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Conserved domains on  [gi|6324655|ref|NP_014724|]
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triacylglycerol lipase [Saccharomyces cerevisiae S288C]

Protein Classification

DUF3336 and Pat_TGL4-5_like domain-containing protein( domain architecture ID 10570541)

DUF3336 and Pat_TGL4-5_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 110-537 0e+00

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


:

Pssm-ID: 132868  Cd Length: 421  Bit Score: 749.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  110 LLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALI--HQSNMNDHYLLGILQQTRRNIGRTALVLSG 187
Cdd:cd07230   1 LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVddDEDGLEDRYLLGMLLQTRKNFGRTALLLSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  188 GSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNsksPNENLLIKISRF 267
Cdd:cd07230  81 GGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDPD---QEENVLQKLSRF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  268 CQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTP 347
Cdd:cd07230 158 LKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSP 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  348 LFEKDPHTGKIKEWGATnlhlsNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITAR 427
Cdd:cd07230 238 LYEKDPKTGEIVPWNPS-----SVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKSESCVGGEVEDELSAR 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  428 FRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMvGQFHEVLKNPSQLFLLHQTTLGA 507
Cdd:cd07230 313 FKRWLNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRSVLSQKYSGDITILPELNY-SDFPKILKNPTPEFMLDACLRGE 391

                       410       420       430
                ....*....|....*....|....*....|
gi 6324655  508 RATWPKISMIQNNCGQEFALDKAITFLKEK 537
Cdd:cd07230 392 RATWPKLSRIRNHCAIELALDKAIQYLRAR 421
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 40-176 4.62e-43

Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. This family is found in bacteria and eukaryotes. This presumed domain is typically between 143 to 227 amino acids in length.


:

Pssm-ID: 432096  Cd Length: 139  Bit Score: 152.30  E-value: 4.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655     40 RKQLLISDLssqkKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWV 119
Cdd:pfam11815   7 RRKRLRKKL----RNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324655    120 RNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRR 176
Cdd:pfam11815  83 RNFAGIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESPSLSLEEKLEFFKETRK 139
 
Name Accession Description Interval E-value
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 110-537 0e+00

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


Pssm-ID: 132868  Cd Length: 421  Bit Score: 749.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  110 LLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALI--HQSNMNDHYLLGILQQTRRNIGRTALVLSG 187
Cdd:cd07230   1 LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVddDEDGLEDRYLLGMLLQTRKNFGRTALLLSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  188 GSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNsksPNENLLIKISRF 267
Cdd:cd07230  81 GGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDPD---QEENVLQKLSRF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  268 CQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTP 347
Cdd:cd07230 158 LKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSP 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  348 LFEKDPHTGKIKEWGATnlhlsNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITAR 427
Cdd:cd07230 238 LYEKDPKTGEIVPWNPS-----SVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKSESCVGGEVEDELSAR 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  428 FRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMvGQFHEVLKNPSQLFLLHQTTLGA 507
Cdd:cd07230 313 FKRWLNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRSVLSQKYSGDITILPELNY-SDFPKILKNPTPEFMLDACLRGE 391

                       410       420       430
                ....*....|....*....|....*....|
gi 6324655  508 RATWPKISMIQNNCGQEFALDKAITFLKEK 537
Cdd:cd07230 392 RATWPKLSRIRNHCAIELALDKAIQYLRAR 421
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 40-176 4.62e-43

Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. This family is found in bacteria and eukaryotes. This presumed domain is typically between 143 to 227 amino acids in length.


Pssm-ID: 432096  Cd Length: 139  Bit Score: 152.30  E-value: 4.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655     40 RKQLLISDLssqkKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWV 119
Cdd:pfam11815   7 RRKRLRKKL----RNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324655    120 RNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRR 176
Cdd:pfam11815  83 RNFAGIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESPSLSLEEKLEFFKETRK 139
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 180-402 1.29e-27

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 112.69  E-value: 1.29e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  180 RTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEipSLLTNVLNMEFNIFNDDNSKSPNEN 259
Cdd:COG1752   6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSAD--ELEELWRSLDRRDLFDLSLPRRLLR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  260 LLIKISRfcqnGTWFNNQPLINTMLSFLGNLTFREAYnktgkiLNITVSPASIYE-QPKLLNNltAPnvlIWSAVCASCS 338
Cdd:COG1752  84 LDLGLSP----GGLLDGDPLRRLLERLLGDRDFEDLP------IPLAVVATDLETgREVVFDS--GP---LADAVRASAA 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324655  339 LPGVFPSTplfekdphtgkikEWGatnlhlsNMKFMDGSVDNDMPISRLSEMfNVDHIIACQVN 402
Cdd:COG1752 149 IPGVFPPV-------------EID-------GRLYVDGGVVNNLPVDPARAL-GADRVIAVDLN 191
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 183-384 1.62e-23

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 98.45  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655    183 LVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEipSLLTNVLNMEFNIFNDDNSKSPNeNLLI 262
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPE--EIEDLLLELDLNLFLSLIRKRAL-SLLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655    263 KISRFCQNGTWFNNQPLINTMLSFLGNLTFRE-------AYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCA 335
Cdd:pfam01734  78 LLRGLIGEGGLFDGDALRELLRKLLGDLTLEElaarlslLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVLA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 6324655    336 SCSLPGVFPstplfekdPHtgkikewgatnlHLSNMKFMDGSVDNDMPI 384
Cdd:pfam01734 158 SSALPGVFP--------PV------------RLDGELYVDGGLVDNVPV 186
 
Name Accession Description Interval E-value
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 110-537 0e+00

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


Pssm-ID: 132868  Cd Length: 421  Bit Score: 749.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  110 LLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALI--HQSNMNDHYLLGILQQTRRNIGRTALVLSG 187
Cdd:cd07230   1 LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVddDEDGLEDRYLLGMLLQTRKNFGRTALLLSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  188 GSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNsksPNENLLIKISRF 267
Cdd:cd07230  81 GGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDPD---QEENVLQKLSRF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  268 CQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTP 347
Cdd:cd07230 158 LKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSP 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  348 LFEKDPHTGKIKEWGATnlhlsNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITAR 427
Cdd:cd07230 238 LYEKDPKTGEIVPWNPS-----SVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKSESCVGGEVEDELSAR 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  428 FRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMvGQFHEVLKNPSQLFLLHQTTLGA 507
Cdd:cd07230 313 FKRWLNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRSVLSQKYSGDITILPELNY-SDFPKILKNPTPEFMLDACLRGE 391

                       410       420       430
                ....*....|....*....|....*....|
gi 6324655  508 RATWPKISMIQNNCGQEFALDKAITFLKEK 537
Cdd:cd07230 392 RATWPKLSRIRNHCAIELALDKAIQYLRAR 421
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 114-529 2.08e-139

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 411.99  E-value: 2.08e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  114 IRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLT--ALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTF 191
Cdd:cd07206   1 LREGLHGNLGNMGNPSLYRHAYFGTKHLIEDYIEEVDLSLEylALLDTKELSVEEKLDFFRRARHAFGRTALMLSGGASL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  192 GLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIpslltnvlnmefnifnddnskspnenllikisrfcqng 271
Cdd:cd07206  81 GLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL-------------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  272 twfnnqplintmlsfLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEK 351
Cdd:cd07206 123 ---------------IGDLTFQEAYERTGRIINITVAPAEPHQNSRLLNALTSPNVLIWSAVLASCAVPGVFPPVMLMAK 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  352 DPHTGKIKewgatnlHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPllkfsntcvggeiekeitarfrnq 431
Cdd:cd07206 188 NRDGEIVP-------YLPGRKWVDGSVSDDLPAKRLARLYNVNHFIVSQTNPHVVP------------------------ 236

