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Conserved domains on  [gi|1711022821|gb|TVR75689|]
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MAG: hypothetical protein EA408_00020, partial [Marinilabiliales bacterium]

Protein Classification

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

patatin-like phospholipase family protein may catalyze the hydrolysis of lipids/phospholipids

CATH:  3.40.1090.10
EC:  3.1.1.-
Gene Ontology:  GO:0052689
PubMed:  11080672
SCOP:  3001121

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 ...
 40-330 2.41e-76

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 240.96  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  40 PIERPTVAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIVRSDEFIAAARGRIEDK 119
Cdd:COG1752     1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 120 YglyylqprpdpAWLRINVSREHLLDFQGVIQsniptnivspflmdfLFMEYLGpaaaaaNYSFDNLLVPFRCIAANIED 199
Cdd:COG1752    81 L-----------LRLDLGLSPGGLLDGDPLRR---------------LLERLLG------DRDFEDLPIPLAVVATDLET 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 200 NRGEVMRYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVhMEFVPDIVIGSVVSGNPEK-PSPHDIVSQ- 277
Cdd:COG1752   129 GREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPA-RALGADRVIAVDLNPPLRKlPSLLDILGRa 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1711022821 278 LQTMLMAYTRYDIGTER-GFMVRPDVPDLNVTDFSQSERVYQIGYEAAIARISE 330
Cdd:COG1752   208 LEIMFNSILRRELALEPaDILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 40-330 2.41e-76

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 240.96  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  40 PIERPTVAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIVRSDEFIAAARGRIEDK 119
Cdd:COG1752     1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 120 YglyylqprpdpAWLRINVSREHLLDFQGVIQsniptnivspflmdfLFMEYLGpaaaaaNYSFDNLLVPFRCIAANIED 199
Cdd:COG1752    81 L-----------LRLDLGLSPGGLLDGDPLRR---------------LLERLLG------DRDFEDLPIPLAVVATDLET 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 200 NRGEVMRYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVhMEFVPDIVIGSVVSGNPEK-PSPHDIVSQ- 277
Cdd:COG1752   129 GREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPA-RALGADRVIAVDLNPPLRKlPSLLDILGRa 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1711022821 278 LQTMLMAYTRYDIGTER-GFMVRPDVPDLNVTDFSQSERVYQIGYEAAIARISE 330
Cdd:COG1752   208 LEIMFNSILRRELALEPaDILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 46-262 2.66e-60

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: 196.23  E-value: 2.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIVRSDEFIAAARGRIEdkyglyyl 125
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDLT-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qpRPDPAWLRINVSREHLLDFQGVIqsniptnivspflmdflfmeylgpaaaaanySFDNLLVPFRCIAANIEDNRGEVM 205
Cdd:cd07205    73 --IPTAGLLRGDKFLELLDEYFGDR-------------------------------DIEDLWIPFFIVATDLTSGKLVVF 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVHmEFVPDIVIGSVV 262
Cdd:cd07205   120 RSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLR-ELGADIIIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 48-248 3.37e-36

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: 133.12  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  48 VVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMmeivrSDEFIAAARGRIEDkyglyylqp 127
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEI-----EDLLLELDLNLFLS--------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 128 RPDPAWLRINVSREHLLDFQGVIQSNIPTNIVSPFLMDFLFMEYLGPAAAAANYSFDNLLVPFRCIAAN--IEDNRGEVM 205
Cdd:pfam01734  67 LIRKRALSLLALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTraRILLPDDLD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVV 248
Cdd:pfam01734 147 DDEDLADAVLASSALPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
46-248 5.24e-13

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 69.74  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAeMMEIVRSDEFiaaargriedkyglyyl 125
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSA-LEDWVTSFSY----------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qprpdpaWlriNVSRehLLDFQ----GVIQSNIPTNIVSPFLmdflfmeylgpaaaaANYSFDNLLVPFRCIAANIEDNR 201
Cdd:PRK10279   68 -------W---DVLR--LMDLSwqrgGLLRGERVFNQYREIM---------------PETEIENCSRRFGAVATNLSTGR 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1711022821 202 GEVMRYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFP--------ADVV 248
Cdd:PRK10279  121 ELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPvsltralgADIV 175
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 40-330 2.41e-76

