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Conserved domains on  [gi|1063729809|ref|NP_001332745|]
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Patatin-like phospholipase family protein [Arabidopsis thaliana]

Protein Classification

patatin-like phospholipase family protein( domain architecture ID 10570544)

patatin-like phospholipase family protein containing a DUF3336 domain, may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 162-571 0e+00

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: 611.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 162 MRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLG 241
Cdd:cd07231     1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 242 AFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFenslhslqffdqlggvfsivkrvmtqgalhdirql 321
Cdd:cd07231    81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 322 qcmlRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVP 401
Cdd:cd07231   126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 402 YHPPFnldpevgtKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRLKdlvrayggrfaaklahlvem 481
Cdd:cd07231   202 YHPPG--------KVSSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK-------------------- 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 482 evkhrcnqvlelgfplgglaKLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIEL 561
Cdd:cd07231   254 --------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGIEL 313

                         410
                  ....*....|
gi 1063729809 562 ALDDSVAILN 571
Cdd:cd07231   314 TLDECVAELR 323
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 96-225 1.94e-45

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: 159.23  E-value: 1.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809  96 YRRKFWRNMMRTALTYEEWAHAAKMLE--------KETPkmnESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLV 167
Cdd:pfam11815   6 GRRKRLRKKLRNAKSYEEWKEAAKELDellgndewKEND---ESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063729809 168 RNLGNMCNSELHK-GRLQVPRHIKEYIDEVSTQLRMVCNSDSeeLSLEEKLSFMHETRH 225
Cdd:pfam11815  83 RNFAGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLAESPS--LSLEEKLEFFKETRK 139
 
Name Accession Description Interval E-value
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 162-571 0e+00

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: 611.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 162 MRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLG 241
Cdd:cd07231     1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 242 AFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFenslhslqffdqlggvfsivkrvmtqgalhdirql 321
Cdd:cd07231    81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 322 qcmlRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVP 401
Cdd:cd07231   126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 402 YHPPFnldpevgtKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRLKdlvrayggrfaaklahlvem 481
Cdd:cd07231   202 YHPPG--------KVSSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK-------------------- 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 482 evkhrcnqvlelgfplgglaKLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIEL 561
Cdd:cd07231   254 --------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGIEL 313

                         410
                  ....*....|
gi 1063729809 562 ALDDSVAILN 571
Cdd:cd07231   314 TLDECVAELR 323
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 96-225 1.94e-45

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: 159.23  E-value: 1.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809  96 YRRKFWRNMMRTALTYEEWAHAAKMLE--------KETPkmnESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLV 167
Cdd:pfam11815   6 GRRKRLRKKLRNAKSYEEWKEAAKELDellgndewKEND---ESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063729809 168 RNLGNMCNSELHK-GRLQVPRHIKEYIDEVSTQLRMVCNSDSeeLSLEEKLSFMHETRH 225
Cdd:pfam11815  83 RNFAGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLAESPS--LSLEEKLEFFKETRK 139
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 229-492 2.04e-24

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 103.44  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 229 RTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVAS-RSWPELQSFFEnSLHSLQFFD-QLGGVFSIV 306
Cdd:COG1752     6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWR-SLDRRDLFDlSLPRRLLRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 307 KRVMTQGALHDIRQLQCMLRNLTSNLTFQEAydmtGRILGITVCSprkhepprclnyLTSPHVVIWS------AVTASCA 380
Cdd:COG1752    85 DLGLSPGGLLDGDPLRRLLERLLGDRDFEDL----PIPLAVVATD------------LETGREVVFDsgpladAVRASAA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 381 FPGLFeaqelmakdrsgeivpyhPPFNLDpevgtksssGRRWRDGSLeVD-LPMMQLKELfNVNHFIVSQANPHIAPLLR 459
Cdd:COG1752   149 IPGVF------------------PPVEID---------GRLYVDGGV-VNnLPVDPARAL-GADRVIAVDLNPPLRKLPS 199

