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Conserved domains on  [gi|767168202|gb|AJS44346|]
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Tgl4p [Saccharomyces cerevisiae YJM1307]

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 ...
 210-632 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: 806.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 210 LLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLME---SDLDDSYLLGILQQTRRNIGRTALVLSG 286
Cdd:cd07230    1 LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVDddeDGLEDRYLLGMLLQTRKNFGRTALLLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 287 GGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQkseSENLLIKISRF 366
Cdd:cd07230   81 GGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDPDQ---EENVLQKLSRF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 367 FKNGTWFDNKHLVNTMIGFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSP 446
Cdd:cd07230  158 LKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 447 LYEKDPKTGERKPWTGsSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQN 526
Cdd:cd07230  238 LYEKDPKTGEIVPWNP-SSVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKSESCVGGEVEDELSARFKRW 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 527 LSSIYNFMANEAIHILEIGSEMGIAKNALTKLRSVLSQQYSGDITILPDMCMLfRIKELLSNPTKEFLLREITNGAKATW 606
Cdd:cd07230  317 LNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRSVLSQKYSGDITILPELNYS-DFPKILKNPTPEFMLDACLRGERATW 395

                        410       420
                 ....*....|....*....|....*.
gi 767168202 607 PKVSIIQNHCGQEFALDKAISYIKGR 632
Cdd:cd07230  396 PKLSRIRNHCAIELALDKAIQYLRAR 421
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 139-275 6.66e-48

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: 166.55  E-value: 6.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  139 YERDILIDKvcsqKQHAMSFEEWCSAGARLDDLTGKTEWKQKLESPLYDYKLIKDLTSRMREERLNRNYAQLLYIIRTNW 218
Cdd:pfam11815   6 GRRKRLRKK----LRNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767168202  219 VRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMES-DLDDSYLLGILQQTRR 275
Cdd:pfam11815  82 KRNFAGIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESpSLSLEEKLEFFKETRK 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 ...
 210-632 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: 806.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 210 LLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLME---SDLDDSYLLGILQQTRRNIGRTALVLSG 286
Cdd:cd07230    1 LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVDddeDGLEDRYLLGMLLQTRKNFGRTALLLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 287 GGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQkseSENLLIKISRF 366
Cdd:cd07230   81 GGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDPDQ---EENVLQKLSRF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 367 FKNGTWFDNKHLVNTMIGFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSP 446
Cdd:cd07230  158 LKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 447 LYEKDPKTGERKPWTGsSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQN 526
Cdd:cd07230  238 LYEKDPKTGEIVPWNP-SSVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKSESCVGGEVEDELSARFKRW 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 527 LSSIYNFMANEAIHILEIGSEMGIAKNALTKLRSVLSQQYSGDITILPDMCMLfRIKELLSNPTKEFLLREITNGAKATW 606
Cdd:cd07230  317 LNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRSVLSQKYSGDITILPELNYS-DFPKILKNPTPEFMLDACLRGERATW 395

                        410       420
                 ....*....|....*....|....*.
gi 767168202 607 PKVSIIQNHCGQEFALDKAISYIKGR 632
Cdd:cd07230  396 PKLSRIRNHCAIELALDKAIQYLRAR 421
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 139-275 6.66e-48

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: 166.55  E-value: 6.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  139 YERDILIDKvcsqKQHAMSFEEWCSAGARLDDLTGKTEWKQKLESPLYDYKLIKDLTSRMREERLNRNYAQLLYIIRTNW 218
Cdd:pfam11815   6 GRRKRLRKK----LRNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767168202  219 VRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMES-DLDDSYLLGILQQTRR 275
Cdd:pfam11815  82 KRNFAGIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESpSLSLEEKLEFFKETRK 139
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 279-497 7.41e-28

