hypothetical protein [Xanthomonas cucurbitae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Abhydrolase super family | cl21494 | alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ... |
40-86 | 9.09e-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 cd00519: Pssm-ID: 473884 [Multi-domain] Cd Length: 229 Bit Score: 42.46 E-value: 9.09e-05
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| Name | Accession | Description | Interval | E-value | ||
| Lipase_3 | cd00519 | Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
40-86 | 9.09e-05 | ||
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: 42.46 E-value: 9.09e-05
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| Lipase_3 | pfam01764 | Lipase (class 3); |
37-95 | 4.10e-04 | ||
Lipase (class 3); Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 39.55 E-value: 4.10e-04
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| Name | Accession | Description | Interval | E-value | ||
| Lipase_3 | cd00519 | Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
40-86 | 9.09e-05 | ||
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: 42.46 E-value: 9.09e-05
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| Lipase_3 | pfam01764 | Lipase (class 3); |
37-95 | 4.10e-04 | ||
Lipase (class 3); Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 39.55 E-value: 4.10e-04
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| Lipase | cd00741 | Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
40-86 | 4.75e-04 | ||
Lipase. 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: 238382 [Multi-domain] Cd Length: 153 Bit Score: 39.79 E-value: 4.75e-04
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| Blast search parameters | ||||
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