|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase super family |
cl37967 |
Lipase; |
300-498 |
1.24e-103 |
|
Lipase;
The actual alignment was detected with superfamily member pfam00151:
Pssm-ID: 395099 Cd Length: 336 Bit Score: 317.08 E-value: 1.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTPG-LGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPmIPYLGFG 378
Cdd:pfam00151 140 NELNYSPSNVHLIGHSLGAHVAGEAGRRTNGkLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRP-IPGLGFG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISQIVDIDGIWEGTRdFAACNHLRSYKYYSDSILNPEGFLGYSCTNEAMFESGQC 458
Cdd:pfam00151 219 ISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKC 297
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1878426127 459 FPCTSSSpCPFMGHHADKFKVHNGAEKLKFYLNTGDSLPF 498
Cdd:pfam00151 298 LPCPKGG-CPQMGHYADKFPGKTSKLEQTFYLNTGSSSPF 336
|
|
| PLAT super family |
cl00011 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
501-613 |
8.23e-54 |
|
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.
The actual alignment was detected with superfamily member cd01759:
Pssm-ID: 412108 Cd Length: 113 Bit Score: 179.10 E-value: 8.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGSNTNRGYFKVALYGVNGNTRQYEIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNILNPLLPKFGA 580
Cdd:cd01759 1 WRYKVSVTLSGKKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
|
90 100 110
....*....|....*....|....*....|...
gi 1878426127 581 TQITVERGRDQKTFKFCGNEKVRENVLQTLSSC 613
Cdd:cd01759 81 EKITVQSGKDGKVFNFCSSETVRENVLQTLTPC 113
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
68-124 |
1.87e-29 |
|
Homeodomain;
:
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 110.28 E-value: 1.87e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1878426127 68 RRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRK 124
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| OAR |
pfam03826 |
OAR motif; The entry represents the OAR motif. |
258-275 |
1.02e-05 |
|
OAR motif; The entry represents the OAR motif.
:
Pssm-ID: 461067 Cd Length: 19 Bit Score: 42.40 E-value: 1.02e-05
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase |
pfam00151 |
Lipase; |
300-498 |
1.24e-103 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 317.08 E-value: 1.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTPG-LGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPmIPYLGFG 378
Cdd:pfam00151 140 NELNYSPSNVHLIGHSLGAHVAGEAGRRTNGkLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRP-IPGLGFG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISQIVDIDGIWEGTRdFAACNHLRSYKYYSDSILNPEGFLGYSCTNEAMFESGQC 458
Cdd:pfam00151 219 ISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKC 297
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1878426127 459 FPCTSSSpCPFMGHHADKFKVHNGAEKLKFYLNTGDSLPF 498
Cdd:pfam00151 298 LPCPKGG-CPQMGHYADKFPGKTSKLEQTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
300-494 |
8.46e-83 |
|
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: 261.02 E-value: 8.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTPG-LGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPmipylgFG 378
Cdd:cd00707 105 DNTGLSLENVHLIGHSLGAHVAGFAGKRLNGkLGRITGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGL------LG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISqivdidgiwegtRDFAACNHLRSYKYYSDSILNPEGFLGYSCTNEAMFESGQC 458
Cdd:cd00707 179 FSQPIGHADFYPNGGRDQPGCPKDILS------------SDFVACSHQRAVHYFAESILSPCGFVAYPCSSYDEFLAGKC 246
|
170 180 190
....*....|....*....|....*....|....*.
gi 1878426127 459 FPCtsSSPCPFMGHHADKFKvHNGaeklKFYLNTGD 494
Cdd:cd00707 247 FPC--GSGCVRMGYHADRFR-REG----KFYLKTNA 275
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
501-613 |
8.23e-54 |
|
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: 179.10 E-value: 8.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGSNTNRGYFKVALYGVNGNTRQYEIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNILNPLLPKFGA 580
Cdd:cd01759 1 WRYKVSVTLSGKKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
|
90 100 110
....*....|....*....|....*....|...
