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Conserved domains on  [gi|1709035576|gb|TSF27542|]
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succinate dehydrogenase iron-sulfur subunit [Salmonella enterica subsp. enterica serovar Chester]

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
 4-238 1.28e-169

succinate dehydrogenase iron-sulfur subunit; Reviewed


:

Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 466.19  E-value: 1.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   4 EFSIYRYNPDVDNAPRMQDYTLEGEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950    1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  83 tqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950   80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709035576 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950  157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-238 1.28e-169

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 466.19  E-value: 1.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   4 EFSIYRYNPDVDNAPRMQDYTLEGEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950    1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  83 tqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950   80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709035576 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950  157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-236 6.26e-129

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: 363.30  E-value: 6.26e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   1 MKLEFSIYRYNPDVDNAPRMQDYTLEGEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:COG0479     1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  80 SALTQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479    79 RDLKDT---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709035576 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479   155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 7-230 2.93e-128

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: 361.36  E-value: 2.93e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   7 IYRYNPDVDNAPRMQDYTLEGEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALTQP 85
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  86 gkKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384  79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709035576 166 PDkFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
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 ...
 5-112 6.10e-46

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: 148.54  E-value: 6.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   5 FSIYRYNPDVD-NAPRMQDYTLEGEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1709035576  83 tqPGKKIVIRPLPGLPVIRDLVVDMGQFYA 112
Cdd:pfam13085  80 --LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 4-238 1.28e-169

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 466.19  E-value: 1.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   4 EFSIYRYNPDVDNAPRMQDYTLEGEEgRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:PRK05950    1 TFKIYRYNPDVDANPRMQTYEVDVDE-CGPMVLDALIKIKnEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  83 tqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSF 162
Cdd:PRK05950   80 --KKGKIVIRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT-PPPARERLQSPEDREKLDGLYECILCACCSTSCPSF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709035576 163 WWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRSA 238
Cdd:PRK05950  157 WWNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLERRV 232
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 1-236 6.26e-129

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: 363.30  E-value: 6.26e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   1 MKLEFSIYRYNPDVDNAPRMQDYTLEGEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:COG0479     1 MTVTLKIWRQDPETDSKPRFQTYEVPVSPG--MTVLDALDYIKEEqDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  80 SALTQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGqNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:COG0479    79 RDLKDT---ITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDG-PAPDNERLQSPEDREKADDLAECILCGACVAAC 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709035576 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQR 236
Cdd:COG0479   155 PNVWANPD-FLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 7-230 2.93e-128

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: 361.36  E-value: 2.93e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   7 IYRYNPDVDNAPRMQDYTLEGEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALTQP 85
Cdd:TIGR00384   1 VLRFNPDVDEKPHLQSYEVPADEG--MTVLDALNYIKdEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  86 gkKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWN 165
Cdd:TIGR00384  79 --VMKIEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPEPEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709035576 166 PDkFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:TIGR00384 157 PE-FLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
7-237 2.54e-125

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 354.65  E-value: 2.54e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   7 IYRYNPDVDNAPRMQDYTLEGEEGrDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALTqpg 86
Cdd:PRK12575    9 IYRYDPDDDAAPRMQRYEIAPRAE-DRMLLDVLGRVKAQDETLSYRRSCREGICGSDAMNINGRNGLACLTNMQALP--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  87 KKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQnPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNP 166
Cdd:PRK12575   85 REIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTV-PPERERLQTPQEREQLDGLYECILCACCSTACPSYWWNP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709035576 167 DKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRS 237
Cdd:PRK12575  164 DKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTMLARRA 234
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 4-234 4.14e-122

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 347.93  E-value: 4.14e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   4 EFSIYRYNPDVDNAPRMQDYTLEGEEGRDMMLlDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAl 82
Cdd:PLN00129   45 EFQIYRWNPDNPGKPHLQSYKVDLNDCGPMVL-DVLIKIKnEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDR- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  83 tQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYL-LNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPS 161
Cdd:PLN00129  123 -DESGPTTITPLPHMFVIKDLVVDMTNFYQQYKSIEPWLkTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPS 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709035576 162 FWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLL 234
Cdd:PLN00129  202 YWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEALDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLG 274
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-238 1.16e-66

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 208.78  E-value: 1.16e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   1 MKLEFSIYRYNPDvdNAPRMQDYTLEGEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLAC---- 75
Cdd:PRK12577    1 MEVLFKILRQKQN--SAPYVQTYTLEVEPG--NTILDCLNRIKwEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  76 ---ITPISALTQPG-KKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECIL 151
Cdd:PRK12577   77 gseLARLSDSNSGAiPEITIAPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTAARQVPEREFLQTPEERSKLDQTGNCIL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576 152 CACCSTSCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGMS-DAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIK 230
Cdd:PRK12577  157 CGACYSECNAREVNPE-FVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235


