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Conserved domains on  [gi|3323358|gb|AAC65980|]
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conserved hypothetical protein [Treponema pallidum subsp. pallidum str. Nichols]

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 ...
 1-285 1.72e-65

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 206.29  E-value: 1.72e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    1 MKWSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGMSVREMEAFFQRdfvisdyVNARDPsacv 80
Cdd:COG1752   5 PKIGLVLSGGGARGAAHIGVLKALEEAGIPP-DVIAGTSAGAIVGALYAAGYSADELEELWRS-------LDRRDL---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   81 eagmvwgARAAFQRLGKLVQLGVSlntlvrGLGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVL 160
Cdd:COG1752  73 -------FDLSLPRRLLRLDLGLS------PGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPL 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358  161 ARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAVTFDRfeqlGLSDFRTGFDVLLRSLSCASHAV 240
Cdd:COG1752 140 ADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNP----PLRKLPSLLDILGRALEIMFNSI 215

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3323358  241 ATQARNYPSACVRVETRRDQS---DFSRPQELVARGYAAvqhARAVLD 285
Cdd:COG1752 216 LRRELALEPADILIEPDLSGIsllDFSRAEELIEAGYEA---ARRALD 260
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-285 1.72e-65

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 206.29  E-value: 1.72e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    1 MKWSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGMSVREMEAFFQRdfvisdyVNARDPsacv 80
Cdd:COG1752   5 PKIGLVLSGGGARGAAHIGVLKALEEAGIPP-DVIAGTSAGAIVGALYAAGYSADELEELWRS-------LDRRDL---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   81 eagmvwgARAAFQRLGKLVQLGVSlntlvrGLGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVL 160
Cdd:COG1752  73 -------FDLSLPRRLLRLDLGLS------PGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPL 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358  161 ARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAVTFDRfeqlGLSDFRTGFDVLLRSLSCASHAV 240
Cdd:COG1752 140 ADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNP----PLRKLPSLLDILGRALEIMFNSI 215

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3323358  241 ATQARNYPSACVRVETRRDQS---DFSRPQELVARGYAAvqhARAVLD 285
Cdd:COG1752 216 LRRELALEPADILIEPDLSGIsllDFSRAEELIEAGYEA---ARRALD 260
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 3-209 8.69e-56

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: 178.51  E-value: 8.69e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    3 WSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGMSVREMEAFFQRDFVIsdyvnardpsacvea 82
Cdd:cd07205   1 IGLALSGGGARGLAHIGVLKALEEAGIPI-DIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTD--------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   83 gmvwgaraaFQRLGKLvqlgvslnTLVRGlGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVLAR 162
Cdd:cd07205  65 ---------LKALSDL--------TIPTA-GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVR 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3323358  163 ALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:cd07205 127 AVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRELGADIIIAV 173
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-209 4.47e-29

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 112.88  E-value: 4.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358     1 MKWSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGmSVREMEAFFqRDFVISDYVNARDPSacv 80
Cdd:PRK10279   4 IKIGLALGSGAARGWSHIGVINALKKVGIEI-DIVAGCSIGSLVGAAYACD-RLSALEDWV-TSFSYWDVLRLMDLS--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    81 eagmvWGaraafqrlgklvqlgvslntlvRGlGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVL 160
Cdd:PRK10279  78 -----WQ----------------------RG-GLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDL 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 3323358   161 ARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:PRK10279 130 HLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPVSLTRALGADIVIAV 178
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 5-198 3.75e-28

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: 107.69  E-value: 3.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358      5 LVLSGGGARGIAHIGVLKALEAlQVPPPQCVVGCSMGAVVGALYALGMSVREMEAFFqRDFVISDYVNARDPsacvEAGM 84
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGE-AGIRFDVISGTSAGAINAALLALGRDPEEIEDLL-LELDLNLFLSLIRK----RALS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358     85 VWGARAAFQRLGKLVQLGVSLNTLVRGLGLDSGEKFATLLTRVTGGKSFHDCK-IPFLCNAVNLCTGAEVVLSSGVLARA 163
Cdd:pfam01734  75 LLALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTvISTALGTRARILLPDDLDDDEDLADA 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 3323358    164 LRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIA 198
Cdd:pfam01734 155 VLASSALPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-285 1.72e-65

