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Conserved domains on  [gi|2104904800|ref|WP_224868489|]
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lipase family protein [Microbulbifer agarilyticus]

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
Lip2 super family cl28574
Predicted lipase [Lipid transport and metabolism];
73-244 2.09e-35

Predicted lipase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG3675:

Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 130.64  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  73 EALIALKGTSNGYDGLTDLNAGLKQF---NTGGFVHQGFYYAFQSFLPELDQFLANLPPDiHTVHCVGHSLGGALATLAA 149
Cdd:COG3675    28 EVIVAFRGTESLTDWLTNLNAAQVPYpfaKTGGKVHRGFYRALQSLRELLEDALRPLSPG-KRLYVTGHSLGGALATLAA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 150 DYLKAKSGCAVN-LYTFGSPRVGLSLFSEgaLRRLGEKNIFRVYHRTDPVPMVPTWPFIHVPNGGLGDLLLNSSvalNPI 228
Cdd:COG3675   107 ADLERNYIFPVRgLYTFGQPRVGDRSFAK--YYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLLWLDSLRK---DML 181

                         170
                  ....*....|....*.
gi 2104904800 229 EYHKMENYIGSLSGSE 244
Cdd:COG3675   182 TDHSMDNYIHHTDLSQ 197
 
Name Accession Description Interval E-value
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
73-244 2.09e-35

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 130.64  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  73 EALIALKGTSNGYDGLTDLNAGLKQF---NTGGFVHQGFYYAFQSFLPELDQFLANLPPDiHTVHCVGHSLGGALATLAA 149
Cdd:COG3675    28 EVIVAFRGTESLTDWLTNLNAAQVPYpfaKTGGKVHRGFYRALQSLRELLEDALRPLSPG-KRLYVTGHSLGGALATLAA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 150 DYLKAKSGCAVN-LYTFGSPRVGLSLFSEgaLRRLGEKNIFRVYHRTDPVPMVPTWPFIHVPNGGLGDLLLNSSvalNPI 228
Cdd:COG3675   107 ADLERNYIFPVRgLYTFGQPRVGDRSFAK--YYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLLWLDSLRK---DML 181

                         170
                  ....*....|....*.
gi 2104904800 229 EYHKMENYIGSLSGSE 244
Cdd:COG3675   182 TDHSMDNYIHHTDLSQ 197
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 5-205 8.98e-33

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: 122.58  E-value: 8.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800   5 TPELSANIANDIYLITNQNTR-----KLFFDLYADQFAFKDDANLQGKTGAFILLKKEQSlglaatgikqrkgEALIALK 79
Cdd:cd00519     4 KLKYYAKLAAAAYCVDANILAkavvfADIALLNVFSPDKLLKTDKQYDTQGYVAVDHDRK-------------TIVIAFR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  80 GTSNGYDGLTDLNAGLKQFN----TGGFVHQGFYYAFQS----FLPELDQFLANLPPdiHTVHCVGHSLGGALATLAADY 151
Cdd:cd00519    71 GTVSLADWLTDLDFSPVPLDpplcSGGKVHSGFYSAYKSlynqVLPELKSALKQYPD--YKIIVTGHSLGGALASLLALD 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104904800 152 LKA-KSGCAVNLYTFGSPRVGLSLFSEgaLRRLGEKNIFRVYHRTDPVPMVPTWP 205
Cdd:cd00519   149 LRLrGPGSDVTVYTFGQPRVGNAAFAE--YLESTKGRVYRVVHGNDIVPRLPPGS 201
Lipase_3 pfam01764
Lipase (class 3);
76-204 5.43e-27

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 104.26  E-value: 5.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  76 IALKGTSNGYDGLTDLNAGLKQFNT----GGFVHQGFYYAF----QSFLPELDQFLANLPPdiHTVHCVGHSLGGALATL 147
Cdd:pfam01764   2 VAFRGTNSILDWLTDFDFSLTPFKDfflgGGKVHSGFLSAYtsvrEQVLAELKRLLEKYPD--YSIVVTGHSLGGALASL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 148 AADYLKAK---SGCAVNLYTFGSPRVGLSLFSEgALRRLGEKNIFRVYHRTDPVPMVPTW 204
Cdd:pfam01764  80 AALDLVENglrLSSRVTVVTFGQPRVGNLEFAK-LHDSQGPKFSYRVVHQRDIVPRLPPI 138
PLN02408 PLN02408
phospholipase A1
 73-222 1.54e-08