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  432 vtkifkffsdetihfldilkelefhpylmtklkhlFLQQYSGNVTILPDLSmVGQFHEVLKNPSQLFLLHQTTLGARATW 511
Cdd:cd07206 237 -----------------------------------FLQEYSGDITIIPPFS-FSNPLKLLSNPSEDELQRLILEGERATW 280

                       410
                ....*....|....*...
gi 6324655  512 PKISMIQNNCGQEFALDK 529
Cdd:cd07206 281 PKIEMIRTQTRISRTLEE 298
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 120-519 3.07e-88

Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 132870  Cd Length: 407  Bit Score: 283.39  E-value: 3.07e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  120 RNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTFGLFHIGVL 199
Cdd:cd07232   7 NNFAGIENGRLYSETYYGTKNLVEEYIDEVEACLKYLRESSQLDLEEKRRLFKRLSTNYGRTALCLSGGAAFAYYHFGVV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  200 AALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFnifnddnsKSPNENLLIKISRFCQNGTWFNNQPL 279
Cdd:cd07232  87 KALLDADLLPNVISGTSGGSLVAALLCTRTDEELKQLLVPELARKI--------TACEPPWLVWIPRWLKTGARFDSVEW 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  280 INTMLSFL-GNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDP-HTGK 357
Cdd:cd07232 159 ARTCCWFTrGSMTFEEAYERTGRILNISVVPADPHSPTILLNYLTSPNCTIWSAVLASAAVPGILNPVVLMMKDPdGTLI 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  358 IKE-WGatnlhlsnMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITARFRNQ--VTK 434
Cdd:cd07232 239 PPFsFG--------SKWKDGSLRTDIPLKALNTLFNVNFSIVSQVNPHINLFFFSSRGSVGRPVSHRKGRGWRGGflLSA 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  435 IFKFFSDETIHFLDILKELEFHPYLMTKL-KHLFLQQYSGNVTILPDLSmVGQFHEVLKNPSQLFLLHQTTLGARATWPK 513
Cdd:cd07232 311 LEQYLKLDIKKWLKVLRDLELLPRPLGQDwSQIFLQDFSGTITIWPRST-LSDFLRILSDPTPEDLERMIHEGQQAAFPK 389


                ....*.
gi 6324655  514 ISMIQN 519
Cdd:cd07232 390 LHFIKN 395
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 106-531 2.32e-83

Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG lipase activity of the lipid particle. Triacylglycerol (TAG) lipases are also necessary for the mobilization of TAG stored in lipid particles. TGL3 contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes. This family includes Tgl3p from Saccharomyces cerevisiae.


Pssm-ID: 132867  Cd Length: 391  Bit Score: 269.94  E-value: 2.32e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  106 DYHRLLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDY-------LEESQAVLTALIHQSNMNDHYLLGILQQTRRNI 178
Cdd:cd07229   2 DILTLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLLIEEYitevaecLEYVTALQTSPMHSKGFSSQAKLDFFHDTRQSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  179 GRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLT--NVLNMEFNIFNDDNSKSP 256
Cdd:cd07229  82 GRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDgdGIDLSAFNRLRGKKSLGY 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  257 -----NENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWS 331
Cdd:cd07229 162 sgygwLGTLGRRIQRLLREGYFLDVKVLEEFVRANLGDLTFEEAYARTGRVLNITVAPSAVSGSPNLLNYLTAPNVLIWS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  332 AVCAS-CSLPGVFPSTPLFEKDPhTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPllk 410
Cdd:cd07229 242 AALASnASSAALYRSVTLLCKDE-TGSIVPWPPVQVLFFRSWRGANYSERESPLARLSELFNVNHFIVSQARPYLAP--- 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  411 fsntcvggeiekeitarfrnqvtkifkFFSDEtihfldiLKELEFHPylmtklkhlflqqysgNVTILPDLSmVGQFHEV 490
Cdd:cd07229 318 ---------------------------FLSSD-------LHENIPGP----------------NITLVPELS-FSDFLRL 346

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 6324655  491 LKNPSQLFLLHQTTLGARATWPKISMIQNNCGQEFALDKAI 531
Cdd:cd07229 347 FQNPTTDEIQYWILKGERGVWPALAALRVRCAVEFELDDGY 387
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 114-535 9.53e-83

Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.


