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Conserved domains on  [gi|1985465607|ref|YP_009998008|]
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head-tail adaptor Ad1 [Proteus phage PM87]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gpW super family cl03738
gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of ...
18-64 3.64e-07

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.


The actual alignment was detected with superfamily member pfam02831:

Pssm-ID: 397116  Cd Length: 62  Bit Score: 42.95  E-value: 3.64e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1985465607 18 EASRAYHDLQIGvSGRVFVDQNSERVEFTAANRQSLLAYLTGLQRQI 64
Cdd:pfam02831  9 EARAALHDLMTG-KRVVTVQKDGRRVEYTAASVTDLKKYIAELERQL 54
 
Name Accession Description Interval E-value
gpW pfam02831
gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of ...
18-64 3.64e-07

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: 42.95  E-value: 3.64e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1985465607 18 EASRAYHDLQIGvSGRVFVDQNSERVEFTAANRQSLLAYLTGLQRQI 64
Cdd:pfam02831  9 EARAALHDLMTG-KRVVTVQKDGRRVEYTAASVTDLKKYIAELERQL 54
 
Name Accession Description Interval E-value
gpW pfam02831
gpW; gpW is a 68 residue protein known to be present in phage particles. Extracts of ...
18-64 3.64e-07

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: 42.95  E-value: 3.64e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1985465607 18 EASRAYHDLQIGvSGRVFVDQNSERVEFTAANRQSLLAYLTGLQRQI 64
Cdd:pfam02831  9 EARAALHDLMTG-KRVVTVQKDGRRVEYTAASVTDLKKYIAELERQL 54
 
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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