NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|766621679|ref|WP_044797222|]
View 

MULTISPECIES: lipase family protein [Bacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 45-197 7.99e-04

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: 40.92  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679  45 LQDNFNANLIASDDIHSVTGFgaYALEDRNTHEIFIVYVGTQpsQIGDLATDGAIGLHNLTNSPILG--------SLAEF 116
Cdd:cd00519   34 LLNVFSPDKLLKTDKQYDTQG--YVAVDHDRKTIVIAFRGTV--SLADWLTDLDFSPVPLDPPLCSGgkvhsgfySAYKS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679 117 QYSQAEKFYEKVKAKNKGKKITLLGHSLGGG----AANTVALRHQEDNINVLALNPAPVLNKDVVKYGYGTNMKNCRsLI 192
Cdd:cd00519  110 LYNQVLPELKSALKQYPDYKIIVTGHSLGGAlaslLALDLRLRGPGSDVTVYTFGQPRVGNAAFAEYLESTKGRVYR-VV 188


                 ....*
gi 766621679 193 NEYDP 197
Cdd:cd00519  189 HGNDI 193
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 45-197 7.99e-04

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: 40.92  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679  45 LQDNFNANLIASDDIHSVTGFgaYALEDRNTHEIFIVYVGTQpsQIGDLATDGAIGLHNLTNSPILG--------SLAEF 116
Cdd:cd00519   34 LLNVFSPDKLLKTDKQYDTQG--YVAVDHDRKTIVIAFRGTV--SLADWLTDLDFSPVPLDPPLCSGgkvhsgfySAYKS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679 117 QYSQAEKFYEKVKAKNKGKKITLLGHSLGGG----AANTVALRHQEDNINVLALNPAPVLNKDVVKYGYGTNMKNCRsLI 192
Cdd:cd00519  110 LYNQVLPELKSALKQYPDYKIIVTGHSLGGAlaslLALDLRLRGPGSDVTVYTFGQPRVGNAAFAEYLESTKGRVYR-VV 188


                 ....*
gi 766621679 193 NEYDP 197
Cdd:cd00519  189 HGNDI 193
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 53-154 9.07e-03

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 38.46  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679  53 LIASDDIHsvtGFGAYALEDRNTHEIFIVYVGTQpsQIGDLATDGAIGLH-----NLTNSPIL------------GSLAE 115
Cdd:COG5153   25 RAANDDID---GHFAVALDEKAIYDTIIAFRGTQ--GKPDWKTDINASLHdydekNKEADEKLplqvhegfeqyaAQVMD 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 766621679 116 FQYSQAEKFYEKVKAKNKGKKITLLGHSLGGGAANTVAL 154
Cdd:COG5153  100 LDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAV 138
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 45-197 7.99e-04

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: 40.92  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679  45 LQDNFNANLIASDDIHSVTGFgaYALEDRNTHEIFIVYVGTQpsQIGDLATDGAIGLHNLTNSPILG--------SLAEF 116
Cdd:cd00519   34 LLNVFSPDKLLKTDKQYDTQG--YVAVDHDRKTIVIAFRGTV--SLADWLTDLDFSPVPLDPPLCSGgkvhsgfySAYKS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679 117 QYSQAEKFYEKVKAKNKGKKITLLGHSLGGG----AANTVALRHQEDNINVLALNPAPVLNKDVVKYGYGTNMKNCRsLI 192
Cdd:cd00519  110 LYNQVLPELKSALKQYPDYKIIVTGHSLGGAlaslLALDLRLRGPGSDVTVYTFGQPRVGNAAFAEYLESTKGRVYR-VV 188


                 ....*
gi 766621679 193 NEYDP 197
Cdd:cd00519  189 HGNDI 193
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 114-198 8.39e-03

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: 37.09  E-value: 8.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679 114 AEFQYSQAEKFYEKVKAKNKGKKITLLGHSLGGG----AANTVALRHQEDNINVLALNPAPVLNKDVVKYGYGTNMKNC- 188
Cdd:cd00741    7 ARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGAlaglAGLDLRGRGLGRLVRVYTFGPPRVGNAAFAEDRLDPSDALFv 86

                         90
                 ....*....|
gi 766621679 189 RSLINEYDPL 198
Cdd:cd00741   87 DRIVNDNDIV 96
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 53-154 9.07e-03

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 38.46  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766621679  53 LIASDDIHsvtGFGAYALEDRNTHEIFIVYVGTQpsQIGDLATDGAIGLH-----NLTNSPIL------------GSLAE 115
Cdd:COG5153   25 RAANDDID---GHFAVALDEKAIYDTIIAFRGTQ--GKPDWKTDINASLHdydekNKEADEKLplqvhegfeqyaAQVMD 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 766621679 116 FQYSQAEKFYEKVKAKNKGKKITLLGHSLGGGAANTVAL 154
Cdd:COG5153  100 LDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAV 138
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH