tail protein [Bacillus phage BCP8-2]
Protein Classification
tail fiber domain-containing protein( domain architecture ID 10620719)
tail fiber domain-containing protein similar to Enterobacteria phage long tail fiber protein p37, a structural component of the distal-half tail fiber, and to the C-terminal chaperone domain of Escherichia coli phage K1F endosialidase, a S74 family serine endopeptidase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Peptidase_S74 | pfam13884 | Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ... |
226-278 | 8.74e-08 | ||
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope. : Pssm-ID: 404724 Cd Length: 56 Bit Score: 48.01 E-value: 8.74e-08
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| Peptidase_S74 | pfam13884 | Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ... |
226-278 | 8.74e-08 | ||
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope. Pssm-ID: 404724 Cd Length: 56 Bit Score: 48.01 E-value: 8.74e-08
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| Peptidase_S74 | pfam13884 | Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ... |
226-278 | 8.74e-08 | ||
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope. Pssm-ID: 404724 Cd Length: 56 Bit Score: 48.01 E-value: 8.74e-08
|
||||||
| Blast search parameters | ||||
|
