|
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 ... |
25-416 |
4.14e-159 |
|
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: 456.28 E-value: 4.14e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 25 MSGMFESWLHKLVSALQMREKDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAH 104
Cdd:TIGR03230 52 VTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 105 VAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTL-SFGLSIGIRMPVGHIDIYPNGGDFQPGC 183
Cdd:TIGR03230 132 VAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 184 GFND---VIGSFAYGTISEMVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKK 260
Cdd:TIGR03230 212 DIQEtllVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 261 RNSKMYLKTRAGMPFKVYHYQLKVHMFSYNNSGDTQPTLYITLYGSNADSQNLPLeIVEKIELNATNTFLVYTEEDLGDL 340
Cdd:TIGR03230 292 RSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQPMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGEL 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569003362 341 LKMRLTWEGVAH-SWYNLWNEFRnylsqpsnpsreLYIRRIRVKSGETQRKVTFCTQDPTKSSISPGQE-LWFHKCQD 416
Cdd:TIGR03230 371 LMVKLKWEKDTYiSWSDWWSSPG------------FHIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
24-271 |
1.65e-110 |
|
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: 326.12 E-value: 1.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 24 YMSGMFESWLHKLVSALQMREkDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGA 103
Cdd:cd00707 45 WTSSGEESWISDLRKAYLSRG-DYNVIVVDWGRGANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 104 HVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTLSFglsiGIRMPVGHIDIYPNGGDFQPGC 183
Cdd:cd00707 124 HVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 184 GFNDVIGSFaygtisemVKCEHERAVHLFVDSlVNQDKPSFAFQCTDSSRFKRGICLSCRKnRCNNIGYNAKkmRKKRNS 263
Cdd:cd00707 200 PKDILSSDF--------VACSHQRAVHYFAES-ILSPCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREG 267
|
....*...
gi 569003362 264 KMYLKTRA 271
Cdd:cd00707 268 KFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
26-275 |
3.07e-105 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 315.15 E-value: 3.07e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 26 SGMFESWLHKLVSALQMREkDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHV 105
Cdd:pfam00151 82 KGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 106 AGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYT-LSFGLSIGIRMPVGHIDIYPNGGDFQPGCG 184
Cdd:pfam00151 161 AGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTrPIPGLGFGISQPVGHVDFFPNGGSEQPGCQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 185 FN---DVIGSFAYGTISEMVKCEHERAVHLFVDSLVNQDkPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKR 261
Cdd:pfam00151 241 KNilsQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKT 319
|
250
....*....|....*..
gi 569003362 262 NS---KMYLKTRAGMPF 275
Cdd:pfam00151 320 SKleqTFYLNTGSSSPF 336
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
278-394 |
1.12e-12 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 63.81 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 278 YHYQLKVHmFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEDLGDLLKMRLTWEgvahswy 355
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNE------- 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 569003362 356 nlwnefrnylsqpsNPSRELYIRRIRVKSGETQRKVTFC 394
Cdd:smart00308 73 --------------HRHPEWFLKSITVKDLPTGGKYHFP 97
|
|
| |
|
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 ... |
25-416 |
4.14e-159 |
|
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: 456.28 E-value: 4.14e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 25 MSGMFESWLHKLVSALQMREKDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAH 104
Cdd:TIGR03230 52 VTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 105 VAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTL-SFGLSIGIRMPVGHIDIYPNGGDFQPGC 183
Cdd:TIGR03230 132 VAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 184 GFND---VIGSFAYGTISEMVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKK 260
Cdd:TIGR03230 212 DIQEtllVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 261 RNSKMYLKTRAGMPFKVYHYQLKVHMFSYNNSGDTQPTLYITLYGSNADSQNLPLeIVEKIELNATNTFLVYTEEDLGDL 340
Cdd:TIGR03230 292 RSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQPMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGEL 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569003362 341 LKMRLTWEGVAH-SWYNLWNEFRnylsqpsnpsreLYIRRIRVKSGETQRKVTFCTQDPTKSSISPGQE-LWFHKCQD 416
Cdd:TIGR03230 371 LMVKLKWEKDTYiSWSDWWSSPG------------FHIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
24-271 |
1.65e-110 |
|
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: 326.12 E-value: 1.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 24 YMSGMFESWLHKLVSALQMREkDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGA 103
Cdd:cd00707 45 WTSSGEESWISDLRKAYLSRG-DYNVIVVDWGRGANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 104 HVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTLSFglsiGIRMPVGHIDIYPNGGDFQPGC 183
Cdd:cd00707 124 HVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 184 GFNDVIGSFaygtisemVKCEHERAVHLFVDSlVNQDKPSFAFQCTDSSRFKRGICLSCRKnRCNNIGYNAKkmRKKRNS 263
Cdd:cd00707 200 PKDILSSDF--------VACSHQRAVHYFAES-ILSPCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREG 267
|
....*...
gi 569003362 264 KMYLKTRA 271
Cdd:cd00707 268 KFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
26-275 |
3.07e-105 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 315.15 E-value: 3.07e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 26 SGMFESWLHKLVSALQMREkDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHV 105
Cdd:pfam00151 82 KGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 106 AGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYT-LSFGLSIGIRMPVGHIDIYPNGGDFQPGCG 184
Cdd:pfam00151 161 AGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTrPIPGLGFGISQPVGHVDFFPNGGSEQPGCQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 185 FN---DVIGSFAYGTISEMVKCEHERAVHLFVDSLVNQDkPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKR 261
Cdd:pfam00151 241 KNilsQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKT 319
|
250
....*....|....*..