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 206.29  E-value: 1.72e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    1 MKWSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGMSVREMEAFFQRdfvisdyVNARDPsacv 80
Cdd:COG1752   5 PKIGLVLSGGGARGAAHIGVLKALEEAGIPP-DVIAGTSAGAIVGALYAAGYSADELEELWRS-------LDRRDL---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   81 eagmvwgARAAFQRLGKLVQLGVSlntlvrGLGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVL 160
Cdd:COG1752  73 -------FDLSLPRRLLRLDLGLS------PGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPL 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358  161 ARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAVTFDRfeqlGLSDFRTGFDVLLRSLSCASHAV 240
Cdd:COG1752 140 ADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNP----PLRKLPSLLDILGRALEIMFNSI 215

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3323358  241 ATQARNYPSACVRVETRRDQS---DFSRPQELVARGYAAvqhARAVLD 285
Cdd:COG1752 216 LRRELALEPADILIEPDLSGIsllDFSRAEELIEAGYEA---ARRALD 260
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 3-209 8.69e-56

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: 178.51  E-value: 8.69e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    3 WSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGMSVREMEAFFQRDFVIsdyvnardpsacvea 82
Cdd:cd07205   1 IGLALSGGGARGLAHIGVLKALEEAGIPI-DIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTD--------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   83 gmvwgaraaFQRLGKLvqlgvslnTLVRGlGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVLAR 162
Cdd:cd07205  65 ---------LKALSDL--------TIPTA-GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVR 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3323358  163 ALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:cd07205 127 AVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVLRELGADIIIAV 173
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 4-209 1.67e-45

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: 152.04  E-value: 1.67e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    4 SLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGMSVREMEafFQRDFVISDYVNARDPSacveag 83
Cdd:cd07228   2 GLALGSGGARGWAHIGVLRALEEEGIEI-DIIAGSSIGALVGALYAAGHLDALEE--WVRSLSQRDVLRLLDLS------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   84 mvwgaraafqrlgklvqlgvslntlVRGLGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVLARA 163
Cdd:cd07228  73 -------------------------ASRSGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDA 127

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 3323358  164 LRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:cd07228 128 IRASISIPGIFAPVEHNGRLLVDGGVVNPIPVSVARALGADIVIAV 173
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 4-195 2.14e-33

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: 122.07  E-value: 2.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    4 SLVLSGGGARGIAHIGVLKALEALQVPPPQcVVGCSMGAVVGALYALGMSVREMEAFFQRdfvisdyvnaRDPSacvEAG 83
Cdd:cd07210   2 ALVLSSGFFGFYAHLGFLAALLEMGLEPSA-ISGTSAGALVGGLFASGISPDEMAELLLS----------LERK---DFW 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   84 MVWGARaafqrlgklvqlgvslntlvRGLGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVLARA 163
Cdd:cd07210  68 MFWDPP--------------------LRGGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEA 127

                       170       180       190
                ....*....|....*....|....*....|..
gi 3323358  164 LRASCAYPGVFAPVRQEGVYLADGCILNNTPV 195
Cdd:cd07210 128 VAASCAVPPLFQPVEIGGRPFVDGGVADRLPF 159
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 5-197 4.43e-30

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: 112.76  E-value: 4.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEALQVPPPQcVVGCSMGAVVGALYALGMSVREMEAFF-QRDFvisdyvnardpsacveag 83
Cdd:cd07207   2 LVFEGGGAKGIAYIGALKALEEAGILKKR-VAGTSAGAITAALLALGYSAADIKDILkETDF------------------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   84 mvwgaraaFQRLGKLVQLGVSLNTLVRGLGLDSGEKFATLL---TRVTGGKSFHDCKIPFLCN---------AVNLCTGA 151
Cdd:cd07207  63 --------AKLLDSPVGLLFLLPSLFKEGGLYKGDALEEWLrelLKEKTGNSFATSLLRDLDDdlgkdlkvvATDLTTGA 134

