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Conserved domains on  [gi|1373912587|ref|XP_024380797|]
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triacylglycerol lipase SDP1-like [Physcomitrium patens]

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 ...
 194-605 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: 612.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 194 IRADLVRNLGNMCNPELHKGRLQTPRLIQEYINEVRYHLRAVCGSDSDSFTLDEKIAFIHETRHGFGRTALLLSGGAALG 273
Cdd:cd07231     1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 274 AFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSFFddpmppmhffenmgsifatahrlltrgavheigml 353
Cdd:cd07231    81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 354 qrkmRQLIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGHLVP 433
Cdd:cd07231   126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 434 YHTPPQVgpgdknmekdIGNRRWRDGSLESDLPMMQLKELFNVNHFIVSQANPHITPFLRFKdfvrayggdfagklahla 513
Cdd:cd07231   202 YHPPGKV----------SSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK------------------ 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 514 emevkhrckqvmemgfevfglaKLFAQDWEGDVTIVMPATFAQFAKIITNPTPIDLRKAVMQGRRCTWAKLSAIQANCGI 593
Cdd:cd07231   254 ----------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGI 311

                         410
                  ....*....|..
gi 1373912587 594 ELMLDECVSELN 605
Cdd:cd07231   312 ELTLDECVAELR 323
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 128-257 1.99e-38

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: 139.58  E-value: 1.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 128 YRRKFWSNLMKTALTYEEWAHAARMLEKEQ-----TRRKDSDLYDEDLVRSKLNELRLRRLEGGVEDILFCIRADLVRNL 202
Cdd:pfam11815   6 GRRKRLRKKLRNAKSYEEWKEAAKELDELLgndewKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLKRNF 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1373912587 203 GNMCNPELHK-GRLQTPRLIQEYINEVRYHLRAVCgsDSDSFTLDEKIAFIHETRH 257
Cdd:pfam11815  86 AGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLA--ESPSLSLEEKLEFFKETRK 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 ...
 194-605 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: 612.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 194 IRADLVRNLGNMCNPELHKGRLQTPRLIQEYINEVRYHLRAVCGSDSDSFTLDEKIAFIHETRHGFGRTALLLSGGAALG 273
Cdd:cd07231     1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 274 AFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSFFddpmppmhffenmgsifatahrlltrgavheigml 353
Cdd:cd07231    81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 354 qrkmRQLIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGHLVP 433
Cdd:cd07231   126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 434 YHTPPQVgpgdknmekdIGNRRWRDGSLESDLPMMQLKELFNVNHFIVSQANPHITPFLRFKdfvrayggdfagklahla 513
Cdd:cd07231   202 YHPPGKV----------SSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK------------------ 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 514 emevkhrckqvmemgfevfglaKLFAQDWEGDVTIVMPATFAQFAKIITNPTPIDLRKAVMQGRRCTWAKLSAIQANCGI 593
Cdd:cd07231   254 ----------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGI 311

                         410
                  ....*....|..
gi 1373912587 594 ELMLDECVSELN 605
Cdd:cd07231   312 ELTLDECVAELR 323
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 128-257 1.99e-38

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: 139.58  E-value: 1.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 128 YRRKFWSNLMKTALTYEEWAHAARMLEKEQ-----TRRKDSDLYDEDLVRSKLNELRLRRLEGGVEDILFCIRADLVRNL 202
Cdd:pfam11815   6 GRRKRLRKKLRNAKSYEEWKEAAKELDELLgndewKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLKRNF 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1373912587 203 GNMCNPELHK-GRLQTPRLIQEYINEVRYHLRAVCgsDSDSFTLDEKIAFIHETRH 257
Cdd:pfam11815  86 AGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLA--ESPSLSLEEKLEFFKETRK 139
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 264-422 4.28e-21

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: 91.90  E-value: 4.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTW----TELQSFFDDPMPPMHFFENMGSIFATAH 339
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 340 RLLTRGAVHEIGMLQRKMRQLIGDLTFQEaydLSGRVLGISVCSPRKLEPPRC----------LNYLTSPHVVIWSAVTA 409
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEE---LAARLSLLLVVALRALLTVIStalgtrarilLPDDLDDDEDLADAVLA 157