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 56.00  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  73 EALIALKGTSNGYDGLTDLNAGLKQF------------NTGGFVHQGFYYAFQSFLP-----------ELDQFLANLPPD 129
Cdd:PLN02408  119 DVVIAFRGTATCLEWLENLRATLTRLpnaptdmngsgdGSGPMVESGFLSLYTSGTAmgpslqemvreEIARLLQSYGDE 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 130 IHTVHCVGHSLGGALATLAADYLKAKSGCA--VNLYTFGSPRVGlslfsEGALRRLGEKN---IFRVYHRTDPVPMVPTW 204
Cdd:PLN02408  199 PLSLTITGHSLGAALATLTAYDIKTTFKRApmVTVISFGGPRVG-----NRSFRRQLEKQgtkVLRIVNSDDVITKVPGF 273

                         170
                  ....*....|....*...
gi 2104904800 205 PfIHVPNGGLGDLLLNSS 222
Cdd:PLN02408  274 V-IDGENDVAKKRDVNVA 290
 
Name Accession Description Interval E-value
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
73-244 2.09e-35

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 130.64  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  73 EALIALKGTSNGYDGLTDLNAGLKQF---NTGGFVHQGFYYAFQSFLPELDQFLANLPPDiHTVHCVGHSLGGALATLAA 149
Cdd:COG3675    28 EVIVAFRGTESLTDWLTNLNAAQVPYpfaKTGGKVHRGFYRALQSLRELLEDALRPLSPG-KRLYVTGHSLGGALATLAA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 150 DYLKAKSGCAVN-LYTFGSPRVGLSLFSEgaLRRLGEKNIFRVYHRTDPVPMVPTWPFIHVPNGGLGDLLLNSSvalNPI 228
Cdd:COG3675   107 ADLERNYIFPVRgLYTFGQPRVGDRSFAK--YYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLLWLDSLRK---DML 181

                         170
                  ....*....|....*.
gi 2104904800 229 EYHKMENYIGSLSGSE 244
Cdd:COG3675   182 TDHSMDNYIHHTDLSQ 197
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 5-205 8.98e-33

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: 122.58  E-value: 8.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800   5 TPELSANIANDIYLITNQNTR-----KLFFDLYADQFAFKDDANLQGKTGAFILLKKEQSlglaatgikqrkgEALIALK 79
Cdd:cd00519     4 KLKYYAKLAAAAYCVDANILAkavvfADIALLNVFSPDKLLKTDKQYDTQGYVAVDHDRK-------------TIVIAFR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  80 GTSNGYDGLTDLNAGLKQFN----TGGFVHQGFYYAFQS----FLPELDQFLANLPPdiHTVHCVGHSLGGALATLAADY 151
Cdd:cd00519    71 GTVSLADWLTDLDFSPVPLDpplcSGGKVHSGFYSAYKSlynqVLPELKSALKQYPD--YKIIVTGHSLGGALASLLALD 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2104904800 152 LKA-KSGCAVNLYTFGSPRVGLSLFSEgaLRRLGEKNIFRVYHRTDPVPMVPTWP 205
Cdd:cd00519   149 LRLrGPGSDVTVYTFGQPRVGNAAFAE--YLESTKGRVYRVVHGNDIVPRLPPGS 201
Lipase_3 pfam01764
Lipase (class 3);
76-204 5.43e-27

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 104.26  E-value: 5.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  76 IALKGTSNGYDGLTDLNAGLKQFNT----GGFVHQGFYYAF----QSFLPELDQFLANLPPdiHTVHCVGHSLGGALATL 147
Cdd:pfam01764   2 VAFRGTNSILDWLTDFDFSLTPFKDfflgGGKVHSGFLSAYtsvrEQVLAELKRLLEKYPD--YSIVVTGHSLGGALASL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 148 AADYLKAK---SGCAVNLYTFGSPRVGLSLFSEgALRRLGEKNIFRVYHRTDPVPMVPTW 204
Cdd:pfam01764  80 AALDLVENglrLSSRVTVVTFGQPRVGNLEFAK-LHDSQGPKFSYRVVHQRDIVPRLPPI 138
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 106-213 2.55e-22

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: 92.18  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 106 QGFYYAFQS----FLPELDQFLANLPPDihTVHCVGHSLGGALATLAADYLKA-KSGCAVNLYTFGSPRVGLSLFSEGAL 180
Cdd:cd00741     1 KGFYKAARSlanlVLPLLKSALAQYPDY--KIHVTGHSLGGALAGLAGLDLRGrGLGRLVRVYTFGPPRVGNAAFAEDRL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2104904800 181 RRLGEKNIFRVYHRTDPVPMVP--TWPFIHV-----PNGG 213
Cdd:cd00741    79 DPSDALFVDRIVNDNDIVPRLPpgGEGYPHGgaefyINGG 118
PLN02408 PLN02408
phospholipase A1
 73-222 1.54e-08