gi 1878426127 581 TQITVERGRDQKTFKFCGNEKVRENVLQTLSSC 613
Cdd:cd01759 81 EKITVQSGKDGKVFNFCSSETVRENVLQTLTPC 113
|
|
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
300-602 |
1.26e-42 |
|
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: 159.29 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTP-GLGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPMiPYLGFG 378
Cdd:TIGR03230 112 EEFNYPWDNVHLLGYSLGAHVAGIAGSLTKhKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRGS-PDRSIG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISQIVDIDGIwEGTRDFAACNHLRSYKYYSDSILNPEG-FLGYSCTNEAMFESGQ 457
Cdd:TIGR03230 191 IQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGL-GNMDQLVKCSHERSIHLFIDSLLNEENpSMAYRCSSKEAFNKGL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 458 CFPCTSSSpCPFMGHHADKFKVHNGAeklKFYLNTGDSLPFSRYRYRVTVTIDG----SNTNRGyFKVALYGVNGNTRQY 533
Cdd:TIGR03230 270 CLSCRKNR-CNKLGYEINKVRTKRSS---KMYLKTREMMPYKVFHYQVKVHFFGktslSHTDQP-MKISLYGTHGEKENI 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878426127 534 EIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNIL-------NPllPKFGATQITVERGRDQKTFKFCGNEKV 602
Cdd:TIGR03230 345 PFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiswsdwwSS--PGFHIRKLRIKSGETQSKVIFSAKEGE 418
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
68-124 |
1.87e-29 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 110.28 E-value: 1.87e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1878426127 68 RRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRK 124
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
68-126 |
4.66e-25 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 98.08 E-value: 4.66e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1878426127 68 RRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRE 126
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
67-123 |
5.10e-25 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 98.09 E-value: 5.10e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1878426127 67 QRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWR 123
Cdd:smart00389 1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
503-604 |
5.10e-14 |
|
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: 68.61 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 503 YRVTVT---IDGSNTNrGYFKVALYGVNGNTRQYEIHK--GTLSPGKTYKLLIDVETEVDELTHVKFIWNNnilNPLLPK 577
Cdd:pfam01477 1 YQVKVVtgdELGAGTD-ADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN---NGLSDE 76
|
90 100
....*....|....*....|....*...
gi 1878426127 578 FGATQITVER-GRDQKTFKFCGNEKVRE 604
Cdd:pfam01477 77 WFLKSITVEVpGETGGKYTFPCNSWVYG 104
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
501-605 |
3.51e-13 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 65.74 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGS--NTNRGYFKVALYG---VNGNTRQYEIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNilnplL 575
Cdd:smart00308 1 GKYKVTVTTGGLdfAGTTASVSLSLVGaegDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR-----H 75
|
90 100 110
....*....|....*....|....*....|
gi 1878426127 576 PKFGATQITVERGRDQKTFKFCGNEKVREN 605
Cdd:smart00308 76 PEWFLKSITVKDLPTGGKYHFPCNSWVYPD 105
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
38-124 |
5.00e-13 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 67.08 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 38 KGQDNSDTEKSHQNQTDESNLEDGSLKKKQRRQRThfTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKN 117
Cdd:COG5576 24 KTTKNKREVEAADSEMKLERKQDGSSPPKSKRRRT--TDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQN 101
|
....*..
gi 1878426127 118 RRAKWRK 124
Cdd:COG5576 102 KRAKEKK 108
|
|
| OAR |
pfam03826 |
OAR motif; The entry represents the OAR motif. |
258-275 |
1.02e-05 |
|
OAR motif; The entry represents the OAR motif.
