NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|10383802|ref|NP_009994|]
View 

triglyceride lipase ATG15 [Saccharomyces cerevisiae S288C]

Protein Classification

lipase family protein( domain architecture ID 10087743)

lipase class 3 family protein may function as a lipase, catalyzing the hydrolysis of ester bonds of insoluble substrates such a triglycerides, or as a feruloyl esterase, hydrolyzing the feruloyl-arabinose ester bond in arabinoxylans and the feruloyl-galactose ester bond in pectin

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016788
PubMed:  9379943|12091482
SCOP:  4000732

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 176-421 4.65e-24

Lipase (class 3). 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: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 100.63  E-value: 4.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 176 DRGTVVSLALMSSNAYVRIPQtgDWRNVTEPWNETEPEDFGWDG-------DGIRGHVFYNEVENIVVLSIKGTSaqglp 248
Cdd:cd00519   1 DYEKLKYYAKLAAAAYCVDAN--ILAKAVVFADIALLNVFSPDKllktdkqYDTQGYVAVDHDRKTIVIAFRGTV----- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 249 gsgedetTGNDKINDNLLFSCCCArvsylWTTVCDCYVKSYicdesclekelrrkdrFYSAVVDIYKGV-------LKEY 321
Cdd:cd00519  74 -------SLADWLTDLDFSPVPLD-----PPLCSGGKVHSG----------------FYSAYKSLYNQVlpelksaLKQY 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 322 PDAAIWVTGHSLGGALASLLGRTFG-------LPAVAFESPGELLPSKRLHlpfppgLPSYMEGIWHFGHNADPIFMGTC 394
Cdd:cd00519 126 PDYKIIVTGHSLGGALASLLALDLRlrgpgsdVTVYTFGQPRVGNAAFAEY------LESTKGRVYRVVHGNDIVPRLPP 199

                       250       260
                ....*....|....*....|....*..
gi 10383802 395 NGASSSCSLvgyametaCHTGRVCVYD 421
Cdd:cd00519 200 GSLTPPEGY--------THVGTEVWID 218
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 176-421 4.65e-24

Lipase (class 3). 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: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 100.63  E-value: 4.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 176 DRGTVVSLALMSSNAYVRIPQtgDWRNVTEPWNETEPEDFGWDG-------DGIRGHVFYNEVENIVVLSIKGTSaqglp 248
Cdd:cd00519   1 DYEKLKYYAKLAAAAYCVDAN--ILAKAVVFADIALLNVFSPDKllktdkqYDTQGYVAVDHDRKTIVIAFRGTV----- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 249 gsgedetTGNDKINDNLLFSCCCArvsylWTTVCDCYVKSYicdesclekelrrkdrFYSAVVDIYKGV-------LKEY 321
Cdd:cd00519  74 -------SLADWLTDLDFSPVPLD-----PPLCSGGKVHSG----------------FYSAYKSLYNQVlpelksaLKQY 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 322 PDAAIWVTGHSLGGALASLLGRTFG-------LPAVAFESPGELLPSKRLHlpfppgLPSYMEGIWHFGHNADPIFMGTC 394
Cdd:cd00519 126 PDYKIIVTGHSLGGALASLLALDLRlrgpgsdVTVYTFGQPRVGNAAFAEY------LESTKGRVYRVVHGNDIVPRLPP 199

                       250       260
                ....*....|....*....|....*..
gi 10383802 395 NGASSSCSLvgyametaCHTGRVCVYD 421
Cdd:cd00519 200 GSLTPPEGY--------THVGTEVWID 218
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 293-356 3.86e-11

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 65.04  E-value: 3.86e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10383802 293 ESCLEKELRRKDRFYSAVVDIYKGVLKEYPDAAIWVTGHSLGGALASLLGRTFGLPAVAFESPG 356
Cdd:COG5153  88 EGFEQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAVATGLSKVTFAAPG 151
Lipase_3 pfam01764
Lipase (class 3);
236-342 2.18e-09

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 55.73  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802   236 VLSIKGTSaqglpgsgedetTGNDKINDnLLFScccaRVSYLWTTVCDCYV-----KSYICDESCLEKELRRkdrfysav 310
Cdd:pfam01764   1 VVAFRGTN------------SILDWLTD-FDFS----LTPFKDFFLGGGKVhsgflSAYTSVREQVLAELKR-------- 55

                          90       100       110
                  ....*....|....*....|....*....|..
gi 10383802   311 vdiykgVLKEYPDAAIWVTGHSLGGALASLLG 342
Cdd:pfam01764  56 ------LLEKYPDYSIVVTGHSLGGALASLAA 81
PLN02934 PLN02934
triacylglycerol lipase
 303-340 9.52e-05

