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Conserved domains on  [gi|15237911|ref|NP_197807|]
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Lipase class 3-related protein [Arabidopsis thaliana]

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, ...
 26-96 4.55e-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: 42.25  E-value: 4.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237911    26 QAIRAMIDKHSESAIWLAGHSLGAALVLLAGKTMKISGFLLES----YIFNPPII-SIPLEQLPGGVLLKGVFRIT 96
Cdd:pfam01764  51 AELKRLLEKYPDYSIVVTGHSLGGALASLAALDLVENGLRLSSrvtvVTFGQPRVgNLEFAKLHDSQGPKFSYRVV 126
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
26-96 4.55e-05

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 42.25  E-value: 4.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237911    26 QAIRAMIDKHSESAIWLAGHSLGAALVLLAGKTMKISGFLLES----YIFNPPII-SIPLEQLPGGVLLKGVFRIT 96
Cdd:pfam01764  51 AELKRLLEKYPDYSIVVTGHSLGGALASLAALDLVENGLRLSSrvtvVTFGQPRVgNLEFAKLHDSQGPKFSYRVV 126
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 25-64 3.73e-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: 3.73e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15237911  25 IQAIRAMIDKHSESAIWLAGHSLGAALVLLAGKTMKISGF 64
Cdd:cd00741  15 LPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGL 54
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
26-96 4.55e-05

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 42.25  E-value: 4.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237911    26 QAIRAMIDKHSESAIWLAGHSLGAALVLLAGKTMKISGFLLES----YIFNPPII-SIPLEQLPGGVLLKGVFRIT 96
Cdd:pfam01764  51 AELKRLLEKYPDYSIVVTGHSLGGALASLAALDLVENGLRLSSrvtvVTFGQPRVgNLEFAKLHDSQGPKFSYRVV 126
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 19-85 3.71e-04

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 40.53  E-value: 3.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237911    19 PRTIHAIQAIRAMIDKH-SESAIWLAGHSLGAALVLLAGKTMKISGFLLESYIFNPPIISIPLEQLPG 85
Cdd:pfam12697  39 PLDLADLADLAALLDELgAARPVVLVGHSLGGAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLAR 106
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 25-64 3.73e-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: 3.73e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15237911  25 IQAIRAMIDKHSESAIWLAGHSLGAALVLLAGKTMKISGF 64
Cdd:cd00741  15 LPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGL 54
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 25-56 4.57e-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: 37.46  E-value: 4.57e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 15237911  25 IQAIRAMIDKHSESAIWLAGHSLGAALVLLAG 56
Cdd:cd00519 115 LPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
 
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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