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Conserved domains on  [gi|25150926|ref|NP_491528|]
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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

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List of domain hits

 Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
83-221 2.90e-52

Lipase (class 3);


:

Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 168.21  E-value: 2.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926    83 FVSFSGTKSKEQLVTELIESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIA 162
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYTSVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 25150926   163 STVFVRNFPETSSRTFSITFGQPRVGNLEYAMTHDKLVAGGSWRLIHGRDIVAHIPFCV 221
Cdd:pfam01764  81 ALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKFSYRVVHQRDIVPRLPPIV 139
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
83-221 2.90e-52

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 168.21  E-value: 2.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926    83 FVSFSGTKSKEQLVTELIESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIA 162
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYTSVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 25150926   163 STVFVRNFPETSSRTFSITFGQPRVGNLEYAMTHDKLVAGGSWRLIHGRDIVAHIPFCV 221
Cdd:pfam01764  81 ALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKFSYRVVHQRDIVPRLPPIV 139
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 26-245 7.66e-49

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: 162.65  E-value: 7.66e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  26 DYELSKRTLEFAAAAYSIDP----EPCISKNNATLLFFKKVECDYM--RDECWSVIAADND--TIFVSFSGTKSKEQLVT 97
Cdd:cd00519   1 DYEKLKYYAKLAAAAYCVDAnilaKAVVFADIALLNVFSPDKLLKTdkQYDTQGYVAVDHDrkTIVIAFRGTVSLADWLT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  98 ELIESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIASTVFVRNFPetSSRT 177
Cdd:cd00519  81 DLDFSPVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDV 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150926 178 FSITFGQPRVGNLEYAMTHDKLVaGGSWRLIHGRDIVAHIPFCVesyarwciPFYNHGSYHHGVEVWF 245
Cdd:cd00519 159 TVYTFGQPRVGNAAFAEYLESTK-GRVYRVVHGNDIVPRLPPGS--------LTPPEGYTHVGTEVWI 217
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
75-254 2.86e-30

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 115.24  E-value: 2.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  75 IAADNDTIFVSFSGTKSKEQLVTELiESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLkdsLPDHKIVFTGHSL 154
Cdd:COG3675  22 ILRSDDEVIVAFRGTESLTDWLTNL-NAAQVPYPFAKTGGKVHRGFYRALQSLRELLEDALRPL---SPGKRLYVTGHSL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926 155 GGAIASIASTVFVRNFPetSSRTFSITFGQPRVGNLEYAMTHDKLVaGGSWRLIHGRDIVAHIPFCVESYA--------- 225
Cdd:COG3675  98 GGALATLAAADLERNYI--FPVRGLYTFGQPRVGDRSFAKYYNLHV-PNSYRIVNNNDIVPLLPPVWMGYDhvgkllwld 174

                       170       180       190
                ....*....|....*....|....*....|....
gi 25150926 226 ---RWCIPFYNHGSYHHGVEVWFP--GNMTSQDT 254
Cdd:COG3675 175 slrKDMLTDHSMDNYIHHTDLSQLltYAYEAAVL 208
PLN00413 PLN00413
triacylglycerol lipase
 56-219 2.43e-09

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 58.10  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926   56 LLFFKKVECDYMRDECWSVI-----AADNDTIFVSFSGTK--SKEQLVTELIESIgrpkHKLHNAGSVHYYFYSAL---K 125
Cdd:PLN00413 171 LLGFYSCPNDFDKQRSTEVIvikdtKDDPNLIIVSFRGTDpfDADDWCTDLDLSW----HEVKNVGKIHGGFMKALglpK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  126 TMWsPME----------------KLLRGLKDSL---PDHKIVFTGHSLGGAIASIASTVFV-RNFPETSSRTFSI-TFGQ 184
Cdd:PLN00413 247 EGW-PEEinldetqnatsllayyTILRHLKEIFdqnPTSKFILSGHSLGGALAILFTAVLImHDEEEMLERLEGVyTFGQ 325

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 25150926  185 PRVGNLEYAM-THDKL--VAGGSWRLIHGRDIVAHIPF 219
Cdd:PLN00413 326 PRVGDEDFGIfMKDKLkeFDVKYERYVYCNDMVPRLPF 363
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
83-221 2.90e-52

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 168.21  E-value: 2.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926    83 FVSFSGTKSKEQLVTELIESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIA 162
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYTSVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASLA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 25150926   163 STVFVRNFPETSSRTFSITFGQPRVGNLEYAMTHDKLVAGGSWRLIHGRDIVAHIPFCV 221
Cdd:pfam01764  81 ALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKFSYRVVHQRDIVPRLPPIV 139
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 26-245 7.66e-49

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: 162.65  E-value: 7.66e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  26 DYELSKRTLEFAAAAYSIDP----EPCISKNNATLLFFKKVECDYM--RDECWSVIAADND--TIFVSFSGTKSKEQLVT 97
Cdd:cd00519   1 DYEKLKYYAKLAAAAYCVDAnilaKAVVFADIALLNVFSPDKLLKTdkQYDTQGYVAVDHDrkTIVIAFRGTVSLADWLT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  98 ELIESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIASTVFVRNFPetSSRT 177
Cdd:cd00519  81 DLDFSPVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDV 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150926 178 FSITFGQPRVGNLEYAMTHDKLVaGGSWRLIHGRDIVAHIPFCVesyarwciPFYNHGSYHHGVEVWF 245
Cdd:cd00519 159 TVYTFGQPRVGNAAFAEYLESTK-GRVYRVVHGNDIVPRLPPGS--------LTPPEGYTHVGTEVWI 217
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 119-285 3.08e-33

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: 119.91  E-value: 3.08e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926 119 YFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIASTVFVRNFPetSSRTFSITFGQPRVGNLEYAMTH-D 197
Cdd:cd00741   2 GFYKAARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGL--GRLVRVYTFGPPRVGNAAFAEDRlD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926 198 KLVAGGSWRLIHGRDIVAHIPFCVESYarwcipfynhgsYHHGVEVWFPGNMTSQDTFKVCTGTplNEDNLCSNTHRYFD 277
Cdd:cd00741  80 PSDALFVDRIVNDNDIVPRLPPGGEGY------------PHGGAEFYINGGKSQPGCCKNVLEA--VDIDFGNIGLSGNG 145


                ....*...
gi 25150926 278 INDHLFYF 285
Cdd:cd00741 146 LCDHLRYF 153
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
75-254 2.86e-30

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 115.24  E-value: 2.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  75 IAADNDTIFVSFSGTKSKEQLVTELiESIGRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLkdsLPDHKIVFTGHSL 154
Cdd:COG3675  22 ILRSDDEVIVAFRGTESLTDWLTNL-NAAQVPYPFAKTGGKVHRGFYRALQSLRELLEDALRPL---SPGKRLYVTGHSL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926 155 GGAIASIASTVFVRNFPetSSRTFSITFGQPRVGNLEYAMTHDKLVaGGSWRLIHGRDIVAHIPFCVESYA--------- 225
Cdd:COG3675  98 GGALATLAAADLERNYI--FPVRGLYTFGQPRVGDRSFAKYYNLHV-PNSYRIVNNNDIVPLLPPVWMGYDhvgkllwld 174

                       170       180       190
                ....*....|....*....|....*....|....
gi 25150926 226 ---RWCIPFYNHGSYHHGVEVWFP--GNMTSQDT 254
Cdd:COG3675 175 slrKDMLTDHSMDNYIHHTDLSQLltYAYEAAVL 208
PLN00413 PLN00413
triacylglycerol lipase
 56-219 2.43e-09

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 58.10  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926   56 LLFFKKVECDYMRDECWSVI-----AADNDTIFVSFSGTK--SKEQLVTELIESIgrpkHKLHNAGSVHYYFYSAL---K 125
Cdd:PLN00413 171 LLGFYSCPNDFDKQRSTEVIvikdtKDDPNLIIVSFRGTDpfDADDWCTDLDLSW----HEVKNVGKIHGGFMKALglpK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  126 TMWsPME----------------KLLRGLKDSL---PDHKIVFTGHSLGGAIASIASTVFV-RNFPETSSRTFSI-TFGQ 184
Cdd:PLN00413 247 EGW-PEEinldetqnatsllayyTILRHLKEIFdqnPTSKFILSGHSLGGALAILFTAVLImHDEEEMLERLEGVyTFGQ 325

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 25150926  185 PRVGNLEYAM-THDKL--VAGGSWRLIHGRDIVAHIPF 219
Cdd:PLN00413 326 PRVGDEDFGIfMKDKLkeFDVKYERYVYCNDMVPRLPF 363
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 29-189 2.79e-08

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


Pssm-ID: 444061  Cd Length: 405  Bit Score: 54.64  E-value: 2.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  29 LSKRTLE-FAAAAYSIDPEPCISKNNATllffkkvecdymrdECWSVIAADNDTIF---VSFSGTKSKEQLVTELIESI- 103
Cdd:COG5153   4 ISEIVYEkLADAATALDIDPFRAANDDI--------------DGHFAVALDEKAIYdtiIAFRGTQGKPDWKTDINASLh 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926 104 --------GRPKHKLHNAGSVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIAStvfvrnfpeTSS 175
Cdd:COG5153  70 dydeknkeADEKLPLQVHEGFEQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVA---------VAT 140

                       170
                ....*....|....
gi 25150926 176 RTFSITFGQPRVGN 189
Cdd:COG5153 141 GLSKVTFAAPGSGN 154
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 108-218 4.18e-07

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 51.11  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  108 HKLHNAGS--VHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVFTGHSLGGAIASIASTVFVRNFPETSSRTFsITFGQP 185
Cdd:PLN03037 279 LSIYKSKSelTRYNKLSASEQVMEEVKRLVNFFKDRGEEVSLTITGHSLGGALALLNAYEAARSVPALSNISV-ISFGAP 357

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 25150926  186 RVGNLEYamtHDKLVAGG--SWRLIHGRDIVAHIP 218
Cdd:PLN03037 358 RVGNLAF---KEKLNELGvkVLRVVNKQDIVPKLP 389
PLN02934 PLN02934
triacylglycerol lipase
 138-219 6.97e-07

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 50.55  E-value: 6.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  138 LKDSLPDH---KIVFTGHSLGGAIASIASTVFVRNFP-ETSSRTFSI-TFGQPRVGNLEYAM---THDKLVAGGSWRLIH 209
Cdd:PLN02934 311 LKSLLKEHknaKFVVTGHSLGGALAILFPTVLVLQEEtEVMKRLLGVyTFGQPRIGNRQLGKfmeAQLNYPVPRYFRVVY 390

                         90
                 ....*....|
gi 25150926  210 GRDIVAHIPF 219
Cdd:PLN02934 391 CNDLVPRLPY 400
PLN02454 PLN02454
triacylglycerol lipase
 121-218 9.12e-07

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 49.84  E-value: 9.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  121 YSALKTMWSPMEKLLRGLKDSLPdhKIVFTGHSLGGAIASIASTVFVRNfpETSSRTFSIT---FGQPRVGNLEYamtHD 197
Cdd:PLN02454 206 LSARSQLLAKIKELLERYKDEKL--SIVLTGHSLGASLATLAAFDIVEN--GVSGADIPVTaivFGSPQVGNKEF---ND 278

                         90       100
                 ....*....|....*....|....
gi 25150926  198 KLVAGGSWRLIHGR---DIVAHIP 218
Cdd:PLN02454 279 RFKEHPNLKILHVRntiDLIPHYP 302
PLN02162 PLN02162
triacylglycerol lipase
 76-219 1.92e-06

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 48.89  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926   76 AADNDTIFVSFSGTKSKEqlVTELIESIGRPKHKLHNAGSVHYYFYSAL-----------------KTMWSPMEKLLRGL 138
Cdd:PLN02162 194 STNPDLIVVSFRGTEPFE--AADWCTDLDLSWYELKNVGKVHAGFSRALglqkdggwpkenisllhQYAYYTIRQMLRDK 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  139 KDSLPDHKIVFTGHSLGGAIASIASTVF-VRNFPETSSRTFSI-TFGQPRVGNLEYAMTHDKLVAGGSW---RLIHGRDI 213
Cdd:PLN02162 272 LARNKNLKYILTGHSLGGALAALFPAILaIHGEDELLDKLEGIyTFGQPRVGDEDFGEFMKGVVKKHGIeyeRFVYNNDV 351


                 ....*.
gi 25150926  214 VAHIPF 219
Cdd:PLN02162 352 VPRVPF 357
PLN02802 PLN02802
triacylglycerol lipase
 147-218 1.90e-04

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 42.84  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150926  147 IVFTGHSLGGAIAS-IASTVFVRNFPETSSRTFSitFGQPRVGNLEYAmthDKLVAGGS--WRLIHGRDIVAHIP 218
Cdd:PLN02802 332 ITVTGHSLGAALALlVADELATCVPAAPPVAVFS--FGGPRVGNRAFA---DRLNARGVkvLRVVNAQDVVTRVP 401
PLN02761 PLN02761
lipase class 3 family protein
 121-243 2.27e-04

lipase class 3 family protein


Pssm-ID: 215406 [Multi-domain]  Cd Length: 527  Bit Score: 42.72  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  121 YSALKTMWSPMEKLLRGLKDSLPDHK--IVFTGHSLGGAIASIA----STVFVRNFPETSSR----TFSitFGQPRVGNL 190
Cdd:PLN02761 268 FSAREQVLAEVKRLVEYYGTEEEGHEisITVTGHSLGASLALVSaydiAELNLNHVPENNYKipitVFS--FSGPRVGNL 345

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150926  191 EYAMTHDKLvAGGSWRLIHGRDIVAHIP-------FCVESYARWCIPFynHGSYHH-GVEV 243
Cdd:PLN02761 346 RFKERCDEL-GVKVLRVVNVHDKVPSVPgiftnekFQFQKYVEEKTSF--PWSYAHvGVEL 403
PLN02324 PLN02324
triacylglycerol lipase
 122-254 4.41e-04

triacylglycerol lipase


Pssm-ID: 177958  Cd Length: 415  Bit Score: 41.54  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926  122 SALKTMWSPMEKLLRGLKDSlpDHKIVFTGHSLGGAIASIASTVFVRN-----FPETSSRTFSIT---FGQPRVGNLEYA 193
Cdd:PLN02324 194 SAQEQVQGELKRLLELYKNE--EISITFTGHSLGAVMSVLSAADLVYGkknkiNISLQKKQVPITvfaFGSPRIGDHNFK 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150926  194 MTHDKLVAGGSWRLIHGRDIVAHIPFCV--------------ESYARWCIPFYNhgsyHHGVEVWFPGNMTSQDT 254
Cdd:PLN02324 272 NLVDSLQPLNILRIVNVPDVAPHYPLLLyteigevleintlnSTYLKRSLNFRN----YHNLEAYLHGVAGMQDT 342
PLN02310 PLN02310
triacylglycerol lipase
 82-218 9.90e-04

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 40.35  E-value: 9.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150926   82 IFVSFSGTKSKEQLVTEL---IESIGRPK-------HKLHNAG--SVHYYFYSALKTMWSPMEKLLRGLKDSLPDHKIVF 149
Cdd:PLN02310 134 IMVAWRGTVAPSEWFLDLetkLEHIDNTNvkvqegfLKIYKSKdeSTRYNKLSASEQVMQEVKRLVNFYRGKGEEVSLTV 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150926  150 TGHSLGGAIASIASTVFVRNFPETSSRTfsITFGQPRVGNLEYamtHDKLVAGG--SWRLIHGRDIVAHIP 218
Cdd:PLN02310 214 TGHSLGGALALLNAYEAATTIPDLFVSV--ISFGAPRVGNIAF---KEKLNELGvkTLRVVVKQDKVPKLP 279
PLN02408 PLN02408
phospholipase A1
 147-218 9.94e-04

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 40.20  E-value: 9.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150926  147 IVFTGHSLGGAIASIASTVFVRNFPETSSRTfSITFGQPRVGNLEYAMTHDKlvAGGS-WRLIHGRDIVAHIP 218
Cdd:PLN02408 202 LTITGHSLGAALATLTAYDIKTTFKRAPMVT-VISFGGPRVGNRSFRRQLEK--QGTKvLRIVNSDDVITKVP 271
 
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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