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 56.00  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  73 EALIALKGTSNGYDGLTDLNAGLKQF------------NTGGFVHQGFYYAFQSFLP-----------ELDQFLANLPPD 129
Cdd:PLN02408  119 DVVIAFRGTATCLEWLENLRATLTRLpnaptdmngsgdGSGPMVESGFLSLYTSGTAmgpslqemvreEIARLLQSYGDE 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 130 IHTVHCVGHSLGGALATLAADYLKAKSGCA--VNLYTFGSPRVGlslfsEGALRRLGEKN---IFRVYHRTDPVPMVPTW 204
Cdd:PLN02408  199 PLSLTITGHSLGAALATLTAYDIKTTFKRApmVTVISFGGPRVG-----NRSFRRQLEKQgtkVLRIVNSDDVITKVPGF 273

                         170
                  ....*....|....*...
gi 2104904800 205 PfIHVPNGGLGDLLLNSS 222
Cdd:PLN02408  274 V-IDGENDVAKKRDVNVA 290
PLN02802 PLN02802
triacylglycerol lipase
 136-202 4.86e-08

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 54.78  E-value: 4.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104904800 136 VGHSLGGALATLAADYLkakSGCA-----VNLYTFGSPRVGLSLFSEgalrRLGEK--NIFRVYHRTDPVPMVP 202
Cdd:PLN02802  335 TGHSLGAALALLVADEL---ATCVpaappVAVFSFGGPRVGNRAFAD----RLNARgvKVLRVVNAQDVVTRVP 401
PLN02571 PLN02571
triacylglycerol lipase
 104-207 4.95e-07

triacylglycerol lipase


Pssm-ID: 215309  Cd Length: 413  Bit Score: 51.43  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 104 VHQGFYYAFQS---------------FLPELDQFLANLPPDIHTVHCVGHSLGGALATL-AAD-----YLKAKS----GC 158
Cdd:PLN02571  184 VHQGWYSIYTSdderspfnktsardqVLNEVGRLVEKYKDEEISITICGHSLGAALATLnAVDivangFNRSKSrpnkSC 263

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2104904800 159 AVNLYTFGSPRVGLSLFSEgALRRLGEKNIFRVYHRTDpvpMVPTWPFI 207
Cdd:PLN02571  264 PVTAFVFASPRVGDSDFKK-LFSGLKDLRVLRVRNLPD---VIPNYPLI 308
PLN02934 PLN02934
triacylglycerol lipase
 137-202 3.58e-06

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 49.01  E-value: 3.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104904800 137 GHSLGGALATLAADYLKAKSGCAV-----NLYTFGSPRVG---LSLFSEGALrRLGEKNIFRVYHRTDPVPMVP 202
Cdd:PLN02934  327 GHSLGGALAILFPTVLVLQEETEVmkrllGVYTFGQPRIGnrqLGKFMEAQL-NYPVPRYFRVVYCNDLVPRLP 399
PLN02324 PLN02324
triacylglycerol lipase
 132-244 4.70e-06

triacylglycerol lipase


Pssm-ID: 177958  Cd Length: 415  Bit Score: 48.47  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 132 TVHCVGHSLGGALATL-AADY-----------LKAKSGCaVNLYTFGSPRVGLSLFsEGALRRLGEKNIFRVYHRTDPVP 199
Cdd:PLN02324  216 SITFTGHSLGAVMSVLsAADLvygkknkinisLQKKQVP-ITVFAFGSPRIGDHNF-KNLVDSLQPLNILRIVNVPDVAP 293

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2104904800 200 MVPTWPFIHVpngglGDLL----LNSSV---ALNPIEYHKMENYIGSLSGSE 244
Cdd:PLN02324  294 HYPLLLYTEI-----GEVLeintLNSTYlkrSLNFRNYHNLEAYLHGVAGMQ 340
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 137-202 5.44e-06

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 48.41  E-value: 5.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2104904800 137 GHSLGGALATLAAdYLKAKSGCAVN---LYTFGSPRVGLSLFSEgALRRLGEKnIFRVYHRTDPVPMVP 202
Cdd:PLN03037  324 GHSLGGALALLNA-YEAARSVPALSnisVISFGAPRVGNLAFKE-KLNELGVK-VLRVVNKQDIVPKLP 389
PLN02310 PLN02310
triacylglycerol lipase
 69-202 2.91e-05

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 45.75  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  69 QRKG--EALIALKGTSNGYDGLTDLNAGLKQF-NTGGFVHQGFY--YAFQSFLPELDQFLANLPPDIHTVHCV------- 136
Cdd:PLN02310  127 QRIGrrDIMVAWRGTVAPSEWFLDLETKLEHIdNTNVKVQEGFLkiYKSKDESTRYNKLSASEQVMQEVKRLVnfyrgkg 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2104904800 137 --------GHSLGGALATLAADYLKAK-SGCAVNLYTFGSPRVGLSLFSEgALRRLGEKNIfRVYHRTDPVPMVP 202
Cdd:PLN02310  207 eevsltvtGHSLGGALALLNAYEAATTiPDLFVSVISFGAPRVGNIAFKE-KLNELGVKTL-RVVVKQDKVPKLP 279
PLN02454 PLN02454
triacylglycerol lipase
 109-205 2.98e-04