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 45.16  E-value: 9.52e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 10383802  303 KDRFYSAVVDIYKGVLKEYPDAAIWVTGHSLGGALASL 340
Cdd:PLN02934 300 ERSAYYAVRSKLKSLLKEHKNAKFVVTGHSLGGALAIL 337
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 176-421 4.65e-24

Lipase (class 3). 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: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 100.63  E-value: 4.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 176 DRGTVVSLALMSSNAYVRIPQtgDWRNVTEPWNETEPEDFGWDG-------DGIRGHVFYNEVENIVVLSIKGTSaqglp 248
Cdd:cd00519   1 DYEKLKYYAKLAAAAYCVDAN--ILAKAVVFADIALLNVFSPDKllktdkqYDTQGYVAVDHDRKTIVIAFRGTV----- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 249 gsgedetTGNDKINDNLLFSCCCArvsylWTTVCDCYVKSYicdesclekelrrkdrFYSAVVDIYKGV-------LKEY 321
Cdd:cd00519  74 -------SLADWLTDLDFSPVPLD-----PPLCSGGKVHSG----------------FYSAYKSLYNQVlpelksaLKQY 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 322 PDAAIWVTGHSLGGALASLLGRTFG-------LPAVAFESPGELLPSKRLHlpfppgLPSYMEGIWHFGHNADPIFMGTC 394
Cdd:cd00519 126 PDYKIIVTGHSLGGALASLLALDLRlrgpgsdVTVYTFGQPRVGNAAFAEY------LESTKGRVYRVVHGNDIVPRLPP 199

                       250       260
                ....*....|....*....|....*..
gi 10383802 395 NGASSSCSLvgyametaCHTGRVCVYD 421
Cdd:cd00519 200 GSLTPPEGY--------THVGTEVWID 218
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 306-396 1.72e-12

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: 65.21  E-value: 1.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 306 FYSAVVDIYKGV-------LKEYPDAAIWVTGHSLGGALASLLGR--------------TFGLPAVAFESpgelLPSKRL 364
Cdd:cd00741   3 FYKAARSLANLVlpllksaLAQYPDYKIHVTGHSLGGALAGLAGLdlrgrglgrlvrvyTFGPPRVGNAA----FAEDRL 78

                        90       100       110
                ....*....|....*....|....*....|..
gi 10383802 365 HlpfppglPSYMEGIWHFGHNADPIFMGTCNG 396
Cdd:cd00741  79 D-------PSDALFVDRIVNDNDIVPRLPPGG 103
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 293-356 3.86e-11

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 65.04  E-value: 3.86e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10383802 293 ESCLEKELRRKDRFYSAVVDIYKGVLKEYPDAAIWVTGHSLGGALASLLGRTFGLPAVAFESPG 356
Cdd:COG5153  88 EGFEQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAVATGLSKVTFAAPG 151
Lipase_3 pfam01764
Lipase (class 3);
236-342 2.18e-09

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 55.73  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802   236 VLSIKGTSaqglpgsgedetTGNDKINDnLLFScccaRVSYLWTTVCDCYV-----KSYICDESCLEKELRRkdrfysav 310
Cdd:pfam01764   1 VVAFRGTN------------SILDWLTD-FDFS----LTPFKDFFLGGGKVhsgflSAYTSVREQVLAELKR-------- 55

                          90       100       110
                  ....*....|....*....|....*....|..
gi 10383802   311 vdiykgVLKEYPDAAIWVTGHSLGGALASLLG 342
Cdd:pfam01764  56 ------LLEKYPDYSIVVTGHSLGGALASLAA 81
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
306-385 1.85e-06

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 49.37  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383802 306 FYSAVVDIY----KGVLKEYPDAAIWVTGHSLGGALASLLGR--------------TFGLPAVAF----ESPGELLPSKR 363
Cdd:COG3675  66 FYRALQSLRelleDALRPLSPGKRLYVTGHSLGGALATLAAAdlernyifpvrglyTFGQPRVGDrsfaKYYNLHVPNSY 145

                        90       100
                ....*....|....*....|....*
gi 10383802 364 LHLPFP---PGLPSYMEGIWHFGHN 385
Cdd:COG3675 146 RIVNNNdivPLLPPVWMGYDHVGKL 170
PLN02934 PLN02934
triacylglycerol lipase
 303-340 9.52e-05

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 45.16  E-value: 9.52e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 10383802  303 KDRFYSAVVDIYKGVLKEYPDAAIWVTGHSLGGALASL 340
Cdd:PLN02934 300 ERSAYYAVRSKLKSLLKEHKNAKFVVTGHSLGGALAIL 337
 
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