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Conserved domains on  [gi|386768533|ref|NP_001246484|]
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uncharacterized protein Dmel_CG13562, isoform C [Drosophila melanogaster]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 64-208 6.73e-09

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 cd00707:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 275  Bit Score: 56.10  E-value: 6.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768533  64 MFYKNNTKTMETSAYDDAYDLSGSGCSPTDKFAIVLHGWIQSCSDEWALSLIERLsYYRGGC-VICIDYSVVASSSY--M 140
Cdd:cd00707    7 LYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAY-LSRGDYnVIVVDWGRGANPNYpqA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768533 141 RLYTNfdtLTGA-ISSIILTLFRQ-GFDPKRGYMFGFSFGGQLASAVGRSLRphHIIESIDTCDMAGPGF 208
Cdd:cd00707   86 VNNTR---VVGAeLAKFLDFLVDNtGLSLENVHLIGHSLGAHVAGFAGKRLN--GKLGRITGLDPAGPLF 150
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 64-208 6.73e-09

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 56.10  E-value: 6.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768533  64 MFYKNNTKTMETSAYDDAYDLSGSGCSPTDKFAIVLHGWIQSCSDEWALSLIERLsYYRGGC-VICIDYSVVASSSY--M 140
Cdd:cd00707    7 LYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAY-LSRGDYnVIVVDWGRGANPNYpqA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768533 141 RLYTNfdtLTGA-ISSIILTLFRQ-GFDPKRGYMFGFSFGGQLASAVGRSLRphHIIESIDTCDMAGPGF 208
Cdd:cd00707   86 VNNTR---VVGAeLAKFLDFLVDNtGLSLENVHLIGHSLGAHVAGFAGKRLN--GKLGRITGLDPAGPLF 150
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 64-208 6.73e-09

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 56.10  E-value: 6.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768533  64 MFYKNNTKTMETSAYDDAYDLSGSGCSPTDKFAIVLHGWIQSCSDEWALSLIERLsYYRGGC-VICIDYSVVASSSY--M 140
Cdd:cd00707    7 LYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAY-LSRGDYnVIVVDWGRGANPNYpqA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768533 141 RLYTNfdtLTGA-ISSIILTLFRQ-GFDPKRGYMFGFSFGGQLASAVGRSLRphHIIESIDTCDMAGPGF 208
Cdd:cd00707   86 VNNTR---VVGAeLAKFLDFLVDNtGLSLENVHLIGHSLGAHVAGFAGKRLN--GKLGRITGLDPAGPLF 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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