|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase |
pfam00151 |
Lipase; |
17-352 |
0e+00 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 587.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 17 KEVCYERLGCFSDDSPWSGIT-ERPLHILPWSPKDVNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFI 95
Cdd:pfam00151 1 KEVCYGQLGCFGDKIPWAGNTlVRPVKSLPWSPKDIDTRFLLYTNENPNNCQLITGDPETIRNSNFNTSRKTRFIIHGFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 96 DKG-EENWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHA 174
Cdd:pfam00151 81 DKGyEESWLSDMCKALFQVEDVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 175 AGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIvPNLGFGMSQVVGHLDFFPNGGVEMPGC 254
Cdd:pfam00151 161 AGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPI-PGLGFGISQPVGHVDFFPNGGSEQPGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 255 KKNILSQIVDIDGIWEGTRdFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGK 334
Cdd:pfam00151 240 QKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGK 318
|
330
....*....|....*...
gi 126318 335 TNDVGQKFYLDTGDASNF 352
Cdd:pfam00151 319 TSKLEQTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
51-348 |
3.04e-155 |
|
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: 441.30 E-value: 3.04e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 51 VNTRFLLYTNENPNNFQEV-AADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCICVDWKGGSRT 129
Cdd:cd00707 1 IDVRFLLYTRENPNCPQLLfADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLSRGDYNVIVVDWGRGANP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 130 GYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLD 209
Cdd:cd00707 81 NYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 210 PSDAKFVDVIHTDGAPivpnlgFGMSQVVGHLDFFPNGGVEMPGCKKNILSqivdidgiwegtRDFAACNHLRSYKYYTD 289
Cdd:cd00707 161 PSDAQFVDVIHTDGGL------LGFSQPIGHADFYPNGGRDQPGCPKDILS------------SDFVACSHQRAVHYFAE 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 126318 290 SIVNPDGFAGFPCASYNVFTANKCFPCPSgGCPQMGHYADRYPGKtndvgQKFYLDTGD 348
Cdd:cd00707 223 SILSPCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHADRFRRE-----GKFYLKTNA 275
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
355-465 |
6.54e-65 |
|
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: 204.52 E-value: 6.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 355 WRYKVSVTLSGK-KVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGA 433
Cdd:cd01759 1 WRYKVSVTLSGKkKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
|
90 100 110
....*....|....*....|....*....|...
gi 126318 434 SKIIVETNV-GKQFNFCSPETVREEVLLTLTPC 465
Cdd:cd01759 81 EKITVQSGKdGKVFNFCSSETVRENVLQTLTPC 113
|
|
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
50-419 |
1.30e-63 |
|
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: 212.45 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 50 DVNTRFLLYTNENPNN--FQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGE-ENWLANVCKNLFKVE-SVNCICVDWKG 125
Cdd:TIGR03230 4 DIESKFSLRTPEEPDDdtCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMfESWVPKLVAALYEREpSANVIVVDWLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 126 GSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPEL 205
Cdd:TIGR03230 84 RAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 206 VRLDPSDAKFVDVIHTD--GApivPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDIDGIwEGTRDFAACNHLRS 283
Cdd:TIGR03230 164 STLSPDDADFVDVLHTNtrGS---PDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGL-GNMDQLVKCSHERS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 284 YKYYTDSIVNPDGFA-GFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNdvgQKFYLDTGDASNFARWRYKVSVT 362
Cdd:TIGR03230 240 IHLFIDSLLNEENPSmAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRS---SKMYLKTREMMPYKVFHYQVKVH 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126318 363 LSGKKVTGH----ILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIW 419
Cdd:TIGR03230 317 FFGKTSLSHtdqpMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKW 377
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
355-457 |
4.65e-20 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 85.00 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 355 WRYKVSVTLSGKKVTG---HILVSLFGNK---GNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNvinptL 428
Cdd:smart00308 1 GKYKVTVTTGGLDFAGttaSVSLSLVGAEgdgKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR-----H 75
|
90 100 110
....*....|....*....|....*....|
gi 126318 429 PRVGASKIIVE-TNVGKQFNFCSPETVREE 457
Cdd:smart00308 76 PEWFLKSITVKdLPTGGKYHFPCNSWVYPD 105
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
357-457 |
1.36e-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: 75.55 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 357 YKVSVT---LSGKKVTGHILVSLFGNKGNSKQYEIFK--GTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLprv 431
Cdd:pfam01477 1 YQVKVVtgdELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW--- 77
|
90 100
....*....|....*....|....*...
