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Conserved domains on  [gi|1390208406|gb|AWK96619|]
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minor nucleoprotein [Zaire ebolavirus]

Protein Classification

Transcript_VP30 domain-containing protein( domain architecture ID 10568835)

Transcript_VP30 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transcript_VP30 pfam11507
Ebola virus-specific transcription factor VP30; VP30 is a nucleocapsid-associated Ebola ...
 142-271 1.87e-81

Ebola virus-specific transcription factor VP30; VP30 is a nucleocapsid-associated Ebola virus-specific transcription factor. It acts by stabilising nascent mRNA in Ebola virus replication. The C terminal domain of VP30 folds into a dimeric helical assembly. VP30 assembles into hexamers in solution by an N-terminal oligomerization domain which activates the transcription function of the protein. The oligomerization is mediated by hydrophobic amino acids at 94-112.


:

Pssm-ID: 402900  Cd Length: 131  Bit Score: 241.48  E-value: 1.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390208406 142 ITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGS 221
Cdd:pfam11507   1 ITLENLGHIAEHLARQDIGKIDDSKLRAALSLCAAGIRKFNKSLINLLCELHLNHEGLGQDQAEPIKETYQGIHLDKGGQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390208406 222 FEAALWQQWDRQSLIMFITAFLNIALQLPCESS-AVVVSGLRTLVPQSDNE 271
Cdd:pfam11507  81 FEAALWQGWDKQSIILFIQAALNIALNIPCESSiAVQASGDHFILPQSDGE 131
 
Name Accession Description Interval E-value
Transcript_VP30 pfam11507
Ebola virus-specific transcription factor VP30; VP30 is a nucleocapsid-associated Ebola ...
 142-271 1.87e-81

Ebola virus-specific transcription factor VP30; VP30 is a nucleocapsid-associated Ebola virus-specific transcription factor. It acts by stabilising nascent mRNA in Ebola virus replication. The C terminal domain of VP30 folds into a dimeric helical assembly. VP30 assembles into hexamers in solution by an N-terminal oligomerization domain which activates the transcription function of the protein. The oligomerization is mediated by hydrophobic amino acids at 94-112.


Pssm-ID: 402900  Cd Length: 131  Bit Score: 241.48  E-value: 1.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390208406 142 ITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGS 221
Cdd:pfam11507   1 ITLENLGHIAEHLARQDIGKIDDSKLRAALSLCAAGIRKFNKSLINLLCELHLNHEGLGQDQAEPIKETYQGIHLDKGGQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390208406 222 FEAALWQQWDRQSLIMFITAFLNIALQLPCESS-AVVVSGLRTLVPQSDNE 271
Cdd:pfam11507  81 FEAALWQGWDKQSIILFIQAALNIALNIPCESSiAVQASGDHFILPQSDGE 131
 
Name Accession Description Interval E-value
Transcript_VP30 pfam11507
Ebola virus-specific transcription factor VP30; VP30 is a nucleocapsid-associated Ebola ...
 142-271 1.87e-81

Ebola virus-specific transcription factor VP30; VP30 is a nucleocapsid-associated Ebola virus-specific transcription factor. It acts by stabilising nascent mRNA in Ebola virus replication. The C terminal domain of VP30 folds into a dimeric helical assembly. VP30 assembles into hexamers in solution by an N-terminal oligomerization domain which activates the transcription function of the protein. The oligomerization is mediated by hydrophobic amino acids at 94-112.


Pssm-ID: 402900  Cd Length: 131  Bit Score: 241.48  E-value: 1.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390208406 142 ITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGS 221
Cdd:pfam11507   1 ITLENLGHIAEHLARQDIGKIDDSKLRAALSLCAAGIRKFNKSLINLLCELHLNHEGLGQDQAEPIKETYQGIHLDKGGQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1390208406 222 FEAALWQQWDRQSLIMFITAFLNIALQLPCESS-AVVVSGLRTLVPQSDNE 271
Cdd:pfam11507  81 FEAALWQGWDKQSIILFIQAALNIALNIPCESSiAVQASGDHFILPQSDGE 131
 
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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