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Conserved domains on  [gi|1242989511|gb|PBJ59301|]
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phospholipase [Mycobacterium avium subsp. hominissuis]

Protein Classification

patatin-like phospholipase family protein( domain architecture ID 10163346)

patatin-like phospholipase family protein similar to Legionella pneumophila VipD and Pseudomonas aeruginosa type III secretion effector protein ExoU

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 12-223 2.92e-66

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: 207.13  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  12 DLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGCHAGELtgaqvKELAFSVPLHKWRDAgPVPYLG 91
Cdd:cd07207     1 NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADI-----KDILKETDFAKLLDS-PVGLLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  92 AAWGLARDTSMYRGDVAHDWIRSELKNFGVSTFGDLVFdgDDLPDERRRRLVVTVADVTAAQLVrlpwdyrRLYGLDPDE 171
Cdd:cd07207    75 LLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLL--RDLDDDLGKDLKVVATDLTTGALV-------VFSAETTPD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242989511 172 QPVADAVRASMAIPFFYRPVKLARADgtacTLVDGGVLSNFPIDTFDRPDGR 223
Cdd:cd07207   146 MPVAKAVRASMSIPFVFKPVRLAKGD----VYVDGGVLDNYPVWLFDGWELS 193
 
Name Accession Description Interval E-value
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 12-223 2.92e-66

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: 207.13  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  12 DLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGCHAGELtgaqvKELAFSVPLHKWRDAgPVPYLG 91
Cdd:cd07207     1 NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADI-----KDILKETDFAKLLDS-PVGLLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  92 AAWGLARDTSMYRGDVAHDWIRSELKNFGVSTFGDLVFdgDDLPDERRRRLVVTVADVTAAQLVrlpwdyrRLYGLDPDE 171
Cdd:cd07207    75 LLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLL--RDLDDDLGKDLKVVATDLTTGALV-------VFSAETTPD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242989511 172 QPVADAVRASMAIPFFYRPVKLARADgtacTLVDGGVLSNFPIDTFDRPDGR 223
Cdd:cd07207   146 MPVAKAVRASMSIPFVFKPVRLAKGD----VYVDGGVLDNYPVWLFDGWELS 193
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 5-322 1.30e-42

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 148.13  E-value: 1.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511   5 TEPAKPVDLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGchageLTGAQVKELAFSVPLHKWRDA 84
Cdd:COG1752     1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAG-----YSADELEELWRSLDRRDLFDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  85 GPVPYLGAAWGLARDTSMYRGDVAHDWIRselKNFGVSTFGDLvfdgddlpderRRRLVVTVADVTAAQLVRLpwdyrrl 164
Cdd:COG1752    76 SLPRRLLRLDLGLSPGGLLDGDPLRRLLE---RLLGDRDFEDL-----------PIPLAVVATDLETGREVVF------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 165 ygldpDEQPVADAVRASMAIPFFYRPVKLaraDGTActLVDGGVLSNFPIDTFDRPDGRaprwPTFGITVMPSPTEGIGA 244
Cdd:COG1752   135 -----DSGPLADAVRASAAIPGVFPPVEI---DGRL--YVDGGVVNNLPVDPARALGAD----RVIAVDLNPPLRKLPSL 200

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242989511 245 vmpalkplrflpqTALLESLLITMLAGHDQTHLSQPwVAARAIAVESTNVGVLDFDvprsRLEELYDSGYAAAQAFLS 322
Cdd:COG1752   201 -------------LDILGRALEIMFNSILRRELALE-PADILIEPDLSGISLLDFS----RAEELIEAGYEAARRALD 260
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 13-218 1.41e-24

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: 98.45  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGcHAGELTGAQVKELAFSVPLHKWRdAGPVPYLGA 92
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALG-RDPEEIEDLLLELDLNLFLSLIR-KRALSLLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  93 AWGLARDTSMYRGDVAHDWIRSELKNFGVSTFGDLVfdgddlpdeRRRRLVVTVADVTAAQLVRLPWDYRRLYGLDPDEQ 172
Cdd:pfam01734  79 LRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARL---------SLLLVVALRALLTVISTALGTRARILLPDDLDDDE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1242989511 173 PVADAVRASMAIPFFYRPVKLaradgTACTLVDGGVLSNFPIDTFD 218
Cdd:pfam01734 150 DLADAVLASSALPGVFPPVRL-----DGELYVDGGLVDNVPVEAAL 190
 
Name Accession Description Interval E-value
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 12-223 2.92e-66

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: 207.13  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  12 DLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGCHAGELtgaqvKELAFSVPLHKWRDAgPVPYLG 91
Cdd:cd07207     1 NLVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADI-----KDILKETDFAKLLDS-PVGLLF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  92 AAWGLARDTSMYRGDVAHDWIRSELKNFGVSTFGDLVFdgDDLPDERRRRLVVTVADVTAAQLVrlpwdyrRLYGLDPDE 171
Cdd:cd07207    75 LLPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATSLL--RDLDDDLGKDLKVVATDLTTGALV-------VFSAETTPD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242989511 172 QPVADAVRASMAIPFFYRPVKLARADgtacTLVDGGVLSNFPIDTFDRPDGR 223
Cdd:cd07207   146 MPVAKAVRASMSIPFVFKPVRLAKGD----VYVDGGVLDNYPVWLFDGWELS 193
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 5-322 1.30e-42

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 148.13  E-value: 1.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511   5 TEPAKPVDLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGchageLTGAQVKELAFSVPLHKWRDA 84
Cdd:COG1752     1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAG-----YSADELEELWRSLDRRDLFDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  85 GPVPYLGAAWGLARDTSMYRGDVAHDWIRselKNFGVSTFGDLvfdgddlpderRRRLVVTVADVTAAQLVRLpwdyrrl 164
Cdd:COG1752    76 SLPRRLLRLDLGLSPGGLLDGDPLRRLLE---RLLGDRDFEDL-----------PIPLAVVATDLETGREVVF------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 165 ygldpDEQPVADAVRASMAIPFFYRPVKLaraDGTActLVDGGVLSNFPIDTFDRPDGRaprwPTFGITVMPSPTEGIGA 244
Cdd:COG1752   135 -----DSGPLADAVRASAAIPGVFPPVEI---DGRL--YVDGGVVNNLPVDPARALGAD----RVIAVDLNPPLRKLPSL 200

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242989511 245 vmpalkplrflpqTALLESLLITMLAGHDQTHLSQPwVAARAIAVESTNVGVLDFDvprsRLEELYDSGYAAAQAFLS 322
Cdd:COG1752   201 -------------LDILGRALEIMFNSILRRELALE-PADILIEPDLSGISLLDFS----RAEELIEAGYEAARRALD 260
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 13-218 1.41e-24

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: 98.45  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGcHAGELTGAQVKELAFSVPLHKWRdAGPVPYLGA 92
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALG-RDPEEIEDLLLELDLNLFLSLIR-KRALSLLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  93 AWGLARDTSMYRGDVAHDWIRSELKNFGVSTFGDLVfdgddlpdeRRRRLVVTVADVTAAQLVRLPWDYRRLYGLDPDEQ 172
Cdd:pfam01734  79 LRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARL---------SLLLVVALRALLTVISTALGTRARILLPDDLDDDE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1242989511 173 PVADAVRASMAIPFFYRPVKLaradgTACTLVDGGVLSNFPIDTFD 218
Cdd:pfam01734 150 DLADAVLASSALPGVFPPVRL-----DGELYVDGGLVDNVPVEAAL 190
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 13-216 5.63e-22

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: 91.07  E-value: 5.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGCHAGELtgaqvkeLAFSVPLHKwrdaGPVPYLGA 92
Cdd:cd07205     3 LALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEI-------EERAKLRST----DLKALSDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  93 AWGLardTSMYRGDVahdwirseLKNFGVSTFGDLVFdgDDLPderrRRLVVTVADVTAAQLVRLpwdyrrlygldpDEQ 172
Cdd:cd07205    72 TIPT---AGLLRGDK--------FLELLDEYFGDRDI--EDLW----IPFFIVATDLTSGKLVVF------------RSG 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1242989511 173 PVADAVRASMAIPFFYRPVKLaraDGtaCTLVDGGVLSNFPIDT 216
Cdd:cd07205   123 SLVRAVRASMSIPGIFPPVKI---DG--QLLVDGGVLNNLPVDV 161
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 11-223 3.74e-19

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: 84.70  E-value: 3.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  11 VDLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGchageLTGAQVKELAFSVPL-HKWRDAGPVPY 89
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASG-----ISPDEMAELLLSLERkDFWMFWDPPLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  90 LGAAwglardtsmyRGDVAHDWIRselKNFGVSTFGDLvfdgddlpderRRRLVVTVADVTAAQLVRLpwdyrrlygldp 169
Cdd:cd07210    76 GGLL----------SGDRFAALLR---EHLPPDRFEEL-----------RIPLAVSVVDLTSRETLLL------------ 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242989511 170 DEQPVADAVRASMAIPFFYRPVKLaraDGTacTLVDGGVLSNFPIDTFDRPDGR 223
Cdd:cd07210   120 SEGDLAEAVAASCAVPPLFQPVEI---GGR--PFVDGGVADRLPFDALRPEIER 168
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 13-215 2.99e-18

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: 81.95  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKfiGL--VGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGCHAGeltgaqVKELAfsvplHKWRDagpvpyl 90
Cdd:cd07209     1 LVLSGGGAL--GAyqAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPEA------VERLE-----KLWRE------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  91 gaawgLARDTSMYRGDVahDWIrselknfgvstfgdLVFDGDDLPDERRRRLVVTVADVTAAQLVRlpwdyrrlYGLDPD 170
Cdd:cd07209    61 -----LSREDVFLRGLL--DRA--------------LDFDTLRLLAILFAGLVIVAVNVLTGEPVY--------FDDIPD 111

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1242989511 171 EQPVaDAVRASMAIPFFYRPVKLaraDGTacTLVDGGVLSNFPID 215
Cdd:cd07209   112 GILP-EHLLASAALPPFFPPVEI---DGR--YYWDGGVVDNTPLS 150
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 13-215 2.41e-16

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: 75.46  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGcHAGELTGAQVKELAFsvplhKWRDAGPVPYLGA 92
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASG-RDLEEALLLLLRLSR-----EVRLRFDGAFPPT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  93 AWGLARDTSMYRGDVAHDWIRSELKNFGVStfgdlvfdgddlpderrrrlvvtvadvtaaqLVRLPWDYRRLYGLDPDEQ 172
Cdd:cd07198    75 GRLLGILRQPLLSALPDDAHEDASGKLFIS-------------------------------LTRLTDGENVLVSDTSKGE 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1242989511 173 pVADAVRASMAIPFFYRPVKLArADGTACtlVDGGVLSNFPID 215
Cdd:cd07198   124 -LWSAVRASSSIPGYFGPVPLS-FRGRRY--GDGGLSNNLPVA 162
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 13-317 3.27e-14

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: 71.49  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYS-IKRVSGVSAGSVVAAILAAGchageltgaQVKELAFSVPLHKWRDAgpvpYLG 91
Cdd:cd07208     1 LVLEGGGMRGAYTAGVLDAFLEAGIRpFDLVIGVSAGALNAASYLSG---------QRGRALRINTKYATDPR----YLG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  92 AAwGLARDTSMYrgDVahDWIrselknFGVSTFGDLVFDgDDLPDERRRRLVVTVADVTAAQLVrlpwdyrrLYGLDPDE 171
Cdd:cd07208    68 LR-SLLRTGNLF--DL--DFL------YDELPDGLDPFD-FEAFAASPARFYVVATDADTGEAV--------YFDKPDIL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 172 QPVADAVRASMAIPFFYRPVKLaraDGTacTLVDGGVLSNFPID--------------TFDRPDGRAPRWptfgitvmps 237
Cdd:cd07208   128 DDLLDALRASSALPGLFPPVRI---DGE--PYVDGGLSDSIPVDkaiedgadkivvilTRPRGYRKKPSK---------- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 238 ptegigavMPALKPLRFLPQTALLESLL---ITMLAGHDQTHLSQPWVAARAIA-VESTNVGVLDFDvpRSRLEELYDSG 313
Cdd:cd07208   193 --------SSPLAKLLYRKYPNLVEALLrrhSRYNETLEFIRRLEAEGKIFVIApEKPLKVSRLERD--PEKLEALYDLG 262


                  ....
gi 1242989511 314 YAAA 317
Cdd:cd07208   263 YEDA 266
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
13-324 1.16e-13

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 70.19  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGchageltgaQvKELAFSV---PLHKWRDAGPVPY 89
Cdd:COG4667     8 LVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYLSR---------Q-PGRARRVitdYATDPRFFSLRNF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  90 L--GAAWGLardtsmyrgdvahDWIRSELKNFgvstfgDLVFDGDDLpDERRRRLVVTVADVTAAQLVrlpwdYRRLYGL 167
Cdd:COG4667    78 LrgGNLFDL-------------DFLYDEIPNE------LLPFDFETF-KASPREFYVVATNADTGEAE-----YFSKKDD 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 168 DPDEQpvaDAVRASMAIPFFYRPVKLaraDGtaCTLVDGGVLSNFPI--------DTFD----RPDG--RAPRWptfgit 233
Cdd:COG4667   133 DYDLL---DALRASSALPLLYPPVEI---DG--KRYLDGGVADSIPVreairdgaDKIVviltRPRGyrKKPSK------ 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 234 vmpsptegigavMPALKPLRFLPQTALLESLLiTMLAGHDQT--HLSQP--WVAARAIAVEST-NVGVLDFDVPrsRLEE 308
Cdd:COG4667   199 ------------FKRLLRRLYRKYPKLVEALL-NRHERYNETleFIEQLekEGKIFVIRPPKPlTVSRLERDPE--KLRA 263

                         330
                  ....*....|....*.
gi 1242989511 309 LYDSGYAAAQAFLSTW 324
Cdd:COG4667   264 LYELGYEDARKFLAEL 279
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 11-215 1.33e-09

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: 56.51  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  11 VDLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGChageltgaQVKELAFSVPLhKWRDAgpVPYL 90
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGH--------LDALEEWVRSL-SQRDV--LRLL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  91 GAAWGLArdtsmyrGDVAHDWIRSELKNFgvstFGDLVFDgdDLPderrRRLVVTVADVTAAQLVRLpwdyrrlygldpD 170
Cdd:cd07228    70 DLSASRS-------GLLKGEKVLEYLREI----MGGVTIE--ELP----IPFAAVATDLQTGKEVWF------------R 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1242989511 171 EQPVADAVRASMAIPFFYRPVKLaraDGTacTLVDGGVLSNFPID 215
Cdd:cd07228   121 EGSLIDAIRASISIPGIFAPVEH---NGR--LLVDGGVVNPIPVS 160
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 140-214 1.45e-06

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: 48.87  E-value: 1.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242989511 140 RRLVVTVADVTAAQLVRLPWDYRRLYGLDPDeQPVADAVRASMAIPFFYRPVKLaRADGTACTLVDGGVLSNFPI 214
Cdd:cd07199    74 PRVLVTAYDLSTGKPVVFSNYDAEEPDDDDD-FKLWDVARATSAAPTYFPPAVI-ESGGDEGAFVDGGVAANNPA 146
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 13-193 2.68e-06

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: 48.80  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAagCHAG-ELTGAQVKELAfsvplHKWRDAGPvPYLG 91
Cdd:cd07232    70 LCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLC--TRTDeELKQLLVPELA-----RKITACEP-PWLV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  92 AAWGLARDTSMYrgDVAhDWIRSELKnfgvSTFGDLVFdgddlpDE--RR--RRLVVTV--ADVTAAQLVrlpwdyrrly 165
Cdd:cd07232   142 WIPRWLKTGARF--DSV-EWARTCCW----FTRGSMTF------EEayERtgRILNISVvpADPHSPTIL---------- 198

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1242989511 166 gLDPDEQP---VADAVRASMAIPFFYRPVKL 193
Cdd:cd07232   199 -LNYLTSPnctIWSAVLASAAVPGILNPVVL 228
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 13-216 9.26e-05

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: 43.54  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAAGCHAGELTgAQVKELAFSvplhkwrdagpvpyLGA 92
Cdd:cd07225    18 LVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMK-QRAREWAKD--------------MTS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  93 AWGLARD-----TSMYRGDVAHDWIRselknfgvSTFGDLVFDGDDLPderrrRLVVTvADVTAAQLvRLP-----WDYr 162
Cdd:cd07225    83 IWKKLLDltypiTSMFSGAAFNRSIH--------SIFGDKQIEDLWLP-----YFTIT-TDITASAM-RVHtdgslWRY- 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242989511 163 rlygldpdeqpvadaVRASMAIPfFYRPVKLARADGTacTLVDGGVLSNFPIDT 216
Cdd:cd07225   147 ---------------VRASMSLS-GYLPPLCDPKDGH--LLMDGGYINNLPADV 182
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 13-57 4.35e-04

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: 41.82  E-value: 4.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILAA 57
Cdd:cd07230    76 LLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCT 120
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 42-208 3.98e-03

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: 38.63  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511  42 VSGVSAGSVVAAILAAGCHAGEL------TGAQVKELAF-SVPLHKWRDAGPVPYLGAawGLARDTSmyrgdvahdwirs 114
Cdd:cd07217    45 VGGTSTGSIIAACIALGMSVTDLlsfytlNGVNMFDKAWlAQRLFLNKLYNQYDPTNL--GKKLNTV------------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 115 elknFGVSTFGDlvfdgddlpDERRRRLVVTVADVTAAQlvrlPW--------DYRRLYGLDPDEQ-PVADAVRASMAIP 185
Cdd:cd07217   110 ----FPETTLGD---------DTLRTLLMIVTRNATTGS----PWpvcnnpeaKYNDSDRSDCNLDlPLWQLVRASTAAP 172

                         170       180
                  ....*....|....*....|...
gi 1242989511 186 FFYRPVKLARADGTACTLVDGGV 208
Cdd:cd07217   173 TFFPPEVVSIAPGTAFVFVDGGV 195
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 130-276 5.16e-03

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: 132855 [Multi-domain]  Cd Length: 309  Bit Score: 38.05  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242989511 130 DGDDLPDERRRRLVVTVADVTAAQLVRL--PWDYRRLYGLDPDeQPVADAVRASMAIPFFYRPVKLARADGtacTLVDGG 207
Cdd:cd07216   121 DLLDEGEEDGCKVFVCATDKDVTGKAVRlrSYPSKDEPSLYKN-ATIWEAARATSAAPTFFDPVKIGPGGR---TFVDGG 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242989511 208 VLSNFPIDTFDRPDGRAPRWPTFGITVMPSptegIGAVMPALKPLRFLPQTALLESLLITMLAGHDQTH 276
Cdd:cd07216   197 LGANNPIREVWSEAVSLWEGLARLVGCLVS----IGTGTPSIKSLGRSAEGAGLLKGLKDLVTDTEAEA 261
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 9-56 5.95e-03

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: 37.86  E-value: 5.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1242989511   9 KPVDLVLSGGGVKFIGLVGAIVALMDAGYSIKRVSGVSAGSVVAAILA 56
Cdd:cd07227     9 QAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYA 56
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 13-56 7.97e-03

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: 36.62  E-value: 7.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1242989511  13 LVLSGGGVKFIGLVGAIVALMDAG--YSIKRVSGVSAGSVVAAILA 56
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGllDCVTYLAGTSGGAWVAATLY 46
 
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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