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Conserved domains on  [gi|922581252|ref|NP_001300196|]
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Fungal lipase-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

lipase family protein( domain architecture ID 10484750)

lipase class 3 family protein may function as a lipase, catalyzing the hydrolysis of ester bonds of insoluble substrates such a triglycerides; similar to Arabidopsis thaliana phospholipase A1 PLIP3 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0006629|GO:0052689
PubMed:  19508187|12369917|9379946|9704093|8453375|8280778|11099800|37582413|31545554
SCOP:  3000102

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
1-117 1.10e-46

Lipase (class 3);


:

Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 149.72  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252    1 MYRNKTAWFGGGNVGFYFARSYNLlWNAGMKEDFNTLKHAYPGYEIWVGGHSLGGSMAALASNYLVANGLATSSNLKMIT 80
Cdd:pfam01764  21 LTPFKDFFLGGGKVHSGFLSAYTS-VREQVLAELKRLLEKYPDYSIVVTGHSLGGALASLAALDLVENGLRLSSRVTVVT 99

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 922581252   81 FGEPRTGDKAFADAHDKMVTY-SYRIVHHKDIVPHIPL 117
Cdd:pfam01764 100 FGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPP 137
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
1-117 1.10e-46

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 149.72  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252    1 MYRNKTAWFGGGNVGFYFARSYNLlWNAGMKEDFNTLKHAYPGYEIWVGGHSLGGSMAALASNYLVANGLATSSNLKMIT 80
Cdd:pfam01764  21 LTPFKDFFLGGGKVHSGFLSAYTS-VREQVLAELKRLLEKYPDYSIVVTGHSLGGALASLAALDLVENGLRLSSRVTVVT 99

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 922581252   81 FGEPRTGDKAFADAHDKMVTY-SYRIVHHKDIVPHIPL 117
Cdd:pfam01764 100 FGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPP 137
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 8-133 3.35e-39

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: 133.37  E-value: 3.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252   8 WFGGGNVGFYFARSYNLLWNAGMKEDFNTLKhAYPGYEIWVGGHSLGGSMAALASNYLVANGLatSSNLKMITFGEPRTG 87
Cdd:cd00519   93 LCSGGKVHSGFYSAYKSLYNQVLPELKSALK-QYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDVTVYTFGQPRVG 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 922581252  88 DKAFADAHDKMVTYSYRIVHHKDIVPHIPLNGMA---EFHHHRNEVWYD 133
Cdd:cd00519  170 NAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTppeGYTHVGTEVWID 218
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
9-134 1.84e-23

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 93.67  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252   9 FGGGNVGFYFARSYNLLWNAGMKEDFNTLKHAYPGYEIWVGGHSLGGSMAALASNYLVANGlaTSSNLKMITFGEPRTGD 88
Cdd:COG3675   53 YPFAKTGGKVHRGFYRALQSLRELLEDALRPLSPGKRLYVTGHSLGGALATLAAADLERNY--IFPVRGLYTFGQPRVGD 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 922581252  89 KAFADAHDKMVTYSYRIVHHKDIVPHIPLNGMAEFHHHRNEVWYDN 134
Cdd:COG3675  131 RSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLLWLDSL 176
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 48-116 2.77e-10

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 58.43  E-value: 2.77e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581252  48 VGGHSLGGSMAaLASNYLVANGLATSSNLKMITFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIP 116
Cdd:PLN03037 322 ITGHSLGGALA-LLNAYEAARSVPALSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
 
Name Accession Description Interval E-value
Lipase_3 pfam01764
Lipase (class 3);
1-117 1.10e-46

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 149.72  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252    1 MYRNKTAWFGGGNVGFYFARSYNLlWNAGMKEDFNTLKHAYPGYEIWVGGHSLGGSMAALASNYLVANGLATSSNLKMIT 80
Cdd:pfam01764  21 LTPFKDFFLGGGKVHSGFLSAYTS-VREQVLAELKRLLEKYPDYSIVVTGHSLGGALASLAALDLVENGLRLSSRVTVVT 99

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 922581252   81 FGEPRTGDKAFADAHDKMVTY-SYRIVHHKDIVPHIPL 117
Cdd:pfam01764 100 FGQPRVGNLEFAKLHDSQGPKfSYRVVHQRDIVPRLPP 137
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 8-133 3.35e-39

