|
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 ... |
50-485 |
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: 517.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 50 RFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQ 129
Cdd:TIGR03230 8 KFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 130 LYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLS 209
Cdd:TIGR03230 88 HYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 210 PDDADFVDVLHTYTR-SFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIA---YGTITEVVKCEHERAVHLFVDSL 285
Cdd:TIGR03230 168 PDDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAekgLGNMDQLVKCSHERSIHLFIDSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 286 VNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIE 365
Cdd:TIGR03230 248 LNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 366 PTFYVTLYGTNADSQTLPLeIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQ-SWYNLWKEFRsylsqprnpgreL 444
Cdd:TIGR03230 328 QPMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------F 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 5174497 445 NIRRIRVKSGETQRKLTFCTEDPENTSISPGRE-LWFRKCRD 485
Cdd:TIGR03230 395 HIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
49-340 |
9.29e-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 [Multi-domain] Cd Length: 275 Bit Score: 362.72 E-value: 9.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 49 VRFNLRTSKDPEHeGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGiFENWLHKLVSALHTREkDANVVVVDWLPLAH 128
Cdd:cd00707 3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 129 QLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRL 208
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 209 SPDDADFVDVLHTYTRSFglsiGIQMPVGHIDIYPNGGDFQPGCGLNDVlgsiaygtITEVVKCEHERAVHLFVDSlVNQ 288
Cdd:cd00707 160 DPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGCPKDIL--------SSDFVACSHQRAVHYFAES-ILS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 5174497 289 DKPSFAFQCTDSNRFKKGICLSCRKnRCNSIGYNAKkmRNKRNSKMYLKTRA 340
Cdd:cd00707 227 PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
12-344 |
8.06e-123 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 362.53 E-value: 8.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 12 SLCY----CFaaGSPVPFGPEGRLEDKLHKPKATQtevKPSVRFNLRTSKDPEheGCYLSVGHSQPLEDCSFNMTAKTFF 87
Cdd:pfam00151 2 EVCYgqlgCF--GDKIPWAGNTLVRPVKSLPWSPK---DIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 88 IIHGWTMSGIFENWLHKLVSALHTREkDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIG 167
Cdd:pfam00151 75 IIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 168 YSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTR-SFGLSIGIQMPVGHIDIYPNGG 246
Cdd:pfam00151 154 HSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRpIPGLGFGISQPVGHVDFFPNGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 247 DFQPGCGLNDVLGSIAYGTITEV---VKCEHERAVHLFVDSLVNQDkPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNA 323
Cdd:pfam00151 234 SEQPGCQKNILSQIIDIDGIWEGtqfVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYA 312
|
330 340
....*....|....*....|....
gi 5174497 324 KKMRNKRNS---KMYLKTRAGMPF 344
Cdd:pfam00151 313 DKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
347-466 |
1.33e-09 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 55.34 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 347 YHYQMKIHvFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVER--IEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWY 424
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHRHPEWF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 5174497 425 nlwkefrsylsqprnpgrelnIRRIRVKSGETQRKLTFCTED 466
Cdd:smart00308 80 ---------------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-236 |
7.32e-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: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 82 TAKTFFIIHGWTMSGifENWlHKLVSALhtrEKDANVVVVDWL-----PLAHQLYTdavnntrvvghsIARMLDWLQEK- 155
Cdd:COG0596 22 DGPPVVLLHGLPGSS--YEW-RPLIPAL---AAGYRVIAPDLRghgrsDKPAGGYT------------LDDLADDLAALl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 156 DDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFegADIHKRLSPDDADFVDVLHTYTRSFGLSI--GIQ 233
Cdd:COG0596 84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAAL--AEPLRRPGLAPEALAALLRALARTDLRERlaRIT 161
|
...
