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Conserved domains on  [gi|569008080|ref|XP_006527530|]
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lipase member M isoform X3 [Mus musculus]

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
1-218 7.08e-11

triacylglycerol lipase


The actual alignment was detected with superfamily member PLN02872:

Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 61.04  E-value: 7.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080   1 MGFIAFsTMPELAHKIKMYFALAPIATVKYARSPGTK---FLLLPDMMIKVlfgrqeFLYQTRFFRQLFIYLcgqmiLDQ 77
Cdd:PLN02872 173 MSLAAL-TQPNVVEMVEAAALLCPISYLDHVTAPLVLrmvFMHLDQMVVAM------GIHQLNFRSDVLVKL-----LDS 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080  78 ICSNIIL---LLGGFNTNN--MNMSRANVYVAHTPAGTSVQNILHWSQAVNSGELRAFDWGSeTKNQEKCNQPTPIRYKV 152
Cdd:PLN02872 241 ICEGHMDcndLLTSITGTNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYGQVNPPAFDL 319
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008080 153 RDMMVPTAMWTG--GQDWLSNPDDVKTLLSEVTN---LIYHKNipeWAHVDFIWGLDAPQRVYNEIIHLMK 218
Cdd:PLN02872 320 SLIPKSLPLWMGygGTDGLADVTDVEHTLAELPSkpeLLYLEN---YGHIDFLLSTSAKEDVYNHMIQFFR 387
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
1-218 7.08e-11

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 61.04  E-value: 7.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080   1 MGFIAFsTMPELAHKIKMYFALAPIATVKYARSPGTK---FLLLPDMMIKVlfgrqeFLYQTRFFRQLFIYLcgqmiLDQ 77
Cdd:PLN02872 173 MSLAAL-TQPNVVEMVEAAALLCPISYLDHVTAPLVLrmvFMHLDQMVVAM------GIHQLNFRSDVLVKL-----LDS 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080  78 ICSNIIL---LLGGFNTNN--MNMSRANVYVAHTPAGTSVQNILHWSQAVNSGELRAFDWGSeTKNQEKCNQPTPIRYKV 152
Cdd:PLN02872 241 ICEGHMDcndLLTSITGTNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYGQVNPPAFDL 319
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008080 153 RDMMVPTAMWTG--GQDWLSNPDDVKTLLSEVTN---LIYHKNipeWAHVDFIWGLDAPQRVYNEIIHLMK 218
Cdd:PLN02872 320 SLIPKSLPLWMGygGTDGLADVTDVEHTLAELPSkpeLLYLEN---YGHIDFLLSTSAKEDVYNHMIQFFR 387
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
2-202 1.02e-03

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: 39.02  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080    2 GFIAFSTMPELAHKIKMYFALAPIatvkyarSPGTKFLLLPDMMIKVLFGRQEFLYQTRFFRQLFIYLCGQMILDQICSN 81
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080   82 IILLLGGFNtnnMNMSRANVYVAHTPAGTSVQNILHWSQAVNSGELRAFDWgsetknqekcnqptpirykvrdmmvPTAM 161
Cdd:pfam00561 153 LLKALPLLN---KRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDE-------------------------PTLI 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 569008080  162 WTGGQDWLsNPDDVKTLLSEVTNLIYHKNIPEWAHVDFIWG 202
Cdd:pfam00561 205 IWGDQDPL-VPPQALEKLAQLFPNARLVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
1-218 7.08e-11

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 61.04  E-value: 7.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080   1 MGFIAFsTMPELAHKIKMYFALAPIATVKYARSPGTK---FLLLPDMMIKVlfgrqeFLYQTRFFRQLFIYLcgqmiLDQ 77
Cdd:PLN02872 173 MSLAAL-TQPNVVEMVEAAALLCPISYLDHVTAPLVLrmvFMHLDQMVVAM------GIHQLNFRSDVLVKL-----LDS 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080  78 ICSNIIL---LLGGFNTNN--MNMSRANVYVAHTPAGTSVQNILHWSQAVNSGELRAFDWGSeTKNQEKCNQPTPIRYKV 152
Cdd:PLN02872 241 ICEGHMDcndLLTSITGTNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYGQVNPPAFDL 319
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569008080 153 RDMMVPTAMWTG--GQDWLSNPDDVKTLLSEVTN---LIYHKNipeWAHVDFIWGLDAPQRVYNEIIHLMK 218
Cdd:PLN02872 320 SLIPKSLPLWMGygGTDGLADVTDVEHTLAELPSkpeLLYLEN---YGHIDFLLSTSAKEDVYNHMIQFFR 387
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
2-202 1.02e-03

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: 39.02  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080    2 GFIAFSTMPELAHKIKMYFALAPIatvkyarSPGTKFLLLPDMMIKVLFGRQEFLYQTRFFRQLFIYLCGQMILDQICSN 81
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAL-------DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569008080   82 IILLLGGFNtnnMNMSRANVYVAHTPAGTSVQNILHWSQAVNSGELRAFDWgsetknqekcnqptpirykvrdmmvPTAM 161
Cdd:pfam00561 153 LLKALPLLN---KRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDE-------------------------PTLI 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 569008080  162 WTGGQDWLsNPDDVKTLLSEVTNLIYHKNIPEWAHVDFIWG 202
Cdd:pfam00561 205 IWGDQDPL-VPPQALEKLAQLFPNARLVVIPDAGHFAFLEG 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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