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MULTISPECIES: succinate dehydrogenase, cytochrome b556 subunit [Mycolicibacterium]

Protein Classification

succinate dehydrogenase, cytochrome b556 subunit( domain architecture ID 10131285)

succinate dehydrogenase, cytochrome b556 subunit (also called the C subunit), 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_TypeA_SdhC_like cd03501
Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like ...
 31-130 4.22e-45

Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. 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. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. 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: 239581  Cd Length: 101  Bit Score: 142.41  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  31 MWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDFWSEGPRH 110
Cdd:cd03501    1 MWAWVLHRITGVVILFYLFLHVLDLSSLRRGPETYNAVIATYKSPIFKLGEFGLVAAVVFHALNGIRLILVDFGSGGPRY 80

                         90       100
                 ....*....|....*....|
gi 500225584 111 QRKMLWIIAGIFIVLFTAGL 130
Cdd:cd03501   81 QRQLFYIVLVLTVVLIVAAG 100
 
Name Accession Description Interval E-value
SQR_TypeA_SdhC_like cd03501
Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like ...
 31-130 4.22e-45

Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. 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. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. 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: 239581  Cd Length: 101  Bit Score: 142.41  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  31 MWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDFWSEGPRH 110
Cdd:cd03501    1 MWAWVLHRITGVVILFYLFLHVLDLSSLRRGPETYNAVIATYKSPIFKLGEFGLVAAVVFHALNGIRLILVDFGSGGPRY 80

                         90       100
                 ....*....|....*....|
gi 500225584 111 QRKMLWIIAGIFIVLFTAGL 130
Cdd:cd03501   81 QRQLFYIVLVLTVVLIVAAG 100
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 20-137 1.53e-34

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


Pssm-ID: 441612  Cd Length: 128  Bit Score: 116.42  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  20 RRRTFYRGDPGMWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRII 99
Cdd:COG2009   11 PHLQIYRLPLTMIVSILHRITGVALFLGLPLLVWWLAASASSPEAFAAVQAFLGSPLGKLVLLGLTWALLYHLLAGIRHL 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500225584 100 LIDFW-SEGPRHQRKMLWIIAGIFIVLfTAGLGVIGMHM 137
Cdd:COG2009   91 LWDFGyGFELETARRSAWVVLVLSVVL-TVLLGVVLWGL 128
succ_dehyd_cytB TIGR02970
succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two ...
 25-128 4.59e-29

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: 102.26  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584   25 YRGDPGMWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDF- 103
Cdd:TIGR02970  12 YRFPITAILSILHRITGVLLFFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKLILWGLLWALLYHLLAGIRHLLWDLg 91

                          90       100
                  ....*....|....*....|....*
gi 500225584  104 WSEGPRHQRKMLWIIAGIFIVLFTA 128
Cdd:TIGR02970  92 YGLELKSARISAWVVLVLSLVLTIL 116
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 20-130 3.31e-14

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: 64.33  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584   20 RRRTFYRGDPGMWSWLLHRISGATIFFFLFVHVLD---TALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGI 96
Cdd:pfam01127   9 PHLGLYRAHLTTWLSILHRITGVALAVLGLIFLLLwllLLLSLLGPESYATVVAWLASPVKLILLLLLLLALFYHAANGI 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 500225584   97 RIILIDFWSEGPRHQRKMLWIIAGIFIVLFTAGL 130
Cdd:pfam01127  89 RHLIWDVGFGLELKTVRKSGAAVLALSVVLVIVL 122
 
Name Accession Description Interval E-value
SQR_TypeA_SdhC_like cd03501
Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like ...
 31-130 4.22e-45

Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. 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. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. 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: 239581  Cd Length: 101  Bit Score: 142.41  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  31 MWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDFWSEGPRH 110
Cdd:cd03501    1 MWAWVLHRITGVVILFYLFLHVLDLSSLRRGPETYNAVIATYKSPIFKLGEFGLVAAVVFHALNGIRLILVDFGSGGPRY 80

                         90       100
                 ....*....|....*....|
gi 500225584 111 QRKMLWIIAGIFIVLFTAGL 130
Cdd:cd03501   81 QRQLFYIVLVLTVVLIVAAG 100
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 20-137 1.53e-34

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


Pssm-ID: 441612  Cd Length: 128  Bit Score: 116.42  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  20 RRRTFYRGDPGMWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRII 99
Cdd:COG2009   11 PHLQIYRLPLTMIVSILHRITGVALFLGLPLLVWWLAASASSPEAFAAVQAFLGSPLGKLVLLGLTWALLYHLLAGIRHL 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500225584 100 LIDFW-SEGPRHQRKMLWIIAGIFIVLfTAGLGVIGMHM 137
Cdd:COG2009   91 LWDFGyGFELETARRSAWVVLVLSVVL-TVLLGVVLWGL 128
succ_dehyd_cytB TIGR02970
succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two ...
 25-128 4.59e-29