Pssm-ID: 461067 Cd Length: 19 Bit Score: 42.40 E-value: 1.02e-05
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase |
pfam00151 |
Lipase; |
300-498 |
1.24e-103 |
|
Lipase;
Pssm-ID: 395099 Cd Length: 336 Bit Score: 317.08 E-value: 1.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTPG-LGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPmIPYLGFG 378
Cdd:pfam00151 140 NELNYSPSNVHLIGHSLGAHVAGEAGRRTNGkLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRP-IPGLGFG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISQIVDIDGIWEGTRdFAACNHLRSYKYYSDSILNPEGFLGYSCTNEAMFESGQC 458
Cdd:pfam00151 219 ISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQ-FVACNHLRSVHYYIDSLLNPRGFPGYPCSSYDAFSQNKC 297
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1878426127 459 FPCTSSSpCPFMGHHADKFKVHNGAEKLKFYLNTGDSLPF 498
Cdd:pfam00151 298 LPCPKGG-CPQMGHYADKFPGKTSKLEQTFYLNTGSSSPF 336
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
300-494 |
8.46e-83 |
|
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: 261.02 E-value: 8.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTPG-LGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPmipylgFG 378
Cdd:cd00707 105 DNTGLSLENVHLIGHSLGAHVAGFAGKRLNGkLGRITGLDPAGPLFSGADPEDRLDPSDAQFVDVIHTDGGL------LG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISqivdidgiwegtRDFAACNHLRSYKYYSDSILNPEGFLGYSCTNEAMFESGQC 458
Cdd:cd00707 179 FSQPIGHADFYPNGGRDQPGCPKDILS------------SDFVACSHQRAVHYFAESILSPCGFVAYPCSSYDEFLAGKC 246
|
170 180 190
....*....|....*....|....*....|....*.
gi 1878426127 459 FPCtsSSPCPFMGHHADKFKvHNGaeklKFYLNTGD 494
Cdd:cd00707 247 FPC--GSGCVRMGYHADRFR-REG----KFYLKTNA 275
|
|
| PLAT_PL |
cd01759 |
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ... |
501-613 |
8.23e-54 |
|
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: 179.10 E-value: 8.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGSNTNRGYFKVALYGVNGNTRQYEIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNILNPLLPKFGA 580
Cdd:cd01759 1 WRYKVSVTLSGKKKVTGTILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINITLPKVGA 80
|
90 100 110
....*....|....*....|....*....|...
gi 1878426127 581 TQITVERGRDQKTFKFCGNEKVRENVLQTLSSC 613
Cdd:cd01759 81 EKITVQSGKDGKVFNFCSSETVRENVLQTLTPC 113
|
|
| lipo_lipase |
TIGR03230 |
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ... |
300-602 |
1.26e-42 |
|
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: 159.29 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 300 ESFQQSPENVHIIGHSLGSHLAAEAGRRTP-GLGRITGLDPAEPYFQGCPILVRLDPSDALFVDVIHSDALPMiPYLGFG 378
Cdd:TIGR03230 112 EEFNYPWDNVHLLGYSLGAHVAGIAGSLTKhKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVLHTNTRGS-PDRSIG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 379 MSQAVGHLDFYPNGGESMPGCEKNLISQIVDIDGIwEGTRDFAACNHLRSYKYYSDSILNPEG-FLGYSCTNEAMFESGQ 457
Cdd:TIGR03230 191 IQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGL-GNMDQLVKCSHERSIHLFIDSLLNEENpSMAYRCSSKEAFNKGL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 458 CFPCTSSSpCPFMGHHADKFKVHNGAeklKFYLNTGDSLPFSRYRYRVTVTIDG----SNTNRGyFKVALYGVNGNTRQY 533
Cdd:TIGR03230 270 CLSCRKNR-CNKLGYEINKVRTKRSS---KMYLKTREMMPYKVFHYQVKVHFFGktslSHTDQP-MKISLYGTHGEKENI 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878426127 534 EIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNIL-------NPllPKFGATQITVERGRDQKTFKFCGNEKV 602
Cdd:TIGR03230 345 PFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYiswsdwwSS--PGFHIRKLRIKSGETQSKVIFSAKEGE 418
|
|
| PLAT_lipase |
cd01755 |
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ... |
501-613 |
2.15e-36 |
|
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: 132.03 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGSNTNR--GYFKVALYGVNGNTRQYEIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNILNPL---- 574
Cdd:cd01755 1 WHYQVKVHLSGKKNLEvdGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNsget 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1878426127 575 LPKFGATQITVERGRDQKTFKFCGNEKVRE-NVLQTLSSC 613
Cdd:cd01755 81 LPKLGARKIRVKSGETQKKFTFCSQDTVRElEVLQTLVKC 120
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
303-429 |
5.40e-30 |
|
