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Conserved domains on  [gi|599082794|dbj|BAO57166|]
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major prion protein, partial [Ziphius cavirostris]

Protein Classification

Prion_bPrPp and PRP domain-containing protein( domain architecture ID 11672301)

Prion_bPrPp and PRP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
 9-228 1.55e-92

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.


:

Pssm-ID: 197548 [Multi-domain]  Cd Length: 218  Bit Score: 270.59  E-value: 1.55e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794     9 KKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGggTHNQW- 87
Cdd:smart00157   1 KKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGG--THNQWn 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794    88 KPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMYRYPNQVYYRPVDQYNNQNSFVHDCV 167
Cdd:smart00157  79 KPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCV 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599082794   168 NItVKQHTVTTTTTKGENFTETDIKMMERVVEEMCTTQYQREYQAYYQRGASVILFSSPPV 228
Cdd:smart00157 159 NI-TIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSVVLFSSPPV 218
Prion_bPrPp super family cl13097
Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of ...
 1-14 1.89e-03

Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of the bovine prion protein (bPrPp). The proteins structure consists of mainly alpha helices. BPrPp forms a stable helix which inserts in a transmembrane location in the bilayer, with the N -terminal (1-30) functioning as a cell-penetrating peptide.


The actual alignment was detected with superfamily member pfam11587:

Pssm-ID: 463301  Cd Length: 30  Bit Score: 34.84  E-value: 1.89e-03
                          10
                  ....*....|....
gi 599082794    1 TWSDMGLCKKRPKP 14
Cdd:pfam11587  17 TWSDVGLCKKRPKP 30
 
Name Accession Description Interval E-value
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
 9-228 1.55e-92

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.


Pssm-ID: 197548 [Multi-domain]  Cd Length: 218  Bit Score: 270.59  E-value: 1.55e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794     9 KKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGggTHNQW- 87
Cdd:smart00157   1 KKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGG--THNQWn 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794    88 KPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMYRYPNQVYYRPVDQYNNQNSFVHDCV 167
Cdd:smart00157  79 KPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCV 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599082794   168 NItVKQHTVTTTTTKGENFTETDIKMMERVVEEMCTTQYQREYQAYYQRGASVILFSSPPV 228
Cdd:smart00157 159 NI-TIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSVVLFSSPPV 218
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 121-228 1.16e-32

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: 114.40  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794  121 MSRPLIHFGSDyEDRYYRENMYRYPNQVYYRPVDQYN-NQNSFVHDCVNItvKQHTVTTTTTKGENFTETDIKMMERVVE 199
Cdd:pfam00377   1 MSKLDIDFGAE-GNRYYEANYWRFPDQIYYRGCSEANvTKEVFVTDCVNA--TVTANQIEPSREQTDNELEQRVLWRLIR 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 599082794  200 EMCTTQYQreyQAYYQRGASV-ILFSSPPV 228
Cdd:pfam00377  78 EMCSLQYC---EFWYRRGAGLrLLLDQPVM 104
Prion_bPrPp pfam11587
Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of ...
 1-14 1.89e-03

Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of the bovine prion protein (bPrPp). The proteins structure consists of mainly alpha helices. BPrPp forms a stable helix which inserts in a transmembrane location in the bilayer, with the N -terminal (1-30) functioning as a cell-penetrating peptide.


Pssm-ID: 463301  Cd Length: 30  Bit Score: 34.84  E-value: 1.89e-03
                          10
                  ....*....|....
gi 599082794    1 TWSDMGLCKKRPKP 14
Cdd:pfam11587  17 TWSDVGLCKKRPKP 30
 
Name Accession Description Interval E-value
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
 9-228 1.55e-92

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.


Pssm-ID: 197548 [Multi-domain]  Cd Length: 218  Bit Score: 270.59  E-value: 1.55e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794     9 KKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGggTHNQW- 87
Cdd:smart00157   1 KKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGG--THNQWn 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794    88 KPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMYRYPNQVYYRPVDQYNNQNSFVHDCV 167
Cdd:smart00157  79 KPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCV 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599082794   168 NItVKQHTVTTTTTKGENFTETDIKMMERVVEEMCTTQYQREYQAYYQRGASVILFSSPPV 228
Cdd:smart00157 159 NI-TIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSVVLFSSPPV 218
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 121-228 1.16e-32

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: 114.40  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599082794  121 MSRPLIHFGSDyEDRYYRENMYRYPNQVYYRPVDQYN-NQNSFVHDCVNItvKQHTVTTTTTKGENFTETDIKMMERVVE 199
Cdd:pfam00377   1 MSKLDIDFGAE-GNRYYEANYWRFPDQIYYRGCSEANvTKEVFVTDCVNA--TVTANQIEPSREQTDNELEQRVLWRLIR 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 599082794  200 EMCTTQYQreyQAYYQRGASV-ILFSSPPV 228
Cdd:pfam00377  78 EMCSLQYC---EFWYRRGAGLrLLLDQPVM 104
Prion_bPrPp pfam11587
Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of ...
 1-14 1.89e-03

Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of the bovine prion protein (bPrPp). The proteins structure consists of mainly alpha helices. BPrPp forms a stable helix which inserts in a transmembrane location in the bilayer, with the N -terminal (1-30) functioning as a cell-penetrating peptide.


Pssm-ID: 463301  Cd Length: 30  Bit Score: 34.84  E-value: 1.89e-03
                          10
                  ....*....|....
gi 599082794    1 TWSDMGLCKKRPKP 14
Cdd:pfam11587  17 TWSDVGLCKKRPKP 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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