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Conserved domains on  [gi|723706771|ref|XP_010322272|]
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lipase [Solanum lycopersicum]

Protein Classification

lipase family protein( domain architecture ID 10087743)

lipase class 3 family protein may function as a lipase, catalyzing the hydrolysis of ester bonds of insoluble substrates such a triglycerides, or as a feruloyl esterase, hydrolyzing the feruloyl-arabinose ester bond in arabinoxylans and the feruloyl-galactose ester bond in pectin

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016788
PubMed:  9379943|12091482
SCOP:  4000732

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 34-261 1.08e-63

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: 202.32  E-value: 1.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  34 NHTLATILVEYAASVYVSDLTELFTWTCPKCNDLTKGFQILELIVDVKR-CLQAFVGVAPNLNAIVIAFRGTQgtSIQNW 112
Cdd:cd00519    1 DYEKLKYYAKLAAAAYCVDANILAKAVVFADIALLNVFSPDKLLKTDKQyDTQGYVAVDHDRKTIVIAFRGTV--SLADW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 113 IADLYWKQLDIEYPGMEDAMVHHGFYSAYHNttLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAMAAFCGLDLTVNYGSR 192
Cdd:cd00519   79 LTDLDFSPVPLDPPLCSGGKVHSGFYSAYKS--LYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGPGS 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 193 NVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLPPYYYYfPQKTYHHFPREVWL-HNLGFGL 261
Cdd:cd00519  157 DVTVYTFGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLT-PPEGYTHVGTEVWIdHLPYFYI 225
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 34-261 1.08e-63

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: 202.32  E-value: 1.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  34 NHTLATILVEYAASVYVSDLTELFTWTCPKCNDLTKGFQILELIVDVKR-CLQAFVGVAPNLNAIVIAFRGTQgtSIQNW 112
Cdd:cd00519    1 DYEKLKYYAKLAAAAYCVDANILAKAVVFADIALLNVFSPDKLLKTDKQyDTQGYVAVDHDRKTIVIAFRGTV--SLADW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 113 IADLYWKQLDIEYPGMEDAMVHHGFYSAYHNttLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAMAAFCGLDLTVNYGSR 192
Cdd:cd00519   79 LTDLDFSPVPLDPPLCSGGKVHSGFYSAYKS--LYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGPGS 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 193 NVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLPPYYYYfPQKTYHHFPREVWL-HNLGFGL 261
Cdd:cd00519  157 DVTVYTFGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLT-PPEGYTHVGTEVWIdHLPYFYI 225
Lipase_3 pfam01764
Lipase (class 3);
98-235 1.56e-41

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 142.01  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771   98 VIAFRGTQgtSIQNWIADLYWKQLDIEYPGMEDAMVHHGFYSAYhnTTLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAM 177
Cdd:pfam01764   1 VVAFRGTN--SILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAY--TSVREQVLAELKRLLEKYPDYSIVVTGHSLGGAL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723706771  178 AAFCGLDLTVNY--GSRNVSVMTFGQPRIGNAAFASYYSKWVPNTI-RVTHEHDIVPHLPP 235
Cdd:pfam01764  77 ASLAALDLVENGlrLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKFSyRVVHQRDIVPRLPP 137
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
86-264 1.36e-38

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 138.35  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  86 AFVGVAPNLNAIVIAFRGTQGTSiqNWIADLYWKQLDIEYpGMEDAMVHHGFYSAYHntTLRPgvlSAVESAKEQYGDIP 165
Cdd:COG3675   18 VFGFILRSDDEVIVAFRGTESLT--DWLTNLNAAQVPYPF-AKTGGKVHRGFYRALQ--SLRE---LLEDALRPLSPGKR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 166 IMVTGHSMGGAMAAFCGLDLTVNYGSRNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLPPYyyyfpQKTY 245
Cdd:COG3675   90 LYVTGHSLGGALATLAAADLERNYIFPVRGLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPV-----WMGY 164

                        170
                 ....*....|....*....
gi 723706771 246 HHFPREVWLHNLGFGLLSY 264
Cdd:COG3675  165 DHVGKLLWLDSLRKDMLTD 183
PLN02310 PLN02310
triacylglycerol lipase
 97-234 2.57e-16

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 79.26  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADLywkQLDIEYPGMEDAMVHHGFYSAY--HNTTLRPGVLSAVESAKEQ-------YG----D 163
Cdd:PLN02310 134 IMVAWRGT--VAPSEWFLDL---ETKLEHIDNTNVKVQEGFLKIYksKDESTRYNKLSASEQVMQEvkrlvnfYRgkgeE 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723706771 164 IPIMVTGHSMGGAMAAFCGLDLTVNYGSRNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLP 234
Cdd:PLN02310 209 VSLTVTGHSLGGALALLNAYEAATTIPDLFVSVISFGAPRVGNIAFKEKLNELGVKTLRVVVKQDKVPKLP 279
 