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 113.46  E-value: 7.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 279 RTALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEipVLLNHILDKEFNIFKDDKQKSESEN 358
Cdd:COG1752    6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSAD--ELEELWRSLDRRDLFDLSLPRRLLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 359 LLIKISRffknGTWFDNKHLVNTMIGFLGDLTFRE--------AYN-RTGKILnitvspasLFEQPRLlnnltapnvliW 429
Cdd:COG1752   84 LDLGLSP----GGLLDGDPLRRLLERLLGDRDFEDlpiplavvATDlETGREV--------VFDSGPL-----------A 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767168202 430 SAVCASCSLPGIFPSsplYEKDpktGERkpwtgsssvkFVDGSVDNDLPISRLSEMfNVDHIIACQVN 497
Cdd:COG1752  141 DAVRASAAIPGVFPP---VEID---GRL----------YVDGGVVNNLPVDPARAL-GADRVIAVDLN 191
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 282-479 9.70e-27

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: 108.08  E-value: 9.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  282 LVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHK-EEIPVLLNHILDKEFnifkDDKQKSESENLL 360
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpEEIEDLLLELDLNLF----LSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  361 IKISRFFKNGTWFDNKHLVNTMIGFLGDLTFRE-------AYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVC 433
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLTLEElaarlslLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767168202  434 ASCSLPGIFPSSPLYEKdpktgerkpwtgsssvKFVDGSVDNDLPI 479
Cdd:pfam01734 157 ASSALPGVFPPVRLDGE----------------LYVDGGLVDNVPV 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 ...
 210-632 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: 806.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 210 LLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLME---SDLDDSYLLGILQQTRRNIGRTALVLSG 286
Cdd:cd07230    1 LLYLIRTTLSRDLGNMGNVNLYRHSHVGTKKLIERYITEALLTLEYLVDddeDGLEDRYLLGMLLQTRKNFGRTALLLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 287 GGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQkseSENLLIKISRF 366
Cdd:cd07230   81 GGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDPDQ---EENVLQKLSRF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 367 FKNGTWFDNKHLVNTMIGFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSP 446
Cdd:cd07230  158 LKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVFPSSP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 447 LYEKDPKTGERKPWTGsSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQN 526
Cdd:cd07230  238 LYEKDPKTGEIVPWNP-SSVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKSESCVGGEVEDELSARFKRW 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 527 LSSIYNFMANEAIHILEIGSEMGIAKNALTKLRSVLSQQYSGDITILPDMCMLfRIKELLSNPTKEFLLREITNGAKATW 606
Cdd:cd07230  317 LNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLRSVLSQKYSGDITILPELNYS-DFPKILKNPTPEFMLDACLRGERATW 395

                        410       420
                 ....*....|....*....|....*.
gi 767168202 607 PKVSIIQNHCGQEFALDKAISYIKGR 632
Cdd:cd07230  396 PKLSRIRNHCAIELALDKAIQYLRAR 421
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 214-624 4.31e-130

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: 392.73  E-value: 4.31e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 214 IRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMESD---LDDSYLLGILQQTRRNIGRTALVLSGGGTF 290
Cdd:cd07206    1 LREGLHGNLGNMGNPSLYRHAYFGTKHLIEDYIEEVDLSLEYLALLDtkeLSVEEKLDFFRRARHAFGRTALMLSGGASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 291 GLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIpvllnhildkefnifkddkqksesenllikisrffkng 370
Cdd:cd07206   81 GLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL-------------------------------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 371 twfdnkhlvntmigfLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEK 450
Cdd:cd07206  123 ---------------IGDLTFQEAYERTGRIINITVAPAEPHQNSRLLNALTSPNVLIWSAVLASCAVPGVFPPVMLMAK 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 451 DPKtGERKPWtgSSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLklslscvggeiedefsarlkqnlssi 530
Cdd:cd07206  188 NRD-GEIVPY--LPGRKWVDGSVSDDLPAKRLARLYNVNHFIVSQTNPHVVPFL-------------------------- 238

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 531 ynfmaneaihileigsemgiaknaltklrsvlsQQYSGDITILPDmcmlFR---IKELLSNPTKEFLLREITNGAKATWP 607
Cdd:cd07206  239 ---------------------------------QEYSGDITIIPP----FSfsnPLKLLSNPSEDELQRLILEGERATWP 281

