NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|517293145|ref|WP_018481963|]
View 

patatin-like phospholipase family protein [Rhizobium ruizarguesonis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 32-308 1.40e-84

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 255.60  E-value: 1.40e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  32 PQKKIKIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAG-KLDELESFARSLTMRRIASL----- 105
Cdd:COG1752    1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDLslprr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 106 ---LDLTIGGSGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNH 182
Cdd:COG1752   81 llrLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 183 RTLVDGALVNPVPVSVCRAYEQPLVVAVNLNydlygrsavvrhnaslsaqevHKQEEAPyarlGMTGVMVQAFNIIQDRI 262
Cdd:COG1752  161 RLYVDGGVVNNLPVDPARALGADRVIAVDLN---------------------PPLRKLP----SLLDILGRALEIMFNSI 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 517293145 263 ARARLAGDPPDISLQPRLSYIGLSEFHRAGEAIERGYEEARARLPE 308
Cdd:COG1752  216 LRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 32-308 1.40e-84

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 255.60  E-value: 1.40e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  32 PQKKIKIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAG-KLDELESFARSLTMRRIASL----- 105
Cdd:COG1752    1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDLslprr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 106 ---LDLTIGGSGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNH 182
Cdd:COG1752   81 llrLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 183 RTLVDGALVNPVPVSVCRAYEQPLVVAVNLNydlygrsavvrhnaslsaqevHKQEEAPyarlGMTGVMVQAFNIIQDRI 262
Cdd:COG1752  161 RLYVDGGVVNNLPVDPARALGADRVIAVDLN---------------------PPLRKLP----SLLDILGRALEIMFNSI 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 517293145 263 ARARLAGDPPDISLQPRLSYIGLSEFHRAGEAIERGYEEARARLPE 308
Cdd:COG1752  216 LRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 38-212 3.09e-82

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: 246.42  E-value: 3.09e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  38 IALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRRIASLLDLTIGGSGLFG 117
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLDLSASRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 118 GMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVNPVPVS 197
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 517293145 198 VCRAYEQPLVVAVNL 212
Cdd:cd07228  161 VARALGADIVIAVDL 175
PRK10279 PRK10279
patatin-like phospholipase RssA;
34-299 9.86e-71

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 221.51  E-value: 9.86e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  34 KKIKIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRRIASLLDLTIGGS 113
Cdd:PRK10279   2 RKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 114 GLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVNP 193
Cdd:PRK10279  82 GLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 194 VPVSVCRAYEQPLVVAVNLNYDLY--------------------GRSAVVRHNASLSAQEVHKQEEAPYArlgmTGVMVQ 253
Cdd:PRK10279 162 VPVSLTRALGADIVIAVDLQHDAHlmqqdllsfnvseensengdSLPWHARLKERLGSITTRRAVTAPTA----MEIMTT 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 517293145 254 AFNIIQDRIARARLAGDPPDISLQPRLSYIGLSEFHRAGEAIERGY 299
Cdd:PRK10279 238 SIQVLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQ 283
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 40-196 1.34e-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: 108.85  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145   40 LALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGK-----LDELESFARSLTMRRI-------ASLLD 107
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRdpeeiEDLLLELDLNLFLSLIrkralslLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  108 LTIGGSGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAA-----------------EVNTGHEVWIANGSLITALRASYA 170
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvistalgtrARILLPDDLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*.
gi 517293145  171 LPGIFEPVRSNHRTLVDGALVNPVPV 196
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPV 186
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 32-308 1.40e-84

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 255.60  E-value: 1.40e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  32 PQKKIKIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAG-KLDELESFARSLTMRRIASL----- 105
Cdd:COG1752    1 APARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDLslprr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 106 ---LDLTIGGSGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNH 182
Cdd:COG1752   81 llrLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 183 RTLVDGALVNPVPVSVCRAYEQPLVVAVNLNydlygrsavvrhnaslsaqevHKQEEAPyarlGMTGVMVQAFNIIQDRI 262
Cdd:COG1752  161 RLYVDGGVVNNLPVDPARALGADRVIAVDLN---------------------PPLRKLP----SLLDILGRALEIMFNSI 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 517293145 263 ARARLAGDPPDISLQPRLSYIGLSEFHRAGEAIERGYEEARARLPE 308
Cdd:COG1752  216 LRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 38-212 3.09e-82

