|
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 ... |
51-485 |
2.87e-177 |
|
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: 505.20 E-value: 2.87e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 51 FNIRTSKDPEQEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQMREKDANVVVVDWLPLAHQL 130
Cdd:TIGR03230 9 FSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 131 YTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSP 210
Cdd:TIGR03230 89 YPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 211 DDADFVDVLHTYTL-SFGLSIGIRMPVGHIDIYPNGGDFQPGCGFND---VIGSFAYGTISEMVKCEHERAVHLFVDSLV 286
Cdd:TIGR03230 169 DDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQEtllVIAEKGLGNMDQLVKCSHERSIHLFIDSLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 287 NQDKPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFKVYHYQLKVHMFSYNNSGDTQP 366
Cdd:TIGR03230 249 NEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 367 TLYITLYGSNADSQNLPLeIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGVAH-SWYNLWNEFRnylsqpsnpsreLY 445
Cdd:TIGR03230 329 PMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------FH 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 188219561 446 IRRIRVKSGETQRKVTFCTQDPTKSSISPGQE-LWFHKCQD 485
Cdd:TIGR03230 396 IRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
49-340 |
1.30e-123 |
|
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: 362.33 E-value: 1.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 49 VAFNIRTSKDPEqEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGmFESWLHKLVSALQMREkDANVVVVDWLPLAH 128
Cdd:cd00707 3 VRFLLYTRENPN-CPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 129 QLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRL 208
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 209 SPDDADFVDVLHTYTLSFglsiGIRMPVGHIDIYPNGGDFQPGCGFNDVIGSFaygtisemVKCEHERAVHLFVDSlVNQ 288
Cdd:cd00707 160 DPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGCPKDILSSDF--------VACSHQRAVHYFAES-ILS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 188219561 289 DKPSFAFQCTDSSRFKRGICLSCRKnRCNNIGYNAKkmRKKRNSKMYLKTRA 340
Cdd:cd00707 227 PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
42-344 |
5.44e-120 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 355.21 E-value: 5.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 42 PATARPS------VAFNIRTSKDPEqeGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQMREkD 115
Cdd:pfam00151 25 PVKSLPWspkdidTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 116 ANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPA 195
Cdd:pfam00151 102 VNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 196 GPMFEGVDINRRLSPDDADFVDVLHTYT-LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFN---DVIGSFAYGTISEMVK 271
Cdd:pfam00151 182 GPYFQGTPEEVRLDPGDADFVDAIHTDTrPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNilsQIIDIDGIWEGTQFVA 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219561 272 CEHERAVHLFVDSLVNQDkPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKRNS---KMYLKTRAGMPF 344
Cdd:pfam00151 262 CNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
347-463 |
1.33e-12 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 63.81 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 347 YHYQLKVHmFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEDLGDLLKMRLTWEgvahswy 424
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNE------- 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 188219561 425 nlwnefrnylsqpsNPSRELYIRRIRVKSGETQRKVTFC 463
Cdd:smart00308 73 --------------HRHPEWFLKSITVKDLPTGGKYHFP 97
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-175 |
1.10e-03 |
|
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: 40.37 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 82 TAKTFFIIHGWTMSGmfESWlHKLVSALQmreKDANVVVVDWL-----PLAHQLYTdavnnTRVVGQRVAGMLDWLQeke 156
Cdd:COG0596 22 DGPPVVLLHGLPGSS--YEW-RPLIPALA---AGYRVIAPDLRghgrsDKPAGGYT-----LDDLADDLAALLDALG--- 87
|
90
....*....|....*....