                         170
                  ....*....|...
gi 1373912587 410 SCAFPGLFEAQEL 422
Cdd:pfam01734 158 SSALPGVFPPVRL 170
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 261-490 1.49e-20

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 92.27  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 261 RTALLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAAT-RTWTELQSFFDDpMPPMHFFE-NMGSIFATA 338
Cdd:COG1752     6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWRS-LDRRDLFDlSLPRRLLRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 339 HRLLTRGAVHEIGMLQRKMRQLIGDLTFQE--------AYDL-SGRVLgisvcsprklepprclnYLTSPHVViwSAVTA 409
Cdd:COG1752    85 DLGLSPGGLLDGDPLRRLLERLLGDRDFEDlpiplavvATDLeTGREV-----------------VFDSGPLA--DAVRA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 410 SCAFPGLFEAQElmakdrtghlvpyhtppqvgpgdknmekdIGNRRWRDGSLESDLPMMQLKELfNVNHFIVSQANPHIT 489
Cdd:COG1752   146 SAAIPGVFPPVE-----------------------------IDGRLYVDGGVVNNLPVDPARAL-GADRVIAVDLNPPLR 195


                  .
gi 1373912587 490 P 490
Cdd:COG1752   196 K 196
 
Name Accession Description Interval E-value
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 194-605 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: 612.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 194 IRADLVRNLGNMCNPELHKGRLQTPRLIQEYINEVRYHLRAVCGSDSDSFTLDEKIAFIHETRHGFGRTALLLSGGAALG 273
Cdd:cd07231     1 LRADLVRNLGNMCNPELHKGRLEVPRLIRDYIAEVKAQLRAVVESDEDELSLEEKLAFFQETRHAFGRTALLLSGGAALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 274 AFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSFFddpmppmhffenmgsifatahrlltrgavheigml 353
Cdd:cd07231    81 TFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFF----------------------------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 354 qrkmRQLIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGHLVP 433
Cdd:cd07231   126 ----RALLGDLTFQEAYDRTGRILGITVCPPRKSEPPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQELMAKDRFGEIVP 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 434 YHTPPQVgpgdknmekdIGNRRWRDGSLESDLPMMQLKELFNVNHFIVSQANPHITPFLRFKdfvrayggdfagklahla 513
Cdd:cd07231   202 YHPPGKV----------SSPRRWRDGSLEQDLPMQQLRELFNVNHFIVSQANPHIVPLLRLK------------------ 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 514 emevkhrckqvmemgfevfglaKLFAQDWEGDVTIVMPATFAQFAKIITNPTPIDLRKAVMQGRRCTWAKLSAIQANCGI 593
Cdd:cd07231   254 ----------------------KLFAQEWEGDITIVMPITWKQLLKIIQNPTPEELRKAAMAGERCTWEKLSAIESNCGI 311

                         410
                  ....*....|..
gi 1373912587 594 ELMLDECVSELN 605
Cdd:cd07231   312 ELTLDECVAELR 323
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 194-599 6.82e-137

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


Pssm-ID: 132845  Cd Length: 298  Bit Score: 411.22  E-value: 6.82e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 194 IRADLVRNLGNMCNPELHKGRLQ-TPRLIQEYINEVRYHLRAVCGSDSDSFTLDEKIAFIHETRHGFGRTALLLSGGAAL 272
Cdd:cd07206     1 LREGLHGNLGNMGNPSLYRHAYFgTKHLIEDYIEEVDLSLEYLALLDTKELSVEEKLDFFRRARHAFGRTALMLSGGASL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 273 GAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELqsffddpmppmhffenmgsifatahrlltrgavheigm 352
Cdd:cd07206    81 GLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL-------------------------------------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 353 lqrkmrqlIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTGHLV 432
Cdd:cd07206   123 --------IGDLTFQEAYERTGRIINITVAPAEPHQNSRLLNALTSPNVLIWSAVLASCAVPGVFPPVMLMAKNRDGEIV 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 433 PYhtppqvgpgdknmekdIGNRRWRDGSLESDLPMMQLKELFNVNHFIVSQANPHITPFLrfkdfvrayggdfagklahl 512
Cdd:cd07206   195 PY----------------LPGRKWVDGSVSDDLPAKRLARLYNVNHFIVSQTNPHVVPFL-------------------- 238

