protein of unknown function [Pseudotevenvirus RB43]
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 ... |
715-770 | 1.36e-15 | ||
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: 71.51 E-value: 1.36e-15
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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 ... |
715-770 | 1.36e-15 | ||
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: 71.51 E-value: 1.36e-15
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| Peptidase_S74_CIMCD | cd10144 | Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ... |
715-783 | 1.19e-03 | ||
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane. Pssm-ID: 381748 [Multi-domain] Cd Length: 113 Bit Score: 39.23 E-value: 1.19e-03
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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 ... |
715-770 | 1.36e-15 | ||
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: 71.51 E-value: 1.36e-15
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| Peptidase_S74_CIMCD | cd10144 | Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ... |
715-783 | 1.19e-03 | ||
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane. Pssm-ID: 381748 [Multi-domain] Cd Length: 113 Bit Score: 39.23 E-value: 1.19e-03
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