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Conserved domains on  [gi|1831512283|ref|NP_001368234|]
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Fungal lipase-like domain-containing protein [Caenorhabditis elegans]

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, ...
 1-44 1.17e-14

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: 64.97  E-value: 1.17e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1831512283   1 MKLLTAGQPRTGDYAYSNWHQNTFAY-SFRIVHAHDMVPHLPFQY 44
Cdd:pfam01764  95 VTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
1-44 1.17e-14

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 64.97  E-value: 1.17e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1831512283   1 MKLLTAGQPRTGDYAYSNWHQNTFAY-SFRIVHAHDMVPHLPFQY 44
Cdd:pfam01764  95 VTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 1-98 2.24e-14

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: 64.83  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512283   1 MKLLTAGQPRTGDYAYSN--WHQNTFAYSFRIVHAHDMVPHLPFqyelvDHDKMYHHRTEIWYNNDMSIGSSYHVCQEA- 77
Cdd:cd00741    58 VRVYTFGPPRVGNAAFAEdrLDPSDALFVDRIVNDNDIVPRLPP-----GGEGYPHGGAEFYINGGKSQPGCCKNVLEAv 132

                          90       100
                  ....*....|....*....|.
gi 1831512283  78 DGFYCSNQNADLSWNDHTHYY 98
Cdd:cd00741   133 DIDFGNIGLSGNGLCDHLRYF 153
PLN00413 PLN00413
triacylglycerol lipase
 5-55 1.23e-04

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 39.61  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831512283   5 TAGQPRTGDYAYSNWHQNT---FAYSF-RIVHAHDMVPHLPFQyelvDHDKMYHH 55
Cdd:PLN00413  322 TFGQPRVGDEDFGIFMKDKlkeFDVKYeRYVYCNDMVPRLPFD----DKTLMFKH 372
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
1-44 1.17e-14

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 64.97  E-value: 1.17e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1831512283   1 MKLLTAGQPRTGDYAYSNWHQNTFAY-SFRIVHAHDMVPHLPFQY 44
Cdd:pfam01764  95 VTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 1-98 2.24e-14

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: 64.83  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512283   1 MKLLTAGQPRTGDYAYSN--WHQNTFAYSFRIVHAHDMVPHLPFqyelvDHDKMYHHRTEIWYNNDMSIGSSYHVCQEA- 77
Cdd:cd00741    58 VRVYTFGPPRVGNAAFAEdrLDPSDALFVDRIVNDNDIVPRLPP-----GGEGYPHGGAEFYINGGKSQPGCCKNVLEAv 132

                          90       100
                  ....*....|....*....|.
gi 1831512283  78 DGFYCSNQNADLSWNDHTHYY 98
Cdd:cd00741   133 DIDFGNIGLSGNGLCDHLRYF 153
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 1-62 5.42e-14

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: 65.19  E-value: 5.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831512283   1 MKLLTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLPFQYELVDHDkMYHHRTEIWYN 62
Cdd:cd00519   158 VTVYTFGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTPPEG-YTHVGTEVWID 218
PLN00413 PLN00413
triacylglycerol lipase
 5-55 1.23e-04

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 39.61  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831512283   5 TAGQPRTGDYAYSNWHQNT---FAYSF-RIVHAHDMVPHLPFQyelvDHDKMYHH 55
Cdd:PLN00413  322 TFGQPRVGDEDFGIFMKDKlkeFDVKYeRYVYCNDMVPRLPFD----DKTLMFKH 372
PLN02934 PLN02934
triacylglycerol lipase
 5-42 1.24e-04

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 39.77  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1831512283   5 TAGQPRTGDYAYSNWHQNTFAYS----FRIVHAHDMVPHLPF 42
Cdd:PLN02934  359 TFGQPRIGNRQLGKFMEAQLNYPvpryFRVVYCNDLVPRLPY 400
 
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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