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 513 aemevkhrckqvmemgfevfglaklfaQDWEGDVTIVMPATFAQFAKIITNPTPIDLRKAVMQGRRCTWAKLSAIQANCG 592
Cdd:cd07206   239 ---------------------------QEYSGDITIIPPFSFSNPLKLLSNPSEDELQRLILEGERATWPKIEMIRTQTR 291


                  ....*..
gi 1373912587 593 IELMLDE 599
Cdd:cd07206   292 ISRTLEE 298
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 190-607 5.60e-125

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: 385.04  E-value: 5.60e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 190 ILFCIRADLVRNLGNMCNPEL----HKGrlqTPRLIQEYINEVRYHLRAVCGSDSDSFTLDEKIAFIHETRHGFGRTALL 265
Cdd:cd07230     1 LLYLIRTTLSRDLGNMGNVNLyrhsHVG---TKKLIERYITEALLTLEYLVDDDEDGLEDRYLLGMLLQTRKNFGRTALL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 266 LSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTE----LQSF-------FDDPMPPMHFFENMGsi 334
Cdd:cd07230    78 LSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEipelLEEFpygdfnvFEDPDQEENVLQKLS-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 335 fatahRLLTRGAVHEIGMLQRKMRQLIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIWSAVTASCAFP 414
Cdd:cd07230   156 -----RFLKYGSWFDISHLTRVMRGFLGDLTFQEAYNRTRRILNITVSPASIYELPRLLNYITAPNVLIWSAVCASCSVP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 415 GLFEAQELMAKD-RTGHLVPYHTPPQvgpgdknmekdignrRWRDGSLESDLPMMQLKELFNVNHFIVSQANPHITPFLR 493
Cdd:cd07230   231 GVFPSSPLYEKDpKTGEIVPWNPSSV---------------KWIDGSVDNDLPMTRLSEMFNVNHFIVSQVNPHVVPFLK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 494 F---------KDFVRAYGGDFAGKLAHLAEMEVKHRCKQVMEMGFEVFGLAKL---FAQDWEGDVTIVMPATFAQFAKII 561
Cdd:cd07230   296 KsescvggevEDELSARFKRWLNNVTDLAKDEVLHRLQLLSELGIFPNLLTKLrsvLSQKYSGDITILPELNYSDFPKIL 375

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1373912587 562 TNPTPIDLRKAVMQGRRCTWAKLSAIQANCGIELMLDECVSELNRR 607
Cdd:cd07230   376 KNPTPEFMLDACLRGERATWPKLSRIRNHCAIELALDKAIQYLRAR 421
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 194-600 7.33e-89

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: 289.17  E-value: 7.33e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 194 IRADLVRNLGNMCNPELH-KGRLQTPRLIQEYINEVRYHLRAVcgSDSDSFTLDEKIAFIHETRHGFGRTALLLSGGAAL 272
Cdd:cd07232     1 LRGCVKNNFAGIENGRLYsETYYGTKNLVEEYIDEVEACLKYL--RESSQLDLEEKRRLFKRLSTNYGRTALCLSGGAAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 273 GAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSFFddpMPPM--HFFENMGSIFATAHRLLTRGA-VHE 349
Cdd:cd07232    79 AYYHFGVVKALLDADLLPNVISGTSGGSLVAALLCTRTDEELKQLL---VPELarKITACEPPWLVWIPRWLKTGArFDS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 350 IGMLQRKMRQLIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRTG 429
Cdd:cd07232   156 VEWARTCCWFTRGSMTFEEAYERTGRILNISVVPADPHSPTILLNYLTSPNCTIWSAVLASAAVPGILNPVVLMMKDPDG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 430 HLVPYHTPpqvgpgdknmekdiGNrRWRDGSLESDLPMMQLKELFNVNHFIVSQANPHITPFL--------RFKDFVRAY 501
Cdd:cd07232   236 TLIPPFSF--------------GS-KWKDGSLRTDIPLKALNTLFNVNFSIVSQVNPHINLFFfssrgsvgRPVSHRKGR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 502 ---GGDFAGKLAHLAEMEVKHRCKQVMEMGFevfgLAKLFAQDW--------EGDVTIVMPATFAQFAKIITNPTPIDLR 570
Cdd:cd07232   301 gwrGGFLLSALEQYLKLDIKKWLKVLRDLEL----LPRPLGQDWsqiflqdfSGTITIWPRSTLSDFLRILSDPTPEDLE 376

                         410       420       430
                  ....*....|....*....|....*....|
gi 1373912587 571 KAVMQGRRCTWAKLSAIQANCGIELMLDEC 600
Cdd:cd07232   377 RMIHEGQQAAFPKLHFIKNRMRIEKAIEDG 406
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 185-608 4.08e-77

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: 257.23  E-value: 4.08e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 185 GGVEDILFCIRADLVRNLGNMCNPELH-KGRLQTPRLIQEYINEVRYHLRAV-----CGSDSDSFTLDEKIAFIHETRHG 258
Cdd:cd07229     1 GDILTLLNLLRSGLVRNLGNITSPKLFtRAYAGTKLLIEEYITEVAECLEYVtalqtSPMHSKGFSSQAKLDFFHDTRQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 259 FGRTALLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSF----------FDDPMPPMHFF 328
Cdd:cd07229    81 FGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFldgdgidlsaFNRLRGKKSLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 329 ENMGSIFAT----AHRLLTRGAVHEIGMLQRKMRQLIGDLTFQEAYDLSGRVLGISVCSPRKLEPPRCLNYLTSPHVVIW 404
Cdd:cd07229   161 YSGYGWLGTlgrrIQRLLREGYFLDVKVLEEFVRANLGDLTFEEAYARTGRVLNITVAPSAVSGSPNLLNYLTAPNVLIW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 405 SAVTAS-CAFPGLFEAQELMAKDRTGHLVPYhtPPqvgpgdknmEKDIGNRRWRDGSL-ESDLPMMQLKELFNVNHFIVS 482
Cdd:cd07229   241 SAALASnASSAALYRSVTLLCKDETGSIVPW--PP---------VQVLFFRSWRGANYsERESPLARLSELFNVNHFIVS 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 483 QANPHITPFLRfkdfvrayggdfagklahlaemevkhrckqvmemgfevfglAKLFAQDWEGDVTIVMPATFAQFAKIIT 562
Cdd:cd07229   310 QARPYLAPFLS-----------------------------------------SDLHENIPGPNITLVPELSFSDFLRLFQ 348

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1373912587 563 NPTPIDLRKAVMQGRRCTWAKLSAIQANCGIELMLDECvseLNRRR 608
Cdd:cd07229   349 NPTTDEIQYWILKGERGVWPALAALRVRCAVEFELDDG---YQVLR 391
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 128-257 1.99e-38

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: 139.58  E-value: 1.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 128 YRRKFWSNLMKTALTYEEWAHAARMLEKEQ-----TRRKDSDLYDEDLVRSKLNELRLRRLEGGVEDILFCIRADLVRNL 202
Cdd:pfam11815   6 GRRKRLRKKLRNAKSYEEWKEAAKELDELLgndewKENDESAYYDYKLVRRVLSQLRRAREEEDLRALLFLLRTCLKRNF 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1373912587 203 GNMCNPELHK-GRLQTPRLIQEYINEVRYHLRAVCgsDSDSFTLDEKIAFIHETRH 257
Cdd:pfam11815  86 AGIENPRLYShTYYGTKNLIEEYIDEVEKSLEYLA--ESPSLSLEEKLEFFKETRK 139
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 264-478 2.50e-33

