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Conserved domains on  [gi|514974671|ref|WP_016662878|]
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MULTISPECIES: patatin-like phospholipase family protein [Bacteroides]

Protein Classification

patatin-like phospholipase family protein( domain architecture ID 11448329)

patatin-like phospholipase family protein such as the secreted form of Pseudomonas aeruginosa phospholipase PlpD, which is secreted through the type V secretion system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 21-303 1.61e-66

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 220.93  E-value: 1.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  21 QKVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKRWYSGqvepeygyy 100
Cdd:COG1752    5 PKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDL--------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 fkqnRPTPEFFNIRFSFkdslhikpqiLPTSMVNPIQMNLVFVELFARAtaacsgDFNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:COG1752   76 ----SLPRRLLRLDLGL----------SPGGLLDGDPLRRLLERLLGDR------DFEDLPIPLAVVATDLETGREVVFD 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 181 RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREDFKPEVIigsVVAANPGKPKENDLMSQLENM--IMQ 258
Cdd:COG1752  136 SGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVI---AVDLNPPLRKLPSLLDILGRAleIMF 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514974671 259 ------KTDYTLPDslgIIMTFKYDDVSLLDFDRLQELHDIGYNRTISLMD 303
Cdd:COG1752  213 nsilrrELALEPAD---ILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 21-303 1.61e-66

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 220.93  E-value: 1.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  21 QKVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKRWYSGqvepeygyy 100
Cdd:COG1752    5 PKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDL--------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 fkqnRPTPEFFNIRFSFkdslhikpqiLPTSMVNPIQMNLVFVELFARAtaacsgDFNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:COG1752   76 ----SLPRRLLRLDLGL----------SPGGLLDGDPLRRLLERLLGDR------DFEDLPIPLAVVATDLETGREVVFD 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 181 RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREDFKPEVIigsVVAANPGKPKENDLMSQLENM--IMQ 258
Cdd:COG1752  136 SGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVI---AVDLNPPLRKLPSLLDILGRAleIMF 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514974671 259 ------KTDYTLPDslgIIMTFKYDDVSLLDFDRLQELHDIGYNRTISLMD 303
Cdd:COG1752  213 nsilrrELALEPAD---ILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 23-236 7.71e-66

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: 215.87  E-value: 7.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  23 VGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDME--ALLRSEDFKRWysgqvepeygyy 100
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEerAKLRSTDLKAL------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 FKQNRPTPEFFNIRfsfkdslhikpqilptsmvnpiqmnlVFVELFARATaaCSGDFNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:cd07205   69 SDLTIPTAGLLRGD--------------------------KFLELLDEYF--GDRDIEDLWIPFFIVATDLTSGKLVVFR 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514974671 181 RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREdFKPEVIIGSVV 236
Cdd:cd07205  121 SGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRE-LGADIIIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 25-221 3.93e-32

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: 123.49  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671   25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKRwysgqvepeygyyFKqN 104
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNL-------------FL-S 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  105 RPTPEFFNIRFSFKDSLHIKPQILPTSMVNPIQMNLVF--VELFARATAACSGDFNRLFVPFRCIASDVYNKKPLI---M 179
Cdd:pfam01734  67 LIRKRALSLLALLRGLIGEGGLFDGDALRELLRKLLGDltLEELAARLSLLLVVALRALLTVISTALGTRARILLPddlD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 514974671  180 RRGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDI 221
Cdd:pfam01734 147 DDEDLADAVLASSALPGVFPPVRLDGELYVDGGLVDNVPVEA 188
PRK10279 PRK10279
patatin-like phospholipase RssA;
19-223 2.28e-14

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 74.36  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  19 QAQKVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPdDMEALLRSedFKRW-------YSG 91
Cdd:PRK10279   2 RKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLS-ALEDWVTS--FSYWdvlrlmdLSW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  92 QvepeYGYYFKQNRptpeFFNirfsfkdslHIKpQILPTSmvnpiqmnlvfvelfarataacsgDFNRLFVPFRCIASDV 171
Cdd:PRK10279  79 Q----RGGLLRGER----VFN---------QYR-EIMPET------------------------EIENCSRRFGAVATNL 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514974671 172 YNKKPLIMRRGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMR 223
Cdd:PRK10279 117 STGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPVSLTR 168
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 21-303 1.61e-66

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 220.93  E-value: 1.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  21 QKVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKRWYSGqvepeygyy 100
Cdd:COG1752    5 PKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDL--------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 fkqnRPTPEFFNIRFSFkdslhikpqiLPTSMVNPIQMNLVFVELFARAtaacsgDFNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:COG1752   76 ----SLPRRLLRLDLGL----------SPGGLLDGDPLRRLLERLLGDR------DFEDLPIPLAVVATDLETGREVVFD 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 181 RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREDFKPEVIigsVVAANPGKPKENDLMSQLENM--IMQ 258
Cdd:COG1752  136 SGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVI---AVDLNPPLRKLPSLLDILGRAleIMF 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514974671 259 ------KTDYTLPDslgIIMTFKYDDVSLLDFDRLQELHDIGYNRTISLMD 303
Cdd:COG1752  213 nsilrrELALEPAD---ILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 23-236 7.71e-66

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: 215.87  E-value: 7.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  23 VGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDME--ALLRSEDFKRWysgqvepeygyy 100
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEerAKLRSTDLKAL------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 FKQNRPTPEFFNIRfsfkdslhikpqilptsmvnpiqmnlVFVELFARATaaCSGDFNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:cd07205   69 SDLTIPTAGLLRGD--------------------------KFLELLDEYF--GDRDIEDLWIPFFIVATDLTSGKLVVFR 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514974671 181 RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREdFKPEVIIGSVV 236
Cdd:cd07205  121 SGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRE-LGADIIIAVDL 175
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 23-232 4.32e-36

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: 133.94  E-value: 4.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  23 VGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDME--ALLRSEDFKRwysgqvepeygyY 100
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEwvRSLSQRDVLR------------L 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 FKQNRPTPEFfnirfsfkdslhikpqilptsmvnpIQMNLVFVELFArATAACSgdFNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:cd07228   69 LDLSASRSGL-------------------------LKGEKVLEYLRE-IMGGVT--IEELPIPFAAVATDLQTGKEVWFR 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514974671 181 RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMReDFKPEVII 232
Cdd:cd07228  121 EGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVSVAR-ALGADIVI 171
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 25-221 3.93e-32

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: 123.49  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671   25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKRwysgqvepeygyyFKqN 104
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNL-------------FL-S 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  105 RPTPEFFNIRFSFKDSLHIKPQILPTSMVNPIQMNLVF--VELFARATAACSGDFNRLFVPFRCIASDVYNKKPLI---M 179
Cdd:pfam01734  67 LIRKRALSLLALLRGLIGEGGLFDGDALRELLRKLLGDltLEELAARLSLLLVVALRALLTVISTALGTRARILLPddlD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 514974671  180 RRGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDI 221
Cdd:pfam01734 147 DDEDLADAVLASSALPGVFPPVRLDGELYVDGGLVDNVPVEA 188
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 25-221 6.78e-29

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: 114.30  E-value: 6.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKrwysgqvepeygyyfkqn 104
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKETDFA------------------ 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 105 rptpeffnirfSFKDSLHIKPQILPTSMVNPIQMN-LVFVELFARATAACSGD----------FNRLFVPFRCIASDVYN 173
Cdd:cd07207   64 -----------KLLDSPVGLLFLLPSLFKEGGLYKgDALEEWLRELLKEKTGNsfatsllrdlDDDLGKDLKVVATDLTT 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514974671 174 KKPLIMRRGD-----LGDAVRASMSFPFVFKPIEIDS--VLAyDGGIYNNFPTDI 221
Cdd:cd07207  133 GALVVFSAETtpdmpVAKAVRASMSIPFVFKPVRLAKgdVYV-DGGVLDNYPVWL 186
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 23-246 2.75e-27

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: 110.51  E-value: 2.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  23 VGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSEDFKRWYSGQVEPEYGYYFK 102
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFWDPPLRGGLLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 103 QNRptpeffnirfsFKDSLhiKPQILPTSMvnpiqmnlvfvelfaratAACSGdfnrlfvPFRCIASDVYNKKPLIMRRG 182
Cdd:cd07210   81 GDR-----------FAALL--REHLPPDRF------------------EELRI-------PLAVSVVDLTSRETLLLSEG 122