gi 126318 432 GASKIIVETNV--GKQFNFCSPETVREE 457
Cdd:pfam01477 78 FLKSITVEVPGetGGKYTFPCNSWVYGS 105
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
130-203 |
5.93e-03 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 36.35 E-value: 5.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126318 130 GYTQASQNIRIVGAEVAYFVEFLQSAFGYSPsnVHVIGHSLGA----HAAGEAGRRTNgtIGRITGLdpaepcfqGTP 203
Cdd:COG1075 39 NYPSTNGSIEDSAEQLAAFVDAVLAATGAEK--VDLVGHSMGGlvarYYLKRLGGAAK--VARVVTL--------GTP 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase |
pfam00151 |
Lipase; |
17-352 |
0e+00 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 587.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 17 KEVCYERLGCFSDDSPWSGIT-ERPLHILPWSPKDVNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFI 95
Cdd:pfam00151 1 KEVCYGQLGCFGDKIPWAGNTlVRPVKSLPWSPKDIDTRFLLYTNENPNNCQLITGDPETIRNSNFNTSRKTRFIIHGFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 96 DKG-EENWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHA 174
Cdd:pfam00151 81 DKGyEESWLSDMCKALFQVEDVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 175 AGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIvPNLGFGMSQVVGHLDFFPNGGVEMPGC 254
Cdd:pfam00151 161 AGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPI-PGLGFGISQPVGHVDFFPNGGSEQPGC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 255 KKNILSQIVDIDGIWEGTRdFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGK 334
Cdd:pfam00151 240 QKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGK 318
|
330
....*....|....*...
gi 126318 335 TNDVGQKFYLDTGDASNF 352
Cdd:pfam00151 319 TSKLEQTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
51-348 |
3.04e-155 |
|
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: 441.30 E-value: 3.04e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 51 VNTRFLLYTNENPNNFQEV-AADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCICVDWKGGSRT 129
Cdd:cd00707 1 IDVRFLLYTRENPNCPQLLfADDPSSLKNSNFNPSRPTRFIIHGWTSSGEESWISDLRKAYLSRGDYNVIVVDWGRGANP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 130 GYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLD 209
Cdd:cd00707 81 NYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 210 PSDAKFVDVIHTDGAPivpnlgFGMSQVVGHLDFFPNGGVEMPGCKKNILSqivdidgiwegtRDFAACNHLRSYKYYTD 289
Cdd:cd00707 161 PSDAQFVDVIHTDGGL------LGFSQPIGHADFYPNGGRDQPGCPKDILS------------SDFVACSHQRAVHYFAE 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 126318 290 SIVNPDGFAGFPCASYNVFTANKCFPCPSgGCPQMGHYADRYPGKtndvgQKFYLDTGD 348
Cdd:cd00707 223 SILSPCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHADRFRRE-----GKFYLKTNA 275
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
355-465 |
6.54e-65 |
|
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: 204.52 E-value: 6.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 355 WRYKVSVTLSGK-KVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGA 433
Cdd:cd01759 1 WRYKVSVTLSGKkKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
|
90 100 110
....*....|....*....|....*....|...
gi 126318 434 SKIIVETNV-GKQFNFCSPETVREEVLLTLTPC 465
Cdd:cd01759 81 EKITVQSGKdGKVFNFCSSETVRENVLQTLTPC 113
|
|
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
50-419 |
1.30e-63 |
|
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: 212.45 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 50 DVNTRFLLYTNENPNN--FQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGE-ENWLANVCKNLFKVE-SVNCICVDWKG 125
Cdd:TIGR03230 4 DIESKFSLRTPEEPDDdtCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMfESWVPKLVAALYEREpSANVIVVDWLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 126 GSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPEL 205
Cdd:TIGR03230 84 RAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 206 VRLDPSDAKFVDVIHTD--GApivPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDIDGIwEGTRDFAACNHLRS 283
Cdd:TIGR03230 164 STLSPDDADFVDVLHTNtrGS---PDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGL-GNMDQLVKCSHERS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 284 YKYYTDSIVNPDGFA-GFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNdvgQKFYLDTGDASNFARWRYKVSVT 362
Cdd:TIGR03230 240 IHLFIDSLLNEENPSmAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRS---SKMYLKTREMMPYKVFHYQVKVH 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126318 363 LSGKKVTGH----ILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIW 419
Cdd:TIGR03230 317 FFGKTSLSHtdqpMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKW 377
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
355-465 |
8.18e-46 |
