NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|311771512|ref|NP_001185759|]
View 

gastric triacylglycerol lipase isoform 4 precursor [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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02872 super family cl28691
triacylglycerol lipase
14-367 7.91e-43

triacylglycerol lipase


The actual alignment was detected with superfamily member PLN02872:

Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 153.48  E-value: 7.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  14 LLTMASLISVLGTTHGLFGKLHPGSPEVTMnISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNT--------- 84
Cdd:PLN02872   3 VLISLFISTSAGGVLTGQSNLLRRSPVESL-CAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLGSQrgppvllqh 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  85 -----------------------DAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQK 141
Cdd:PLN02872  82 glfmagdawflnspeqslgfilaDHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQELALYDLAEMIHYVYSITNSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512 142 qLHYVGHSQGTTIGFIAFsTNPSLAKRIKTFYALAPVATVKY-TKSLInkLRFVPQSLFKFIFGDKIfYPHNFFDQFLAT 220
Cdd:PLN02872 162 -IFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHvTAPLV--LRMVFMHLDQMVVAMGI-HQLNFRSDVLVK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512 221 EVCSREMLNLLCSNALFIICGfdsKN--FNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSpVQNRMHYDQS 298
Cdd:PLN02872 237 LLDSICEGHMDCNDLLTSITG---TNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYGQV 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311771512 299 QPPYYNVTAMNVPIAVW--NGGKDLLADPQDVGLLLPKL---PNLIYHKEipfYNHLDFIWAMDAPQEVYNDIV 367
Cdd:PLN02872 313 NPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELpskPELLYLEN---YGHIDFLLSTSAKEDVYNHMI 383
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
14-367 7.91e-43

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 153.48  E-value: 7.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  14 LLTMASLISVLGTTHGLFGKLHPGSPEVTMnISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNT--------- 84
Cdd:PLN02872   3 VLISLFISTSAGGVLTGQSNLLRRSPVESL-CAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLGSQrgppvllqh 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  85 -----------------------DAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQK 141
Cdd:PLN02872  82 glfmagdawflnspeqslgfilaDHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQELALYDLAEMIHYVYSITNSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512 142 qLHYVGHSQGTTIGFIAFsTNPSLAKRIKTFYALAPVATVKY-TKSLInkLRFVPQSLFKFIFGDKIfYPHNFFDQFLAT 220
Cdd:PLN02872 162 -IFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHvTAPLV--LRMVFMHLDQMVVAMGI-HQLNFRSDVLVK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512 221 EVCSREMLNLLCSNALFIICGfdsKN--FNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSpVQNRMHYDQS 298
Cdd:PLN02872 237 LLDSICEGHMDCNDLLTSITG---TNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYGQV 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311771512 299 QPPYYNVTAMNVPIAVW--NGGKDLLADPQDVGLLLPKL---PNLIYHKEipfYNHLDFIWAMDAPQEVYNDIV 367
Cdd:PLN02872 313 NPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELpskPELLYLEN---YGHIDFLLSTSAKEDVYNHMI 383
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
85-354 8.04e-18

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: 81.78  E-value: 8.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512   85 DAGYDVWLGNSRGNTWARRNLYYSpdsvefwAFSFDEMAKYdlpatIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPS 164
Cdd:pfam00561  25 RDGFRVIALDLRGFGKSSRPKAQD-------DYRTDDLAED-----LEYILEALGLEKVNLVGHSMGGLIALAYAAKYPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  165 lakRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSRemLNLLCSNALFiicgfdS 244
Cdd:pfam00561  93 ---RVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLR--LRLLKALPLL------N 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  245 KNFntSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWgspvqnrmhydqsqppyynvtamnvPIAVWNGGKDLLAD 324
Cdd:pfam00561 162 KRF--PSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDE-------------------------PTLIIWGDQDPLVP 214
                         250       260       270
                  ....*....|....*....|....*....|
gi 311771512  325 PQDVGLLLPKLPNLIYHKEIPFYnHLDFIW 354
Cdd:pfam00561 215 PQALEKLAQLFPNARLVVIPDAG-HFAFLE 243
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
117-172 7.34e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.02  E-value: 7.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311771512 117 FSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGttiGFIA-FSTNPSLAKRIKTF 172
Cdd:COG4757   83 AGYRDWGELDLPAVLDALRARFPGLPLLLVGHSLG---GQLLgLAPNAERVDRLVTV 136
CYCLIN_CLBs_yeast_rpt1 cd20568
first cyclin box found in yeast B-type cyclins; This subfamily includes Saccharomyces ...
189-243 4.61e-03

first cyclin box found in yeast B-type cyclins; This subfamily includes Saccharomyces cerevisiae G2/mitotic-specific cyclins 1-4 (ScCLB1-4), S-phase entry cyclins 5-6 (ScCLB5-6), and Schizosaccharomyces pombe G2/mitotic-specific cyclins, cig1, cig2 and cdc13. ScCLB1-4 are essential for the control of the cell cycle at the G2/M (mitosis) transition. They interact with the CDC2 protein kinase to form maturation promoting factor (MPF). ScCLB5-6 interact with CDC28 and are involved in DNA replication in Saccharomyces cerevisiae. ScCLB5 is required for efficient progression through S phase and possibly for the normal progression through meiosis. ScCLB6 is involved in G1/S and or S phase progression. Cig1 is required for efficient passage of the G1/S transition. Cig2 and cdc13 are essential for the control of the cell cycle at the G2/M and G1/S (mitosis) transitions. They interact with the cdc2 protein kinase to form MPF. Members in this family contain two cyclin boxes. This model corresponds to the first one. The cyclin box is a protein binding domain.