                        410
                 ....*....|....*..
gi 767168202 608 KVSIIQNHCGQEFALDK 624
Cdd:cd07206  282 KIEMIRTQTRISRTLEE 298
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 220-626 3.30e-95

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: 305.73  E-value: 3.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 220 RNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMESDLDDSY-LLGILQQTRRNIGRTALVLSGGGTFGLFHIGVL 298
Cdd:cd07232    7 NNFAGIENGRLYSETYYGTKNLVEEYIDEVEACLKYLRESSQLDLEeKRRLFKRLSTNYGRTALCLSGGAAFAYYHFGVV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 299 GTLFELDLLPRVISGSSAGAIVASILSVHHKEEI-----PVLLNHIldkefnifkddkqKSESENLLIKISRFFKNGTWF 373
Cdd:cd07232   87 KALLDADLLPNVISGTSGGSLVAALLCTRTDEELkqllvPELARKI-------------TACEPPWLVWIPRWLKTGARF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 374 DNKHLVNTMIGFL-GDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEKDP 452
Cdd:cd07232  154 DSVEWARTCCWFTrGSMTFEEAYERTGRILNISVVPADPHSPTILLNYLTSPNCTIWSAVLASAAVPGILNPVVLMMKDP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 453 KTGERKPWTGSSsvKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQN--LSSI 530
Cdd:cd07232  234 DGTLIPPFSFGS--KWKDGSLRTDIPLKALNTLFNVNFSIVSQVNPHINLFFFSSRGSVGRPVSHRKGRGWRGGflLSAL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 531 YNFMANEAIHILEIGSEMGIAKNALTKLRS-VLSQQYSGDITILPDmCMLFRIKELLSNPTKEFLLREITNGAKATWPKV 609
Cdd:cd07232  312 EQYLKLDIKKWLKVLRDLELLPRPLGQDWSqIFLQDFSGTITIWPR-STLSDFLRILSDPTPEDLERMIHEGQQAAFPKL 390

                        410
                 ....*....|....*..
gi 767168202 610 SIIQNHCGQEFALDKAI 626
Cdd:cd07232  391 HFIKNRMRIEKAIEDGR 407
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 214-627 6.06e-89

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: 285.89  E-value: 6.06e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 214 IRTNWVRNLGNMGNVNLYRHsHVGTKYLIDEYMMESRLALESLMESDLDDSYL---LGILQQTRRNIGRTALVLSGGGTF 290
Cdd:cd07231    1 LRADLVRNLGNMCNPELHKG-RLEVPRLIRDYIAEVKAQLRAVVESDEDELSLeekLAFFQETRHAFGRTALLLSGGAAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 291 GLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIpvllnhildkefnifkddkqksesenllikiSRFFKng 370
Cdd:cd07231   80 GTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEEL-------------------------------QSFFR-- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 371 twfdnkhlvntmiGFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEK 450
Cdd:cd07231  127 -------------ALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAK 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 451 DpKTGERKPW----TGSSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLklslscvggeiedefsarlkqn 526
Cdd:cd07231  194 D-RFGEIVPYhppgKVSSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLL---------------------- 250

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 527 lssiynfmaneaihileigsemgiaknaltKLRSVLSQQYSGDITILpdmcMLFRIKELL---SNPTKEFLLREITNGAK 603
Cdd:cd07231  251 ------------------------------RLKKLFAQEWEGDITIV----MPITWKQLLkiiQNPTPEELRKAAMAGER 296

                        410       420
                 ....*....|....*....|....
gi 767168202 604 ATWPKVSIIQNHCGQEFALDKAIS 627
Cdd:cd07231  297 CTWEKLSAIESNCGIELTLDECVA 320
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 209-626 2.30e-85