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: 115.29 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 303 QQSPENVHIIGHSLGSHLAAEAGRR-----TPGLGRITGLDPAEPYFQGCPiLVRLDPSDALFVDVIH--SDALPMIPyl 375
Cdd:cd00741 24 QYPDYKIHVTGHSLGGALAGLAGLDlrgrgLGRLVRVYTFGPPRVGNAAFA-EDRLDPSDALFVDRIVndNDIVPRLP-- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1878426127 376 GFGMSQAVGHLDFYPNGGESMPGCEKNLISQiVDIDGIWEGTRDFAACNHLRSY 429
Cdd:cd00741 101 PGGEGYPHGGAEFYINGGKSQPGCCKNVLEA-VDIDFGNIGLSGNGLCDHLRYF 153
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
68-124 |
1.87e-29 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 110.28 E-value: 1.87e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1878426127 68 RRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRK 124
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
68-126 |
4.66e-25 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 98.08 E-value: 4.66e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1878426127 68 RRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRE 126
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
67-123 |
5.10e-25 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 98.09 E-value: 5.10e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1878426127 67 QRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWR 123
Cdd:smart00389 1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
501-610 |
2.20e-14 |
|
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: 69.68 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTV-TID--GSNTnRGYFKVALYGVNGNTRQYEIHKGTLS--PGKTYKLLIDVETEVDELTHVKFIWNNNILNpll 575
Cdd:cd00113 1 CRYTVTIkTGDkkGAGT-DSNISLALYGENGNSSDIPILDGPGSfeRGSTDTFQIDLKLDIGDITKVYLRRDGSGLS--- 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1878426127 576 PKFGATQITVERGRDQKTFKFCGNEKVRENVLQTL 610
Cdd:cd00113 77 DGWYCESITVQALGTKKVYTFPVNRWVLGGKWYTS 111
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
503-604 |
5.10e-14 |
|
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: 68.61 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 503 YRVTVT---IDGSNTNrGYFKVALYGVNGNTRQYEIHK--GTLSPGKTYKLLIDVETEVDELTHVKFIWNNnilNPLLPK 577
Cdd:pfam01477 1 YQVKVVtgdELGAGTD-ADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN---NGLSDE 76
|
90 100
....*....|....*....|....*...
gi 1878426127 578 FGATQITVER-GRDQKTFKFCGNEKVRE 604
Cdd:pfam01477 77 WFLKSITVEVpGETGGKYTFPCNSWVYG 104
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
501-605 |
3.51e-13 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 65.74 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGS--NTNRGYFKVALYG---VNGNTRQYEIHKGTLSPGKTYKLLIDVETEVDELTHVKFIWNNNilnplL 575
Cdd:smart00308 1 GKYKVTVTTGGLdfAGTTASVSLSLVGaegDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR-----H 75
|
90 100 110
....*....|....*....|....*....|
gi 1878426127 576 PKFGATQITVERGRDQKTFKFCGNEKVREN 605
Cdd:smart00308 76 PEWFLKSITVKDLPTGGKYHFPCNSWVYPD 105
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
38-124 |
5.00e-13 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 67.08 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 38 KGQDNSDTEKSHQNQTDESNLEDGSLKKKQRRQRThfTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKN 117
Cdd:COG5576 24 KTTKNKREVEAADSEMKLERKQDGSSPPKSKRRRT--TDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQN 101
|
....*..
gi 1878426127 118 RRAKWRK 124
Cdd:COG5576 102 KRAKEKK 108
|
|
| OAR |
pfam03826 |
OAR motif; The entry represents the OAR motif. |
258-275 |
1.02e-05 |
|
OAR motif; The entry represents the OAR motif.
Pssm-ID: 461067 Cd Length: 19 Bit Score: 42.40 E-value: 1.02e-05
|
| PLAT_LPL |
cd01758 |
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ... |
501-597 |
2.58e-03 |
|
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: 38.53 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426127 501 YRYRVTVTIDGSnTNRGY----FKVALYGVNGNTRQYEIHKGTLSPG-KTYKLLIDVETEVDELTHVKFIWNNN--ILNP 573
Cdd:cd01758 1 FHYQLKIHFFNQ-TNRIEtdptFTISLYGTLGESENLPLTLPEGITGnKTNSFLITTEKDIGDLLMLKLKWEGSslWSNS 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1878426127 574 LLPKFGAT--------------QITVERGRDQKTFKFC 597
Cdd:cd01758 80 WWTVQTIIpwsgwwrgsgltirKIRVKAGETQKKMTFC 117
|
|
| |
