|
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 ... |
33-473 |
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: 925.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 33 NFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVD 112
Cdd:TIGR03230 1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 113 WLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYA 192
Cdd:TIGR03230 81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 193 DAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 273 HLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNTKMYLKTRAQMPYKVFHYQVKIHFFGK 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 353 TNVTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSDWWTPFAFTIQRVR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 126313 433 VKSGETQKKVVFCSRDGS-SRLGKGEEAAIFVKCLEQPVSRK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
|
|
| Lipase |
pfam00151 |
Lipase; |
34-338 |
2.72e-146 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 421.85 E-value: 2.72e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 34 FEGIESKFSLRTPAEPDEdvCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREpDSNVIVVDW 113
Cdd:pfam00151 33 PKDIDTRFLLYTNENPNN--CQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 114 LVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYAD 193
Cdd:pfam00151 110 KSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 194 APIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSIH 273
Cdd:pfam00151 190 EEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVH 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126313 274 LFIDSLLYEEkPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNT---KMYLKTRAQMPY 338
Cdd:pfam00151 270 YYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
37-334 |
1.85e-124 |
|
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: 363.87 E-value: 1.85e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 37 IESKFSLRTPaEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMyESWVPKLVDALYKREpDSNVIVVDWLVR 116
Cdd:cd00707 1 IDVRFLLYTR-ENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 117 AQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPI 196
Cdd:cd00707 78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 197 RLSPDDADFVDVLHTYTRGspdrsIGIQKPVGHIDIYPNGGGFQPGCNLGEALRliaekgfsdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126313 277 DSLLYeEKPSMAYRCNTKEAFEKGLCLSCRKnRCNNLGYKVNrvRTKRNTKMYLKTRA 334
Cdd:cd00707 222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
341-448 |
1.75e-14 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 69.21 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 341 FHYQVKIHFFGKTnVTKVDQPFLISLYGT---LDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEK--DTFF 415
Cdd:smart00308 1 GKYKVTVTTGGLD-FAGTTASVSLSLVGAegdGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHrhPEWF 79
|
90 100 110
....*....|....*....|....*....|...
gi 126313 416 swsdwwtpfaftIQRVRVKSGETQKKVVFCSRD 448
Cdd:smart00308 80 ------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| MhpC |
COG0596 |
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ... |
69-197 |
1.98e-04 |
|
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 223669 [Multi-domain] Cd Length: 282 Bit Score: 43.08 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 69 FNHTSKTFVVIHGWTVTGMYESWVPKlvdALYKREPDSNVIVVDWlvRAQQHYPVSAAYTKLVGKDVAMFIDwmeekfNY 148
Cdd:COG0596 17 AGGGGPPLVLLHGFPGSSSVWRPVFK---VLPALAARYRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------AL 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 126313 149 PLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIR 197
Cdd:COG0596 86 GLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 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 ... |
33-473 |
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: 925.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 33 NFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVD 112
Cdd:TIGR03230 1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 113 WLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYA 192
Cdd:TIGR03230 81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 193 DAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 273 HLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNTKMYLKTRAQMPYKVFHYQVKIHFFGK 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 353 TNVTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSDWWTPFAFTIQRVR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 126313 433 VKSGETQKKVVFCSRDGS-SRLGKGEEAAIFVKCLEQPVSRK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
|
|
| Lipase |
pfam00151 |
Lipase; |
34-338 |
2.72e-146 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 421.85 E-value: 2.72e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 34 FEGIESKFSLRTPAEPDEdvCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREpDSNVIVVDW 113
Cdd:pfam00151 33 PKDIDTRFLLYTNENPNN--CQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 114 LVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYAD 193
Cdd:pfam00151 110 KSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 194 APIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSIH 273
Cdd:pfam00151 190 EEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVH 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126313 274 LFIDSLLYEEkPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNT---KMYLKTRAQMPY 338
Cdd:pfam00151 270 YYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
37-334 |
1.85e-124 |
|
