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Conserved domains on  [gi|308249926|gb|EFO93878|]
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hypothetical protein CRE_12782 [Caenorhabditis remanei]

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);
93-230 9.17e-58

Lipase (class 3);


:

Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 181.69  E-value: 9.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926   93 VISFRGTQGFLQLIEEADKSVFQSQSQWIAGGKVSKYFGDAFnTLWNAGMKDDVNNLIHKYPTFEVWVTGHSLGGSMASL 172
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAY-TSVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 308249926  173 AASYIVANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAY-SYRVTHNRDIVPHIPNE 230
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPI 138
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
93-230 9.17e-58

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 181.69  E-value: 9.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926   93 VISFRGTQGFLQLIEEADKSVFQSQSQWIAGGKVSKYFGDAFnTLWNAGMKDDVNNLIHKYPTFEVWVTGHSLGGSMASL 172
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAY-TSVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 308249926  173 AASYIVANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAY-SYRVTHNRDIVPHIPNE 230
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPI 138
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 35-244 2.44e-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: 163.42  E-value: 2.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  35 NTFFPLAAAAYSSNPQTCLSAKFTNSQ--LRRQLNVQCDAGGKNDICSAYTALLPDNKAIVISFRGTQGFLQLIEEADKS 112
Cdd:cd00519    6 KYYAKLAAAAYCVDANILAKAVVFADIalLNVFSPDKLLKTDKQYDTQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 113 VFQSQSQWIAGGKVSKYFGDAFNTLWNAGMKDDVNNLiHKYPTFEVWVTGHSLGGSMASLAASYIVANKivTGDKVKLIT 192
Cdd:cd00519   86 PVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSAL-KQYPDYKIIVTGHSLGGALASLLALDLRLRG--PGSDVTVYT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 308249926 193 YGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIP---NEGMEDYKHHKAEVFY 244
Cdd:cd00519  163 FGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPpgsLTPPEGYTHVGTEVWI 217
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
88-237 1.67e-29

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 112.93  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  88 DNKAIVISFRGTQGFLQLIeeADKSVFQ-SQSQWIAGGKVSKYFGDAFNTLWnAGMKDDVNNLihkYPTFEVWVTGHSLG 166
Cdd:COG3675   25 SDDEVIVAFRGTESLTDWL--TNLNAAQvPYPFAKTGGKVHRGFYRALQSLR-ELLEDALRPL---SPGKRLYVTGHSLG 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308249926 167 GSMASLAASYIVANKIvtgDKVK-LITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIPNEGMEdYKH 237
Cdd:COG3675   99 GALATLAAADLERNYI---FPVRgLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMG-YDH 166
PLN02162 PLN02162
triacylglycerol lipase
 92-238 1.62e-07

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 52.35  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  92 IVISFRGTQGFlqliEEAD--KSVFQSQSQWIAGGKVSKYFGDAFNTLWNAGMKDDVNNLIHKYPTFEV----------- 158
Cdd:PLN02162 200 IVVSFRGTEPF----EAADwcTDLDLSWYELKNVGKVHAGFSRALGLQKDGGWPKENISLLHQYAYYTIrqmlrdklarn 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 159 -----WVTGHSLGGSMASL-AASYIVANKIVTGDKVKLI-TYGQPRTGTTPF-----AVAHDAQMAYSyRVTHNRDIVPH 226
Cdd:PLN02162 276 knlkyILTGHSLGGALAALfPAILAIHGEDELLDKLEGIyTFGQPRVGDEDFgefmkGVVKKHGIEYE-RFVYNNDVVPR 354

                        170
                 ....*....|....
gi 308249926 227 IP--NEGMEDYKHH 238
Cdd:PLN02162 355 VPfdDKLLFSYKHY 368
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
93-230 9.17e-58

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 181.69  E-value: 9.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926   93 VISFRGTQGFLQLIEEADKSVFQSQSQWIAGGKVSKYFGDAFnTLWNAGMKDDVNNLIHKYPTFEVWVTGHSLGGSMASL 172
Cdd:pfam01764   1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAY-TSVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 308249926  173 AASYIVANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAY-SYRVTHNRDIVPHIPNE 230
Cdd:pfam01764  80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPI 138
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 35-244 2.44e-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: 163.42  E-value: 2.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  35 NTFFPLAAAAYSSNPQTCLSAKFTNSQ--LRRQLNVQCDAGGKNDICSAYTALLPDNKAIVISFRGTQGFLQLIEEADKS 112
Cdd:cd00519    6 KYYAKLAAAAYCVDANILAKAVVFADIalLNVFSPDKLLKTDKQYDTQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 113 VFQSQSQWIAGGKVSKYFGDAFNTLWNAGMKDDVNNLiHKYPTFEVWVTGHSLGGSMASLAASYIVANKivTGDKVKLIT 192
Cdd:cd00519   86 PVPLDPPLCSGGKVHSGFYSAYKSLYNQVLPELKSAL-KQYPDYKIIVTGHSLGGALASLLALDLRLRG--PGSDVTVYT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 308249926 193 YGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIP---NEGMEDYKHHKAEVFY 244
Cdd:cd00519  163 FGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPpgsLTPPEGYTHVGTEVWI 217
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 128-283 1.55e-34

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: 122.61  E-value: 1.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 128 KYFGDAFNTLWNAGMKDdVNNLIHKYPTFEVWVTGHSLGGSMASLAASYIVANKivTGDKVKLITYGQPRTGTTPFAV-- 205
Cdd:cd00741    1 KGFYKAARSLANLVLPL-LKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRG--LGRLVRVYTFGPPRVGNAAFAEdr 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308249926 206 AHDAQMAYSYRVTHNRDIVPHIPNEGMeDYKHHKAEVFYKESMKAGATFKVCSSADESNDCSNGLLITaSVSDHLTYF 283
Cdd:cd00741   78 LDPSDALFVDRIVNDNDIVPRLPPGGE-GYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGN-GLCDHLRYF 153
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
88-237 1.67e-29

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 112.93  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  88 DNKAIVISFRGTQGFLQLIeeADKSVFQ-SQSQWIAGGKVSKYFGDAFNTLWnAGMKDDVNNLihkYPTFEVWVTGHSLG 166
Cdd:COG3675   25 SDDEVIVAFRGTESLTDWL--TNLNAAQvPYPFAKTGGKVHRGFYRALQSLR-ELLEDALRPL---SPGKRLYVTGHSLG 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308249926 167 GSMASLAASYIVANKIvtgDKVK-LITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIPNEGMEdYKH 237
Cdd:COG3675   99 GALATLAAADLERNYI---FPVRgLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMG-YDH 166
PLN02162 PLN02162
triacylglycerol lipase
 92-238 1.62e-07

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 52.35  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  92 IVISFRGTQGFlqliEEAD--KSVFQSQSQWIAGGKVSKYFGDAFNTLWNAGMKDDVNNLIHKYPTFEV----------- 158
Cdd:PLN02162 200 IVVSFRGTEPF----EAADwcTDLDLSWYELKNVGKVHAGFSRALGLQKDGGWPKENISLLHQYAYYTIrqmlrdklarn 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 159 -----WVTGHSLGGSMASL-AASYIVANKIVTGDKVKLI-TYGQPRTGTTPF-----AVAHDAQMAYSyRVTHNRDIVPH 226
Cdd:PLN02162 276 knlkyILTGHSLGGALAALfPAILAIHGEDELLDKLEGIyTFGQPRVGDEDFgefmkGVVKKHGIEYE-RFVYNNDVVPR 354

                        170
                 ....*....|....
gi 308249926 227 IP--NEGMEDYKHH 238
Cdd:PLN02162 355 VPfdDKLLFSYKHY 368
PLN02802 PLN02802
triacylglycerol lipase
 92-228 1.71e-07

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 52.08  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  92 IVISFRGTQGFLQLIE---------EADKSVFQSQSQwiagGKVSKYFGDAFNTlwnAGMK---------DDVNNLIHKY 153
Cdd:PLN02802 253 IVIALRGTATCLEWAEnlraglvpmPGDDDDAGDQEQ----PKVECGFLSLYKT---AGAHvpslsesvvGEVRRLMEKY 325

