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Conserved domains on  [gi|17196626|ref|NP_079501|]
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1-acylglycerol-3-phosphate O-acyltransferase PNPLA3 [Homo sapiens]

Protein Classification

patatin-like phospholipase domain-containing protein; patatin-like phospholipase family protein( domain architecture ID 10163449)

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_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 8-259 0e+00

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: 534.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   8 WSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPS 87
Cdd:cd07221   1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  88 FNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDG 167
Cdd:cd07221  81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 168 GVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFR 247
Cdd:cd07221 161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                       250
                ....*....|..
gi 17196626 248 FLEEKGICNRPQ 259
Cdd:cd07221 241 FLEENGICNRPQ 252
 
Name Accession Description Interval E-value
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 8-259 0e+00

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: 534.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   8 WSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPS 87
Cdd:cd07221   1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  88 FNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDG 167
Cdd:cd07221  81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 168 GVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFR 247
Cdd:cd07221 161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                       250
                ....*....|..
gi 17196626 248 FLEEKGICNRPQ 259
Cdd:cd07221 241 FLEENGICNRPQ 252
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-178 2.42e-22

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: 94.21  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626    10 LSFAGCGFLGFYHVGATRCLSEHAPHllrdARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGI------ 83
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626    84 -----------FHPSFNLSKFLRQGL---------CKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALV 143
Cdd:pfam01734  77 allrgligeggLFDGDALRELLRKLLgdltleelaARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17196626   144 CSCFIPFYsgLIPPSFRGVRYVDGGVSDNVPFIDA 178
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 10-251 5.62e-14

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 71.86  E-value: 5.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAphllRDARMLFGASAGALhcVGVL--SGIPLEQTLQVLSDL----------VRKAR 77
Cdd:COG1752   9 LVLSGGGARGAAHIGVLKALEEAG----IPPDVIAGTSAGAI--VGALyaAGYSADELEELWRSLdrrdlfdlslPRRLL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  78 SRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLvsdFRSkDEVVDALVCSCFIPfysGLIPP 157
Cdd:COG1752  83 RLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVV---FDS-GPLADAVRASAAIP---GVFPP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 158 -SFRGVRYVDGGVSDNVPF-----IDAKTTITVSPFYGEYDIcPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPP-- 229
Cdd:COG1752 156 vEIDGRLYVDGGVVNNLPVdparaLGADRVIAVDLNPPLRKL-PSLLDILGRALEIMFNSILRRELALEPADILIEPDls 234

                       250       260
                ....*....|....*....|....*..
gi 17196626 230 -----DLKVLGEICLRGYLDAFRFLEE 251
Cdd:COG1752 235 gisllDFSRAEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 8-259 0e+00

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: 534.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   8 WSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPS 87
Cdd:cd07221   1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  88 FNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDG 167
Cdd:cd07221  81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 168 GVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFR 247
Cdd:cd07221 161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                       250
                ....*....|..
gi 17196626 248 FLEEKGICNRPQ 259
Cdd:cd07221 241 FLEENGICNRPQ 252
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 9-251 3.29e-147

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: 420.22  E-value: 3.29e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   9 SLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPSF 88
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  89 NLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGG 168
Cdd:cd07204  81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 169 VSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRF 248
Cdd:cd07204 161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                ...
gi 17196626 249 LEE 251
Cdd:cd07204 241 LER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 5-251 1.76e-120

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: 352.51  E-value: 1.76e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   5 ERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIF 84
Cdd:cd07220   2 DSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  85 HPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRY 164
Cdd:cd07220  82 HPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRY 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 165 VDGGVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLD 244
Cdd:cd07220 162 VDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRD 241


                ....*..
gi 17196626 245 AFRFLEE 251
Cdd:cd07220 242 ALRFLKE 248
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 2-402 4.44e-108

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: 326.87  E-value: 4.44e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   2 YDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNI 81
Cdd:cd07223   4 LEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  82 GIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRG 161
Cdd:cd07223  84 GIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 162 VRYVDGGVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRG 241
Cdd:cd07223 164 ERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQG 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 242 YLDAFRFLEEKGICNRPQPGLKSSSEGmdpevamPSWANMSLDSSPESaalavRLEGDELLDHLRLSILPWDESILDTLS 321
Cdd:cd07223 244 YLDALRFLERRGLTKEPVLWSLVSKEP-------PAPADGPRDTGHDQ-----GQKGGLSLNWDVPNVLVKDVPNFEQLS 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 322 PRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTLPVESAIAIVQRLVTWLPDMPDDVLWLQWV----TSQVFTRV 397
Cdd:cd07223 312 PELEAALKKACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLlkstALEVYSRA 391