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3323358  152 EVVLSSGV-----LARALRASCAYPGVFAPVR-QEGVYLADGCILNNTPVWI 197
Cdd:cd07207 135 LVVFSAETtpdmpVAKAVRASMSIPFVFKPVRlAKGDVYVDGGVLDNYPVWL 186
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-209 4.47e-29

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 112.88  E-value: 4.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358     1 MKWSLVLSGGGARGIAHIGVLKALEALQVPPpQCVVGCSMGAVVGALYALGmSVREMEAFFqRDFVISDYVNARDPSacv 80
Cdd:PRK10279   4 IKIGLALGSGAARGWSHIGVINALKKVGIEI-DIVAGCSIGSLVGAAYACD-RLSALEDWV-TSFSYWDVLRLMDLS--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    81 eagmvWGaraafqrlgklvqlgvslntlvRGlGLDSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVL 160
Cdd:PRK10279  78 -----WQ----------------------RG-GLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDL 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 3323358   161 ARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:PRK10279 130 HLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPVPVSLTRALGADIVIAV 178
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 5-198 3.75e-28

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: 107.69  E-value: 3.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358      5 LVLSGGGARGIAHIGVLKALEAlQVPPPQCVVGCSMGAVVGALYALGMSVREMEAFFqRDFVISDYVNARDPsacvEAGM 84
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGE-AGIRFDVISGTSAGAINAALLALGRDPEEIEDLL-LELDLNLFLSLIRK----RALS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358     85 VWGARAAFQRLGKLVQLGVSLNTLVRGLGLDSGEKFATLLTRVTGGKSFHDCK-IPFLCNAVNLCTGAEVVLSSGVLARA 163
Cdd:pfam01734  75 LLALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTvISTALGTRARILLPDDLDDDEDLADA 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 3323358    164 LRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIA 198
Cdd:pfam01734 155 VLASSALPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 5-195 8.73e-23

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: 92.79  E-value: 8.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEALQvPPPQCVVGCSMGAVVGALYALGMSVREMEAFFQRdfvISDYVNARDPSacveagm 84
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERG-PLIDIIAGTSAGAIVAALLASGRDLEEALLLLLR---LSREVRLRFDG------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   85 vwgaraAFQRLGKLvqLGVSLNTLVRGLGLDSGEkfatlltrvtggksfhDCKIPFLCNAVNLCTGAEVVL---SSGVLA 161
Cdd:cd07198  70 ------AFPPTGRL--LGILRQPLLSALPDDAHE----------------DASGKLFISLTRLTDGENVLVsdtSKGELW 125

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 3323358  162 RALRASCAYPGVFAPV--RQEGVYLADGCILNNTPV 195
Cdd:cd07198 126 SAVRASSSIPGYFGPVplSFRGRRYGDGGLSNNLPV 161
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 5-209 1.52e-22

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: 93.13  E-value: 1.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEALqVPPPQCVVGCSMGAVVGALYALGMS--VREMEAFFQrdfvisdyvnardpSACVEA 82
Cdd:cd07209   1 LVLSGGGALGAYQAGVLKALAEA-GIEPDIISGTSIGAINGALIAGGDPeaVERLEKLWR--------------ELSRED 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   83 GMVWGaraafqrlgklvqlgvslnTLVRGLGLDSGEKFATLLTRVTGGksfhdckipflcnAVNLCTGAEVVLSSGVLAR 162
Cdd:cd07209  66 VFLRG-------------------LLDRALDFDTLRLLAILFAGLVIV-------------AVNVLTGEPVYFDDIPDGI 113

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3323358  163 ---ALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:cd07209 114 lpeHLLASAALPPFFPPVEIDGRYYWDGGVVDNTPLSPAIDLGADEIIVV 163
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 5-296 2.12e-21

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: 92.08  E-value: 2.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEALQVpPPQCVVGCSMGAVVGALYALGMSVREMeafFQRdfvisdyvnARDpsACVEAGM 84
Cdd:cd07225  18 LVLGGGGARGCAHIGVIKALEEAGI-PVDMVGGTSIGAFIGALYAEERNISRM---KQR---------ARE--WAKDMTS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   85 VWgaraafqrlGKLVQLGVSLNTLVrglgldSGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVLARAL 164
Cdd:cd07225  83 IW---------KKLLDLTYPITSMF------SGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358  165 RASCAYPGVFAPV--RQEGVYLADGCILNNTPVWIARAQGFDAVLAV---TFDRFEQLGLSDFRTGFDVLLRSLSCASHA 239
Cdd:cd07225 148 RASMSLSGYLPPLcdPKDGHLLMDGGYINNLPADVARSMGAKTVIAIdvgSQDETDLTNYGDALSGWWLLWKRWNPLAEK 227

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3323358  240 VAT------QARNYPSACVR-VETRRDQS---------------DFSRPQELVARGYaavQHARAVLDVFFARGVRGML 296
Cdd:cd07225 228 VKVpnmaeiQSRLAYVSCVRqLEEVKSSDyceylrppidkyktlDFGKFDEICEVGY---QHGKTVFDGWKRSGVLEKM 303
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 5-209 4.55e-20

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: 87.55  E-value: 4.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEALQVpPPQCVVGCSMGAVVGALYALGMSVREMEaffqrdfvisdyvnARDPSACVEAGM 84
Cdd:cd07227  13 LVLGGGGARGISHIGILQALEEAGI-PIDAIGGTSIGSFVGGLYAREADLVPIF--------------GRAKKFAGRMAS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   85 VWgaRAAFQrlgkLVQLGVSLNTlvrglgldsGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLSSGVLARAL 164
Cdd:cd07227  78 MW--RFLSD----VTYPFASYTT---------GHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYI 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 3323358  165 RASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:cd07227 143 RASMSLAGLLPPLSDNGSMLLDGGYMDNLPVSPMRSLGIRDIFAV 187
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 5-255 1.62e-15

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: 74.95  E-value: 1.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEALQVPPPQCVVGCSMGAVVGALYALGMSVREMEaffqrdfVISDYvnARDPsacveagm 84
Cdd:cd07208   1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALR-------INTKY--ATDP-------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   85 vwgaraAFQRLGKLVQLGVSLN-------TLVRGLGLDsgekFATLLTRvtggksfhdcKIPFLCNAVNLCTGAEVVLSS 157
Cdd:cd07208  64 ------RYLGLRSLLRTGNLFDldflydeLPDGLDPFD----FEAFAAS----------PARFYVVATDADTGEAVYFDK 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358  158 GV----LARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV-TFDRFEQLGLSDFRTGFDVLLRS 232
Cdd:cd07208 124 PDilddLLDALRASSALPGLFPPVRIDGEPYVDGGLSDSIPVDKAIEDGADKIVVIlTRPRGYRKKPSKSSPLAKLLYRK 203

                       250       260
                ....*....|....*....|...
gi 3323358  233 LSCASHAVATQARNYPSACVRVE 255
Cdd:cd07208 204 YPNLVEALLRRHSRYNETLEFIR 226
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 5-192 4.23e-13

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 68.39  E-value: 4.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEA-LQVPPPQC---VVGCSMGAVVGALYALGMSVREMEAFFQRDfvisdyvnardpsacv 80
Cdd:COG3621  10 LSLDGGGIRGLIPARILAELEErLGKPLAEYfdlIAGTSTGGIIALGLAAGYSAEEILDLYEEE---------------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   81 eagmvwgARAAFQRLgklvqlgvSLNTLVRGLGLD----SGEKFATLLTRVTGGKSFHDCKIPFLCNAVNLCTGAEVVLS 156
Cdd:COG3621  74 -------GKEIFPKS--------RWRKLLSLRGLFgpkyDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFK 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3323358  157 SGV----------LARALRASCAYPGVFAPVR-----QEGVYLADGCI-LNN 192
Cdd:COG3621 139 SPHakfdrdrdflLVDVARATSAAPTYFPPAQiknltGEGYALIDGGVfANN 190
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
1-209 5.09e-13

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 67.88  E-value: 5.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    1 MKWSLVLSGGGARGIAHIGVLKALEALQVPPPqCVVGCSMGAVVGALYALGMSVREMEaffqrdfVISDYVNARDpsacv 80
Cdd:COG4667   4 MKTALVLEGGGMRGIFTAGVLDALLEEGIPFD-LVIGVSAGALNGASYLSRQPGRARR-------VITDYATDPR----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   81 eagmvwgaraaFqrlgklvqlgVSLNTLVRG---LGLDsgekfatLLTRVTGGK-------SFHDCKIPFLCNAVNLCTG 150
Cdd:COG4667  71 -----------F----------FSLRNFLRGgnlFDLD-------FLYDEIPNEllpfdfeTFKASPREFYVVATNADTG 122

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3323358  151 AEVVLS----SGVLARALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIARAQGFDAVLAV 209
Cdd:COG4667 123 EAEYFSkkddDYDLLDALRASSALPLLYPPVEIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 5-178 3.99e-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: 48.03  E-value: 3.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKA-LEALQVppPQCVVGCSMGAVVGALYAlgmsVREMEaffQRDFVISDYVnARDPSACVEAG 83
Cdd:cd07232  70 LCLSGGAAFAYYHFGVVKAlLDADLL--PNVISGTSGGSLVAALLC----TRTDE---ELKQLLVPEL-ARKITACEPPW 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   84 MVWGARA----------------------------AFQRLGKLVQLGVSlntlvrglgldSGEKFATlltrvtggksfhd 135
Cdd:cd07232 140 LVWIPRWlktgarfdsvewartccwftrgsmtfeeAYERTGRILNISVV-----------PADPHSP------------- 195

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 3323358  136 ckiPFLCNAVnlcTGAEVVLSSGVLaralrASCAYPGVFAPVR 178
Cdd:cd07232 196 ---TILLNYL---TSPNCTIWSAVL-----ASAAVPGILNPVV 227
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 5-67 6.93e-06

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: 47.22  E-value: 6.93e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3323358    5 LVLSGGGARGIAHIGVLKAL-EALQVppPQCVVGCSMGAVVGALyalgMSVRE-------MEAFFQRDFVI 67
Cdd:cd07230  76 LLLSGGGTFGMFHIGVLKALfEANLL--PRIISGSSAGSIVAAI----LCTHTdeeipelLEEFPYGDFNV 140
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 5-178 9.86e-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: 46.44  E-value: 9.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKAL---EALqvppPQCVVGCSMGAVVGALyaLGMSVREMeaffqrdfVISDYVnardpsacve 81
Cdd:cd07206  72 LMLSGGASLGLFHLGVVKALweqDLL----PRVISGSSAGAIVAAL--LGTHTDEE--------LIGDLT---------- 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   82 agmvwgARAAFQRLGKLVQLGVSlntlvrglgldsgekfatlltrvtgGKSFHDCkiPFLCNAVnlcTGAEVVLSSGVLa 161
Cdd:cd07206 128 ------FQEAYERTGRIINITVA-------------------------PAEPHQN--SRLLNAL---TSPNVLIWSAVL- 170

                       170
                ....*....|....*..
gi 3323358  162 ralrASCAYPGVFAPVR 178
Cdd:cd07206 171 ----ASCAVPGVFPPVM 183
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 4-109 4.25e-05

Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG lipase activity of the lipid particle. Triacylglycerol (TAG) lipases are also necessary for the mobilization of TAG stored in lipid particles. TGL3 contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes. This family includes Tgl3p from Saccharomyces cerevisiae.


Pssm-ID: 132867  Cd Length: 391  Bit Score: 44.60  E-value: 4.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    4 SLVLSGGGARGIAHIGVLKALeALQVPPPQCVVGCSMGAVVGALyaLGMSVREMEAFFQRDFVISDYVNAR--DPSACVE 81
Cdd:cd07229  85 ALVLQGGSIFGLCHLGVVKAL-WLRGLLPRIITGTATGALIAAL--VGVHTDEELLRFLDGDGIDLSAFNRlrGKKSLGY 161

                        90       100
                ....*....|....*....|....*...
gi 3323358   82 AGMVWGARaAFQRLGKLVQLGVSLNTLV 109
Cdd:cd07229 162 SGYGWLGT-LGRRIQRLLREGYFLDVKV 188
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 5-200 6.43e-05

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: 43.47  E-value: 6.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEA-LQVPPPQC-----VVGCSMGAVVGALYALG-MSVREMEAFFQRDfvisdyvnardps 77
Cdd:cd07199   2 LSLDGGGIRGIIPAEILAELEKrLGKPSRIAdlfdlIAGTSTGGIIALGLALGrYSAEELVELYEEL------------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   78 acveagmvwgARAAFQRLGklvqlgvslntlvrglgldsgekfatlltrvtggksfhdckIPflcnAVNLCTGAEVVLSS 157
Cdd:cd07199  69 ----------GRKIFPRVL-----------------------------------------VT----AYDLSTGKPVVFSN 93

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3323358  158 GV-----------LARALRASCAYPGVFAPVR----QEGVYLADGCILNNTPVWIARA 200
Cdd:cd07199  94 YDaeepdddddfkLWDVARATSAAPTYFPPAViesgGDEGAFVDGGVAANNPALLALA 151
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 5-49 6.86e-05

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: 42.40  E-value: 6.86e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3323358    5 LVLSGGGARGIAHIGVLKAL-EALQVPPPQCVVGCSMGAVVGALYA 49
Cdd:cd01819   1 LSFSGGGFRGMYHAGVLSALaERGLLDCVTYLAGTSGGAWVAATLY 46
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 5-198 1.27e-04

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: 43.01  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358    5 LVLSGGGARGIAHIGVLKALEAL-QVPPPQC---VVGCSMGAVVGALYAL-GMSVREMEAFFqrDFVISDyVNARDPSAC 79
Cdd:cd07211  11 LSIDGGGTRGVVALEILRKIEKLtGKPIHELfdyICGVSTGAILAFLLGLkKMSLDECEELY--RKLGKD-VFSQNTYIS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323358   80 VEAGMVWgaRAAF-----------QRLGKLVQLGVSLNTlvrglgldSGEKFATLLTRVTGG--KSFHDCKIPFLCNAVN 146
Cdd:cd07211  88 GTSRLVL--SHAYydtetwekilkEMMGSDELIDTSADP--------NCPKVACVSTQVNRTplKPYVFRNYNHPPGTRS 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3323358  147 LCTGaevvlSSGVLAR-ALRASCAYPGVFAPVRQEGVYLADGCILNNTPVWIA 198
Cdd:cd07211 158 HYLG-----SCKHKLWeAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALA 205
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 4-62 1.87e-04

Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.


Pssm-ID: 132869  Cd Length: 323  Bit Score: 42.44  E-value: 1.87e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3323358    4 SLVLSGGGARGIAHIGVLKALEALQVpPPQCVVGCSMGAVVGALYALGMSvREMEAFFQ 62
Cdd:cd07231  70 ALLLSGGAALGTFHVGVVRTLVEHQL-LPRVIAGSSVGSIVCAIIATRTD-EELQSFFR 126
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 5-61 9.60e-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: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 37.27  E-value: 9.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3323358    5 LVLSGGGARGIAHIGVLKALeaLQVPP-----PQCVVGCSMGAVVGALYALGMSVREMEAFF 61
Cdd:cd07213   5 LSLDGGGVKGIVQLVLLKRL--AEEFPsfldqIDLFAGTSAGSLIALGLALGYSPRQVLKLY 64
 
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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