Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from ...
8-615
0e+00
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organized so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.
The actual alignment was detected with superfamily member pfam01065:
Pssm-ID: 395846 Cd Length: 586 Bit Score: 634.64 E-value: 0e+00
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from ...
616-838
8.44e-91
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organized so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.
The actual alignment was detected with superfamily member pfam03678:
Pssm-ID: 308977 Cd Length: 241 Bit Score: 288.03 E-value: 8.44e-91
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from ...
8-615
0e+00
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organized so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.
Pssm-ID: 395846 Cd Length: 586 Bit Score: 634.64 E-value: 0e+00
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from ...
616-838
8.44e-91
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organized so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.
Pssm-ID: 308977 Cd Length: 241 Bit Score: 288.03 E-value: 8.44e-91
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from ...
8-615
0e+00
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organized so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.
Pssm-ID: 395846 Cd Length: 586 Bit Score: 634.64 E-value: 0e+00
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from ...
616-838
8.44e-91
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organized so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.
Pssm-ID: 308977 Cd Length: 241 Bit Score: 288.03 E-value: 8.44e-91
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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