|
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: 912.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 33 DFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230 1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 113 WLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230 81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 273 HLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 353 ESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 126314 433 VKAGETQKKVIFCSREKV-SHLQKGKAPAVFVKCHDKSLNKK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
|
|
| Lipase |
pfam00151 |
Lipase; |
31-338 |
2.37e-169 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 480.02 E-value: 2.37e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 31 RRDFIDIESKFALRTPEDTaeDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREpDSNVIV 110
Cdd:pfam00151 30 PWSPKDIDTRFLLYTNENP--NNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVIC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 111 VDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFE 190
Cdd:pfam00151 107 VDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 191 YAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHER 270
Cdd:pfam00151 187 GTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHLR 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126314 271 SIHLFIDSLLNeENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSS---KMYLKTRSQMPY 338
Cdd:pfam00151 267 SVHYYIDSLLN-PRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
37-334 |
3.19e-128 |
|
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: 373.12 E-value: 3.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 37 IESKFALRTPEDtAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMyESWVPKLVAALYKREpDSNVIVVDWLSR 116
Cdd:cd00707 1 IDVRFLLYTREN-PNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 117 AQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPS 196
Cdd:cd00707 78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 197 RLSPDDADFVDVLHTFtrgspGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRviaerglgdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126314 277 DSLLNeENPSKAYRCSSKEAFEKGLCLSCRKnRCNNLGYEINkvRAKRSSKMYLKTRS 334
Cdd:cd00707 222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
341-452 |
2.21e-19 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 83.07 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 341 FHYQVKIHFSGTESETHTNQaFEISLYGTVA---ESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDsyfsw 417
Cdd:smart00308 1 GKYKVTVTTGGLDFAGTTAS-VSLSLVGAEGdgkESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR----- 74
|
90 100 110
....*....|....*....|....*....|....*
gi 126314 418 sdwwsSPGFAIQKIRVKAGETQKKVIFCSREKVSH 452
Cdd:smart00308 75 -----HPEWFLKSITVKDLPTGGKYHFPCNSWVYP 104
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
74-227 |
6.13e-04 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 41.14 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 74 KTFMVIHGWTVTGmyESWVPkLVAALykrEPDSNVIVVDWLSRAQEHYPvSAGYT-KLVGQDVARFINWMEeefnypLDN 152
Cdd:COG0596 24 PPVVLLHGLPGSS--YEWRP-LIPAL---AAGYRVIAPDLRGHGRSDKP-AGGYTlDDLADDLAALLDALG------LER 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126314 153 VHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPnfEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIG-IQKPV 227
Cdd:COG0596 91 VVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA--ALAEPLRRPGLAPEALAALLRALARTDLRERLArITVPT 164
|
|
| |
|
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: 912.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 33 DFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230 1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 113 WLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230 81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 273 HLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 353 ESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 126314 433 VKAGETQKKVIFCSREKV-SHLQKGKAPAVFVKCHDKSLNKK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
|
|
| Lipase |
pfam00151 |
Lipase; |
31-338 |
2.37e-169 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 480.02 E-value: 2.37e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 31 RRDFIDIESKFALRTPEDTaeDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREpDSNVIV 110
Cdd:pfam00151 30 PWSPKDIDTRFLLYTNENP--NNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVIC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 111 VDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFE 190
Cdd:pfam00151 107 VDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 191 YAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHER 270
Cdd:pfam00151 187 GTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHLR 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126314 271 SIHLFIDSLLNeENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSS---KMYLKTRSQMPY 338
Cdd:pfam00151 267 SVHYYIDSLLN-PRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
37-334 |
3.19e-128 |
|
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: 373.12 E-value: 3.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 37 IESKFALRTPEDtAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMyESWVPKLVAALYKREpDSNVIVVDWLSR 116
Cdd:cd00707 1 IDVRFLLYTREN-PNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 117 AQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPS 196
Cdd:cd00707 78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 197 RLSPDDADFVDVLHTFtrgspGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRviaerglgdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126314 277 DSLLNeENPSKAYRCSSKEAFEKGLCLSCRKnRCNNLGYEINkvRAKRSSKMYLKTRS 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 |
7.08e-68 |
|
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: 213.41 E-value: 7.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 341 FHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVST-NKTYSFLIYTEVDIGELLMLKLKWKSDSYFS--- 416
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITgNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSnsw 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 126314 417 --------WSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKC 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 |
6.69e-51 |
|
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: 168.63 E-value: 6.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 341 FHYQVKIHFSGtESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSdW 420
Cdd:cd01755 1 WHYQVKVHLSG-KKNLEVDGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNS-G 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 126314 421 WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLqkgKAPAVFVKC 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 |
7.04e-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: 7.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 127 YTKLVGQDVARFINWMEEEF--NYPLDNVHLLGYSLGAHAAGIAGSLTNK----KVNRITGLDPAGPNFEyAEAPSRLSP 200
Cdd:cd00741 2 GFYKAARSLANLVLPLLKSAlaQYPDYKIHVTGHSLGGALAGLAGLDLRGrglgRLVRVYTFGPPRVGNA-AFAEDRLDP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126314 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 |
4.37e-22 |
|
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: 90.95 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 343 YQVKIHfSGTESETHTNQAFEISLYGTVAESENIPFTL--PEVSTNKTYSFLIYTEVDIGELLMLKLKWKSdsyfswsdW 420
Cdd:pfam01477 1 YQVKVV-TGDELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN--------N 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 126314 421 WSSPGFAIQKIRV-KAGETQKKVIFCSREKVSHLQKGKAPAVFV 463
Cdd:pfam01477 72 GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
341-452 |
2.21e-19 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 83.07 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 341 FHYQVKIHFSGTESETHTNQaFEISLYGTVA---ESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDsyfsw 417
Cdd:smart00308 1 GKYKVTVTTGGLDFAGTTAS-VSLSLVGAEGdgkESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR----- 74
|
90 100 110
....*....|....*....|....*....|....*
gi 126314 418 sdwwsSPGFAIQKIRVKAGETQKKVIFCSREKVSH 452
Cdd:smart00308 75 -----HPEWFLKSITVKDLPTGGKYHFPCNSWVYP 104
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
342-452 |
2.41e-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: 51.96 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 342 HYQVKIHFSGtESETHTNQAFEISLYGTVAESENIPFTLPEVS--TNKTYSFLIYTEVDIGELLMLKLKWKSDSyfswsd 419
Cdd:cd00113 2 RYTVTIKTGD-KKGAGTDSNISLALYGENGNSSDIPILDGPGSfeRGSTDTFQIDLKLDIGDITKVYLRRDGSG------ 74
|
90 100 110
....*....|....*....|....*....|...
gi 126314 420 wwSSPGFAIQKIRVKAGETQKKVIFCSREKVSH 452
Cdd:cd00113 75 --LSDGWYCESITVQALGTKKVYTFPVNRWVLG 105
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
74-207 |
1.71e-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: 52.12 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 74 KTFMVIHGWTvtGMYESWvPKLVAALYKREPDsnVIVVDWL-------SRAQEHYPVSagytklvgqDVARFINWMEEEF 146
Cdd:pfam00561 1 PPVLLLHGLP--GSSDLW-RKLAPALARDGFR--VIALDLRgfgkssrPKAQDDYRTD---------DLAEDLEYILEAL 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126314 147 nyPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVD 207
Cdd:pfam00561 67 --GLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFD 125
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
343-451 |
4.36e-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: 42.74 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 343 YQVKIHFSGTESETHTnqaFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSwsdwwS 422
Cdd:cd01759 3 YKVSVTLSGKKKVTGT---ILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINI-----T 74
|
90 100
....*....|....*....|....*....
gi 126314 423 SPGFAIQKIRVKAGETQKKVIFCSREKVS 451
Cdd:cd01759 75 LPKVGAEKITVQSGKDGKVFNFCSSETVR 103
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
74-227 |
6.13e-04 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 41.14 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 74 KTFMVIHGWTVTGmyESWVPkLVAALykrEPDSNVIVVDWLSRAQEHYPvSAGYT-KLVGQDVARFINWMEeefnypLDN 152
Cdd:COG0596 24 PPVVLLHGLPGSS--YEWRP-LIPAL---AAGYRVIAPDLRGHGRSDKP-AGGYTlDDLADDLAALLDALG------LER 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126314 153 VHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPnfEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIG-IQKPV 227
Cdd:COG0596 91 VVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA--ALAEPLRRPGLAPEALAALLRALARTDLRERLArITVPT 164
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
78-185 |
7.49e-04 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 40.76 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 78 VIHGWTVT-GMYESWVPKLVAALYkrepdsNVIVVDWL-----SRAQEHYPvsaGYTKLVgQDVARFINWMEEEFNYPld 151
Cdd:COG2267 33 LVHGLGEHsGRYAELAEALAAAGY------AVLAFDLRghgrsDGPRGHVD---SFDDYV-DDLRAALDALRARPGLP-- 100
|
90 100 110
....*....|....*....|....*....|....
gi 126314 152 nVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPA 185
Cdd:COG2267 101 -VVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
75-182 |
4.86e-03 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 38.32 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126314 75 TFMVIHG--WtVTGMYESWVPklVAALYKREPDSNVIVVDWlSRAQEH-YPVSAgytklvgQDVARFINWMEE---EFNY 148
Cdd:COG0657 15 VVVYFHGggW-VSGSKDTHDP--LARRLAARAGAAVVSVDY-RLAPEHpFPAAL-------EDAYAALRWLRAnaaELGI 83
|
90 100 110
....*....|....*....|....*....|....*
gi 126314 149 PLDNVHLLGYSLGAH-AAGIAGSLTNKKVNRITGL 182
Cdd:COG0657 84 DPDRIAVAGDSAGGHlAAALALRARDRGGPRPAAQ 118
|
|
| |