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1063729809 460 LKD-LVRAYGGRFAAKLAHLVEMEvkhRCNQVLE 492
Cdd:COG1752   200 LLDiLGRALEIMFNSILRRELALE---PADILIE 230
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 232-390 1.39e-19

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: 87.28  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWP-ELQSFFENSLHSL---QFFDQLGGVFSIVK 307
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPeEIEDLLLELDLNLflsLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 308 RVMTQGALHDIRQLQCMLRNLTSNLTFQEA--------YDMTGRILGITVCSPRKHEPPRcLNYLTSPHVVIWSAVTASC 379
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEELaarlslllVVALRALLTVISTALGTRARIL-LPDDLDDDEDLADAVLASS 159

                         170
                  ....*....|.
gi 1063729809 380 AFPGLFEAQEL 390
Cdd:pfam01734 160 ALPGVFPPVRL 170
PRK10279 PRK10279
patatin-like phospholipase RssA;
232-385 7.94e-05

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 45.47  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELqsffENSLHSLQFFD---------QLGG- 301
Cdd:PRK10279    8 LALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSAL----EDWVTSFSYWDvlrlmdlswQRGGl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 302 -----VFSIVKRVMTqgaLHDIRQLQCMLRNLTSNLTfqeaydmTGRILgitvcsprkhepprclnYLTSPHvvIWSAVT 376
Cdd:PRK10279   84 lrgerVFNQYREIMP---ETEIENCSRRFGAVATNLS-------TGREL-----------------WFTEGD--LHLAIR 134


                  ....*....
gi 1063729809 377 ASCAFPGLF 385
Cdd:PRK10279  135 ASCSMPGLM 143
 
Name Accession Description Interval E-value
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 162-571 0e+00

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: 611.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 162 MRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLG 241
Cdd:cd07231     1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 242 AFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFenslhslqffdqlggvfsivkrvmtqgalhdirql 321
Cdd:cd07231    81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 322 qcmlRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVP 401
Cdd:cd07231   126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 402 YHPPFnldpevgtKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRLKdlvrayggrfaaklahlvem 481
Cdd:cd07231   202 YHPPG--------KVSSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK-------------------- 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 482 evkhrcnqvlelgfplgglaKLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIEL 561
Cdd:cd07231   254 --------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGIEL 313

                         410
                  ....*....|
gi 1063729809 562 ALDDSVAILN 571
Cdd:cd07231   314 TLDECVAELR 323
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 162-565 4.15e-147

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: 433.95  E-value: 4.15e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 162 MRADLVRNLGNMCNSELHKGRLQVPRH-IKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASL 240
Cdd:cd07206     1 LREGLHGNLGNMGNPSLYRHAYFGTKHlIEDYIEEVDLSLEYLALLDTKELSVEEKLDFFRRARHAFGRTALMLSGGASL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 241 GAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELqsffenslhslqffdqlggvfsivkrvmtqgalhdirq 320
Cdd:cd07206    81 GLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL-------------------------------------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 321 lqcmlrnlTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIV 400
Cdd:cd07206   123 --------IGDLTFQEAYERTGRIINITVAPAEPHQNSRLLNALTSPNVLIWSAVLASCAVPGVFPPVMLMAKNRDGEIV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 401 PYHPpfnldpevgtksssGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPllrlkdlvrayggrfaaklahlve 480
Cdd:cd07206   195 PYLP--------------GRKWVDGSVSDDLPAKRLARLYNVNHFIVSQTNPHVVP------------------------ 236

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 481 mevkhrcnqvlelgfplgglaklFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIE 560
Cdd:cd07206   237 -----------------------FLQEYSGDITIIPPFSFSNPLKLLSNPSEDELQRLILEGERATWPKIEMIRTQTRIS 293


                  ....*
gi 1063729809 561 LALDD 565
Cdd:cd07206   294 RTLEE 298
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 158-570 2.33e-120

