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Conserved domains on  [gi|281366229|ref|NP_001163445|]
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brummer, isoform B [Drosophila melanogaster]

Protein Classification

patatin-like phospholipase domain-containing protein; patatin-like phospholipase family protein( domain architecture ID 10163430)

patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids| patatin-like phospholipase family protein may catalyze 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_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 1-245 0e+00

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


:

Pssm-ID: 132857  Cd Length: 245  Bit Score: 536.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   1 MNLSFAGCGFLGIYHVGVAVCFKKYAPHLLLEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSFN 80
Cdd:cd07218    1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  81 IQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGAF 160
Cdd:cd07218   81 IQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 161 SDNLPILDENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQFLH 240
Cdd:cd07218  161 SDNLPTLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRFLH 240


                 ....*
gi 281366229 241 RNNLI 245
Cdd:cd07218  241 RNNLI 245
 
Name Accession Description Interval E-value
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 1-245 0e+00

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


Pssm-ID: 132857  Cd Length: 245  Bit Score: 536.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   1 MNLSFAGCGFLGIYHVGVAVCFKKYAPHLLLEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSFN 80
Cdd:cd07218    1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  81 IQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGAF 160
Cdd:cd07218   81 IQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 161 SDNLPILDENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQFLH 240
Cdd:cd07218  161 SDNLPTLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRFLH 240


                 ....*
gi 281366229 241 RNNLI 245
Cdd:cd07218  241 RNNLI 245
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 3-168 5.73e-20

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: 88.05  E-value: 5.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229    3 LSFAGCGFLGIYHVGVAVCFKKYAPHLllEKIGGASAGSLAACCLLCDLPLGSMTSDFFRV-----VNEARRYSLGPFSP 77
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRF--DVISGTSAGAINAALLALGRDPEEIEDLLLELdlnlfLSLIRKRALSLLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   78 SFNI--------QTCLLEGLQKHLPDDAHKRVNGRL-------------HISLTRVYDGKNVIISEFESREEVLQALLCA 136
Cdd:pfam01734  79 LRGLigegglfdGDALRELLRKLLGDLTLEELAARLslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLAS 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 281366229  137 CFIPGFsgILPPRFRGVRYMDGAFSDNLPILD 168
Cdd:pfam01734 159 SALPGV--FPPVRLDGELYVDGGLVDNVPVEA 188
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 2-241 3.20e-13

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 69.93  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVavcfkkyaphL--LLEK------IGGASAGSLAACCLLCDLPLGSMTsDFFRVVNEARRYSLG 73
Cdd:COG1752    8 GLVLSGGGARGAAHIGV----------LkaLEEAgippdvIAGTSAGAIVGALYAAGYSADELE-ELWRSLDRRDLFDLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  74 PFSPSFNIQTCLLEG-----------LQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFEsreeVLQALLCACFIPGf 142
Cdd:COG1752   77 LPRRLLRLDLGLSPGglldgdplrrlLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGP----LADAVRASAAIPG- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 143 sgILPP-RFRGVRYMDGAFSDNLPI--LDENT------ITVSPfcgesdicPRDQSSQLFHLnwANTSIEISRQNINR-- 211
Cdd:COG1752  152 --VFPPvEIDGRLYVDGGVVNNLPVdpARALGadrviaVDLNP--------PLRKLPSLLDI--LGRALEIMFNSILRre 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 281366229 212 ----FVRILFPPRPEFLSKF--------CQQGFDDALQFLHR 241
Cdd:COG1752  220 lalePADILIEPDLSGISLLdfsraeelIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 1-245 0e+00

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


Pssm-ID: 132857  Cd Length: 245  Bit Score: 536.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   1 MNLSFAGCGFLGIYHVGVAVCFKKYAPHLLLEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSFN 80
Cdd:cd07218    1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  81 IQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGAF 160
Cdd:cd07218   81 IQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 161 SDNLPILDENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQFLH 240
Cdd:cd07218  161 SDNLPTLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRFLH 240


                 ....*
gi 281366229 241 RNNLI 245
Cdd:cd07218  241 RNNLI 245
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 2-241 2.04e-128