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514974671 183 DLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREDFkpEVIIGSVVAANPGKPKEN 246
Cdd:cd07210  123 DLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPFDALRPEI--ERILYHHVAPRRPWERLN 184
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 23-249 9.87e-25

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: 105.56  E-value: 9.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  23 VGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLR--SEDFKRWYSGQVEPEYgyy 100
Cdd:cd07225   16 IALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRARewAKDMTSIWKKLLDLTY--- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 fkqnrPTPEFFNIRfSFKDSLHikpqilptSMVNPIQMnlvfvelfarataacsgdfNRLFVPFRCIASDVYNKKPLIMR 180
Cdd:cd07225   93 -----PITSMFSGA-AFNRSIH--------SIFGDKQI-------------------EDLWLPYFTITTDITASAMRVHT 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514974671 181 RGDLGDAVRASMSFPFVFKPI--EIDSVLAYDGGIYNNFPTDIMREDFKPEVIigsvvAANPGKPKENDLM 249
Cdd:cd07225  140 DGSLWRYVRASMSLSGYLPPLcdPKDGHLLMDGGYINNLPADVARSMGAKTVI-----AIDVGSQDETDLT 205
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 25-220 6.86e-24

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: 98.95  E-value: 6.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPDDMEALLRSedfkrwYSGQVEPEYGYYFKqn 104
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLR------LSREVRLRFDGAFP-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 105 rPTPEFFNIRFSFKDSLHIKPQILPTSmvnpiqmnlvfvelfarataacsgdfNRLFVPFRCIaSDVYNKKPLIMRRGDL 184
Cdd:cd07198   73 -PTGRLLGILRQPLLSALPDDAHEDAS--------------------------GKLFISLTRL-TDGENVLVSDTSKGEL 124

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 514974671 185 GDAVRASMSFPFVFKPIEIDS--VLAYDGGIYNNFPTD 220
Cdd:cd07198  125 WSAVRASSSIPGYFGPVPLSFrgRRYGDGGLSNNLPVA 162
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 25-295 1.57e-19

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: 87.73  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGySPDDMEALlrsEDFkrWysgqvepeygyyfkqn 104
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGG-DPEAVERL---EKL--W---------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 105 rptpeffnirfsfkDSLHIKPqilptsmvnpiqmnlVFVELFARATaacsGDFNRL------FVPFRCIASDVYNKKPLI 178
Cdd:cd07209   59 --------------RELSRED---------------VFLRGLLDRA----LDFDTLrllailFAGLVIVAVNVLTGEPVY 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 179 ---MRRGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDiMREDFKPEVIIgsVVAANPGKPkenDLMSQLENM 255
Cdd:cd07209  106 fddIPDGILPEHLLASAALPPFFPPVEIDGRYYWDGGVVDNTPLS-PAIDLGADEII--VVSLSDKGR---DDRKGTPPT 179

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 514974671 256 IMQKTDYTLPDSLGIimtfkyddvsllDFDRLQELHDIGY 295
Cdd:cd07209  180 TLIEILPRLFLRSGL------------DSERIRHNLELGY 207
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 21-245 3.50e-19

Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. 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 family includes NTE1 from fungi.


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 88.32  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  21 QKVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYspDDMEALLRSEDFkrwySGQVEPEYGYY 100
Cdd:cd07227    9 QAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREA--DLVPIFGRAKKF----AGRMASMWRFL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 FKQNRPTPEF-----FN--IRFSFKDSlHIKpqilptsmvnpiqmnlvfvelfarataacsgDFnrlFVPFRCIASDVYN 173
Cdd:cd07227   83 SDVTYPFASYttgheFNrgIWKTFGNT-HIE-------------------------------DF---WIPFYANSTNITH 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514974671 174 KKPLIMRRGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMREDFKPEVIIGSVVAANPGKPKE 245
Cdd:cd07227  128 SRMEIHSSGYAWRYIRASMSLAGLLPPLSDNGSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMD 199
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 25-218 8.87e-16