gi 5174497 234 MPV 236
Cdd:COG0596 162 VPT 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 ... |
50-485 |
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: 517.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 50 RFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQ 129
Cdd:TIGR03230 8 KFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 130 LYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLS 209
Cdd:TIGR03230 88 HYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYADAPSTLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 210 PDDADFVDVLHTYTR-SFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIA---YGTITEVVKCEHERAVHLFVDSL 285
Cdd:TIGR03230 168 PDDADFVDVLHTNTRgSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAekgLGNMDQLVKCSHERSIHLFIDSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 286 VNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIE 365
Cdd:TIGR03230 248 LNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 366 PTFYVTLYGTNADSQTLPLeIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQ-SWYNLWKEFRsylsqprnpgreL 444
Cdd:TIGR03230 328 QPMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------F 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 5174497 445 NIRRIRVKSGETQRKLTFCTEDPENTSISPGRE-LWFRKCRD 485
Cdd:TIGR03230 395 HIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
49-340 |
9.29e-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 [Multi-domain] Cd Length: 275 Bit Score: 362.72 E-value: 9.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 49 VRFNLRTSKDPEHeGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGiFENWLHKLVSALHTREkDANVVVVDWLPLAH 128
Cdd:cd00707 3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 129 QLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRL 208
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPEDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 209 SPDDADFVDVLHTYTRSFglsiGIQMPVGHIDIYPNGGDFQPGCGLNDVlgsiaygtITEVVKCEHERAVHLFVDSlVNQ 288
Cdd:cd00707 160 DPSDAQFVDVIHTDGGLL----GFSQPIGHADFYPNGGRDQPGCPKDIL--------SSDFVACSHQRAVHYFAES-ILS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 5174497 289 DKPSFAFQCTDSNRFKKGICLSCRKnRCNSIGYNAKkmRNKRNSKMYLKTRA 340
Cdd:cd00707 227 PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
12-344 |
8.06e-123 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 362.53 E-value: 8.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 12 SLCY----CFaaGSPVPFGPEGRLEDKLHKPKATQtevKPSVRFNLRTSKDPEheGCYLSVGHSQPLEDCSFNMTAKTFF 87
Cdd:pfam00151 2 EVCYgqlgCF--GDKIPWAGNTLVRPVKSLPWSPK---DIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 88 IIHGWTMSGIFENWLHKLVSALHTREkDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIG 167
Cdd:pfam00151 75 IIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 168 YSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTR-SFGLSIGIQMPVGHIDIYPNGG 246
Cdd:pfam00151 154 HSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRpIPGLGFGISQPVGHVDFFPNGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 247 DFQPGCGLNDVLGSIAYGTITEV---VKCEHERAVHLFVDSLVNQDkPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNA 323
Cdd:pfam00151 234 SEQPGCQKNILSQIIDIDGIWEGtqfVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYA 312
|
330 340
....*....|....*....|....
gi 5174497 324 KKMRNKRNS---KMYLKTRAGMPF 344
Cdd:pfam00151 313 DKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
347-483 |
1.37e-76 |
|
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: 236.52 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 347 YHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNL 426
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 5174497 427 WKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKC 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 |
9.47e-45 |
|
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: 153.22 E-value: 9.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 347 YHYQMKIHVFSYKNMgEIEPTFYVTLYGTNADSQTLPLEIVErIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNL 426
Cdd:cd01755 1 WHYQVKVHLSGKKNL-EVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 5174497 427 WkefrsylsqprnPGRELNIRRIRVKSGETQRKLTFCTEDPENTSispGRELWFRKC 483
Cdd:cd01755 79 E------------TLPKLGARKIRVKSGETQKKFTFCSQDTVREL---EVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
136-278 |
2.19e-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: 101.81 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 136 NNTRVVGHSIARMLDWLQEK--DDFSLGNVHLIGYSLGAHVAGYAGNFVKGT----VGRITGLDPAGPMFEGADIhKRLS 209
