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Conserved domains on  [gi|1002291737|ref|XP_015650213|]
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succinate dehydrogenase [ubiquinone] iron-sulfur subunit 1, mitochondrial isoform X2 [Oryza sativa Japonica Group]

Protein Classification

succinate dehydrogenase iron-sulfur subunit( domain architecture ID 11476389)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 3-281 4.80e-180

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


:

Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 496.62  E-value: 4.80e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737   3 AAALLRRSPAARALLSPALSSRLVASKPHSSSPAPPPPpskaGANTKTFSIYRWDPDSPStKPHLKDYKVDLSDCGPMVL 82
Cdd:PLN00129    2 AAGLLRRLAGAKAGLLAPAAAASAAASAETKASSKGSK----PSNLKEFQIYRWNPDNPG-KPHLQSYKVDLNDCGPMVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  83 DVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSASSASTI-SPLPHMFVIKDLVVDMTNFYNQYKSV 161
Cdd:PLN00129   77 DVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTiTPLPHMFVIKDLVVDMTNFYQQYKSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 162 EPWLKRKDAPPQPGKEIPQTKADRAKLDGMYECILCACCSTSCPSYWWNPEEYLGPAALLHANRWIQDSRDQFTKERLDS 241
Cdd:PLN00129  157 EPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEA 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002291737 242 INDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKLQLEA 281
Cdd:PLN00129  237 LDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 3-281 4.80e-180

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 496.62  E-value: 4.80e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737   3 AAALLRRSPAARALLSPALSSRLVASKPHSSSPAPPPPpskaGANTKTFSIYRWDPDSPStKPHLKDYKVDLSDCGPMVL 82
Cdd:PLN00129    2 AAGLLRRLAGAKAGLLAPAAAASAAASAETKASSKGSK----PSNLKEFQIYRWNPDNPG-KPHLQSYKVDLNDCGPMVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  83 DVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSASSASTI-SPLPHMFVIKDLVVDMTNFYNQYKSV 161
Cdd:PLN00129   77 DVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTiTPLPHMFVIKDLVVDMTNFYQQYKSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 162 EPWLKRKDAPPQPGKEIPQTKADRAKLDGMYECILCACCSTSCPSYWWNPEEYLGPAALLHANRWIQDSRDQFTKERLDS 241
Cdd:PLN00129  157 EPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEA 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002291737 242 INDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKLQLEA 281
Cdd:PLN00129  237 LDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 47-281 2.94e-113

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: 325.55  E-value: 2.94e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  47 NTKTFSIYRWDPDSPStKPHLKDYKVDLsDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKI 126
Cdd:COG0479     1 MTVTLKIWRQDPETDS-KPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 127 SSASSASTISPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPQpgKEIPQTKADRAKLDGMYECILCACCSTSCPS 206
Cdd:COG0479    79 RDLKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPD--NERLQSPEDREKADDLAECILCGACVAACPN 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002291737 207 YWWNPeEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKLQLEA 281
Cdd:COG0479   157 VWANP-DFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 53-275 5.69e-102

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: 296.65  E-value: 5.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  53 IYRWDPDSPsTKPHLKDYKVDLSDCgPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSASSA 132
Cdd:TIGR00384   1 VLRFNPDVD-EKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 133 STI-SPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPqPGKEIPQTKADRAKLDGMYECILCACCSTSCPSYWWNP 211
Cdd:TIGR00384  79 VMKiEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPE-PEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002291737 212 eEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIK 275
Cdd:TIGR00384 158 -EFLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 50-156 1.11e-44

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: 146.61  E-value: 1.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  50 TFSIYRWDPDSPSTKPHLKDYKVDLsDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSA 129
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 1002291737 130 SSASTI-SPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085  80 LGQDITlEPLPGFPVIRDLVVDRSAFFE 107
 