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: 278.80  E-value: 2.30e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 209 QLLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMESDLDDSYLLGILQQ--------TRRNIGRT 280
Cdd:cd07229    5 TLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLLIEEYITEVAECLEYVTALQTSPMHSKGFSSQakldffhdTRQSFGRT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 281 ALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLN--HILDKEFNIFKDDKQKSES-- 356
Cdd:cd07229   85 ALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDgdGIDLSAFNRLRGKKSLGYSgy 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 357 ---ENLLIKISRFFKNGTWFDNKHLVNTMIGFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVC 433
Cdd:cd07229  165 gwlGTLGRRIQRLLREGYFLDVKVLEEFVRANLGDLTFEEAYARTGRVLNITVAPSAVSGSPNLLNYLTAPNVLIWSAAL 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 434 AS-CSLPGIFPSSPLYEKDPkTGERKPWTGSSSVKF----VDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSL 508
Cdd:cd07229  245 ASnASSAALYRSVTLLCKDE-TGSIVPWPPVQVLFFrswrGANYSERESPLARLSELFNVNHFIVSQARPYLAPFLSSDL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 509 scvggeiedefsarlkqnlssiynfmaNEAIHILEigsemgiaknaltklrsvlsqqysgdITILPDMCmLFRIKELLSN 588
Cdd:cd07229  324 ---------------------------HENIPGPN--------------------------ITLVPELS-FSDFLRLFQN 349

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 767168202 589 PTKEFLLREITNGAKATWPKVSIIQNHCGQEFALDKAI 626
Cdd:cd07229  350 PTTDEIQYWILKGERGVWPALAALRVRCAVEFELDDGY 387
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 139-275 6.66e-48

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: 166.55  E-value: 6.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  139 YERDILIDKvcsqKQHAMSFEEWCSAGARLDDLTGKTEWKQKLESPLYDYKLIKDLTSRMREERLNRNYAQLLYIIRTNW 218
Cdd:pfam11815   6 GRRKRLRKK----LRNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767168202  219 VRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMES-DLDDSYLLGILQQTRR 275
Cdd:pfam11815  82 KRNFAGIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESpSLSLEEKLEFFKETRK 139
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 282-490 1.28e-36

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: 135.93  E-value: 1.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 282 LVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHhkeeipvllnhildkefnifkddkqKSESENLli 361
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASG-------------------------RDLEEAL-- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 362 kisrffkngtwfdnkhLVNTMIGFLGDLTFREAYNRTGKILNITVSPASLF-----------EQPRLLNNLTAPNV---- 426
Cdd:cd07198   54 ----------------LLLLRLSREVRLRFDGAFPPTGRLLGILRQPLLSAlpddahedasgKLFISLTRLTDGENvlvs 117

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767168202 427 -----LIWSAVCASCSLPGIFPSSPLYEKDpktgerkpwtgsssVKFVDGSVDNDLPISRLSEMFNVDH 490
Cdd:cd07198  118 dtskgELWSAVRASSSIPGYFGPVPLSFRG--------------RRYGDGGLSNNLPVAELGNTINVSP 172
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 279-497 7.41e-28

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 113.46  E-value: 7.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 279 RTALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEipVLLNHILDKEFNIFKDDKQKSESEN 358
Cdd:COG1752    6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSAD--ELEELWRSLDRRDLFDLSLPRRLLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 359 LLIKISRffknGTWFDNKHLVNTMIGFLGDLTFRE--------AYN-RTGKILnitvspasLFEQPRLlnnltapnvliW 429
Cdd:COG1752   84 LDLGLSP----GGLLDGDPLRRLLERLLGDRDFEDlpiplavvATDlETGREV--------VFDSGPL-----------A 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767168202 430 SAVCASCSLPGIFPSsplYEKDpktGERkpwtgsssvkFVDGSVDNDLPISRLSEMfNVDHIIACQVN 497
Cdd:COG1752  141 DAVRASAAIPGVFPP---VEID---GRL----------YVDGGVVNNLPVDPARAL-GADRVIAVDLN 191
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 282-479 9.70e-27

