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Conserved domains on  [gi|446120294|ref|WP_000198149|]
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MULTISPECIES: phage head-tail joining protein [Bacteria]

Protein Classification

gpW family protein( domain architecture ID 10500737)

gpW family protein similar to Escherichia coli Lambda prophage-derived head-to-tail joining protein W (gpW) that is required for the stabilization of DNA within the phage head and for attachment of tails onto the head during morphogenesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gpW pfam02831
gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of ...
1-62 2.67e-24

gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of phage-infected cells lacking gpW contain DNA-filled heads, and active tails, but no infectious virions. gpW is required for the addition of gpFII to the head, which is, in turn, required for the attachment of tails. Since gpFII and tails are known to be attached at the connector, gpW is also likely to assemble at this site. The addition of gpW to filled heads increases the DNase resistance of the packaged DNA, suggesting that gpW either forms a plug at the connector to prevent ejection of the DNA, or binds directly to the DNA. The large number of positively charged residues in gpW (its calculated pI is 10.8) is consistent with a role in DNA interaction.


:

Pssm-ID: 397116  Cd Length: 62  Bit Score: 85.71  E-value: 2.67e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446120294   1 MTRQEELAAARAALHDLMTGKRVATVQKDGRRVEFTATSVSDLKKYIAELEVQTGMTQRRRG 62
Cdd:pfam02831  1 MTLIAELAEARAALHDLMTGKRVVTVQKDGRRVEYTAASVTDLKKYIAELERQLGATGRRRG 62
 
Name Accession Description Interval E-value
gpW pfam02831
gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of ...
1-62 2.67e-24

gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of phage-infected cells lacking gpW contain DNA-filled heads, and active tails, but no infectious virions. gpW is required for the addition of gpFII to the head, which is, in turn, required for the attachment of tails. Since gpFII and tails are known to be attached at the connector, gpW is also likely to assemble at this site. The addition of gpW to filled heads increases the DNase resistance of the packaged DNA, suggesting that gpW either forms a plug at the connector to prevent ejection of the DNA, or binds directly to the DNA. The large number of positively charged residues in gpW (its calculated pI is 10.8) is consistent with a role in DNA interaction.


Pssm-ID: 397116  Cd Length: 62  Bit Score: 85.71  E-value: 2.67e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446120294   1 MTRQEELAAARAALHDLMTGKRVATVQKDGRRVEFTATSVSDLKKYIAELEVQTGMTQRRRG 62
Cdd:pfam02831  1 MTLIAELAEARAALHDLMTGKRVVTVQKDGRRVEYTAASVTDLKKYIAELERQLGATGRRRG 62
 
Name Accession Description Interval E-value
gpW pfam02831
gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of ...
1-62 2.67e-24

gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of phage-infected cells lacking gpW contain DNA-filled heads, and active tails, but no infectious virions. gpW is required for the addition of gpFII to the head, which is, in turn, required for the attachment of tails. Since gpFII and tails are known to be attached at the connector, gpW is also likely to assemble at this site. The addition of gpW to filled heads increases the DNase resistance of the packaged DNA, suggesting that gpW either forms a plug at the connector to prevent ejection of the DNA, or binds directly to the DNA. The large number of positively charged residues in gpW (its calculated pI is 10.8) is consistent with a role in DNA interaction.


Pssm-ID: 397116  Cd Length: 62  Bit Score: 85.71  E-value: 2.67e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446120294   1 MTRQEELAAARAALHDLMTGKRVATVQKDGRRVEFTATSVSDLKKYIAELEVQTGMTQRRRG 62
Cdd:pfam02831  1 MTLIAELAEARAALHDLMTGKRVVTVQKDGRRVEYTAASVTDLKKYIAELERQLGATGRRRG 62
 
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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