NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2797114151|gb|XFE85678|]
View 

succinate dehydrogenase, hydrophobic membrane anchor protein [Ensifer aridi]

Protein Classification

succinate dehydrogenase, hydrophobic membrane anchor protein( domain architecture ID 10005406)

succinate dehydrogenase, hydrophobic membrane anchor protein (SdhD), together with subunit SdhC, acts to anchor the catalytic components of succinate dehydrogenase to the cytoplasmic membrane

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SdhD COG2142
Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];
1-124 1.19e-41

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


:

Pssm-ID: 441745  Cd Length: 124  Bit Score: 133.80  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151   1 MDMRTPLGKVRGLGSAKEGTDHFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMR 80
Cdd:COG2142     1 MVYRTPLKRARGLGSAKSGTHHWLLQRVTAVALVVLVLWFLFFLLSLPGADYAEVAAWFASPFWAILTLLFLLSALYHAW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2797114151  81 IGMQVIIEDYVHAEGAKIALLMLNTFFAIAIGGLCLFAILKIAF 124
Cdd:COG2142    81 LGLRVVIEDYVHGTGLRLALLLLLTLALVALAAAGVFALLRIAL 124
 
Name Accession Description Interval E-value
SdhD COG2142
Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];
1-124 1.19e-41

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


Pssm-ID: 441745  Cd Length: 124  Bit Score: 133.80  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151   1 MDMRTPLGKVRGLGSAKEGTDHFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMR 80
Cdd:COG2142     1 MVYRTPLKRARGLGSAKSGTHHWLLQRVTAVALVVLVLWFLFFLLSLPGADYAEVAAWFASPFWAILTLLFLLSALYHAW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2797114151  81 IGMQVIIEDYVHAEGAKIALLMLNTFFAIAIGGLCLFAILKIAF 124
Cdd:COG2142    81 LGLRVVIEDYVHGTGLRLALLLLLTLALVALAAAGVFALLRIAL 124
SQR_TypeC_SdhD_like cd03495
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 22-120 3.09e-34

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit-like; composed of predominantly uncharacterized bacterial proteins with similarity to the E. coli SdhD subunit. One characterized protein is the respiratory Complex II SdhD subunit of the only eukaryotic member, Reclinomonas americana. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. It 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. E. coli SQR is classified as Type C SQRs because it contains two transmembrane subunits and one heme group. The SdhD and SdhC subunits are membrane anchor subunits containing 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: 239575  Cd Length: 100  Bit Score: 114.23  E-value: 3.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  22 HFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEGAKIALL 101
Cdd:cd03495     2 HWWAQRVTAVALVPLVLWFVFSVALLLGASYAEVVAWLAHPFNAILLILTLVSAFYHARLGMQVVIEDYVHSEGLRLALI 81

                          90
                  ....*....|....*....
gi 2797114151 102 MLNTFFAIAIGGLCLFAIL 120
Cdd:cd03495    82 IAVKLFAIATAAAGIFAIL 100
succ_dehyd_anc TIGR02968
succinate dehydrogenase, hydrophobic membrane anchor protein; In E. coli and many other ...
 16-120 2.09e-29

succinate dehydrogenase, hydrophobic membrane anchor protein; 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 SdhD, the hydrophobic membrane anchor protein. SdhC is apocytochrome b558, which also plays a role in anchoring the complex. [Energy metabolism, TCA cycle]


Pssm-ID: 274369  Cd Length: 105  Bit Score: 102.26  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  16 AKEGTDHFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEG 95
Cdd:TIGR02968   1 ARSGLRDWLLQRVTAVVLALYTIFLIGFLLALPGLTYEAWRALFAHPWMKIFTLLALLALLYHAWIGMRVVLEDYVKPEG 80

                          90       100
                  ....*....|....*....|....*
gi 2797114151  96 AKIALLMLNTFFAIAIGGLCLFAIL 120
Cdd:TIGR02968  81 LRLVLQVLIILFLVAYLIWGAFILW 105
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 1-111 8.14e-11

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: 55.08  E-value: 8.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151   1 MDMRTPLGKVRGLGSAKEGTDHFWRQRLTAVANLPLLIFFVFF-----VARYAGAPHAEVVAALSNPFVAVIMAFVVTSA 75
Cdd:pfam01127   1 MRKNRPLSPHLGLYRAHLTTWLSILHRITGVALAVLGLIFLLLwllllLSLLGPESYATVVAWLASPVKLILLLLLLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2797114151  76 LVHMRIGMQVIIEDY-----VHAEGAKIALLMLNTFFAIAI 111
Cdd:pfam01127  81 FYHAANGIRHLIWDVgfgleLKTVRKSGAAVLALSVVLVIV 121
 
