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Conserved domains on  [gi|1821362974|gb|QIM06641|]
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C hexon protein, partial [Fowl aviadenovirus sp.]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Adeno_hexon_C super family cl15558
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from ...
 91-330 3.08e-146

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: 415.14  E-value: 3.08e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974  91 NATNDQTFVDYLGAKNALYSVPAGSTALTINIPARTWEGMRGWSFTRIKAAETPQLGAQYDVNFKYSGSIAYSDGGFYLS 170
Cdd:pfam03678   1 NATNDQNFADYLGAKNNLYQVPANTNTLVINIPDRTWEAFRGWSFNRLKASETPMIGATYDVNFKYSGSIPYLDGTFYLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974 171 HTFRNMSILFDTSINWPGNDRLLTPNMFEIKRSVALDTEGFTMSQCDITKDWYLIQMATNYNFVYNGYRFWPDRQYFHYD 250
Cdd:pfam03678  81 HTFQRVSIQFDSSVPWPGNDRLLIPNWFEIKRDPNMDSEGYTMSQSTMTKDWFLVQMAANYNQAYQGYKFPVDSKYFHYD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974 251 FLRNFDPMTRQGPNFALPGLFDLVSYTPTTDNSGQQPSQEAVRNNSGFIAPRSWPVWSAHQGESWPANWPYPLCGQQAIQ 330
Cdd:pfam03678 161 FLENFDPMSRQVPIYGNGTIYDLYTAYITNQRTMSAPGQDIIRNNSGFEAKRSNPPMLSNTGHLYPANWPYPLIGPNAIE 240
Adeno_hexon super family cl03086
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from ...
 1-90 1.79e-50

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: 178.95  E-value: 1.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974   1 RSQLLGNSRYVNFHIQVPQKFFAIKNLLLLSGSYTYEWVLRKDPNMILQSSLGNDLRADGASIIYNEVNLMANFMPMDHN 80
Cdd:pfam01065 497 RSQLLGNGRYCRFHIQVPQKFFAIKNLLLLPGTYTYEWVFRKDPNMVLQSSLGNDLRADGATIVYTEINLMASFFPMDHN 576

                          90
                  ....*....|
gi 1821362974  81 TSNQLELMLR 90
Cdd:pfam01065 577 TSNQLELMLR 586
 
Name Accession Description Interval E-value
Adeno_hexon_C pfam03678
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from ...
 91-330 3.08e-146

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: 415.14  E-value: 3.08e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974  91 NATNDQTFVDYLGAKNALYSVPAGSTALTINIPARTWEGMRGWSFTRIKAAETPQLGAQYDVNFKYSGSIAYSDGGFYLS 170
Cdd:pfam03678   1 NATNDQNFADYLGAKNNLYQVPANTNTLVINIPDRTWEAFRGWSFNRLKASETPMIGATYDVNFKYSGSIPYLDGTFYLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974 171 HTFRNMSILFDTSINWPGNDRLLTPNMFEIKRSVALDTEGFTMSQCDITKDWYLIQMATNYNFVYNGYRFWPDRQYFHYD 250
Cdd:pfam03678  81 HTFQRVSIQFDSSVPWPGNDRLLIPNWFEIKRDPNMDSEGYTMSQSTMTKDWFLVQMAANYNQAYQGYKFPVDSKYFHYD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974 251 FLRNFDPMTRQGPNFALPGLFDLVSYTPTTDNSGQQPSQEAVRNNSGFIAPRSWPVWSAHQGESWPANWPYPLCGQQAIQ 330
Cdd:pfam03678 161 FLENFDPMSRQVPIYGNGTIYDLYTAYITNQRTMSAPGQDIIRNNSGFEAKRSNPPMLSNTGHLYPANWPYPLIGPNAIE 240
Adeno_hexon pfam01065
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from ...
 1-90 1.79e-50

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: 178.95  E-value: 1.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974   1 RSQLLGNSRYVNFHIQVPQKFFAIKNLLLLSGSYTYEWVLRKDPNMILQSSLGNDLRADGASIIYNEVNLMANFMPMDHN 80
Cdd:pfam01065 497 RSQLLGNGRYCRFHIQVPQKFFAIKNLLLLPGTYTYEWVFRKDPNMVLQSSLGNDLRADGATIVYTEINLMASFFPMDHN 576

                          90
                  ....*....|
gi 1821362974  81 TSNQLELMLR 90
Cdd:pfam01065 577 TSNQLELMLR 586
 
Name Accession Description Interval E-value
Adeno_hexon_C pfam03678
Hexon, adenovirus major coat protein, C-terminal domain; Hexon is the major coat protein from ...
 91-330 3.08e-146

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: 415.14  E-value: 3.08e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974  91 NATNDQTFVDYLGAKNALYSVPAGSTALTINIPARTWEGMRGWSFTRIKAAETPQLGAQYDVNFKYSGSIAYSDGGFYLS 170
Cdd:pfam03678   1 NATNDQNFADYLGAKNNLYQVPANTNTLVINIPDRTWEAFRGWSFNRLKASETPMIGATYDVNFKYSGSIPYLDGTFYLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974 171 HTFRNMSILFDTSINWPGNDRLLTPNMFEIKRSVALDTEGFTMSQCDITKDWYLIQMATNYNFVYNGYRFWPDRQYFHYD 250
Cdd:pfam03678  81 HTFQRVSIQFDSSVPWPGNDRLLIPNWFEIKRDPNMDSEGYTMSQSTMTKDWFLVQMAANYNQAYQGYKFPVDSKYFHYD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974 251 FLRNFDPMTRQGPNFALPGLFDLVSYTPTTDNSGQQPSQEAVRNNSGFIAPRSWPVWSAHQGESWPANWPYPLCGQQAIQ 330
Cdd:pfam03678 161 FLENFDPMSRQVPIYGNGTIYDLYTAYITNQRTMSAPGQDIIRNNSGFEAKRSNPPMLSNTGHLYPANWPYPLIGPNAIE 240
Adeno_hexon pfam01065
Hexon, adenovirus major coat protein, N-terminal domain; Hexon is the major coat protein from ...
 1-90 1.79e-50

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: 178.95  E-value: 1.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821362974   1 RSQLLGNSRYVNFHIQVPQKFFAIKNLLLLSGSYTYEWVLRKDPNMILQSSLGNDLRADGASIIYNEVNLMANFMPMDHN 80
Cdd:pfam01065 497 RSQLLGNGRYCRFHIQVPQKFFAIKNLLLLPGTYTYEWVFRKDPNMVLQSSLGNDLRADGATIVYTEINLMASFFPMDHN 576

                          90
                  ....*....|
gi 1821362974  81 TSNQLELMLR 90
Cdd:pfam01065 577 TSNQLELMLR 586
 
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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