|
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: 155.15 E-value: 8.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 355 WRYKVSVTLSGKK---VTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVIN----PT 427
Cdd:cd01755 1 WHYQVKVHLSGKKnleVDGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINsnsgET 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 126318 428 LPRVGASKIIVETNV-GKQFNFCSPETVRE-EVLLTLTPC 465
Cdd:cd01755 81 LPKLGARKIRVKSGEtQKKFTFCSQDTVRElEVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
136-284 |
2.14e-35 |
|
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: 128.77 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 136 QNIRIVGAEVAYFVEFLQSAFG--YSPSNVHVIGHSLGAHAAGEAGRRTNGT----IGRITGLDPAEPCFQGTPElVRLD 209
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSALaqYPDYKIHVTGHSLGGALAGLAGLDLRGRglgrLVRVYTFGPPRVGNAAFAE-DRLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126318 210 PSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQiVDIDGIWEGTRDFAACNHLRSY 284
Cdd:cd00741 80 PSDALFVDRIVNDNDIVPRLPPGGEGYPHGGAEFYINGGKSQPGCCKNVLEA-VDIDFGNIGLSGNGLCDHLRYF 153
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
355-457 |
4.65e-20 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 85.00 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 355 WRYKVSVTLSGKKVTG---HILVSLFGNK---GNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNvinptL 428
Cdd:smart00308 1 GKYKVTVTTGGLDFAGttaSVSLSLVGAEgdgKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR-----H 75
|
90 100 110
....*....|....*....|....*....|
gi 126318 429 PRVGASKIIVE-TNVGKQFNFCSPETVREE 457
Cdd:smart00308 76 PEWFLKSITVKdLPTGGKYHFPCNSWVYPD 105
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
357-457 |
1.36e-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: 75.55 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 357 YKVSVT---LSGKKVTGHILVSLFGNKGNSKQYEIFK--GTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLprv 431
Cdd:pfam01477 1 YQVKVVtgdELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW--- 77
|
90 100
....*....|....*....|....*...
gi 126318 432 GASKIIVETNV--GKQFNFCSPETVREE 457
Cdd:pfam01477 78 FLKSITVEVPGetGGKYTFPCNSWVYGS 105
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
355-463 |
1.37e-15 |
|
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: 72.76 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 355 WRYKVSVTLSGKKVTG---HILVSLFGNKGNSKQYEIFKG--TLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLp 429
Cdd:cd00113 1 CRYTVTIKTGDKKGAGtdsNISLALYGENGNSSDIPILDGpgSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGW- 79
|
90 100 110
....*....|....*....|....*....|....*
gi 126318 430 rvGASKIIVETNV-GKQFNFCSPETVREEVLLTLT 463
Cdd:cd00113 80 --YCESITVQALGtKKVYTFPVNRWVLGGKWYTSV 112
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
118-265 |
7.62e-04 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 40.95 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126318 118 CICVDWKG-------GSRTGYTQASqnirivgaeVAYFVEFLQSAFGYSPsnVHVIGHSLG----AHAAGEAGRRtngtI 186
Cdd:pfam00561 30 VIALDLRGfgkssrpKAQDDYRTDD---------LAEDLEYILEALGLEK--VNLVGHSMGgliaLAYAAKYPDR----V 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126318 187 GRITGLDPAEPCFQGTPELVRLDPSDAKFVDVihTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDI 265
Cdd:pfam00561 95 KALVLLGALDPPHELDEADRFILALFPGFFDG--FVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGDYAL 171
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
130-203 |
5.93e-03 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 36.35 E-value: 5.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126318 130 GYTQASQNIRIVGAEVAYFVEFLQSAFGYSPsnVHVIGHSLGA----HAAGEAGRRTNgtIGRITGLdpaepcfqGTP 203
Cdd:COG1075 39 NYPSTNGSIEDSAEQLAAFVDAVLAATGAEK--VDLVGHSMGGlvarYYLKRLGGAAK--VARVVTL--------GTP 104
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
357-419 |
6.48e-03 |
|
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of plasma lipoprotein triglycerides (TGs) and has therefeore has a profound influence on triglyceride and high-density lipoprotein (HDL) cholesterol levels in the blood. In general, PLAT/LH2 domain's proposed function is to mediate interaction with lipids or membrane bound proteins.
Pssm-ID: 238856 Cd Length: 137 Bit Score: 36.99 E-value: 6.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126318 357 YKVSVTLSGKKVTGHI----LVSLFGNKGNSKQYEI-FKGTLKPDSTHSNEFDSDVDVGDLQMVKFIW 419
Cdd:cd01758 3 YQLKIHFFNQTNRIETdptfTISLYGTLGESENLPLtLPEGITGNKTNSFLITTEKDIGDLLMLKLKW 70
|
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