|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
131-269 |
6.71e-63 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 196.33 E-value: 6.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 131 VMSFRGTQGATQLTEEILDFFTGKKPFFNDAGHIFTYFYDAFFfLWNGGLQQEIRRLKYQYPEYELWVTGHSLGGAIASI 210
Cdd:pfam01764 1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 211 AASYVVHSGLYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPY-SFRIVHHRDIVPHIPPQY 269
Cdd:pfam01764 80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
80-287 |
1.77e-54 |
|
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: 178.05 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 80 AAAFNNNPQKCFKNSM-PTMTLSKTFSVNC-SEVGPQTDCFGFTSFDTTQKVVVMSFRGTQGATQLTEEILDFFTGKKPF 157
Cdd:cd00519 13 AAAYCVDANILAKAVVfADIALLNVFSPDKlLKTDKQYDTQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFSPVPLDPP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 158 FNDAGHIFTYFYDAFFFLWNGGLQqEIRRLKYQYPEYELWVTGHSLGGAIASIAASYVVHSGLytGDQVKLVTMGQPRTG 237
Cdd:cd00519 93 LCSGGKVHSGFYSAYKSLYNQVLP-ELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDVTVYTFGQPRVG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30145767 238 DYDYAVWHDKTFPYSFRIVHHRDIVPHIPPQYGKDE--LFHHRTEVWYNNNM 287
Cdd:cd00519 170 NAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTPPegYTHVGTEVWIDHLP 221
|
|
| Lip2 |
COG3675 |
Predicted lipase [Lipid transport and metabolism]; |
113-293 |
5.08e-30 |
|
Predicted lipase [Lipid transport and metabolism];
Pssm-ID: 442891 [Multi-domain] Cd Length: 266 Bit Score: 115.24 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 113 PQTDCFGFTSFDttQKVVVMSFRGTQGATQLTEEiLDFFTGKKPFFNDAGHIFTYFYDAFFFLWngglqQEIRR-LKYQY 191
Cdd:COG3675 14 GDPEVFGFILRS--DDEVIVAFRGTESLTDWLTN-LNAAQVPYPFAKTGGKVHRGFYRALQSLR-----ELLEDaLRPLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 192 PEYELWVTGHSLGGAIASIAASYVVHSglYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPYSFRIVHHRDIVPHIPPQYGk 271
Cdd:COG3675 86 PGKRLYVTGHSLGGALATLAAADLERN--YIFPVRGLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWM- 162
|
170 180
....*....|....*....|..
gi 30145767 272 dELFHHRTEVWYNNNMSSTDPY 293
Cdd:COG3675 163 -GYDHVGKLLWLDSLRKDMLTD 183
|
|
| PLN02162 |
PLN02162 |
triacylglycerol lipase |
115-266 |
1.71e-08 |
|
triacylglycerol lipase
Pssm-ID: 177821 Cd Length: 475 Bit Score: 55.44 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 115 TDCFGFTSFDTTQKVVVMSFRGTQ---GATQLTEEILDFFTGKkpffnDAGHIFTYFYDAFFFLWNGGLQQEIRRLKYQY 191
Cdd:PLN02162 185 TQAFVFKTSSTNPDLIVVSFRGTEpfeAADWCTDLDLSWYELK-----NVGKVHAGFSRALGLQKDGGWPKENISLLHQY 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 192 PEYEL----------------WVTGHSLGGAIASI-AASYVVHSGLYTGDQVK-LVTMGQPRTGDYDY-----AVWHDKT 248
Cdd:PLN02162 260 AYYTIrqmlrdklarnknlkyILTGHSLGGALAALfPAILAIHGEDELLDKLEgIYTFGQPRVGDEDFgefmkGVVKKHG 339
|
170
....*....|....*...
