|
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 ... |
50-411 |
6.51e-125 |
|
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: 368.84 E-value: 6.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 50 RFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQ 129
Cdd:TIGR03230 8 KFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 130 LYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITA------------------ 191
Cdd:TIGR03230 88 HYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGldpagptfeyadapstls 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 192 ------------------------------------------------------------ITEVVKCEHERAVHLFVDSL 211
Cdd:TIGR03230 168 pddadfvdvlhtntrgspdrsigiqrpvghidiypnggtfqpgcdiqetllviaekglgnMDQLVKCSHERSIHLFIDSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 212 VNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIE 291
Cdd:TIGR03230 248 LNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 292 PTFYVTLYGTNADSQTLPLeIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQ-SWYNLWKEFRsylsqprnpgreL 370
Cdd:TIGR03230 328 QPMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------F 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 808175995 371 NIRRIRVKSGETQRKLTFCTEDPENTSISPGRE-LWFRKCRD 411
Cdd:TIGR03230 395 HIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
273-409 |
1.81e-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: 233.82 E-value: 1.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 273 YHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNL 352
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808175995 353 WKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKC 409
Cdd:cd01758 81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
|
|
| Lipase |
pfam00151 |
Lipase; |
12-270 |
2.46e-72 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 230.41 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 12 SLCY----CFaaGSPVPFGPEGRLEDKLHKPKATQtevKPSVRFNLRTSKDPEheGCYLSVGHSQPLEDCSFNMTAKTFF 87
Cdd:pfam00151 2 EVCYgqlgCF--GDKIPWAGNTLVRPVKSLPWSPK---DIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 88 IIHGWTMSGIFENWLHKLVSALHTREkDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIG 167
Cdd:pfam00151 75 IIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 168 YSLGAHVAGYAGNFVKGTVGRITA-------------------------------------------------------- 191
Cdd:pfam00151 154 HSLGAHVAGEAGRRTNGKLGRITGldpagpyfqgtpeevrldpgdadfvdaihtdtrpipglgfgisqpvghvdffpngg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 192 ----------------------ITEVVKCEHERAVHLFVDSLVNQDkPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNA 249
Cdd:pfam00151 234 seqpgcqknilsqiididgiweGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYA 312
|
330 340
....*....|....*....|....
gi 808175995 250 KKMRNKRNS---KMYLKTRAGMPF 270
Cdd:pfam00151 313 DKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
273-392 |
1.14e-09 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 55.34 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 273 YHYQMKIHvFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVER--IEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWY 350
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHRHPEWF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 808175995 351 nlwkefrsylsqprnpgrelnIRRIRVKSGETQRKLTFCTED 392
Cdd:smart00308 80 ---------------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-197 |
2.95e-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: 41.91 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 82 TAKTFFIIHGWTMSGifENWlHKLVSALhtrEKDANVVVVDWL-----PLAHQLYTdavnntrvvghsIARMLDWLQEK- 155
Cdd:COG0596 22 DGPPVVLLHGLPGSS--YEW-RPLIPAL---AAGYRVIAPDLRghgrsDKPAGGYT------------LDDLADDLAALl 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 808175995 156 DDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITAITEVVK 197
Cdd:COG0596 84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA 125
|
|
| |
|
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 ... |
50-411 |
6.51e-125 |
|
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: 368.84 E-value: 6.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 50 RFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQ 129
Cdd:TIGR03230 8 KFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 130 LYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITA------------------ 191
Cdd:TIGR03230 88 HYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGldpagptfeyadapstls 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 192 ------------------------------------------------------------ITEVVKCEHERAVHLFVDSL 211
Cdd:TIGR03230 168 pddadfvdvlhtntrgspdrsigiqrpvghidiypnggtfqpgcdiqetllviaekglgnMDQLVKCSHERSIHLFIDSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 212 VNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIE 291
Cdd:TIGR03230 248 LNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTSLSHTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 292 PTFYVTLYGTNADSQTLPLeIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQ-SWYNLWKEFRsylsqprnpgreL 370
Cdd:TIGR03230 328 QPMKISLYGTHGEKENIPF-TLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiSWSDWWSSPG------------F 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 808175995 371 NIRRIRVKSGETQRKLTFCTEDPENTSISPGRE-LWFRKCRD 411
Cdd:TIGR03230 395 HIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEaAVFVKCKE 436
|
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
273-409 |
1.81e-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: 233.82 E-value: 1.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 273 YHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNL 352
Cdd:cd01758 1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808175995 353 WKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKC 409
Cdd:cd01758 81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
49-266 |
2.04e-74 |
|
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: 233.67 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 49 VRFNLRTSKDPEHeGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGiFENWLHKLVSALHTREkDANVVVVDWLPLAH 128
Cdd:cd00707 3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 129 QLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITA----------------- 191
Cdd:cd00707 80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGldpagplfsgadpedrl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 192 ---------------------------------------------ITEVVKCEHERAVHLFVDSlVNQDKPSFAFQCTDS 226
Cdd:cd00707 160 dpsdaqfvdvihtdggllgfsqpighadfypnggrdqpgcpkdilSSDFVACSHQRAVHYFAES-ILSPCGFVAYPCSSY 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 808175995 227 NRFKKGICLSCRKnRCNSIGYNAKkmRNKRNSKMYLKTRA 266
Cdd:cd00707 239 DEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
|
|
| Lipase |
pfam00151 |
Lipase; |
12-270 |
2.46e-72 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 230.41 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 12 SLCY----CFaaGSPVPFGPEGRLEDKLHKPKATQtevKPSVRFNLRTSKDPEheGCYLSVGHSQPLEDCSFNMTAKTFF 87
Cdd:pfam00151 2 EVCYgqlgCF--GDKIPWAGNTLVRPVKSLPWSPK---DIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 88 IIHGWTMSGIFENWLHKLVSALHTREkDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIG 167
Cdd:pfam00151 75 IIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 168 YSLGAHVAGYAGNFVKGTVGRITA-------------------------------------------------------- 191
Cdd:pfam00151 154 HSLGAHVAGEAGRRTNGKLGRITGldpagpyfqgtpeevrldpgdadfvdaihtdtrpipglgfgisqpvghvdffpngg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 192 ----------------------ITEVVKCEHERAVHLFVDSLVNQDkPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNA 249
Cdd:pfam00151 234 seqpgcqknilsqiididgiweGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYA 312
|
330 340
....*....|....*....|....
gi 808175995 250 KKMRNKRNS---KMYLKTRAGMPF 270
Cdd:pfam00151 313 DKFPGKTSKleqTFYLNTGSSSPF 336
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
273-409 |
9.82e-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: 151.29 E-value: 9.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 273 YHYQMKIHVFSYKNMgEIEPTFYVTLYGTNADSQTLPLEIVErIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNL 352
Cdd:cd01755 1 WHYQVKVHLSGKKNL-EVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808175995 353 WkefrsylsqprnPGRELNIRRIRVKSGETQRKLTFCTEDPENTSispGRELWFRKC 409
Cdd:cd01755 79 E------------TLPKLGARKIRVKSGETQKKFTFCSQDTVREL---EVLQTLVKC 120
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
275-407 |
2.94e-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: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 275 YQMKIHvFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVE-RIEQNATNTFLVYTEEDLGDLLKIQLTWEGAsqswynlw 353
Cdd:pfam01477 1 YQVKVV-TGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNN-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 808175995 354 kefrsylsqprNPGRELNIRRIRV-KSGETQRKLTFCTEDPENTSISPGRELWFR 407
Cdd:pfam01477 72 -----------GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
273-392 |
1.14e-09 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 55.34 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 273 YHYQMKIHvFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVER--IEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWY 350
Cdd:smart00308 1 GKYKVTVT-TGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHRHPEWF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 808175995 351 nlwkefrsylsqprnpgrelnIRRIRVKSGETQRKLTFCTED 392
Cdd:smart00308 80 ---------------------LKSITVKDLPTGGKYHFPCNS 100
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
136-193 |
9.41e-08 |
|
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: 51.35 E-value: 9.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808175995 136 NNTRVVGHSIARMLDWLQEK--DDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVG--RITAIT 193
Cdd:cd00741 1 KGFYKAARSLANLVLPLLKSalAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGLgrLVRVYT 62
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
273-392 |
1.57e-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: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 273 YHYQMKIHVFSYKNMGeIEPTFYVTLYGTNADSQTLP-LEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWE--GASQSW 349
Cdd:cd00113 1 CRYTVTIKTGDKKGAG-TDSNISLALYGENGNSSDIPiLDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDgsGLSDGW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 808175995 350 YnlwkefrsylsqprnpgrelnIRRIRVKSGETQRKLTFCTED 392
Cdd:cd00113 80 Y---------------------CESITVQALGTKKVYTFPVNR 101
|
|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
295-350 |
4.77e-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: 4.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808175995 295 YVTLYGTNADSQTLPLEIVER--IEQNATNTFLVYTEEDLGDLLKIQLtW---EGASQSWY 350
Cdd:cd01752 22 TITLYGAEGESEPHHLRDPEKpiFERGSVDSFLLTTPFPLGELQSIRL-WhdnSGLSPSWY 81
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
84-193 |
1.99e-05 |
|
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: 45.57 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 84 KTFFIIHGWTMSGifENWlHKLVSALhtREKDANVVVVDWLplAHQLYTDAVNNTRVVGHSIARMLDWLQEKddFSLGNV 163
Cdd:pfam00561 1 PPVLLLHGLPGSS--DLW-RKLAPAL--ARDGFRVIALDLR--GFGKSSRPKAQDDYRTDDLAEDLEYILEA--LGLEKV 71
|
90 100 110
....*....|....*....|....*....|.
gi 808175995 164 HLIGYSLG-AHVAGYAGNFVKgtvgRITAIT 193
Cdd:pfam00561 72 NLVGHSMGgLIALAYAAKYPD----RVKALV 98
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-197 |
2.95e-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: 41.91 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 82 TAKTFFIIHGWTMSGifENWlHKLVSALhtrEKDANVVVVDWL-----PLAHQLYTdavnntrvvghsIARMLDWLQEK- 155
Cdd:COG0596 22 DGPPVVLLHGLPGSS--YEW-RPLIPAL---AAGYRVIAPDLRghgrsDKPAGGYT------------LDDLADDLAALl 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 808175995 156 DDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITAITEVVK 197
Cdd:COG0596 84 DALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA 125
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
293-392 |
3.83e-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: 39.66 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808175995 293 TFYVTLYGTNADSQTLplEIVER-IEQNATNTFLVYTEEDLGDLLKIQLTWEgasQSWYNLwkefrsylSQPRnpgreLN 371
Cdd:cd01759 18 TILVSLYGNKGNTRQY--EIFKGtLKPGNTYSAFIDVDVDVGPLTKVKFIWN---NNVINI--------TLPK-----VG 79
|
90 100
....*....|....*....|.
gi 808175995 372 IRRIRVKSGETQRKLTFCTED 392
Cdd:cd01759 80 AEKITVQSGKDGKVFNFCSSE 100
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
295-350 |
2.18e-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: 37.92 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808175995 295 YVTLYGTNADSQTLPLEIVERI---EQNATNTFLVYTeEDLGDLLKIQLTWEGA--SQSWY 350
Cdd:cd01756 22 FITLYGENGDTGKRKLKKSNNKnkfERGQTDKFTVEA-VDLGKLKKIRIGHDNSglGAGWF 81
|
|
| |