Name Accession Description Interval E-value
PLN00129 PLN00129
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
 3-281 4.80e-180

succinate dehydrogenase [ubiquinone] iron-sulfur subunit


Pssm-ID: 215067 [Multi-domain]  Cd Length: 276  Bit Score: 496.62  E-value: 4.80e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737   3 AAALLRRSPAARALLSPALSSRLVASKPHSSSPAPPPPpskaGANTKTFSIYRWDPDSPStKPHLKDYKVDLSDCGPMVL 82
Cdd:PLN00129    2 AAGLLRRLAGAKAGLLAPAAAASAAASAETKASSKGSK----PSNLKEFQIYRWNPDNPG-KPHLQSYKVDLNDCGPMVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  83 DVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSASSASTI-SPLPHMFVIKDLVVDMTNFYNQYKSV 161
Cdd:PLN00129   77 DVLIKIKNEQDPSLTFRRSCREGICGSCAMNIDGKNTLACLTKIDRDESGPTTiTPLPHMFVIKDLVVDMTNFYQQYKSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 162 EPWLKRKDAPPQPGKEIPQTKADRAKLDGMYECILCACCSTSCPSYWWNPEEYLGPAALLHANRWIQDSRDQFTKERLDS 241
Cdd:PLN00129  157 EPWLKTKKPPEDGQKEHLQSKEDRAKLDGMYECILCACCSTSCPSYWWNPEKFLGPAALLHAYRWISDSRDEYTKERLEA 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002291737 242 INDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKLQLEA 281
Cdd:PLN00129  237 LDDEFKLYRCHTIRNCSNACPKGLNPAKAIAKIKQLLGLG 276
sdhB PRK05950
succinate dehydrogenase iron-sulfur subunit; Reviewed
 50-280 8.95e-145

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 235652 [Multi-domain]  Cd Length: 232  Bit Score: 405.33  E-value: 8.95e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  50 TFSIYRWDPDSPStKPHLKDYKVDLSDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSA 129
Cdd:PRK05950    1 TFKIYRYNPDVDA-NPRMQTYEVDVDECGPMVLDALIKIKNEIDPTLTFRRSCREGVCGSDAMNINGKNGLACITPISDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 130 SSASTI-SPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDapPQPGKEIPQTKADRAKLDGMYECILCACCSTSCPSYW 208
Cdd:PRK05950   80 KKGKIViRPLPGLPVIKDLVVDMTQFYAQYRSIKPYLINDT--PPPARERLQSPEDREKLDGLYECILCACCSTSCPSFW 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002291737 209 WNPEEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKLQLE 280
Cdd:PRK05950  158 WNPDKFLGPAALLQAYRFIADSRDEATGERLDILDDPFGVFRCHTIMNCVEVCPKGLNPTKAIGEIKRMLLE 229
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 47-281 2.94e-113

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: 325.55  E-value: 2.94e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  47 NTKTFSIYRWDPDSPStKPHLKDYKVDLsDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKI 126
Cdd:COG0479     1 MTVTLKIWRQDPETDS-KPRFQTYEVPV-SPGMTVLDALDYIKEEQDPTLAFRRSCREGICGSCAMVINGRPRLACQTHV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 127 SSASSASTISPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPQpgKEIPQTKADRAKLDGMYECILCACCSTSCPS 206
Cdd:COG0479    79 RDLKDTITIEPLRNFPVIKDLVVDRSAFFDKLKKVKPYLSPDGPAPD--NERLQSPEDREKADDLAECILCGACVAACPN 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002291737 207 YWWNPeEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKLQLEA 281
Cdd:COG0479   157 VWANP-DFLGPAALAQAYRFALDPRDEETEERLEALEDEEGVWRCTTCGNCTEVCPKGIPPTKAIAKLKREALKR 230
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 53-275 5.69e-102

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: 296.65  E-value: 5.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  53 IYRWDPDSPsTKPHLKDYKVDLSDCgPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSASSA 132
Cdd:TIGR00384   1 VLRFNPDVD-EKPHLQSYEVPADEG-MTVLDALNYIKDEQDPSLAFRRSCRNGICGSCAMNVNGKPVLACKTKVEDLGQP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 133 STI-SPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPqPGKEIPQTKADRAKLDGMYECILCACCSTSCPSYWWNP 211
Cdd:TIGR00384  79 VMKiEPLPNLPVIKDLVVDMGPFYAKLEAIKPYLIRKSQPE-PEGEFLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002291737 212 eEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIK 275
Cdd:TIGR00384 158 -EFLGPAALTAAYRFLIDSRDHATKDRLEGLNDKNGVWRCTTCMNCSEVCPKGVNPARAIEKLK 220
PRK12575 PRK12575
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
46-277 1.88e-99

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 171592 [Multi-domain]  Cd Length: 235  Bit Score: 291.09  E-value: 1.88e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  46 ANTKTFSIYRWDPDsPSTKPHLKDYKVDLSDCGPMVLDVLLKIKnEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTK 125
Cdd:PRK12575    2 ADTRILHIYRYDPD-DDAAPRMQRYEIAPRAEDRMLLDVLGRVK-AQDETLSYRRSCREGICGSDAMNINGRNGLACLTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 126 ISSASSASTISPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPQpgKEIPQTKADRAKLDGMYECILCACCSTSCP 205
Cdd:PRK12575   80 MQALPREIVLRPLPGLPVVRDLIVDMTDFFNQYHSIRPYLINDTVPPE--RERLQTPQEREQLDGLYECILCACCSTACP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002291737 206 SYWWNPEEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIKKL 277
Cdd:PRK12575  158 SYWWNPDKFVGPAGLLQAYRFIADSRDDATAARLDDLEDPYRLFRCRTIMNCVDVCPKGLNPARAIGQIRTM 229
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
50-275 5.61e-55

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 180.66  E-value: 5.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  50 TFSIYRWDPDSPstkPHLKDYKVDLsDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLAC------- 122
Cdd:PRK12577    4 LFKILRQKQNSA---PYVQTYTLEV-EPGNTILDCLNRIKWEQDGSLAFRKNCRNTICGSCAMRINGRSALACkenvgse 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 123 LTKISSASSASTIS----PLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKdAPPQPGKEIPQTKADRAKLDGMYECILCA 198
Cdd:PRK12577   80 LARLSDSNSGAIPEitiaPLGNMPVIKDLVVDMSSFWQNLEAVDPYVSTA-ARQVPEREFLQTPEERSKLDQTGNCILCG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002291737 199 CCSTSCPSYWWNPeEYLGPAALLHANRWIQDSRDQFTKERLDSIN-DEFKLYRCHTIKNCTHACPKGLNPAKHIDTIK 275
Cdd:PRK12577  159 ACYSECNAREVNP-EFVGPHALAKAQRMVADSRDTATEQRLELYNqGTAGVWGCTRCYYCNSVCPMEVAPLDQITKIK 235
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
50-278 2.66e-53

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 174.55  E-value: 2.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  50 TFSIYRWDPDSPStkpHLKDYKVDLsDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSA 129
Cdd:PRK12576   10 IFKVKRYDPEKGS---WWQEYKVKV-DRFTQVTEALRRIKEEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVLDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 130 SSASTIS----PLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPQPGKEIPQTKADRAKLDGMYECILCACCSTSCP 205
Cdd:PRK12576   86 AKKYNSVitiePMDYFKVVKDLIVDFDEFYERMFKVKPRLYRAKEVLEGKAEHRLKPEDQKELWKFAQCIWCGLCVSACP 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002291737 206 SYWWNPeEYLGPAALLHANRWIQDSRDQFTKERLDSINDefKLYRCHTIKNCTHACPKGLNPAKhidTIKKLQ 278
Cdd:PRK12576  166 VVAIDP-EFLGPAAHAKGYRFLADPRDTITEERMKILID--SSWRCTYCYSCSNVCPRDIEPVT---AIKKTR 232
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
45-275 4.72e-47

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 157.56  E-value: 4.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  45 GANTKTFSIYRWDPDSPStKPHLKDYKVDLSDcGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLT 124
Cdd:PRK12385    3 EMKNLKIEVLRYNPEVDT-EPHSQTYEVPYDE-TTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 125 KISSASSASTISPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPQPGKEIpQTKADRAKLDGMYECILCACCSTSC 204
Cdd:PRK12385   81 FLRDYTGGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNDRTPDDGPNK-QTPAQMAKYHQFSGCINCGLCYAAC 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002291737 205 PSYWWNPeEYLGPAALLHANRWIQDSRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKHIDTIK 275
Cdd:PRK12385  160 PQFGLNP-EFIGPAAITLAHRYNLDSRDHGKKERMKQLNGQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGK 229
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 50-156 1.11e-44

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: 146.61  E-value: 1.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  50 TFSIYRWDPDSPSTKPHLKDYKVDLsDCGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISSA 129
Cdd:pfam13085   1 TLRVFRYDPRVDRDEPYYQEYEVPY-EEGMTVLDALNKIKEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTLIDDL 79

