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Conserved domains on  [gi|2112362621|gb|UCS23955|]
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uncharacterized protein GW608_M13915 [Nakaseomyces glabratus]

Protein Classification

triacylglycerol lipase family protein( domain architecture ID 10163457)

triacylglycerol lipase family protein similar to Saccharomyces cerevisiae triacylglycerol lipase 3 that acts as a lipid particle-localized triacylglycerol (TAG) lipase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 126-590 1.70e-161

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: 466.78  E-value: 1.70e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 126 EKIKEKFSTTGPCMLRNFAGIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVLDKSMT------------PTSFFQRCKLS 193
Cdd:cd07229     1 GDILTLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLLIEEYITEVAECLEYVTALQTspmhskgfssqaKLDFFHDTRQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 194 LGTTALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSRLLTGNVILDMIRNDMDLVRSCG 273
Cdd:cd07229    81 FGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDGDGIDLSAFNRLRGKKSLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 274 YGNMEQHVNLGKLVQNLIHHGYSQDVYLFIQFVLKyIVKDMTFEEAYQATGKAFNVVIHPIDKS-CPNLLNYVTTPNVLI 352
Cdd:cd07229   161 YSGYGWLGTLGRRIQRLLREGYFLDVKVLEEFVRA-NLGDLTFEEAYARTGRVLNITVAPSAVSgSPNLLNYLTAPNVLI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 353 RSAIECSLGSGV-LSSNTKLLCKNLNNDTVRFLEfgkaGADQFLAPEQATNLDDVESPYTRLTELFNVNNFIVSLAKPYL 431
Cdd:cd07229   240 WSAALASNASSAaLYRSVTLLCKDETGSIVPWPP----VQVLFFRSWRGANYSERESPLARLSELFNVNHFIVSQARPYL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 432 APLVGNDLKheiktskyyyykhypqttddidlpeLNIPQLNFTEMEPLAFkfkYHLERKLKNIATMEfrhrmevldnlgl 511
Cdd:cd07229   316 APFLSSDLH-------------------------ENIPGPNITLVPELSF---SDFLRLFQNPTTDE------------- 354

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112362621 512 lfpfikrliidektprsateiaivpkikslsvtriiegqldnIPYWIKCGEQSTWPVLSLLKTRCAVELKLNEIIKMRR 590
Cdd:cd07229   355 ------------------------------------------IQYWILKGERGVWPALAALRVRCAVEFELDDGYQVLR 391
 
Name Accession Description Interval E-value
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 126-590 1.70e-161

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: 466.78  E-value: 1.70e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 126 EKIKEKFSTTGPCMLRNFAGIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVLDKSMT------------PTSFFQRCKLS 193
Cdd:cd07229     1 GDILTLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLLIEEYITEVAECLEYVTALQTspmhskgfssqaKLDFFHDTRQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 194 LGTTALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSRLLTGNVILDMIRNDMDLVRSCG 273
Cdd:cd07229    81 FGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDGDGIDLSAFNRLRGKKSLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 274 YGNMEQHVNLGKLVQNLIHHGYSQDVYLFIQFVLKyIVKDMTFEEAYQATGKAFNVVIHPIDKS-CPNLLNYVTTPNVLI 352
Cdd:cd07229   161 YSGYGWLGTLGRRIQRLLREGYFLDVKVLEEFVRA-NLGDLTFEEAYARTGRVLNITVAPSAVSgSPNLLNYLTAPNVLI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 353 RSAIECSLGSGV-LSSNTKLLCKNLNNDTVRFLEfgkaGADQFLAPEQATNLDDVESPYTRLTELFNVNNFIVSLAKPYL 431
Cdd:cd07229   240 WSAALASNASSAaLYRSVTLLCKDETGSIVPWPP----VQVLFFRSWRGANYSERESPLARLSELFNVNHFIVSQARPYL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 432 APLVGNDLKheiktskyyyykhypqttddidlpeLNIPQLNFTEMEPLAFkfkYHLERKLKNIATMEfrhrmevldnlgl 511
Cdd:cd07229   316 APFLSSDLH-------------------------ENIPGPNITLVPELSF---SDFLRLFQNPTTDE------------- 354

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112362621 512 lfpfikrliidektprsateiaivpkikslsvtriiegqldnIPYWIKCGEQSTWPVLSLLKTRCAVELKLNEIIKMRR 590
Cdd:cd07229   355 ------------------------------------------IQYWILKGERGVWPALAALRVRCAVEFELDDGYQVLR 391
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 65-191 2.01e-26

