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Conserved domains on  [gi|18396010|ref|NP_565323|]
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alpha/beta-Hydrolases superfamily 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, ...
 69-171 7.54e-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 cd00519:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 229  Bit Score: 55.56  E-value: 7.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010  69 RHLKDDADFSIFGGIFEYKSLQPD------VVDSGVPRYVIAFRGTLTKADSITrDI-----ELDIHIIRNGL-HR---- 132
Cdd:cd00519  27 VVFADIALLNVFSPDKLLKTDKQYdtqgyvAVDHDRKTIVIAFRGTVSLADWLT-DLdfspvPLDPPLCSGGKvHSgfys 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18396010 133 --TSRFEIAMQAVRSMADSVGASSFWLTGHSLGAAMALLAG 171
Cdd:cd00519 106 ayKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 69-171 7.54e-09

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: 55.56  E-value: 7.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010  69 RHLKDDADFSIFGGIFEYKSLQPD------VVDSGVPRYVIAFRGTLTKADSITrDI-----ELDIHIIRNGL-HR---- 132
Cdd:cd00519  27 VVFADIALLNVFSPDKLLKTDKQYdtqgyvAVDHDRKTIVIAFRGTVSLADWLT-DLdfspvPLDPPLCSGGKvHSgfys 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18396010 133 --TSRFEIAMQAVRSMADSVGASSFWLTGHSLGAAMALLAG 171
Cdd:cd00519 106 ayKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
100-190 4.53e-07

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 50.52  E-value: 4.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010 100 RYVIAFRGTLTKADSITrDIELDIHIIRNGL-----HRTsrFEIAMQAVRSMADSV-----GASSFWLTGHSLGAAMALL 169
Cdd:COG3675  28 EVIVAFRGTESLTDWLT-NLNAAQVPYPFAKtggkvHRG--FYRALQSLRELLEDAlrplsPGKRLYVTGHSLGGALATL 104

                        90       100
                ....*....|....*....|.
gi 18396010 170 AgktmgksGVYIKSLLFNPPY 190
Cdd:COG3675 105 A-------AADLERNYIFPVR 118
Lipase_3 pfam01764
Lipase (class 3);
102-171 1.74e-05

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 44.17  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010   102 VIAFRGTLTKADSITrDIELDIHIIRNGLHRTSRFEIAM-QAVRSMADSVGAS-----------SFWLTGHSLGAAMALL 169
Cdd:pfam01764   1 VVAFRGTNSILDWLT-DFDFSLTPFKDFFLGGGKVHSGFlSAYTSVREQVLAElkrllekypdySIVVTGHSLGGALASL 79


                  ..
gi 18396010   170 AG 171
Cdd:pfam01764  80 AA 81
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 69-171 7.54e-09

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: 55.56  E-value: 7.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010  69 RHLKDDADFSIFGGIFEYKSLQPD------VVDSGVPRYVIAFRGTLTKADSITrDI-----ELDIHIIRNGL-HR---- 132
Cdd:cd00519  27 VVFADIALLNVFSPDKLLKTDKQYdtqgyvAVDHDRKTIVIAFRGTVSLADWLT-DLdfspvPLDPPLCSGGKvHSgfys 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18396010 133 --TSRFEIAMQAVRSMADSVGASSFWLTGHSLGAAMALLAG 171
Cdd:cd00519 106 ayKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
100-190 4.53e-07

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 50.52  E-value: 4.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010 100 RYVIAFRGTLTKADSITrDIELDIHIIRNGL-----HRTsrFEIAMQAVRSMADSV-----GASSFWLTGHSLGAAMALL 169
Cdd:COG3675  28 EVIVAFRGTESLTDWLT-NLNAAQVPYPFAKtggkvHRG--FYRALQSLRELLEDAlrplsPGKRLYVTGHSLGGALATL 104

                        90       100
                ....*....|....*....|.
gi 18396010 170 AgktmgksGVYIKSLLFNPPY 190
Cdd:COG3675 105 A-------AADLERNYIFPVR 118
Lipase_3 pfam01764
Lipase (class 3);
102-171 1.74e-05

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 44.17  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396010   102 VIAFRGTLTKADSITrDIELDIHIIRNGLHRTSRFEIAM-QAVRSMADSVGAS-----------SFWLTGHSLGAAMALL 169
Cdd:pfam01764   1 VVAFRGTNSILDWLT-DFDFSLTPFKDFFLGGGKVHSGFlSAYTSVREQVLAElkrllekypdySIVVTGHSLGGALASL 79


                  ..
gi 18396010   170 AG 171
Cdd:pfam01764  80 AA 81
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 140-172 1.80e-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: 41.33  E-value: 1.80e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 18396010 140 MQAVRSMADSVGASSFWLTGHSLGAAMALLAGK 172
Cdd:cd00741  15 LPLLKSALAQYPDYKIHVTGHSLGGALAGLAGL 47
 
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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