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Conserved domains on  [gi|442618548|ref|NP_001262472|]
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succinate dehydrogenase, subunit C, isoform B [Drosophila melanogaster]

Protein Classification

succinate:quinone oxidoreductase subunit C( domain architecture ID 10131276)

succinate:quinone oxidoreductase transmembrane subunit C, together with the D subunit, acts to anchor the catalytic components of succinate dehydrogenase to the cytoplasmic membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SQR_TypeC_SdhC cd03499
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) ...
 52-170 8.16e-34

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) subunit; composed of bacterial SdhC and eukaryotic large cytochrome b binding (CybL) proteins. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this family reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Proteins in this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. The heme and quinone binding sites reside in the transmembrane subunits. The SdhC or CybL protein is one of the two transmembrane subunits of bacterial and eukaryotic SQRs. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.


:

Pssm-ID: 239579  Cd Length: 117  Bit Score: 115.71  E-value: 8.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEglQLSGATLTALKFIIAYPAGYHTA 131
Cdd:cd03499    1 RPLSPHLTIYRPPLTAILSILHRITGVALFLGLPLLLWWLLASLSSPESFESVSA--LLGSWLGKLVLFGLTWALFYHLL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442618548 132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILAL 170
Cdd:cd03499   79 NGIRHLIWDLGKGLELKTVYKSGYAVLVLSVVLTVLLGI 117
 
Name Accession Description Interval E-value
SQR_TypeC_SdhC cd03499
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) ...
 52-170 8.16e-34

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) subunit; composed of bacterial SdhC and eukaryotic large cytochrome b binding (CybL) proteins. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this family reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Proteins in this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. The heme and quinone binding sites reside in the transmembrane subunits. The SdhC or CybL protein is one of the two transmembrane subunits of bacterial and eukaryotic SQRs. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.


Pssm-ID: 239579  Cd Length: 117  Bit Score: 115.71  E-value: 8.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEglQLSGATLTALKFIIAYPAGYHTA 131
Cdd:cd03499    1 RPLSPHLTIYRPPLTAILSILHRITGVALFLGLPLLLWWLLASLSSPESFESVSA--LLGSWLGKLVLFGLTWALFYHLL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442618548 132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILAL 170
Cdd:cd03499   79 NGIRHLIWDLGKGLELKTVYKSGYAVLVLSVVLTVLLGI 117
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 49-168 3.07e-24

Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.


Pssm-ID: 426067  Cd Length: 122  Bit Score: 91.29  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548   49 RLGRELSPHLTIYQPQLTSMLSICHRGTGLA---LGVGVWGLGLGALISSHDISHYVTMVEGLqlSGATLTALKFIIAYP 125
Cdd:pfam01127   2 RKNRPLSPHLGLYRAHLTTWLSILHRITGVAlavLGLIFLLLWLLLLLSLLGPESYATVVAWL--ASPVKLILLLLLLLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 442618548  126 AGYHTANGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAIL 168
Cdd:pfam01127  80 LFYHAANGIRHLIWDVGFGLELKTVRKSGAAVLALSVVLVIVL 122
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 52-171 1.27e-17

Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and conversion];


Pssm-ID: 441612  Cd Length: 128  Bit Score: 74.43  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEGLQLSGATLTALKFIIAYpaGYHTA 131
Cdd:COG2009    7 RPLSPHLQIYRLPLTMIVSILHRITGVALFLGLPLLVWWLAASASSPEAFAAVQAFLGSPLGKLVLLGLTWAL--LYHLL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 442618548 132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILALL 171
Cdd:COG2009   85 AGIRHLLWDFGYGFELETARRSAWVVLVLSVVLTVLLGVV 124
succ_dehyd_cytB TIGR02970
succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two ...
 52-171 1.21e-14

succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two small, hydrophobic, mutually homologous subunits of succinate dehydrogenase, a TCA cycle enzyme, are SdhC and SdhD. This family is the SdhC, the cytochrome b subunit, called b556 in bacteria and b560 in mitochondria. SdhD (see TIGR02968) is called the hydrophobic membrane anchor subunit, although both SdhC and SdhD participate in anchoring the complex. In some bacteria, this cytochrome b subunit is replaced my a member of the cytochrome b558 family (see TIGR02046). [Energy metabolism, TCA cycle]