                  ....*...
gi 1709035576 231 SMLLQRSA 238
Cdd:PRK12577  236 QEILARKD 243
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-231 3.05e-59

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 188.42  E-value: 3.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   1 MKLEFSIYRYNPDvdNAPRMQDYTLEGEegRDMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACIT-P 78
Cdd:PRK12576    7 KEVIFKVKRYDPE--KGSWWQEYKVKVD--RFTQVTEALRRIKeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTlV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  79 ISALTQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLL-NNGQNPPAREHLQMPEQREKLDGLYECILCACCST 157
Cdd:PRK12576   83 LDVAKKYNSVITIEPMDYFKVVKDLIVDFDEFYERMFKVKPRLYrAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVS 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709035576 158 SCPSFWWNPdKFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDafSVFRCHSIMNCVSVCPKGLNPTRAIGHIKS 231
Cdd:PRK12576  163 ACPVVAIDP-EFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVTAIKKTRS 233
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
1-226 4.92e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 176.43  E-value: 4.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   1 MKLEfsIYRYNPDVDNAPRMQDYTLEGEEgrDMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITpi 79
Cdd:PRK12385    7 LKIE--VLRYNPEVDTEPHSQTYEVPYDE--TTSLLDALGYIKDNlAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  80 sALTQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSC 159
Cdd:PRK12385   81 -FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYHQFSGCINCGLCYAAC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709035576 160 PSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPTRAI 226
Cdd:PRK12385  160 PQFGLNPE-FIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAI 225
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 2-220 1.08e-49

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 162.43  E-value: 1.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   2 KLEFSIYRYNP-DVDNAPRMQDYTLEGEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPI 79
Cdd:PRK13552    4 TLTFNIFRYNPqDPGSKPHMVTYQLEETPG--MTLFIALNRIREEqDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  80 SALtqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQ-YEKIKPYLLNNGQNPPAREHLQM-PEQREKLDGLYECILCACCST 157
Cdd:PRK13552   82 SDY--PDGVITLMPLPVFKLIGDLSVNTGKWFREmSERVESWIHTDKEFDIHRLEERMePEEADEIYELDRCIECGCCVA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709035576 158 SCPSFWWNPDkFIGPAGLLAAYRFLIDSRDTETDSRL-EGMSDAFSVFRCHSIMNCVSVCPKGL 220
Cdd:PRK13552  160 ACGTKQMRED-FVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDL 222
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 5-112 6.10e-46

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: 148.54  E-value: 6.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   5 FSIYRYNPDVD-NAPRMQDYTLEGEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISAL 82
Cdd:pfam13085   2 LRVFRYDPRVDrDEPYYQEYEVPYEEG--MTVLDALNKIKEEqDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1709035576  83 tqPGKKIVIRPLPGLPVIRDLVVDMGQFYA 112
Cdd:pfam13085  80 --LGQDITLEPLPGFPVIRDLVVDRSAFFE 107
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 7-226 4.47e-35

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 130.13  E-value: 4.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   7 IYRYNPDVDnAPRMQDYTLEGEEGrdMMLLDALIQLKEK-DPSLSFRRSCREGVCGSDGLNMNGKNGLACITPIsaltQP 85
Cdd:PRK06259    8 VKRFDPEKD-EPHFESYEVPVKEG--MTVLDALEYINKTyDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV----ED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  86 GkkIVIRPLpGLPVIRDLVVDMGQFYAQYEKIKPYLLnngqnpPAREHLQMPEQREKLDGLYECILCACCSTSCPSFwwN 165
Cdd:PRK06259   81 G--MIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQ------RKNEKITYPEDIEDIKKLRGCIECLSCVSTCPAR--K 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709035576 166 PDKFIGPAGLLAAYRFLIDSRDTETDSRlegmsDAF--SVFRCHSIMNCVSVCPKGLN-PTRAI 226
Cdd:PRK06259  150 VSDYPGPTFMRQLARFAFDPRDEGDREK-----EAFdeGLYNCTTCGKCVEVCPKEIDiPGKAI 208
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 2-223 5.29e-22

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 90.91  E-value: 5.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   2 KLEFSIYRYNpdvDNAPRMQDYTLEGEEGrdMMLLDALIQLK-EKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPIS 80
Cdd:PRK12386    4 TAKFRVWRGD---ASGGELQDYTVEVNEG--EVVLDVIHRLQaTQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  81 ALTqPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYllnngqNPPAR----EHLQMPEQREKLDGLYECILCACCS 156
Cdd:PRK12386   79 TFD-EDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSF------TPPKDlqpgEYRMQQVDVERSQEFRKCIECFLCQ 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709035576 157 TSC---PSFWWNPDKFIGPagllaayRFLI-----DSRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCPKGLNPT 223
Cdd:PRK12386  152 NVChvvRDHEENKPAFAGP-------RFLMriaelEMHPLDTADRRAEAQEEHGLGYCNITKCCTEVCPEHIKIT 219
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 55-229 2.07e-21