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: 363.87 E-value: 1.85e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 37 IESKFSLRTPaEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMyESWVPKLVDALYKREpDSNVIVVDWLVR 116
Cdd:cd00707 1 IDVRFLLYTR-ENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 117 AQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPI 196
Cdd:cd00707 78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 197 RLSPDDADFVDVLHTYTRGspdrsIGIQKPVGHIDIYPNGGGFQPGCNLGEALRliaekgfsdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126313 277 DSLLYeEKPSMAYRCNTKEAFEKGLCLSCRKnRCNNLGYKVNrvRTKRNTKMYLKTRA 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 |
9.32e-70 |
|
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: 218.80 E-value: 9.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 341 FHYQVKIHFFGKTNVTKVDQPFLISLYGTLDESENIPFTLPEV-SSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFS--- 416
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGiTGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSnsw 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 126313 417 --------WSDWWTPFAFTIQRVRVKSGETQKKVVFCSRDGSSRLGKGEEAAIFVKC 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 |
6.28e-53 |
|
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: 174.41 E-value: 6.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 341 FHYQVKIHFFGKTNvTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSdW 420
Cdd:cd01755 1 WHYQVKVHLSGKKN-LEVDGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNS-G 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 126313 421 WTPFAFTIQRVRVKSGETQKKVVFCSRDGSSRLgkgEEAAIFVKC 465
Cdd:cd01755 79 ETLPKLGARKIRVKSGETQKKFTFCSQDTVREL---EVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
126-271 |
8.35e-28 |
|
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: 108.36 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 126 AYTKLVGKDVAMFIDWMEEKF--NYPLNNVHLLGYSLGAHAAGIAGSLTKK----KVNRITGLDPAGPTFeYADAPIRLS 199
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSAlaQYPDYKIHVTGHSLGGALAGLAGLDLRGrglgRLVRVYTFGPPRVGN-AAFAEDRLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126313 200 PDDADFVDVLHTYTRGSPDRS-IGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERS 271
Cdd:cd00741 80 PSDALFVDRIVNDNDIVPRLPpGGEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRY 152
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
343-463 |
7.49e-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: 87.49 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 343 YQVKIHFfGKTNVTKVDQPFLISLYGTLDESENIPFTL--PEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKdtffswsdW 420
Cdd:pfam01477 1 YQVKVVT-GDELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN--------N 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 126313 421 WTPFAFTIQRVRV-KSGETQKKVVFCSRDGSSRLGKGEEAAIFV 463
Cdd:pfam01477 72 GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
341-448 |
1.75e-14 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 69.21 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 341 FHYQVKIHFFGKTnVTKVDQPFLISLYGT---LDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEK--DTFF 415
Cdd:smart00308 1 GKYKVTVTTGGLD-FAGTTASVSLSLVGAegdGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHrhPEWF 79
|
90 100 110
....*....|....*....|....*....|...
gi 126313 416 swsdwwtpfaftIQRVRVKSGETQKKVVFCSRD 448
Cdd:smart00308 80 ------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
342-446 |
1.72e-07 |
|
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: 49.64 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 342 HYQVKIHFfGKTNVTKVDQPFLISLYGTLDESENIPFTLPEVS--SNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFswsD 419
Cdd:cd00113 2 RYTVTIKT-GDKKGAGTDSNISLALYGENGNSSDIPILDGPGSfeRGSTDTFQIDLKLDIGDITKVYLRRDGSGLS---D 77
|
90 100
....*....|....*....|....*..
gi 126313 420 WWTPfaftiQRVRVKSGETQKKVVFCS 446
Cdd:cd00113 78 GWYC-----ESITVQALGTKKVYTFPV 99
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
74-207 |
3.62e-07 |
|
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: 51.35 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 74 KTFVVIHGWTvtGMYESWvPKLVDALYKREPDsnVIVVDWlvRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPlnNV 153
Cdd:pfam00561 1 PPVLLLHGLP--GSSDLW-RKLAPALARDGFR--VIALDL--RGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLE--KV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 126313 154 HLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIRLSPDDADFVD 207
Cdd:pfam00561 72 NLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFD 125
|
|
| MhpC |
COG0596 |
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ... |
69-197 |
1.98e-04 |
|
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 223669 [Multi-domain] Cd Length: 282 Bit Score: 43.08 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 69 FNHTSKTFVVIHGWTVTGMYESWVPKlvdALYKREPDSNVIVVDWlvRAQQHYPVSAAYTKLVGKDVAMFIDwmeekfNY 148
Cdd:COG0596 17 AGGGGPPLVLLHGFPGSSSVWRPVFK---VLPALAARYRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------AL 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 126313 149 PLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIR 197
Cdd:COG0596 86 GLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
343-448 |
1.61e-03 |
|
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: 38.11 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313 343 YQVKIHFFGKTNVTKVdqpFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSwsdwwT 422
Cdd:cd01759 3 YKVSVTLSGKKKVTGT---ILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINI-----T 74
|
90 100
....*....|....*....|....*.
gi 126313 423 PFAFTIQRVRVKSGETQKKVVFCSRD 448
Cdd:cd01759 75 LPKVGAEKITVQSGKDGKVFNFCSSE 100
|
|
|