NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958666215|ref|XP_038944553|]
View 

lipase member H isoform X2 [Rattus norvegicus]

Protein Classification

lipase family protein( domain architecture ID 10091066)

lipase family protein belonging to the alpha/beta hydrolase superfamily may function as a lipase/phospholipase, such as lipase member H that hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
78-347 1.54e-121

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: 353.86  E-value: 1.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  78 VRLMLYTQRDQTCAQVINSTALGSL-----NVTKKTTFIIHGFRPTGSPpVWMEELVQSLISVQEMNVVVVDWNRGATTv 152
Cdd:cd00707     3 VRFLLYTRENPNCPQLLFADDPSSLknsnfNPSRPTRFIIHGWTSSGEE-SWISDLRKAYLSRGDYNVIVVDWGRGANP- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 153 IYPHASSKTRKVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLD 231
Cdd:cd00707    81 NYPQAVNNTRVVGAELAKFLDFLVDNtGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 232 PSDAQFVDVIHSDTDALGYREALGHIDFYPNGGLDQPGCPKTIFGGIkYFKCDHQMSVFLYLASLQNNCSITAYPCDSYR 311
Cdd:cd00707   161 PSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSSD-FVACSHQRAVHYFAESILSPCGFVAYPCSSYD 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958666215 312 DYRNGKCVSCGAGhivsCPSLGYYADNWRE----YLWDRD 347
Cdd:cd00707   240 EFLAGKCFPCGSG----CVRMGYHADRFRRegkfYLKTNA 275
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
78-347 1.54e-121

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: 353.86  E-value: 1.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  78 VRLMLYTQRDQTCAQVINSTALGSL-----NVTKKTTFIIHGFRPTGSPpVWMEELVQSLISVQEMNVVVVDWNRGATTv 152
Cdd:cd00707     3 VRFLLYTRENPNCPQLLFADDPSSLknsnfNPSRPTRFIIHGWTSSGEE-SWISDLRKAYLSRGDYNVIVVDWGRGANP- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 153 IYPHASSKTRKVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLD 231
Cdd:cd00707    81 NYPQAVNNTRVVGAELAKFLDFLVDNtGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 232 PSDAQFVDVIHSDTDALGYREALGHIDFYPNGGLDQPGCPKTIFGGIkYFKCDHQMSVFLYLASLQNNCSITAYPCDSYR 311
Cdd:cd00707   161 PSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSSD-FVACSHQRAVHYFAESILSPCGFVAYPCSSYD 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958666215 312 DYRNGKCVSCGAGhivsCPSLGYYADNWRE----YLWDRD 347
Cdd:cd00707   240 EFLAGKCFPCGSG----CVRMGYHADRFRRegkfYLKTNA 275
Lipase pfam00151
Lipase;
78-363 5.35e-91

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 278.17  E-value: 5.35e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  78 VRLMLYTQRDQTCAQVIN---STALGS-LNVTKKTTFIIHGFRPTGSPPVWMEELVQSLISVQEMNVVVVDWNRGATTvI 153
Cdd:pfam00151  38 TRFLLYTNENPNNCQLITgdpETIRNSnFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVEDVNVICVDWKSGSRT-H 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 154 YPHASSKTRKVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLDP 232
Cdd:pfam00151 117 YTQAVQNIRVVGAEVANLLQWLSNElNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDP 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 233 SDAQFVDVIHSDTD-----ALGYREALGHIDFYPNGGLDQPGCPK----------TIFGGIKYFKCDHQMSVFLYLASLQ 297
Cdd:pfam00151 197 GDADFVDAIHTDTRpipglGFGISQPVGHVDFFPNGGSEQPGCQKnilsqiididGIWEGTQFVACNHLRSVHYYIDSLL 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958666215 298 NNCSITAYPCDSYRDYRNGKCVSCGAGhivSCPSLGYYADNWREylwDRDPPMTKAFFDTAETKPY 363
Cdd:pfam00151 277 NPRGFPGYPCSSYDAFSQNKCLPCPKG---GCPQMGHYADKFPG---KTSKLEQTFYLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
87-372 1.77e-50

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: 176.24  E-value: 1.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  87 DQTC---AQVINSTALGSLNVTKKTTFIIHGFRPTGSPPVWMEELVQSLISVQ-EMNVVVVDWNRGATTViYPHASSKTR 162
Cdd:TIGR03230  19 DDTCyivPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREpSANVIVVDWLSRAQQH-YPTSAAYTK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 163 KVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLDPSDAQFVDVI 241
Cdd:TIGR03230  98 LVGKDVAKFVNWMQEEfNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 242 HSDT-----DALGYREALGHIDFYPNGGLDQPGC---------PKTIFGGI-KYFKCDHQMSVFLYLASLQNNCSIT-AY 305
Cdd:TIGR03230 178 HTNTrgspdRSIGIQRPVGHIDIYPNGGTFQPGCdiqetllviAEKGLGNMdQLVKCSHERSIHLFIDSLLNEENPSmAY 257
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666215 306 PCDSYRDYRNGKCVSCGAGHivsCPSLGYYADNWREylwDRDppmTKAFFDTAETKPYCIYHYFVDI 372
Cdd:TIGR03230 258 RCSSKEAFNKGLCLSCRKNR---CNKLGYEINKVRT---KRS---SKMYLKTREMMPYKVFHYQVKV 315
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
78-347 1.54e-121

