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Conserved domains on  [gi|194097335|ref|NP_000227.2|]
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hepatic triacylglycerol lipase precursor [Homo sapiens]

Protein Classification

Pancreat_lipase_like and PLAT_LPL domain-containing protein (domain architecture ID 11988341)

Pancreat_lipase_like and PLAT_LPL domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
24-349 2.46e-164

Lipase;


:

Pssm-ID: 278576  Cd Length: 336  Bit Score: 472.70  E-value: 2.46e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   24 GQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ-GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQ 102
Cdd:pfam00151  12 GDKIPWAGNTLVRPVKSLPWSPKDIDTRFLLYTNENPnNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  103 MVAALKSQpaQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIG 182
Cdd:pfam00151  92 MCKALFQV--EDVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  183 GthKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRH 262
Cdd:pfam00151 170 G--KLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  263 IAQHGFNAITQTIKCSHERSVHLFIDSLLHAgTQSMAYPCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSK---RL 339
Cdd:pfam00151 248 IDIDGIWEGTQFVACNHLRSVHYYIDSLLNP-RGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTF 326
                         330
                  ....*....|
gi 194097335  340 FLVTRAQSPF 349
Cdd:pfam00151 327 YLNTGSSSPF 336
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
352-487 7.94e-72

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: 227.66  E-value: 7.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 352 YHYQFKIQFINQTETP-IQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVW 430
Cdd:cd01758    1 FHYQLKIHFFNQTNRIeTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194097335 431 DTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIFVKC 487
Cdd:cd01758   81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
 
Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
24-349 2.46e-164

Lipase;


Pssm-ID: 278576  Cd Length: 336  Bit Score: 472.70  E-value: 2.46e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   24 GQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ-GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQ 102
Cdd:pfam00151  12 GDKIPWAGNTLVRPVKSLPWSPKDIDTRFLLYTNENPnNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  103 MVAALKSQpaQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIG 182
Cdd:pfam00151  92 MCKALFQV--EDVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  183 GthKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRH 262
Cdd:pfam00151 170 G--KLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  263 IAQHGFNAITQTIKCSHERSVHLFIDSLLHAgTQSMAYPCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSK---RL 339
Cdd:pfam00151 248 IDIDGIWEGTQFVACNHLRSVHYYIDSLLNP-RGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTF 326
                         330
                  ....*....|
gi 194097335  340 FLVTRAQSPF 349
Cdd:pfam00151 327 YLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
62-497 2.37e-150

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  Cd Length: 442  Bit Score: 440.87  E-value: 2.37e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   62 CQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAAL-KSQPAQpvNVGLVDWITLAHDHYTIAVRNTRLV 140
Cdd:TIGR03230  22 CYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALyEREPSA--NVIVVDWLSRAQQHYPTSAAYTKLV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  141 GKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIggTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAI 220
Cdd:TIGR03230 100 GKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLT--KHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  221 HTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY 300
Cdd:TIGR03230 178 HTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEENPSMAY 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  301 PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQFKIQFINQT-ETPIQTTFTMSLLGT 379
Cdd:TIGR03230 258 RCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTsLSHTDQPMKISLYGT 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  380 KEKMQKIPITLGKgIASNKTYSFLITLDVDIGELIMIKFKWENSavwanvwdtvqTIIPWSTGPRHSGLVLKTIRVKAGE 459
Cdd:TIGR03230 338 HGEKENIPFTLPE-VSTNKTYSFLITTDVDIGELLMVKLKWEKD-----------TYISWSDWWSSPGFHIRKLRIKSGE 405
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 194097335  460 TQQRMTFCS-ENTDDLLLRPTQEKIFVKCeiKSKTSKRK 497
Cdd:TIGR03230 406 TQSKVIFSAkEGEFSYLQRGGEAAVFVKC--KEKSLSRK 442
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
49-345 3.95e-110

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  Cd Length: 275  Bit Score: 331.52  E-value: 3.95e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  49 KTRFLLFGETNQGC--QIRINHPDTLQECGFNSSLPLVMIIHGWSVDGvLENWIWQMVAALKSQPAqpVNVGLVDWITLA 126
Cdd:cd00707    2 DVRFLLYTRENPNCpqLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRGD--YNVIVVDWGRGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 127 HDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGthKIGRITGLDAAGPLFEGSAPS 206
Cdd:cd00707   79 NPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNG--KLGRITGLDPAGPLFSGADPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 207 NRLSPDDANFVDAIHTFTREhmglsVGIKQPIGHYDFYPNGGSFQPGCHFLelyrhiaqhgfNAITQTIKCSHERSVHLF 286
Cdd:cd00707  157 DRLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPKD-----------ILSSDFVACSHQRAVHYF 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194097335 287 IDSLLhAGTQSMAYPCGDMNSFSQGLCLSCKKGrCNTLGYHVRQEPRSKSkrLFLVTRA 345
Cdd:cd00707  221 AESIL-SPCGFVAYPCSSYDEFLAGKCFPCGSG-CVRMGYHADRFRREGK--FYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
352-487 7.94e-72