Name Accession Description Interval E-value
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 34-261 1.08e-63

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: 202.32  E-value: 1.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  34 NHTLATILVEYAASVYVSDLTELFTWTCPKCNDLTKGFQILELIVDVKR-CLQAFVGVAPNLNAIVIAFRGTQgtSIQNW 112
Cdd:cd00519    1 DYEKLKYYAKLAAAAYCVDANILAKAVVFADIALLNVFSPDKLLKTDKQyDTQGYVAVDHDRKTIVIAFRGTV--SLADW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 113 IADLYWKQLDIEYPGMEDAMVHHGFYSAYHNttLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAMAAFCGLDLTVNYGSR 192
Cdd:cd00519   79 LTDLDFSPVPLDPPLCSGGKVHSGFYSAYKS--LYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALDLRLRGPGS 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 193 NVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLPPYYYYfPQKTYHHFPREVWL-HNLGFGL 261
Cdd:cd00519  157 DVTVYTFGQPRVGNAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLT-PPEGYTHVGTEVWIdHLPYFYI 225
Lipase_3 pfam01764
Lipase (class 3);
98-235 1.56e-41

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 142.01  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771   98 VIAFRGTQgtSIQNWIADLYWKQLDIEYPGMEDAMVHHGFYSAYhnTTLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAM 177
Cdd:pfam01764   1 VVAFRGTN--SILDWLTDFDFSLTPFKDFFLGGGKVHSGFLSAY--TSVREQVLAELKRLLEKYPDYSIVVTGHSLGGAL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723706771  178 AAFCGLDLTVNY--GSRNVSVMTFGQPRIGNAAFASYYSKWVPNTI-RVTHEHDIVPHLPP 235
Cdd:pfam01764  77 ASLAALDLVENGlrLSSRVTVVTFGQPRVGNLEFAKLHDSQGPKFSyRVVHQRDIVPRLPP 137
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
86-264 1.36e-38

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 138.35  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  86 AFVGVAPNLNAIVIAFRGTQGTSiqNWIADLYWKQLDIEYpGMEDAMVHHGFYSAYHntTLRPgvlSAVESAKEQYGDIP 165
Cdd:COG3675   18 VFGFILRSDDEVIVAFRGTESLT--DWLTNLNAAQVPYPF-AKTGGKVHRGFYRALQ--SLRE---LLEDALRPLSPGKR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 166 IMVTGHSMGGAMAAFCGLDLTVNYGSRNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLPPYyyyfpQKTY 245
Cdd:COG3675   90 LYVTGHSLGGALATLAAADLERNYIFPVRGLYTFGQPRVGDRSFAKYYNLHVPNSYRIVNNNDIVPLLPPV-----WMGY 164

                        170
                 ....*....|....*....
gi 723706771 246 HHFPREVWLHNLGFGLLSY 264
Cdd:COG3675  165 DHVGKLLWLDSLRKDMLTD 183
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 135-295 1.14e-35

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: 127.23  E-value: 1.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 135 HGFYSAYHNttLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAMAAFCGLDLTVNYGSRNVSVMTFGQPRIGNAAFAS--Y 212
Cdd:cd00741    1 KGFYKAARS--LANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGLGRLVRVYTFGPPRVGNAAFAEdrL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 213 YSKWVPNTIRVTHEHDIVPHLPPYyyyfpQKTYHHFPREVWLHNlgfGLLSYTVEKVCDDSGEDPSCSRSVTGRSIKDHL 292
Cdd:cd00741   79 DPSDALFVDRIVNDNDIVPRLPPG-----GEGYPHGGAEFYING---GKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHL 150


                 ...
gi 723706771 293 TYY 295
Cdd:cd00741  151 RYF 153
PLN02310 PLN02310
triacylglycerol lipase
 97-234 2.57e-16

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 79.26  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADLywkQLDIEYPGMEDAMVHHGFYSAY--HNTTLRPGVLSAVESAKEQ-------YG----D 163
Cdd:PLN02310 134 IMVAWRGT--VAPSEWFLDL---ETKLEHIDNTNVKVQEGFLKIYksKDESTRYNKLSASEQVMQEvkrlvnfYRgkgeE 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723706771 164 IPIMVTGHSMGGAMAAFCGLDLTVNYGSRNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLP 234
Cdd:PLN02310 209 VSLTVTGHSLGGALALLNAYEAATTIPDLFVSVISFGAPRVGNIAFKEKLNELGVKTLRVVVKQDKVPKLP 279
PLN02408 PLN02408
phospholipase A1
 97-234 1.78e-13

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 70.64  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTQ--GTSIQNWIADLywKQLDIEYPGMED------AMVHHGFYSAYHNTT-----LRPGVLSAVESAKEQYGD 163
Cdd:PLN02408 120 VVIAFRGTAtcLEWLENLRATL--TRLPNAPTDMNGsgdgsgPMVESGFLSLYTSGTamgpsLQEMVREEIARLLQSYGD 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 723706771 164 IP--IMVTGHSMGGAMAAFCGLDLTVNYGSRN-VSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLP 234
Cdd:PLN02408 198 EPlsLTITGHSLGAALATLTAYDIKTTFKRAPmVTVISFGGPRVGNRSFRRQLEKQGTKVLRIVNSDDVITKVP 271
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 97-234 2.62e-13

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 70.75  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTQGTSiqNWIADLywkQLDIEY------PGMEDAMVHHGFYSAYHNTT--LRPGVLSAVESA----------- 157
Cdd:PLN03037 237 IVVAWRGTVAPT--EWFMDL---RTSLEPfdcdgdHGKNVVKVQSGFLSIYKSKSelTRYNKLSASEQVmeevkrlvnff 311

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723706771 158 KEQYGDIPIMVTGHSMGGAMAAFCGLDLTVNYGS-RNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLP 234
Cdd:PLN03037 312 KDRGEEVSLTITGHSLGGALALLNAYEAARSVPAlSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
PLN02802 PLN02802
triacylglycerol lipase
 97-256 5.67e-13

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 69.80  E-value: 5.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADLywKQLDIEYPGMEDAM-------VHHGFYSAY-----HNTTLRPGVLSAVESAKEQYG-- 162
Cdd:PLN02802 253 IVIALRGT--ATCLEWAENL--RAGLVPMPGDDDDAgdqeqpkVECGFLSLYktagaHVPSLSESVVGEVRRLMEKYKge 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 163 DIPIMVTGHSMGGAMAAFCGLDL-TVNYGSRNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVPHLPPYYYYFP 241
Cdd:PLN02802 329 ELSITVTGHSLGAALALLVADELaTCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQDVVTRVPGIAPREE 408

                        170
                 ....*....|....*..
gi 723706771 242 QKT--YHHFPREVWLHN 256
Cdd:PLN02802 409 LHKwaYAHVGAELRLDS 425
PLN02753 PLN02753
triacylglycerol lipase
 97-234 9.04e-13

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 68.97  E-value: 9.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADL--YWKQL---DIEYPGmEDAMVHHGFYSAYHNT---------TLRPGVLSAVESAKEQYG 162
Cdd:PLN02753 229 IAIAWRGT--VTKLEWIADLkdYLKPVsenKIRCPD-PAVKVESGFLDLYTDKdttckfakfSAREQILTEVKRLVEEHG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 163 D-----IPIMVTGHSMGGAMA-------AFCGLDLTVNYGSRNVSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIV 230
Cdd:PLN02753 306 DdddsdLSITVTGHSLGGALAilsaydiAEMGLNRSKKGKVIPVTVLTYGGPRVGNVRFKDRMEELGVKVLRVVNVHDVV 385


                 ....
gi 723706771 231 PHLP 234
Cdd:PLN02753 386 PKSP 389
PLN02934 PLN02934
triacylglycerol lipase
 95-248 1.58e-12

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 68.27  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  95 NAIVIAFRGTQGTSIQNWIADLYWKQLDIEYPGMedamVHHGFYSA-------------YHNTTLRPGVLSAVESAKE-- 159
Cdd:PLN02934 221 NLIVISFRGTEPFDADDWGTDFDYSWYEIPKVGK----VHMGFLEAmglgnrddtttfqTSLQTKATSELKEEESKKNll 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 160 --------------------QYGDIPIMVTGHSMGGAMAAFCGLDLTVNYGS----RNVSVMTFGQPRIGNAAFA----S 211
Cdd:PLN02934 297 emversayyavrsklksllkEHKNAKFVVTGHSLGGALAILFPTVLVLQEETevmkRLLGVYTFGQPRIGNRQLGkfmeA 376

