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Conserved domains on  [gi|767963065|ref|XP_011538171|]
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inactive pancreatic lipase-related protein 1 isoform X1 [Homo sapiens]

Protein Classification

Pancreat_lipase_like and PLAT_PL domain-containing protein( domain architecture ID 11988342)

Pancreat_lipase_like and PLAT_PL domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
1-204 4.91e-122

Lipase;


:

Pssm-ID: 395099  Cd Length: 336  Bit Score: 353.29  E-value: 4.91e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065    1 MLDILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPG-LSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPlI 79
Cdd:pfam00151 134 LLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGkLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRP-I 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   80 PFLGFGTNQQMGHLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRdFVACNHLRSYKYYLESILNPDGFAAYPCTSYKS 159
Cdd:pfam00151 213 PGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDA 291
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767963065  160 FESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNF 204
Cdd:pfam00151 292 FSQNKCLPCPKGGCPQMGHYADKFPGKTSKLEQTFYLNTGSSSPF 336
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
207-318 2.80e-64

PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238857  Cd Length: 113  Bit Score: 198.36  E-value: 2.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065 207 WRYGVSITLSG-RTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINPTLPKVGA 285
Cdd:cd01759    1 WRYKVSVTLSGkKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767963065 286 TKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC 318
Cdd:cd01759   81 EKITVQSGKDGKVFNFCSSETVRENVLQTLTPC 113
 
Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
1-204 4.91e-122

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 353.29  E-value: 4.91e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065    1 MLDILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPG-LSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPlI 79
Cdd:pfam00151 134 LLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGkLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRP-I 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   80 PFLGFGTNQQMGHLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRdFVACNHLRSYKYYLESILNPDGFAAYPCTSYKS 159
Cdd:pfam00151 213 PGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDA 291
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767963065  160 FESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNF 204
Cdd:pfam00151 292 FSQNKCLPCPKGGCPQMGHYADKFPGKTSKLEQTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
1-200 8.73e-91

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  Cd Length: 275  Bit Score: 271.81  E-value: 8.73e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   1 MLDILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPG-LSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPli 79
Cdd:cd00707   99 FLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGkLGRITGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGL-- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065  80 pflgFGTNQQMGHLDFFPNGGESMPGCKKNALSqivdldgiwagtRDFVACNHLRSYKYYLESILNPDGFAAYPCTSYKS 159
Cdd:cd00707  177 ----LGFSQPIGHADFYPNGGRDQPGCPKDILS------------SDFVACSHQRAVHYFAESILSPCGFVAYPCSSYDE 240
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767963065 160 FESDKCFPCPDqGCPQMGHYADKFAGrtseeQQKFFLNTGE 200
Cdd:cd00707  241 FLAGKCFPCGS-GCVRMGYHADRFRR-----EGKFYLKTNA 275
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
207-318 2.80e-64

PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238857  Cd Length: 113  Bit Score: 198.36  E-value: 2.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065 207 WRYGVSITLSG-RTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINPTLPKVGA 285
Cdd:cd01759    1 WRYKVSVTLSGkKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767963065 286 TKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC 318
Cdd:cd01759   81 EKITVQSGKDGKVFNFCSSETVRENVLQTLTPC 113
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
8-307 3.47e-46

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: 161.60  E-value: 3.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065    8 EYSYPPSKVHLIGHSLGAHVAGEAGSKTP-GLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPlIPFLGFGT 86
Cdd:TIGR03230 113 EFNYPWDNVHLLGYSLGAHVAGIAGSLTKhKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRG-SPDRSIGI 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   87 NQQMGHLDFFPNGGESMPGCK-KNALSQIVDldgiwAGTRD---FVACNHLRSYKYYLESILNPDGFA-AYPCTSYKSFE 161
Cdd:TIGR03230 192 QRPVGHIDIYPNGGTFQPGCDiQETLLVIAE-----KGLGNmdqLVKCSHERSIHLFIDSLLNEENPSmAYRCSSKEAFN 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065  162 SDKCFPCPDQGCPQMGHYADKFAGRTSeeqQKFFLNTGEASNFARWRYGVSITLSGRTA---TGQ-IKVALFGNKGNTHQ 237
Cdd:TIGR03230 267 KGLCLSCRKNRCNKLGYEINKVRTKRS---SKMYLKTREMMPYKVFHYQVKVHFFGKTSlshTDQpMKISLYGTHGEKEN 343
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767963065  238 YSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINP-----TLPKVGATKITVQKGEEKTVYNFCSEDTV 307
Cdd:TIGR03230 344 IPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISwsdwwSSPGFHIRKLRIKSGETQSKVIFSAKEGE 418
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
207-310 4.69e-25