                          90       100
                  ....*....|....*....|....*...
gi 1002291737 130 SSASTI-SPLPHMFVIKDLVVDMTNFYN 156
Cdd:pfam13085  80 LGQDITlEPLPGFPVIRDLVVDRSAFFE 107
frdB PRK13552
fumarate reductase iron-sulfur subunit; Provisional
 50-265 7.87e-38

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 184136 [Multi-domain]  Cd Length: 239  Bit Score: 133.54  E-value: 7.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  50 TFSIYRWDPDSPSTKPHLKDYKVDLSDcgPMVLDVLL-KIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKISS 128
Cdd:PRK13552    6 TFNIFRYNPQDPGSKPHMVTYQLEETP--GMTLFIALnRIREEQDPSLQFDFVCRAGICGSCAMVINGRPTLACRTLTSD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 129 ASSAS-TISPLPHMFVIKDLVVDMTNFYNQ-YKSVEPWLkRKDAPPQPGKeiPQTKADRAKLDGMYE---CILCACCSTS 203
Cdd:PRK13552   84 YPDGViTLMPLPVFKLIGDLSVNTGKWFREmSERVESWI-HTDKEFDIHR--LEERMEPEEADEIYEldrCIECGCCVAA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002291737 204 CPSYWWNPeEYLGPAALLHANRWIQDSRDQFTKERL-DSINDEFKLYRCHTIKNCTHACPKGL 265
Cdd:PRK13552  161 CGTKQMRE-DFVGAVGLNRIARFELDPRDERTDEDFyELIGNDDGVFGCMSLLGCEDNCPKDL 222
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 49-277 6.51e-34

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 128.20  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  49 KTFSIYRWDPDSPSTKPHLKDYKVDLSDcGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKiss 128
Cdd:PRK06259    2 KMITITVKRFDPEKDEPHFESYEVPVKE-GMTVLDALEYINKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTE--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 129 ASSASTISPLpHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAPPQPGKEIPQTKADRakldgmyECILCACCSTSCPSYw 208
Cdd:PRK06259   78 VEDGMIIEPL-DFPVIKDLIVDREPYYKKLKSLRNYLQRKNEKITYPEDIEDIKKLR-------GCIECLSCVSTCPAR- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 209 wNPEEYLGPAALLHANRWIQDSRDQFTKERlDSINDefKLYRCHTIKNCTHACPKGLN-PAKHIDTIKKL 277
Cdd:PRK06259  149 -KVSDYPGPTFMRQLARFAFDPRDEGDREK-EAFDE--GLYNCTTCGKCVEVCPKEIDiPGKAIEKLRAL 214
PRK12386 PRK12386
fumarate reductase iron-sulfur subunit; Provisional
 48-265 9.35e-20

fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 237086 [Multi-domain]  Cd Length: 251  Bit Score: 85.91  E-value: 9.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  48 TKTFSIYRWDPDSPStkphLKDYKVDLSDcGPMVLDVLLKIKNEQDPSLTFRRSCREGICGSCAMNIDGDNGLACLTKIS 127
Cdd:PRK12386    4 TAKFRVWRGDASGGE----LQDYTVEVNE-GEVVLDVIHRLQATQAPDLAVRWNCKAGKCGSCSAEINGRPRLMCMTRMS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 128 --SASSASTISPLPHMFVIKDLVVDMTNFYNQYKSVEPWLKRKDAppQPGKEIPQtKADRAKLDGMYECILCACCSTSC- 204
Cdd:PRK12386   79 tfDEDETVTVTPMRTFPVIRDLVTDVSFNYEKAREIPSFTPPKDL--QPGEYRMQ-QVDVERSQEFRKCIECFLCQNVCh 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002291737 205 --PSYWWNPEEYLGPAALLHANRWIQDSRDqfTKERLDSINDEFKLYRCHTIKNCTHACPKGL 265
Cdd:PRK12386  156 vvRDHEENKPAFAGPRFLMRIAELEMHPLD--TADRRAEAQEEHGLGYCNITKCCTEVCPEHI 216
sdhB PRK08640
succinate dehydrogenase iron-sulfur subunit; Reviewed
 47-265 9.64e-16