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: 104.53  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621  65 EAIKELDSSESYDDWCERATIVDEITGANLWRRNFFSRRYDFRSVLEQYASLTKNLNENDIEKIkekFSTTGPCMLRNFA 144
Cdd:pfam11815  10 RLRKKLRNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRAL---LFLLRTCLKRNFA 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2112362621 145 GIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVLDKSMTPT-----SFFQRCK 191
Cdd:pfam11815  87 GIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESPSLSleeklEFFKETR 138
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 196-266 8.30e-12

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 65.69  E-value: 8.30e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112362621 196 TTALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGC-LSNEELSRLLTGNVILDMIRNDM 266
Cdd:COG1752     6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWRSLDRRDLFDLSL 77
 
Name Accession Description Interval E-value
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 126-590 1.70e-161

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: 466.78  E-value: 1.70e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 126 EKIKEKFSTTGPCMLRNFAGIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVLDKSMT------------PTSFFQRCKLS 193
Cdd:cd07229     1 GDILTLLNLLRSGLVRNLGNITSPKLFTRAYAGTKLLIEEYITEVAECLEYVTALQTspmhskgfssqaKLDFFHDTRQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 194 LGTTALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSRLLTGNVILDMIRNDMDLVRSCG 273
Cdd:cd07229    81 FGRTALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGVHTDEELLRFLDGDGIDLSAFNRLRGKKSLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 274 YGNMEQHVNLGKLVQNLIHHGYSQDVYLFIQFVLKyIVKDMTFEEAYQATGKAFNVVIHPIDKS-CPNLLNYVTTPNVLI 352
Cdd:cd07229   161 YSGYGWLGTLGRRIQRLLREGYFLDVKVLEEFVRA-NLGDLTFEEAYARTGRVLNITVAPSAVSgSPNLLNYLTAPNVLI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 353 RSAIECSLGSGV-LSSNTKLLCKNLNNDTVRFLEfgkaGADQFLAPEQATNLDDVESPYTRLTELFNVNNFIVSLAKPYL 431
Cdd:cd07229   240 WSAALASNASSAaLYRSVTLLCKDETGSIVPWPP----VQVLFFRSWRGANYSERESPLARLSELFNVNHFIVSQARPYL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 432 APLVGNDLKheiktskyyyykhypqttddidlpeLNIPQLNFTEMEPLAFkfkYHLERKLKNIATMEfrhrmevldnlgl 511
Cdd:cd07229   316 APFLSSDLH-------------------------ENIPGPNITLVPELSF---SDFLRLFQNPTTDE------------- 354

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112362621 512 lfpfikrliidektprsateiaivpkikslsvtriiegqldnIPYWIKCGEQSTWPVLSLLKTRCAVELKLNEIIKMRR 590
Cdd:cd07229   355 ------------------------------------------IQYWILKGERGVWPALAALRVRCAVEFELDDGYQVLR 391
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 141-591 5.10e-58

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: 200.14  E-value: 5.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 141 RNFAGIVDKKLFTKSLMGTKLLIEQHLE---RTIDGLDVLDKSMTPTSF----FQRCKLSLGTTALILQGGSFFGLFHLG 213
Cdd:cd07230    11 RDLGNMGNVNLYRHSHVGTKKLIERYITealLTLEYLVDDDEDGLEDRYllgmLLQTRKNFGRTALLLSGGGTFGMFHIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 214 VIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSRLLTgnvilDMIRNDMDLVRSCGygnmeQHVNLGKLVQNLIHH 293
Cdd:cd07230    91 VLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLE-----EFPYGDFNVFEDPD-----QEENVLQKLSRFLKY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 294 GYSQDVYLFIQfVLKYIVKDMTFEEAYQATGKAFNVVIhpidkSC------PNLLNYVTTPNVLIRSAI--ECSLgSGVL 365
Cdd:cd07230   161 GSWFDISHLTR-VMRGFLGDLTFQEAYNRTRRILNITV-----SPasiyelPRLLNYITAPNVLIWSAVcaSCSV-PGVF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 366 SSNTkLLCKN-LNNDTVRFlefgKAGADQFlapeqatnLD---DVESPYTRLTELFNVNNFIVSLAKPYLAPLvgndLKH 441
Cdd:cd07230   234 PSSP-LYEKDpKTGEIVPW----NPSSVKW--------IDgsvDNDLPMTRLSEMFNVNHFIVSQVNPHVVPF----LKK 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 442 EIKTSkyyyykhypqtTDDIDlpelnipqlnftemEPLAFKFKYHLErKLKNIATMEFRHRMEVLDNLGlLFP--FIK-R 518
Cdd:cd07230   297 SESCV-----------GGEVE--------------DELSARFKRWLN-NVTDLAKDEVLHRLQLLSELG-IFPnlLTKlR 349