Name Accession Description Interval E-value
SdhD COG2142
Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];
1-124 1.19e-41

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


Pssm-ID: 441745  Cd Length: 124  Bit Score: 133.80  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151   1 MDMRTPLGKVRGLGSAKEGTDHFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMR 80
Cdd:COG2142     1 MVYRTPLKRARGLGSAKSGTHHWLLQRVTAVALVVLVLWFLFFLLSLPGADYAEVAAWFASPFWAILTLLFLLSALYHAW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2797114151  81 IGMQVIIEDYVHAEGAKIALLMLNTFFAIAIGGLCLFAILKIAF 124
Cdd:COG2142    81 LGLRVVIEDYVHGTGLRLALLLLLTLALVALAAAGVFALLRIAL 124
SQR_TypeC_SdhD_like cd03495
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 22-120 3.09e-34

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit-like; composed of predominantly uncharacterized bacterial proteins with similarity to the E. coli SdhD subunit. One characterized protein is the respiratory Complex II SdhD subunit of the only eukaryotic member, Reclinomonas americana. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. It 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. E. coli SQR is classified as Type C SQRs because it contains two transmembrane subunits and one heme group. The SdhD and SdhC subunits are membrane anchor subunits containing 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: 239575  Cd Length: 100  Bit Score: 114.23  E-value: 3.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  22 HFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEGAKIALL 101
Cdd:cd03495     2 HWWAQRVTAVALVPLVLWFVFSVALLLGASYAEVVAWLAHPFNAILLILTLVSAFYHARLGMQVVIEDYVHSEGLRLALI 81

                          90
                  ....*....|....*....
gi 2797114151 102 MLNTFFAIAIGGLCLFAIL 120
Cdd:cd03495    82 IAVKLFAIATAAAGIFAIL 100
succ_dehyd_anc TIGR02968
succinate dehydrogenase, hydrophobic membrane anchor protein; In E. coli and many other ...
 16-120 2.09e-29

succinate dehydrogenase, hydrophobic membrane anchor protein; 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 SdhD, the hydrophobic membrane anchor protein. SdhC is apocytochrome b558, which also plays a role in anchoring the complex. [Energy metabolism, TCA cycle]


Pssm-ID: 274369  Cd Length: 105  Bit Score: 102.26  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  16 AKEGTDHFWRQRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEG 95
Cdd:TIGR02968   1 ARSGLRDWLLQRVTAVVLALYTIFLIGFLLALPGLTYEAWRALFAHPWMKIFTLLALLALLYHAWIGMRVVLEDYVKPEG 80

                          90       100
                  ....*....|....*....|....*
gi 2797114151  96 AKIALLMLNTFFAIAIGGLCLFAIL 120
Cdd:TIGR02968  81 LRLVLQVLIILFLVAYLIWGAFILW 105
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 1-111 8.14e-11

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: 55.08  E-value: 8.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151   1 MDMRTPLGKVRGLGSAKEGTDHFWRQRLTAVANLPLLIFFVFF-----VARYAGAPHAEVVAALSNPFVAVIMAFVVTSA 75
Cdd:pfam01127   1 MRKNRPLSPHLGLYRAHLTTWLSILHRITGVALAVLGLIFLLLwllllLSLLGPESYATVVAWLASPVKLILLLLLLLAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2797114151  76 LVHMRIGMQVIIEDY-----VHAEGAKIALLMLNTFFAIAI 111
Cdd:pfam01127  81 FYHAANGIRHLIWDVgfgleLKTVRKSGAAVLALSVVLVIV 121
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 24-119 1.88e-07

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: 45.73  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  24 WRQRLTAVANLPLLIFFVFFVARYAGAPHA--EVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEGAKIALL 101
Cdd:cd03493     1 ILHRITGVALLLFLPLHLLGLLALLGGPYAfaEVVAFLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYGKGLELKLRKA 80

                          90
                  ....*....|....*...
gi 2797114151 102 MLNTFFAIAIGGLCLFAI 119
Cdd:cd03493    81 LGYAVLALSVLLTVLLLF 98
SQR_TypeC_CybS cd03496
SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to ...
 17-117 7.11e-04

SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Eukaryotic SQRs 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. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. CybS and CybL are the two transmembrane proteins of eukaryotic SQRs. They contain heme and quinone binding sites. CybS is the eukaryotic homolog of the bacterial SdhD subunit. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the transmembrane 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. Mutations in human Complex II result in various physiological disorders including hereditary paraganglioma and pheochromocytoma tumors. The gene encoding for the SdhD subunit is classified as a tumor suppressor gene.


