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Conserved domains on  [gi|821658117|gb|AKH60660|]
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portal protein, partial [Salmonella phage SEN2]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P22_portal super family cl24922
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages ...
1-81 1.38e-32

Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages is a dodecameric structure consisting of a hip (2), a leg(1) and a barrel(3). DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Domains 1 and 3 are mostly helical and form the majority of the DNA-translocating channel. Domain 2 adopts an alpha-beta-fold characterized by two sheets of eight beta-strands, which cross each other to form a beta-barrel-like structure.


The actual alignment was detected with superfamily member pfam16510:

Pssm-ID: 293119  Cd Length: 668  Bit Score: 120.08  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821658117    1 QGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAAKIAEIFNNMDLNKQSEFREFLKTVASFQQDRS 80
Cdd:pfam16510 588 QGQQDPEMVAAQGVLMQGQAELQKAQNEELAIQIKAFQAQTEARVAEAKMVQILASADSAKQAEIREALKMLHQFQKEQG 667

                  .
gi 821658117   81 E 81
Cdd:pfam16510 668 D 668
 
Name Accession Description Interval E-value
P22_portal pfam16510
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages ...
1-81 1.38e-32

Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages is a dodecameric structure consisting of a hip (2), a leg(1) and a barrel(3). DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Domains 1 and 3 are mostly helical and form the majority of the DNA-translocating channel. Domain 2 adopts an alpha-beta-fold characterized by two sheets of eight beta-strands, which cross each other to form a beta-barrel-like structure.


Pssm-ID: 293119  Cd Length: 668  Bit Score: 120.08  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821658117    1 QGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAAKIAEIFNNMDLNKQSEFREFLKTVASFQQDRS 80
Cdd:pfam16510 588 QGQQDPEMVAAQGVLMQGQAELQKAQNEELAIQIKAFQAQTEARVAEAKMVQILASADSAKQAEIREALKMLHQFQKEQG 667

                  .
gi 821658117   81 E 81
Cdd:pfam16510 668 D 668
 
Name Accession Description Interval E-value
P22_portal pfam16510
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages ...
1-81 1.38e-32

Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages is a dodecameric structure consisting of a hip (2), a leg(1) and a barrel(3). DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Domains 1 and 3 are mostly helical and form the majority of the DNA-translocating channel. Domain 2 adopts an alpha-beta-fold characterized by two sheets of eight beta-strands, which cross each other to form a beta-barrel-like structure.


Pssm-ID: 293119  Cd Length: 668  Bit Score: 120.08  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821658117    1 QGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAAKIAEIFNNMDLNKQSEFREFLKTVASFQQDRS 80
Cdd:pfam16510 588 QGQQDPEMVAAQGVLMQGQAELQKAQNEELAIQIKAFQAQTEARVAEAKMVQILASADSAKQAEIREALKMLHQFQKEQG 667

                  .
gi 821658117   81 E 81
Cdd:pfam16510 668 D 668
 
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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