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: 375.15  E-value: 2.04e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVAVCFKKYAPHLLL--EKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSF 79
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQnaRRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  80 NIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGA 159
Cdd:cd07204   81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 160 FSDNLPIL-DENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQF 238
Cdd:cd07204  161 LSDNLPILdDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                 ...
gi 281366229 239 LHR 241
Cdd:cd07204  241 LER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 1-242 2.76e-110

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 329.01  E-value: 2.76e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   1 MNLSFAGCGFLGIYHVGVAVCFKKYAPHLL--LEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPS 78
Cdd:cd07220    5 WNISFAGCGFLGVYHVGVASCLLEHAPFLVanARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPLHPS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  79 FNIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDG 158
Cdd:cd07220   85 FNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 159 AFSDNLPILD-ENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQ 237
Cdd:cd07220  165 GISDNLPQYElKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRDALR 244


                 ....*
gi 281366229 238 FLHRN 242
Cdd:cd07220  245 FLKEN 249
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 2-246 1.63e-93

Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes and is an indicator of the nutritional state. PNPLA3 is also known as adiponutrin (ADPN) or iPLA2-epsilon. Human adiponutrins are bound to the cell membrane of adipocytes and show transacylase, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: ADPN (adiponutrin) from mammals, PNPLA3 (Patatin-like phospholipase domain-containing protein 3), and iPLA2-epsilon (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132860  Cd Length: 252  Bit Score: 286.29  E-value: 1.63e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVAVCFKKYAPHLL--LEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSF 79
Cdd:cd07221    2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLrdARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPSF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  80 NIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGA 159
Cdd:cd07221   82 NLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 160 FSDNLPILD-ENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQF 238
Cdd:cd07221  162 VSDNVPFFDaKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFRF 241


                 ....*...
gi 281366229 239 LHRNNLIN 246
Cdd:cd07221  242 LEENGICN 249
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 2-243 3.60e-77

Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene sequence-2), shows both lipase and transacylation activities. GS2 lipase is expressed in various tissues, predominantly in muscle and adipocytes tissue. It is also expressed in keratinocytes and shows retinyl ester hydrolase, acylglycerol, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: GS2 from mammals, PNPLA4 (Patatin-like phospholipase domain-containing protein 4), and iPLA2-eta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132861 [Multi-domain]  Cd Length: 246  Bit Score: 243.78  E-value: 3.60e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVAVCFKKYAPHLL--LEKIGGASAGSLAACCLLCDLPLGSMTSDF-FRVVNEARRYSLGPFSPS 78
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLkrVKRFAGASAGSLVAAVLLTAPEKIEECKEFtYKFAEEVRKQRFGAMTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  79 FNIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDG 158
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 159 AFSDNLPIL-DENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQ 237
Cdd:cd07222  161 GFTNSLPVLpVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                 ....*.
gi 281366229 238 FLHRNN 243
Cdd:cd07222  241 FLKKEN 246
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 2-244 5.36e-74

Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), plays a role in regulation of adipocyte differentiation. PNPLA5 is expressed in brain tissue in high mRNA levels and low levels in liver tissue. There is no concrete evidence in support of the enzymatic activity of GS2L. This family includes patatin-like proteins: GS2L (GS2-like) and PNPLA5 (Patatin-like phospholipase domain-containing protein 5) reported exclusively in mammals.


Pssm-ID: 132862  Cd Length: 405  Bit Score: 240.97  E-value: 5.36e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVAVCFKKYAPHLL--LEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSF 79
Cdd:cd07223   11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLqgARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPAY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  80 NIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGA 159
Cdd:cd07223   91 APIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDGA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 160 FSDNLPILD-ENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQF 238
Cdd:cd07223  171 LSNNLPFSDcPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALRF 250


                 ....*.
gi 281366229 239 LHRNNL 244
Cdd:cd07223  251 LERRGL 256
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-243 1.91e-70

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 230.94  E-value: 1.91e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVAVCFKKYAPHLL--LEKIGGASAGSLAACCLLCDLPLgsmtSDFFRVVN----EARRYSLGPF 75
Cdd:cd07219   14 SISFSGSGFLSFYQAGVVDALRDLAPRMLetAHRVAGTSAGSVIAALVVCGISM----DEYLRVLNvgvaEVRKSFLGPL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  76 SPSFNIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRY 155
Cdd:cd07219   90 SPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 156 MDGAFSDNLPI-LDENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDD 234
Cdd:cd07219  170 IDGGFTGMQPCsFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQD 249