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308249926 154 P--TFEVWVTGHSLGGSMASLAASYIvANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIP 228
Cdd:PLN02802 326 KgeELSITVTGHSLGAALALLVADEL-ATCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQDVVTRVP 401
PLN02934 PLN02934
triacylglycerol lipase
 88-244 3.72e-07

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 50.94  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  88 DNKAIVISFRGTQ--------------------------GFLQ---LIEEADKSVFQSQSQWIAGGKVSKYFGDAFNTLW 138
Cdd:PLN02934 219 DANLIVISFRGTEpfdaddwgtdfdyswyeipkvgkvhmGFLEamgLGNRDDTTTFQTSLQTKATSELKEEESKKNLLEM 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 139 nagMKDDVNNLI----------HKYPTFEVwvTGHSLGGSMASLAASYIVAN--KIVTGDKVKLITYGQPRTGTTPFAVA 206
Cdd:PLN02934 299 ---VERSAYYAVrsklksllkeHKNAKFVV--TGHSLGGALAILFPTVLVLQeeTEVMKRLLGVYTFGQPRIGNRQLGKF 373

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 308249926 207 HDAQMAYS----YRVTHNRDIVPHIP-NEGMEDYKHHKAEVFY 244
Cdd:PLN02934 374 MEAQLNYPvpryFRVVYCNDLVPRLPyDDKTFLYKHFGVCLYY 416
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 160-228 6.32e-07

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 50.34  E-value: 6.32e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308249926 160 VTGHSLGGSMASLAAsYIVANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIP 228
Cdd:PLN03037 322 ITGHSLGGALALLNA-YEAARSVPALSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
PLN02454 PLN02454
triacylglycerol lipase
 146-228 1.98e-06

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 48.68  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 146 VNNLIHKYP--TFEVWVTGHSLGGSMASLAASYIVANKIVTGD-KVKLITYGQPRTGTTPFavaHDAQMAYS-YRVTHNR 221
Cdd:PLN02454 216 IKELLERYKdeKLSIVLTGHSLGASLATLAAFDIVENGVSGADiPVTAIVFGSPQVGNKEF---NDRFKEHPnLKILHVR 292

                         90
                 ....*....|
gi 308249926 222 ---DIVPHIP 228
Cdd:PLN02454 293 ntiDLIPHYP 302
PLN02408 PLN02408
phospholipase A1
 92-228 2.50e-06

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 48.29  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  92 IVISFRGTQGFLQLIEEADKSVFQ---SQSQWIAGGKVSKYFGDA-FNTLWNAG----------MKDDVNNLIHKY--PT 155
Cdd:PLN02408 120 VVIAFRGTATCLEWLENLRATLTRlpnAPTDMNGSGDGSGPMVESgFLSLYTSGtamgpslqemVREEIARLLQSYgdEP 199

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308249926 156 FEVWVTGHSLGGSMASLAAsYIVANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIP 228
Cdd:PLN02408 200 LSLTITGHSLGAALATLTA-YDIKTTFKRAPMVTVISFGGPRVGNRSFRRQLEKQGTKVLRIVNSDDVITKVP 271
PLN02571 PLN02571
triacylglycerol lipase
 92-234 1.61e-05

triacylglycerol lipase


Pssm-ID: 215309  Cd Length: 413  Bit Score: 46.03  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  92 IVISFRGTQGFLQLIEE-------ADKSVFQSQSQ-WIAGGKVSKYFGDAFNTLWN-AGMKDDVNN----LIHKYPTFEV 158
Cdd:PLN02571 147 IVIAWRGTVQTLEWVNDfefnlvsASKIFGESNDQpKVHQGWYSIYTSDDERSPFNkTSARDQVLNevgrLVEKYKDEEI 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 159 WVT--GHSLGGSMASLAASYIVAN----KIVTGDK---VKLITYGQPRTGTTPFAVAHDAQMAYSYRVTHN-RDIVPHIP 228
Cdd:PLN02571 227 SITicGHSLGAALATLNAVDIVANgfnrSKSRPNKscpVTAFVFASPRVGDSDFKKLFSGLKDLRVLRVRNlPDVIPNYP 306


                 ....*.
gi 308249926 229 NEGMED 234
Cdd:PLN02571 307 LIGYSD 312
PLN02310 PLN02310
triacylglycerol lipase
 160-228 3.21e-05

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 44.98  E-value: 3.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308249926 160 VTGHSLGGSMASLAASYivANKIVTGDKVKLITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIP 228
Cdd:PLN02310 213 VTGHSLGGALALLNAYE--AATTIPDLFVSVISFGAPRVGNIAFKEKLNELGVKTLRVVVKQDKVPKLP 279
PLN02753 PLN02753
triacylglycerol lipase
 101-238 3.48e-05

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 45.09  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 101 GFLQLIEEADKSV----FQSQSQWIAGGK-VSKYFGDafntlwnagmkDDVNNLihkyptfEVWVTGHSLGGSMASLAAs 175
Cdd:PLN02753 270 GFLDLYTDKDTTCkfakFSAREQILTEVKrLVEEHGD-----------DDDSDL-------SITVTGHSLGGALAILSA- 330

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308249926 176 YIVANKIVTGDK------VKLITYGQPRTGTTPFAVAHDAQMAYSYRVTHNRDIVPHIPNEGMEDYKHH 238
Cdd:PLN02753 331 YDIAEMGLNRSKkgkvipVTVLTYGGPRVGNVRFKDRMEELGVKVLRVVNVHDVVPKSPGLFLNESRPH 399
PLN00413 PLN00413
triacylglycerol lipase
 88-249 4.50e-05

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 44.62  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  88 DNKAIVISFRGTQGFlqlieEADKSVFQSQSQWIAGGKVSKYFGDAFNTL------WNAGMKDD---------------- 145
Cdd:PLN00413 198 DPNLIIVSFRGTDPF-----DADDWCTDLDLSWHEVKNVGKIHGGFMKALglpkegWPEEINLDetqnatsllayytilr 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 146 -VNNLIHKYPTFEVWVTGHSLGGSMASLAASYIVANkivtgDKVKLI-------TYGQPRTGTTPFAVAHDAQMAySYRV 217
Cdd:PLN00413 273 hLKEIFDQNPTSKFILSGHSLGGALAILFTAVLIMH-----DEEEMLerlegvyTFGQPRVGDEDFGIFMKDKLK-EFDV 346

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 308249926 218 THNR-----DIVPHIP-NEGMEDYKHHKAEVFYKESMK 249
Cdd:PLN00413 347 KYERyvycnDMVPRLPfDDKTLMFKHFGACLYCDSFYK 384
PLN02719 PLN02719
triacylglycerol lipase
 145-228 6.31e-04

triacylglycerol lipase


Pssm-ID: 178321  Cd Length: 518  Bit Score: 41.23  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 145 DVNNLIHKYPTFE-----VWVTGHSLGGSMASLAAsYIVA----NKIVTGD--KVKLITYGQPRTGTTPFAVAHDAQMAY 213
Cdd:PLN02719 282 EVKRLVERYGDEEgeelsITVTGHSLGGALAVLSA-YDVAemglNRTRKGKviPVTAFTYGGPRVGNIRFKERIEELGVK 360

                         90
                 ....*....|....*
gi 308249926 214 SYRVTHNRDIVPHIP 228
Cdd:PLN02719 361 VLRVVNEHDVVAKSP 375
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 75-244 7.10e-04

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


Pssm-ID: 444061  Cd Length: 405  Bit Score: 40.77  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926  75 KNDICSAYTALLPDNKAI---VISFRGTQG-------FLQL--------IEEADKSVFQSQSQWiaggkvsKYFGDAFNT 136
Cdd:COG5153   27 ANDDIDGHFAVALDEKAIydtIIAFRGTQGkpdwktdINASlhdydeknKEADEKLPLQVHEGF-------EQYAAQVMD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308249926 137 LWNAGMKDDVNNLIHKYPTFEVWVTGHSLGGSMASLAA-----SYIVANKIVTGDKVKLITYGQP----RTGTTPFAVAH 207
Cdd:COG5153  100 LDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAvatglSKVTFAAPGSGNHALADDLGKRidagEFVKSLDAVAG 179

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 308249926 208 DAQMAYSYRVTHNRdiVPHIPNEGMEDYKHHKAEVFY 244
Cdd:COG5153  180 PGDSFFGGAFKQFG--HVGEFNHIGNDSGTAHPAKFT 214
 
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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