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 240.96  E-value: 2.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  40 PIERPTVAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIVRSDEFIAAARGRIEDK 119
Cdd:COG1752     1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 120 YglyylqprpdpAWLRINVSREHLLDFQGVIQsniptnivspflmdfLFMEYLGpaaaaaNYSFDNLLVPFRCIAANIED 199
Cdd:COG1752    81 L-----------LRLDLGLSPGGLLDGDPLRR---------------LLERLLG------DRDFEDLPIPLAVVATDLET 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 200 NRGEVMRYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVhMEFVPDIVIGSVVSGNPEK-PSPHDIVSQ- 277
Cdd:COG1752   129 GREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPA-RALGADRVIAVDLNPPLRKlPSLLDILGRa 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1711022821 278 LQTMLMAYTRYDIGTER-GFMVRPDVPDLNVTDFSQSERVYQIGYEAAIARISE 330
Cdd:COG1752   208 LEIMFNSILRRELALEPaDILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 46-262 2.66e-60

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: 196.23  E-value: 2.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIVRSDEFIAAARGRIEdkyglyyl 125
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDLT-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qpRPDPAWLRINVSREHLLDFQGVIqsniptnivspflmdflfmeylgpaaaaanySFDNLLVPFRCIAANIEDNRGEVM 205
Cdd:cd07205    73 --IPTAGLLRGDKFLELLDEYFGDR-------------------------------DIEDLWIPFFIVATDLTSGKLVVF 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVHmEFVPDIVIGSVV 262
Cdd:cd07205   120 RSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLR-ELGADIIIAVDL 175
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 46-258 1.22e-42

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: 149.73  E-value: 1.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMmeivrsdEFIAAARGRieDKYGLYyl 125
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALE-------EWVRSLSQR--DVLRLL-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qprpDPAWLRinvsrehlldfQGVIQSNIptnivspfLMDFLFmEYLGPAaaaanySFDNLLVPFRCIAANIEDNRGEVM 205
Cdd:cd07228    70 ----DLSASR-----------SGLLKGEK--------VLEYLR-EIMGGV------TIEELPIPFAAVATDLQTGKEVWF 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVHMeFVPDIVI 258
Cdd:cd07228   120 REGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVSVARA-LGADIVI 171
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 48-248 3.37e-36

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: 133.12  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  48 VVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMmeivrSDEFIAAARGRIEDkyglyylqp 127
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEI-----EDLLLELDLNLFLS--------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 128 RPDPAWLRINVSREHLLDFQGVIQSNIPTNIVSPFLMDFLFMEYLGPAAAAANYSFDNLLVPFRCIAAN--IEDNRGEVM 205
Cdd:pfam01734  67 LIRKRALSLLALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTraRILLPDDLD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVV 248
Cdd:pfam01734 147 DDEDLADAVLASSALPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 48-247 8.31e-31

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: 118.15  E-value: 8.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  48 VVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIvrSDEFiaaargriedkyglyylqp 127
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDI--LKET------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 128 rpdpawlrinvSREHLLDFQGVIQSNIPTNIVSPFLMDFLFME-YLGPAAAAANYS----------FDNLLVPFRCIAAN 196
Cdd:cd07207    61 -----------DFAKLLDSPVGLLFLLPSLFKEGGLYKGDALEeWLRELLKEKTGNsfatsllrdlDDDLGKDLKVVATD 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1711022821 197 IEDNRGEVmRYG------SLADAVRASMTFPFYFKPITID-GRLMMDGGMFNNFPADV 247
Cdd:cd07207   130 LTTGALVV-FSAettpdmPVAKAVRASMSIPFVFKPVRLAkGDVYVDGGVLDNYPVWL 186
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 45-322 2.12e-30

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: 120.58  E-value: 2.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  45 TVAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEivrsdefiaAARGRIEDKYGLyy 124
Cdd:cd07225    15 SIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQ---------RAREWAKDMTSI-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 125 lqprpdpaWLRInvsrehlLDFQGVIQS-----NIPTNIVSPFlmdflfmeylgpaaaaANYSFDNLLVPFRCIAANIED 199
Cdd:cd07225    84 --------WKKL-------LDLTYPITSmfsgaAFNRSIHSIF----------------GDKQIEDLWLPYFTITTDITA 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 200 NRGEVMRYGSLADAVRASMTFPFYFKPIT--IDGRLMMDGGMFNNFPADVVHMEFVPDIV---IGSV-----------VS 263
Cdd:cd07225   133 SAMRVHTDGSLWRYVRASMSLSGYLPPLCdpKDGHLLMDGGYINNLPADVARSMGAKTVIaidVGSQdetdltnygdaLS 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 264 G--------NP--EK---PSPHDIVSQLqtmlmAYtrydIGTERG----------FMVRPDVPDLNVTDFSQSERVYQIG 320
Cdd:cd07225   213 GwwllwkrwNPlaEKvkvPNMAEIQSRL-----AY----VSCVRQleevkssdycEYLRPPIDKYKTLDFGKFDEICEVG 283


                  ..
gi 1711022821 321 YE 322
Cdd:cd07225   284 YQ 285
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 46-266 3.25e-29

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: 114.75  E-value: 3.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEIVRSDEFIAAARgriedkyglyyl 125
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELLLSLERKDFWM------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qpRPDPAWlrinvsREHLLDFQGVIQsniptnivspflmdfLFMEYLGPAaaaanySFDNLLVPFRCIAANIEDNRGEVM 205
Cdd:cd07210    69 --FWDPPL------RGGLLSGDRFAA---------------LLREHLPPD------RFEELRIPLAVSVVDLTSRETLLL 119

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVHMEFVPdIVIGSVVSGNP 266
Cdd:cd07210   120 SEGDLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPFDALRPEIER-ILYHHVAPRRP 179
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 49-247 2.14e-27

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: 108.20  E-value: 2.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  49 VLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMmeIVRSDEFIAAARgriedkyglyylqPR 128
Cdd:cd07198     2 VLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEA--LLLLLRLSREVR-------------LR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 129 PDPAWLRinVSREHLLDFQGVIQSNIPTNIVSpflmdflfmeylgpaaaaanysfdnLLVPFRCIAANIEDnrGEVMRY- 207
Cdd:cd07198    67 FDGAFPP--TGRLLGILRQPLLSALPDDAHED-------------------------ASGKLFISLTRLTD--GENVLVs 117

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1711022821 208 ----GSLADAVRASMTFPFYFKPI--TIDGRLMMDGGMFNNFPADV 247
Cdd:cd07198   118 dtskGELWSAVRASSSIPGYFGPVplSFRGRRYGDGGLSNNLPVAE 163
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 46-305 6.82e-26

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: 106.81  E-value: 6.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAEMMEivRSDEFIaaarGRIEDKYGLYYl 125
Cdd:cd07227    11 IGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFG--RAKKFA----GRMASMWRFLS- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qprpDPAWLRINVSREHLLDfQGVIQSNIPTNIvspflmdflfmeylgpaaaaanysfDNLLVPFRCIAANIEDNRGEVM 205
Cdd:cd07227    84 ----DVTYPFASYTTGHEFN-RGIWKTFGNTHI-------------------------EDFWIPFYANSTNITHSRMEIH 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 206 RYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPadVVHMEFVPDIVIGSVVSGNPEKPSPHDIVSQLQTMLMAY 285
Cdd:cd07227   134 SSGYAWRYIRASMSLAGLLPPLSDNGSMLLDGGYMDNLP--VSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFF 211

                         250       260
                  ....*....|....*....|
gi 1711022821 286 TRYDigterGFMVRPDVPDL 305
Cdd:cd07227   212 NRWN-----PFSSRPNVPSM 226
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 48-329 5.97e-21

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: 91.20  E-value: 5.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  48 VVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGysPAEMMEivrsdefiaaargRIEDkyglyylqp 127
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGG--DPEAVE-------------RLEK--------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 128 rpdpAWLRInvSREHLLdFQGVIQSNIPTNIVSPFLMDFLFMEYlgpaaaaanYSFDNLLVPFRCIaaniednrgEVMRY 207
Cdd:cd07209    57 ----LWREL--SREDVF-LRGLLDRALDFDTLRLLAILFAGLVI---------VAVNVLTGEPVYF---------DDIPD 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 208 GSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVhMEFVPDIVIgsVVSGNPekPSPHDIVSQLQTMLmaytr 287
Cdd:cd07209   112 GILPEHLLASAALPPFFPPVEIDGRYYWDGGVVDNTPLSPA-IDLGADEII--VVSLSD--KGRDDRKGTPPTTL----- 181

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1711022821 288 ydigtergFMVRPDVPDLNVTDFSQSERVYQIGYEAAIARIS 329
Cdd:cd07209   182 --------IEILPRLFLRSGLDSERIRHNLELGYLDTLRADS 215
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 49-324 5.98e-18

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: 83.81  E-value: 5.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  49 VLSGGGAKGIAHIGVLQALEENGI-PVDYIAGTSIGAIVGGLYAAGyspaemmeivrsdefiaaargriEDKYGL-YYLQ 126
Cdd:cd07208     2 VLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYLSG-----------------------QRGRALrINTK 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 127 PRPDPAWLRIN--VSREHLLDFQGVIqsNIPTNIVSPFLMDflfmeylgpaaaaanySFDNLLVPFRCIAANIEDNRGEV 204
Cdd:cd07208    59 YATDPRYLGLRslLRTGNLFDLDFLY--DELPDGLDPFDFE----------------AFAASPARFYVVATDADTGEAVY 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 205 MRYGS----LADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADV-VHMEFVPDIVIGSVVSGNPEKPSPHDIVSQL- 278
Cdd:cd07208   121 FDKPDilddLLDALRASSALPGLFPPVRIDGEPYVDGGLSDSIPVDKaIEDGADKIVVILTRPRGYRKKPSKSSPLAKLl 200

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1711022821 279 --------QTMLMAYTRYDIG------TERG---FMVRPDVPdLNV----TDFSQSERVYQIGYEAA 324
Cdd:cd07208   201 yrkypnlvEALLRRHSRYNETlefirrLEAEgkiFVIAPEKP-LKVsrleRDPEKLEALYDLGYEDA 266
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
46-330 3.65e-16

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 78.67  E-value: 3.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAivggLYAAGYspaemmeivrsdefIAAARGRIEDkyglYYL 125
Cdd:COG4667     6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGA----LNGASY--------------LSRQPGRARR----VIT 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 QPRPDPAWLRIN--VSREHLLDFQGVIQSnIPTNIVsPFlmDFlfmeylgpAAAAANysfdnlLVPFRCIAANIEDNRGE 203
Cdd:COG4667    64 DYATDPRFFSLRnfLRGGNLFDLDFLYDE-IPNELL-PF--DF--------ETFKAS------PREFYVVATNADTGEAE 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 204 VMR----YGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFP--------ADVVhmefvpdIVIGSVVSGNPEKPSP 271
Cdd:COG4667   126 YFSkkddDYDLLDALRASSALPLLYPPVEIDGKRYLDGGVADSIPvreairdgADKI-------VVILTRPRGYRKKPSK 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 272 HDIVSQL---------QTMLMAYTRYDIgtERGFM-----------VRPDVPdLNV----TDFSQSERVYQIGYEAAIAR 327
Cdd:COG4667   199 FKRLLRRlyrkypklvEALLNRHERYNE--TLEFIeqlekegkifvIRPPKP-LTVsrleRDPEKLRALYELGYEDARKF 275


                  ...
gi 1711022821 328 ISE 330
Cdd:COG4667   276 LAE 278
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 50-273 1.18e-14

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 74.56  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  50 LSGGGAKGIAHIGVLQALEEN-GIP----VDYIAGTSIGAIVGGLYAAGYSPAEMMEI----------VRSDEFIAAARG 114
Cdd:COG3621    12 LDGGGIRGLIPARILAELEERlGKPlaeyFDLIAGTSTGGIIALGLAAGYSAEEILDLyeeegkeifpKSRWRKLLSLRG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 115 RIEDKYGLYYLqprpdpawlrinvsREHLLDFQGVIQ-SNIPTNIVSPflmdflfmeylgpaaaaanySFD---NLLVPF 190
Cdd:COG3621    92 LFGPKYDSEGL--------------EKVLKEYFGDTTlGDLKTPVLIP--------------------SYDldnGKPVFF 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 191 RCIAANIEDNRGEvmrygSLADAVRASMTFPFYFKPITID-----GRLMMDGGMFNNFPA-----DVVHMEFVP--DIVI 258
Cdd:COG3621   138 KSPHAKFDRDRDF-----LLVDVARATSAAPTYFPPAQIKnltgeGYALIDGGVFANNPAlcalaEALKLLGPDldDILV 212

                         250
                  ....*....|....*
gi 1711022821 259 GSVVSGNPEKPSPHD 273
Cdd:COG3621   213 LSLGTGTAPRSIPYK 227
PRK10279 PRK10279
patatin-like phospholipase RssA;
46-248 5.24e-13

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 69.74  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  46 VAVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYAAGYSPAeMMEIVRSDEFiaaargriedkyglyyl 125
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSA-LEDWVTSFSY----------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 126 qprpdpaWlriNVSRehLLDFQ----GVIQSNIPTNIVSPFLmdflfmeylgpaaaaANYSFDNLLVPFRCIAANIEDNR 201
Cdd:PRK10279   68 -------W---DVLR--LMDLSwqrgGLLRGERVFNQYREIM---------------PETEIENCSRRFGAVATNLSTGR 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1711022821 202 GEVMRYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFP--------ADVV 248
Cdd:PRK10279  121 ELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPvsltralgADIV 175
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 50-290 1.93e-10