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: 102.26  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584   25 YRGDPGMWSWLLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDF- 103
Cdd:TIGR02970  12 YRFPITAILSILHRITGVLLFFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKLILWGLLWALLYHLLAGIRHLLWDLg 91

                          90       100
                  ....*....|....*....|....*
gi 500225584  104 WSEGPRHQRKMLWIIAGIFIVLFTA 128
Cdd:TIGR02970  92 YGLELKSARISAWVVLVLSLVLTIL 116
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 35-132 2.37e-15

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: 66.92  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  35 LLHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDFWSEGPRHQRKM 114
Cdd:cd03493    1 ILHRITGVALLLFLPLHLLGLLALLGGPYAFAEVVAFLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYGKGLELKLRKA 80

                         90
                 ....*....|....*...
gi 500225584 115 LWIIAGIFIVLFTAGLGV 132
Cdd:cd03493   81 LGYAVLALSVLLTVLLLF 98
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 20-130 3.31e-14

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: 64.33  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584   20 RRRTFYRGDPGMWSWLLHRISGATIFFFLFVHVLD---TALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGI 96
Cdd:pfam01127   9 PHLGLYRAHLTTWLSILHRITGVALAVLGLIFLLLwllLLLSLLGPESYATVVAWLASPVKLILLLLLLLALFYHAANGI 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 500225584   97 RIILIDFWSEGPRHQRKMLWIIAGIFIVLFTAGL 130
Cdd:pfam01127  89 RHLIWDVGFGLELKTVRKSGAAVLALSVVLVIVL 122
SdhD COG2142
Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];
15-133 1.74e-12

Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];


Pssm-ID: 441745  Cd Length: 124  Bit Score: 59.84  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  15 RSKPTRRRTFYRGDPGMWSWLLHRISGATIFFFLFVHVLdtALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALN 94
Cdd:COG2142    4 RTPLKRARGLGSAKSGTHHWLLQRVTAVALVVLVLWFLF--FLLSLPGADYAEVAAWFASPFWAILTLLFLLSALYHAWL 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500225584  95 GIRIILIDFwseGPRHQRKMLWIIAGIFIVLFTAGLGVI 133
Cdd:COG2142   82 GLRVVIEDY---VHGTGLRLALLLLLTLALVALAAAGVF 117
SQR_TypeA_SdhD_like cd03500
Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase D (SdhD)-like ...
 30-133 3.97e-10

Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase D (SdhD)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. 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. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. 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: 239580  Cd Length: 106  Bit Score: 53.43  E-value: 3.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  30 GMWSWLLHRISGATIFFFLFVHVLDTALVRVSPQA-YNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDfWSEGP 108
Cdd:cd03500    1 ESLAWLFQRITGVFLVFLLAGHFWVQHMDNGGDVIdFAFVANRLASPLWKVWDLLLLVLALLHGGNGLRNILLD-YVRRP 79

                         90       100
                 ....*....|....*....|....*
gi 500225584 109 RHQRKMLWIIAGIFIVLFTAGLGVI 133
Cdd:cd03500   80 RLRRAVKGLLYVAGLLLIVLGTYVI 104
SQR_TypeC_SdhC cd03499
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) ...
 36-103 5.40e-08

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: 47.91  E-value: 5.40e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500225584  36 LHRISGATIFFFLFVHVLDTALVRVSPQAYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIILIDF 103
Cdd:cd03499   21 LHRITGVALFLGLPLLLWWLLASLSSPESFESVSALLGSWLGKLVLFGLTWALFYHLLNGIRHLIWDL 88
SQR_TypeB_1_TM cd03497
Succinate:quinone oxidoreductase (SQR) Type B subfamily 1, transmembrane subunit; composed of ...
 32-133 2.25e-04

Succinate:quinone oxidoreductase (SQR) Type B subfamily 1, transmembrane subunit; composed of proteins similar to Bacillus subtilis SQR. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Bacillus subtilis SQR reduces low potential quinones such as menaquinone. SQR is also called succinate dehydrogenase (Sdh) 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. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside on the transmembrane subunit. The transmembrane subunit of Bacillus subtilis SQR is also called Sdh cytochrome b558 subunit. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron acceptor (quinone). The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.


Pssm-ID: 239577  Cd Length: 207  Bit Score: 39.22  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500225584  32 WSWLLHRISGATIFFFLFVHVLDT----ALVRVSPQ-------AYNEVIETYKTPIVGLMEIGLVAAVLYHALNGIRIIL 100
Cdd:cd03497   91 WMYTLQRITGIILLVFIAWHVWHTrfaeALGHVDIQtpeageaNLSAMRNALASPLMLIFYIIGVLAAVFHFANGLWTFL 170

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 500225584 101 IDfW--SEGPRHQRKMLWIIAGIFIVLFTAGLGVI 133
Cdd:cd03497  171 IT-WgiTVSPRSQRVSTYVCLLVFVVVSFMGVAAI 204
 
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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