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: 108.08  E-value: 9.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  282 LVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHK-EEIPVLLNHILDKEFnifkDDKQKSESENLL 360
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpEEIEDLLLELDLNLF----LSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202  361 IKISRFFKNGTWFDNKHLVNTMIGFLGDLTFRE-------AYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVC 433
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLTLEElaarlslLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767168202  434 ASCSLPGIFPSSPLYEKdpktgerkpwtgsssvKFVDGSVDNDLPI 479
Cdd:pfam01734 157 ASSALPGVFPPVRLDGE----------------LYVDGGLVDNVPV 186
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 282-480 2.55e-24

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: 101.20  E-value: 2.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 282 LVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHK-EEIPVLLNHILdkeFNIFKDDkqkseSENLL 360
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSaADIKDILKETD---FAKLLDS-----PVGLL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 361 IKISRFFKNGTWFDNKHLVNTM--------IGFLGDLTFREAYNRTGKILNITVSPASLfEQPRLLNNLTAPNVLIWSAV 432
Cdd:cd07207   74 FLLPSLFKEGGLYKGDALEEWLrellkektGNSFATSLLRDLDDDLGKDLKVVATDLTT-GALVVFSAETTPDMPVAKAV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767168202 433 CASCSLPGIFPSSPLYEKDpktgerkpwtgsssvKFVDGSVDNDLPIS 480
Cdd:cd07207  153 RASMSIPFVFKPVRLAKGD---------------VYVDGGVLDNYPVW 185
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 282-494 5.83e-19

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: 84.77  E-value: 5.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 282 LVLSGGGTFGLFHIGVLGTLFELDLL--PRVISGSSAGAIVASILsvhhkeeipvllnhildkefnifkddkqksesenl 359
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAATL----------------------------------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 360 likisrffkngtwfdnkhlvntmigflgdltfreaYNRTGKILNITVSP---ASLFEQPRLLNNLTAPN----------V 426
Cdd:cd01819   46 -----------------------------------YPPSSSLDNKPRQSleeALSGKLWVSFTPVTAGEnvlvsrfvskE 90

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767168202 427 LIWSAVCASCSLPGIFPSSPLYEKDPKTGERKpwtgSSSVKFVDGSVDNDLPISRLSEMF-NVDHIIAC 494
Cdd:cd01819   91 ELIRALFASGSWPSYFGLIPPAELYTSKSNLK----EKGVRLVDGGVSNNLPAPVLLRPGrGVTLTISP 155
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 280-496 2.25e-15

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: 74.89  E-value: 2.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 280 TALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASI----LSVHHKEEIPVLLNHildkefnIFKDDKQKSE 355
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALyaagYSPEEIEERAKLRST-------DLKALSDLTI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 356 SENLLIKISRFFKngtWFDNkhlvntmigFLGDLTFREaynrtgkiLNITVSPASlfeqprllNNLTAPNVLI------W 429
Cdd:cd07205   74 PTAGLLRGDKFLE---LLDE---------YFGDRDIED--------LWIPFFIVA--------TDLTSGKLVVfrsgslV 125

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767168202 430 SAVCASCSLPGIFPssPLYEKDpktgerkpwtgsssVKFVDGSVDNDLPISRLSEMfNVDHIIACQV 496
Cdd:cd07205  126 RAVRASMSIPGIFP--PVKIDG--------------QLLVDGGVLNNLPVDVLREL-GADIIIAVDL 175
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 282-497 7.74e-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: 68.47  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 282 LVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILsVHHKEEIPVLLNHILDKefnifkddkqksesenllI 361
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALI-AGGDPEAVERLEKLWRE------------------L 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 362 KISRFFKNGtwFDNKHLVNTMIGFLGDLTFR---EAYN-RTGkilnitvspaslfeQPRLLNNLtaPNVLIWSAVCASCS 437
Cdd:cd07209   62 SREDVFLRG--LLDRALDFDTLRLLAILFAGlviVAVNvLTG--------------EPVYFDDI--PDGILPEHLLASAA 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 438 LPGIFPSsplyekdPKTGERkpwtgsssvKFVDGSVDNDLPISRLSEMfNVDHIIACQVN 497
Cdd:cd07209  124 LPPFFPP-------VEIDGR---------YYWDGGVVDNTPLSPAIDL-GADEIIVVSLS 166
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 282-492 3.62e-12