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: 126.30  E-value: 2.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSFFDDpmppmhffenmgsifatahrllt 343
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 344 rgavheigmlqrkMRQLIGDLTFQEAYDLSGRVLGISVCS-----------PRKLEPPRCLNYLTSPHVV---------I 403
Cdd:cd07198    58 -------------RLSREVRLRFDGAFPPTGRLLGILRQPllsalpddaheDASGKLFISLTRLTDGENVlvsdtskgeL 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1373912587 404 WSAVTASCAFPGLFEAQELMakdrtghlvpyhtppqvgpgdknmekdIGNRRWRDGSLESDLPMMQLKELFNVNH 478
Cdd:cd07198   125 WSAVRASSSIPGYFGPVPLS---------------------------FRGRRYGDGGLSNNLPVAELGNTINVSP 172
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 264-422 4.28e-21

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: 91.90  E-value: 4.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTW----TELQSFFDDPMPPMHFFENMGSIFATAH 339
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 340 RLLTRGAVHEIGMLQRKMRQLIGDLTFQEaydLSGRVLGISVCSPRKLEPPRC----------LNYLTSPHVVIWSAVTA 409
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEE---LAARLSLLLVVALRALLTVIStalgtrarilLPDDLDDDEDLADAVLA 157

                         170
                  ....*....|...
gi 1373912587 410 SCAFPGLFEAQEL 422
Cdd:pfam01734 158 SSALPGVFPPVRL 170
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 261-490 1.49e-20

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 92.27  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 261 RTALLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAAT-RTWTELQSFFDDpMPPMHFFE-NMGSIFATA 338
Cdd:COG1752     6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWRS-LDRRDLFDlSLPRRLLRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 339 HRLLTRGAVHEIGMLQRKMRQLIGDLTFQE--------AYDL-SGRVLgisvcsprklepprclnYLTSPHVViwSAVTA 409
Cdd:COG1752    85 DLGLSPGGLLDGDPLRRLLERLLGDRDFEDlpiplavvATDLeTGREV-----------------VFDSGPLA--DAVRA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 410 SCAFPGLFEAQElmakdrtghlvpyhtppqvgpgdknmekdIGNRRWRDGSLESDLPMMQLKELfNVNHFIVSQANPHIT 489
Cdd:COG1752   146 SAAIPGVFPPVE-----------------------------IDGRLYVDGGVVNNLPVDPARAL-GADRVIAVDLNPPLR 195


                  .
gi 1373912587 490 P 490
Cdd:COG1752   196 K 196
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 264-432 2.10e-12

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: 66.92  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAAT----------RTWTELQSFFDDPMPPMHFFEN--- 330
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALgysaadikdiLKETDFAKLLDSPVGLLFLLPSlfk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 331 MGSIF--ATAHRLLtrgavheIGMLQRKMRQLIGDLTFQEAYDLSGRVLGISVC--SPRKLEpprCLNYLTSPHVVIWSA 406
Cdd:cd07207    82 EGGLYkgDALEEWL-------RELLKEKTGNSFATSLLRDLDDDLGKDLKVVATdlTTGALV---VFSAETTPDMPVAKA 151

                         170       180
                  ....*....|....*....|....*.
gi 1373912587 407 VTASCAFPGLFEAQELmakDRTGHLV 432
Cdd:cd07207   152 VRASMSIPFVFKPVRL---AKGDVYV 174
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 262-417 5.81e-10

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: 59.10  E-value: 5.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 262 TALLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICS-FAATRTWTELQSffddpmppmhFFENMGSIFATAHR 340
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGAlYAAGYSPEEIEE----------RAKLRSTDLKALSD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 341 L-LTRGAVHEIGMLQRKMRQLIGDLTFQE--------AYDL-SGRvlgisvcsprklepprclnyltsPHVV----IWSA 406
Cdd:cd07205    71 LtIPTAGLLRGDKFLELLDEYFGDRDIEDlwipffivATDLtSGK-----------------------LVVFrsgsLVRA 127

                         170
                  ....*....|.
gi 1373912587 407 VTASCAFPGLF 417
Cdd:cd07205   128 VRASMSIPGIF 138
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 264-422 1.05e-08

