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Conserved domains on  [gi|11079226|gb|AAG21693|]
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prion protein [Homo sapiens]

Protein Classification

Prion_bPrPp and PRP domain-containing protein( domain architecture ID 12110435)

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 ...
 23-240 5.40e-113

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: 323.36  E-value: 5.40e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226     23 KKRPKPGG-WNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQpHGGGWGQGGGTHSQWNK 101
Cdd:smart00157   1 KKRPKPGGgWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQP-HGGGWGQGGGTHNQWNK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226    102 PSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVN 181
Cdd:smart00157  80 PSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVN 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 11079226    182 ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPV 240
Cdd:smart00157 160 ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSVVLFSSPPV 218
Prion_bPrPp pfam11587
Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of ...
 1-28 1.04e-11

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: 57.95  E-value: 1.04e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 11079226     1 MAN--LGCWMLVLFVATWSDLGLCKKRPKP 28
Cdd:pfam11587   1 MAKhqLGCWLLVLFVATWSDVGLCKKRPKP 30
 
Name Accession Description Interval E-value
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
 23-240 5.40e-113

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: 323.36  E-value: 5.40e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226     23 KKRPKPGG-WNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQpHGGGWGQGGGTHSQWNK 101
Cdd:smart00157   1 KKRPKPGGgWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQP-HGGGWGQGGGTHNQWNK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226    102 PSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVN 181
Cdd:smart00157  80 PSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVN 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 11079226    182 ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPV 240
Cdd:smart00157 160 ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSVVLFSSPPV 218
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 134-251 7.66e-42

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: 139.06  E-value: 7.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226   134 MSRPIIHFGSDyEDRYYRENMHRYPNQVYYRPMDE-YSNQNNFVHDCVNITIKQHTVTTTTkGENFTETDVKMMERVVEQ 212
Cdd:pfam00377   1 MSKLDIDFGAE-GNRYYEANYWRFPDQIYYRGCSEaNVTKEVFVTDCVNATVTANQIEPSR-EQTDNELEQRVLWRLIRE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 11079226   213 MCITQYEresQAYYQRGSSM-VLFSSPPVILLISFLIFLI 251
Cdd:pfam00377  79 MCSLQYC---EFWYRRGAGLrLLLDQPVMVCLLLLLWFLV 115
Prion_bPrPp pfam11587
Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of ...
 1-28 1.04e-11

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: 57.95  E-value: 1.04e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 11079226     1 MAN--LGCWMLVLFVATWSDLGLCKKRPKP 28
Cdd:pfam11587   1 MAKhqLGCWLLVLFVATWSDVGLCKKRPKP 30
 
Name Accession Description Interval E-value
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
 23-240 5.40e-113

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: 323.36  E-value: 5.40e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226     23 KKRPKPGG-WNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQpHGGGWGQGGGTHSQWNK 101
Cdd:smart00157   1 KKRPKPGGgWNTGGSRYPGQGSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQP-HGGGWGQGGGTHNQWNK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226    102 PSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVN 181
Cdd:smart00157  80 PSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVN 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 11079226    182 ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPV 240
Cdd:smart00157 160 ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQKESQAYYQRGSSVVLFSSPPV 218
Prion pfam00377
Prion/Doppel alpha-helical domain; The prion protein is thought to be the infectious agent ...
 134-251 7.66e-42

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: 139.06  E-value: 7.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11079226   134 MSRPIIHFGSDyEDRYYRENMHRYPNQVYYRPMDE-YSNQNNFVHDCVNITIKQHTVTTTTkGENFTETDVKMMERVVEQ 212
Cdd:pfam00377   1 MSKLDIDFGAE-GNRYYEANYWRFPDQIYYRGCSEaNVTKEVFVTDCVNATVTANQIEPSR-EQTDNELEQRVLWRLIRE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 11079226   213 MCITQYEresQAYYQRGSSM-VLFSSPPVILLISFLIFLI 251
Cdd:pfam00377  79 MCSLQYC---EFWYRRGAGLrLLLDQPVMVCLLLLLWFLV 115
Prion_bPrPp pfam11587
Major prion protein bPrPp - N terminal; This family represents the N-terminal domain (1-30) of ...
 1-28 1.04e-11

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: 57.95  E-value: 1.04e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 11079226     1 MAN--LGCWMLVLFVATWSDLGLCKKRPKP 28
Cdd:pfam11587   1 MAKhqLGCWLLVLFVATWSDVGLCKKRPKP 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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