MULTISPECIES: tail fiber domain-containing protein [Enterobacteriaceae]
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
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 ... |
116-170 | 7.80e-07 | ||
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: 44.93 E-value: 7.80e-07
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| Name | Accession | Description | Interval | E-value | ||
| Peptidase_S74 | pfam13884 | Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ... |
116-170 | 7.80e-07 | ||
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: 44.93 E-value: 7.80e-07
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| Name | Accession | Description | Interval | E-value | ||
| Peptidase_S74 | pfam13884 | Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ... |
116-170 | 7.80e-07 | ||
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: 44.93 E-value: 7.80e-07
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