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 42.52  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 109 YYAFQSFLPELDQFLANLPPDIHTVHCVGHSLGGALATLAA-DYLKAKSGCA---VNLYTFGSPRVGLSLFSEgalrRLG 184
Cdd:PLN02454  206 LSARSQLLAKIKELLERYKDEKLSIVLTGHSLGASLATLAAfDIVENGVSGAdipVTAIVFGSPQVGNKEFND----RFK 281

                          90       100
                  ....*....|....*....|.
gi 2104904800 185 EKNIFRVYHRTDPVPMVPTWP 205
Cdd:PLN02454  282 EHPNLKILHVRNTIDLIPHYP 302
PLN00413 PLN00413
triacylglycerol lipase
 75-206 4.25e-04

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 42.31  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  75 LIALKGTS--NGYDGLTDLNAGLKQFNTGGFVHQGFY-------------------------YAFQSFLPELDQFLANLP 127
Cdd:PLN00413  203 IVSFRGTDpfDADDWCTDLDLSWHEVKNVGKIHGGFMkalglpkegwpeeinldetqnatslLAYYTILRHLKEIFDQNP 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 128 PDIHTVhcVGHSLGGALATL---------AADYLKAKSGcavnLYTFGSPRVG---LSLFSEGALRRLGEKNIFRVYHRT 195
Cdd:PLN00413  283 TSKFIL--SGHSLGGALAILftavlimhdEEEMLERLEG----VYTFGQPRVGdedFGIFMKDKLKEFDVKYERYVYCND 356

                         170
                  ....*....|.
gi 2104904800 196 dpvpMVPTWPF 206
Cdd:PLN00413  357 ----MVPRLPF 363
PLN02753 PLN02753
triacylglycerol lipase
 132-202 6.76e-04

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 41.62  E-value: 6.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2104904800 132 TVHCVGHSLGGALATLAADYL------KAKSG--CAVNLYTFGSPRVGLSLFSEgALRRLGEKnIFRVYHRTDPVPMVP 202
Cdd:PLN02753  313 SITVTGHSLGGALAILSAYDIaemglnRSKKGkvIPVTVLTYGGPRVGNVRFKD-RMEELGVK-VLRVVNVHDVVPKSP 389
PLN02761 PLN02761
lipase class 3 family protein
 132-202 1.21e-03

lipase class 3 family protein


Pssm-ID: 215406 [Multi-domain]  Cd Length: 527  Bit Score: 40.80  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 132 TVHCVGHSLGGALATLAA---------DYLKAKSGCAVNLYTFGSPRVGLSLFSEgALRRLGEKnIFRVYHRTDPVPMVP 202
Cdd:PLN02761  295 SITVTGHSLGASLALVSAydiaelnlnHVPENNYKIPITVFSFSGPRVGNLRFKE-RCDELGVK-VLRVVNVHDKVPSVP 372
PLN02719 PLN02719
triacylglycerol lipase
 132-202 1.59e-03

triacylglycerol lipase


Pssm-ID: 178321  Cd Length: 518  Bit Score: 40.46  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 132 TVHCVGHSLGGALATLAAdYLKAKSG---------CAVNLYTFGSPRVGLSLFSEgALRRLGEKnIFRVYHRTDPVPMVP 202
Cdd:PLN02719  299 SITVTGHSLGGALAVLSA-YDVAEMGlnrtrkgkvIPVTAFTYGGPRVGNIRFKE-RIEELGVK-VLRVVNEHDVVAKSP 375
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 75-199 3.43e-03

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


Pssm-ID: 444061  Cd Length: 405  Bit Score: 39.23  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800  75 LIALKGTSNGYDGLTDLNAGLKQF---------NTGGFVHQGFY-YAFQSFLPELDQFLANLPPDIHT-----VHCVGHS 139
Cdd:COG5153    48 IIAFRGTQGKPDWKTDINASLHDYdeknkeadeKLPLQVHEGFEqYAAQVMDLDYDGAEELAAEVKKQypdaeLSLTGHS 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104904800 140 LGGALATLAAdylKAKSGCAVnlyTFGSPRVGLSLFSEGALRRLgekNIFRVYHRTDPVP 199
Cdd:COG5153   128 LGGALASLVA---VATGLSKV---TFAAPGSGNHALADDLGKRI---DAGEFVKSLDAVA 178
 
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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