Pssm-ID: 274370  Cd Length: 120  Bit Score: 66.44  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548   52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEGLQLSGATLTALKFIIAYpaGYHTA 131
Cdd:TIGR02970   3 RPLSPHLQIYRFPITAILSILHRITGVLLFFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKLILWGLLWAL--LYHLL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 442618548  132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILALL 171
Cdd:TIGR02970  81 AGIRHLLWDLGYGLELKSARISAWVVLVLSLVLTILAGIW 120
PLN00127 PLN00127
succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional
 45-171 2.80e-10

succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional


Pssm-ID: 177738  Cd Length: 178  Bit Score: 56.04  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  45 EKNERlgRELSPHL-------TIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDIShyVTMVEGLQLSGATLTA 117
Cdd:PLN00127  47 MLLEK--RPLSPDVmdidgksTHYKFPVVALSSITNRVTGCVLSGGAAGGGVLALVGGSEAV--PATMEGFKSGGPLIVF 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442618548 118 -LKFIIAYPAGYHTANGIRHLLWD-TGRFLKIKEVYSTGYAMVATSFVLSAILALL 171
Cdd:PLN00127 123 pAKFAVSFPFVYHTLGGLRHLVWDkTTEGLDNPSVEASSYGLFGASAALSAAAAVL 178
 
Name Accession Description Interval E-value
SQR_TypeC_SdhC cd03499
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) ...
 52-170 8.16e-34

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) subunit; composed of bacterial SdhC and eukaryotic large cytochrome b binding (CybL) proteins. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this family reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Proteins in this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. The heme and quinone binding sites reside in the transmembrane subunits. The SdhC or CybL protein is one of the two transmembrane subunits of bacterial and eukaryotic SQRs. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.


Pssm-ID: 239579  Cd Length: 117  Bit Score: 115.71  E-value: 8.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEglQLSGATLTALKFIIAYPAGYHTA 131
Cdd:cd03499    1 RPLSPHLTIYRPPLTAILSILHRITGVALFLGLPLLLWWLLASLSSPESFESVSA--LLGSWLGKLVLFGLTWALFYHLL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442618548 132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILAL 170
Cdd:cd03499   79 NGIRHLIWDLGKGLELKTVYKSGYAVLVLSVVLTVLLGI 117
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 49-168 3.07e-24

Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.


Pssm-ID: 426067  Cd Length: 122  Bit Score: 91.29  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548   49 RLGRELSPHLTIYQPQLTSMLSICHRGTGLA---LGVGVWGLGLGALISSHDISHYVTMVEGLqlSGATLTALKFIIAYP 125
Cdd:pfam01127   2 RKNRPLSPHLGLYRAHLTTWLSILHRITGVAlavLGLIFLLLWLLLLLSLLGPESYATVVAWL--ASPVKLILLLLLLLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 442618548  126 AGYHTANGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAIL 168
Cdd:pfam01127  80 LFYHAANGIRHLIWDVGFGLELKTVRKSGAAVLALSVVLVIVL 122
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 52-171 1.27e-17

Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and conversion];


Pssm-ID: 441612  Cd Length: 128  Bit Score: 74.43  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEGLQLSGATLTALKFIIAYpaGYHTA 131
Cdd:COG2009    7 RPLSPHLQIYRLPLTMIVSILHRITGVALFLGLPLLVWWLAASASSPEAFAAVQAFLGSPLGKLVLLGLTWAL--LYHLL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 442618548 132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILALL 171
Cdd:COG2009   85 AGIRHLLWDFGYGFELETARRSAWVVLVLSVVLTVLLGVV 124
succ_dehyd_cytB TIGR02970
succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two ...
 52-171 1.21e-14

succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two small, hydrophobic, mutually homologous subunits of succinate dehydrogenase, a TCA cycle enzyme, are SdhC and SdhD. This family is the SdhC, the cytochrome b subunit, called b556 in bacteria and b560 in mitochondria. SdhD (see TIGR02968) is called the hydrophobic membrane anchor subunit, although both SdhC and SdhD participate in anchoring the complex. In some bacteria, this cytochrome b subunit is replaced my a member of the cytochrome b558 family (see TIGR02046). [Energy metabolism, TCA cycle]


Pssm-ID: 274370  Cd Length: 120  Bit Score: 66.44  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548   52 RELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEGLQLSGATLTALKFIIAYpaGYHTA 131
Cdd:TIGR02970   3 RPLSPHLQIYRFPITAILSILHRITGVLLFFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKLILWGLLWAL--LYHLL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 442618548  132 NGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILALL 171
Cdd:TIGR02970  81 AGIRHLLWDLGYGLELKSARISAWVVLVLSLVLTILAGIW 120
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 71-170 4.87e-11

Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, transmembrane subunits; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol, while QFR catalyzes the reverse reaction. SQR, also called succinate dehydrogenase or Complex II, is part of the citric acid cycle and the aerobic respiratory chain, while QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQRs may reduce either high or low potential quinones while QFRs oxidize only low potential quinols. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit(s) containing the electron donor/acceptor (quinol or quinone). The reversible reduction of quinone is an essential feature of respiration, allowing the transfer of electrons between respiratory complexes. SQRs and QFRs can be classified into five types (A-E) according to the number of their hydrophobic subunits and heme groups. This classification is consistent with the characteristics and phylogeny of the catalytic and iron-sulfur subunits. Type E proteins, e.g. non-classical archael SQRs, contain atypical transmembrane subunits and are not included in this hierarchy. The heme and quinone binding sites reside in the transmembrane subunits. Although succinate oxidation and fumarate reduction are carried out by separate enzymes in most organisms, some bifunctional enzymes that exhibit both SQR and QFR activities exist.


Pssm-ID: 239573  Cd Length: 98  Bit Score: 56.52  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  71 ICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEglQLSGATLTALKFIIAYPAGYHTANGIRHLLWDTGRFLKIKEV 150
Cdd:cd03493    1 ILHRITGVALLLFLPLHLLGLLALLGGPYAFAEVVA--FLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYGKGLELKLR 78

                         90       100
                 ....*....|....*....|
gi 442618548 151 YSTGYAMVATSFVLSAILAL 170
Cdd:cd03493   79 KALGYAVLALSVLLTVLLLF 98
PLN00127 PLN00127
succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional
 45-171 2.80e-10

succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional


Pssm-ID: 177738  Cd Length: 178  Bit Score: 56.04  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  45 EKNERlgRELSPHL-------TIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDIShyVTMVEGLQLSGATLTA 117
Cdd:PLN00127  47 MLLEK--RPLSPDVmdidgksTHYKFPVVALSSITNRVTGCVLSGGAAGGGVLALVGGSEAV--PATMEGFKSGGPLIVF 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442618548 118 -LKFIIAYPAGYHTANGIRHLLWD-TGRFLKIKEVYSTGYAMVATSFVLSAILALL 171
Cdd:PLN00127 123 pAKFAVSFPFVYHTLGGLRHLVWDkTTEGLDNPSVEASSYGLFGASAALSAAAAVL 178
PLN00130 PLN00130
succinate dehydrogenase (SDH3); Provisional
 27-138 8.67e-06

succinate dehydrogenase (SDH3); Provisional


Pssm-ID: 177741 [Multi-domain]  Cd Length: 213  Bit Score: 44.37  E-value: 8.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618548  27 VSMKVVSVAETQKDESFfeknerlgRELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVE 106
Cdd:PLN00130 108 ISGDIKTTQEEPKIKSF--------RPLSPHLSVYQPQMNSMLSIFNRISGVYLTGVTFAGYLLYLKMGMICLTYPSFYQ 179

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442618548 107 GLQLSGATLTALKFIIAYPAGYHTANGIRHLL 138
Cdd:PLN00130 180 VLYHTQQQLPVITSVTALAAIYHTIKSTHSLL 211
sdhC PRK09487
succinate dehydrogenase cytochrome b556 subunit;
118-171 9.22e-04

succinate dehydrogenase cytochrome b556 subunit;


Pssm-ID: 181900  Cd Length: 129  Bit Score: 37.43  E-value: 9.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442618548 118 LKFI---IAYPAGYHTANGIRHLLWDTGRFlkiKEVYSTGYAMVATSFVLSAILALL 171
Cdd:PRK09487  70 VKFImwgILTALAYHVVVGIRHLLMDFGYL---EETLEAGKRSAKISFVITVVLSLL 123
PLN00126 PLN00126
succinate dehydrogenase, cytochrome b subunit family; Provisional
 52-79 6.43e-03

succinate dehydrogenase, cytochrome b subunit family; Provisional


Pssm-ID: 165695  Cd Length: 129  Bit Score: 35.13  E-value: 6.43e-03
                         10        20
                 ....*....|....*....|....*...
gi 442618548  52 RELSPHLTIYQPQLTSMLSICHRGTGLA 79
Cdd:PLN00126  82 RPLSPHLPLKKPQLSATFSISHRIFGAA 109
 
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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