NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|392898334|ref|NP_500090|]
View 

Fungal lipase-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

lipase family protein( domain architecture ID 10484750)

lipase class 3 family protein may function as a lipase, catalyzing the hydrolysis of ester bonds of insoluble substrates such a triglycerides; similar to Arabidopsis thaliana phospholipase A1 PLIP3 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0006629|GO:0052689
PubMed:  19508187|12369917|9379946|9704093|8453375|8280778|11099800|37582413|31545554
SCOP:  3000102

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 pfam01764
Lipase (class 3);
132-269 2.64e-55

Lipase (class 3);


:

Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 177.07  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  132 VMSFRATNTGTQLEEEFLNYFVAKKAFF-DSGYIFEFFYDAYLaLWKGGLEAEMRNLKYRYPDYEVWVTGHSLGAALASV 210
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFlGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  211 GASWVVKTGLFKPEQMKLLTAGQPRTGDYAYSNWHQNTFAY-SFRIVHAHDMVPHLPFQY 269
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
132-269 2.64e-55

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 177.07  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  132 VMSFRATNTGTQLEEEFLNYFVAKKAFF-DSGYIFEFFYDAYLaLWKGGLEAEMRNLKYRYPDYEVWVTGHSLGAALASV 210
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFlGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  211 GASWVVKTGLFKPEQMKLLTAGQPRTGDYAYSNWHQNTFAY-SFRIVHAHDMVPHLPFQY 269
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 85-287 1.64e-44

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: 152.25  E-value: 1.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  85 AQKCFDNNWPTMKLSKRILVNCsdpspilpltqCAMITAVDTTQKVLVMSFRATNTGTQLEEEFLNYFV-AKKAFFDSGY 163
Cdd:cd00519   30 ADIALLNVFSPDKLLKTDKQYD-----------TQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFSPVpLDPPLCSGGK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 164 IFEFFYDAYLALWKGGLEAEMRNLKYrYPDYEVWVTGHSLGAALASVGASWVVKTGLFKPeqMKLLTAGQPRTGDYAYSN 243
Cdd:cd00519   99 VHSGFYSAYKSLYNQVLPELKSALKQ-YPDYKIIVTGHSLGGALASLLALDLRLRGPGSD--VTVYTFGQPRVGNAAFAE 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392898334 244 WHQNTFAYSFRIVHAHDMVPHLPFQYELVDHDkMYHHRTEIWYN 287
Cdd:cd00519  176 YLESTKGRVYRVVHGNDIVPRLPPGSLTPPEG-YTHVGTEVWID 218
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
129-298 2.71e-24

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 99.83  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 129 KVLVMSFRATNTGTQLEEEFLNYFVAKKAFFDSGYIFEFFYDAYLALWKGgLEAEMRNLkyrYPDYEVWVTGHSLGAALA 208
Cdd:COG3675   27 DEVIVAFRGTESLTDWLTNLNAAQVPYPFAKTGGKVHRGFYRALQSLREL-LEDALRPL---SPGKRLYVTGHSLGGALA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 209 SVGASWVVKTGLFKPEQmkLLTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLPFQYELVDHDKMYHhrteiWYNN 288
Cdd:COG3675  103 TLAAADLERNYIFPVRG--LYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLL-----WLDS 175

                        170
                 ....*....|
gi 392898334 289 DMSIGSSYHV 298
Cdd:COG3675  176 LRKDMLTDHS 185
PLN02934 PLN02934
triacylglycerol lipase
 198-287 6.48e-08

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 54.02  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 198 VTGHSLGAALASVGASWVVKTGlfKPEQMKLL----TAGQPRTGDYAYSNWHQNTFAYS----FRIVHAHDMVPHLPFQy 269
Cdd:PLN02934 325 VTGHSLGGALAILFPTVLVLQE--ETEVMKRLlgvyTFGQPRIGNRQLGKFMEAQLNYPvpryFRVVYCNDLVPRLPYD- 401

                         90       100
                 ....*....|....*....|.
gi 392898334 270 elvdhDKMY---HHRTEIWYN 287
Cdd:PLN02934 402 -----DKTFlykHFGVCLYYD 417
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
132-269 2.64e-55