gi 30145767 249 FPYSfRIVHHRDIVPHIP 266
Cdd:PLN02162 340 IEYE-RFVYNNDVVPRVP 356
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
131-269 |
6.71e-63 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 196.33 E-value: 6.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 131 VMSFRGTQGATQLTEEILDFFTGKKPFFNDAGHIFTYFYDAFFfLWNGGLQQEIRRLKYQYPEYELWVTGHSLGGAIASI 210
Cdd:pfam01764 1 VVAFRGTNSILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAYT-SVREQVLAELKRLLEKYPDYSIVVTGHSLGGALASL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 211 AASYVVHSGLYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPY-SFRIVHHRDIVPHIPPQY 269
Cdd:pfam01764 80 AALDLVENGLRLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPPIV 139
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
80-287 |
1.77e-54 |
|
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: 178.05 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 80 AAAFNNNPQKCFKNSM-PTMTLSKTFSVNC-SEVGPQTDCFGFTSFDTTQKVVVMSFRGTQGATQLTEEILDFFTGKKPF 157
Cdd:cd00519 13 AAAYCVDANILAKAVVfADIALLNVFSPDKlLKTDKQYDTQGYVAVDHDRKTIVIAFRGTVSLADWLTDLDFSPVPLDPP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 158 FNDAGHIFTYFYDAFFFLWNGGLQqEIRRLKYQYPEYELWVTGHSLGGAIASIAASYVVHSGLytGDQVKLVTMGQPRTG 237
Cdd:cd00519 93 LCSGGKVHSGFYSAYKSLYNQVLP-ELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDVTVYTFGQPRVG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30145767 238 DYDYAVWHDKTFPYSFRIVHHRDIVPHIPPQYGKDE--LFHHRTEVWYNNNM 287
Cdd:cd00519 170 NAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTPPegYTHVGTEVWIDHLP 221
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
167-320 |
1.63e-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: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 167 YFYDAFFFLWNGgLQQEIRRLKYQYPEYELWVTGHSLGGAIASIAASYVVHSGLytGDQVKLVTMGQPRTGDYDYAV--W 244
Cdd:cd00741 2 GFYKAARSLANL-VLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGL--GRLVRVYTFGPPRVGNAAFAEdrL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30145767 245 HDKTFPYSFRIVHHRDIVPHIPPqyGKDELFHHRTEVWYNNNMSSTDPYLICAEA-DGLYCSNRQLDSYPPDHLTYF 320
Cdd:cd00741 79 DPSDALFVDRIVNDNDIVPRLPP--GGEGYPHGGAEFYINGGKSQPGCCKNVLEAvDIDFGNIGLSGNGLCDHLRYF 153
|
|
| Lip2 |
COG3675 |
Predicted lipase [Lipid transport and metabolism]; |
113-293 |
5.08e-30 |
|
Predicted lipase [Lipid transport and metabolism];
Pssm-ID: 442891 [Multi-domain] Cd Length: 266 Bit Score: 115.24 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 113 PQTDCFGFTSFDttQKVVVMSFRGTQGATQLTEEiLDFFTGKKPFFNDAGHIFTYFYDAFFFLWngglqQEIRR-LKYQY 191
Cdd:COG3675 14 GDPEVFGFILRS--DDEVIVAFRGTESLTDWLTN-LNAAQVPYPFAKTGGKVHRGFYRALQSLR-----ELLEDaLRPLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 192 PEYELWVTGHSLGGAIASIAASYVVHSglYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPYSFRIVHHRDIVPHIPPQYGk 271
Cdd:COG3675 86 PGKRLYVTGHSLGGALATLAAADLERN--YIFPVRGLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWM- 162
|
170 180
....*....|....*....|..
gi 30145767 272 dELFHHRTEVWYNNNMSSTDPY 293
Cdd:COG3675 163 -GYDHVGKLLWLDSLRKDMLTD 183
|
|
| PLN02162 |
PLN02162 |
triacylglycerol lipase |
115-266 |
1.71e-08 |
|
triacylglycerol lipase
Pssm-ID: 177821 Cd Length: 475 Bit Score: 55.44 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 115 TDCFGFTSFDTTQKVVVMSFRGTQ---GATQLTEEILDFFTGKkpffnDAGHIFTYFYDAFFFLWNGGLQQEIRRLKYQY 191
Cdd:PLN02162 185 TQAFVFKTSSTNPDLIVVSFRGTEpfeAADWCTDLDLSWYELK-----NVGKVHAGFSRALGLQKDGGWPKENISLLHQY 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 192 PEYEL----------------WVTGHSLGGAIASI-AASYVVHSGLYTGDQVK-LVTMGQPRTGDYDY-----AVWHDKT 248
Cdd:PLN02162 260 AYYTIrqmlrdklarnknlkyILTGHSLGGALAALfPAILAIHGEDELLDKLEgIYTFGQPRVGDEDFgefmkGVVKKHG 339
|
170
....*....|....*...
gi 30145767 249 FPYSfRIVHHRDIVPHIP 266
Cdd:PLN02162 340 IEYE-RFVYNNDVVPRVP 356
|
|
| CVT17 |
COG5153 |
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ... |
116-212 |
2.89e-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: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 116 DCFGFTSFDTTQKVV---VMSFRGTQG----ATQLTEEILDFFTGKK---PFFNDAGHIFTYFYDAFFFLWNGGLQQEI- 184
Cdd:COG5153 30 DIDGHFAVALDEKAIydtIIAFRGTQGkpdwKTDINASLHDYDEKNKeadEKLPLQVHEGFEQYAAQVMDLDYDGAEELa 109
|
90 100
....*....|....*....|....*...
