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Conserved domains on  [gi|493799464|ref|WP_006747407|]
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lipase class 3 [Thioalkalivibrio paradoxus]

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, ...
 18-222 1.42e-08

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: 54.40  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493799464  18 MTLATIAY---KPLDRVADALANPDLATQGRWA-LEWRVWGDGCQMFVARDDLTGQIAISIRGSAaSPQteefwiDWFEq 93
Cdd:cd00519    9 AKLAAAAYcvdANILAKAVVFADIALLNVFSPDkLLKTDKQYDTQGYVAVDHDRKTIVIAFRGTV-SLA------DWLT- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493799464  94 DLNTLGLSpwLYGDGPRGAYV------SWGSL--DGLTSLLSLVDErtTPETTLVeyL------AAqqpfpgvvpvvghg 159
Cdd:cd00519   81 DLDFSPVP--LDPPLCSGGKVhsgfysAYKSLynQVLPELKSALKQ--YPDYKII--VtghslgGA-------------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493799464 160 vggtLAYMLAGYLQQHIGDRSLQFwpVTFGAPTAGNPAFAKWMEdefaASAGRFY---NTIDLVPH 222
Cdd:cd00519  141 ----LASLLALDLRLRGPGSDVTV--YTFGQPRVGNAAFAEYLE----STKGRVYrvvHGNDIVPR 196
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 18-222 1.42e-08

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: 54.40  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493799464  18 MTLATIAY---KPLDRVADALANPDLATQGRWA-LEWRVWGDGCQMFVARDDLTGQIAISIRGSAaSPQteefwiDWFEq 93
Cdd:cd00519    9 AKLAAAAYcvdANILAKAVVFADIALLNVFSPDkLLKTDKQYDTQGYVAVDHDRKTIVIAFRGTV-SLA------DWLT- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493799464  94 DLNTLGLSpwLYGDGPRGAYV------SWGSL--DGLTSLLSLVDErtTPETTLVeyL------AAqqpfpgvvpvvghg 159
Cdd:cd00519   81 DLDFSPVP--LDPPLCSGGKVhsgfysAYKSLynQVLPELKSALKQ--YPDYKII--VtghslgGA-------------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493799464 160 vggtLAYMLAGYLQQHIGDRSLQFwpVTFGAPTAGNPAFAKWMEdefaASAGRFY---NTIDLVPH 222
Cdd:cd00519  141 ----LASLLALDLRLRGPGSDVTV--YTFGQPRVGNAAFAEYLE----STKGRVYrvvHGNDIVPR 196
Lipase_3 pfam01764
Lipase (class 3);
186-223 3.64e-05

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 43.02  E-value: 3.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 493799464  186 VTFGAPTAGNPAFAKWMEDEFAASAGRFYNTIDLVPHA 223
Cdd:pfam01764  98 VTFGQPRVGNLEFAKLHDSQGPKFSYRVVHQRDIVPRL 135
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 18-222 1.42e-08

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: 54.40  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493799464  18 MTLATIAY---KPLDRVADALANPDLATQGRWA-LEWRVWGDGCQMFVARDDLTGQIAISIRGSAaSPQteefwiDWFEq 93
Cdd:cd00519    9 AKLAAAAYcvdANILAKAVVFADIALLNVFSPDkLLKTDKQYDTQGYVAVDHDRKTIVIAFRGTV-SLA------DWLT- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493799464  94 DLNTLGLSpwLYGDGPRGAYV------SWGSL--DGLTSLLSLVDErtTPETTLVeyL------AAqqpfpgvvpvvghg 159
Cdd:cd00519   81 DLDFSPVP--LDPPLCSGGKVhsgfysAYKSLynQVLPELKSALKQ--YPDYKII--VtghslgGA-------------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493799464 160 vggtLAYMLAGYLQQHIGDRSLQFwpVTFGAPTAGNPAFAKWMEdefaASAGRFY---NTIDLVPH 222
Cdd:cd00519  141 ----LASLLALDLRLRGPGSDVTV--YTFGQPRVGNAAFAEYLE----STKGRVYrvvHGNDIVPR 196
Lipase_3 pfam01764
Lipase (class 3);
186-223 3.64e-05

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 43.02  E-value: 3.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 493799464  186 VTFGAPTAGNPAFAKWMEDEFAASAGRFYNTIDLVPHA 223
Cdd:pfam01764  98 VTFGQPRVGNLEFAKLHDSQGPKFSYRVVHQRDIVPRL 135
 
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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