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 177.07  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  132 VMSFRATNTGTQLEEEFLNYFVAKKAFF-DSGYIFEFFYDAYLaLWKGGLEAEMRNLKYRYPDYEVWVTGHSLGAALASV 210
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFlGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  211 GASWVVKTGLFKPEQMKLLTAGQPRTGDYAYSNWHQNTFAY-SFRIVHAHDMVPHLPFQY 269
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 85-287 1.64e-44

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: 152.25  E-value: 1.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334  85 AQKCFDNNWPTMKLSKRILVNCsdpspilpltqCAMITAVDTTQKVLVMSFRATNTGTQLEEEFLNYFV-AKKAFFDSGY 163
Cdd:cd00519   30 ADIALLNVFSPDKLLKTDKQYD-----------TQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFSPVpLDPPLCSGGK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 164 IFEFFYDAYLALWKGGLEAEMRNLKYrYPDYEVWVTGHSLGAALASVGASWVVKTGLFKPeqMKLLTAGQPRTGDYAYSN 243
Cdd:cd00519   99 VHSGFYSAYKSLYNQVLPELKSALKQ-YPDYKIIVTGHSLGGALASLLALDLRLRGPGSD--VTVYTFGQPRVGNAAFAE 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392898334 244 WHQNTFAYSFRIVHAHDMVPHLPFQYELVDHDkMYHHRTEIWYN 287
Cdd:cd00519  176 YLESTKGRVYRVVHGNDIVPRLPPGSLTPPEG-YTHVGTEVWID 218
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 168-323 9.43e-36

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: 126.85  E-value: 9.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 168 FYDAYLALWKGgLEAEMRNLKYRYPDYEVWVTGHSLGAALASVGASWVVKTGLFKPeqMKLLTAGQPRTGDYAYSN--WH 245
Cdd:cd00741    3 FYKAARSLANL-VLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGLGRL--VRVYTFGPPRVGNAAFAEdrLD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392898334 246 QNTFAYSFRIVHAHDMVPHLPFqyelvDHDKMYHHRTEIWYNNDMSIGSSYHVCQEA-DGFYCSNQNADLSWNDHTHYY 323
Cdd:cd00741   80 PSDALFVDRIVNDNDIVPRLPP-----GGEGYPHGGAEFYINGGKSQPGCCKNVLEAvDIDFGNIGLSGNGLCDHLRYF 153
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
129-298 2.71e-24

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 99.83  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 129 KVLVMSFRATNTGTQLEEEFLNYFVAKKAFFDSGYIFEFFYDAYLALWKGgLEAEMRNLkyrYPDYEVWVTGHSLGAALA 208
Cdd:COG3675   27 DEVIVAFRGTESLTDWLTNLNAAQVPYPFAKTGGKVHRGFYRALQSLREL-LEDALRPL---SPGKRLYVTGHSLGGALA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 209 SVGASWVVKTGLFKPEQmkLLTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLPFQYELVDHDKMYHhrteiWYNN 288
Cdd:COG3675  103 TLAAADLERNYIFPVRG--LYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLL-----WLDS 175

                        170
                 ....*....|
gi 392898334 289 DMSIGSSYHV 298
Cdd:COG3675  176 LRKDMLTDHS 185
PLN02934 PLN02934
triacylglycerol lipase
 198-287 6.48e-08

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 54.02  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 198 VTGHSLGAALASVGASWVVKTGlfKPEQMKLL----TAGQPRTGDYAYSNWHQNTFAYS----FRIVHAHDMVPHLPFQy 269
Cdd:PLN02934 325 VTGHSLGGALAILFPTVLVLQE--ETEVMKRLlgvyTFGQPRIGNRQLGKFMEAQLNYPvpryFRVVYCNDLVPRLPYD- 401

                         90       100
                 ....*....|....*....|.
gi 392898334 270 elvdhDKMY---HHRTEIWYN 287
Cdd:PLN02934 402 -----DKTFlykHFGVCLYYD 417
PLN02802 PLN02802
triacylglycerol lipase
 183-291 8.11e-08

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 53.62  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 183 EMRNL--KYRYPDYEVWVTGHSLGAALASVGASwVVKTGLFKPEQMKLLTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHD 260
Cdd:PLN02802 317 EVRRLmeKYKGEELSITVTGHSLGAALALLVAD-ELATCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQD 395

                         90       100       110
                 ....*....|....*....|....*....|...
gi 392898334 261 MVPHLPFQYELVDHDKM-YHHR-TEIWYNNDMS 291
Cdd:PLN02802 396 VVTRVPGIAPREELHKWaYAHVgAELRLDSKMS 428
PLN00413 PLN00413
triacylglycerol lipase
 192-280 4.40e-07

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 51.17  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 192 PDYEVWVTGHSLGAALASVGASWVVktgLFKPEQM-----KLLTAGQPRTGDYAYSNWHQNT---FAYSF-RIVHAHDMV 262
Cdd:PLN00413 282 PTSKFILSGHSLGGALAILFTAVLI---MHDEEEMlerleGVYTFGQPRVGDEDFGIFMKDKlkeFDVKYeRYVYCNDMV 358

                         90
                 ....*....|....*...
gi 392898334 263 PHLPFQyelvDHDKMYHH 280
Cdd:PLN00413 359 PRLPFD----DKTLMFKH 372
PLN02753 PLN02753
triacylglycerol lipase
 193-266 5.84e-07

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 50.87  E-value: 5.84e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392898334 193 DYEVWVTGHSLGAALASVGASWVVKTGLFKPEQMKL-----LTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLP 266
Cdd:PLN02753 311 DLSITVTGHSLGGALAILSAYDIAEMGLNRSKKGKVipvtvLTYGGPRVGNVRFKDRMEELGVKVLRVVNVHDVVPKSP 389
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 123-264 1.37e-06

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


Pssm-ID: 444061  Cd Length: 405  Bit Score: 49.63  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 123 AVDTTQKVL---VMSFRATNTGTQLEEEF---LNYFVAK------KAFFDSGYIFEFFYDAYLALWKGGLEAEMRNLKYR 190
Cdd:COG5153   36 AVALDEKAIydtIIAFRGTQGKPDWKTDInasLHDYDEKnkeadeKLPLQVHEGFEQYAAQVMDLDYDGAEELAAEVKKQ 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392898334 191 YPDYEVWVTGHSLGAALASVGAswvVKTGLFKpeqmklLTAGQPRTGDYAYSNWHQNTFAySFRIVHAHDMVPH 264
Cdd:COG5153  116 YPDAELSLTGHSLGGALASLVA---VATGLSK------VTFAAPGSGNHALADDLGKRID-AGEFVKSLDAVAG 179
PLN02719 PLN02719
triacylglycerol lipase
 135-266 2.69e-06

triacylglycerol lipase


Pssm-ID: 178321  Cd Length: 518  Bit Score: 48.93  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 135 FRATNTGTQLEEEFLNYFVAKkaffDSGYIFEFFYDAYLALwkggleAEMRNLKYRYPDYE-----VWVTGHSLGAALAS 209
Cdd:PLN02719 244 FRCPDPAVKAESGFLDLYTDK----DTCCNFSKFSAREQVL------TEVKRLVERYGDEEgeelsITVTGHSLGGALAV 313

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392898334 210 VGASWVVKTGLFKPEQMKLL-----TAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLP 266
Cdd:PLN02719 314 LSAYDVAEMGLNRTRKGKVIpvtafTYGGPRVGNIRFKERIEELGVKVLRVVNEHDVVAKSP 375
PLN02571 PLN02571
triacylglycerol lipase
 183-267 3.72e-05

triacylglycerol lipase


Pssm-ID: 215309  Cd Length: 413  Bit Score: 45.26  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 183 EMRNLKYRYPDYEVWVT--GHSLGAALASVGASWVVKTGLFKPEQMK----LLTA---GQPRTGDyaySNWHQNTFAYS- 252
Cdd:PLN02571 213 EVGRLVEKYKDEEISITicGHSLGAALATLNAVDIVANGFNRSKSRPnkscPVTAfvfASPRVGD---SDFKKLFSGLKd 289