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: 133.37  E-value: 3.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252   8 WFGGGNVGFYFARSYNLLWNAGMKEDFNTLKhAYPGYEIWVGGHSLGGSMAALASNYLVANGLatSSNLKMITFGEPRTG 87
Cdd:cd00519   93 LCSGGKVHSGFYSAYKSLYNQVLPELKSALK-QYPDYKIIVTGHSLGGALASLLALDLRLRGP--GSDVTVYTFGQPRVG 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 922581252  88 DKAFADAHDKMVTYSYRIVHHKDIVPHIPLNGMA---EFHHHRNEVWYD 133
Cdd:cd00519  170 NAAFAEYLESTKGRVYRVVHGNDIVPRLPPGSLTppeGYTHVGTEVWID 218
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 15-168 3.53e-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: 120.68  E-value: 3.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  15 GFYfaRSYNLLWNAGMKEDFNTLKhAYPGYEIWVGGHSLGGSMAALASNYLVANGLatSSNLKMITFGEPRTGDKAFAD- 93
Cdd:cd00741    2 GFY--KAARSLANLVLPLLKSALA-QYPDYKIHVTGHSLGGALAGLAGLDLRGRGL--GRLVRVYTFGPPRVGNAAFAEd 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581252  94 -AHDKMVTYSYRIVHHKDIVPHIPLNGMAeFHHHRNEVWYDNDMLKAV--FKECDAQESPFCSDSHLDYEIEDHHRYF 168
Cdd:cd00741   77 rLDPSDALFVDRIVNDNDIVPRLPPGGEG-YPHGGAEFYINGGKSQPGccKNVLEAVDIDFGNIGLSGNGLCDHLRYF 153
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
9-134 1.84e-23

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 93.67  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252   9 FGGGNVGFYFARSYNLLWNAGMKEDFNTLKHAYPGYEIWVGGHSLGGSMAALASNYLVANGlaTSSNLKMITFGEPRTGD 88
Cdd:COG3675   53 YPFAKTGGKVHRGFYRALQSLRELLEDALRPLSPGKRLYVTGHSLGGALATLAAADLERNY--IFPVRGLYTFGQPRVGD 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 922581252  89 KAFADAHDKMVTYSYRIVHHKDIVPHIPLNGMAEFHHHRNEVWYDN 134
Cdd:COG3675  131 RSFAKYYNLHVPNSYRIVNNNDIVPLLPPVWMGYDHVGKLLWLDSL 176
PLN03037 PLN03037
lipase class 3 family protein; Provisional
 48-116 2.77e-10

lipase class 3 family protein; Provisional


Pssm-ID: 215547  Cd Length: 525  Bit Score: 58.43  E-value: 2.77e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581252  48 VGGHSLGGSMAaLASNYLVANGLATSSNLKMITFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIP 116
Cdd:PLN03037 322 ITGHSLGGALA-LLNAYEAARSVPALSNISVISFGAPRVGNLAFKEKLNELGVKVLRVVNKQDIVPKLP 389
PLN02802 PLN02802
triacylglycerol lipase
 41-125 1.24e-09

triacylglycerol lipase


Pssm-ID: 215432  Cd Length: 509  Bit Score: 56.32  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  41 YPGYE--IWVGGHSLGGSMAALASNYLvANGLATSSNLKMITFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIPLN 118
Cdd:PLN02802 325 YKGEElsITVTGHSLGAALALLVADEL-ATCVPAAPPVAVFSFGGPRVGNRAFADRLNARGVKVLRVVNAQDVVTRVPGI 403


