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Conserved domains on  [gi|506326519|ref|NP_001265186|]
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prion-like protein doppel precursor [Mus musculus]

Protein Classification

Doppel and Prion domain-containing protein( domain architecture ID 10568668)

Doppel and Prion domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 64-178 5.81e-76

Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent that causes transmissible spongiform encephalopathies, such as scrapie and BSE. It is thought that the prion protein can exist in two different forms: one is the normal cellular protein, and the other is the infectious form which can change the normal prion protein into the infectious form. It has been found that the prion alpha-helical domain is also found in the Doppel protein.


:

Pssm-ID: 425648  Cd Length: 115  Bit Score: 222.64  E-value: 5.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506326519   64 GRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEIC 143
Cdd:pfam00377   1 MSKLDIDFGAEGNRYYEANYWRFPDQIYYRGCSEANVTKEVFVTDCVNATVTANQIEPSREQTDNELEQRVLWRLIREMC 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 506326519  144 SAKHCDFWLERGAALRVAVDQPAMVCLLGFVWFIV 178
Cdd:pfam00377  81 SLQYCEFWYRRGAGLRLLLDQPVMVCLLLLLWFLV 115
Doppel pfam11466
Prion-like protein Doppel; Dpl is a homolog related to the prion protein (PrP). Dpl is toxic ...
 1-30 1.57e-11

Prion-like protein Doppel; Dpl is a homolog related to the prion protein (PrP). Dpl is toxic to neurons and is expressed in the brains of mice that do not express PrP. In DHPC and SDS micelles, Dpl shoes about 40% alpha-helical structure however in aqueous solution it consists of a random coil. The alpha helical segment can adopt a transmembrane localization also in a membrane. The unprocessed Dpl protein is thought to posses a possible channel formation mechanism which may be related to toxicity through direct interaction with cell membranes and damage to the cell membrane. It is suggested that the peptide is neither in an entirely random coil nor in a completely alpha-helical conformation, possible continuously interchanging between the two conformations.


:

Pssm-ID: 402876  Cd Length: 30  Bit Score: 56.32  E-value: 1.57e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 506326519    1 MKNRLGTWWVAILCMLLASHLSTVKARGIK 30
Cdd:pfam11466   1 MRKHLGTWWLAIVCVLLFSHLSLVKARGIK 30
 
Name Accession Description Interval E-value
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 64-178 5.81e-76

Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent that causes transmissible spongiform encephalopathies, such as scrapie and BSE. It is thought that the prion protein can exist in two different forms: one is the normal cellular protein, and the other is the infectious form which can change the normal prion protein into the infectious form. It has been found that the prion alpha-helical domain is also found in the Doppel protein.


Pssm-ID: 425648  Cd Length: 115  Bit Score: 222.64  E-value: 5.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506326519   64 GRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEIC 143
Cdd:pfam00377   1 MSKLDIDFGAEGNRYYEANYWRFPDQIYYRGCSEANVTKEVFVTDCVNATVTANQIEPSREQTDNELEQRVLWRLIREMC 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 506326519  144 SAKHCDFWLERGAALRVAVDQPAMVCLLGFVWFIV 178
Cdd:pfam00377  81 SLQYCEFWYRRGAGLRLLLDQPVMVCLLLLLWFLV 115
Doppel pfam11466
Prion-like protein Doppel; Dpl is a homolog related to the prion protein (PrP). Dpl is toxic ...
 1-30 1.57e-11

Prion-like protein Doppel; Dpl is a homolog related to the prion protein (PrP). Dpl is toxic to neurons and is expressed in the brains of mice that do not express PrP. In DHPC and SDS micelles, Dpl shoes about 40% alpha-helical structure however in aqueous solution it consists of a random coil. The alpha helical segment can adopt a transmembrane localization also in a membrane. The unprocessed Dpl protein is thought to posses a possible channel formation mechanism which may be related to toxicity through direct interaction with cell membranes and damage to the cell membrane. It is suggested that the peptide is neither in an entirely random coil nor in a completely alpha-helical conformation, possible continuously interchanging between the two conformations.


Pssm-ID: 402876  Cd Length: 30  Bit Score: 56.32  E-value: 1.57e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 506326519    1 MKNRLGTWWVAILCMLLASHLSTVKARGIK 30
Cdd:pfam11466   1 MRKHLGTWWLAIVCVLLFSHLSLVKARGIK 30
 
Name Accession Description Interval E-value
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 64-178 5.81e-76

Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent that causes transmissible spongiform encephalopathies, such as scrapie and BSE. It is thought that the prion protein can exist in two different forms: one is the normal cellular protein, and the other is the infectious form which can change the normal prion protein into the infectious form. It has been found that the prion alpha-helical domain is also found in the Doppel protein.


Pssm-ID: 425648  Cd Length: 115  Bit Score: 222.64  E-value: 5.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506326519   64 GRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEIC 143
Cdd:pfam00377   1 MSKLDIDFGAEGNRYYEANYWRFPDQIYYRGCSEANVTKEVFVTDCVNATVTANQIEPSREQTDNELEQRVLWRLIREMC 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 506326519  144 SAKHCDFWLERGAALRVAVDQPAMVCLLGFVWFIV 178
Cdd:pfam00377  81 SLQYCEFWYRRGAGLRLLLDQPVMVCLLLLLWFLV 115
Doppel pfam11466
Prion-like protein Doppel; Dpl is a homolog related to the prion protein (PrP). Dpl is toxic ...
 1-30 1.57e-11

Prion-like protein Doppel; Dpl is a homolog related to the prion protein (PrP). Dpl is toxic to neurons and is expressed in the brains of mice that do not express PrP. In DHPC and SDS micelles, Dpl shoes about 40% alpha-helical structure however in aqueous solution it consists of a random coil. The alpha helical segment can adopt a transmembrane localization also in a membrane. The unprocessed Dpl protein is thought to posses a possible channel formation mechanism which may be related to toxicity through direct interaction with cell membranes and damage to the cell membrane. It is suggested that the peptide is neither in an entirely random coil nor in a completely alpha-helical conformation, possible continuously interchanging between the two conformations.


Pssm-ID: 402876  Cd Length: 30  Bit Score: 56.32  E-value: 1.57e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 506326519    1 MKNRLGTWWVAILCMLLASHLSTVKARGIK 30
Cdd:pfam11466   1 MRKHLGTWWLAIVCVLLFSHLSLVKARGIK 30
 
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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