gi 30145767 185 RRLKYQYPEYELWVTGHSLGGAIASIAA 212
Cdd:COG5153 110 AEVKKQYPDAELSLTGHSLGGALASLVA 137
|
|
| PLN02802 |
PLN02802 |
triacylglycerol lipase |
182-294 |
9.85e-08 |
|
triacylglycerol lipase
Pssm-ID: 215432 Cd Length: 509 Bit Score: 53.24 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 182 QEIRRL--KYQYPEYELWVTGHSLGGAIASIAASYVVhSGLYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPYSFRIVHHR 259
Cdd:PLN02802 316 GEVRRLmeKYKGEELSITVTGHSLGAALALLVADELA-TCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQ 394
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 30145767 260 DIVPHIPPQYGKDELF-----HHRTEVWYNNNMSstdPYL 294
Cdd:PLN02802 395 DVVTRVPGIAPREELHkwayaHVGAELRLDSKMS---PYL 431
|
|
| PLN00413 |
PLN00413 |
triacylglycerol lipase |
114-266 |
4.44e-07 |
|
triacylglycerol lipase
Pssm-ID: 165792 Cd Length: 479 Bit Score: 51.17 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 114 QTDCFGFTS----FDTTQKVVVMSFRGTQGATQLteeILDFFTGKKPFFND---------------AGHIFTYFYDAFff 174
Cdd:PLN00413 168 KMDLLGFYScpndFDKQRSTEVIVIKDTKDDPNL---IIVSFRGTDPFDADdwctdldlswhevknVGKIHGGFMKAL-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 175 lwngGLQQE-----------------------IRRLKY---QYPEYELWVTGHSLGGAIASI-AASYVVHSGLYTGDQVK 227
Cdd:PLN00413 243 ----GLPKEgwpeeinldetqnatsllayytiLRHLKEifdQNPTSKFILSGHSLGGALAILfTAVLIMHDEEEMLERLE 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30145767 228 LV-TMGQPRTGDYDYAVWHD---KTFPYSF-RIVHHRDIVPHIP 266
Cdd:PLN00413 319 GVyTFGQPRVGDEDFGIFMKdklKEFDVKYeRYVYCNDMVPRLP 362
|
|
| PLN02408 |
PLN02408 |
phospholipase A1 |
130-266 |
2.16e-06 |
|
phospholipase A1
Pssm-ID: 215228 Cd Length: 365 Bit Score: 48.68 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 130 VVMSFRGTqgATQLteEILDFF-----------TGKKPFFNDAGHIFTyfyDAFFFLWNGG------LQQ----EIRRLK 188
Cdd:PLN02408 120 VVIAFRGT--ATCL--EWLENLratltrlpnapTDMNGSGDGSGPMVE---SGFLSLYTSGtamgpsLQEmvreEIARLL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 189 YQYPEYEL--WVTGHSLGGAIASIAAsYVVHSGLYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPYSFRIVHHRDIVPHIP 266
Cdd:PLN02408 193 QSYGDEPLslTITGHSLGAALATLTA-YDIKTTFKRAPMVTVISFGGPRVGNRSFRRQLEKQGTKVLRIVNSDDVITKVP 271
|
|
| PLN03037 |
PLN03037 |
lipase class 3 family protein; Provisional |
130-266 |
5.21e-06 |
|
lipase class 3 family protein; Provisional
Pssm-ID: 215547 Cd Length: 525 Bit Score: 48.03 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 130 VVMSFRGTQGATqltEEILDFFTGKKPFFNDAGHIFTYF--YDAFFFLWNGG--------------LQQEIRRL----KY 189
Cdd:PLN03037 237 IVVAWRGTVAPT---EWFMDLRTSLEPFDCDGDHGKNVVkvQSGFLSIYKSKseltrynklsaseqVMEEVKRLvnffKD 313
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30145767 190 QYPEYELWVTGHSLGGAIASIAAsYVVHSGLYTGDQVKLVTMGQPRTGDYDYAVWHDKTFPYSFRIVHHRDIVPHIP 266
Cdd:PLN03037 314 RGEEVSLTITGHSLGGALALLNA-YEAARSVPALSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
|
|
| PLN02571 |
PLN02571 |
triacylglycerol lipase |
183-267 |
1.75e-05 |
|
triacylglycerol lipase
Pssm-ID: 215309 Cd Length: 413 Bit Score: 46.03 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 183 EIRRL--KYQYPEYELWVTGHSLGGAIASIAASYVVHSGLYTGDQ-------VKLVTMGQPRTGDYDYAvwhdKTFP--- 250
Cdd:PLN02571 213 EVGRLveKYKDEEISITICGHSLGAALATLNAVDIVANGFNRSKSrpnkscpVTAFVFASPRVGDSDFK----KLFSglk 288
|
90
....*....|....*....
