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Conserved domains on  [gi|981587763|ref|WP_059788642|]
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patatin-like phospholipase family protein [Burkholderia ubonensis]

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 ...
 29-312 2.54e-23

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 99.21  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  29 PMARRALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCARWRALPVKAFAALKPVTEYL 108
Cdd:COG1752    3 ARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRRLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 109 HVADM---SALGSASGLTEHVYPALGIA-VDRIRAAVGIdgsfSVCCFDDKTVVPIPHPNLdLQRLVAAASLPIFMPAVM 184
Cdd:COG1752   83 RLDLGlspGGLLDGDPLRRLLERLLGDRdFEDLPIPLAV----VATDLETGREVVFDSGPL-ADAVRASAAIPGVFPPVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 185 ADGKTWTDAVWIKDANLTSCVERGARELWLVWCIGDTPAYhNGAFNQYVHMIEMsavgalngelaMIADINRRIARGETv 264
Cdd:COG1752  158 IDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLRKL-PSLLDILGRALEI-----------MFNSILRRELALEP- 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 981587763 265 fghdqpiVVHVIKPEVPLPLDPDFYRgridAATLIDMGYRDARRTLRA 312
Cdd:COG1752  225 -------ADILIEPDLSGISLLDFSR----AEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 29-312 2.54e-23

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 99.21  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  29 PMARRALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCARWRALPVKAFAALKPVTEYL 108
Cdd:COG1752    3 ARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRRLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 109 HVADM---SALGSASGLTEHVYPALGIA-VDRIRAAVGIdgsfSVCCFDDKTVVPIPHPNLdLQRLVAAASLPIFMPAVM 184
Cdd:COG1752   83 RLDLGlspGGLLDGDPLRRLLERLLGDRdFEDLPIPLAV----VATDLETGREVVFDSGPL-ADAVRASAAIPGVFPPVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 185 ADGKTWTDAVWIKDANLTSCVERGARELWLVWCIGDTPAYhNGAFNQYVHMIEMsavgalngelaMIADINRRIARGETv 264
Cdd:COG1752  158 IDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLRKL-PSLLDILGRALEI-----------MFNSILRRELALEP- 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 981587763 265 fghdqpiVVHVIKPEVPLPLDPDFYRgridAATLIDMGYRDARRTLRA 312
Cdd:COG1752  225 -------ADILIEPDLSGISLLDFSR----AEELIEAGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 35-192 1.49e-14

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: 72.26  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763   35 LVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCA------------RWRALPVKAFAALK 102
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDllleldlnlflsLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  103 PVTEYLHVADMSALGS------ASGLTEHVYPALGIAVDRIRAAVGIDGSFSVCCFDDKTVVPIPHPNLDLQRLVAA-AS 175
Cdd:pfam01734  81 GLIGEGGLFDGDALREllrkllGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVLAsSA 160

                         170
                  ....*....|....*..
gi 981587763  176 LPIFMPAVMADGKTWTD 192
Cdd:pfam01734 161 LPGVFPPVRLDGELYVD 177
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 35-215 3.55e-11

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: 62.69  E-value: 3.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  35 LVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVL--PDELCARWRALpvkafaalkpvteylhvaD 112
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPeaVERLEKLWREL------------------S 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 113 MSALGSASGLTEHvypalgIAVDRIRAAVGIDGSFSVCCFDDKTVVPIpHPNLDLQR-----LVAAASLPIFMPAVMADG 187
Cdd:cd07209   63 REDVFLRGLLDRA------LDFDTLRLLAILFAGLVIVAVNVLTGEPV-YFDDIPDGilpehLLASAALPPFFPPVEIDG 135

                        170       180
                 ....*....|....*....|....*...
gi 981587763 188 KTWTDAVWIKDANLTSCVERGARELWLV 215
Cdd:cd07209  136 RYYWDGGVVDNTPLSPAIDLGADEIIVV 163
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 29-312 2.54e-23

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 99.21  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  29 PMARRALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCARWRALPVKAFAALKPVTEYL 108
Cdd:COG1752    3 ARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRRLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 109 HVADM---SALGSASGLTEHVYPALGIA-VDRIRAAVGIdgsfSVCCFDDKTVVPIPHPNLdLQRLVAAASLPIFMPAVM 184
Cdd:COG1752   83 RLDLGlspGGLLDGDPLRRLLERLLGDRdFEDLPIPLAV----VATDLETGREVVFDSGPL-ADAVRASAAIPGVFPPVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 185 ADGKTWTDAVWIKDANLTSCVERGARELWLVWCIGDTPAYhNGAFNQYVHMIEMsavgalngelaMIADINRRIARGETv 264
Cdd:COG1752  158 IDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLRKL-PSLLDILGRALEI-----------MFNSILRRELALEP- 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 981587763 265 fghdqpiVVHVIKPEVPLPLDPDFYRgridAATLIDMGYRDARRTLRA 312
Cdd:COG1752  225 -------ADILIEPDLSGISLLDFSR----AEELIEAGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 35-192 1.49e-14

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: 72.26  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763   35 LVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCA------------RWRALPVKAFAALK 102
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDllleldlnlflsLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  103 PVTEYLHVADMSALGS------ASGLTEHVYPALGIAVDRIRAAVGIDGSFSVCCFDDKTVVPIPHPNLDLQRLVAA-AS 175
Cdd:pfam01734  81 GLIGEGGLFDGDALREllrkllGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVLAsSA 160