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: 246.42  E-value: 3.09e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  38 IALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRRIASLLDLTIGGSGLFG 117
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLDLSASRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 118 GMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVNPVPVS 197
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 517293145 198 VCRAYEQPLVVAVNL 212
Cdd:cd07228  161 VARALGADIVIAVDL 175
PRK10279 PRK10279
patatin-like phospholipase RssA;
34-299 9.86e-71

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 221.51  E-value: 9.86e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  34 KKIKIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRRIASLLDLTIGGS 113
Cdd:PRK10279   2 RKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 114 GLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVNP 193
Cdd:PRK10279  82 GLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 194 VPVSVCRAYEQPLVVAVNLNYDLY--------------------GRSAVVRHNASLSAQEVHKQEEAPYArlgmTGVMVQ 253
Cdd:PRK10279 162 VPVSLTRALGADIVIAVDLQHDAHlmqqdllsfnvseensengdSLPWHARLKERLGSITTRRAVTAPTA----MEIMTT 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 517293145 254 AFNIIQDRIARARLAGDPPDISLQPRLSYIGLSEFHRAGEAIERGY 299
Cdd:PRK10279 238 SIQVLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQ 283
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 38-212 2.02e-55

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: 177.74  E-value: 2.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  38 IALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRRIASLLDLTIGGSGLFG 117
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDLTIPTAGLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 118 GMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVNPVPVS 197
Cdd:cd07205   81 GDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVD 160

                        170
                 ....*....|....*
gi 517293145 198 VCRAYEQPLVVAVNL 212
Cdd:cd07205  161 VLRELGADIIIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 40-196 1.34e-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: 108.85  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145   40 LALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGK-----LDELESFARSLTMRRI-------ASLLD 107
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRdpeeiEDLLLELDLNLFLSLIrkralslLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  108 LTIGGSGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAA-----------------EVNTGHEVWIANGSLITALRASYA 170
Cdd:pfam01734  81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvistalgtrARILLPDDLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*.
gi 517293145  171 LPGIFEPVRSNHRTLVDGALVNPVPV 196
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPV 186
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 38-197 3.82e-28

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: 108.59  E-value: 3.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  38 IALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGK-LDELESFARSLTMRRIASLLDLTiGGSGLF 116
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGIsPDEMAELLLSLERKDFWMFWDPP-LRGGLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 117 GGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVNPVPV 196
Cdd:cd07210   80 SGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPF 159


                 .
gi 517293145 197 S 197
Cdd:cd07210  160 D 160
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 40-199 1.03e-26

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: 103.19  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  40 LALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRRIASLLDLTIGGSGLFGGM 119
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGRLLGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 120 RLTKRMQEHLEGLNVEDLDRPFVAVAAeVNTGHEVWIAN---GSLITALRASYALPGIFEPV--RSNHRTLVDGALVNPV 194
Cdd:cd07198   81 LRQPLLSALPDDAHEDASGKLFISLTR-LTDGENVLVSDtskGELWSAVRASSSIPGYFGPVplSFRGRRYGDGGLSNNL 159


                 ....*
gi 517293145 195 PVSVC 199
Cdd:cd07198  160 PVAEL 164
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 40-211 2.03e-25

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: 101.21  E-value: 2.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  40 LALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALvGGCYLAGKL----DELESFARSLTMRRI--ASLLDLTIggs 113
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAI-NGALIAGGDpeavERLEKLWRELSREDVflRGLLDRAL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 114 glfggmrLTKRMQEhleglnVEDLDRPFVAVAAEVNTGHEV---WIANGSLITALRASYALPGIFEPVRSNHRTLVDGAL 190
Cdd:cd07209   77 -------DFDTLRL------LAILFAGLVIVAVNVLTGEPVyfdDIPDGILPEHLLASAALPPFFPPVEIDGRYYWDGGV 143

                        170       180
                 ....*....|....*....|...
gi 517293145 191 VNPVPVSVC--RAYEQPLVVAVN 211
Cdd:cd07209  144 VDNTPLSPAidLGADEIIVVSLS 166
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 38-211 4.08e-24

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: 99.78  E-value: 4.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  38 IALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGK-----LDELESFARSLTmRRIASLLDLTIGG 112
Cdd:cd07225   16 IALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERnisrmKQRAREWAKDMT-SIWKKLLDLTYPI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 113 SGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPV---RSNHrTLVDGA 189
Cdd:cd07225   95 TSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPLcdpKDGH-LLMDGG 173