                 ....*..
gi 922581252 119 GMAEFHH 125
Cdd:PLN02802 404 APREELH 410
PLN02310 PLN02310
triacylglycerol lipase
 48-116 7.46e-08

triacylglycerol lipase


Pssm-ID: 215176  Cd Length: 405  Bit Score: 51.14  E-value: 7.46e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581252  48 VGGHSLGGSMAALasNYLVANGLATSSNLKMITFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIP 116
Cdd:PLN02310 213 VTGHSLGGALALL--NAYEAATTIPDLFVSVISFGAPRVGNIAFKEKLNELGVKTLRVVVKQDKVPKLP 279
PLN02753 PLN02753
triacylglycerol lipase
 46-116 1.39e-07

triacylglycerol lipase


Pssm-ID: 178354  Cd Length: 531  Bit Score: 50.48  E-value: 1.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581252  46 IWVGGHSLGGSMAALASNYLVANGLATSSNLKMI-----TFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIP 116
Cdd:PLN02753 314 ITVTGHSLGGALAILSAYDIAEMGLNRSKKGKVIpvtvlTYGGPRVGNVRFKDRMEELGVKVLRVVNVHDVVPKSP 389
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 37-119 5.35e-07

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


Pssm-ID: 444061  Cd Length: 405  Bit Score: 48.47  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  37 LKHAYPGYEIWVGGHSLGGSMAALASnylVANGLATssnlkmITFGEPRTGDKAFADAHDKMVTySYRIVHHKDIVPHIP 116
Cdd:COG5153  112 VKKQYPDAELSLTGHSLGGALASLVA---VATGLSK------VTFAAPGSGNHALADDLGKRID-AGEFVKSLDAVAGPG 181


                 ...
gi 922581252 117 LNG 119
Cdd:COG5153  182 DSF 184
PLN02454 PLN02454
triacylglycerol lipase
 17-156 1.07e-06

triacylglycerol lipase


Pssm-ID: 215249  Cd Length: 414  Bit Score: 47.53  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  17 YFARSYNLlwnAGMKEDFNTLKHAYPGyeIWVGGHSLGGSMAALASNYLVANGLATSS-NLKMITFGEPRTGDKAFADAH 95
Cdd:PLN02454 206 LSARSQLL---AKIKELLERYKDEKLS--IVLTGHSLGASLATLAAFDIVENGVSGADiPVTAIVFGSPQVGNKEFNDRF 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581252  96 DKMVtySYRIVHHK---DIVPHIP--LNGMAefhhhrnevwYDNDMLkavfkECDAQESPFCSDSH 156
Cdd:PLN02454 281 KEHP--NLKILHVRntiDLIPHYPggLLGYV----------NTGTEL-----VIDTRKSPFLKDSK 329
PLN02408 PLN02408
phospholipase A1
 30-116 1.38e-06

phospholipase A1


Pssm-ID: 215228  Cd Length: 365  Bit Score: 47.14  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  30 MKEDFNTLKHAYPG--YEIWVGGHSLGGSMAALASnYLVANGLATSSNLKMITFGEPRTGDKAFADAHDKMVTYSYRIVH 107
Cdd:PLN02408 184 VREEIARLLQSYGDepLSLTITGHSLGAALATLTA-YDIKTTFKRAPMVTVISFGGPRVGNRSFRRQLEKQGTKVLRIVN 262


                 ....*....
gi 922581252 108 HKDIVPHIP 116
Cdd:PLN02408 263 SDDVITKVP 271
PLN02162 PLN02162
triacylglycerol lipase
 7-118 1.57e-06

triacylglycerol lipase


Pssm-ID: 177821  Cd Length: 475  Bit Score: 47.35  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252   7 AWFGGGNVGFY---FARSYNLLWNAGMKEDFNTLKHAYPGYEI----------------WVGGHSLGGSMAALASNYLVA 67
Cdd:PLN02162 222 SWYELKNVGKVhagFSRALGLQKDGGWPKENISLLHQYAYYTIrqmlrdklarnknlkyILTGHSLGGALAALFPAILAI 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581252  68 NGL-ATSSNLKMI-TFGEPRTGDKAFADAHDKMVTYS----YRIVHHKDIVPHIPLN 118
Cdd:PLN02162 302 HGEdELLDKLEGIyTFGQPRVGDEDFGEFMKGVVKKHgieyERFVYNNDVVPRVPFD 358
PLN00413 PLN00413
triacylglycerol lipase
 42-134 1.04e-05

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 45.01  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  42 PGYEIWVGGHSLGGSMAALASNYLVANglatsSNLKMI-------TFGEPRTGDKAFAD-AHDKM----VTYSyRIVHHK 109
Cdd:PLN00413 282 PTSKFILSGHSLGGALAILFTAVLIMH-----DEEEMLerlegvyTFGQPRVGDEDFGIfMKDKLkefdVKYE-RYVYCN 355