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: 369.63  E-value: 2.33e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 158 IMFCMRADLVRNLGNMCNSELHkgrlqvpRH--------IKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGR 229
Cdd:cd07230     1 LLYLIRTTLSRDLGNMGNVNLY-------RHshvgtkklIERYITEALLTLEYLVDDDEDGLEDRYLLGMLLQTRKNFGR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 230 TALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENSLHS-LQFF---DQLGGVFSI 305
Cdd:cd07230    74 TALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGdFNVFedpDQEENVLQK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 306 VKRVMTQGALHDIRQLQCMLRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLF 385
Cdd:cd07230   154 LSRFLKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVPGVF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 386 EAQELMAKD-RSGEIVPYHPpfnldpevgtkssSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRL---- 460
Cdd:cd07230   234 PSSPLYEKDpKTGEIVPWNP-------------SSVKWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLKKsesc 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 461 -----KDLVRAYGGRFAAKLAHLVEMEVKHRCNQVLELGFPLGGLAKL---FAQEWEGDVTVVMPATLAQYSKIIQNPTH 532
Cdd:cd07230   301 vggevEDELSARFKRWLNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLrsvLSQKYSGDITILPELNYSDFPKILKNPTP 380

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1063729809 533 VELQKAANQGRRCTWEKLSAIKSNCGIELALDDSVAIL 570
Cdd:cd07230   381 EFMLDACLRGERATWPKLSRIRNHCAIELALDKAIQYL 418
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 189-565 3.49e-91

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: 293.02  E-value: 3.49e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 189 IKEYIDEVSTQLRMVcnSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGS 268
Cdd:cd07232    29 VEEYIDEVEACLKYL--RESSQLDLEEKRRLFKRLSTNYGRTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 269 IICAVVASRSWPELQSFFENSLhSLQFFDQLGGVFSIVKRVMTQGALHDI----RQLQCMLRnltSNLTFQEAYDMTGRI 344
Cdd:cd07232   107 LVAALLCTRTDEELKQLLVPEL-ARKITACEPPWLVWIPRWLKTGARFDSvewaRTCCWFTR---GSMTFEEAYERTGRI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 345 LGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVPYHPPfnldpevgtksssGRRWRD 424
Cdd:cd07232   183 LNISVVPADPHSPTILLNYLTSPNCTIWSAVLASAAVPGILNPVVLMMKDPDGTLIPPFSF-------------GSKWKD 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 425 GSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLL--------RLKDLVRAY---GGRFAAKLAHLVEMEVKHRCNQVLEL 493
Cdd:cd07232   250 GSLRTDIPLKALNTLFNVNFSIVSQVNPHINLFFfssrgsvgRPVSHRKGRgwrGGFLLSALEQYLKLDIKKWLKVLRDL 329

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063729809 494 GF---PLGGLA-KLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIELALDD 565
Cdd:cd07232   330 ELlprPLGQDWsQIFLQDFSGTITIWPRSTLSDFLRILSDPTPEDLERMIHEGQQAAFPKLHFIKNRMRIEKAIED 405
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 153-565 6.09e-73

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: 243.75  E-value: 6.09e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 153 GSLRDIMFCMRADLVRNLGNMCNSELHKGRLQVPRH-IKEYIDEVSTQLRMV-----CNSDSEELSLEEKLSFMHETRHA 226
Cdd:cd07229     1 GDILTLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLlIEEYITEVAECLEYVtalqtSPMHSKGFSSQAKLDFFHDTRQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 227 FGRTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENSLHSLQFFDQLGGVFSI- 305
Cdd:cd07229    81 FGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDGDGIDLSAFNRLRGKKSLg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 306 -------------VKRVMTQGALHDIRQLQCMLRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIW 372
Cdd:cd07229   161 ysgygwlgtlgrrIQRLLREGYFLDVKVLEEFVRANLGDLTFEEAYARTGRVLNITVAPSAVSGSPNLLNYLTAPNVLIW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 373 SAVTAS-CAFPGLFEAQELMAKDRSGEIVPYHPPFNLDPevgtksssgRRWRDGSL-EVDLPMMQLKELFNVNHFIVSQA 450
Cdd:cd07229   241 SAALASnASSAALYRSVTLLCKDETGSIVPWPPVQVLFF---------RSWRGANYsERESPLARLSELFNVNHFIVSQA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 451 NPHIAPLLR--LKDLVRAyggrfaaklAHLVEMEvkhrcnqvlELGFplGGLAKLFaqewegdvtvvmpatlaqyskiiQ 528
Cdd:cd07229   312 RPYLAPFLSsdLHENIPG---------PNITLVP---------ELSF--SDFLRLF-----------------------Q 348

