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Conserved domains on  [gi|373254158|emb|CCD67058|]
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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:0016787|GO:0006629
PubMed:  19508187|12369917|9379946|9704093
SCOP:  3000102

Graphical summary

 Zoom to residue level

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Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
129-266 3.96e-59

Lipase (class 3);


:

Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 186.31  E-value: 3.96e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  129 VMSFRGTDSPLQLTDEILDFFTGKKQFFPDAGNIFTYFYDAFFfLWNAGLQQDIRQLKYKYPDYELWVVGHSLGGAIASV 208
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 373254158  209 AASYVVHTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPY-SFRIVHHKDIVPHIPPQ 266
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPI 138
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
129-266 3.96e-59

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 186.31  E-value: 3.96e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  129 VMSFRGTDSPLQLTDEILDFFTGKKQFFPDAGNIFTYFYDAFFfLWNAGLQQDIRQLKYKYPDYELWVVGHSLGGAIASV 208
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 373254158  209 AASYVVHTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPY-SFRIVHHKDIVPHIPPQ 266
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPI 138
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 71-287 6.25e-51

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: 168.42  E-value: 6.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  71 TKIVPMTAAANNVNPEKCFKSRI-PTMSISKTFSTNC-SEVGPQSNCFGFTSFDTTQKVLVMSFRGTDSPLQLTDEILDF 148
Cdd:cd00519    6 KYYAKLAAAAYCVDANILAKAVVfADIALLNVFSPDKlLKTDKQYDTQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 149 FTGKKQFFPDAGNIFTYFYDAFFFLWNAGLQQDIRQLKyKYPDYELWVVGHSLGGAIASVAASYVVHTGLftGDKVKLVT 228
Cdd:cd00519   86 PVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSALK-QYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDVTVYT 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373254158 229 MGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIPPQEGADK--LFHHRTEVWYNNNMTT 287
Cdd:cd00519  163 FGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTPPegYTHVGTEVWIDHLPYF 223
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
116-317 1.60e-28

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 111.00  E-value: 1.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 116 FGFTSFDttQKVLVMSFRGTDSplqLTDEI--LDFFTGKKQFFPDAGNIFTYFYDAFFFLWnAGLQQDIRQLkykYPDYE 193
Cdd:COG3675   19 FGFILRS--DDEVIVAFRGTES---LTDWLtnLNAAQVPYPFAKTGGKVHRGFYRALQSLR-ELLEDALRPL---SPGKR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 194 LWVVGHSLGGAIASVAASYVVHTGLFTgdKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIPPQEGADKlf 273
Cdd:COG3675   90 LYVTGHSLGGALATLAAADLERNYIFP--VRGLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMGYD-- 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 373254158 274 HHRTEVWYNNNMTTTDPYHicaeadglYCSNRQLDTDIPDHLTY 317
Cdd:COG3675  166 HVGKLLWLDSLRKDMLTDH--------SMDNYIHHTDLSQLLTY 201
PLN02802 PLN02802
triacylglycerol lipase
 180-265 1.78e-06

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 49.38  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 180 QDIRQL--KYKYPDYELWVVGHSLGGAIASVAASYVVhTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVHHK 257
Cdd:PLN02802 316 GEVRRLmeKYKGEELSITVTGHSLGAALALLVADELA-TCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQ 394


                 ....*...
gi 373254158 258 DIVPHIPP 265
Cdd:PLN02802 395 DVVTRVPG 402
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
129-266 3.96e-59

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 186.31  E-value: 3.96e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  129 VMSFRGTDSPLQLTDEILDFFTGKKQFFPDAGNIFTYFYDAFFfLWNAGLQQDIRQLKYKYPDYELWVVGHSLGGAIASV 208
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 373254158  209 AASYVVHTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPY-SFRIVHHKDIVPHIPPQ 266
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPI 138
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 71-287 6.25e-51

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: 168.42  E-value: 6.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  71 TKIVPMTAAANNVNPEKCFKSRI-PTMSISKTFSTNC-SEVGPQSNCFGFTSFDTTQKVLVMSFRGTDSPLQLTDEILDF 148
Cdd:cd00519    6 KYYAKLAAAAYCVDANILAKAVVfADIALLNVFSPDKlLKTDKQYDTQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 149 FTGKKQFFPDAGNIFTYFYDAFFFLWNAGLQQDIRQLKyKYPDYELWVVGHSLGGAIASVAASYVVHTGLftGDKVKLVT 228
Cdd:cd00519   86 PVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSALK-QYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDVTVYT 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373254158 229 MGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIPPQEGADK--LFHHRTEVWYNNNMTT 287
Cdd:cd00519  163 FGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTPPegYTHVGTEVWIDHLPYF 223
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 165-318 1.21e-37

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: 131.47  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 165 YFYDAFFFLWNAgLQQDIRQLKYKYPDYELWVVGHSLGGAIASVAASYVVHTGLftGDKVKLVTMGQPRTGDYDYA--TW 242
Cdd:cd00741    2 GFYKAARSLANL-VLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGL--GRLVRVYTFGPPRVGNAAFAedRL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373254158 243 HDKTFPYSFRIVHHKDIVPHIPPqeGADKLFHHRTEVWYNNNMTTTDPYHICAEA-DGLYCSNRQLDTDIPDHLTYF 318
Cdd:cd00741   79 DPSDALFVDRIVNDNDIVPRLPP--GGEGYPHGGAEFYINGGKSQPGCCKNVLEAvDIDFGNIGLSGNGLCDHLRYF 153
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
116-317 1.60e-28

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 111.00  E-value: 1.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 116 FGFTSFDttQKVLVMSFRGTDSplqLTDEI--LDFFTGKKQFFPDAGNIFTYFYDAFFFLWnAGLQQDIRQLkykYPDYE 193
Cdd:COG3675   19 FGFILRS--DDEVIVAFRGTES---LTDWLtnLNAAQVPYPFAKTGGKVHRGFYRALQSLR-ELLEDALRPL---SPGKR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 194 LWVVGHSLGGAIASVAASYVVHTGLFTgdKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIPPQEGADKlf 273
Cdd:COG3675   90 LYVTGHSLGGALATLAAADLERNYIFP--VRGLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMGYD-- 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 373254158 274 HHRTEVWYNNNMTTTDPYHicaeadglYCSNRQLDTDIPDHLTY 317
Cdd:COG3675  166 HVGKLLWLDSLRKDMLTDH--------SMDNYIHHTDLSQLLTY 201
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 117-235 1.27e-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: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 117 GFTSFDTTQKVL---VMSFRGTDS-PLQLTD--EIL-DFF----TGKKQFFPDAGNIFTYFYDAFFFLWNAGLQQDIRQL 185
Cdd:COG5153   33 GHFAVALDEKAIydtIIAFRGTQGkPDWKTDinASLhDYDeknkEADEKLPLQVHEGFEQYAAQVMDLDYDGAEELAAEV 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 373254158 186 KYKYPDYELWVVGHSLGGAIASVAAsyvVHTGLFTgdkvklVTMGQPRTG 235
Cdd:COG5153  113 KKQYPDAELSLTGHSLGGALASLVA---VATGLSK------VTFAAPGSG 153
PLN02802 PLN02802
triacylglycerol lipase
 180-265 1.78e-06

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 49.38  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 180 QDIRQL--KYKYPDYELWVVGHSLGGAIASVAASYVVhTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVHHK 257
Cdd:PLN02802 316 GEVRRLmeKYKGEELSITVTGHSLGAALALLVADELA-TCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQ 394


                 ....*...
gi 373254158 258 DIVPHIPP 265
Cdd:PLN02802 395 DVVTRVPG 402
PLN02162 PLN02162
triacylglycerol lipase
 113-264 2.26e-06

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 48.89  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 113 SNCFGFTSFDTTQKVLVMSFRGTDsPLQLTDEILDFFTGKKQFfPDAGNIFTYFYDAFFFLWNAGLQQDIRQLKYKYPDY 192
Cdd:PLN02162 185 TQAFVFKTSSTNPDLIVVSFRGTE-PFEAADWCTDLDLSWYEL-KNVGKVHAGFSRALGLQKDGGWPKENISLLHQYAYY 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 193 EL----------------WVVGHSLGGAIASV-AASYVVHTGLFTGDKVK-LVTMGQPRTGDYDYATWHD---KTFPYSF 251
Cdd:PLN02162 263 TIrqmlrdklarnknlkyILTGHSLGGALAALfPAILAIHGEDELLDKLEgIYTFGQPRVGDEDFGEFMKgvvKKHGIEY 342

                        170
                 ....*....|....
gi 373254158 252 -RIVHHKDIVPHIP 264
Cdd:PLN02162 343 eRFVYNNDVVPRVP 356
PLN00413 PLN00413
triacylglycerol lipase
 123-264 1.20e-05

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 46.55  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 123 TTQKVLVMSFRGTDsPLQLTDEILDFFTGKKQFFpDAGNIFTYFYDAFfflwnaGLQQD--------------------- 181
Cdd:PLN00413 197 DDPNLIIVSFRGTD-PFDADDWCTDLDLSWHEVK-NVGKIHGGFMKAL------GLPKEgwpeeinldetqnatsllayy 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 182 --IRQLKY---KYPDYELWVVGHSLGGAIASV-AASYVVHTGLFTGDKVKLV-TMGQPRTGDYDYATWHD---KTFPYSF 251
Cdd:PLN00413 269 tiLRHLKEifdQNPTSKFILSGHSLGGALAILfTAVLIMHDEEEMLERLEGVyTFGQPRVGDEDFGIFMKdklKEFDVKY 348

                        170
                 ....*....|....
gi 373254158 252 -RIVHHKDIVPHIP 264
Cdd:PLN00413 349 eRYVYCNDMVPRLP 362
PLN02408 PLN02408
phospholipase A1
 178-264 5.49e-05

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 44.44  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 178 LQQDIRQLKYKYPDYEL--WVVGHSLGGAIASVAAsYVVHTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVH 255
Cdd:PLN02408 184 VREEIARLLQSYGDEPLslTITGHSLGAALATLTA-YDIKTTFKRAPMVTVISFGGPRVGNRSFRRQLEKQGTKVLRIVN 262


                 ....*....
gi 373254158 256 HKDIVPHIP 264
Cdd:PLN02408 263 SDDVITKVP 271
PLN02719 PLN02719
triacylglycerol lipase
 79-264 8.05e-05

triacylglycerol lipase


Pssm-ID: 178321  Cd Length: 518  Bit Score: 44.31  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  79 AANNVNPEKCF-KSRIptmsiSKTFSTNCSEVG--PQSNCFGFTSFDTTQKVLVMSFRGTDSPLQLTDEILDFFTgkkqf 155
Cdd:PLN02719 168 ATSNINLPNFFsKSRW-----SKVWSKNANWIGyvAVSDDDEATRCRLGRRDIAIAWRGTVTRLEWIADLKDFLK----- 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 156 fPDAGNIF----------TYFYDAF--------FFLWNAGLQ--QDIRQLKYKYPDYE-----LWVVGHSLGGAIASVAA 210
Cdd:PLN02719 238 -PVSGNGFrcpdpavkaeSGFLDLYtdkdtccnFSKFSAREQvlTEVKRLVERYGDEEgeelsITVTGHSLGGALAVLSA 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 373254158 211 SYVVHTGLFTGDKVKLV-----TMGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIP 264
Cdd:PLN02719 317 YDVAEMGLNRTRKGKVIpvtafTYGGPRVGNIRFKERIEELGVKVLRVVNEHDVVAKSP 375
PLN02753 PLN02753
triacylglycerol lipase
 79-264 1.04e-04

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 43.93  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  79 AANNVNPEKCF-KSRIptmsiSKTFSTNCSEVGPQSNCFGFTSFDTT-QKVLVMSFRGTDSPLQLTDEILDFF---TGKK 153
Cdd:PLN02753 183 ATSNINLPNFFsKSRW-----SKVWSKNANWMGYVAVSDDETSRNRLgRRDIAIAWRGTVTKLEWIADLKDYLkpvSENK 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 154 QFFPD-AGNIFTYFYDAF--------FFLWNAGLQ--QDIRQLKYKY-----PDYELWVVGHSLGGAIASVAASYVVHTG 217
Cdd:PLN02753 258 IRCPDpAVKVESGFLDLYtdkdttckFAKFSAREQilTEVKRLVEEHgddddSDLSITVTGHSLGGALAILSAYDIAEMG 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 373254158 218 LFTGDKVKLV-----TMGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIP 264
Cdd:PLN02753 338 LNRSKKGKVIpvtvlTYGGPRVGNVRFKDRMEELGVKVLRVVNVHDVVPKSP 389
PLN02934 PLN02934
triacylglycerol lipase
 196-282 1.34e-04

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 43.62  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 196 VVGHSLGGAIASVAAS-YVVHTGLFTGDKVKLV-TMGQPRTGDYDYATWHDKTFPYS----FRIVHHKDIVPHIPPQega 269
Cdd:PLN02934 325 VTGHSLGGALAILFPTvLVLQEETEVMKRLLGVyTFGQPRIGNRQLGKFMEAQLNYPvpryFRVVYCNDLVPRLPYD--- 401

                         90
                 ....*....|....*.
gi 373254158 270 DKLF---HHRTEVWYN 282
Cdd:PLN02934 402 DKTFlykHFGVCLYYD 417
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 194-264 1.63e-04

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 43.40  E-value: 1.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373254158 194 LWVVGHSLGGAIASVAAsYVVHTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIP 264
Cdd:PLN03037 320 LTITGHSLGGALALLNA-YEAARSVPALSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
PLN02571 PLN02571
triacylglycerol lipase
 112-265 2.11e-04

triacylglycerol lipase


Pssm-ID: 215309  Cd Length: 413  Bit Score: 42.57  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 112 QSNCFGFTSFDTTQ-------KVLVMSFRGTDSPLQLTDEILDFFTGKKQFFPDAGN----------IFTYFYDAFFFLW 174
Cdd:PLN02571 124 ESNWMGYVAVATDEgkallgrRDIVIAWRGTVQTLEWVNDFEFNLVSASKIFGESNDqpkvhqgwysIYTSDDERSPFNK 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 175 NAGLQQDIRQL-----KYKYPDYELWVVGHSLGGAIASVAASYVVHTGLFTGDK-------VKLVTMGQPRTGDYDYAtw 242
Cdd:PLN02571 204 TSARDQVLNEVgrlveKYKDEEISITICGHSLGAALATLNAVDIVANGFNRSKSrpnkscpVTAFVFASPRVGDSDFK-- 281

                        170       180
                 ....*....|....*....|....*...
gi 373254158 243 hdKTFP-----YSFRIVHHKDIVPHIPP 265
Cdd:PLN02571 282 --KLFSglkdlRVLRVRNLPDVIPNYPL 307
PLN02310 PLN02310
triacylglycerol lipase
 113-264 2.76e-04

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 42.28  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 113 SNCFGFTSF---DTTQKV----LVMSFRGTDSPlqlTDEILDFFTGKKQFfpDAGNI-----FTYFYDAF--------FF 172
Cdd:PLN02310 112 SNWMGYVAVsrdEESQRIgrrdIMVAWRGTVAP---SEWFLDLETKLEHI--DNTNVkvqegFLKIYKSKdestrynkLS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 173 LWNAGLQQDIRQLKY---KYPDYELWVVGHSLGGAIASVAA--SYVVHTGLFtgdkVKLVTMGQPRTGDYDYATWHDKTF 247
Cdd:PLN02310 187 ASEQVMQEVKRLVNFyrgKGEEVSLTVTGHSLGGALALLNAyeAATTIPDLF----VSVISFGAPRVGNIAFKEKLNELG 262

                        170
                 ....*....|....*..
gi 373254158 248 PYSFRIVHHKDIVPHIP 264
Cdd:PLN02310 263 VKTLRVVVKQDKVPKLP 279
PLN02454 PLN02454
triacylglycerol lipase
 178-264 2.80e-04

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 42.52  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158 178 LQQDIRQLKYKYPDYELWVV--GHSLGGAIASVAASYVVHTGLFTGD-KVKLVTMGQPRTGDYDYatwHDKTFPYS-FRI 253
Cdd:PLN02454 212 LLAKIKELLERYKDEKLSIVltGHSLGASLATLAAFDIVENGVSGADiPVTAIVFGSPQVGNKEF---NDRFKEHPnLKI 288

                         90
                 ....*....|....
gi 373254158 254 VHHK---DIVPHIP 264
Cdd:PLN02454 289 LHVRntiDLIPHYP 302
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
179-211 3.95e-03

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 38.33  E-value: 3.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 373254158 179 QQD----IRQLKYKYPDYELWVVGHSLGGAIASVAAS 211
Cdd:COG4757   90 ELDlpavLDALRARFPGLPLLLVGHSLGGQLLGLAPN 126
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 196-298 5.00e-03

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 37.84  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373254158  196 VVGHSLGGAIASVAASYVVHTGLFTGDKVKLVTMGQPRTGDYDYATWHDKTFPYSFRIVHHKDIVPHIPPQEGADKLFHH 275
Cdd:pfam12697  63 LVGHSLGGAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALAR 142

                          90       100       110
                  ....*....|....*....|....*....|
gi 373254158  276 RTEVWYNNNMTTTD-------PYHICAEAD 298
Cdd:pfam12697 143 LAALLAALALLPLAawrdlpvPVLVLAEED 172
 
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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