                         90       100
                 ....*....|....*....|....*.
gi 922581252 110 DIVPHIPLNGMA-EFHHHRNEVWYDN 134
Cdd:PLN00413 356 DMVPRLPFDDKTlMFKHFGACLYCDS 381
PLN02934 PLN02934
triacylglycerol lipase
 48-143 2.86e-05

triacylglycerol lipase


Pssm-ID: 215504  Cd Length: 515  Bit Score: 43.62  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  48 VGGHSLGGSMAALASNYLVANGLATSSN--LKMITFGEPRTGDKA---FADAH-DKMVTYSYRIVHHKDIVPHIPLNGMA 121
Cdd:PLN02934 325 VTGHSLGGALAILFPTVLVLQEETEVMKrlLGVYTFGQPRIGNRQlgkFMEAQlNYPVPRYFRVVYCNDLVPRLPYDDKT 404

                         90       100
                 ....*....|....*....|...
gi 922581252 122 -EFHHHRNEVWYDNDMLKAVFKE 143
Cdd:PLN02934 405 fLYKHFGVCLYYDSRYFGQKMDE 427
PLN02571 PLN02571
triacylglycerol lipase
 46-122 5.58e-05

triacylglycerol lipase


Pssm-ID: 215309  Cd Length: 413  Bit Score: 42.57  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  46 IWVGGHSLGGSMAALASNYLVANGLATSSNLK-------MITFGEPRTGD----KAFADAHDKMVtysYRIVHHKDIVPH 114
Cdd:PLN02571 228 ITICGHSLGAALATLNAVDIVANGFNRSKSRPnkscpvtAFVFASPRVGDsdfkKLFSGLKDLRV---LRVRNLPDVIPN 304


                 ....*...
gi 922581252 115 IPLNGMAE 122
Cdd:PLN02571 305 YPLIGYSD 312
PLN02719 PLN02719
triacylglycerol lipase
 46-116 6.98e-05

triacylglycerol lipase


Pssm-ID: 178321  Cd Length: 518  Bit Score: 42.38  E-value: 6.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581252  46 IWVGGHSLGGSMAALASNYLVANGLATSSNLKMI-----TFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIP 116
Cdd:PLN02719 300 ITVTGHSLGGALAVLSAYDVAEMGLNRTRKGKVIpvtafTYGGPRVGNIRFKERIEELGVKVLRVVNEHDVVAKSP 375
PLN02324 PLN02324
triacylglycerol lipase
 30-117 1.28e-04

triacylglycerol lipase


Pssm-ID: 177958  Cd Length: 415  Bit Score: 41.54  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581252  30 MKEDFNTLKHAYPGYEIWVG--GHSLGGSMAALASNYLV---ANGLATSSNLKMI-----TFGEPRTGDKAFADAHDKMV 99
Cdd:PLN02324 199 VQGELKRLLELYKNEEISITftGHSLGAVMSVLSAADLVygkKNKINISLQKKQVpitvfAFGSPRIGDHNFKNLVDSLQ 278

                         90
                 ....*....|....*....
gi 922581252 100 TYS-YRIVHHKDIVPHIPL 117
Cdd:PLN02324 279 PLNiLRIVNVPDVAPHYPL 297
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
37-72 4.87e-04

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 39.48  E-value: 4.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 922581252  37 LKHAYPGYEIWVGGHSLGGSMAALASNYLVANGLAT 72
Cdd:COG4757  100 LRARFPGLPLLLVGHSLGGQLLGLAPNAERVDRLVT 135
PLN02761 PLN02761
lipase class 3 family protein
 46-116 1.13e-03

lipase class 3 family protein


Pssm-ID: 215406 [Multi-domain]  Cd Length: 527  Bit Score: 38.87  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581252  46 IWVGGHSLGGSMAALAS--------NYLVANGLATSsnLKMITFGEPRTGDKAFADAHDKMVTYSYRIVHHKDIVPHIP 116
Cdd:PLN02761 296 ITVTGHSLGASLALVSAydiaelnlNHVPENNYKIP--ITVFSFSGPRVGNLRFKERCDELGVKVLRVVNVHDKVPSVP 372
 
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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