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: 353.86  E-value: 1.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  78 VRLMLYTQRDQTCAQVINSTALGSL-----NVTKKTTFIIHGFRPTGSPpVWMEELVQSLISVQEMNVVVVDWNRGATTv 152
Cdd:cd00707     3 VRFLLYTRENPNCPQLLFADDPSSLknsnfNPSRPTRFIIHGWTSSGEE-SWISDLRKAYLSRGDYNVIVVDWGRGANP- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 153 IYPHASSKTRKVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLD 231
Cdd:cd00707    81 NYPQAVNNTRVVGAELAKFLDFLVDNtGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 232 PSDAQFVDVIHSDTDALGYREALGHIDFYPNGGLDQPGCPKTIFGGIkYFKCDHQMSVFLYLASLQNNCSITAYPCDSYR 311
Cdd:cd00707   161 PSDAQFVDVIHTDGGLLGFSQPIGHADFYPNGGRDQPGCPKDILSSD-FVACSHQRAVHYFAESILSPCGFVAYPCSSYD 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958666215 312 DYRNGKCVSCGAGhivsCPSLGYYADNWRE----YLWDRD 347
Cdd:cd00707   240 EFLAGKCFPCGSG----CVRMGYHADRFRRegkfYLKTNA 275
Lipase pfam00151
Lipase;
78-363 5.35e-91

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 278.17  E-value: 5.35e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  78 VRLMLYTQRDQTCAQVIN---STALGS-LNVTKKTTFIIHGFRPTGSPPVWMEELVQSLISVQEMNVVVVDWNRGATTvI 153
Cdd:pfam00151  38 TRFLLYTNENPNNCQLITgdpETIRNSnFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVEDVNVICVDWKSGSRT-H 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 154 YPHASSKTRKVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLDP 232
Cdd:pfam00151 117 YTQAVQNIRVVGAEVANLLQWLSNElNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDP 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 233 SDAQFVDVIHSDTD-----ALGYREALGHIDFYPNGGLDQPGCPK----------TIFGGIKYFKCDHQMSVFLYLASLQ 297
Cdd:pfam00151 197 GDADFVDAIHTDTRpipglGFGISQPVGHVDFFPNGGSEQPGCQKnilsqiididGIWEGTQFVACNHLRSVHYYIDSLL 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958666215 298 NNCSITAYPCDSYRDYRNGKCVSCGAGhivSCPSLGYYADNWREylwDRDPPMTKAFFDTAETKPY 363
Cdd:pfam00151 277 NPRGFPGYPCSSYDAFSQNKCLPCPKG---GCPQMGHYADKFPG---KTSKLEQTFYLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
87-372 1.77e-50

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: 176.24  E-value: 1.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215  87 DQTC---AQVINSTALGSLNVTKKTTFIIHGFRPTGSPPVWMEELVQSLISVQ-EMNVVVVDWNRGATTViYPHASSKTR 162
Cdd:TIGR03230  19 DDTCyivPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREpSANVIVVDWLSRAQQH-YPTSAAYTK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 163 KVALILKEFIDQMLAK-GASLDNIYMIGVSLGAHIAGFVGEMYSGKLGRITGLDPAGPLFNGRPPEDRLDPSDAQFVDVI 241
Cdd:TIGR03230  98 LVGKDVAKFVNWMQEEfNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 242 HSDT-----DALGYREALGHIDFYPNGGLDQPGC---------PKTIFGGI-KYFKCDHQMSVFLYLASLQNNCSIT-AY 305
Cdd:TIGR03230 178 HTNTrgspdRSIGIQRPVGHIDIYPNGGTFQPGCdiqetllviAEKGLGNMdQLVKCSHERSIHLFIDSLLNEENPSmAY 257
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958666215 306 PCDSYRDYRNGKCVSCGAGHivsCPSLGYYADNWREylwDRDppmTKAFFDTAETKPYCIYHYFVDI 372
Cdd:TIGR03230 258 RCSSKEAFNKGLCLSCRKNR---CNKLGYEINKVRT---KRS---SKMYLKTREMMPYKVFHYQVKV 315
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
161-289 6.69e-26

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: 102.19  E-value: 6.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958666215 161 TRKVALILKEFIDQMLAKG---ASLDNIYMIGVSLGAHIAGFVG----EMYSGKLGRITGLDPAGPLFNGRPPeDRLDPS 233
Cdd:cd00741     3 FYKAARSLANLVLPLLKSAlaqYPDYKIHVTGHSLGGALAGLAGldlrGRGLGRLVRVYTFGPPRVGNAAFAE-DRLDPS 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958666215 234 DAQFVDVIHSDTDALGY------REALGHIDFYPNGGLDQPGCPKTI-------FGGIK---YFKCDHQMSV 289
Cdd:cd00741    82 DALFVDRIVNDNDIVPRlppggeGYPHGGAEFYINGGKSQPGCCKNVleavdidFGNIGlsgNGLCDHLRYF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH