hypothetical protein [Bacteroides clarus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| BACON super family | cl15232 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
50-125 | 2.77e-06 | ||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. The actual alignment was detected with superfamily member cd14948: Pssm-ID: 449511 [Multi-domain] Cd Length: 83 Bit Score: 45.33 E-value: 2.77e-06
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| Name | Accession | Description | Interval | E-value | ||
| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
50-125 | 2.77e-06 | ||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 45.33 E-value: 2.77e-06
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| Name | Accession | Description | Interval | E-value | ||
| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
50-125 | 2.77e-06 | ||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 45.33 E-value: 2.77e-06
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| Blast search parameters | ||||
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