Pssm-ID: 132869  Cd Length: 323  Bit Score: 266.24  E-value: 9.53e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  114 IRTKWVRNLGNMNNVNLYRHsHTGTKQIIHDYLEESQAVLTALihqSNMNDHYL-----LGILQQTRRNIGRTALVLSGG 188
Cdd:cd07231   1 LRADLVRNLGNMCNPELHKG-RLEVPRLIRDYIAEVKAQLRAV---VESDEDELsleekLAFFQETRHAFGRTALLLSGG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  189 STFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLnmefnifnddnskspnenllikisrfc 268
Cdd:cd07231  77 AALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFFRALL--------------------------- 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  269 qngtwfnnqplintmlsflGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPL 348
Cdd:cd07231 130 -------------------GDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQEL 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  349 FEKDpHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFsntcvggeiekeitarf 428
Cdd:cd07231 191 MAKD-RFGEIVPYHPPGKVSSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRL----------------- 252

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  429 rnqvtkifkffsdetihfldilkelefhpylmtklKHLFLQQYSGNVTILPdLSMVGQFHEVLKNPSQLFLLHQTTLGAR 508
Cdd:cd07231 253 -----------------------------------KKLFAQEWEGDITIVM-PITWKQLLKIIQNPTPEELRKAAMAGER 296

                       410       420
                ....*....|....*....|....*..
gi 6324655  509 ATWPKISMIQNNCGQEFALDKAITFLK 535
Cdd:cd07231 297 CTWEKLSAIESNCGIELTLDECVAELR 323
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 40-176 4.62e-43

Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. This family is found in bacteria and eukaryotes. This presumed domain is typically between 143 to 227 amino acids in length.


Pssm-ID: 432096  Cd Length: 139  Bit Score: 152.30  E-value: 4.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655     40 RKQLLISDLssqkKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWV 119
Cdd:pfam11815   7 RRKRLRKKL----RNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324655    120 RNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRR 176
Cdd:pfam11815  83 RNFAGIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESPSLSLEEKLEFFKETRK 139
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 183-395 1.54e-39

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 143.64  E-value: 1.54e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  183 LVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNvlnmefnifnddnskspnenlli 262
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  263 kisrfcqngtwfnnqplintMLSFLGNLTFREAYNKTGKILNITVSP-----------ASIYEQPKLLNNLTAPNV---- 327
Cdd:cd07198  58 --------------------RLSREVRLRFDGAFPPTGRLLGILRQPllsalpddaheDASGKLFISLTRLTDGENvlvs 117

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324655  328 -----LIWSAVCASCSLPGVFPSTPLFekdphtgkikewgatnlhLSNMKFMDGSVDNDMPISRLSEMFNVDH 395
Cdd:cd07198 118 dtskgELWSAVRASSSIPGYFGPVPLS------------------FRGRRYGDGGLSNNLPVAELGNTINVSP 172
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 180-402 1.29e-27

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 112.69  E-value: 1.29e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  180 RTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEipSLLTNVLNMEFNIFNDDNSKSPNEN 259
Cdd:COG1752   6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSAD--ELEELWRSLDRRDLFDLSLPRRLLR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  260 LLIKISRfcqnGTWFNNQPLINTMLSFLGNLTFREAYnktgkiLNITVSPASIYE-QPKLLNNltAPnvlIWSAVCASCS 338
Cdd:COG1752  84 LDLGLSP----GGLLDGDPLRRLLERLLGDRDFEDLP------IPLAVVATDLETgREVVFDS--GP---LADAVRASAA 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324655  339 LPGVFPSTplfekdphtgkikEWGatnlhlsNMKFMDGSVDNDMPISRLSEMfNVDHIIACQVN 402
Cdd:COG1752 149 IPGVFPPV-------------EID-------GRLYVDGGVVNNLPVDPARAL-GADRVIAVDLN 191
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 183-399 1.49e-23