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: 67.63  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 282 LVLSGGGTFGLFHIGVLGTLFELDLLP-RVISGSSAGAIV-ASILSVHHKEEIPVLLNHILDKEFnifkddkqksesenl 359
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPfDLVIGVSAGALNaASYLSGQRGRALRINTKYATDPRY--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 360 lIKISRFFKNGTWFDNKHLVNTMIGFLGDLTFrEAYNRTGKILNITVSPASlFEQPRLLnNLTAPNVLIWSAVCASCSLP 439
Cdd:cd07208   66 -LGLRSLLRTGNLFDLDFLYDELPDGLDPFDF-EAFAASPARFYVVATDAD-TGEAVYF-DKPDILDDLLDALRASSALP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767168202 440 GIFPSSPLYEkdpktgerkpwtgsssVKFVDGSVDNDLPISRLSEMfNVDHII 492
Cdd:cd07208  142 GLFPPVRIDG----------------EPYVDGGLSDSIPVDKAIED-GADKIV 177
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
276-479 2.73e-11

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 65.19  E-value: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 276 NIGRTALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAI-VASILSVHHKEEIPVLLNHILDKEFNIFKddkqks 354
Cdd:COG4667    2 NMMKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALnGASYLSRQPGRARRVITDYATDPRFFSLR------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 355 esenllikisRFFKNGTWFDNKHLVNTMIGFLGDLTFrEAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWsaVCA 434
Cdd:COG4667   76 ----------NFLRGGNLFDLDFLYDEIPNELLPFDF-ETFKASPREFYVVATNADTGEAEYFSKKDDDYDLLDA--LRA 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767168202 435 SCSLPGIfpsSPLYEKDpktGerkpwtgsssVKFVDGSVDNDLPI 479
Cdd:COG4667  143 SSALPLL---YPPVEID---G----------KRYLDGGVADSIPV 171
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 280-324 7.71e-09

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: 56.97  E-value: 7.71e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767168202 280 TALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASIL 324
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLF 45
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 281-496 3.06e-06

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: 48.42  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 281 ALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHkeeipvllnhilDKEFNIFKDDKQKSESENLL 360
Cdd:cd07228    2 GLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGH------------LDALEEWVRSLSQRDVLRLL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 361 -IKISRffknGTWFDNKHLVNTMIGFLGDLTFREAYNRTGKI-LNITVSPASLFEQPRLLnnltapnvliwSAVCASCSL 438
Cdd:cd07228   70 dLSASR----SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVaTDLQTGKEVWFREGSLI-----------DAIRASISI 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 439 PGIFpssplyekdpktgerKP--WTGSssvKFVDGSVDNDLPISrLSEMFNVDHIIACQV 496
Cdd:cd07228  135 PGIF---------------APveHNGR---LLVDGGVVNPIPVS-VARALGADIVIAVDL 175
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 282-443 7.34e-03

Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 39.55  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 282 LVLSGGGTFGLFHIGVL-----GTLFELDLLPRVISGSSAGAIVASILSVHHK-----EEIPVLLNHildkefNIFKDDK 351
Cdd:cd07211   11 LSIDGGGTRGVVALEILrkiekLTGKPIHELFDYICGVSTGAILAFLLGLKKMsldecEELYRKLGK------DVFSQNT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767168202 352 QKSESENLLIKISrFFKNGTWfdnKHLVNTMIGFLGDLTFrEAYNRTGKI--LNITVSPASLfeQPRLLNNLTAP----- 424
Cdd:cd07211   85 YISGTSRLVLSHA-YYDTETW---EKILKEMMGSDELIDT-SADPNCPKVacVSTQVNRTPL--KPYVFRNYNHPpgtrs 157

                        170       180
                 ....*....|....*....|....*
gi 767168202 425 ------NVLIWSAVCASCSLPGIFP 443
Cdd:cd07211  158 hylgscKHKLWEAIRASSAAPGYFE 182
 
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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