succinate dehydrogenase iron-sulfur subunit; Reviewed


Pssm-ID: 181515 [Multi-domain]  Cd Length: 249  Bit Score: 74.64  E-value: 9.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  47 NTKTFSIYRWDpdSPSTKPHLKDYKVDLSDcGPMVLDVLLKI-------KNEQDPSLTFRRSCREGICGSCAMNIDGDNG 119
Cdd:PRK08640    4 KTVRLIIKRQD--GPDSKPYWEEFEIPYRP-NMNVISALMEIrrnpvnaKGEKTTPVVWDMNCLEEVCGACSMVINGKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 120 LACLTKISSASSASTISPLPHMFVIKDLVVDMTNFYNQYKSVEPWLK-RKDAPPQPGKEIPQTKADRakldgMYE---CI 195
Cdd:PRK08640   81 QACTALIDQLEQPIRLEPMSTFPVVRDLQVDRSRMFDNLKRVKAWIPiDGTYDLGPGPRMPEEKRQW-----AYElskCM 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002291737 196 LCACCSTSCPSYwwNPE-EYLGPAALLHANRWIQDSRDQFTK-ERLDSINDEFKLYRCHTIKNCTHACPKGL 265
Cdd:PRK08640  156 TCGCCLEACPNV--NEKsDFIGPAAISQVRLFNAHPTGEMHKeERLRALMGDGGIADCGNAQNCVRVCPKGI 225
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 193-266 4.63e-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: 4.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002291737 193 ECILCACCSTSCPSYWWNPEEylgPAALlhanrwiqdsRDQFTKERLDSINDEFKLYRCHTIKNCTHACPKGLN 266
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDE---PKKL----------MRAAYLGDLEELQANKVANLCSECGLCEYACPMGLD 61
PRK07570 PRK07570
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
 56-205 1.46e-07

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated


Pssm-ID: 181038 [Multi-domain]  Cd Length: 250  Bit Score: 51.37  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737  56 WDPDSPSTKPHLKDYKVDlsDCGP-M----VLDVLlkikNEQ------DPsLTFRRSCREGICGSCAMNIDG------DN 118
Cdd:PRK07570    8 WRQKGPDDKGKFETYEVD--DISPdMsfleMLDVL----NEQliekgeEP-VAFDHDCREGICGMCGLVINGrphgpdRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 119 GLACLTkissassastisplpHMF-------------------VIKDLVVDMTNF-----YNQYKSVE----PwlkrkDA 170
Cdd:PRK07570   81 TTTCQL---------------HMRsfkdgdtitiepwraaafpVIKDLVVDRSALdriiqAGGYVSVNtggaP-----DA 140

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002291737 171 PPQPgkeIPQTKADRAkLDGMyECILCACCSTSCP 205
Cdd:PRK07570  141 NAIP---VPKEDADRA-FDAA-ACIGCGACVAACP 170
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 194-265 1.01e-06

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: 45.38  E-value: 1.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002291737 194 CILCACCSTSCPSYwwnpeeylgpaaLLHANRWIQDSRDQFTKERLDS---INDEFKLYRCHTIKNCTHACPKGL 265
Cdd:pfam13183   2 CIRCGACLAACPVY------------LVTGGRFPGDPRGGAAALLGRLealEGLAEGLWLCTLCGACTEVCPVGI 64
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 137-272 4.81e-05

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 44.30  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 137 PLPHMFVIKDLVVDMTNFYNQYKSVEPW--LKRKDAPPQPGKEIPQTKADRAkLDGMYECILCACCSTSCPSYWWNPEEY 214
Cdd:COG0247    22 FLELELGKIKYAFDPDNKLNPGKIGLLNpgVELLGDGDLHDKNLKTLPWKEL-LDALDACVGCGFCRAMCPSYKATGDEK 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 215 LGPAALLHANRWIQDSRDQFTkerldsINDEFK--LYRCHTIKNCTHACPKGLNPAKHID 272
Cdd:COG0247   101 DSPRGRINLLREVLEGELPLD------LSEEVYevLDLCLTCKACETACPSGVDIADLIA 154
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
194-280 1.23e-03

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


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 36.80  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291737 194 CILCACCSTSCPSYWW---NPEEYLgpaallhanRWIQdsrdqftKERLDSINDEFKLYRCHTIKNCTHACPKGLNPAKH 270
Cdd:COG1150     5 CYQCGTCTASCPVARAmdyNPRKII---------RLAQ-------LGLKEEVLKSDSIWLCVSCYTCTERCPRGIDIADV 68

                          90
                  ....*....|
gi 1002291737 271 IDTIKKLQLE 280
Cdd:COG1150    69 MDALRNLAIR 78
 
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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