                ....*
gi 17196626 398 LMCLL 402
Cdd:cd07223 392 KSQLL 396
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 9-253 3.10e-97

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: 293.10  E-value: 3.10e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   9 SLSFAGCGFLGFYHVGATRCLSEHAPHLLRDarMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPSF 88
Cdd:cd07218   2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLLN--KISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  89 NLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGG 168
Cdd:cd07218  80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 169 VSDNVPFIDaKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRF 248
Cdd:cd07218 160 FSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRF 238


                ....*
gi 17196626 249 LEEKG 253
Cdd:cd07218 239 LHRNN 243
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 10-253 4.97e-70

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: 222.98  E-value: 4.97e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALhCVGVLSGIP--LEQTLQVLSDLVRKARSRNIGIFHPS 87
Cdd:cd07222   2 LSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSL-VAAVLLTAPekIEECKEFTYKFAEEVRKQRFGAMTPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  88 FNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDG 167
Cdd:cd07222  81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 168 GVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFR 247
Cdd:cd07222 161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                ....*.
gi 17196626 248 FLEEKG 253
Cdd:cd07222 241 FLKKEN 246
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 10-186 1.28e-66

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: 211.43  E-value: 1.28e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAPHllrdARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPSFN 89
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  90 LSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSdFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGV 169
Cdd:cd07198  77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                       170
                ....*....|....*..
gi 17196626 170 SDNVPFIDAKTTITVSP 186
Cdd:cd07198 156 SNNLPVAELGNTINVSP 172
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 9-249 2.49e-65

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: 215.53  E-value: 2.49e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   9 SLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPSF 88
Cdd:cd07219  14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  89 NLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGG 168
Cdd:cd07219  94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 169 VSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRF 248
Cdd:cd07219 174 FTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253


                .
gi 17196626 249 L 249
Cdd:cd07219 254 L 254
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 10-186 3.90e-37

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: 133.69  E-value: 3.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAPHllRDARMLFGASAGALHCVGVLsgipleqtlqvlsdlvrkarsrnigifHPSFN 89
Cdd:cd01819   1 LSFSGGGFRGMYHAGVLSALAERGLL--DCVTYLAGTSGGAWVAATLY---------------------------PPSSS 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  90 LSKFLRQGLCkclpanvhQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPP----------SF 159
Cdd:cd01819  52 LDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKE 123

                       170       180       190
                ....*....|....*....|....*....|..
gi 17196626 160 RGVRYVDGGVSDNVPFI-----DAKTTITVSP 186
Cdd:cd01819 124 KGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 11-251 3.97e-34

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: 128.22  E-value: 3.97e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  11 SFAGCGFLGFYHVGATRCLSEHapHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIgifhpSFNL 90
Cdd:cd07224   3 SFSAAGLLFPYHLGVLSLLIEA--GVINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNGT-----AFRL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  91 SKFLRQGLCKCLPANVHQLIS-GKIGISLTRVS---DGEnvLVSDFRSKDEVVDALVCSCFIPFYSGLIPPS-FRGVRYV 165
Cdd:cd07224  76 GGVLRDELDKTLPDDAHERCNrGRIRVAVTQLFpvpRGL--LVSSFDSKSDLIDALLASCNIPGYLAPWPATmFRGKLCV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 166 DGGVSDNVP-FIDAKTTITVSPFYGEYdicPKVKSTNFLHVDITKLSlrlcTGNLYLLSRAFVPPDLKVLGEICLRGYLD 244
Cdd:cd07224 154 DGGFALFIPpTTAADRTVRVCPFPASR---SSIKGQNLDNDDTEDVP----YSRRQLLNWALEPADDAMLLELFNEGYKD 226


                ....*..
gi 17196626 245 AFRFLEE 251
Cdd:cd07224 227 ANEWAKE 233
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-178 2.42e-22

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: 94.21  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626    10 LSFAGCGFLGFYHVGATRCLSEHAPHllrdARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGI------ 83
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626    84 -----------FHPSFNLSKFLRQGL---------CKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALV 143
Cdd:pfam01734  77 allrgligeggLFDGDALRELLRKLLgdltleelaARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17196626   144 CSCFIPFYsgLIPPSFRGVRYVDGGVSDNVPFIDA 178
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 10-251 5.62e-14

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 71.86  E-value: 5.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAphllRDARMLFGASAGALhcVGVL--SGIPLEQTLQVLSDL----------VRKAR 77
Cdd:COG1752   9 LVLSGGGARGAAHIGVLKALEEAG----IPPDVIAGTSAGAI--VGALyaAGYSADELEELWRSLdrrdlfdlslPRRLL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  78 SRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLvsdFRSkDEVVDALVCSCFIPfysGLIPP 157
Cdd:COG1752  83 RLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVV---FDS-GPLADAVRASAAIP---GVFPP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 158 -SFRGVRYVDGGVSDNVPF-----IDAKTTITVSPFYGEYDIcPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPP-- 229
Cdd:COG1752 156 vEIDGRLYVDGGVVNNLPVdparaLGADRVIAVDLNPPLRKL-PSLLDILGRALEIMFNSILRRELALEPADILIEPDls 234