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1063729809 529 NPTHVELQKAANQGRRCTWEKLSAIKSNCGIELALDD 565
Cdd:cd07229   349 NPTTDEIQYWILKGERGVWPALAALRVRCAVEFELDD 385
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 96-225 1.94e-45

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: 159.23  E-value: 1.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809  96 YRRKFWRNMMRTALTYEEWAHAAKMLE--------KETPkmnESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLV 167
Cdd:pfam11815   6 GRRKRLRKKLRNAKSYEEWKEAAKELDellgndewKEND---ESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063729809 168 RNLGNMCNSELHK-GRLQVPRHIKEYIDEVSTQLRMVCNSDSeeLSLEEKLSFMHETRH 225
Cdd:pfam11815  83 RNFAGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLAESPS--LSLEEKLEFFKETRK 139
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 232-444 1.21e-38

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: 141.32  E-value: 1.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENslhslqffdqlggvfsivkrvmt 311
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 312 qgalhdirqlqcmLRNLTSNLTFQEAYDMTGRILGITVCS-----------PRKHEPPRCLNYLTSPHVV---------I 371
Cdd:cd07198    58 -------------RLSREVRLRFDGAFPPTGRLLGILRQPllsalpddaheDASGKLFISLTRLTDGENVlvsdtskgeL 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063729809 372 WSAVTASCAFPGLFEAQELMakdrsgeivpyhppfnldpevgtksSSGRRWRDGSLEVDLPMMQLKELFNVNH 444
Cdd:cd07198   125 WSAVRASSSIPGYFGPVPLS-------------------------FRGRRYGDGGLSNNLPVAELGNTINVSP 172
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 229-492 2.04e-24

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 103.44  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 229 RTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVAS-RSWPELQSFFEnSLHSLQFFD-QLGGVFSIV 306
Cdd:COG1752     6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWR-SLDRRDLFDlSLPRRLLRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 307 KRVMTQGALHDIRQLQCMLRNLTSNLTFQEAydmtGRILGITVCSprkhepprclnyLTSPHVVIWS------AVTASCA 380
Cdd:COG1752    85 DLGLSPGGLLDGDPLRRLLERLLGDRDFEDL----PIPLAVVATD------------LETGREVVFDsgpladAVRASAA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 381 FPGLFeaqelmakdrsgeivpyhPPFNLDpevgtksssGRRWRDGSLeVD-LPMMQLKELfNVNHFIVSQANPHIAPLLR 459
Cdd:COG1752   149 IPGVF------------------PPVEID---------GRLYVDGGV-VNnLPVDPARAL-GADRVIAVDLNPPLRKLPS 199

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1063729809 460 LKD-LVRAYGGRFAAKLAHLVEMEvkhRCNQVLE 492
Cdd:COG1752   200 LLDiLGRALEIMFNSILRRELALE---PADILIE 230
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 232-390 1.39e-19

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: 87.28  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWP-ELQSFFENSLHSL---QFFDQLGGVFSIVK 307
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPeEIEDLLLELDLNLflsLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 308 RVMTQGALHDIRQLQCMLRNLTSNLTFQEA--------YDMTGRILGITVCSPRKHEPPRcLNYLTSPHVVIWSAVTASC 379
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEELaarlslllVVALRALLTVISTALGTRARIL-LPDDLDDDEDLADAVLASS 159

                         170
                  ....*....|.
gi 1063729809 380 AFPGLFEAQEL 390
Cdd:pfam01734 160 ALPGVFPPVRL 170
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 232-394 1.18e-15