gi 188219561 157 efsLGNVHLIGYSLGAHVA 175
Cdd:COG0596 88 ---LERVVLVGHSMGGMVA 103
|
|
| |
|
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 ... |
51-485 |
2.87e-177 |
|
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: 505.20 E-value: 2.87e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 51 FNIRTSKDPEQEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQMREKDANVVVVDWLPLAHQL 130
Cdd:TIGR03230 9 FSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 131 YTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSP 210
Cdd:TIGR03230 89 YPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 211 DDADFVDVLHTYTL-SFGLSIGIRMPVGHIDIYPNGGDFQPGCGFND---VIGSFAYGTISEMVKCEHERAVHLFVDSLV 286
Cdd:TIGR03230 169 DDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQEtllVIAEKGLGNMDQLVKCSHERSIHLFIDSLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 287 NQDKPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFKVYHYQLKVHMFSYNNSGDTQP 366
Cdd:TIGR03230 249 NEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTDQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 367 TLYITLYGSNADSQNLPLeIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGVAH-SWYNLWNEFRnylsqpsnpsreLY 445
Cdd:TIGR03230 329 PMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------FH 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 188219561 446 IRRIRVKSGETQRKVTFCTQDPTKSSISPGQE-LWFHKCQD 485
Cdd:TIGR03230 396 IRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
49-340 |
1.30e-123 |
|
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: 362.33 E-value: 1.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 49 VAFNIRTSKDPEqEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGmFESWLHKLVSALQMREkDANVVVVDWLPLAH 128
Cdd:cd00707 3 VRFLLYTRENPN-CPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 129 QLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRL 208
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 209 SPDDADFVDVLHTYTLSFglsiGIRMPVGHIDIYPNGGDFQPGCGFNDVIGSFaygtisemVKCEHERAVHLFVDSlVNQ 288
Cdd:cd00707 160 DPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGCPKDILSSDF--------VACSHQRAVHYFAES-ILS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 188219561 289 DKPSFAFQCTDSSRFKRGICLSCRKnRCNNIGYNAKkmRKKRNSKMYLKTRA 340
Cdd:cd00707 227 PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
42-344 |
5.44e-120 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 355.21 E-value: 5.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 42 PATARPS------VAFNIRTSKDPEqeGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQMREkD 115
Cdd:pfam00151 25 PVKSLPWspkdidTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 116 ANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPA 195
Cdd:pfam00151 102 VNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 196 GPMFEGVDINRRLSPDDADFVDVLHTYT-LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFN---DVIGSFAYGTISEMVK 271
Cdd:pfam00151 182 GPYFQGTPEEVRLDPGDADFVDAIHTDTrPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNilsQIIDIDGIWEGTQFVA 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219561 272 CEHERAVHLFVDSLVNQDkPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKRNS---KMYLKTRAGMPF 344
Cdd:pfam00151 262 CNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
347-483 |
5.81e-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: 211.87 E-value: 5.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 347 YHYQLKVHMFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGVAHSWYNL 426
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 188219561 427 WNEFRNYLSQPSNPSRELYIRRIRVKSGETQRKVTFCTQDPTKSSISPGQELWFHKC 483
Cdd:cd01758 81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
347-483 |
1.19e-39 |
|
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: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 347 YHYQLKVHMFSYNNSgDTQPTLYITLYGSNADSQNLPLEIVEkIELNATNTFLVYTEEDLGDLLKMRLTWEGVAHSWYNL 426
Cdd:cd01755 1 WHYQVKVHLSGKKNL-EVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 188219561 427 WNefrnylsqpsnpSRELYIRRIRVKSGETQRKVTFCTQDPtksSISPGQELWFHKC 483
Cdd:cd01755 79 ET------------LPKLGARKIRVKSGETQKKFTFCSQDT---VRELEVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
136-278 |
3.93e-25 |
|
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238382 [Multi-domain] Cd Length: 153 Bit Score: 101.04 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 136 NNTRVVGQRVAGMLDWLQEK--EEFSLGNVHLIGYSLGAHVAGYAGNFVKGT----VGRITGLDPAGPMFEGVDiNRRLS 209