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: 61.58  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  50 LSGGGAKGIAHIGVLQALEE---NGIPV----DYIAGTSIGAIVGGLYAAG-YSPAEMMEIVRsdefiaaARGRiedkyg 121
Cdd:cd07199     4 LDGGGIRGIIPAEILAELEKrlgKPSRIadlfDLIAGTSTGGIIALGLALGrYSAEELVELYE-------ELGR------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 122 lyylqprpdpawlRInvsrehlldFQGVI--QSNIPTNIVspflmdFLFmeylgpaaaaANYSFDNLLVPFRCiaanied 199
Cdd:cd07199    71 -------------KI---------FPRVLvtAYDLSTGKP------VVF----------SNYDAEEPDDDDDF------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 200 nrgevmrygSLADAVRASMTFPFYFKPITI----DGRLMMDGGMFNNFPA-----DVVHMEFVP--DIVIGSVVSGNPEK 268
Cdd:cd07199   106 ---------KLWDVARATSAAPTYFPPAVIesggDEGAFVDGGVAANNPAllalaEALRLLAPDkdDILVLSLGTGTSPS 176

                         250       260
                  ....*....|....*....|..
gi 1711022821 269 PSPHDIVSQLQTMLMAYTRYDI 290
Cdd:cd07199   177 SSSSKKASRWGGLGWGRPLLDI 198
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 48-91 3.01e-09

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: 55.88  E-value: 3.01e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1711022821  48 VVLSGGGAKGIAHIGVLQALEENGI--PVDYIAGTSIGAIVGGLYA 91
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATLY 46
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 47-105 1.97e-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: 53.38  E-value: 1.97e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  47 AVVLSGGGAKGIAHIGVLQAL-EENGIPvDYIAGTSIGAIVGGLYAAgYSPAEMMEIVRS 105
Cdd:cd07230    75 ALLLSGGGTFGMFHIGVLKALfEANLLP-RIISGSSAGSIVAAILCT-HTDEEIPELLEE 132
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 47-104 2.38e-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: 49.96  E-value: 2.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1711022821  47 AVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLyAAGYSPAEMMEIVR 104
Cdd:cd07232    69 ALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAAL-LCTRTDEELKQLLV 125
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 47-89 2.50e-06

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: 49.13  E-value: 2.50e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1711022821  47 AVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGL 89
Cdd:cd07206    71 ALMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAAL 113
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 49-282 3.64e-06

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: 48.79  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  49 VLS--GGGAKGIAHIGVLQALEEN-GIPV----DYIAGTSIGAIVG-GLYAAGYSPAEMMEI---------VRSDEFIAA 111
Cdd:cd07211    10 ILSidGGGTRGVVALEILRKIEKLtGKPIhelfDYICGVSTGAILAfLLGLKKMSLDECEELyrklgkdvfSQNTYISGT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 112 ARGRIedkYGLYYlqprPDPAW---LRINVSREHLLDFQGViqSNIP-----TNIVS-PFLMDFLFMEYLGPAAAAANYs 182
Cdd:cd07211    90 SRLVL---SHAYY----DTETWekiLKEMMGSDELIDTSAD--PNCPkvacvSTQVNrTPLKPYVFRNYNHPPGTRSHY- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821 183 fdnllvPFRCiaaniednrgevmrYGSLADAVRASMTFPFYFKPITIDGRLMMDGGMFNNFPADVVHME---FVPDIVIG 259
Cdd:cd07211   160 ------LGSC--------------KHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEaklLWPDTPIQ 219

                         250       260
                  ....*....|....*....|....
gi 1711022821 260 SVVS-GNPEKPSPHDIVSQLQTML 282
Cdd:cd07211   220 CLVSvGTGRYPSSVRLETGGYTSL 243
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 50-124 2.88e-05

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: 46.13  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711022821  50 LSGGGAKGIAHIGVLQALEENGiP-----VDYIAGTSIGAIVGGLYAAGYSP---AEMMEIVRSDEFIAAARGRIEDKYG 121
Cdd:cd07213     7 LDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSPrqvLKLYEEVGLKVFSKSSAGGGAGNNQ 85


                  ...
gi 1711022821 122 LYY 124
Cdd:cd07213    86 YFA 88
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 47-91 4.37e-05

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: 45.52  E-value: 4.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1711022821  47 AVVLSGGGAKGIAHIGVLQALEENGIPVDYIAGTSIGAIVGGLYA 91
Cdd:cd07231    70 ALLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIA 114
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 51-103 1.51e-03

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


Pssm-ID: 132863  Cd Length: 233  Bit Score: 40.40  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1711022821  51 SGGGAKGIAHIGVLQALEENGIPVDY--IAGTSIGAIVGGLYAAGYSPAEMMEIV 103
Cdd:cd07224     5 SAAGLLFPYHLGVLSLLIEAGVINETtpLAGASAGSLAAACSASGLSPEEALEAT 59
 
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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