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: 56.53  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSII-CSFAAtrtwtelqsffddpmppmhffeNMGSIFATAHRL- 341
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINgALIAG----------------------GDPEAVERLEKLw 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 342 --LTRGAVheigMLQRKMRQLIgDLTFQEAYDLsgRVLGISVCSPRKLEPPRCLnYLTSPHVVIWSAVTASCAFPGLFEA 419
Cdd:cd07209    59 reLSREDV----FLRGLLDRAL-DFDTLRLLAI--LFAGLVIVAVNVLTGEPVY-FDDIPDGILPEHLLASAALPPFFPP 130


                  ...
gi 1373912587 420 QEL 422
Cdd:cd07209   131 VEI 133
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 262-422 1.71e-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: 55.81  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 262 TALLLSGGAALGAFHLGVVRTLIEHRLLPRVI----AGASVGSIICSFAATRTW------TELQSFFDDPMPPMHffenm 331
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAIsgtsAGALVGGLFASGISPDEMaelllsLERKDFWMFWDPPLR----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 332 gSIFATAHRLLTRgavheigmlqrkMRQLIGDLTFQEaydlSGRVLGISVCSprkLEPPRCLnYLTSPHVVIWsaVTASC 411
Cdd:cd07210    76 -GGLLSGDRFAAL------------LREHLPPDRFEE----LRIPLAVSVVD---LTSRETL-LLSEGDLAEA--VAASC 132

                         170
                  ....*....|.
gi 1373912587 412 AFPGLFEAQEL 422
Cdd:cd07210   133 AVPPLFQPVEI 143
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 263-421 6.58e-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: 47.27  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 263 ALLLSGGAALGAFHLGVVRTLIEHRLLPRVIAGASVGSIICSFAATRTWTELQSFFDDpmppmhffENMGSIFatahRLL 342
Cdd:cd07228     2 GLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRS--------LSQRDVL----RLL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 343 TRgAVHEIGMLQ-RK----MRQLIGDLTFQE--------AYDLSgrvLGISVcsprklepprclnYLTSPHVViwSAVTA 409
Cdd:cd07228    70 DL-SASRSGLLKgEKvleyLREIMGGVTIEElpipfaavATDLQ---TGKEV-------------WFREGSLI--DAIRA 130

                         170
                  ....*....|..
gi 1373912587 410 SCAFPGLFEAQE 421
Cdd:cd07228   131 SISIPGIFAPVE 142
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 264-381 1.33e-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: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEH--RLL--PRVIAGASVGSIICSFAATRtwtelqsffddpmPPMHFFENMGSIFATAH 339
Cdd:cd07204     2 LSFSGCGFLGIYHVGVASALREHapRLLqnARRIAGASAGAIVAAVVLCG-------------VSMEEACSFILKVVSEA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1373912587 340 RLLTRGAVHEIGMLQRKMRQLIGDLTFQEAYDL-SGRvLGISV 381
Cdd:cd07204    69 RRRSLGPLHPSFNLLKILRQGLEKILPDDAHELaSGR-LHISL 110
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 264-308 3.30e-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: 45.10  E-value: 3.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1373912587 264 LLLSGGAALGAFHLGVVRTLIEHRLL--PRVIAGASVGSIICSFAAT 308
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAATLYP 47
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 264-430 2.10e-03

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 41.04  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 264 LLLSGGAALGAFHLGVVRTlIEHRLLPR------VIAGASVGSIICSFAATR-TWTELQSFFDD------PMPPMHFFEN 330
Cdd:COG3621    10 LSLDGGGIRGLIPARILAE-LEERLGKPlaeyfdLIAGTSTGGIIALGLAAGySAEEILDLYEEegkeifPKSRWRKLLS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373912587 331 MGSIFATAHRllTRGavheigmLQRKMRQLIGDLTFQE--------AYDLSGRvlgisvcSPR-----KLEPPRCLNYLt 397
Cdd:COG3621    89 LRGLFGPKYD--SEG-------LEKVLKEYFGDTTLGDlktpvlipSYDLDNG-------KPVffkspHAKFDRDRDFL- 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1373912587 398 sphvvIWSAVTASCAFPGLFEAQELMAKDRTGH 430
Cdd:COG3621   152 -----LVDVARATSAAPTYFPPAQIKNLTGEGY 179
 
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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