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: 78.03  E-value: 8.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNI-PIDYITGTSMGAIIGSLYAmgyspddmeallrsedfkrwySGQvePEYGYYFKQ 103
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYL---------------------SGQ--RGRALRINT 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 104 NRPT-PEFFNIRFSFKDSlhikpqilptSMVNpiqMNLVFVELFARAtaaCSGDFNRLF---VPFRCIASDVYNKKPLIM 179
Cdd:cd07208   58 KYATdPRYLGLRSLLRTG----------NLFD---LDFLYDELPDGL---DPFDFEAFAaspARFYVVATDADTGEAVYF 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 514974671 180 RRGDLGD----AVRASMSFPFVFKPIEIDSVLAYDGGIYNNFP 218
Cdd:cd07208  122 DKPDILDdlldALRASSALPGLFPPVRIDGEPYVDGGLSDSIP 164
PRK10279 PRK10279
patatin-like phospholipase RssA;
19-223 2.28e-14

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 74.36  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  19 QAQKVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMGYSPdDMEALLRSedFKRW-------YSG 91
Cdd:PRK10279   2 RKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLS-ALEDWVTS--FSYWdvlrlmdLSW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  92 QvepeYGYYFKQNRptpeFFNirfsfkdslHIKpQILPTSmvnpiqmnlvfvelfarataacsgDFNRLFVPFRCIASDV 171
Cdd:PRK10279  79 Q----RGGLLRGER----VFN---------QYR-EIMPET------------------------EIENCSRRFGAVATNL 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 514974671 172 YNKKPLIMRRGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPTDIMR 223
Cdd:PRK10279 117 STGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPVSLTR 168
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
22-213 4.32e-13

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 70.19  E-value: 4.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  22 KVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAmgyspddmeallrsedfkrwySGQvePEYGY-Y 100
Cdd:COG4667    5 KTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYL---------------------SRQ--PGRARrV 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 101 FKQNRPTPEFFNIRfSFkdslhikpqILPTSMVNpiqMNLVFVELFARATAAcsgDFNRLF---VPFRCIASD------V 171
Cdd:COG4667   62 ITDYATDPRFFSLR-NF---------LRGGNLFD---LDFLYDEIPNELLPF---DFETFKaspREFYVVATNadtgeaE 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 514974671 172 YnKKPLIMRRgDLGDAVRASMSFPFVFKPIEIDSVLAYDGGI 213
Cdd:COG4667  126 Y-FSKKDDDY-DLLDALRASSALPLLYPPVEIDGKRYLDGGV 165
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 22-88 8.11e-11

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: 64.59  E-value: 8.11e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  22 KVGLVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMgYSPDDMEALLR---SEDFKRW 88
Cdd:cd07232   67 RTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLCT-RTDEELKQLLVpelARKITAC 135
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 25-219 2.80e-09

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 59.15  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEEN-NIPI----DYITGTSMGAIIGSLYAMGYSPDDMEALlrsedfkrwysgqvepeygy 99
Cdd:COG3621   10 LSLDGGGIRGLIPARILAELEERlGKPLaeyfDLIAGTSTGGIIALGLAAGYSAEEILDL-------------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 100 yFKQNRPTPefFNIRFSFKdslhikpQILPTSMVNPI--QMNL--VFVELFARAT-AACSGdfnRLFVPfrciASDVYNK 174
Cdd:COG3621   70 -YEEEGKEI--FPKSRWRK-------LLSLRGLFGPKydSEGLekVLKEYFGDTTlGDLKT---PVLIP----SYDLDNG 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 175 KPLIM------RRGDLG----DAVRASMSFPFVFKPIEIDSVLAY-----DGGIYNNFPT 219
Cdd:COG3621  133 KPVFFksphakFDRDRDfllvDVARATSAAPTYFPPAQIKNLTGEgyaliDGGVFANNPA 192
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 25-219 9.25e-09

Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 57.65  E-value: 9.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNI-PI----DYITGTSMGAIIGSLYAM-GYSPDDMEALLRSedfkrwYSGQVepeyg 98
Cdd:cd07211   11 LSIDGGGTRGVVALEILRKIEKLTGkPIhelfDYICGVSTGAILAFLLGLkKMSLDECEELYRK------LGKDV----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  99 yyFKQNRPTpeFFNIRFSFKDSLH---IKPQILPTSMVNPIQMNlvfvelfaraTAACSGdfnrlfVPFRCIASDVYNK- 174
Cdd:cd07211   80 --FSQNTYI--SGTSRLVLSHAYYdteTWEKILKEMMGSDELID----------TSADPN------CPKVACVSTQVNRt 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514974671 175 --KPLIMR----------------RGDLGDAVRASMSFPFVFKPIEIDSVLAYDGGIYNNFPT 219
Cdd:cd07211  140 plKPYVFRnynhppgtrshylgscKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPT 202
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 25-232 4.62e-08

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: 53.19  E-value: 4.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNI--PIDYITGTSMGAIIGSLYamgyspddmeallrsedfkrwysgqvepeygyyfk 102
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL----------------------------------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671 103 qnrpTPEFFNIrfsfkdslHIKPQilptSMVNPIQMNLVFVElfarataacsgdFNRLFVPFRCIASDVynkkpliMRRG 182
Cdd:cd01819   46 ----YPPSSSL--------DNKPR----QSLEEALSGKLWVS------------FTPVTAGENVLVSRF-------VSKE 90

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514974671 183 DLGDAVRASMSFPFVFKPI------------EIDSVLAYDGGIYNNFPTDIMREDF-KPEVII 232
Cdd:cd01819   91 ELIRALFASGSWPSYFGLIppaelytsksnlKEKGVRLVDGGVSNNLPAPVLLRPGrGVTLTI 153
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 25-219 7.49e-08

Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; 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: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 54.26  E-value: 7.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEE---NNIPI----DYITGTSMGAIIG-SLYAMGYSPDDMEALLRsedfkrwysgqvepE 96
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKrlgKPSRIadlfDLIAGTSTGGIIAlGLALGRYSAEELVELYE--------------E 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  97 YGyyfkqnrptPEFFnirfsfkdslhiKPQILPTSMVNPiqmNLVFVelFARATAACSGDFNRLFvpfrciasdvynkkp 176
Cdd:cd07199   68 LG---------RKIF------------PRVLVTAYDLST---GKPVV--FSNYDAEEPDDDDDFK--------------- 106

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 514974671 177 limrrgdLGDAVRASMSFPFVFKPIEIDSV----LAYDGGIYNNFPT 219
Cdd:cd07199  107 -------LWDVARATSAAPTYFPPAVIESGgdegAFVDGGVAANNPA 146
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 25-82 1.06e-07

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: 54.92  E-value: 1.06e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMgYSPDDMEALLRS 82
Cdd:cd07230   76 LLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCT-HTDEEIPELLEE 132
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 25-66 6.33e-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: 51.83  E-value: 6.33e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSL 66
Cdd:cd07206   72 LMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAAL 113
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 25-83 2.86e-05

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: 47.30  E-value: 2.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYAMgYSPDDMEALLRSE 83
Cdd:cd07229   86 LVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAALVGV-HTDEELLRFLDGD 143
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 25-68 1.29e-04

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: 44.75  E-value: 1.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNIPIDYITGTSMGAIIGSLYA 68
Cdd:cd07231   71 LLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIA 114
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 25-108 6.18e-04

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: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 42.87  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALE-----ENNIP-------IDYITGTSMGAIIGSLYAMGYSPDDMEALLRSE-----DFKR 87
Cdd:cd07217    4 LALDGGGIRGLLSVEILGRIEkdlrtHLDDPefrlgdyFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNgvnmfDKAW 83

                         90       100
                 ....*....|....*....|.
gi 514974671  88 WYSGqvePEYGYYFKQNRPTP 108
Cdd:cd07217   84 LAQR---LFLNKLYNQYDPTN 101
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 25-75 8.71e-04

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: 41.89  E-value: 8.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 514974671  25 LVLSGGGAKGMTHIGIIRALEENNiP-----IDYITGTSMGAIIGSLYAMGYSPDD 75
Cdd:cd07213    5 LSLDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSPRQ 59
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 25-94 8.74e-04

Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 42.32  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514974671  25 LVLSGGGAKGMTHIGIIRALE-ENNIPI----DYITGTSMGAIIGSLYAMGYSPDDMEAL---LRSEDFKRW---YSGQV 93
Cdd:cd07212    2 LCLDGGGIRGLVLIQMLIAIEkALGRPIrelfDWIAGTSTGGILALALLHGKSLREARRLylrMKDRVFDGSrpyNSEPL 81


                 .
gi 514974671  94 E 94
Cdd:cd07212   82 E 82
 
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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