gi 569003362 262 NS---KMYLKTRAGMPF 275
Cdd:pfam00151 320 SKleqTFYLNTGSSSPF 336
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
278-414 |
1.10e-67 |
|
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: 211.48 E-value: 1.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 278 YHYQLKVHMFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGVAHSWYNL 357
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 569003362 358 WNEFRNYLSQPSNPSRELYIRRIRVKSGETQRKVTFCTQDPTKSSISPGQELWFHKC 414
Cdd:cd01758 81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
278-414 |
3.64e-40 |
|
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: 139.35 E-value: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 278 YHYQLKVHMFSYNNSgDTQPTLYITLYGSNADSQNLPLEIVEkIELNATNTFLVYTEEDLGDLLKMRLTWEGVAHSWYNL 357
Cdd:cd01755 1 WHYQVKVHLSGKKNL-EVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 569003362 358 WNefrnylsqpsnpSRELYIRRIRVKSGETQRKVTFCTQDPtksSISPGQELWFHKC 414
Cdd:cd01755 79 ET------------LPKLGARKIRVKSGETQKKFTFCSQDT---VRELEVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
67-209 |
9.58e-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: 9.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 67 NNTRVVGQRVAGMLDWLQEK--EEFSLGNVHLIGYSLGAHVAGYAGNFVKGT----VGRITGLDPAGPMFEGVDiNRRLS 140
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSalAQYPDYKIHVTGHSLGGALAGLAGLDLRGRglgrLVRVYTFGPPRVGNAAFA-EDRLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569003362 141 PDDADFVDVLHTYT--LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFN---DVIGSFAYGTISEMVKCEHERAV 209
Cdd:cd00741 80 PSDALFVDRIVNDNdiVPRLPPGGEGYPHGGAEFYINGGKSQPGCCKNvleAVDIDFGNIGLSGNGLCDHLRYF 153
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
280-412 |
5.00e-21 |
|
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: 87.87 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 280 YQLKVHMFSYNNSGdTQPTLYITLYGSNADSQNLPLEIVEK-IELNATNTFLVYTEEDLGDLLKMRLTWEGvahswynlw 358
Cdd:pfam01477 1 YQVKVVTGDELGAG-TDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDN--------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 569003362 359 nefrnylsqpSNPSRELYIRRIRV-KSGETQRKVTFCTQDPTKSSISPGQELWFH 412
Cdd:pfam01477 71 ----------NGLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
278-394 |
1.12e-12 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 63.81 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 278 YHYQLKVHmFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEDLGDLLKMRLTWEgvahswy 355
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNE------- 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 569003362 356 nlwnefrnylsqpsNPSRELYIRRIRVKSGETQRKVTFC 394
Cdd:smart00308 73 --------------HRHPEWFLKSITVKDLPTGGKYHFP 97
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
278-394 |
3.27e-08 |
|
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: 51.57 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 278 YHYQLKVHmFSYNNSGDTQPTLYITLYGSNADSQNLP-LEIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGvahswyn 356
Cdd:cd00113 1 CRYTVTIK-TGDKKGAGTDSNISLALYGENGNSSDIPiLDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDG------- 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 569003362 357 lwnefrnylsqpSNPSRELYIRRIRVKSGETQRKVTFC 394
Cdd:cd00113 73 ------------SGLSDGWYCESITVQALGTKKVYTFP 98
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
27-165 |
1.10e-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: 43.65 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 27 GMFESWlHKLVSALQmrEKDANVVVVDWL-------PLAHQLYTDAVnntrvvgqrVAGMLDWLQEKeeFSLGNVHLIGY 99
Cdd:pfam00561 11 GSSDLW-RKLAPALA--RDGFRVIALDLRgfgkssrPKAQDDYRTDD---------LAEDLEYILEA--LGLEKVNLVGH 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003362 100 SLG-AHVAGYAGNFVKGtVGRITGLDPAGPMFEGVDINRRLSPDDADFVD--VLHTYTLSFGLSIGIRM 165
Cdd:pfam00561 77 SMGgLIALAYAAKYPDR-VKALVLLGALDPPHELDEADRFILALFPGFFDgfVADFAPNPLGRLVAKLL 144
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|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
295-355 |
1.16e-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: 41.49 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569003362 295 TQPTLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEDLGDLLKMRLtW---EGVAHSWY 355
Cdd:cd01752 17 TTAKVTITLYGAEGESEPHHLRDPEKpiFERGSVDSFLLTTPFPLGELQSIRL-WhdnSGLSPSWY 81
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
292-397 |
8.11e-04 |
|
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: 38.89 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003362 292 SGDTQPTLYITLYGSNADSQNLplEIVE-KIELNATNTFLVYTEEDLGDLLKMRLTWEGvahswyNLWNEFRNYLSQpsn 370
Cdd:cd01759 12 KKKVTGTILVSLYGNKGNTRQY--EIFKgTLKPGNTYSAFIDVDVDVGPLTKVKFIWNN------NVINITLPKVGA--- 80
|
90 100
....*....|....*....|....*..
gi 569003362 371 psrelyiRRIRVKSGETQRKVTFCTQD 397
Cdd:cd01759 81 -------EKITVQSGKDGKVFNFCSSE 100
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
300-345 |
7.08e-03 |
|
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: 36.38 E-value: 7.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 569003362 300 YITLYGSNADSQNLPL---EIVEKIELNATNTFLVYTeEDLGDLLKMRL 345
Cdd:cd01756 22 FITLYGENGDTGKRKLkksNNKNKFERGQTDKFTVEA-VDLGKLKKIRI 69
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| |
