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Conserved domains on  [gi|126313|sp|P11602|]
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RecName: Full=Lipoprotein lipase; Short=LPL; AltName: Full=Phospholipase A1; Flags: Precursor

Protein Classification

lipo_lipase family protein( domain architecture ID 11496507)

lipo_lipase family protein

Graphical summary

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List of domain hits

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 ...
33-473 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: 925.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      33 NFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVD 112
Cdd:TIGR03230   1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     113 WLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYA 192
Cdd:TIGR03230  81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     193 DAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     273 HLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNTKMYLKTRAQMPYKVFHYQVKIHFFGK 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     353 TNVTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSDWWTPFAFTIQRVR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 126313     433 VKSGETQKKVVFCSRDGS-SRLGKGEEAAIFVKCLEQPVSRK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
 
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 ...
33-473 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: 925.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      33 NFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVD 112
Cdd:TIGR03230   1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     113 WLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYA 192
Cdd:TIGR03230  81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     193 DAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     273 HLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNTKMYLKTRAQMPYKVFHYQVKIHFFGK 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     353 TNVTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSDWWTPFAFTIQRVR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 126313     433 VKSGETQKKVVFCSRDGS-SRLGKGEEAAIFVKCLEQPVSRK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
Lipase pfam00151
Lipase;
34-338 2.72e-146

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 421.85  E-value: 2.72e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      34 FEGIESKFSLRTPAEPDEdvCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREpDSNVIVVDW 113
Cdd:pfam00151  33 PKDIDTRFLLYTNENPNN--CQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDW 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     114 LVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYAD 193
Cdd:pfam00151 110 KSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     194 APIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSIH 273
Cdd:pfam00151 190 EEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVH 269
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126313     274 LFIDSLLYEEkPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNT---KMYLKTRAQMPY 338
Cdd:pfam00151 270 YYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
37-334 1.85e-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  Cd Length: 275  Bit Score: 363.87  E-value: 1.85e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313    37 IESKFSLRTPaEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMyESWVPKLVDALYKREpDSNVIVVDWLVR 116
Cdd:cd00707   1 IDVRFLLYTR-ENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   117 AQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPI 196
Cdd:cd00707  78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   197 RLSPDDADFVDVLHTYTRGspdrsIGIQKPVGHIDIYPNGGGFQPGCNLGEALRliaekgfsdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 126313   277 DSLLYeEKPSMAYRCNTKEAFEKGLCLSCRKnRCNNLGYKVNrvRTKRNTKMYLKTRA 334
Cdd:cd00707 222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
341-448 1.75e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 69.21  E-value: 1.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      341 FHYQVKIHFFGKTnVTKVDQPFLISLYGT---LDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEK--DTFF 415
Cdd:smart00308   1 GKYKVTVTTGGLD-FAGTTASVSLSLVGAegdGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHrhPEWF 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 126313      416 swsdwwtpfaftIQRVRVKSGETQKKVVFCSRD 448
Cdd:smart00308  80 ------------LKSITVKDLPTGGKYHFPCNS 100
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
69-197 1.98e-04

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 43.08  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313    69 FNHTSKTFVVIHGWTVTGMYESWVPKlvdALYKREPDSNVIVVDWlvRAQQHYPVSAAYTKLVGKDVAMFIDwmeekfNY 148
Cdd:COG0596  17 AGGGGPPLVLLHGFPGSSSVWRPVFK---VLPALAARYRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------AL 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 126313   149 PLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIR 197
Cdd:COG0596  86 GLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
 
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 ...
33-473 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: 925.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      33 NFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVD 112
Cdd:TIGR03230   1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     113 WLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYA 192
Cdd:TIGR03230  81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     193 DAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     273 HLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNTKMYLKTRAQMPYKVFHYQVKIHFFGK 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     353 TNVTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSDWWTPFAFTIQRVR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 126313     433 VKSGETQKKVVFCSRDGS-SRLGKGEEAAIFVKCLEQPVSRK 473
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSRK 442
Lipase pfam00151
Lipase;
34-338 2.72e-146

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 421.85  E-value: 2.72e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      34 FEGIESKFSLRTPAEPDEdvCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREpDSNVIVVDW 113
Cdd:pfam00151  33 PKDIDTRFLLYTNENPNN--CQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVICVDW 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     114 LVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYAD 193
Cdd:pfam00151 110 KSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYFQGTP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     194 APIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSIH 273
Cdd:pfam00151 190 EEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVH 269
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126313     274 LFIDSLLYEEkPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNT---KMYLKTRAQMPY 338
Cdd:pfam00151 270 YYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
37-334 1.85e-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  Cd Length: 275  Bit Score: 363.87  E-value: 1.85e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313    37 IESKFSLRTPaEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMyESWVPKLVDALYKREpDSNVIVVDWLVR 116
Cdd:cd00707   1 IDVRFLLYTR-ENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   117 AQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPI 196
Cdd:cd00707  78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   197 RLSPDDADFVDVLHTYTRGspdrsIGIQKPVGHIDIYPNGGGFQPGCNLGEALRliaekgfsdvdQLVKCSHERSIHLFI 276
Cdd:cd00707 158 RLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 126313   277 DSLLYeEKPSMAYRCNTKEAFEKGLCLSCRKnRCNNLGYKVNrvRTKRNTKMYLKTRA 334
Cdd:cd00707 222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
341-465 9.32e-70