Pssm-ID: 239576  Cd Length: 104  Bit Score: 36.45  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  17 KEGTDHFWRQRLTAVANLPLLIffvffVARYAGAPHAEVVAALSnpfvavimafvvTSALVHMRIGMQVIIEDYVHAEG- 95
Cdd:cd03496     1 LHGSYHWTFERILAVSLLPLTP-----AAFFAPGLSPVMDAALA------------AALLLHSHWGFESCIIDYVPKRVg 63

                          90       100
                  ....*....|....*....|....*
gi 2797114151  96 ---AKIALLMLNTFFAIAIGGLCLF 117
Cdd:cd03496    64 gklHKLAMYLLYAGSALSLAGLYYF 88
SQR_TypeC_SdhD cd03494
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 26-103 2.09e-03

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. E. coli SQR, a member of this subfamily, reduces the high potential quinine, 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. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. SdhD and SdhC are the two transmembrane proteins of bacterial SQRs. They 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: 239574  Cd Length: 99  Bit Score: 34.89  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2797114151  26 QRLTAVANLPLLIFFVFFVARYAGAPHAEVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEGAKIALLML 103
Cdd:cd03494     5 QRVTAVIMALYTIFLVGFLLASPPLTYEAWSGLFSSLWMKIFTLLALLALLLHAWIGLWDILTDYVKPAGLRLLLQVL 82
SQR_TypeA_SdhD_like cd03500
Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase D (SdhD)-like ...
 26-118 4.06e-03

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: 34.56  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  26 QRLTAVAnLPLLIFFVFFVARYAG----APHAEVVAALSNPFVAVIMAFVVTSALVHMRIGMQVIIEDYVHAEGAKIA-- 99
Cdd:cd03500     8 QRITGVF-LVFLLAGHFWVQHMDNggdvIDFAFVANRLASPLWKVWDLLLLVLALLHGGNGLRNILLDYVRRPRLRRAvk 86

                          90       100
                  ....*....|....*....|
gi 2797114151 100 -LLMLNTFFAIAIGGLCLFA 118
Cdd:cd03500    87 gLLYVAGLLLIVLGTYVIFA 106
CybS pfam05328
CybS, succinate dehydrogenase cytochrome B small subunit; This family consists of several ...
 18-114 8.30e-03

CybS, succinate dehydrogenase cytochrome B small subunit; This family consists of several eukaryotic succinate dehydrogenase [ubiquinone] cytochrome B small subunit, mitochondrial precursor (CybS) proteins. SDHD encodes the small subunit (cybS) of cytochrome b in succinate-ubiquinone oxidoreductase (mitochondrial complex II). Mitochondrial complex II is involved in the Krebs cycle and in the aerobic electron transport chain. It contains four proteins. The catalytic core consists of a flavoprotein and an iron-sulfur protein; these proteins are anchored to the mitochondrial inner membrane by the large subunit of cytochrome b (cybL) and cybS, which together comprise the heme-protein cytochrome b. Mutations in the SDHD gene can lead to hereditary paraganglioma, characterized by the development of benign, vascularised tumours in the head and neck.


Pssm-ID: 461624  Cd Length: 131  Bit Score: 34.13  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797114151  18 EGTDHFWRQRLTAVANLPLLIffvffVARYAGAPHAEVVAALSnpfvavimafvvTSALVHMRIGMQVIIEDYVHAE--- 94
Cdd:pfam05328  29 HGSYHWTFERIVAVGLLPLTP-----APFAAGSPSPVLDAVLA------------SSLLGHCHIGFQSCIIDYIPKRvyg 91

                          90       100
                  ....*....|....*....|.
gi 2797114151  95 -GAKIALLMLNTFFAIAIGGL 114
Cdd:pfam05328  92 kWHKAAMYLLYLGTGVSLYGL 112
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH