|
Name |
Accession |
Description |
Interval |
E-value |
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
53-488 |
7.05e-173 |
|
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: 493.64 E-value: 7.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 53 FNIRTSKDPEHEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQTREKEANVVVVDWLPLAHQL 132
Cdd:TIGR03230 9 FSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 133 YIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSP 212
Cdd:TIGR03230 89 YPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 213 DDADFVDVLHTYTL-SFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFA---YGTISEMVKCEHERAVHLFVDSLV 288
Cdd:TIGR03230 169 DDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAekgLGNMDQLVKCSHERSIHLFIDSLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 289 NQDKPSFAFQCTDPNRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFRVYHYQLKVHMFSYKNSGDIQP 368
Cdd:TIGR03230 249 NEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 369 DLYITLYGSNADSQNLPLeIVEKIELNATNTFLVYTEEYLGDLFKIRLTWEGVSS-SWYNLWNEFRsylsqpsspsreLH 447
Cdd:TIGR03230 329 PMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------FH 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 83304379 448 IRRIRVKSGETQRKVAFCVQDPMKNSISPGQE-LWFYKCQND 488
Cdd:TIGR03230 396 IRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKEK 437
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
51-342 |
4.50e-122 |
|
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: 358.09 E-value: 4.50e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 51 VTFNIRTSKDPEHeGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGmFESWLHKLVSALQTREkEANVVVVDWLPLAH 130
Cdd:cd00707 3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 131 QLYIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRL 210
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 211 SPDDADFVDVLHTYTLSFglsiGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFaygtisemVKCEHERAVHLFVDSlVNQ 290
Cdd:cd00707 160 DPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGCPKDILSSDF--------VACSHQRAVHYFAES-ILS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 83304379 291 DKPSFAFQCTDPNRFKRGICLSCRKnRCNNIGYNAKkmRKKRNSKMYLKTRA 342
Cdd:cd00707 227 PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
47-346 |
3.44e-118 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 350.59 E-value: 3.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 47 TKPSVTFNIRTSKDPEheGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQTREKeANVVVVDWL 126
Cdd:pfam00151 34 KDIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVED-VNVICVDWK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 127 PLAHQLYIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDI 206
Cdd:pfam00151 111 SGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTPE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 207 NRRLSPDDADFVDVLHTYT-LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFAYGTISE---MVKCEHERAVHL 282
Cdd:pfam00151 191 EVRLDPGDADFVDAIHTDTrPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEgtqFVACNHLRSVHY 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83304379 283 FVDSLVNQDkPSFAFQCTDPNRFKRGICLSCRKNRCNNIGYNAKKMRKKRNS---KMYLKTRAGMPF 346
Cdd:pfam00151 271 YIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
349-468 |
4.53e-10 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 56.88 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 349 YHYQLKVHmFSYKNSGDIQPDLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEYLGDLFKIRLTWEGVSSSWY 426
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHRHPEWF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 83304379 427 nlwnefrsylsqpsspsrelhIRRIRVKSGETQRKVAFCVQD 468
Cdd:smart00308 80 ---------------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
53-488 |
7.05e-173 |
|
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: 493.64 E-value: 7.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 53 FNIRTSKDPEHEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQTREKEANVVVVDWLPLAHQL 132
Cdd:TIGR03230 9 FSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 133 YIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSP 212
Cdd:TIGR03230 89 YPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 213 DDADFVDVLHTYTL-SFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFA---YGTISEMVKCEHERAVHLFVDSLV 288
Cdd:TIGR03230 169 DDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAekgLGNMDQLVKCSHERSIHLFIDSLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 289 NQDKPSFAFQCTDPNRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFRVYHYQLKVHMFSYKNSGDIQP 368
Cdd:TIGR03230 249 NEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 369 DLYITLYGSNADSQNLPLeIVEKIELNATNTFLVYTEEYLGDLFKIRLTWEGVSS-SWYNLWNEFRsylsqpsspsreLH 447
Cdd:TIGR03230 329 PMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------FH 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 83304379 448 IRRIRVKSGETQRKVAFCVQDPMKNSISPGQE-LWFYKCQND 488
Cdd:TIGR03230 396 IRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKEK 437
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
51-342 |
4.50e-122 |
|
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: 358.09 E-value: 4.50e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 51 VTFNIRTSKDPEHeGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGmFESWLHKLVSALQTREkEANVVVVDWLPLAH 130
Cdd:cd00707 3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 131 QLYIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRL 210
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 211 SPDDADFVDVLHTYTLSFglsiGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFaygtisemVKCEHERAVHLFVDSlVNQ 290
Cdd:cd00707 160 DPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGCPKDILSSDF--------VACSHQRAVHYFAES-ILS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 83304379 291 DKPSFAFQCTDPNRFKRGICLSCRKnRCNNIGYNAKkmRKKRNSKMYLKTRA 342
Cdd:cd00707 227 PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
47-346 |
3.44e-118 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 350.59 E-value: 3.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 47 TKPSVTFNIRTSKDPEheGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQTREKeANVVVVDWL 126
Cdd:pfam00151 34 KDIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVED-VNVICVDWK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 127 PLAHQLYIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDI 206
Cdd:pfam00151 111 SGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTPE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 207 NRRLSPDDADFVDVLHTYT-LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFAYGTISE---MVKCEHERAVHL 282
Cdd:pfam00151 191 EVRLDPGDADFVDAIHTDTrPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEgtqFVACNHLRSVHY 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83304379 283 FVDSLVNQDkPSFAFQCTDPNRFKRGICLSCRKNRCNNIGYNAKKMRKKRNS---KMYLKTRAGMPF 346
Cdd:pfam00151 271 YIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
349-485 |
7.26e-65 |
|
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: 206.09 E-value: 7.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 349 YHYQLKVHMFSYKNSGDIQPDLYITLYGSNADSQNLPLEIVEKIELNATNTFLVYTEEYLGDLFKIRLTWEGVSSSWYNL 428
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 83304379 429 WNEFRSYLSQPSSPSRELHIRRIRVKSGETQRKVAFCVQDPMKNSISPGQELWFYKC 485
Cdd:cd01758 81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
349-485 |
1.78e-38 |
|
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: 136.27 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 349 YHYQLKVHMFSYKNSgDIQPDLYITLYGSNADSQNLPLEIVEkIELNATNTFLVYTEEYLGDLFKIRLTWEGVSSSWYNL 428
Cdd:cd01755 1 WHYQVKVHLSGKKNL-EVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 83304379 429 WNefrsylsqpsspSRELHIRRIRVKSGETQRKVAFCVQDPMKnsiSPGQELWFYKC 485
Cdd:cd01755 79 ET------------LPKLGARKIRVKSGETQKKFTFCSQDTVR---ELEVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
138-280 |
4.54e-25 |
|
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: 100.65 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 138 SNTRVVGRRVAGMLNWLQEKG--EFSLGDVHLIGYSLGAHVAGYAGNFVKGT----VGRITGLDPAGPMFEGVDiNRRLS 211
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSAlaQYPDYKIHVTGHSLGGALAGLAGLDLRGRglgrLVRVYTFGPPRVGNAAFA-EDRLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83304379 212 PDDADFVDVLHTYT--LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFN---DVMGSFAYGTISEMVKCEHERAV 280
Cdd:cd00741 80 PSDALFVDRIVNDNdiVPRLPPGGEGYPHGGAEFYINGGKSQPGCCKNvleAVDIDFGNIGLSGNGLCDHLRYF 153
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
351-482 |
3.05e-18 |
|
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: 80.17 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 351 YQLKVHMFSYKNSGdIQPDLYITLYGSNADSQNLPLEIVEK-IELNATNTFLVYTEEYLGDLFKIRLTWEGvssswynlw 429
Cdd:pfam01477 1 YQVKVVTGDELGAG-TDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDN--------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 83304379 430 nefrsylsqpSSPSRELHIRRIRV-KSGETQRKVAFCVQDPMKNSISPGQELWF 482
Cdd:pfam01477 71 ----------NGLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVF 114
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
349-468 |
4.53e-10 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 56.88 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 349 YHYQLKVHmFSYKNSGDIQPDLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEYLGDLFKIRLTWEGVSSSWY 426
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHRHPEWF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 83304379 427 nlwnefrsylsqpsspsrelhIRRIRVKSGETQRKVAFCVQD 468
Cdd:smart00308 80 ---------------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
349-468 |
1.78e-06 |
|
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: 46.95 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 349 YHYQLKVHmFSYKNSGDIQPDLYITLYGSNADSQNLP-LEIVEKIELNATNTFLVYTEEYLGDLFKIRLTWE--GVSSSW 425
Cdd:cd00113 1 CRYTVTIK-TGDKKGAGTDSNISLALYGENGNSSDIPiLDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDgsGLSDGW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 83304379 426 YnlwnefrsylsqpsspsrelhIRRIRVKSGETQRKVAFCVQD 468
Cdd:cd00113 80 Y---------------------CESITVQALGTKKVYTFPVNR 101
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
86-236 |
2.11e-06 |
|
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: 49.04 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 86 KTFFIIHGWTMSGmfESWlHKLVSALQtrEKEANVVVVDWL-------PLAHQLYIDAVsntrvvgrrVAGMLNWLQEKg 158
Cdd:pfam00561 1 PPVLLLHGLPGSS--DLW-RKLAPALA--RDGFRVIALDLRgfgkssrPKAQDDYRTDD---------LAEDLEYILEA- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83304379 159 eFSLGDVHLIGYSLG-AHVAGYAGNFVKGtVGRITGLDPAGPMFEGVDINRRLSPDDADFVD--VLHTYTLSFGLSIGIR 235
Cdd:pfam00561 66 -LGLEKVNLVGHSMGgLIALAYAAKYPDR-VKALVLLGALDPPHELDEADRFILALFPGFFDgfVADFAPNPLGRLVAKL 143
|
.
gi 83304379 236 M 236
Cdd:pfam00561 144 L 144
|
|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
371-426 |
2.29e-04 |
|
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.
Pssm-ID: 238850 Cd Length: 120 Bit Score: 40.72 E-value: 2.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83304379 371 YITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEYLGDLFKIRLtW---EGVSSSWY 426
Cdd:cd01752 22 TITLYGAEGESEPHHLRDPEKpiFERGSVDSFLLTTPFPLGELQSIRL-WhdnSGLSPSWY 81
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
369-426 |
3.96e-04 |
|
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.
Pssm-ID: 238854 Cd Length: 120 Bit Score: 40.23 E-value: 3.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83304379 369 DLYITLYGSNADSQNLPL---EIVEKIELNATNTFLVYTeEYLGDLFKIRLtW---EGVSSSWY 426
Cdd:cd01756 20 NVFITLYGENGDTGKRKLkksNNKNKFERGQTDKFTVEA-VDLGKLKKIRI-GhdnSGLGAGWF 81
|
|
| |