                 ....*....
gi 281366229 235 ALQFLHRNN 243
Cdd:cd07219  250 TVLYLRRLN 258
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 3-176 1.77e-56

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: 187.16  E-value: 1.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   3 LSFAGCGFLGIYHVGVAVCFKKYAPHLllEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSFNIQ 82
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLI--DIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGRLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  83 TCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISeFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGAFSD 162
Cdd:cd07198   79 GILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGLSN 157

                        170
                 ....*....|....*
gi 281366229 163 NLPILD-ENTITVSP 176
Cdd:cd07198  158 NLPVAElGNTINVSP 172
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 3-176 1.19e-34

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: 127.92  E-value: 1.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   3 LSFAGCGFLGIYHVGVAVCFKKYAPHLLLEKIGGASAGSLAACCLLcdlplgsmtsdffrvvnearryslgpfSPSFNIQ 82
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY---------------------------PPSSSLD 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  83 TCLLEGLQKHLpddahkrvNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPR----------FRG 152
Cdd:cd01819   54 NKPRQSLEEAL--------SGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPAelytsksnlkEKG 125

                        170       180       190
                 ....*....|....*....|....*....|
gi 281366229 153 VRYMDGAFSDNLPIL------DENTITVSP 176
Cdd:cd01819  126 VRLVDGGVSNNLPAPvllrpgRGVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 4-177 7.97e-29

Patatin-like phospholipase; 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: 132863  Cd Length: 233  Bit Score: 114.36  E-value: 7.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   4 SFAGCGFLGIYHVGVAvcfkkyapHLLLEK--------IGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLgpf 75
Cdd:cd07224    3 SFSAAGLLFPYHLGVL--------SLLIEAgvinettpLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNGT--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  76 spSFNIQTCLLEGLQKHLPDDAHKRVN-GRLHISLTR---VYDGKNViiSEFESREEVLQALLCACFIPGFSGILPP-RF 150
Cdd:cd07224   72 --AFRLGGVLRDELDKTLPDDAHERCNrGRIRVAVTQlfpVPRGLLV--SSFDSKSDLIDALLASCNIPGYLAPWPAtMF 147

                        170       180
                 ....*....|....*....|....*....
gi 281366229 151 RGVRYMDGAFSDNLPILD--ENTITVSPF 177
Cdd:cd07224  148 RGKLCVDGGFALFIPPTTaaDRTVRVCPF 176
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 3-168 5.73e-20

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: 88.05  E-value: 5.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229    3 LSFAGCGFLGIYHVGVAVCFKKYAPHLllEKIGGASAGSLAACCLLCDLPLGSMTSDFFRV-----VNEARRYSLGPFSP 77
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRF--DVISGTSAGAINAALLALGRDPEEIEDLLLELdlnlfLSLIRKRALSLLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   78 SFNI--------QTCLLEGLQKHLPDDAHKRVNGRL-------------HISLTRVYDGKNVIISEFESREEVLQALLCA 136
Cdd:pfam01734  79 LRGLigegglfdGDALRELLRKLLGDLTLEELAARLslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLAS 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 281366229  137 CFIPGFsgILPPRFRGVRYMDGAFSDNLPILD 168
Cdd:pfam01734 159 SALPGV--FPPVRLDGELYVDGGLVDNVPVEA 188
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 2-241 3.20e-13

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 69.93  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVavcfkkyaphL--LLEK------IGGASAGSLAACCLLCDLPLGSMTsDFFRVVNEARRYSLG 73
Cdd:COG1752    8 GLVLSGGGARGAAHIGV----------LkaLEEAgippdvIAGTSAGAIVGALYAAGYSADELE-ELWRSLDRRDLFDLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  74 PFSPSFNIQTCLLEG-----------LQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFEsreeVLQALLCACFIPGf 142
Cdd:COG1752   77 LPRRLLRLDLGLSPGglldgdplrrlLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGP----LADAVRASAAIPG- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 143 sgILPP-RFRGVRYMDGAFSDNLPI--LDENT------ITVSPfcgesdicPRDQSSQLFHLnwANTSIEISRQNINR-- 211
Cdd:COG1752  152 --VFPPvEIDGRLYVDGGVVNNLPVdpARALGadrviaVDLNP--------PLRKLPSLLDI--LGRALEIMFNSILRre 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 281366229 212 ----FVRILFPPRPEFLSKF--------CQQGFDDALQFLHR 241
Cdd:COG1752  220 lalePADILIEPDLSGISLLdfsraeelIEAGYEAARRALDE 261
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
7-166 2.21e-11

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 64.80  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   7 GCGFLGIYHVGVAVCF---KKYAPHLLlekigGASAGSLAACCLLCDLPLGSMTSdFFRVVNEARRYSLGPF---SPSFN 80
Cdd:COG4667   12 GGGMRGIFTAGVLDALleeGIPFDLVI-----GVSAGALNGASYLSRQPGRARRV-ITDYATDPRFFSLRNFlrgGNLFD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  81 IQTCLLEGLQKHLP--DDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGilPPRFRGVRYMDG 158
Cdd:COG4667   86 LDFLYDEIPNELLPfdFETFKASPREFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP--PVEIDGKRYLDG 163


                 ....*...
gi 281366229 159 AFSDNLPI 166
Cdd:COG4667  164 GVADSIPV 171
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 3-166 1.71e-06

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: 48.31  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   3 LSFAGCGFLGIYHVGVAVCFKKYapHLLLEKIGGASAGSLAACcLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSFNI- 81
Cdd:cd07205    3 LALSGGGARGLAHIGVLKALEEA--GIPIDIVSGTSAGAIVGA-LYAAGYSPEEIEERAKLRSTDLKALSDLTIPTAGLl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  82 -QTCLLEGLQKHLPDdahKRVNG---RLHISLTRVYDGKNVIISefesREEVLQALLCACFIPGfsgILPPRF-RGVRYM 156
Cdd:cd07205   80 rGDKFLELLDEYFGD---RDIEDlwiPFFIVATDLTSGKLVVFR----SGSLVRAVRASMSIPG---IFPPVKiDGQLLV 149

                        170
                 ....*....|
gi 281366229 157 DGAFSDNLPI 166
Cdd:cd07205  150 DGGVLNNLPV 159
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 3-239 1.34e-05

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: 46.52  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   3 LSFAGCGFLGIYHVGVavcFKKYAPHLL-LEKIGGASAGSLAACCLLCDLPLG---------SMT-SDFFrvvnearrys 71
Cdd:cd07209    1 LVLSGGGALGAYQAGV---LKALAEAGIePDIISGTSIGAINGALIAGGDPEAverleklwrELSrEDVF---------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  72 lgpfspsfniqtcLLEGLQKHLPDD---AHKRVNGRLHISLTRVYDGKNVIISEfESREEVLQALLCACFIPGFsgiLPP 148
Cdd:cd07209   68 -------------LRGLLDRALDFDtlrLLAILFAGLVIVAVNVLTGEPVYFDD-IPDGILPEHLLASAALPPF---FPP 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229 149 -RFRGVRYMDGAFSDNLPI---LD--ENTITVSPFcgeSDICPRDQSSQLFhlnwaNTSIEISRQNINRfvrilFPPRPE 222
Cdd:cd07209  131 vEIDGRYYWDGGVVDNTPLspaIDlgADEIIVVSL---SDKGRDDRKGTPP-----TTLIEILPRLFLR-----SGLDSE 197

                        250
                 ....*....|....*..
gi 281366229 223 FLSKFCQQGFDDALQFL 239
Cdd:cd07209  198 RIRHNLELGYLDTLRAD 214
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 2-166 3.08e-04

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: 42.33  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229   2 NLSFAGCGFLGIYHVGVAvcfkkyapHLLLE------KIGGASAGSLAACCLLCDLPLGSMTSdffRVVNEARRYSLGPF 75
Cdd:cd07210    2 ALVLSSGFFGFYAHLGFL--------AALLEmglepsAISGTSAGALVGGLFASGISPDEMAE---LLLSLERKDFWMFW 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366229  76 SPSfnIQTCLLEG------LQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEfesrEEVLQALLCACFIPGFSGilPPR 149
Cdd:cd07210   71 DPP--LRGGLLSGdrfaalLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSE----GDLAEAVAASCAVPPLFQ--PVE 142

                        170
                 ....*....|....*..
gi 281366229 150 FRGVRYMDGAFSDNLPI 166
Cdd:cd07210  143 IGGRPFVDGGVADRLPF 159
 
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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