                       250       260
                ....*....|....*....|....*..
gi 17196626 230 -----DLKVLGEICLRGYLDAFRFLEE 251
Cdd:COG1752 235 gisllDFSRAEELIEAGYEAARRALDE 261
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 10-272 2.92e-11

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 63.78  E-value: 2.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHaphLLRDARMLFGASAGALHCVGVLSGIPlEQTLQVLSDLVRKA---------RSRN 80
Cdd:cd07208   1 LVLEGGGMRGAYTAGVLDAFLEA---GIRPFDLVIGVSAGALNAASYLSGQR-GRALRINTKYATDPrylglrsllRTGN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  81 IgifhpsFNLSKFLRQGLCKCLPANVHQLISGKIG--ISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGliPPS 158
Cdd:cd07208  77 L------FDLDFLYDELPDGLDPFDFEAFAASPARfyVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFP--PVR 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 159 FRGVRYVDGGVSDNVPFI----DAKTTITVspfygeydICPKVKSTNFLHVDITKLSLRLCTG--NLY--LLSRAfvppd 230
Cdd:cd07208 149 IDGEPYVDGGLSDSIPVDkaieDGADKIVV--------ILTRPRGYRKKPSKSSPLAKLLYRKypNLVeaLLRRH----- 215

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17196626 231 lkvlgeICLRGYLDAFRFLEEKG--ICNRPQPGLKSSSEGMDPE 272
Cdd:cd07208 216 ------SRYNETLEFIRRLEAEGkiFVIAPEKPLKVSRLERDPE 253
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
42-184 6.30e-11

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 62.87  E-value: 6.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  42 MLFGASAGALHCVGVLSGIPlEQTLQVLSDLVRkaRSRNIGIFH-----PSFNLsKFLRQGLCKCL-PANVHQLISGKIG 115
Cdd:COG4667  36 LVIGVSAGALNGASYLSRQP-GRARRVITDYAT--DPRFFSLRNflrggNLFDL-DFLYDEIPNELlPFDFETFKASPRE 111

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17196626 116 --ISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGliPPSFRGVRYVDGGVSDNVPFIDAK----TTITV 184
Cdd:COG4667 112 fyVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP--PVEIDGKRYLDGGVADSIPVREAIrdgaDKIVV 184
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 10-174 8.18e-10

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: 58.44  E-value: 8.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAphlLRDARMLfGASAGALhcVGVL--SGIPLeqtlqvlSDLVRKARSRNIGIFHPS 87
Cdd:cd07207   2 LVFEGGGAKGIAYIGALKALEEAG---ILKKRVA-GTSAGAI--TAALlaLGYSA-------ADIKDILKETDFAKLLDS 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  88 FN------LSKFLRQGLCK--CLPANVHQLISGKIGISL--------------------TRVSDGENVLVSDFRSKD-EV 138
Cdd:cd07207  69 PVgllfllPSLFKEGGLYKgdALEEWLRELLKEKTGNSFatsllrdldddlgkdlkvvaTDLTTGALVVFSAETTPDmPV 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17196626 139 VDALVCSCFIPFYsglippsFRGVR------YVDGGVSDNVP 174
Cdd:cd07207 149 AKAVRASMSIPFV-------FKPVRlakgdvYVDGGVLDNYP 183
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 16-175 4.38e-09

Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 56.59  E-value: 4.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  16 GFLGFY-HVGATRCLSEHAphlLRDARMLfGASAGALhcVGVL--SGIPLEQTLQVLSDLVRK------ARSRNIGIFHP 86
Cdd:cd07210   8 GFFGFYaHLGFLAALLEMG---LEPSAIS-GTSAGAL--VGGLfaSGISPDEMAELLLSLERKdfwmfwDPPLRGGLLSG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  87 SfNLSKFLRQGLckcLPANVHQLiSGKIGISLTRVSDGENVLVSdfrsKDEVVDALVCSCFIPFYSGliPPSFRGVRYVD 166
Cdd:cd07210  82 D-RFAALLREHL---PPDRFEEL-RIPLAVSVVDLTSRETLLLS----EGDLAEAVAASCAVPPLFQ--PVEIGGRPFVD 150


                ....*....
gi 17196626 167 GGVSDNVPF 175
Cdd:cd07210 151 GGVADRLPF 159
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 10-212 4.66e-09