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112362621 519 LIIDEKTprsATEIAIVPKIKSLSVTRII-----EGQLDNipywIKCGEQSTWPVLSLLKTRCAVELKLNEIIKMRRG 591
Cdd:cd07230   350 SVLSQKY---SGDITILPELNYSDFPKILknptpEFMLDA----CLRGERATWPKLSRIRNHCAIELALDKAIQYLRA 420
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 138-435 2.20e-55

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: 189.34  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 138 CMLRNFAGIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVL----DKSMTP---TSFFQRCKLSLGTTALILQGGSFFGLF 210
Cdd:cd07206     4 GLHGNLGNMGNPSLYRHAYFGTKHLIEDYIEEVDLSLEYLalldTKELSVeekLDFFRRARHAFGRTALMLSGGASLGLF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 211 HLGVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELsrlltgnvildmirndmdlvrscgygnmeqhvnlgklvqnl 290
Cdd:cd07206    84 HLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL----------------------------------------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 291 ihhgysqdvylfiqfvlkyiVKDMTFEEAYQATGKAFNVVIHPIDKS-CPNLLNYVTTPNVLIRSAIECSLGSGVLSSNT 369
Cdd:cd07206   123 --------------------IGDLTFQEAYERTGRIINITVAPAEPHqNSRLLNALTSPNVLIWSAVLASCAVPGVFPPV 182

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112362621 370 KLLCKNLNNDTVRFLEFGKAGaDQFLApeqatnlDDVesPYTRLTELFNVNNFIVSLAKPYLAPLV 435
Cdd:cd07206   183 MLMAKNRDGEIVPYLPGRKWV-DGSVS-------DDL--PAKRLARLYNVNHFIVSQTNPHVVPFL 238
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 138-579 1.25e-53

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: 187.86  E-value: 1.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 138 CMLRNFAGIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVLDKSMTPT-----SFFQRCKLSLGTTALILQGGSFFGLFHL 212
Cdd:cd07232     4 CVKNNFAGIENGRLYSETYYGTKNLVEEYIDEVEACLKYLRESSQLDleekrRLFKRLSTNYGRTALCLSGGAAFAYYHF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 213 GVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSRLLTGNViLDMIRNDMDLVRscgygnmeqhvnlgKLVQNLIH 292
Cdd:cd07232    84 GVVKALLDADLLPNVISGTSGGSLVAALLCTRTDEELKQLLVPEL-ARKITACEPPWL--------------VWIPRWLK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 293 HGYSQDVYLFIQFVLKYIVKDMTFEEAYQATGKAFNVVIHPIDKSCPN-LLNYVTTPNVLIRSAIECSLG-SGVLSSnTK 370
Cdd:cd07232   149 TGARFDSVEWARTCCWFTRGSMTFEEAYERTGRILNISVVPADPHSPTiLLNYLTSPNCTIWSAVLASAAvPGILNP-VV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 371 LLCKNLNNDTVRFLEFGKAGADQFLApeqatnlddVESPYTRLTELFNVNNFIVSLAKPYLAPLVGNDLKHEIKTSKYYY 450
Cdd:cd07232   228 LMMKDPDGTLIPPFSFGSKWKDGSLR---------TDIPLKALNTLFNVNFSIVSQVNPHINLFFFSSRGSVGRPVSHRK 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 451 YKHYPQttddidlpelnipqlnftemeplafKFKYH-LERKLKNIATMEFRhrmeVLDNLGLLFPFIKRLIIDEKTPRSA 529
Cdd:cd07232   299 GRGWRG-------------------------GFLLSaLEQYLKLDIKKWLK----VLRDLELLPRPLGQDWSQIFLQDFS 349

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2112362621 530 TEIAIVPKIKSLSVTRIIEG-QLDNIPYWIKCGEQSTWPVLSLLKTRCAVE 579
Cdd:cd07232   350 GTITIWPRSTLSDFLRILSDpTPEDLERMIHEGQQAAFPKLHFIKNRMRIE 400
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 139-434 2.56e-34

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: 132.58  E-value: 2.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 139 MLRNFAGIVdKKLFTKSLMGTKLLIEQHLERTIDGLDVL---DKSMTPT----SFFQRCKLSLGTTALILQGGSFFGLFH 211
Cdd:cd07231     5 LVRNLGNMC-NPELHKGRLEVPRLIRDYIAEVKAQLRAVvesDEDELSLeeklAFFQETRHAFGRTALLLSGGAALGTFH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 212 LGVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSrlltgnvildmirndmDLVRSCgygnmeqhvnlgklvqnli 291
Cdd:cd07231    84 VGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQ----------------SFFRAL------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 292 hhgysqdvylfiqfvlkyiVKDMTFEEAYQATGKAFNVVIHPIDKS-CPNLLNYVTTPNVLIRSAIECSLGSGVLSSNTK 370
Cdd:cd07231   129 -------------------LGDLTFQEAYDRTGRILGITVCPPRKSePPRLLNYLTSPHVVIWSAVAASCAFPGLFEAQE 189