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: 76.16  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVAS-RSWPELQSFFENSLHSlQFFDQLGGVFSIVKRVM 310
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALgYSAADIKDILKETDFA-KLLDSPVGLLFLLPSLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 311 TQGALHDIRQLQCMLRNLTSNLT--------FQEAYDMTGRILGITVCSPRKHEPPRcLNYLTSPHVVIWSAVTASCAFP 382
Cdd:cd07207    81 KEGGLYKGDALEEWLRELLKEKTgnsfatslLRDLDDDLGKDLKVVATDLTTGALVV-FSAETTPDMPVAKAVRASMSIP 159

                         170
                  ....*....|..
gi 1063729809 383 GLFEAQELMAKD 394
Cdd:cd07207   160 FVFKPVRLAKGD 171
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 230-385 2.58e-12

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: 66.03  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 230 TALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVAS-RSWPELQSFFENSLHSLQFFDQL----GGVFS 304
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAgYSPEEIEERAKLRSTDLKALSDLtiptAGLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 305 I---VKRVMTQGALHDIRQLQCMLRNLTSNLTfqeaydmTGRilgitvcsprkhepprclnyltsPHVV----IWSAVTA 377
Cdd:cd07205    81 GdkfLELLDEYFGDRDIEDLWIPFFIVATDLT-------SGK-----------------------LVVFrsgsLVRAVRA 130


                  ....*...
gi 1063729809 378 SCAFPGLF 385
Cdd:cd07205   131 SMSIPGIF 138
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 232-390 9.72e-12

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: 65.39  E-value: 9.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVAS---RSWPELQSFFENsLHSLQFFDQlGGVFSIVKR 308
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGgdpEAVERLEKLWRE-LSREDVFLR-GLLDRALDF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 309 VMTQGALHDIRQLQCMLRNLTsnltfqeaydmTGRILgitvcspRKHEPPRclnYLTSPHVViwsavtASCAFPGLFEAQ 388
Cdd:cd07209    79 DTLRLLAILFAGLVIVAVNVL-----------TGEPV-------YFDDIPD---GILPEHLL------ASAALPPFFPPV 131


                  ..
gi 1063729809 389 EL 390
Cdd:cd07209   132 EI 133
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 230-390 3.23e-08

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: 55.04  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 230 TALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVAS----RSWPELqsffensLHSLQFFDqlggvFSI 305
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASgispDEMAEL-------LLSLERKD-----FWM 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 306 VKRVMTQGALHDIRQLQCMLRNLTSNLTFQEAydmtgRI-LGITVCSPRKHEPprclNYLTSPHVVIWsaVTASCAFPGL 384
Cdd:cd07210    69 FWDPPLRGGLLSGDRFAALLREHLPPDRFEEL-----RIpLAVSVVDLTSRET----LLLSEGDLAEA--VAASCAVPPL 137


                  ....*.
gi 1063729809 385 FEAQEL 390
Cdd:cd07210   138 FQPVEI 143
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 231-389 4.40e-07

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: 50.74  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 231 ALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELqsffENSLHSLQFFDQLG-GVFSivkrV 309
Cdd:cd07228     2 GLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDAL----EEWVRSLSQRDVLRlLDLS----A 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 310 MTQGALHDIRQLQcMLRNLTSNLTFQE--------AYDM-TGRILgitvcsprkhepprclnYLTSPHVViwSAVTASCA 380
Cdd:cd07228    74 SRSGLLKGEKVLE-YLREIMGGVTIEElpipfaavATDLqTGKEV-----------------WFREGSLI--DAIRASIS 133


                  ....*....
gi 1063729809 381 FPGLFEAQE 389
Cdd:cd07228   134 IPGIFAPVE 142
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 232-445 1.06e-05