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 89.28  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  55 CREGVCGSDGLNMNGKNGLACITPISALTQPgkkIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKP-------YLLNNGQN 127
Cdd:PRK08640   63 CLEEVCGACSMVINGKPRQACTALIDQLEQP---IRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAwipidgtYDLGPGPR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576 128 PParehlqmPEQREKLDGLYECILCACCSTSCPSFwwNPD-KFIGPAGLLAAYRF-LIDSRDTETDSRLEGMSDAFSVFR 205
Cdd:PRK08640  140 MP-------EEKRQWAYELSKCMTCGCCLEACPNV--NEKsDFIGPAAISQVRLFnAHPTGEMHKEERLRALMGDGGIAD 210

                         170       180
                  ....*....|....*....|....
gi 1709035576 206 CHSIMNCVSVCPKGLNPTRAIGHI 229
Cdd:PRK08640  211 CGNAQNCVRVCPKGIPLTTSIAAM 234
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 1-221 5.53e-10

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 57.53  E-value: 5.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576   1 MKLEFSIYRyNPDVDNAPRMQDYTLEGEEGrDMMLLDALIQLKE------KDPsLSFRRSCREGVCGSDGLNMNGK-NGL 73
Cdd:PRK07570    1 MKLTLKIWR-QKGPDDKGKFETYEVDDISP-DMSFLEMLDVLNEqliekgEEP-VAFDHDCREGICGMCGLVINGRpHGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576  74 ACITPISALT----QPGKKIVIRPL--PGLPVIRDLVVDMGQFyaqyEKI----KPYLLNNGQNPPAREHLQMPEQREKL 143
Cdd:PRK07570   78 DRGTTTCQLHmrsfKDGDTITIEPWraAAFPVIKDLVVDRSAL----DRIiqagGYVSVNTGGAPDANAIPVPKEDADRA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576 144 DGLYECILCACCSTSCPSfwwnpdkfiGPAGLLAAYRF----LIDSRDTETDSRLEGMSDAFSV--F-RCHSIMNCVSVC 216
Cdd:PRK07570  154 FDAAACIGCGACVAACPN---------GSAMLFTGAKVshlaLLPQGQPERARRVRAMVAQMDEegFgNCTNTGECEAVC 224


                  ....*
gi 1709035576 217 PKGLN 221
Cdd:PRK07570  225 PKGIS 229
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 148-221 3.08e-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: 49.00  E-value: 3.08e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709035576 148 ECILCACCSTSCPSFWWNPDKfigPAGLLAAYRFlidsrdtetdSRLEGMSDAFSVFRCHSIMNCVSVCPKGLN 221
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKLMRAAYL----------GDLEELQANKVANLCSECGLCEYACPMGLD 61
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 149-220 2.76e-07

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: 46.54  E-value: 2.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709035576 149 CILCACCSTSCPSFwwnpdkfigpagLLAAYRFLIDSRDTETDSRLE---GMSDAFSVFRCHSIMNCVSVCPKGL 220
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRleaLEGLAEGLWLCTLCGACTEVCPVGI 64
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
145-236 4.53e-05

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 40.65  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576 145 GLYECILCACCSTSCPSFWW---NPDKFIgpagllaaYRFLIDSRDTETDSRlegmsdafSVFRCHSIMNCVSVCPKGLN 221
Cdd:COG1150     1 NLKKCYQCGTCTASCPVARAmdyNPRKII--------RLAQLGLKEEVLKSD--------SIWLCVSCYTCTERCPRGID 64

                          90
                  ....*....|....*
gi 1709035576 222 PTRAIGHIKSMLLQR 236
Cdd:COG1150    65 IADVMDALRNLAIRE 79
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 119-235 1.09e-04

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 42.76  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709035576 119 PYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSrlEGMS 198
Cdd:COG0247    50 PGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELPLDLS--EEVY 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709035576 199 DAFsvFRCHSIMNCVSVCPKGLNptraIGHIKSMLLQ 235
Cdd:COG0247   128 EVL--DLCLTCKACETACPSGVD----IADLIAEARA 158
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 149-217 1.24e-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: 36.07  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709035576 149 CILCACCSTSCPSFWWnpdkfigpagllaayrflidsRDTETDSRLEGMSDAFSVFRCHSIMNCVSVCP 217
Cdd:pfam13237   9 CIGCGRCTAACPAGLT---------------------RVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
 
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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