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112362621 371 LLCKNLNNDTVRFLEFGKAgadqflAPEQATNLDDVES--PYTRLTELFNVNNFIVSLAKPYLAPL 434
Cdd:cd07231   190 LMAKDRFGEIVPYHPPGKV------SSPRRWRDGSLEQdlPMQQLRELFNVNHFIVSQANPHIVPL 249
DUF3336 pfam11815
Domain of unknown function (DUF3336); This family of proteins are functionally uncharacterized. ...
 65-191 2.01e-26

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: 104.53  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621  65 EAIKELDSSESYDDWCERATIVDEITGANLWRRNFFSRRYDFRSVLEQYASLTKNLNENDIEKIkekFSTTGPCMLRNFA 144
Cdd:pfam11815  10 RLRKKLRNAKSYEEWKEAAKELDELLGNDEWKENDESAYYDYKLVRRVLSQLRRAREEEDLRAL---LFLLRTCLKRNFA 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2112362621 145 GIVDKKLFTKSLMGTKLLIEQHLERTIDGLDVLDKSMTPT-----SFFQRCK 191
Cdd:pfam11815  87 GIENPRLYSHTYYGTKNLIEEYIDEVEKSLEYLAESPSLSleeklEFFKETR 138
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 199-272 7.21e-12

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: 63.90  E-value: 7.21e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112362621 199 LILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGCLSNEELSRLLTGNVILDM-IRNDMDLVRSC 272
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVrLRFDGAFPPTG 75
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 196-266 8.30e-12

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 65.69  E-value: 8.30e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112362621 196 TTALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGC-LSNEELSRLLTGNVILDMIRNDM 266
Cdd:COG1752     6 KIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAgYSADELEELWRSLDRRDLFDLSL 77
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 199-359 6.04e-10

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: 58.77  E-value: 6.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 199 LILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVfgclsneeLSRLLTGNVILDMIRN-DMDLVRSCGYGNM 277
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAAL--------LALGRDPEEIEDLLLElDLNLFLSLIRKRA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 278 EQHVNLGKLVQNLihHGYSQDVYLFIqfVLKYIVKDMTFEEAYQATGKAFNVVIH--------PIDKSCPNLLNYVTTPN 349
Cdd:pfam01734  73 LSLLALLRGLIGE--GGLFDGDALRE--LLRKLLGDLTLEELAARLSLLLVVALRalltvistALGTRARILLPDDLDDD 148

                         170
                  ....*....|
gi 2112362621 350 VLIRSAIECS 359
Cdd:pfam01734 149 EDLADAVLAS 158
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 197-242 4.27e-08

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: 53.32  E-value: 4.27e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2112362621 197 TALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFG 242
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYA 46
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 199-243 1.57e-07

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: 52.29  E-value: 1.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2112362621 199 LILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGC 243
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAG 45
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 197-253 4.05e-07

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: 51.19  E-value: 4.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2112362621 197 TALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGC-LSNEELSRLL 253
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASgISPDEMAELL 58
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 198-248 3.50e-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: 47.65  E-value: 3.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2112362621 198 ALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVF--GCLSNEE 248
Cdd:cd07228     2 GLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYaaGHLDALE 54
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 199-252 1.28e-04

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: 42.79  E-value: 1.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 199 LILQGGSFFGLFHLGVIKALLSQNL--MPNIISGSSMGACIAS----VFGCLSNEELSRL 252
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAAtlypPSSSLDNKPRQSL 60
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 199-359 1.80e-04

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: 42.65  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 199 LILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVFGC-LSNEELSRLltgnvILDMIRNDMdlvrscgygnM 277
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALgYSAADIKDI-----LKETDFAKL----------L 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112362621 278 EQHVNLGKLVQNLIHHG--YSQDvYLF------IQFVLKYIVKDMTFEEAYQATGKAFNVVIHPIDKSCPNLLNYVTTPN 349
Cdd:cd07207    67 DSPVGLLFLLPSLFKEGglYKGD-ALEewlrelLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVVFSAETTPD 145

                         170
                  ....*....|
gi 2112362621 350 VLIRSAIECS 359
Cdd:cd07207   146 MPVAKAVRAS 155
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 185-241 7.23e-04

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


Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 42.00  E-value: 7.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2112362621 185 SFFQRCKLSL-GTT-ALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIASVF 241
Cdd:cd07225     2 SDFSRLARVLtGNSiALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALY 60
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
195-239 2.54e-03

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 40.15  E-value: 2.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2112362621 195 GTTALILQGGSFFGLFHLGVIKALLSQNLMPNIISGSSMGACIAS 239
Cdd:COG4667     4 MKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGA 48
 
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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