                        170       180
                 ....*....|....*....|..
gi 517293145 190 LVNPVPVSVCRAYEQPLVVAVN 211
Cdd:cd07225  174 YINNLPADVARSMGAKTVIAID 195
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 38-212 1.45e-21

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: 92.17  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  38 IALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYlAGKLDELESFARSLTMR-RIAS----LLDLTIGG 112
Cdd:cd07227   11 IGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLY-AREADLVPIFGRAKKFAgRMASmwrfLSDVTYPF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 113 SGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANGSLITALRASYALPGIFEPVRSNHRTLVDGALVN 192
Cdd:cd07227   90 ASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSDNGSMLLDGGYMD 169

                        170       180
                 ....*....|....*....|
gi 517293145 193 PVPVSVCRAYEQPLVVAVNL 212
Cdd:cd07227  170 NLPVSPMRSLGIRDIFAVDV 189
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 40-204 4.15e-21

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: 90.75  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  40 LALGGGAARGWAHIGVLRALDEAKV-EIGMIAGTSIGALVGGCYLAGKL-DELESFARSLTMRRIASLLDLtIGGSGLFG 117
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYLSGQRgRALRINTKYATDPRYLGLRSL-LRTGNLFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 118 GMRLTKRMQEHLEGLNVEDLDR---PFVAVAAEVNTGHEVWI----ANGSLITALRASYALPGIFEPVRSNHRTLVDGAL 190
Cdd:cd07208   80 LDFLYDELPDGLDPFDFEAFAAspaRFYVVATDADTGEAVYFdkpdILDDLLDALRASSALPGLFPPVRIDGEPYVDGGL 159

                        170
                 ....*....|....
gi 517293145 191 VNPVPVSvcRAYEQ 204
Cdd:cd07208  160 SDSIPVD--KAIED 171
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
37-204 1.23e-20

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 89.45  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  37 KIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDE-LESFARSLTMRRIASLLDLtIGGSGL 115
Cdd:COG4667    5 KTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYLSRQPGRaRRVITDYATDPRFFSLRNF-LRGGNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 116 FGGMRLTKRMQEHLEGLNVEDL---DRPFVAVAAEVNTGHEVWI----ANGSLITALRASYALPGIFEPVRSNHRTLVDG 188
Cdd:COG4667   84 FDLDFLYDEIPNELLPFDFETFkasPREFYVVATNADTGEAEYFskkdDDYDLLDALRASSALPLLYPPVEIDGKRYLDG 163

                        170
                 ....*....|....*.
gi 517293145 189 ALVNPVPVSvcRAYEQ 204
Cdd:COG4667  164 GVADSIPVR--EAIRD 177
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 40-198 5.87e-17

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: 77.70  E-value: 5.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  40 LALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAG-KLDELESFA-----RSLTMRRIA--SLLDLTIG 111
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGySAADIKDILketdfAKLLDSPVGllFLLPSLFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 112 GSGLFGGMRLTKRMQEHLEGLNV------------EDLDRPFVAVAAEVNTGHEVWI-----ANGSLITALRASYALPGI 174
Cdd:cd07207   82 EGGLYKGDALEEWLRELLKEKTGnsfatsllrdldDDLGKDLKVVATDLTTGALVVFsaettPDMPVAKAVRASMSIPFV 161

                        170       180
                 ....*....|....*....|....*.
gi 517293145 175 FEPVRsNHR--TLVDGALVNPVPVSV 198
Cdd:cd07207  162 FKPVR-LAKgdVYVDGGVLDNYPVWL 186
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 31-194 2.55e-10

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 60.30  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  31 APQKKIKIaLALGGGAARGWAHIGVLRALDEA-KVEIG----MIAGTSIGALVGGCYLAGK-LDELES---------FAR 95
Cdd:COG3621    2 SANKPFRI-LSLDGGGIRGLIPARILAELEERlGKPLAeyfdLIAGTSTGGIIALGLAAGYsAEEILDlyeeegkeiFPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  96 SLtMRRIASLLDLTiggSGLFGGMRLTKRMQEHLEGLNVEDLDRPFVAVAAEVNTGHEVWIANG----------SLITAL 165
Cdd:COG3621   81 SR-WRKLLSLRGLF---GPKYDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFKSPhakfdrdrdfLLVDVA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517293145 166 RASYALPGIFEPVRSNH-----RTLVDGALV--NPV 194
Cdd:COG3621  157 RATSAAPTYFPPAQIKNltgegYALIDGGVFanNPA 192
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 39-195 7.71e-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: 49.90  E-value: 7.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  39 ALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVG---GCY----LAGKLDELESFARSltmRRIaslLDLTIG 111
Cdd:cd07206   71 ALMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAallGTHtdeeLIGDLTFQEAYERT---GRI---INITVA 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 112 GSGLFGGMRLtkrmqehlegLNVedLDRPFVAvaaevntgheVWiangsliTALRASYALPGIFEPVR------------ 179
Cdd:cd07206  145 PAEPHQNSRL----------LNA--LTSPNVL----------IW-------SAVLASCAVPGVFPPVMlmaknrdgeivp 195