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: 218.80  E-value: 9.32e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   341 FHYQVKIHFFGKTNVTKVDQPFLISLYGTLDESENIPFTLPEV-SSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFS--- 416
Cdd:cd01758   1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGiTGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSnsw 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 126313   417 --------WSDWWTPFAFTIQRVRVKSGETQKKVVFCSRDGSSRLGKGEEAAIFVKC 465
Cdd:cd01758  81 wtvqtiipWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
PLAT_lipase cd01755
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ...
341-465 6.28e-53

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: 174.41  E-value: 6.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   341 FHYQVKIHFFGKTNvTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSdW 420
Cdd:cd01755   1 WHYQVKVHLSGKKN-LEVDGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNS-G 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 126313   421 WTPFAFTIQRVRVKSGETQKKVVFCSRDGSSRLgkgEEAAIFVKC 465
Cdd:cd01755  79 ETLPKLGARKIRVKSGETQKKFTFCSQDTVREL---EVLQTLVKC 120
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
126-271 8.35e-28

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: 108.36  E-value: 8.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   126 AYTKLVGKDVAMFIDWMEEKF--NYPLNNVHLLGYSLGAHAAGIAGSLTKK----KVNRITGLDPAGPTFeYADAPIRLS 199
Cdd:cd00741   1 KGFYKAARSLANLVLPLLKSAlaQYPDYKIHVTGHSLGGALAGLAGLDLRGrglgRLVRVYTFGPPRVGN-AAFAEDRLD 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126313   200 PDDADFVDVLHTYTRGSPDRS-IGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERS 271
Cdd:cd00741  80 PSDALFVDRIVNDNDIVPRLPpGGEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRY 152
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
343-463 7.49e-21

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 87.49  E-value: 7.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313     343 YQVKIHFfGKTNVTKVDQPFLISLYGTLDESENIPFTL--PEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKdtffswsdW 420
Cdd:pfam01477   1 YQVKVVT-GDELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN--------N 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 126313     421 WTPFAFTIQRVRV-KSGETQKKVVFCSRDGSSRLGKGEEAAIFV 463
Cdd:pfam01477  72 GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
341-448 1.75e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 69.21  E-value: 1.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      341 FHYQVKIHFFGKTnVTKVDQPFLISLYGT---LDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEK--DTFF 415
Cdd:smart00308   1 GKYKVTVTTGGLD-FAGTTASVSLSLVGAegdGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHrhPEWF 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 126313      416 swsdwwtpfaftIQRVRVKSGETQKKVVFCSRD 448
Cdd:smart00308  80 ------------LKSITVKDLPTGGKYHFPCNS 100
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
342-446 1.72e-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: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   342 HYQVKIHFfGKTNVTKVDQPFLISLYGTLDESENIPFTLPEVS--SNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFswsD 419
Cdd:cd00113   2 RYTVTIKT-GDKKGAGTDSNISLALYGENGNSSDIPILDGPGSfeRGSTDTFQIDLKLDIGDITKVYLRRDGSGLS---D 77
                        90       100
                ....*....|....*....|....*..
gi 126313   420 WWTPfaftiQRVRVKSGETQKKVVFCS 446
Cdd:cd00113  78 GWYC-----ESITVQALGTKKVYTFPV 99
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
74-207 3.62e-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: 51.35  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313      74 KTFVVIHGWTvtGMYESWvPKLVDALYKREPDsnVIVVDWlvRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPlnNV 153
Cdd:pfam00561   1 PPVLLLHGLP--GSSDLW-RKLAPALARDGFR--VIALDL--RGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLE--KV 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126313     154 HLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIRLSPDDADFVD 207
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFD 125
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
69-197 1.98e-04

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 43.08  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313    69 FNHTSKTFVVIHGWTVTGMYESWVPKlvdALYKREPDSNVIVVDWlvRAQQHYPVSAAYTKLVGKDVAMFIDwmeekfNY 148
Cdd:COG0596  17 AGGGGPPLVLLHGFPGSSSVWRPVFK---VLPALAARYRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------AL 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 126313   149 PLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIR 197
Cdd:COG0596  86 GLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
343-448 1.61e-03

PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238857  Cd Length: 113  Bit Score: 38.11  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126313   343 YQVKIHFFGKTNVTKVdqpFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSwsdwwT 422
Cdd:cd01759   3 YKVSVTLSGKKKVTGT---ILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWNNNVINI-----T 74
                        90       100
                ....*....|....*....|....*.
gi 126313   423 PFAFTIQRVRVKSGETQKKVVFCSRD 448
Cdd:cd01759  75 LPKVGAEKITVQSGKDGKVFNFCSSE 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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