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 723706771 212 YYSKWVPNTIRVTHEHDIVPHLPpyyyyFPQKT--YHHF 248
Cdd:PLN02934 377 QLNYPVPRYFRVVYCNDLVPRLP-----YDDKTflYKHF 410
PLN02761 PLN02761
lipase class 3 family protein
 97-234 2.94e-12

lipase class 3 family protein


Pssm-ID: 215406 [Multi-domain]  Cd Length: 527  Bit Score: 67.38  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADLYwkqlDI-------EYPGMEDAMVHHGFYSAYHNT------TLRPGVLSAVESAKEQYG- 162
Cdd:PLN02761 214 IVIAWRGT--VTYLEWIYDLK----DIlcsanfgDDPSIKIELGFHDLYTKKEDSckfssfSAREQVLAEVKRLVEYYGt 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 163 -----DIPIMVTGHSMGGAMAAFCGLD---LTVNYGSRN-----VSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDI 229
Cdd:PLN02761 288 eeeghEISITVTGHSLGASLALVSAYDiaeLNLNHVPENnykipITVFSFSGPRVGNLRFKERCDELGVKVLRVVNVHDK 367


                 ....*
gi 723706771 230 VPHLP 234
Cdd:PLN02761 368 VPSVP 372
PLN02571 PLN02571
triacylglycerol lipase
 97-238 2.42e-11

triacylglycerol lipase


Pssm-ID: 215309  Cd Length: 413  Bit Score: 64.52  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADLYWKQLD---IEYPGMEDAMVHHGFYSAY---------HNTTLRPGVLSAVESAKEQYGD- 163
Cdd:PLN02571 147 IVIAWRGT--VQTLEWVNDFEFNLVSaskIFGESNDQPKVHQGWYSIYtsdderspfNKTSARDQVLNEVGRLVEKYKDe 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 164 -IPIMVTGHSMGGAMAAFCGLDLTVNYGSRN---------VSVMTFGQPRIGNAAFASYYSKWVP-NTIRVTHEHDIVPH 232
Cdd:PLN02571 225 eISITICGHSLGAALATLNAVDIVANGFNRSksrpnkscpVTAFVFASPRVGDSDFKKLFSGLKDlRVLRVRNLPDVIPN 304


                 ....*.
gi 723706771 233 LPPYYY 238
Cdd:PLN02571 305 YPLIGY 310
PLN02719 PLN02719
triacylglycerol lipase
 97-234 5.77e-11

triacylglycerol lipase


Pssm-ID: 178321  Cd Length: 518  Bit Score: 63.57  E-value: 5.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWIADL--YWKQLDIEYPGMEDAMV--HHGFYSAYHNT---------TLRPGVLSAVESAKEQYGD 163
Cdd:PLN02719 215 IAIAWRGT--VTRLEWIADLkdFLKPVSGNGFRCPDPAVkaESGFLDLYTDKdtccnfskfSAREQVLTEVKRLVERYGD 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 164 -----IPIMVTGHSMGGAMAAFCGLDLTVNYGSRN-------VSVMTFGQPRIGNAAFASYYSKWVPNTIRVTHEHDIVP 231
Cdd:PLN02719 293 eegeeLSITVTGHSLGGALAVLSAYDVAEMGLNRTrkgkvipVTAFTYGGPRVGNIRFKERIEELGVKVLRVVNEHDVVA 372


                 ...
gi 723706771 232 HLP 234
Cdd:PLN02719 373 KSP 375
PLN02454 PLN02454
triacylglycerol lipase
 97-234 7.69e-11

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 62.94  E-value: 7.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgTSIQNWI----ADL----------------YWKQLDIEYPGMEDAMVHHGFYSAYHNT---------TLR 147
Cdd:PLN02454 132 IYVAWRGT--TRNYEWVdvlgAKLtsadpllpgpeqdgvvSGSSSDSDDDDEKGPKVMLGWLTIYTSDdprspftklSAR 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 148 PGVLSAVESAKEQYGD--IPIMVTGHSMGGAMAAFCGLDLTVNYGSRN---VSVMTFGQPRIGNAAFASYYSKWvPNtIR 222
Cdd:PLN02454 210 SQLLAKIKELLERYKDekLSIVLTGHSLGASLATLAAFDIVENGVSGAdipVTAIVFGSPQVGNKEFNDRFKEH-PN-LK 287

                        170
                 ....*....|....*
gi 723706771 223 VTH---EHDIVPHLP 234
Cdd:PLN02454 288 ILHvrnTIDLIPHYP 302
PLN00413 PLN00413
triacylglycerol lipase
 59-248 6.82e-10

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 60.03  E-value: 6.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  59 WTCPKCNDLTKGFQILeLIVDVKrclqafvgVAPNLnaIVIAFRGTQGTSIQNWIADLywkqlDIE-YPGMEDAMVHHGF 137
Cdd:PLN00413 175 YSCPNDFDKQRSTEVI-VIKDTK--------DDPNL--IIVSFRGTDPFDADDWCTDL-----DLSwHEVKNVGKIHGGF 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 138 YSAY----------------HNTTLRPGVLSAVESAKEQYGDIP---IMVTGHSMGGAMAAFCGLDLTVN----YGSRNV 194
Cdd:PLN00413 239 MKALglpkegwpeeinldetQNATSLLAYYTILRHLKEIFDQNPtskFILSGHSLGGALAILFTAVLIMHdeeeMLERLE 318

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 195 SVMTFGQPRIGNAAFASYY----SKWVPNTIRVTHEHDIVPHLPpyyyyFPQKT--YHHF 248
Cdd:PLN00413 319 GVYTFGQPRVGDEDFGIFMkdklKEFDVKYERYVYCNDMVPRLP-----FDDKTlmFKHF 373
PLN02162 PLN02162
triacylglycerol lipase
 12-246 3.85e-09

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 57.75  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  12 FMCLIACSTAR-EFKVK-DQGAIYNHTLATIL---VEYAASVYVSDLTElFTWTCpkcnDLTKGFQILELIVDVKrCLQA 86
Cdd:PLN02162 114 YTSFIGCSDRRiELDEKiDVGSIEYKSMLSIMaskISYESKPFINSVVK-NTWKM----DLVGNYDFYNAFQESK-LTQA 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  87 FV--GVAPNLNAIVIAFRGTQGTSIQNWIADLYWKQLDIEYPGMedamVHHGFYSA-------------------YHNTT 145
Cdd:PLN02162 188 FVfkTSSTNPDLIVVSFRGTEPFEAADWCTDLDLSWYELKNVGK----VHAGFSRAlglqkdggwpkenisllhqYAYYT 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 146 LRPGVLSAVESAKeqygDIPIMVTGHSMGGAMAAFCGLDLTVnYGSRNV-----SVMTFGQPRIGNAAFASYYSKWVPN- 219
Cdd:PLN02162 264 IRQMLRDKLARNK----NLKYILTGHSLGGALAALFPAILAI-HGEDELldkleGIYTFGQPRVGDEDFGEFMKGVVKKh 338

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 723706771 220 ---TIRVTHEHDIVPHLP-------PYYYYFPQKTYH 246
Cdd:PLN02162 339 gieYERFVYNNDVVPRVPfddkllfSYKHYGPCNSFN 375
PLN02324 PLN02324
triacylglycerol lipase
 97-238 7.90e-09

triacylglycerol lipase


Pssm-ID: 177958  Cd Length: 415  Bit Score: 56.56  E-value: 7.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771  97 IVIAFRGTqgtsIQnwiadLYWKQLDIEYPgMEDAM-------------VHHGFYSAYHNTTLRP--GVLSAVESAKEQY 161
Cdd:PLN02324 134 IVVAWRGT----LQ-----PYEWANDFDFP-LESAIsvfpvtdpkdnprIGSGWLDIYTASDSRSpyDTTSAQEQVQGEL 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 162 G---------DIPIMVTGHSMGGAMAAFCGLDLTvnYGSRN------------VSVMTFGQPRIGNAAFASYYSKWVP-N 219
Cdd:PLN02324 204 KrllelykneEISITFTGHSLGAVMSVLSAADLV--YGKKNkinislqkkqvpITVFAFGSPRIGDHNFKNLVDSLQPlN 281

                        170
                 ....*....|....*....
gi 723706771 220 TIRVTHEHDIVPHLPPYYY 238
Cdd:PLN02324 282 ILRIVNVPDVAPHYPLLLY 300
M20_dipept_Sso-CP2 cd05681
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 113-192 5.81e-03

uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.


Pssm-ID: 349930 [Multi-domain]  Cd Length: 429  Bit Score: 38.47  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723706771 113 IADLYWKQLDieYPGMEDAMVH-HGFYSAYHNTTLRPGVLSAVESAKEQYGDIPIMVTGHSMGGAMAAFC-GLDLTV--- 187
Cdd:cd05681  318 ILSLLRKHLD--KNGFDDIEIHdLLGEKPFRTDPDAPFVQAVIESAKEVYGQDPIVLPNSAGTGPMYPFYdALEVPVvai 395


                 ....*...
gi 723706771 188 ---NYGSR 192
Cdd:cd05681  396 gvgNAGSN 403
 
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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