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 96.56  E-value: 4.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   207 WRYGVSITLSGRTATG---QIKVALFGNK---GNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNvinptL 280
Cdd:smart00308   1 GKYKVTVTTGGLDFAGttaSVSLSLVGAEgdgKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR-----H 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 767963065   281 PKVGATKITVQKGEEKTVYNFCSEDTVRED 310
Cdd:smart00308  76 PEWFLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
209-316 4.57e-16

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 72.85  E-value: 4.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065  209 YGVSIT---LSGRTATGQIKVALFGNKGNTHQYSIFRGI--LKPGSTHSYEFDAKLDVGTIEKVKFLWNNnviNPTLPKV 283
Cdd:pfam01477   1 YQVKVVtgdELGAGTDADVYISLYGKVGESAQLEITLDNpdFERGAEDSFEIDTDWDVGAILKINLHWDN---NGLSDEW 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767963065  284 GATKITVQK-GEEKTVYNFCSEDTVREDTLLTLT 316
Cdd:pfam01477  78 FLKSITVEVpGETGGKYTFPCNSWVYGSKKYKET 111
 
Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
1-204 4.91e-122

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 353.29  E-value: 4.91e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065    1 MLDILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPG-LSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPlI 79
Cdd:pfam00151 134 LLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGkLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRP-I 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   80 PFLGFGTNQQMGHLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRdFVACNHLRSYKYYLESILNPDGFAAYPCTSYKS 159
Cdd:pfam00151 213 PGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDA 291
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767963065  160 FESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNF 204
Cdd:pfam00151 292 FSQNKCLPCPKGGCPQMGHYADKFPGKTSKLEQTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
1-200 8.73e-91

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  Cd Length: 275  Bit Score: 271.81  E-value: 8.73e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   1 MLDILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPG-LSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPli 79
Cdd:cd00707   99 FLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGkLGRITGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGL-- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065  80 pflgFGTNQQMGHLDFFPNGGESMPGCKKNALSqivdldgiwagtRDFVACNHLRSYKYYLESILNPDGFAAYPCTSYKS 159
Cdd:cd00707  177 ----LGFSQPIGHADFYPNGGRDQPGCPKDILS------------SDFVACSHQRAVHYFAESILSPCGFVAYPCSSYDE 240
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767963065 160 FESDKCFPCPDqGCPQMGHYADKFAGrtseeQQKFFLNTGE 200
Cdd:cd00707  241 FLAGKCFPCGS-GCVRMGYHADRFRR-----EGKFYLKTNA 275
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
207-318 2.80e-64

PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238857  Cd Length: 113  Bit Score: 198.36  E-value: 2.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065 207 WRYGVSITLSG-RTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINPTLPKVGA 285
Cdd:cd01759    1 WRYKVSVTLSGkKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767963065 286 TKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC 318
Cdd:cd01759   81 EKITVQSGKDGKVFNFCSSETVRENVLQTLTPC 113
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
8-307 3.47e-46

