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Conserved domains on  [gi|530393096|ref|XP_005269599|]
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lipase member J isoform X4 [Homo sapiens]

Protein Classification

lipase family protein( domain architecture ID 706631)

lipase family protein that may function as a lipase, catalyzing the hydrolysis of ester bonds of insoluble substrates such a triglycerides

EC:  3.1.1.-
Gene Ontology:  GO:0016298|GO:0016788|GO:0006629

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02872 super family cl28691
triacylglycerol lipase
1-246 9.19e-16

triacylglycerol lipase


The actual alignment was detected with superfamily member PLN02872:

Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 75.67  E-value: 9.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096   1 MAKYDLPASIDFtVKQTRQEEIFYVGHSQGTTIGFITFsTISKIAERIKIFFALAPVFSTKYLKSPLI-RMTY-KWKSIV 78
Cdd:PLN02872 142 LALYDLAEMIHY-VYSITNSKIFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHVTAPLVlRMVFmHLDQMV 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096  79 MAFSgnkdfLPKTSFKKFIGSKLcplqiFDKIC---LNILFMMFGYDPKN--LNMSRLDVYFSHNPAGTSVQNMLHWSQL 153
Cdd:PLN02872 220 VAMG-----IHQLNFRSDVLVKL-----LDSICeghMDCNDLLTSITGTNccFNASRIDYYLEYEPHPSSVKNLRHLFQM 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096 154 LNSTHLKAYDWGSPDlNLVHYNQTTSPLYNMTNMNVATAIW--NGKSDLLADPEDVNILHSEITNHIYYKTISYYNHIDS 231
Cdd:PLN02872 290 IRKGTFAHYDYGIFK-NLKLYGQVNPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELPSKPELLYLENYGHIDF 368
                        250
                 ....*....|....*
gi 530393096 232 LFGLDVYDQVYHEII 246
Cdd:PLN02872 369 LLSTSAKEDVYNHMI 383
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
1-246 9.19e-16

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 75.67  E-value: 9.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096   1 MAKYDLPASIDFtVKQTRQEEIFYVGHSQGTTIGFITFsTISKIAERIKIFFALAPVFSTKYLKSPLI-RMTY-KWKSIV 78
Cdd:PLN02872 142 LALYDLAEMIHY-VYSITNSKIFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHVTAPLVlRMVFmHLDQMV 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096  79 MAFSgnkdfLPKTSFKKFIGSKLcplqiFDKIC---LNILFMMFGYDPKN--LNMSRLDVYFSHNPAGTSVQNMLHWSQL 153
Cdd:PLN02872 220 VAMG-----IHQLNFRSDVLVKL-----LDSICeghMDCNDLLTSITGTNccFNASRIDYYLEYEPHPSSVKNLRHLFQM 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096 154 LNSTHLKAYDWGSPDlNLVHYNQTTSPLYNMTNMNVATAIW--NGKSDLLADPEDVNILHSEITNHIYYKTISYYNHIDS 231
Cdd:PLN02872 290 IRKGTFAHYDYGIFK-NLKLYGQVNPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELPSKPELLYLENYGHIDF 368
                        250
                 ....*....|....*
gi 530393096 232 LFGLDVYDQVYHEII 246
Cdd:PLN02872 369 LLSTSAKEDVYNHMI 383
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
1-234 1.73e-04

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: 41.72  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096    1 MAKYDLPASIDFTVKQTRQEEIFYVGHSQGTTIGFITFstiSKIAERIKIFFALAPVfstkylkSPLIRMTYKWKSIVMA 80
Cdd:pfam00561  50 YRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYA---AKYPDRVKALVLLGAL-------DPPHELDEADRFILAL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096   81 FSGNKDFLPKTSFKKFIGSKLCPLQIFDKICLNILFMMfgyDPKNLNMSRLDVYFSHNPAGTSVQNMLHWSQLLNSthlK 160
Cdd:pfam00561 120 FPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL---PLLNKRFPSGDYALAKSLVTGALLFIETWSTELRA---K 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530393096  161 AYDWGSPDlnlvhynqttsplynmtnmnvaTAIWNGKSDLLADPEDVNILHsEITNHIYYKTISYYNHIDSLFG 234
Cdd:pfam00561 194 FLGRLDEP----------------------TLIIWGDQDPLVPPQALEKLA-QLFPNARLVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
1-246 9.19e-16

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 75.67  E-value: 9.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096   1 MAKYDLPASIDFtVKQTRQEEIFYVGHSQGTTIGFITFsTISKIAERIKIFFALAPVFSTKYLKSPLI-RMTY-KWKSIV 78
Cdd:PLN02872 142 LALYDLAEMIHY-VYSITNSKIFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHVTAPLVlRMVFmHLDQMV 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096  79 MAFSgnkdfLPKTSFKKFIGSKLcplqiFDKIC---LNILFMMFGYDPKN--LNMSRLDVYFSHNPAGTSVQNMLHWSQL 153
Cdd:PLN02872 220 VAMG-----IHQLNFRSDVLVKL-----LDSICeghMDCNDLLTSITGTNccFNASRIDYYLEYEPHPSSVKNLRHLFQM 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096 154 LNSTHLKAYDWGSPDlNLVHYNQTTSPLYNMTNMNVATAIW--NGKSDLLADPEDVNILHSEITNHIYYKTISYYNHIDS 231
Cdd:PLN02872 290 IRKGTFAHYDYGIFK-NLKLYGQVNPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELPSKPELLYLENYGHIDF 368
                        250
                 ....*....|....*
gi 530393096 232 LFGLDVYDQVYHEII 246
Cdd:PLN02872 369 LLSTSAKEDVYNHMI 383
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
1-234 1.73e-04

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: 41.72  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096    1 MAKYDLPASIDFTVKQTRQEEIFYVGHSQGTTIGFITFstiSKIAERIKIFFALAPVfstkylkSPLIRMTYKWKSIVMA 80
Cdd:pfam00561  50 YRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYA---AKYPDRVKALVLLGAL-------DPPHELDEADRFILAL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530393096   81 FSGNKDFLPKTSFKKFIGSKLCPLQIFDKICLNILFMMfgyDPKNLNMSRLDVYFSHNPAGTSVQNMLHWSQLLNSthlK 160
Cdd:pfam00561 120 FPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL---PLLNKRFPSGDYALAKSLVTGALLFIETWSTELRA---K 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530393096  161 AYDWGSPDlnlvhynqttsplynmtnmnvaTAIWNGKSDLLADPEDVNILHsEITNHIYYKTISYYNHIDSLFG 234
Cdd:pfam00561 194 FLGRLDEP----------------------TLIIWGDQDPLVPPQALEKLA-QLFPNARLVVIPDAGHFAFLEG 244
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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