gi 30145767 251 --YSFRIVHHRDIVPHIPP 267
Cdd:PLN02571 289 dlRVLRVRNLPDVIPNYPL 307
|
|
| PLN02934 |
PLN02934 |
triacylglycerol lipase |
198-266 |
1.79e-05 |
|
triacylglycerol lipase
Pssm-ID: 215504 Cd Length: 515 Bit Score: 46.31 E-value: 1.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30145767 198 VTGHSLGGAIASIAAS-YVVHSGLYTGDQVKLV-TMGQPRTGDYDYAVWHDKTFPYS----FRIVHHRDIVPHIP 266
Cdd:PLN02934 325 VTGHSLGGALAILFPTvLVLQEETEVMKRLLGVyTFGQPRIGNRQLGKFMEAQLNYPvpryFRVVYCNDLVPRLP 399
|
|
| PLN02310 |
PLN02310 |
triacylglycerol lipase |
182-266 |
7.08e-05 |
|
triacylglycerol lipase
Pssm-ID: 215176 Cd Length: 405 Bit Score: 44.21 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 182 QEIRRLKYQY----PEYELWVTGHSLGGAIASIAA--SYVVHSGLYtgdqVKLVTMGQPRTGDYDYAVWHDKTFPYSFRI 255
Cdd:PLN02310 193 QEVKRLVNFYrgkgEEVSLTVTGHSLGGALALLNAyeAATTIPDLF----VSVISFGAPRVGNIAFKEKLNELGVKTLRV 268
|
90
....*....|.
gi 30145767 256 VHHRDIVPHIP 266
Cdd:PLN02310 269 VVKQDKVPKLP 279
|
|
| PLN02719 |
PLN02719 |
triacylglycerol lipase |
183-266 |
9.60e-05 |
|
triacylglycerol lipase
Pssm-ID: 178321 Cd Length: 518 Bit Score: 43.92 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 183 EIRRLKYQY-----PEYELWVTGHSLGGAIASIAASYVVHSGLYTGDQVKLV-----TMGQPRTGDYDYAVWHDKTFPYS 252
Cdd:PLN02719 282 EVKRLVERYgdeegEELSITVTGHSLGGALAVLSAYDVAEMGLNRTRKGKVIpvtafTYGGPRVGNIRFKERIEELGVKV 361
|
90
....*....|....
gi 30145767 253 FRIVHHRDIVPHIP 266
Cdd:PLN02719 362 LRVVNEHDVVAKSP 375
|
|
| PLN02753 |
PLN02753 |
triacylglycerol lipase |
183-266 |
1.23e-04 |
|
triacylglycerol lipase
Pssm-ID: 178354 Cd Length: 531 Bit Score: 43.55 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 183 EIRRLKYQY-----PEYELWVTGHSLGGAIASIAASYVVHSGLYTGDQVKLV-----TMGQPRTGDYDYAVWHDKTFPYS 252
Cdd:PLN02753 296 EVKRLVEEHgddddSDLSITVTGHSLGGALAILSAYDIAEMGLNRSKKGKVIpvtvlTYGGPRVGNVRFKDRMEELGVKV 375
|
90
....*....|....
gi 30145767 253 FRIVHHRDIVPHIP 266
Cdd:PLN02753 376 LRVVNVHDVVPKSP 389
|
|
| PLN02324 |
PLN02324 |
triacylglycerol lipase |
180-266 |
1.78e-04 |
|
triacylglycerol lipase
Pssm-ID: 177958 Cd Length: 415 Bit Score: 43.08 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 180 LQQEIRRLK--YQYPEYELWVTGHSLGGAIASIAASYVVH---SGLYTGDQVKLVTM-----GQPRTGDYDYAVWHDKTF 249
Cdd:PLN02324 199 VQGELKRLLelYKNEEISITFTGHSLGAVMSVLSAADLVYgkkNKINISLQKKQVPItvfafGSPRIGDHNFKNLVDSLQ 278
|
90
....*....|....*...
gi 30145767 250 PYS-FRIVHHRDIVPHIP 266
Cdd:PLN02324 279 PLNiLRIVNVPDVAPHYP 296
|
|
| PLN02454 |
PLN02454 |
triacylglycerol lipase |
180-266 |
3.57e-04 |
|
triacylglycerol lipase
Pssm-ID: 215249 Cd Length: 414 Bit Score: 42.13 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30145767 180 LQQEIRRLKYQYPEYELWV--TGHSLGGAIASIAASYVVHSGLYTGD-QVKLVTMGQPRTGDYDYavwHDKTFPYS-FRI 255
Cdd:PLN02454 212 LLAKIKELLERYKDEKLSIvlTGHSLGASLATLAAFDIVENGVSGADiPVTAIVFGSPQVGNKEF---NDRFKEHPnLKI 288
|
90
....*....|....
gi 30145767 256 VHHR---DIVPHIP 266
Cdd:PLN02454 289 LHVRntiDLIPHYP 302
|
|
|