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSalAQYPDYKIHVTGHSLGGALAGLAGLDLRGRglgrLVRVYTFGPPRVGNAAFAE-DRLD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174497 210 PDDADFVDVLHTYTRSFGL--SIGIQMPVGHIDIYPNGGDFQPGC---GLNDVLGSIAYGTITEVVKCEHERAV 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 |
3.72e-18 |
|
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: 80.17 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 349 YQMKIHvFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVE-RIEQNATNTFLVYTEEDLGDLLKIQLTWEGAsqswynlw 427
Cdd:pfam01477 1 YQVKVV-TGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNN-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 5174497 428 kefrsylsqprNPGRELNIRRIRV-KSGETQRKLTFCTEDPENTSISPGRELWFR 481
Cdd:pfam01477 72 -----------GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
347-466 |
1.33e-09 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 55.34 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 347 YHYQMKIHvFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVER--IEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWY 424
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHRHPEWF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 5174497 425 nlwkefrsylsqprnpgrelnIRRIRVKSGETQRKLTFCTED 466
Cdd:smart00308 80 ---------------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
347-466 |
1.68e-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: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 347 YHYQMKIHVFSYKNMGeIEPTFYVTLYGTNADSQTLP-LEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWE--GASQSW 423
Cdd:cd00113 1 CRYTVTIKTGDKKGAG-TDSNISLALYGENGNSSDIPiLDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDgsGLSDGW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 5174497 424 YnlwkefrsylsqprnpgrelnIRRIRVKSGETQRKLTFCTED 466
Cdd:cd00113 80 Y---------------------CESITVQALGTKKVYTFPVNR 101
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
84-234 |
6.86e-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: 50.58 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 84 KTFFIIHGWTMSGifENWlHKLVSALhtREKDANVVVVDWLplAHQLYTDAVNNTRVVGHSIARMLDWLQEKddFSLGNV 163
Cdd:pfam00561 1 PPVLLLHGLPGSS--DLW-RKLAPAL--ARDGFRVIALDLR--GFGKSSRPKAQDDYRTDDLAEDLEYILEA--LGLEKV 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174497 164 HLIGYSLG-AHVAGYAGNFVKGtVGRITGLDPAGPMFEGADIHKRLSPDDADFVD--VLHTYTRSFGLSIGIQM 234
Cdd:pfam00561 72 NLVGHSMGgLIALAYAAKYPDR-VKALVLLGALDPPHELDEADRFILALFPGFFDgfVADFAPNPLGRLVAKLL 144
|
|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
369-424 |
5.41e-06 |
|
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: 45.34 E-value: 5.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174497 369 YVTLYGTNADSQTLPLEIVER--IEQNATNTFLVYTEEDLGDLLKIQLtW---EGASQSWY 424
Cdd:cd01752 22 TITLYGAEGESEPHHLRDPEKpiFERGSVDSFLLTTPFPLGELQSIRL-WhdnSGLSPSWY 81
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
367-466 |
4.02e-04 |
|
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.
Pssm-ID: 238857 Cd Length: 113 Bit Score: 40.04 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 367 TFYVTLYGTNADSQTLplEIVER-IEQNATNTFLVYTEEDLGDLLKIQLTWEgasQSWYNLwkefrsylSQPRnpgreLN 445
Cdd:cd01759 18 TILVSLYGNKGNTRQY--EIFKGtLKPGNTYSAFIDVDVDVGPLTKVKFIWN---NNVINI--------TLPK-----VG 79
|
90 100
....*....|....*....|.
gi 5174497 446 IRRIRVKSGETQRKLTFCTED 466
Cdd:cd01759 80 AEKITVQSGKDGKVFNFCSSE 100
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-236 |
7.32e-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: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 82 TAKTFFIIHGWTMSGifENWlHKLVSALhtrEKDANVVVVDWL-----PLAHQLYTdavnntrvvghsIARMLDWLQEK- 155
Cdd:COG0596 22 DGPPVVLLHGLPGSS--YEW-RPLIPAL---AAGYRVIAPDLRghgrsDKPAGGYT------------LDDLADDLAALl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174497 156 DDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFegADIHKRLSPDDADFVDVLHTYTRSFGLSI--GIQ 233
Cdd:COG0596 84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAAL--AEPLRRPGLAPEALAALLRALARTDLRERlaRIT 161
|
...
gi 5174497 234 MPV 236
Cdd:COG0596 162 VPT 164
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
369-424 |
2.82e-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: 37.53 E-value: 2.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174497 369 YVTLYGTNADSQTLPLEIVERI---EQNATNTFLVYTeEDLGDLLKIQLTWEGA--SQSWY 424
Cdd:cd01756 22 FITLYGENGDTGKRKLKKSNNKnkfERGQTDKFTVEA-VDLGKLKKIRIGHDNSglGAGWF 81
|
|
| |