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: 161.60  E-value: 3.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065    8 EYSYPPSKVHLIGHSLGAHVAGEAGSKTP-GLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPlIPFLGFGT 86
Cdd:TIGR03230 113 EFNYPWDNVHLLGYSLGAHVAGIAGSLTKhKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRG-SPDRSIGI 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   87 NQQMGHLDFFPNGGESMPGCK-KNALSQIVDldgiwAGTRD---FVACNHLRSYKYYLESILNPDGFA-AYPCTSYKSFE 161
Cdd:TIGR03230 192 QRPVGHIDIYPNGGTFQPGCDiQETLLVIAE-----KGLGNmdqLVKCSHERSIHLFIDSLLNEENPSmAYRCSSKEAFN 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065  162 SDKCFPCPDQGCPQMGHYADKFAGRTSeeqQKFFLNTGEASNFARWRYGVSITLSGRTA---TGQ-IKVALFGNKGNTHQ 237
Cdd:TIGR03230 267 KGLCLSCRKNRCNKLGYEINKVRTKRS---SKMYLKTREMMPYKVFHYQVKVHFFGKTSlshTDQpMKISLYGTHGEKEN 343
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767963065  238 YSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINP-----TLPKVGATKITVQKGEEKTVYNFCSEDTV 307
Cdd:TIGR03230 344 IPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISwsdwwSSPGFHIRKLRIKSGETQSKVIFSAKEGE 418
PLAT_lipase cd01755
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ...
207-318 6.54e-43

PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major subgroups, the lipoprotein lipase (LPL) and the pancreatic triglyceride lipase. LPL is a key enzyme in catabolism of plasma lipoprotein triglycerides (TGs). The central role of triglyceride lipases is in energy production. In general, PLAT/LH2 domain's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238853  Cd Length: 120  Bit Score: 143.59  E-value: 6.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065 207 WRYGVSITLSGRTA---TGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVIN----PT 279
Cdd:cd01755    1 WHYQVKVHLSGKKNlevDGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINsnsgET 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767963065 280 LPKVGATKITVQKGEEKTVYNFCSEDTVREDT-LLTLTPC 318
Cdd:cd01755   81 LPKLGARKIRVKSGETQKKFTFCSQDTVRELEvLQTLVKC 120
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
9-136 2.61e-31

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: 114.91  E-value: 2.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   9 YSYPPSKVHLIGHSLGAHVAGEAG-----SKTPGLSRITGLDPVEASFESTPEEvRLDPSDADFVDVIHTDAAPLIPFLG 83
Cdd:cd00741   23 AQYPDYKIHVTGHSLGGALAGLAGldlrgRGLGRLVRVYTFGPPRVGNAAFAED-RLDPSDALFVDRIVNDNDIVPRLPP 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767963065  84 FGTNQQMGHLDFFPNGGESMPGCKKNALSQiVDLDGIWAGTRDFVACNHLRSY 136
Cdd:cd00741  102 GGEGYPHGGAEFYINGGKSQPGCCKNVLEA-VDIDFGNIGLSGNGLCDHLRYF 153
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
207-310 4.69e-25

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 96.56  E-value: 4.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065   207 WRYGVSITLSGRTATG---QIKVALFGNK---GNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNvinptL 280
Cdd:smart00308   1 GKYKVTVTTGGLDFAGttaSVSLSLVGAEgdgKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR-----H 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 767963065   281 PKVGATKITVQKGEEKTVYNFCSEDTVRED 310
Cdd:smart00308  76 PEWFLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
207-316 1.09e-23

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 93.56  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065 207 WRYGVSITLSGRTATG---QIKVALFGNKGNTHQYSIFRGIL--KPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINptlP 281
Cdd:cd00113    1 CRYTVTIKTGDKKGAGtdsNISLALYGENGNSSDIPILDGPGsfERGSTDTFQIDLKLDIGDITKVYLRRDGSGLS---D 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767963065 282 KVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLT 316
Cdd:cd00113   78 GWYCESITVQALGTKKVYTFPVNRWVLGGKWYTSV 112
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
209-316 4.57e-16

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 72.85  E-value: 4.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963065  209 YGVSIT---LSGRTATGQIKVALFGNKGNTHQYSIFRGI--LKPGSTHSYEFDAKLDVGTIEKVKFLWNNnviNPTLPKV 283
Cdd:pfam01477   1 YQVKVVtgdELGAGTDADVYISLYGKVGESAQLEITLDNpdFERGAEDSFEIDTDWDVGAILKINLHWDN---NGLSDEW 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767963065  284 GATKITVQK-GEEKTVYNFCSEDTVREDTLLTLT 316
Cdd:pfam01477  78 FLKSITVEVpGETGGKYTFPCNSWVYGSKKYKET 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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