                        170
                 ....*....|....*...
gi 517293145 180 --SNHRtLVDGALVNPVP 195
Cdd:cd07206  196 ylPGRK-WVDGSVSDDLP 212
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 37-89 1.93e-06

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


Pssm-ID: 132870  Cd Length: 407  Bit Score: 48.80  E-value: 1.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517293145  37 KIALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGcYLAGKLDE 89
Cdd:cd07232   67 RTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAA-LLCTRTDE 118
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 39-98 3.04e-06

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: 48.22  E-value: 3.04e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  39 ALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLT 98
Cdd:cd07231   70 ALLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFFRALL 129
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 40-203 1.40e-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: 44.33  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  40 LALGGGAARGWAHIGVLRALDEAKVE--IGMIAGTSIGALVGGCY--LAGKLDELesfarsltmrriaslldltiggsgL 115
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAATLypPSSSLDNK------------------------P 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 116 FGGMRLTKRMQEHLEGLNVEDldrPFVAVAAEVNTGHEVWiangsliTALRASY---ALPGIFEPVR---------SNHR 183
Cdd:cd01819   57 RQSLEEALSGKLWVSFTPVTA---GENVLVSRFVSKEELI-------RALFASGswpSYFGLIPPAElytsksnlkEKGV 126

                        170       180
                 ....*....|....*....|
gi 517293145 184 TLVDGALVNPVPVSVCRAYE 203
Cdd:cd01819  127 RLVDGGVSNNLPAPVLLRPG 146
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 29-198 4.59e-05

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: 44.55  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  29 PPAPQKKIKIaLALGGGAARGWAHIGVLRALDEakvEIG--------MIAGTSIGALVgGCYLAGK---LDELESFARSL 97
Cdd:cd07211    1 PPVKGRGIRI-LSIDGGGTRGVVALEILRKIEK---LTGkpihelfdYICGVSTGAIL-AFLLGLKkmsLDECEELYRKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  98 TmRRIASLLDLTIGGSGLF---------GGMRLTKRMQEHLEGLNV-EDLDRP-FVAVAAEVNTGHE---VW-------- 155
Cdd:cd07211   76 G-KDVFSQNTYISGTSRLVlshayydteTWEKILKEMMGSDELIDTsADPNCPkVACVSTQVNRTPLkpyVFrnynhppg 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517293145 156 ---IANGS----LITALRASYALPGIFEPVRSNHRTLVDGALV--NPVPVSV 198
Cdd:cd07211  155 trsHYLGSckhkLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLanNPTALAL 206
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 39-101 7.48e-05

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: 44.14  E-value: 7.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517293145  39 ALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVGGCYLAGKLDELESFARSLTMRR 101
Cdd:cd07230   75 ALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGD 137
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 40-194 8.90e-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: 40.39  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145  40 LALGGGAARGWAHIGVLRALDEA---KVEIG----MIAGTSIGALVGGCYLAGKL--DELESFARSLtMRRIASLLDLTi 110
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKRlgkPSRIAdlfdLIAGTSTGGIIALGLALGRYsaEELVELYEEL-GRKIFPRVLVT- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517293145 111 ggsglfgGMRLTKRmqehleglnvedldRPFV---AVAAEVNTGHEVwiangSLITALRASYALPGIFEPVR----SNHR 183
Cdd:cd07199   80 -------AYDLSTG--------------KPVVfsnYDAEEPDDDDDF-----KLWDVARATSAAPTYFPPAViesgGDEG 133

                        170
                 ....*....|...
gi 517293145 184 TLVDGALV--NPV 194
Cdd:cd07199  134 AFVDGGVAanNPA 146
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 39-82 4.45e-03

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: 38.44  E-value: 4.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 517293145  39 ALALGGGAARGWAHIGVLRALDEAKVEIGMIAGTSIGALVG---GCY 82
Cdd:cd07229   85 ALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAalvGVH 131
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH