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Conserved domains on  [gi|2328739638|ref|WP_265371330|]
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patatin-like phospholipase family protein [Prosthecochloris sp. SCSIO W1101]

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 ...
 7-250 1.57e-74

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 227.48  E-value: 1.57e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLDWLDLS-----------GL 75
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFdlslprrllrlDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  76 TLSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDG 155
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLYVDG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638 156 VLMENVPLSPLLELGWRPFVCVDLMGSHifRKPDNIVDLLLNAFYSTLKSTTA--MQTEEADLKIELGLGAFSLVDTRQV 233
Cdd:COG1752   167 GVVNNLPVDPARALGADRVIAVDLNPPL--RKLPSLLDILGRALEIMFNSILRreLALEPADILIEPDLSGISLLDFSRA 244

                         250
                  ....*....|....*..
gi 2328739638 234 PQLIETGYRESLPLLRQ 250
Cdd:COG1752   245 EELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 7-250 1.57e-74

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 227.48  E-value: 1.57e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLDWLDLS-----------GL 75
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFdlslprrllrlDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  76 TLSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDG 155
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLYVDG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638 156 VLMENVPLSPLLELGWRPFVCVDLMGSHifRKPDNIVDLLLNAFYSTLKSTTA--MQTEEADLKIELGLGAFSLVDTRQV 233
Cdd:COG1752   167 GVVNNLPVDPARALGADRVIAVDLNPPL--RKLPSLLDILGRALEIMFNSILRreLALEPADILIEPDLSGISLLDFSRA 244

                         250
                  ....*....|....*..
gi 2328739638 234 PQLIETGYRESLPLLRQ 250
Cdd:COG1752   245 EELIEAGYEAARRALDE 261
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 7-179 8.90e-64

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: 197.00  E-value: 8.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDL--DWLDLSGLTLSQFGLLS 84
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRstDLKALSDLTIPTAGLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  85 NKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDGVLMENVPLS 164
Cdd:cd07205    81 GDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVD 160

                         170
                  ....*....|....*
gi 2328739638 165 PLLELGWRPFVCVDL 179
Cdd:cd07205   161 VLRELGADIIIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 9-167 5.53e-25

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: 97.68  E-value: 5.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLD--------------WLDLSG 74
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDlnlflslirkralsLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  75 LTLSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIV------------ATDIGNGEKIVLK-----QGDVAEAVMASSC 137
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltviSTALGTRARILLPddlddDEDLADAVLASSA 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2328739638 138 IPAVFKPVEIGERMLVDGVLMENVPLSPLL 167
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPVEAAL 190
PRK10279 PRK10279
patatin-like phospholipase RssA;
3-179 2.02e-23

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 96.32  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   3 RTASIGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIAS-------------LRAFGMgWREIEniALDLDW 69
Cdd:PRK10279    2 RKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAayacdrlsaledwVTSFSY-WDVLR--LMDLSW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  70 ldlsgltlSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGE 149
Cdd:PRK10279   79 --------QRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNG 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 2328739638 150 RMLVDGVLMENVPLSPLLELGWRPFVCVDL 179
Cdd:PRK10279  151 YWLVDGAVVNPVPVSLTRALGADIVIAVDL 180
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 7-250 1.57e-74

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 227.48  E-value: 1.57e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLDWLDLS-----------GL 75
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFdlslprrllrlDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  76 TLSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDG 155
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLYVDG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638 156 VLMENVPLSPLLELGWRPFVCVDLMGSHifRKPDNIVDLLLNAFYSTLKSTTA--MQTEEADLKIELGLGAFSLVDTRQV 233
Cdd:COG1752   167 GVVNNLPVDPARALGADRVIAVDLNPPL--RKLPSLLDILGRALEIMFNSILRreLALEPADILIEPDLSGISLLDFSRA 244

                         250
                  ....*....|....*..
gi 2328739638 234 PQLIETGYRESLPLLRQ 250
Cdd:COG1752   245 EELIEAGYEAARRALDE 261
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 7-179 8.90e-64

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: 197.00  E-value: 8.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDL--DWLDLSGLTLSQFGLLS 84
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRstDLKALSDLTIPTAGLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  85 NKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDGVLMENVPLS 164
Cdd:cd07205    81 GDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVD 160

                         170
                  ....*....|....*
gi 2328739638 165 PLLELGWRPFVCVDL 179
Cdd:cd07205   161 VLRELGADIIIAVDL 175
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 7-179 3.36e-41

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: 139.33  E-value: 3.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIAlDLDWLDLSGL---TLSQFGLL 83
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVR-SLSQRDVLRLldlSASRSGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  84 SNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDGVLMENVPL 163
Cdd:cd07228    80 KGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPV 159

                         170
                  ....*....|....*.
gi 2328739638 164 SPLLELGWRPFVCVDL 179
Cdd:cd07228   160 SVARALGADIVIAVDL 175
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 7-168 8.98e-41

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: 139.79  E-value: 8.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   7 IGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLDWLDLSGL--TLSQFGLLS 84
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFwdPPLRGGLLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  85 NKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDGVLMENVPLS 164
Cdd:cd07210    81 GDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPFD 160


                  ....
gi 2328739638 165 PLLE 168
Cdd:cd07210   161 ALRP 164
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 9-222 4.83e-32

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: 117.01  E-value: 4.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGM--GWREIENIaldldWLDLSGLT-LSQFGLLSN 85
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDpeAVERLEKL-----WRELSREDvFLRGLLDRA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  86 KKFGRIvrgllgkRRIEDASVPLAIVATDIGNGEKIVL---KQGDVAEAVMASSCIPAVFKPVEIGERMLVDGVLMENVP 162
Cdd:cd07209    76 LDFDTL-------RLLAILFAGLVIVAVNVLTGEPVYFddiPDGILPEHLLASAALPPFFPPVEIDGRYYWDGGVVDNTP 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638 163 LSPLLELGWRPFVCVDLMGSHIFRKPDNIVDLLLNAFYStLKSTTAMQTEEADLKIELGL 222
Cdd:cd07209   149 LSPAIDLGADEIIVVSLSDKGRDDRKGTPPTTLIEILPR-LFLRSGLDSERIRHNLELGY 207
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 9-164 1.08e-25

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: 99.66  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLDWLDL---------SGLTLS- 78
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKETDFAKLldspvgllfLLPSLFk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  79 QFGLLSNKKFGRIVRGLLGKRRI------------EDASVPLAIVATDIGNGEKIVLKQGD-----VAEAVMASSCIPAV 141
Cdd:cd07207    82 EGGLYKGDALEEWLRELLKEKTGnsfatsllrdldDDLGKDLKVVATDLTTGALVVFSAETtpdmpVAKAVRASMSIPFV 161

                         170       180
                  ....*....|....*....|....
gi 2328739638 142 FKPVEIG-ERMLVDGVLMENVPLS 164
Cdd:cd07207   162 FKPVRLAkGDVYVDGGVLDNYPVW 185
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 9-167 5.53e-25

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: 97.68  E-value: 5.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLD--------------WLDLSG 74
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDlnlflslirkralsLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  75 LTLSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIV------------ATDIGNGEKIVLK-----QGDVAEAVMASSC 137
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltviSTALGTRARILLPddlddDEDLADAVLASSA 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2328739638 138 IPAVFKPVEIGERMLVDGVLMENVPLSPLL 167
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPVEAAL 190
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 9-166 1.33e-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: 93.56  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMgWREIENIALDLDWLDLSGLTLSQF---GLLSN 85
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGR-DLEEALLLLLRLSREVRLRFDGAFpptGRLLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  86 KKFGRIVRGLLGKrRIEDASVPLAIVATDIGNGEKIVLKQ---GDVAEAVMASSCIPAVFKPVE--IGERMLVDGVLMEN 160
Cdd:cd07198    80 ILRQPLLSALPDD-AHEDASGKLFISLTRLTDGENVLVSDtskGELWSAVRASSSIPGYFGPVPlsFRGRRYGDGGLSNN 158


                  ....*.
gi 2328739638 161 VPLSPL 166
Cdd:cd07198   159 LPVAEL 164
PRK10279 PRK10279
patatin-like phospholipase RssA;
3-179 2.02e-23

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 96.32  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   3 RTASIGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIAS-------------LRAFGMgWREIEniALDLDW 69
Cdd:PRK10279    2 RKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAayacdrlsaledwVTSFSY-WDVLR--LMDLSW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  70 ldlsgltlSQFGLLSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGE 149
Cdd:PRK10279   79 --------QRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNG 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 2328739638 150 RMLVDGVLMENVPLSPLLELGWRPFVCVDL 179
Cdd:PRK10279  151 YWLVDGAVVNPVPVSLTRALGADIVIAVDL 180
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 6-188 2.17e-22

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: 92.94  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   6 SIGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLD------WLDLSGLTLSQ 79
Cdd:cd07227    10 AIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAgrmasmWRFLSDVTYPF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  80 FGLLSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPVEIGERMLVDGVLME 159
Cdd:cd07227    90 ASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSDNGSMLLDGGYMD 169

                         170       180
                  ....*....|....*....|....*....
gi 2328739638 160 NVPLSPLLELGWRPFVCVDLmGSHIFRKP 188
Cdd:cd07227   170 NLPVSPMRSLGIRDIFAVDV-GSVDDRTP 197
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 9-256 5.73e-20

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: 86.12  E-value: 5.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIEVHAL-SGTSIGSFIAS---LRAFGMGWREIENIALDLDWLDLSGL--TLSQFGL 82
Cdd:cd07208     1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLvIGVSAGALNAAsylSGQRGRALRINTKYATDPRYLGLRSLlrTGNLFDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  83 lsNKKFGRIVRGL--LGKRRIEDASVPLAIVATDIGNGEKIVLKQGDV----AEAVMASSCIPAVFKPVEIGERMLVDGV 156
Cdd:cd07208    81 --DFLYDELPDGLdpFDFEAFAASPARFYVVATDADTGEAVYFDKPDIlddlLDALRASSALPGLFPPVRIDGEPYVDGG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638 157 LMENVPLSPLLELGWRPFVCVdLMGSHIFRKPDNIVDLLLNAFYstlksttamqteeadlkielglgafslvdtRQVPQL 236
Cdd:cd07208   159 LSDSIPVDKAIEDGADKIVVI-LTRPRGYRKKPSKSSPLAKLLY------------------------------RKYPNL 207

                         250       260
                  ....*....|....*....|....*.
gi 2328739638 237 IETG------YRESLPLLRQLKDDGN 256
Cdd:cd07208   208 VEALlrrhsrYNETLEFIRRLEAEGK 233
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 6-182 1.19e-16

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: 77.83  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   6 SIGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRAFGMGWREIENIALDLDW---------LDLSGLT 76
Cdd:cd07225    15 SIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKdmtsiwkklLDLTYPI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  77 LSQFgllSNKKFGRIVRGLLGKRRIEDASVPLAIVATDIGNGEKIVLKQGDVAEAVMASSCIPAVFKPV---EIGeRMLV 153
Cdd:cd07225    95 TSMF---SGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPLcdpKDG-HLLM 170

                         170       180
                  ....*....|....*....|....*....
gi 2328739638 154 DGVLMENVPLSPLLELGWRPFVCVDLmGS 182
Cdd:cd07225   171 DGGYINNLPADVARSMGAKTVIAIDV-GS 198
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
2-197 1.73e-11

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 62.87  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   2 DRTASIGLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGS-FIASL------------------RAFgMGWReieN 62
Cdd:COG4667     1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGAlNGASYlsrqpgrarrvitdyatdPRF-FSLR---N 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  63 IA-----LDLDWLdlsgltlsqFGLLSNKKFGrivrglLGKRRIEDASVPLAIVATDIGNGEKIVLK----QGDVAEAVM 133
Cdd:COG4667    77 FLrggnlFDLDFL---------YDEIPNELLP------FDFETFKASPREFYVVATNADTGEAEYFSkkddDYDLLDALR 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2328739638 134 ASSCIPAVFKPVEIGERMLVDGVLMENVPLSPLLELGWRPFVCV--------------DLMGSHIFRKPDNIVDLLLN 197
Cdd:COG4667   142 ASSALPLLYPPVEIDGKRYLDGGVADSIPVREAIRDGADKIVVIltrprgyrkkpskfKRLLRRLYRKYPKLVEALLN 219
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 3-169 6.84e-07

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 49.13  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   3 RTAsigLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLrafgMGWREIENIaldldwldLSGLTLSQfgl 82
Cdd:cd07206    69 RTA---LMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAAL----LGTHTDEEL--------IGDLTFQE--- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  83 lSNKKFGRIVR-GLLGKRRIEDASVPLAIVATDigngekiVLkqgdVAEAVMASSCIPAVFKPVE-------------IG 148
Cdd:cd07206   131 -AYERTGRIINiTVAPAEPHQNSRLLNALTSPN-------VL----IWSAVLASCAVPGVFPPVMlmaknrdgeivpyLP 198

                         170       180
                  ....*....|....*....|.
gi 2328739638 149 ERMLVDGVLMENVPLSPLLEL 169
Cdd:cd07206   199 GRKWVDGSVSDDLPAKRLARL 219
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 9-179 1.82e-06

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: 46.64  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELAIE--VHALSGTSIGSFIASLrafgmgwreienialdldwldLSGLTLSqfglLSNK 86
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAAT---------------------LYPPSSS----LDNK 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  87 KFGRIVRGLLGKRRIE--DASVPLAIVATDIGngekivlKQGDVAEAVMASSCIPAVFKPVEIGERM------------L 152
Cdd:cd01819    56 PRQSLEEALSGKLWVSftPVTAGENVLVSRFV-------SKEELIRALFASGSWPSYFGLIPPAELYtsksnlkekgvrL 128

                         170       180
                  ....*....|....*....|....*..
gi 2328739638 153 VDGVLMENVPLSPLLELGWRPFVCVDL 179
Cdd:cd01819   129 VDGGVSNNLPAPVLLRPGRGVTLTISP 155
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 8-165 5.74e-06

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 46.19  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   8 GLALGGGAVLGAAHVGVLRALDELAIE----VHALSGTSIGSFIASLRAFGM----GWREIENIALDLDWLDLSGLTLSq 79
Cdd:cd07204     1 NLSFSGCGFLGIYHVGVASALREHAPRllqnARRIAGASAGAIVAAVVLCGVsmeeACSFILKVVSEARRRSLGPLHPS- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  80 FGLLsnkkfgRIVRGLLGKRRIEDA----SVPLAIVATDIGNGEKIVLKQ----GDVAEAVMASSCIP--AVFKPVEIGE 149
Cdd:cd07204    80 FNLL------KILRQGLEKILPDDAhelaSGRLHISLTRVSDGENVLVSEfdskEELIQALVCSCFIPfyCGLIPPKFRG 153

                         170
                  ....*....|....*.
gi 2328739638 150 RMLVDGVLMENVPLSP 165
Cdd:cd07204   154 VRYIDGGLSDNLPILD 169
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 3-52 1.92e-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: 45.14  E-value: 1.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2328739638   3 RTAsigLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASLRA 52
Cdd:cd07231    68 RTA---LLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIA 114
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 1-50 1.20e-04

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: 42.64  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2328739638   1 MDRTAsigLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIASL 50
Cdd:cd07232    65 YGRTA---LCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAAL 111
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 9-162 1.92e-04

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 41.89  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDELA----IEVHALSGTSIGSFIASLRAFGMGWREIENIALD-----LDWLDLSGLTLSQ 79
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEFpsflDQIDLFAGTSAGSLIALGLALGYSPRQVLKLYEEvglkvFSKSSAGGGAGNN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  80 FglLSNKKFGRIVRG-LLGKRRIEDASVPLAIVATDIGNGEK-------------IVLKQG---DVAEAVMASSCIPAVF 142
Cdd:cd07213    85 Q--YFAAGFLKAFAEvFFGDLTLGDLKRKVLVPSFQLDSGKDdpnrrwkpklfhnFPGEPDldeLLVDVCLRSSAAPTYF 162

                         170       180
                  ....*....|....*....|
gi 2328739638 143 KPVEigerMLVDGVLMENVP 162
Cdd:cd07213   163 PSYQ----GYVDGGVFANNP 178
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 9-155 2.87e-04

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: 41.16  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638   9 LALGGGAVLGAAHVGVLRALDEL---AIEVHAL----SGTSIGSFIASLRAFGMgwREIENIaldldwldlsgltLSQFG 81
Cdd:cd07199     2 LSLDGGGIRGIIPAEILAELEKRlgkPSRIADLfdliAGTSTGGIIALGLALGR--YSAEEL-------------VELYE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328739638  82 LLSNKKFGRivrgllgkrriedasvpLAIVATDIGNGEKIVLKQGD-----------VAEAVMASSCIPAVFKPVEI--- 147
Cdd:cd07199    67 ELGRKIFPR-----------------VLVTAYDLSTGKPVVFSNYDaeepdddddfkLWDVARATSAAPTYFPPAVIesg 129


                  ....*....
gi 2328739638 148 -GERMLVDG 155
Cdd:cd07199   130 gDEGAFVDG 138
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 3-49 3.46e-04

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


Pssm-ID: 132868  Cd Length: 421  Bit Score: 41.44  E-value: 3.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2328739638   3 RTAsigLALGGGAVLGAAHVGVLRALDELAIEVHALSGTSIGSFIAS 49
Cdd:cd07230    73 RTA---LLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAA 116
 
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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