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Conserved domains on  [gi|758063|emb|CAA29413|]
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gastric lipase 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

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List of domain hits

Name Accession Description Interval E-value
PLN02872 super family cl28691
triacylglycerol lipase
4-390 9.52e-59

triacylglycerol lipase


The actual alignment was detected with superfamily member PLN02872:

Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 196.24  E-value: 9.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063      4 LLTMASLISVLGTTHGLFGKLHPGSPEVTMnISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGntGQR-PVVFL 82
Cdd:PLN02872   3 VLISLFISTSAGGVLTGQSNLLRRSPVESL-CAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLG--SQRgPPVLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063     83 QHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTG 162
Cdd:PLN02872  80 QHGLFMAGDAWFLNSPEQSLGFILADHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQELALYDLAEMIHYVYSITN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    163 QKqLHYVGHSQGTTIGFIAFsTNPSLAKRIKTFYALAPVATVKY-TKSLInkLRFVPQSLFKFIFGDKIfYPHNFFDQFL 241
Cdd:PLN02872 160 SK-IFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHvTAPLV--LRMVFMHLDQMVVAMGI-HQLNFRSDVL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    242 ATEVCSREMLNLLCSNALFIICGfdsKN--FNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSpVQNRMHYD 319
Cdd:PLN02872 235 VKLLDSICEGHMDCNDLLTSITG---TNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYG 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758063    320 QSQPPYYNVTAMNVPIAVW--NGGKDLLADPQDVGLLLPKL---PNLIYHKEipfYNHLDFIWAMDAPQEVYNDIV 390
Cdd:PLN02872 311 QVNPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELpskPELLYLEN---YGHIDFLLSTSAKEDVYNHMI 383
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
4-390 9.52e-59

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 196.24  E-value: 9.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063      4 LLTMASLISVLGTTHGLFGKLHPGSPEVTMnISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGntGQR-PVVFL 82
Cdd:PLN02872   3 VLISLFISTSAGGVLTGQSNLLRRSPVESL-CAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLG--SQRgPPVLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063     83 QHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTG 162
Cdd:PLN02872  80 QHGLFMAGDAWFLNSPEQSLGFILADHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQELALYDLAEMIHYVYSITN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    163 QKqLHYVGHSQGTTIGFIAFsTNPSLAKRIKTFYALAPVATVKY-TKSLInkLRFVPQSLFKFIFGDKIfYPHNFFDQFL 241
Cdd:PLN02872 160 SK-IFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHvTAPLV--LRMVFMHLDQMVVAMGI-HQLNFRSDVL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    242 ATEVCSREMLNLLCSNALFIICGfdsKN--FNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSpVQNRMHYD 319
Cdd:PLN02872 235 VKLLDSICEGHMDCNDLLTSITG---TNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYG 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758063    320 QSQPPYYNVTAMNVPIAVW--NGGKDLLADPQDVGLLLPKL---PNLIYHKEipfYNHLDFIWAMDAPQEVYNDIV 390
Cdd:PLN02872 311 QVNPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELpskPELLYLEN---YGHIDFLLSTSAKEDVYNHMI 383
Abhydro_lipase pfam04083
Partial alpha/beta-hydrolase lipase region; This family corresponds to a N-terminal part of an ...
35-97 4.06e-32

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: 115.71  E-value: 4.06e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758063      35 ISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNL 97
Cdd:pfam04083   1 VSEIIRYYGYPVEEHEVTTEDGYILTLHRIPAGRNNSNGKGGKPVVLLQHGLLASSDNWVTNG 63
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
75-177 1.51e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.84  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    75 GQRPVVFLqHGLLASATNWisnlpnNSLAFILADAGYDVWlgnsrgntwarrNLYYSPDsvefwAFSFDEMAKYdLPATI 154
Cdd:COG1075   4 TRYPVVLV-HGLGGSAASW------APLAPRLRAAGYPVY------------ALNYPST-----NGSIEDSAEQ-LAAFV 58
                        90       100
                ....*....|....*....|...
gi 758063   155 DFIVKKTGQKQLHYVGHSQGTTI 177
Cdd:COG1075  59 DAVLAATGAEKVDLVGHSMGGLV 81
CYCLIN_CLBs_yeast_rpt1 cd20568
first cyclin box found in yeast B-type cyclins; This subfamily includes Saccharomyces ...
212-266 4.95e-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: 4.95e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 758063   212 NKLRFVPQSLFKFIfgdkifyphNFFDQFLATEVCSREMLNLLCSNALFIICGFD 266
Cdd:cd20568  53 EKFRLLPETLFLAV---------NIIDRFLSKRVVSLNKLQLVGISALFIASKYE 98
 
Name Accession Description Interval E-value
PLN02872 PLN02872
triacylglycerol lipase
4-390 9.52e-59

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 196.24  E-value: 9.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063      4 LLTMASLISVLGTTHGLFGKLHPGSPEVTMnISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGntGQR-PVVFL 82
Cdd:PLN02872   3 VLISLFISTSAGGVLTGQSNLLRRSPVESL-CAQLIHPAGYSCTEHTIQTKDGYLLALQRVSSRNPRLG--SQRgPPVLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063     83 QHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTG 162
Cdd:PLN02872  80 QHGLFMAGDAWFLNSPEQSLGFILADHGFDVWVGNVRGTRWSYGHVTLSEKDKEFWDWSWQELALYDLAEMIHYVYSITN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    163 QKqLHYVGHSQGTTIGFIAFsTNPSLAKRIKTFYALAPVATVKY-TKSLInkLRFVPQSLFKFIFGDKIfYPHNFFDQFL 241
Cdd:PLN02872 160 SK-IFIVGHSQGTIMSLAAL-TQPNVVEMVEAAALLCPISYLDHvTAPLV--LRMVFMHLDQMVVAMGI-HQLNFRSDVL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    242 ATEVCSREMLNLLCSNALFIICGfdsKN--FNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSpVQNRMHYD 319
Cdd:PLN02872 235 VKLLDSICEGHMDCNDLLTSITG---TNccFNASRIDYYLEYEPHPSSVKNLRHLFQMIRKGTFAHYDYGI-FKNLKLYG 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758063    320 QSQPPYYNVTAMNVPIAVW--NGGKDLLADPQDVGLLLPKL---PNLIYHKEipfYNHLDFIWAMDAPQEVYNDIV 390
Cdd:PLN02872 311 QVNPPAFDLSLIPKSLPLWmgYGGTDGLADVTDVEHTLAELpskPELLYLEN---YGHIDFLLSTSAKEDVYNHMI 383
Abhydro_lipase pfam04083
Partial alpha/beta-hydrolase lipase region; This family corresponds to a N-terminal part of an ...
35-97 4.06e-32

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: 115.71  E-value: 4.06e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758063      35 ISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNL 97
Cdd:pfam04083   1 VSEIIRYYGYPVEEHEVTTEDGYILTLHRIPAGRNNSNGKGGKPVVLLQHGLLASSDNWVTNG 63
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
78-377 1.32e-23

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: 98.35  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063      78 PVVFLQHGLLASATNWISNLPNnslafiLADAGYDVWLGNSRGNTWARRNLYYSpdsvefwAFSFDEMAKYdlpatIDFI 157
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPA------LARDGFRVIALDLRGFGKSSRPKAQD-------DYRTDDLAED-----LEYI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063     158 VKKTGQKQLHYVGHSQGTTIGFIAFSTNPSlakRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFF 237
Cdd:pfam00561  63 LEALGLEKVNLVGHSMGGLIALAYAAKYPD---RVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063     238 DQFLATEVCSRemLNLLCSNALFiicgfdSKNFntSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWgspvqnrmh 317
Cdd:pfam00561 140 VAKLLALLLLR--LRLLKALPLL------NKRF--PSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDE--------- 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063     318 ydqsqppyynvtamnvPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYnHLDFIW 377
Cdd:pfam00561 201 ----------------PTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG-HFAFLE 243
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
75-177 1.51e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.84  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    75 GQRPVVFLqHGLLASATNWisnlpnNSLAFILADAGYDVWlgnsrgntwarrNLYYSPDsvefwAFSFDEMAKYdLPATI 154
Cdd:COG1075   4 TRYPVVLV-HGLGGSAASW------APLAPRLRAAGYPVY------------ALNYPST-----NGSIEDSAEQ-LAAFV 58
                        90       100
                ....*....|....*....|...
gi 758063   155 DFIVKKTGQKQLHYVGHSQGTTI 177
Cdd:COG1075  59 DAVLAATGAEKVDLVGHSMGGLV 81
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
45-192 4.62e-07

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 50.39  E-value: 4.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    45 PNEEYEVVTEDGYILEVNRIPYGKKnsgntgQRPVVFLQHGLLASATNWisnlpnNSLAFILADAGYDVWLGNSRGNTWA 124
Cdd:COG2267   2 TRRLVTLPTRDGLRLRGRRWRPAGS------PRGTVVLVHGLGEHSGRY------AELAEALAAAGYAVLAFDLRGHGRS 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758063   125 RRNLYYSPDsvefwafsFDEMAKyDLPATIDFIVKKTGQKqLHYVGHSQGTTIGFIAFSTNPSLAKRI 192
Cdd:COG2267  70 DGPRGHVDS--------FDDYVD-DLRAALDALRARPGLP-VVLLGHSMGGLIALLYAARYPDRVAGL 127
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
47-195 3.74e-06

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 48.34  E-value: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063    47 EEYEVVTEDGYILEVNRIPygkknsGNTGQRPVVflqhgLLASAT-----------NWisnlpnnslafiLADAGYDVWL 115
Cdd:COG4757   8 ESVTITAADGYPLAARLFP------PAGPPRAVV-----LINPATgvpqrfyrpfaRY------------LAERGFAVLT 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758063   116 ------GNSRgntwarrnlyysPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGttiGFIA-FSTNPSL 188
Cdd:COG4757  65 ydyrgiGLSR------------PGSLRGFDAGYRDWGELDLPAVLDALRARFPGLPLLLVGHSLG---GQLLgLAPNAER 129

                ....*..
gi 758063   189 AKRIKTF 195
Cdd:COG4757 130 VDRLVTV 136
CYCLIN_CLBs_yeast_rpt1 cd20568
first cyclin box found in yeast B-type cyclins; This subfamily includes Saccharomyces ...
212-266 4.95e-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: 4.95e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 758063   212 NKLRFVPQSLFKFIfgdkifyphNFFDQFLATEVCSREMLNLLCSNALFIICGFD 266
Cdd:cd20568  53 EKFRLLPETLFLAV---------NIIDRFLSKRVVSLNKLQLVGISALFIASKYE 98
CYCLIN_CCNB3_rpt1 cd20508
first cyclin box found in G2/mitotic-specific cyclin-B3 (CCNB3) and similar proteins; CCNB3 is ...
238-266 9.49e-03

first cyclin box found in G2/mitotic-specific cyclin-B3 (CCNB3) and similar proteins; CCNB3 is a mitotic B-type cyclin that promotes the metaphase-anaphase transition. It controls anaphase onset independent of spindle assembly checkpoint in meiotic oocytes. CCNB3 contains two cyclin boxes. This model corresponds to the first one. The cyclin box is a protein binding domain.


Pssm-ID: 410212 [Multi-domain]  Cd Length: 142  Bit Score: 36.46  E-value: 9.49e-03
                        10        20
                ....*....|....*....|....*....
gi 758063   238 DQFLATEVCSREMLNLLCSNALFIICGFD 266
Cdd:cd20508  77 DLYLSKKVVKKEKLQLLGATAILIASKFD 105
 
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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