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSalAQYPDYKIHVTGHSLGGALAGLAGLDLRGRglgrLVRVYTFGPPRVGNAAFA-EDRLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219561 210 PDDADFVDVLHTYT--LSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFN---DVIGSFAYGTISEMVKCEHERAV 278
Cdd:cd00741 80 PSDALFVDRIVNDNdiVPRLPPGGEGYPHGGAEFYINGGKSQPGCCKNvleAVDIDFGNIGLSGNGLCDHLRYF 153
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
349-481 |
7.36e-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: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 349 YQLKVHMFSYNNSGdTQPTLYITLYGSNADSQNLPLEIVEK-IELNATNTFLVYTEEDLGDLLKMRLTWEGvahswynlw 427
Cdd:pfam01477 1 YQVKVVTGDELGAG-TDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDN--------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 188219561 428 nefrnylsqpSNPSRELYIRRIRV-KSGETQRKVTFCTQDPTKSSISPGQELWFH 481
Cdd:pfam01477 71 ----------NGLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
347-463 |
1.33e-12 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 63.81 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 347 YHYQLKVHmFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEDLGDLLKMRLTWEgvahswy 424
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNE------- 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 188219561 425 nlwnefrnylsqpsNPSRELYIRRIRVKSGETQRKVTFC 463
Cdd:smart00308 73 --------------HRHPEWFLKSITVKDLPTGGKYHFP 97
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
347-463 |
3.19e-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: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 347 YHYQLKVHmFSYNNSGDTQPTLYITLYGSNADSQNLP-LEIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGvahswyn 425
Cdd:cd00113 1 CRYTVTIK-TGDKKGAGTDSNISLALYGENGNSSDIPiLDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDG------- 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 188219561 426 lwnefrnylsqpSNPSRELYIRRIRVKSGETQRKVTFC 463
Cdd:cd00113 73 ------------SGLSDGWYCESITVQALGTKKVYTFP 98
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
84-234 |
5.45e-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: 50.97 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 84 KTFFIIHGWTMSGmfESWlHKLVSALQmrEKDANVVVVDWL-------PLAHQLYTDAVnntrvvgqrVAGMLDWLQEKe 156
Cdd:pfam00561 1 PPVLLLHGLPGSS--DLW-RKLAPALA--RDGFRVIALDLRgfgkssrPKAQDDYRTDD---------LAEDLEYILEA- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 157 eFSLGNVHLIGYSLG-AHVAGYAGNFVKGtVGRITGLDPAGPMFEGVDINRRLSPDDADFVD--VLHTYTLSFGLSIGIR 233
Cdd:pfam00561 66 -LGLEKVNLVGHSMGgLIALAYAAKYPDR-VKALVLLGALDPPHELDEADRFILALFPGFFDgfVADFAPNPLGRLVAKL 143
|
.
gi 188219561 234 M 234
Cdd:pfam00561 144 L 144
|
|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
364-424 |
1.30e-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: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219561 364 TQPTLYITLYGSNADSQNLPLEIVEK--IELNATNTFLVYTEEDLGDLLKMRLtW---EGVAHSWY 424
Cdd:cd01752 17 TTAKVTITLYGAEGESEPHHLRDPEKpiFERGSVDSFLLTTPFPLGELQSIRL-WhdnSGLSPSWY 81
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
361-466 |
1.05e-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: 38.89 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 361 SGDTQPTLYITLYGSNADSQNLplEIVE-KIELNATNTFLVYTEEDLGDLLKMRLTWEGvahswyNLWNEFRNYLSQpsn 439
Cdd:cd01759 12 KKKVTGTILVSLYGNKGNTRQY--EIFKgTLKPGNTYSAFIDVDVDVGPLTKVKFIWNN------NVINITLPKVGA--- 80
|
90 100
....*....|....*....|....*..
gi 188219561 440 psrelyiRRIRVKSGETQRKVTFCTQD 466
Cdd:cd01759 81 -------EKITVQSGKDGKVFNFCSSE 100
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-175 |
1.10e-03 |
|
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: 40.37 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219561 82 TAKTFFIIHGWTMSGmfESWlHKLVSALQmreKDANVVVVDWL-----PLAHQLYTdavnnTRVVGQRVAGMLDWLQeke 156
Cdd:COG0596 22 DGPPVVLLHGLPGSS--YEW-RPLIPALA---AGYRVIAPDLRghgrsDKPAGGYT-----LDDLADDLAALLDALG--- 87
|
90
....*....|....*....
gi 188219561 157 efsLGNVHLIGYSLGAHVA 175
Cdd:COG0596 88 ---LERVVLVGHSMGGMVA 103
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
369-414 |
8.23e-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: 8.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 188219561 369 YITLYGSNADSQNLPL---EIVEKIELNATNTFLVYTeEDLGDLLKMRL 414
Cdd:cd01756 22 FITLYGENGDTGKRKLkksNNKNKFERGQTDKFTVEA-VDLGKLKKIRI 69
|
|
| |