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 97.49  E-value: 1.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  183 LVLSGGSTFGLFHIGVLAALFESDL--MPKVISGSSAGAIVASIFcvhttqeipslltnvlnmefnifnddnskspnenl 260
Cdd:cd01819   1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL----------------------------------- 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  261 likisrfcqngtwfnnqplintmlsflgnltfreaYNKTGKILNITVSP---ASIYEQPKLLNNLTAPN----------V 327
Cdd:cd01819  46 -----------------------------------YPPSSSLDNKPRQSleeALSGKLWVSFTPVTAGEnvlvsrfvskE 90

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324655  328 LIWSAVCASCSLPGVFPSTPLFEKDPhtgkikewGATNLHLSNMKFMDGSVDNDMPISRLSEMF-NVDHIIAC 399
Cdd:cd01819  91 ELIRALFASGSWPSYFGLIPPAELYT--------SKSNLKEKGVRLVDGGVSNNLPAPVLLRPGrGVTLTISP 155
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 183-384 1.62e-23

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 98.45  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655    183 LVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEipSLLTNVLNMEFNIFNDDNSKSPNeNLLI 262
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPE--EIEDLLLELDLNLFLSLIRKRAL-SLLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655    263 KISRFCQNGTWFNNQPLINTMLSFLGNLTFRE-------AYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCA 335
Cdd:pfam01734  78 LLRGLIGEGGLFDGDALRELLRKLLGDLTLEElaarlslLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVLA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 6324655    336 SCSLPGVFPstplfekdPHtgkikewgatnlHLSNMKFMDGSVDNDMPI 384
Cdd:pfam01734 158 SSALPGVFP--------PV------------RLDGELYVDGGLVDNVPV 186
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 183-385 6.35e-21

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 91.19  E-value: 6.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  183 LVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCV-HTTQEIPSLLtnvLNMEFNIFNDDNSkspneNLL 261
Cdd:cd07207   2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALgYSAADIKDIL---KETDFAKLLDSPV-----GLL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  262 IKISRFCQNGTWFNNQPLINTM--------LSFLGNLTFREAYNKTGKILNITVSPASIyEQPKLLNNLTAPNVLIWSAV 333
Cdd:cd07207  74 FLLPSLFKEGGLYKGDALEEWLrellkektGNSFATSLLRDLDDDLGKDLKVVATDLTT-GALVVFSAETTPDMPVAKAV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6324655  334 CASCSLPGVFpstplfekDPHTgkikewgatnlHLSNMKFMDGSVDNDMPIS 385
Cdd:cd07207 153 RASMSIPFVF--------KPVR-----------LAKGDVYVDGGVLDNYPVW 185
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 181-401 2.27e-16

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 77.59  E-value: 2.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  181 TALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCV-HTTQEIPSLLTNvLNMEFNIFNDDNSKSPNen 259
Cdd:cd07205   1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAgYSPEEIEERAKL-RSTDLKALSDLTIPTAG-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  260 lLIKISRFcqngtwfnnqplINTMLSFLGNLTFREaynktgkiLNITVSPASiyeqpkllNNLTAPNVLI------WSAV 333
Cdd:cd07205  78 -LLRGDKF------------LELLDEYFGDRDIED--------LWIPFFIVA--------TDLTSGKLVVfrsgslVRAV 128

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324655  334 CASCSLPGVFPstPLFEKdphtgkikewgatnlhlsNMKFMDGSVDNDMPISRLSEMfNVDHIIACQV 401
Cdd:cd07205 129 RASMSIPGIFP--PVKID------------------GQLLVDGGVLNNLPVDVLREL-GADIIIAVDL 175
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 183-402 1.01e-13

