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Conserved domains on  [gi|1829519429|ref|NP_001366495|]
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lipase member I isoform 7 precursor [Homo sapiens]

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, ...
 16-144 1.39e-63

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 cd00707:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 275  Bit Score: 201.32  E-value: 1.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  16 GLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGiQFIKCNHQRAVHLF 95
Cdd:cd00707   142 GLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-DFVACSHQRAVHYF 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1829519429  96 MASLETNCNFISFPCRSYKDYKTSLCVDCDcfkeKSCPRLGYQAKLFKG 144
Cdd:cd00707   221 AESILSPCGFVAYPCSSYDEFLAGKCFPCG----SGCVRMGYHADRFRR 265
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 16-144 1.39e-63

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 201.32  E-value: 1.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  16 GLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGiQFIKCNHQRAVHLF 95
Cdd:cd00707   142 GLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-DFVACSHQRAVHYF 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1829519429  96 MASLETNCNFISFPCRSYKDYKTSLCVDCDcfkeKSCPRLGYQAKLFKG 144
Cdd:cd00707   221 AESILSPCGFVAYPCSSYDEFLAGKCFPCG----SGCVRMGYHADRFRR 265
Lipase pfam00151
Lipase;
15-169 1.91e-51

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 172.24  E-value: 1.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  15 SGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSN-----GLGIQEPLGHIDFYPNGGNKQPGCPKSIFS---------- 79
Cdd:pfam00151 176 TGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRpipglGFGISQPVGHVDFFPNGGSEQPGCQKNILSqiididgiwe 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  80 GIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCdcfKEKSCPRLGYQAKLFKGVLKermegrPLRTTV 159
Cdd:pfam00151 256 GTQFVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKCLPC---PKGGCPQMGHYADKFPGKTS------KLEQTF 326

                         170
                  ....*....|
gi 1829519429 160 FLDTSGTYPF 169
Cdd:pfam00151 327 YLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
 15-138 1.55e-27

lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.


Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 110.75  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  15 SGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNG-----LGIQEPLGHIDFYPNGGNKQPGCP-KSIFSGI------- 81
Cdd:TIGR03230 148 TGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRGspdrsIGIQRPVGHIDIYPNGGTFQPGCDiQETLLVIaekglgn 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  82 --QFIKCNHQRAVHLFMASL-ETNCNFISFPCRSYKDYKTSLCVDCdcfKEKSCPRLGYQ 138
Cdd:TIGR03230 228 mdQLVKCSHERSIHLFIDSLlNEENPSMAYRCSSKEAFNKGLCLSC---RKNRCNKLGYE 284
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 16-144 1.39e-63

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 201.32  E-value: 1.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  16 GLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGiQFIKCNHQRAVHLF 95
Cdd:cd00707   142 GLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-DFVACSHQRAVHYF 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1829519429  96 MASLETNCNFISFPCRSYKDYKTSLCVDCDcfkeKSCPRLGYQAKLFKG 144
Cdd:cd00707   221 AESILSPCGFVAYPCSSYDEFLAGKCFPCG----SGCVRMGYHADRFRR 265
Lipase pfam00151
Lipase;
15-169 1.91e-51

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 172.24  E-value: 1.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  15 SGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSN-----GLGIQEPLGHIDFYPNGGNKQPGCPKSIFS---------- 79
Cdd:pfam00151 176 TGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRpipglGFGISQPVGHVDFFPNGGSEQPGCQKNILSqiididgiwe 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  80 GIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCdcfKEKSCPRLGYQAKLFKGVLKermegrPLRTTV 159
Cdd:pfam00151 256 GTQFVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKCLPC---PKGGCPQMGHYADKFPGKTS------KLEQTF 326

                         170
                  ....*....|
gi 1829519429 160 FLDTSGTYPF 169
Cdd:pfam00151 327 YLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
 15-138 1.55e-27

lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.


Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 110.75  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  15 SGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNG-----LGIQEPLGHIDFYPNGGNKQPGCP-KSIFSGI------- 81
Cdd:TIGR03230 148 TGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRGspdrsIGIQRPVGHIDIYPNGGTFQPGCDiQETLLVIaekglgn 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  82 --QFIKCNHQRAVHLFMASL-ETNCNFISFPCRSYKDYKTSLCVDCdcfKEKSCPRLGYQ 138
Cdd:TIGR03230 228 mdQLVKCSHERSIHLFIDSLlNEENPSMAYRCSSKEAFNKGLCLSC---RKNRCNKLGYE 284
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 16-92 1.36e-10

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: 58.67  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829519429  16 GLDPAGPRFSRKPPYsRLDYTDAKFVDVIHSDSN------GLGIQEPLGHIDFYPNGGNKQPGCPK----------SIFS 79
Cdd:cd00741    62 TFGPPRVGNAAFAED-RLDPSDALFVDRIVNDNDivprlpPGGEGYPHGGAEFYINGGKSQPGCCKnvleavdidfGNIG 140

                          90
                  ....*....|...
gi 1829519429  80 GIQFIKCNHQRAV 92
Cdd:cd00741   141 LSGNGLCDHLRYF 153
 
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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