hypothetical protein, partial [Citrobacter braakii]
tail fiber domain-containing protein( domain architecture ID 82077)
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_CIMCD super family | cl16452 | Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ... |
22-73 | 6.71e-05 | ||
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. The actual alignment was detected with superfamily member cd10144: Pssm-ID: 418048 [Multi-domain] Cd Length: 113 Bit Score: 38.46 E-value: 6.71e-05
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Name | Accession | Description | Interval | E-value | ||
Peptidase_S74_CIMCD | cd10144 | Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ... |
22-73 | 6.71e-05 | ||
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: 38.46 E-value: 6.71e-05
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Name | Accession | Description | Interval | E-value | ||
Peptidase_S74_CIMCD | cd10144 | Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ... |
22-73 | 6.71e-05 | ||
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: 38.46 E-value: 6.71e-05
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Blast search parameters | ||||
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