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: 227.66  E-value: 7.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 352 YHYQFKIQFINQTETP-IQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVW 430
Cdd:cd01758    1 FHYQLKIHFFNQTNRIeTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194097335 431 DTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIFVKC 487
Cdd:cd01758   81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
352-473 3.67e-21

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608  Cd Length: 105  Bit Score: 89.62  E-value: 3.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   352 YHYQFKIQFINQTETPIQTTFTMSLLGTK-EKMQKIPITLGKGI-ASNKTYSFLITLDVDIGELIMIKFKWENSavwanv 429
Cdd:smart00308   1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEgDGKESKLDYLFKGIfARGSTYEFTFDVDEDFGELGAVKIKNEHR------ 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 194097335   430 wdtvqtiipwstgprHSGLVLKTIRVKAGETQQRMTFCSENTDD 473
Cdd:smart00308  75 ---------------HPEWFLKSITVKDLPTGGKYHFPCNSWVY 103
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
354-485 6.38e-17

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: 307568  Cd Length: 115  Bit Score: 77.86  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  354 YQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKG-IASNKTYSFLITLDVDIGELIMIKFKWENSAvwanvwdt 432
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDNNG-------- 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194097335  433 vqtiipwstgpRHSGLVLKTIRV-KAGETQQRMTFCSENTDDLLLRPTQEKIFV 485
Cdd:pfam01477  73 -----------LSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
 
Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
24-349 2.46e-164

Lipase;


Pssm-ID: 278576  Cd Length: 336  Bit Score: 472.70  E-value: 2.46e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   24 GQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ-GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQ 102
Cdd:pfam00151  12 GDKIPWAGNTLVRPVKSLPWSPKDIDTRFLLYTNENPnNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  103 MVAALKSQpaQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIG 182
Cdd:pfam00151  92 MCKALFQV--EDVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  183 GthKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRH 262
Cdd:pfam00151 170 G--KLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  263 IAQHGFNAITQTIKCSHERSVHLFIDSLLHAgTQSMAYPCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSK---RL 339
Cdd:pfam00151 248 IDIDGIWEGTQFVACNHLRSVHYYIDSLLNP-RGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTF 326
                         330
                  ....*....|
gi 194097335  340 FLVTRAQSPF 349
Cdd:pfam00151 327 YLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
62-497 2.37e-150

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  Cd Length: 442  Bit Score: 440.87  E-value: 2.37e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   62 CQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAAL-KSQPAQpvNVGLVDWITLAHDHYTIAVRNTRLV 140
Cdd:TIGR03230  22 CYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALyEREPSA--NVIVVDWLSRAQQHYPTSAAYTKLV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  141 GKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIggTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAI 220
Cdd:TIGR03230 100 GKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLT--KHKVNRITGLDPAGPTFEYADAPSTLSPDDADFVDVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  221 HTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY 300
Cdd:TIGR03230 178 HTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEENPSMAY 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  301 PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQFKIQFINQT-ETPIQTTFTMSLLGT 379
Cdd:TIGR03230 258 RCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGKTsLSHTDQPMKISLYGT 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  380 KEKMQKIPITLGKgIASNKTYSFLITLDVDIGELIMIKFKWENSavwanvwdtvqTIIPWSTGPRHSGLVLKTIRVKAGE 459
Cdd:TIGR03230 338 HGEKENIPFTLPE-VSTNKTYSFLITTDVDIGELLMVKLKWEKD-----------TYISWSDWWSSPGFHIRKLRIKSGE 405
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 194097335  460 TQQRMTFCS-ENTDDLLLRPTQEKIFVKCeiKSKTSKRK 497
Cdd:TIGR03230 406 TQSKVIFSAkEGEFSYLQRGGEAAVFVKC--KEKSLSRK 442
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
49-345 3.95e-110

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  Cd Length: 275  Bit Score: 331.52  E-value: 3.95e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  49 KTRFLLFGETNQGC--QIRINHPDTLQECGFNSSLPLVMIIHGWSVDGvLENWIWQMVAALKSQPAqpVNVGLVDWITLA 126
Cdd:cd00707    2 DVRFLLYTRENPNCpqLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRGD--YNVIVVDWGRGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 127 HDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGthKIGRITGLDAAGPLFEGSAPS 206
Cdd:cd00707   79 NPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNG--KLGRITGLDPAGPLFSGADPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 207 NRLSPDDANFVDAIHTFTREhmglsVGIKQPIGHYDFYPNGGSFQPGCHFLelyrhiaqhgfNAITQTIKCSHERSVHLF 286
Cdd:cd00707  157 DRLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPKD-----------ILSSDFVACSHQRAVHYF 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194097335 287 IDSLLhAGTQSMAYPCGDMNSFSQGLCLSCKKGrCNTLGYHVRQEPRSKSkrLFLVTRA 345
Cdd:cd00707  221 AESIL-SPCGFVAYPCSSYDEFLAGKCFPCGSG-CVRMGYHADRFRREGK--FYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
352-487 7.94e-72

