hypothetical protein [Nostoc sp. C052]
Protein Classification
alpha/beta hydrolase family protein( domain architecture ID 229394)
alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Abhydrolase super family | cl21494 | alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ... |
4-40 | 3.51e-05 | ||
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom. The actual alignment was detected with superfamily member pfam01764: Pssm-ID: 473884 [Multi-domain] Cd Length: 139 Bit Score: 37.24 E-value: 3.51e-05
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| Lipase_3 | pfam01764 | Lipase (class 3); |
4-40 | 3.51e-05 | ||
Lipase (class 3); Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 37.24 E-value: 3.51e-05
|
||||||
| Lipase_3 | cd00519 | Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
11-39 | 2.66e-03 | ||
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site. Pssm-ID: 238287 [Multi-domain] Cd Length: 229 Bit Score: 32.45 E-value: 2.66e-03
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| Lipase_3 | pfam01764 | Lipase (class 3); |
4-40 | 3.51e-05 | ||
Lipase (class 3); Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 37.24 E-value: 3.51e-05
|
||||||
| Lipase_3 | cd00519 | Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
11-39 | 2.66e-03 | ||
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site. Pssm-ID: 238287 [Multi-domain] Cd Length: 229 Bit Score: 32.45 E-value: 2.66e-03
|
||||||
| Blast search parameters | ||||
|