Pssm-ID: 410271  Cd Length: 134  Bit Score: 36.89  E-value: 4.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 311771512 189 NKLRFVPQSLFKFIfgdkifyphNFFDQFLATEVCSREMLNLLCSNALFIICGFD 243
Cdd:cd20568   53 EKFRLLPETLFLAV---------NIIDRFLSKRVVSLNKLQLVGISALFIASKYE 98
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
14-367 7.91e-43

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 153.48  E-value: 7.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  14 LLTMASLISVLGTTHGLFGKLHPGSPEVTMnISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNT--------- 84
Cdd:PLN02872   3 VLISLFISTSAGGVLTGQSNLLRRSPVESL-CAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLGSQrgppvllqh 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  85 -----------------------DAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQK 141
Cdd:PLN02872  82 glfmagdawflnspeqslgfilaDHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQELALYDLAEMIHYVYSITNSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512 142 qLHYVGHSQGTTIGFIAFsTNPSLAKRIKTFYALAPVATVKY-TKSLInkLRFVPQSLFKFIFGDKIfYPHNFFDQFLAT 220
Cdd:PLN02872 162 -IFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHvTAPLV--LRMVFMHLDQMVVAMGI-HQLNFRSDVLVK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512 221 EVCSREMLNLLCSNALFIICGfdsKN--FNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSpVQNRMHYDQS 298
Cdd:PLN02872 237 LLDSICEGHMDCNDLLTSITG---TNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYGQV 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311771512 299 QPPYYNVTAMNVPIAVW--NGGKDLLADPQDVGLLLPKL---PNLIYHKEipfYNHLDFIWAMDAPQEVYNDIV 367
Cdd:PLN02872 313 NPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELpskPELLYLEN---YGHIDFLLSTSAKEDVYNHMI 383
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
85-354 8.04e-18

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: 81.78  E-value: 8.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512   85 DAGYDVWLGNSRGNTWARRNLYYSpdsvefwAFSFDEMAKYdlpatIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPS 164
Cdd:pfam00561  25 RDGFRVIALDLRGFGKSSRPKAQD-------DYRTDDLAED-----LEYILEALGLEKVNLVGHSMGGLIALAYAAKYPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  165 lakRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSRemLNLLCSNALFiicgfdS 244
Cdd:pfam00561  93 ---RVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLR--LRLLKALPLL------N 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  245 KNFntSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWgspvqnrmhydqsqppyynvtamnvPIAVWNGGKDLLAD 324
Cdd:pfam00561 162 KRF--PSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDE-------------------------PTLIIWGDQDPLVP 214
                         250       260       270
                  ....*....|....*....|....*....|
gi 311771512  325 PQDVGLLLPKLPNLIYHKEIPFYnHLDFIW 354
Cdd:pfam00561 215 PQALEKLAQLFPNARLVVIPDAG-HFAFLE 243
Abhydro_lipase pfam04083
Partial alpha/beta-hydrolase lipase region; This family corresponds to a N-terminal part of an ...
45-92 3.21e-16

Partial alpha/beta-hydrolase lipase region; This family corresponds to a N-terminal part of an alpha/beta hydrolase domain.


Pssm-ID: 461162 [Multi-domain]  Cd Length: 63  Bit Score: 72.19  E-value: 3.21e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 311771512   45 ISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTDAGYDVWL 92
Cdd:pfam04083   1 VSEIIRYYGYPVEEHEVTTEDGYILTLHRIPAGRNNSNGKGGKPVVLL 48
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
117-172 7.34e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.02  E-value: 7.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311771512 117 FSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGttiGFIA-FSTNPSLAKRIKTF 172
Cdd:COG4757   83 AGYRDWGELDLPAVLDALRARFPGLPLLLVGHSLG---GQLLgLAPNAERVDRLVTV 136
CYCLIN_CLBs_yeast_rpt1 cd20568
first cyclin box found in yeast B-type cyclins; This subfamily includes Saccharomyces ...
189-243 4.61e-03

first cyclin box found in yeast B-type cyclins; This subfamily includes Saccharomyces cerevisiae G2/mitotic-specific cyclins 1-4 (ScCLB1-4), S-phase entry cyclins 5-6 (ScCLB5-6), and Schizosaccharomyces pombe G2/mitotic-specific cyclins, cig1, cig2 and cdc13. ScCLB1-4 are essential for the control of the cell cycle at the G2/M (mitosis) transition. They interact with the CDC2 protein kinase to form maturation promoting factor (MPF). ScCLB5-6 interact with CDC28 and are involved in DNA replication in Saccharomyces cerevisiae. ScCLB5 is required for efficient progression through S phase and possibly for the normal progression through meiosis. ScCLB6 is involved in G1/S and or S phase progression. Cig1 is required for efficient passage of the G1/S transition. Cig2 and cdc13 are essential for the control of the cell cycle at the G2/M and G1/S (mitosis) transitions. They interact with the cdc2 protein kinase to form MPF. Members in this family contain two cyclin boxes. This model corresponds to the first one. The cyclin box is a protein binding domain.


Pssm-ID: 410271  Cd Length: 134  Bit Score: 36.89  E-value: 4.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 311771512 189 NKLRFVPQSLFKFIfgdkifyphNFFDQFLATEVCSREMLNLLCSNALFIICGFD 243
Cdd:cd20568   53 EKFRLLPETLFLAV---------NIIDRFLSKRVVSLNKLQLVGISALFIASKYE 98
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
85-154 6.21e-03

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.96  E-value: 6.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771512  85 DAGYDVWlgnsrgntwarrNLYYSPDsvefwAFSFDEMAKYdLPATIDFIVKKTGQKQLHYVGHSQGTTI 154
Cdd:COG1075   30 AAGYPVY------------ALNYPST-----NGSIEDSAEQ-LAAFVDAVLAATGAEKVDLVGHSMGGLV 81
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH