|
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 ... |
33-472 |
0e+00 |
|
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: 880.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 33 DFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230 1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 113 WLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230 81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 273 HLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 353 EDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 126723006 433 VKAGETQKKVIFCAREKV-SHLQKGKDSAVFVKCHDKSLKK 472
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSR 441
|
|
| Lipase |
pfam00151 |
Lipase; |
30-338 |
1.41e-168 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 477.70 E-value: 1.41e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 30 AGRDFSDIESKFALRTPEDTaeDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREpDSNVI 109
Cdd:pfam00151 29 LPWSPKDIDTRFLLYTNENP--NNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 110 VVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNF 189
Cdd:pfam00151 106 CVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 190 EYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHE 269
Cdd:pfam00151 186 QGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHL 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723006 270 RSIHLFIDSLLNeENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSS---KMYLKTRSQMPY 338
Cdd:pfam00151 266 RSVHYYIDSLLN-PRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
37-334 |
8.10e-127 |
|
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: 369.26 E-value: 8.10e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 37 IESKFALRTPEDtAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMyESWVPKLVAALYKREpDSNVIVVDWLYR 116
Cdd:cd00707 1 IDVRFLLYTREN-PNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 117 AQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPS 196
Cdd:cd00707 78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 197 RLSPDDADFVDVLHTFtrgspGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRviaerglgdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126723006 277 DSLLNeENPSKAYRCNSKEAFEKGLCLSCRKnRCNNLGYEINkvRAKRSSKMYLKTRS 334
Cdd:cd00707 222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
341-452 |
4.29e-17 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 76.53 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 341 FHYQVKIHFSGtEDGKQHNQAFEISLYGTVA---ESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWisdsyfsw 417
Cdd:smart00308 1 GKYKVTVTTGG-LDFAGTTASVSLSLVGAEGdgkESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKN-------- 71
|
90 100 110
....*....|....*....|....*....|....*
gi 126723006 418 pdWWSSPSFVIERIRVKAGETQKKVIFCAREKVSH 452
Cdd:smart00308 72 --EHRHPEWFLKSITVKDLPTGGKYHFPCNSWVYP 104
|
|
| MhpC |
COG0596 |
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ... |
77-197 |
2.56e-04 |
|
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 223669 [Multi-domain] Cd Length: 282 Bit Score: 42.69 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 77 VVIHGWTVTGMYESWVPKLVAALYKRepdSNVIVVDWlyRAQQHYPVSAGYTKLVGNDVARFINwmeeefNYPLDNVHLL 156
Cdd:COG0596 25 VLLHGFPGSSSVWRPVFKVLPALAAR---YRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------ALGLEKVVLV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 126723006 157 GYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSR 197
Cdd:COG0596 94 GHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
|
|
|
|
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 ... |
33-472 |
0e+00 |
|
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: 880.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 33 DFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230 1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 113 WLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230 81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 273 HLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 353 EDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 126723006 433 VKAGETQKKVIFCAREKV-SHLQKGKDSAVFVKCHDKSLKK 472
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSR 441
|
|
| Lipase |
pfam00151 |
Lipase; |
30-338 |
1.41e-168 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 477.70 E-value: 1.41e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 30 AGRDFSDIESKFALRTPEDTaeDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREpDSNVI 109
Cdd:pfam00151 29 LPWSPKDIDTRFLLYTNENP--NNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 110 VVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNF 189
Cdd:pfam00151 106 CVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 190 EYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHE 269
Cdd:pfam00151 186 QGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHL 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723006 270 RSIHLFIDSLLNeENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSS---KMYLKTRSQMPY 338
Cdd:pfam00151 266 RSVHYYIDSLLN-PRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
37-334 |
8.10e-127 |
|
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: 369.26 E-value: 8.10e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 37 IESKFALRTPEDtAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMyESWVPKLVAALYKREpDSNVIVVDWLYR 116
Cdd:cd00707 1 IDVRFLLYTREN-PNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 117 AQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPS 196
Cdd:cd00707 78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 197 RLSPDDADFVDVLHTFtrgspGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRviaerglgdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126723006 277 DSLLNeENPSKAYRCNSKEAFEKGLCLSCRKnRCNNLGYEINkvRAKRSSKMYLKTRS 334
Cdd:cd00707 222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
341-465 |
2.27e-62 |
|
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: 199.15 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 341 FHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVST-NKTYSFLIYTEVDIGELLMMKLKWISDSYFSWP- 418
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITgNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSw 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 126723006 419 ----------DWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKC 465
Cdd:cd01758 81 wtvqtiipwsGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
341-465 |
2.67e-47 |
|
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: 159.00 E-value: 2.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 341 FHYQVKIHFSGTEDGKQhNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPdW 420
Cdd:cd01755 1 WHYQVKVHLSGKKNLEV-DGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNS-G 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 126723006 421 WSSPSFVIERIRVKAGETQKKVIFCAREKVSHLqkgKDSAVFVKC 465
Cdd:cd01755 79 ETLPKLGARKIRVKSGETQKKFTFCSQDTVREL---EVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
127-271 |
2.01e-27 |
|
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: 107.20 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 127 YTKLVGNDVARFINWMEEEF--NYPLDNVHLLGYSLGAHAAGVAGSLTNK----KVNRITGLDPAGPNFEyAEAPSRLSP 200
Cdd:cd00741 2 GFYKAARSLANLVLPLLKSAlaQYPDYKIHVTGHSLGGALAGLAGLDLRGrglgRLVRVYTFGPPRVGNA-AFAEDRLDP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126723006 201 DDADFVDVLHT----FTRGSPGrsiGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERS 271
Cdd:cd00741 81 SDALFVDRIVNdndiVPRLPPG---GEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRY 152
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
343-463 |
8.11e-25 |
|
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: 98.66 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 343 YQVKIHfSGTEDGKQHNQAFEISLYGTVAESENIPFTL--PEVSTNKTYSFLIYTEVDIGELLMMKLKWISdsyfswpdW 420
Cdd:pfam01477 1 YQVKVV-TGDELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN--------N 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 126723006 421 WSSPSFVIERIRV-KAGETQKKVIFCAREKVSHLQKGKDSAVFV 463
Cdd:pfam01477 72 GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
341-452 |
4.29e-17 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 76.53 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 341 FHYQVKIHFSGtEDGKQHNQAFEISLYGTVA---ESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWisdsyfsw 417
Cdd:smart00308 1 GKYKVTVTTGG-LDFAGTTASVSLSLVGAEGdgkESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKN-------- 71
|
90 100 110
....*....|....*....|....*....|....*
gi 126723006 418 pdWWSSPSFVIERIRVKAGETQKKVIFCAREKVSH 452
Cdd:smart00308 72 --EHRHPEWFLKSITVKDLPTGGKYHFPCNSWVYP 104
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
342-445 |
1.33e-10 |
|
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: 58.50 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 342 HYQVKIHFSGTEDGKQHNQaFEISLYGTVAESENIPFTLPEVS--TNKTYSFLIYTEVDIGELLMMKLKWisDSYFSWPD 419
Cdd:cd00113 2 RYTVTIKTGDKKGAGTDSN-ISLALYGENGNSSDIPILDGPGSfeRGSTDTFQIDLKLDIGDITKVYLRR--DGSGLSDG 78
|
90 100
....*....|....*....|....*.
gi 126723006 420 WwsspsfVIERIRVKAGETQKKVIFC 445
Cdd:cd00113 79 W------YCESITVQALGTKKVYTFP 98
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
74-207 |
3.93e-08 |
|
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: 54.05 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 74 KTFVVIHGWTvtGMYESWvPKLVAALYKREPDsnVIVVDWLYRAQ-QHYPVSAGYTKLvgnDVARFINWMEEEFnyPLDN 152
Cdd:pfam00561 1 PPVLLLHGLP--GSSDLW-RKLAPALARDGFR--VIALDLRGFGKsSRPKAQDDYRTD---DLAEDLEYILEAL--GLEK 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 126723006 153 VHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVD 207
Cdd:pfam00561 71 VNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFD 125
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
343-451 |
8.31e-05 |
|
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: 41.97 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 343 YQVKIHFSGTEDGKQHnqaFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKW----ISDSYfswp 418
Cdd:cd01759 3 YKVSVTLSGKKKVTGT---ILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWnnnvINITL---- 75
|
90 100 110
....*....|....*....|....*....|...
gi 126723006 419 dwwssPSFVIERIRVKAGETQKKVIFCAREKVS 451
Cdd:cd01759 76 -----PKVGAEKITVQSGKDGKVFNFCSSETVR 103
|
|
| MhpC |
COG0596 |
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ... |
77-197 |
2.56e-04 |
|
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 223669 [Multi-domain] Cd Length: 282 Bit Score: 42.69 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 77 VVIHGWTVTGMYESWVPKLVAALYKRepdSNVIVVDWlyRAQQHYPVSAGYTKLVGNDVARFINwmeeefNYPLDNVHLL 156
Cdd:COG0596 25 VLLHGFPGSSSVWRPVFKVLPALAAR---YRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------ALGLEKVVLV 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 126723006 157 GYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSR 197
Cdd:COG0596 94 GHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
|
|
|