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 47.73  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEH--KLL--PRIIAGSSVGSIICAVVASRswPELQsffenslHSLQFFdqLGGVFSIVK 307
Cdd:cd07204     2 LSFSGCGFLGIYHVGVASALREHapRLLqnARRIAGASAGAIVAAVVLCG--VSME-------EACSFI--LKVVSEARR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 308 RvmTQGALHDIRQLQCMLRNLTSNLTFQEAYDM-TGRiLGITVCSPRKHEpprclNYL----TSPHVVIwSAVTASCAFP 382
Cdd:cd07204    71 R--SLGPLHPSFNLLKILRQGLEKILPDDAHELaSGR-LHISLTRVSDGE-----NVLvsefDSKEELI-QALVCSCFIP 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063729809 383 GLfeaqelmakdrSGeIVPyhPPFNldpevgtksssGRRWRDGSLEVDLPMMQLKELFNVNHF 445
Cdd:cd07204   142 FY-----------CG-LIP--PKFR-----------GVRYIDGGLSDNLPILDDENTITVSPF 179
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 232-448 7.89e-05

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: 43.56  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLL--PRIIAGSSVGSIICAVVASRSwpelqsffenslhslqffdqlggvfsivkrv 309
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAATLYPPS------------------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 310 mtqGALHDIrqLQCMLRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPprclnyltsphvviWSAVTASCAFPGLFeaqe 389
Cdd:cd01819    50 ---SSLDNK--PRQSLEEALSGKLWVSFTPVTAGENVLVSRFVSKEEL--------------IRALFASGSWPSYF---- 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063729809 390 lmakdrsgeivPYHPPFNLDPEVGTKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVS 448
Cdd:cd01819   107 -----------GLIPPAELYTSKSNLKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
PRK10279 PRK10279
patatin-like phospholipase RssA;
232-385 7.94e-05

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 45.47  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELqsffENSLHSLQFFD---------QLGG- 301
Cdd:PRK10279    8 LALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSAL----EDWVTSFSYWDvlrlmdlswQRGGl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 302 -----VFSIVKRVMTqgaLHDIRQLQCMLRNLTSNLTfqeaydmTGRILgitvcsprkhepprclnYLTSPHvvIWSAVT 376
Cdd:PRK10279   84 lrgerVFNQYREIMP---ETEIENCSRRFGAVATNLS-------TGREL-----------------WFTEGD--LHLAIR 134


                  ....*....
gi 1063729809 377 ASCAFPGLF 385
Cdd:PRK10279  135 ASCSMPGLM 143
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 232-397 4.89e-04

Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 42.97  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 232 LLLSGGASLGAFHVGVVRTLvEHKLLPRI------IAGSSVGSIICAVVASR-SWPELQSFFEN------SLHSLQFFDQ 298
Cdd:COG3621    10 LSLDGGGIRGLIPARILAEL-EERLGKPLaeyfdlIAGTSTGGIIALGLAAGySAEEILDLYEEegkeifPKSRWRKLLS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 299 LGGVFsivkrvmtqGALHDIRQLQCMLRNLTSNLTFQE--------AYDMTGRILgITVCSPrKHEPPRCLNYLtsphvv 370
Cdd:COG3621    89 LRGLF---------GPKYDSEGLEKVLKEYFGDTTLGDlktpvlipSYDLDNGKP-VFFKSP-HAKFDRDRDFL------ 151

                         170       180
                  ....*....|....*....|....*..
gi 1063729809 371 IWSAVTASCAFPGLFEAQELMAKDRSG 397
Cdd:COG3621   152 LVDVARATSAAPTYFPPAQIKNLTGEG 178
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 260-386 5.78e-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: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063729809 260 IIAGSSVGSIICAVVASRSWP--ELQSFFENSLHSLqfFDQlGGVFSIVKRVMTQGALHDIRQLQCMLRN-LTSNLTFQE 336
Cdd:cd07211    44 YICGVSTGAILAFLLGLKKMSldECEELYRKLGKDV--FSQ-NTYISGTSRLVLSHAYYDTETWEKILKEmMGSDELIDT 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063729809 337 AYDMTGR---ILGITVCSPR---------KHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFE 386
Cdd:cd07211   121 SADPNCPkvaCVSTQVNRTPlkpyvfrnyNHPPGTRSHYLGSCKHKLWEAIRASSAAPGYFE 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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