                         170
                  ....*....|....*..
gi 981587763  176 LPIFMPAVMADGKTWTD 192
Cdd:pfam01734 161 LPGVFPPVRLDGELYVD 177
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
28-312 1.49e-11

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 65.19  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  28 DPMARRALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGvlpdelcARWRALPVkafaalkpvteY 107
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYLSR-------QPGRARRV-----------I 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 108 LHVADMSALGSASGL--------TEHVY-----PALGIAVDRIRAAvgiDGSFSVCCFDDKT-----VVPIPHPNLDLQR 169
Cdd:COG4667   63 TDYATDPRFFSLRNFlrggnlfdLDFLYdeipnELLPFDFETFKAS---PREFYVVATNADTgeaeyFSKKDDDYDLLDA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 170 LVAAASLPIFMPAVMADGKTWTD-----AVWIKDAnltscVERGAREL---------------WLVWcigdtpaYHNGAF 229
Cdd:COG4667  140 LRASSALPLLYPPVEIDGKRYLDggvadSIPVREA-----IRDGADKIvviltrprgyrkkpsKFKR-------LLRRLY 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 230 NQYVHMIEmsavgalngelAMIADINR-RIARGETVFGHDQPIVVhVIKPEVPLPL-----DPDfyrgRIDAatLIDMGY 303
Cdd:COG4667  208 RKYPKLVE-----------ALLNRHERyNETLEFIEQLEKEGKIF-VIRPPKPLTVsrlerDPE----KLRA--LYELGY 269


                 ....*....
gi 981587763 304 RDARRTLRA 312
Cdd:COG4667  270 EDARKFLAE 278
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 35-215 3.55e-11

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: 62.69  E-value: 3.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  35 LVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVL--PDELCARWRALpvkafaalkpvteylhvaD 112
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPeaVERLEKLWREL------------------S 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 113 MSALGSASGLTEHvypalgIAVDRIRAAVGIDGSFSVCCFDDKTVVPIpHPNLDLQR-----LVAAASLPIFMPAVMADG 187
Cdd:cd07209   63 REDVFLRGLLDRA------LDFDTLRLLAILFAGLVIVAVNVLTGEPV-YFDDIPDGilpehLLASAALPPFFPPVEIDG 135

                        170       180
                 ....*....|....*....|....*...
gi 981587763 188 KTWTDAVWIKDANLTSCVERGARELWLV 215
Cdd:cd07209  136 RYYWDGGVVDNTPLSPAIDLGADEIIVV 163
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 35-183 6.12e-11

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: 61.20  E-value: 6.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  35 LVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCARwraLPVKAFAALK------PVTEYL 108
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLL---LLRLSREVRLrfdgafPPTGRL 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981587763 109 HvaDMSALGSASGLTEhvypalgiavDRIRAAVGIDGSFSVCCFDDKTVVPIPHPNLDL-QRLVAAASLPIFMPAV 183
Cdd:cd07198   78 L--GILRQPLLSALPD----------DAHEDASGKLFISLTRLTDGENVLVSDTSKGELwSAVRASSSIPGYFGPV 141
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 35-192 6.90e-10

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: 59.93  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  35 LVLAGGGMRVAYQAGAIKALFDEGLR-FSHADGASGGTINLSALLSGvlpdelcARWRALPVkaFAALKPVTEYLHVADM 113
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRpFDLVIGVSAGALNAASYLSG-------QRGRALRI--NTKYATDPRYLGLRSL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 114 SALGSASGL--TEHVYPALGIAVDrIRAAVGIDGSFSVCCFDDKTVVPIPHP-----NLDLQRLVAAASLPIFMPAVMAD 186
Cdd:cd07208   72 LRTGNLFDLdfLYDELPDGLDPFD-FEAFAASPARFYVVATDADTGEAVYFDkpdilDDLLDALRASSALPGLFPPVRID 150


                 ....*.
gi 981587763 187 GKTWTD 192
Cdd:cd07208  151 GEPYVD 156
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 34-192 2.61e-06

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: 48.50  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763  34 ALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELcarwralpVKAFAALKPVTEYLHVADM 113
Cdd:cd07210    2 ALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEM--------AELLLSLERKDFWMFWDPP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981587763 114 SALGSASG------LTEHvypalgIAVDRIRAAvgiDGSFSVCCFDDKTVVPIPHPNLDLQRLVAA-ASLPIFMPAVMAD 186
Cdd:cd07210   74 LRGGLLSGdrfaalLREH------LPPDRFEEL---RIPLAVSVVDLTSRETLLLSEGDLAEAVAAsCAVPPLFQPVEIG 144


                 ....*.
gi 981587763 187 GKTWTD 192
Cdd:cd07210  145 GRPFVD 150
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 35-78 7.57e-04

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: 40.73  E-value: 7.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 981587763  35 LVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTInLSALL 78
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAI-TAALL 44
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 34-104 9.70e-04

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: 40.22  E-value: 9.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981587763  34 ALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTINLSALLSGVLPDELCARWRALPVKAFAALKPV 104
Cdd:cd07205    2 GLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDLT 72
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 35-79 2.23e-03

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 38.94  E-value: 2.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 981587763  35 LVLAGGGMRVAYQAGAIKALFDEGLRFS--HADGASGGTINLSALLS 79
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLLDCvtYLAGTSGGAWVAATLYP 47
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 30-86 3.61e-03

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: 39.94  E-value: 3.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 981587763  30 MARRALVLAGGGMRVAYQAGAIKALFDEGLRFSHADGASGGTInLSALLSGVLPDEL 86
Cdd:cd07232   65 YGRTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSL-VAALLCTRTDEEL 120
 
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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