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: 227.66  E-value: 7.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 352 YHYQFKIQFINQTETP-IQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVW 430
Cdd:cd01758    1 FHYQLKIHFFNQTNRIeTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194097335 431 DTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIFVKC 487
Cdd:cd01758   81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
PLAT_lipase cd01755
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ...
352-487 1.08e-44

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: 155.15  E-value: 1.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 352 YHYQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKgIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVWd 431
Cdd:cd01755    1 WHYQVKVHLSGKKNLEVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSG- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194097335 432 tvqtiipwstgPRHSGLVLKTIRVKAGETQQRMTFCSENTDDlllRPTQEKIFVKC 487
Cdd:cd01755   79 -----------ETLPKLGARKIRVKSGETQKKFTFCSQDTVR---ELEVLQTLVKC 120
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
135-283 1.89e-27

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  Cd Length: 153  Bit Score: 108.36  E-value: 1.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 135 RNTRLVGKEVAALLRWLEES--VQLSRSHVHLIGYSLGAHVSGFAGSSIGGTH--KIGRITGLDAAGPLFEGSAPsNRLS 210
Cdd:cd00741    1 KGFYKAARSLANLVLPLLKSalAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGlgRLVRVYTFGPPRVGNAAFAE-DRLD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194097335 211 PDDANFVDAIHTFTREHMGLS-VGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSV 283
Cdd:cd00741   80 PSDALFVDRIVNDNDIVPRLPpGGEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRYF 153
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
352-484 3.49e-21

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: 90.09  E-value: 3.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 352 YHYQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKG-IASNKTYSFLITLDVDIGELIMIKFKWENSAVWAnvw 430
Cdd:cd00113    1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGsFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSD--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194097335 431 dtvqtiipwstgprhsGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIF 484
Cdd:cd00113   78 ----------------GWYCESITVQALGTKKVYTFPVNRWVLGGKWYTSVRSL 115
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
352-473 3.67e-21

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608  Cd Length: 105  Bit Score: 89.62  E-value: 3.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335   352 YHYQFKIQFINQTETPIQTTFTMSLLGTK-EKMQKIPITLGKGI-ASNKTYSFLITLDVDIGELIMIKFKWENSavwanv 429
Cdd:smart00308   1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEgDGKESKLDYLFKGIfARGSTYEFTFDVDEDFGELGAVKIKNEHR------ 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 194097335   430 wdtvqtiipwstgprHSGLVLKTIRVKAGETQQRMTFCSENTDD 473
Cdd:smart00308  75 ---------------HPEWFLKSITVKDLPTGGKYHFPCNSWVY 103
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
354-485 6.38e-17

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: 307568  Cd Length: 115  Bit Score: 77.86  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335  354 YQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKG-IASNKTYSFLITLDVDIGELIMIKFKWENSAvwanvwdt 432
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDNNG-------- 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194097335  433 vqtiipwstgpRHSGLVLKTIRV-KAGETQQRMTFCSENTDDLLLRPTQEKIFV 485
Cdd:pfam01477  73 -----------LSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
368-471 2.72e-06

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: 46.59  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 368 IQTTFTMSLLGTKEKMQKIPITLGKGIASNkTYSFLITLDVDIGELIMIKFKWENSAVwanvwdtvqtiipwstGPRHSG 447
Cdd:cd01759   15 VTGTILVSLYGNKGNTRQYEIFKGTLKPGN-TYSAFIDVDVDVGPLTKVKFIWNNNVI----------------NITLPK 77
                         90       100
                 ....*....|....*....|....
gi 194097335 448 LVLKTIRVKAGETQQRMTFCSENT 471
Cdd:cd01759   78 VGAEKITVQSGKDGKVFNFCSSET 101
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
214-297 6.20e-03

The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins (Sema3s) are secreted regulator molecules involved in the development of the nervous system, vasculogenesis, angiogenesis,and tumorigenesis. There are 7 distinct subfamilies named Sema3A to 3G. Sema3s function as repellent signals during axon guidance by repelling neurons away from the source of Sema3s. However, Sema3s that are secreted by tumor cells play an inhibitory role in tumor growth and angiogenesis (specifically Sema3B and Sema3F). Sema3s functions by forming complexes with neuropilins and A-type plexins, where neuropilins serve as the ligand binding moiety and the plexins function as signal transduction component. Sema3s primarily inhibit the cell motility and migration of tumor and endothelial cells by inducing collapse of the actin cytoskeleton via neuropilins and plexins. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200500  Cd Length: 471  Bit Score: 38.88  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097335 214 ANFVDAIHTFTREHMglsvgikqpighydfYPNG-GSFQPGCHFLELYRHIAQHGFNAITQTI-----KCS---HERSVH 284
Cdd:cd11239   69 ANFVRVLQPYNRTHL---------------YACGtGAFHPICAFINVGRRLEDPIFKLDDSSLesgrgKCPfdpNQPFAS 133
                         90
                 ....*....|...
gi 194097335 285 LFIDSLLHAGTQS 297
Cdd:cd11239  134 VLIDGELYSGTAI 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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