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 subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 57.30  E-value: 4.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNI---GIFHP 86
Cdd:cd07213   5 LSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSaggGAGNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  87 SFNLSKFLRQGLCKCLPA------------NVHQLISGKigisltrvSDGE--------NVLVSDFRSKDEVVDALVCSC 146
Cdd:cd07213  85 QYFAAGFLKAFAEVFFGDltlgdlkrkvlvPSFQLDSGK--------DDPNrrwkpklfHNFPGEPDLDELLVDVCLRSS 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17196626 147 FIPFYSglipPSFRGvrYVDGGVSDNVPFIDAKTTItvspfYGEYDICPKVKstnflhvDITKLSL 212
Cdd:cd07213 157 AAPTYF----PSYQG--YVDGGVFANNPSLCAIAQA-----IGEEGLNIDLK-------DIVVLSL 204
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 10-205 1.48e-07

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: 52.98  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHapHLLrdARMLFGASAGALhcVGVLSGIPLEQtlQVLSDLV------RKARSRNIgi 83
Cdd:cd07206  72 LMLSGGASLGLFHLGVVKALWEQ--DLL--PRVISGSSAGAI--VAALLGTHTDE--ELIGDLTfqeayeRTGRIINI-- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  84 fhpsfnlskflrqglcKCLPANVHQliSGKIGISLTrvsdGENVLVsdfRSkdevvdALVCSCFIPF-----------YS 152
Cdd:cd07206 142 ----------------TVAPAEPHQ--NSRLLNALT----SPNVLI---WS------AVLASCAVPGvfppvmlmaknRD 190

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17196626 153 GLIPPSFRGVRYVDGGVSDNVP------------FIDAKTTITVSPFYGEY----DICPKVKSTNFLHV 205
Cdd:cd07206 191 GEIVPYLPGRKWVDGSVSDDLPakrlarlynvnhFIVSQTNPHVVPFLQEYsgdiTIIPPFSFSNPLKL 259
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 10-250 2.41e-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: 51.52  E-value: 2.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  10 LSFAGCGFLGFYHVGATRCLSEHAPHLlrDarMLFGASAGALHCVGVLSGipLEQTLQVLSDLVRKARSRNIgifhpsfn 89
Cdd:cd07209   1 LVLSGGGALGAYQAGVLKALAEAGIEP--D--IISGTSIGAINGALIAGG--DPEAVERLEKLWRELSREDV-------- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  90 lskFLRQGLCKCLP---ANVHQLISGKIGISLTRVSDGENVLVSDfRSKDEVVDALVCSCFIPfysGLIPP-SFRGVRYV 165
Cdd:cd07209  67 ---FLRGLLDRALDfdtLRLLAILFAGLVIVAVNVLTGEPVYFDD-IPDGILPEHLLASAALP---PFFPPvEIDGRYYW 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626 166 DGGVSDNVP---FIDAK-TTITVSPFYGEydicPKVKSTNFLHVDITKLSLRLctgnlyllsRAFVPPDLKVLGEICLRG 241
Cdd:cd07209 140 DGGVVDNTPlspAIDLGaDEIIVVSLSDK----GRDDRKGTPPTTLIEILPRL---------FLRSGLDSERIRHNLELG 206


                ....*....
gi 17196626 242 YLDAFRFLE 250
Cdd:cd07209 207 YLDTLRADS 215
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 8-174 4.80e-07

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: 49.85  E-value: 4.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626   8 WSLSFAGCGFLGFYHVGATRCLSEHA--PHllrdarMLFGASAGALhcVGVL--SGIPLEQTLQVLSDLVRKARSRNiGI 83
Cdd:cd07205   1 IGLALSGGGARGLAHIGVLKALEEAGipID------IVSGTSAGAI--VGALyaAGYSPEEIEERAKLRSTDLKALS-DL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17196626  84 FHPSFNL--SKFLRQGLCKCLPA-NVHQLisgKIG--ISLTRVSDGENVLvsdFRSKDeVVDALVCSCFIPfysGLIPP- 157
Cdd:cd07205  72 TIPTAGLlrGDKFLELLDEYFGDrDIEDL---WIPffIVATDLTSGKLVV---FRSGS-LVRAVRASMSIP---GIFPPv 141

                       170
                ....*....|....*..
gi 17196626 158 SFRGVRYVDGGVSDNVP 174
Cdd:cd07205 142 KIDGQLLVDGGVLNNLP 158
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 9-53 3.39e-03

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: 39.36  E-value: 3.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17196626   9 SLSFAGCGFLGFYHVGATRCLSEHapHLLrdARMLFGASAGALHC 53
Cdd:cd07231  70 ALLLSGGAALGTFHVGVVRTLVEH--QLL--PRVIAGSSVGSIVC 110
 
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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