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 70.78  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  183 LVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLltnvlnmefnifnddnskspnENLLI 262
Cdd:cd07209   1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPEAVERL---------------------EKLWR 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  263 KISRfcqNGTWFNNQPLINTMLSFLGNLTFREAYNKTGkILNITvSPASIYEQpkllnnlTAPNVLIWSAVCASCSLPGV 342
Cdd:cd07209  60 ELSR---EDVFLRGLLDRALDFDTLRLLAILFAGLVIV-AVNVL-TGEPVYFD-------DIPDGILPEHLLASAALPPF 127

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  343 FPSTplfekdphtgKIKEwgatnlhlsnMKFMDGSVDNDMPISRLSEMfNVDHIIACQVN 402
Cdd:cd07209 128 FPPV----------EIDG----------RYYWDGGVVDNTPLSPAIDL-GADEIIVVSLS 166
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 181-227 7.59e-11

Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 62.75  E-value: 7.59e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6324655  181 TALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCV 227
Cdd:cd07210   1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFAS 47
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 183-344 1.69e-06

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 50.30  E-value: 1.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  183 LVLSGGSTFGLFHIGVLAALFESDLMP-KVISGSSAGAIVAsifcvhttqeiPSLLTNVLNMEFNiFNDDNSKSPNenlL 261
Cdd:cd07208   1 LVLEGGGMRGAYTAGVLDAFLEAGIRPfDLVIGVSAGALNA-----------ASYLSGQRGRALR-INTKYATDPR---Y 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  262 IKISRFCQNGTWFNNQPLINTMLSFLGNLTFrEAYNKTGKILNITVSPASIYeQPKLLnNLTAPNVLIWSAVCASCSLPG 341
Cdd:cd07208  66 LGLRSLLRTGNLFDLDFLYDELPDGLDPFDF-EAFAASPARFYVVATDADTG-EAVYF-DKPDILDDLLDALRASSALPG 142


                ...
gi 6324655  342 VFP 344
Cdd:cd07208 143 LFP 145
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
177-344 2.91e-06

Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 49.78  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  177 NIGRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASifcvhttqeipSLLTNV--LNMEFNI-FNDDNS 253
Cdd:COG4667   2 NMMKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGA-----------SYLSRQpgRARRVITdYATDPR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  254 kspnenlLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFrEAYNKTGKILNITVSPAS----IYEQPKLLNnltaPNVLI 329
Cdd:COG4667  71 -------FFSLRNFLRGGNLFDLDFLYDEIPNELLPFDF-ETFKASPREFYVVATNADtgeaEYFSKKDDD----YDLLD 138

                       170
                ....*....|....*
gi 6324655  330 WsaVCASCSLPGVFP 344
Cdd:COG4667 139 A--LRASSALPLLYP 151
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 182-401 1.53e-05

Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 46.11  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  182 ALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCvhtTQEIPSLLTNVLNMefnifnddnskspnenll 261
Cdd:cd07228   2 GLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYA---AGHLDALEEWVRSL------------------ 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324655  262 ikisrfcqngTWFNNQPLINTMLSFLGNLtfreaynKTGKILNI---TVSPASIYEQPKLL-----NNLTAPNVLI---- 329
Cdd:cd07228  61 ----------SQRDVLRLLDLSASRSGLL-------KGEKVLEYlreIMGGVTIEELPIPFaavatDLQTGKEVWFregs 123

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324655  330 -WSAVCASCSLPGVFpstplfekDPHtgkikewgatnlHLSNMKFMDGSVDNDMPISrLSEMFNVDHIIACQV 401
Cdd:cd07228 124 lIDAIRASISIPGIF--------APV------------EHNGRLLVDGGVVNPIPVS-VARALGADIVIAVDL 175
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 180-228 1.25e-03

Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologous to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.


Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 41.62  E-value: 1.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6324655  180 RTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVH 228
Cdd:cd07225  15 SIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEE 63
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 175-229 1.71e-03

Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This family includes NTE1 from fungi.


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 40.94  E-value: 1.71e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324655  175 RRNIGRT-ALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHT 229
Cdd:cd07227   4 RRLCGQAiGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREA 59
 
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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