                         90
                 ....*....|....*...
gi 392898334 253 ---FRIVHAHDMVPHLPF 267
Cdd:PLN02571 290 lrvLRVRNLPDVIPNYPL 307
PLN02761 PLN02761
lipase class 3 family protein
 182-270 6.05e-05

lipase class 3 family protein


Pssm-ID: 215406 [Multi-domain]  Cd Length: 527  Bit Score: 44.65  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 182 AEMRNLKYRYPDYE------VWVTGHSLGAALASVGASWVVKTGL-FKPEQ-----MKLLTAGQPRTGDYAYSNWHQNTF 249
Cdd:PLN02761 276 AEVKRLVEYYGTEEegheisITVTGHSLGASLALVSAYDIAELNLnHVPENnykipITVFSFSGPRVGNLRFKERCDELG 355

                         90       100
                 ....*....|....*....|....*...
gi 392898334 250 AYSFRIVHAHDMVPHLP-------FQYE 270
Cdd:PLN02761 356 VKVLRVVNVHDKVPSVPgiftnekFQFQ 383
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 198-266 3.04e-04

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 42.63  E-value: 3.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392898334 198 VTGHSLGAALASVGAsWVVKTGLFKPEQMKLLTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLP 266
Cdd:PLN03037 322 ITGHSLGGALALLNA-YEAARSVPALSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
PLN02408 PLN02408
phospholipase A1
 108-266 4.86e-04

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 41.75  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 108 DPSPILPLTQCAMITAVDTTQ----------KVLVMSFRATNTGTQLEEEF---LNYFV-----AKKAFFDSGYIFEffy 169
Cdd:PLN02408  87 EKAPSWVATQSSWIGYVAVCQdkeeiarlgrRDVVIAFRGTATCLEWLENLratLTRLPnaptdMNGSGDGSGPMVE--- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 170 DAYLALWKGGLEA----------EMRNLKYRYPD--YEVWVTGHSLGAALASVGAsWVVKTGLFKPEQMKLLTAGQPRTG 237
Cdd:PLN02408 164 SGFLSLYTSGTAMgpslqemvreEIARLLQSYGDepLSLTITGHSLGAALATLTA-YDIKTTFKRAPMVTVISFGGPRVG 242

                        170       180
                 ....*....|....*....|....*....
gi 392898334 238 DYAYSNWHQNTFAYSFRIVHAHDMVPHLP 266
Cdd:PLN02408 243 NRSFRRQLEKQGTKVLRIVNSDDVITKVP 271
PLN02310 PLN02310
triacylglycerol lipase
 198-266 8.48e-04

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 40.74  E-value: 8.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 198 VTGHSLGAALASVGAsWVVKTGLfkPEQ-MKLLTAGQPRTGDYAYSNWHQNTFAYSFRIVHAHDMVPHLP 266
Cdd:PLN02310 213 VTGHSLGGALALLNA-YEAATTI--PDLfVSVISFGAPRVGNIAFKEKLNELGVKTLRVVVKQDKVPKLP 279
PLN02162 PLN02162
triacylglycerol lipase
 182-278 1.50e-03

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 40.03  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 182 AEMRNLKYrypdyevWVTGHSLGAALASVGASWVVKTG----LFKPEqmKLLTAGQPRTGDYAYSNW-----HQNTFAYS 252
Cdd:PLN02162 273 ARNKNLKY-------ILTGHSLGGALAALFPAILAIHGedelLDKLE--GIYTFGQPRVGDEDFGEFmkgvvKKHGIEYE 343

                         90       100
                 ....*....|....*....|....*.
gi 392898334 253 fRIVHAHDMVPHLPFQYELVDHDKMY 278
Cdd:PLN02162 344 -RFVYNNDVVPRVPFDDKLLFSYKHY 368
PLN02454 PLN02454
triacylglycerol lipase
 180-266 1.96e-03

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 39.82  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392898334 180 LEAEMRNLKYRYPDYEVWV--TGHSLGAALASVGASWVVKTGLFKPE-QMKLLTAGQPRTGDYAYSNW---HQNtfaysF 253
Cdd:PLN02454 212 LLAKIKELLERYKDEKLSIvlTGHSLGASLATLAAFDIVENGVSGADiPVTAIVFGSPQVGNKEFNDRfkeHPN-----L 286

                         90
                 ....*....|....*.
gi 392898334 254 RIVHAH---DMVPHLP 266
Cdd:PLN02454 287 KILHVRntiDLIPHYP 302
 
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