFFQAYRDV---MPFLITKDTNEPTRerfQTAEDRERFDDTTKCILCA 169
Cdd:PRK08640  84 TALIDQL--EQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVkawIPIDGTYDLGPGPR---MPEEKRQWAYELSKCMTCG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 170 ACTSSCPVFWNDGQYFGPAAI-----VNAHrfifDSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACPRGIEVTKAIQEV 244
Cdd:PRK08640 159 CCLEACPNVNEKSDFIGPAAIsqvrlFNAH----PTGEMHKEERLRALMGDGGIADCGNAQNCVRVCPKGIPLTTSIAAM 234


                 ...
gi 502766287 245 KRA 247
Cdd:PRK08640 235 NRE 237
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
164-249 4.26e-11

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 57.60  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 164 KCILCAACTSSCPVFWNDGqyFGPAAIVnaHRFIFDSRDEageqrleILNDRDgVWRCRTTFNCTDACPRGIEVTKAIQE 243
Cdd:COG1150    4 KCYQCGTCTASCPVARAMD--YNPRKII--RLAQLGLKEE-------VLKSDS-IWLCVSCYTCTERCPRGIDIADVMDA 71


                 ....*.
gi 502766287 244 VKRALI 249
Cdd:COG1150   72 LRNLAI 77
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 164-235 4.33e-10

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: 54.24  E-value: 4.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766287  164 KCILCAACTSSCPVFwndgqyfgpaaIVNAHRFIFDSRDEAGEQRLEILN---DRDGVWRCRTTFNCTDACPRGI 235
Cdd:pfam13183   1 RCIRCGACLAACPVY-----------LVTGGRFPGDPRGGAAALLGRLEAlegLAEGLWLCTLCGACTEVCPVGI 64
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 161-232 6.04e-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: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 48.40  E-value: 6.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502766287  161 DTTKCILCAACTSSCPVFWndgqyfgpaaivnahrfifdSRDEAGEQRLEILNDRDGVWRCRTTFNCTDACP 232
Cdd:pfam13237   5 DPDKCIGCGRCTAACPAGL--------------------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 72-238 7.88e-08

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 51.76  E-value: 7.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287  72 CAHGICGSDAMRING------KNRLACKTLIKDINPEKPITIEPI--KGLTVLKDLVVDMEPF---FQA--YRDVM---- 134
Cdd:PRK07570  58 CREGICGMCGLVINGrphgpdRGTTTCQLHMRSFKDGDTITIEPWraAAFPVIKDLVVDRSALdriIQAggYVSVNtgga 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 135 ----PFLITKDTNEptrERFQTAEdrerfddttkCILCAACTSSCPvfwndgqyfgpaaivNAHRFIFDS---------- 200
Cdd:PRK07570 138 pdanAIPVPKEDAD---RAFDAAA----------CIGCGACVAACP---------------NGSAMLFTGakvshlallp 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 502766287 201 --RDEAGEQRLEILN--DRDGVWRCRTTFNCTDACPRGIEVT 238
Cdd:PRK07570 190 qgQPERARRVRAMVAqmDEEGFGNCTNTGECEAVCPKGISLE 231
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 135-252 4.90e-07

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 50.08  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 135 PFLITKDTNEPTRERFQTAEDRERFDDTTKCILCAACTSSCPVFWNDGQY-FGPAAIVNAHRFIFDSRDEAGEQRleilN 213
Cdd:COG0247   50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEkDSPRGRINLLREVLEGELPLDLSE----E 125

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502766287 214 DRDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITRR 252
Cdd:COG0247  126 VYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERG 164
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 38-98 2.95e-03

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: 35.83  E-value: 2.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502766287  38 WQDFVLEIDPKERVLDGLHKIKwdedgtLTFRRSCAHGICGS------------------DAMRINGKNRLACKTLIKD 98
Cdd:cd00207    7 GSGVEVEVPEGETLLDAAREAG------IDIPYSCRAGACGTckvevvegevdqsdpsllDEEEAEGGYVLACQTRVTD 79
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 165-235 3.77e-03

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: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 34.81  E-value: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502766287  165 CILCAACTSSCPVFWndgqyfgpaaivnahRFIFDSRDEAGEQRLEIlndrdGVWRCRTTFNCTDACPRGI 235
Cdd:pfam12838   1 CIGCGACVAACPVGA---------------ITLDEVGEKKGTKTVVI-----DPERCVGCGACVAVCPTGA 51
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
155-245 5.44e-03

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 37.54  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766287 155 DRERFDDttkCILCAACTSSCPVFWNDGQYFGPAAI-VNAHRFifdsRDEAGEqrleiLNDrDGVWRCRTTFNCTDACPR 233
Cdd:PRK11168   2 SDTSFDS---CIKCTVCTTACPVARVNPLYPGPKQAgPDGERL----RLKDGA-----LYD-ESLKYCSNCKRCEVACPS 68

                         90
                 ....*....|..
gi 502766287 234 GIEVTKAIQEVK 245
Cdd:PRK11168  69 GVKIGDIIQRAR 80
 
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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