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Conserved domains on  [gi|496061621|ref|WP_008786128|]
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MULTISPECIES: patatin family protein [Citrobacter]

Protein Classification

patatin family protein( domain architecture ID 11468705)

patatin family protein similar to Escherichia coli YjjU; the family includes putative phospholipases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
20-303 8.03e-128

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


:

Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 367.57  E-value: 8.03e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  20 FQPGNMALVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPVRFVR 99
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 100 GGNLIDLDWLVDSTA-SQMPLAMDnaeRLFAAGKAFYMCACRGDDYTPGYFSPNR--QNWLDLIRASSAIPGFYRtGVVL 176
Cdd:COG4667   80 GGNLFDLDFLYDEIPnELLPFDFE---TFKASPREFYVVATNADTGEAEYFSKKDddYDLLDALRASSALPLLYP-PVEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 177 DGVNYLDGGVSDAIPVQEAAKQGAKTLVVIRTVPSQMYYTPQWFKRMERWLGeSSLQPFLNLVQHHETSYRAIQSFIEKP 256
Cdd:COG4667  156 DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLY-RKYPKLVEALLNRHERYNETLEFIEQL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 496061621 257 PGKLRIFEIYPPKPLHSMALGSRIPALREDYKTGRLCGRYFLATVGK 303
Cdd:COG4667  235 EKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELKA 281
 
Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
20-303 8.03e-128

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 367.57  E-value: 8.03e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  20 FQPGNMALVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPVRFVR 99
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 100 GGNLIDLDWLVDSTA-SQMPLAMDnaeRLFAAGKAFYMCACRGDDYTPGYFSPNR--QNWLDLIRASSAIPGFYRtGVVL 176
Cdd:COG4667   80 GGNLFDLDFLYDEIPnELLPFDFE---TFKASPREFYVVATNADTGEAEYFSKKDddYDLLDALRASSALPLLYP-PVEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 177 DGVNYLDGGVSDAIPVQEAAKQGAKTLVVIRTVPSQMYYTPQWFKRMERWLGeSSLQPFLNLVQHHETSYRAIQSFIEKP 256
Cdd:COG4667  156 DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLY-RKYPKLVEALLNRHERYNETLEFIEQL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 496061621 257 PGKLRIFEIYPPKPLHSMALGSRIPALREDYKTGRLCGRYFLATVGK 303
Cdd:COG4667  235 EKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELKA 281
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 27-294 7.44e-90

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: 270.63  E-value: 7.44e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFMRAQFNPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPVRFVRGGNLIDL 106
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRSLLRTGNLFDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 107 DWLVDSTasQMPLAMDNAERLFAAGKAFYMCACRGDDYTPGYFSPN--RQNWLDLIRASSAIPGFYRtGVVLDGVNYLDG 184
Cdd:cd07208   81 DFLYDEL--PDGLDPFDFEAFAASPARFYVVATDADTGEAVYFDKPdiLDDLLDALRASSALPGLFP-PVRIDGEPYVDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 185 GVSDAIPVQEAAKQGAKTLVVIRTVPSQMYYTPQWFKrmerWLGESSLQPFLNLVQ---HHETSYRAIQSFIEKPPGKLR 261
Cdd:cd07208  158 GLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSS----PLAKLLYRKYPNLVEallRRHSRYNETLEFIRRLEAEGK 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 496061621 262 IFEIYPPKPLHSMALGSRIPALREDYKTGRLCG 294
Cdd:cd07208  234 IFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA 266
DUF6363 pfam19890
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ...
 232-305 3.35e-25

Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. This domain is found at the C-terminal of patatin-like proteins from bacteria. There is a conserved tyrosine residue and a conserved FxxxPP sequence motif.


Pssm-ID: 466223 [Multi-domain]  Cd Length: 75  Bit Score: 96.83  E-value: 3.35e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496061621  232 LQPFLNLVQHHETSYRAIQSFIEKPPGKLRIFEIYPPKPLHSMALGSRIPALREDYKTGRLCGRYFLATVGKLL 305
Cdd:pfam19890   1 YPKLVDALLKRYESYNETLDFIENPEKEGKAFVIRPEKPLKSSRLESDPEKLEADYELGYEDGRRFLEELKEFL 74
 
Name Accession Description Interval E-value
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
20-303 8.03e-128

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 367.57  E-value: 8.03e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  20 FQPGNMALVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPVRFVR 99
Cdd:COG4667    1 SNMMKTALVLEGGGMRGIFTAGVLDALLEEGI-PFDLVIGVSAGALNGASYLSRQPGRARRVITDYATDPRFFSLRNFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 100 GGNLIDLDWLVDSTA-SQMPLAMDnaeRLFAAGKAFYMCACRGDDYTPGYFSPNR--QNWLDLIRASSAIPGFYRtGVVL 176
Cdd:COG4667   80 GGNLFDLDFLYDEIPnELLPFDFE---TFKASPREFYVVATNADTGEAEYFSKKDddYDLLDALRASSALPLLYP-PVEI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 177 DGVNYLDGGVSDAIPVQEAAKQGAKTLVVIRTVPSQMYYTPQWFKRMERWLGeSSLQPFLNLVQHHETSYRAIQSFIEKP 256
Cdd:COG4667  156 DGKRYLDGGVADSIPVREAIRDGADKIVVILTRPRGYRKKPSKFKRLLRRLY-RKYPKLVEALLNRHERYNETLEFIEQL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 496061621 257 PGKLRIFEIYPPKPLHSMALGSRIPALREDYKTGRLCGRYFLATVGK 303
Cdd:COG4667  235 EKEGKIFVIRPPKPLTVSRLERDPEKLRALYELGYEDARKFLAELKA 281
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 27-294 7.44e-90

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: 270.63  E-value: 7.44e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFMRAQFNPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPVRFVRGGNLIDL 106
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPFDLVIGVSAGALNAASYLSGQRGRALRINTKYATDPRYLGLRSLLRTGNLFDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 107 DWLVDSTasQMPLAMDNAERLFAAGKAFYMCACRGDDYTPGYFSPN--RQNWLDLIRASSAIPGFYRtGVVLDGVNYLDG 184
Cdd:cd07208   81 DFLYDEL--PDGLDPFDFEAFAASPARFYVVATDADTGEAVYFDKPdiLDDLLDALRASSALPGLFP-PVRIDGEPYVDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 185 GVSDAIPVQEAAKQGAKTLVVIRTVPSQMYYTPQWFKrmerWLGESSLQPFLNLVQ---HHETSYRAIQSFIEKPPGKLR 261
Cdd:cd07208  158 GLSDSIPVDKAIEDGADKIVVILTRPRGYRKKPSKSS----PLAKLLYRKYPNLVEallRRHSRYNETLEFIRRLEAEGK 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 496061621 262 IFEIYPPKPLHSMALGSRIPALREDYKTGRLCG 294
Cdd:cd07208  234 IFVIAPEKPLKVSRLERDPEKLEALYDLGYEDA 266
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 27-195 1.71e-36

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: 130.15  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFMRAQFNPfELFYGTSAGAQNLSAYLCNQPGYGRKVIM-RYTTRREFFDPVRFVRGGNLID 105
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLI-DIIAGTSAGAIVAALLASGRDLEEALLLLlRLSREVRLRFDGAFPPTGRLLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 106 LDWLVDSTASQmplamdNAERLFAAGKAFYMCACRGDDYTPGYFSPNRQNWLDLIRASSAIPGFYRTGVV-LDGVNYLDG 184
Cdd:cd07198   80 ILRQPLLSALP------DDAHEDASGKLFISLTRLTDGENVLVSDTSKGELWSAVRASSSIPGYFGPVPLsFRGRRYGDG 153

                        170
                 ....*....|.
gi 496061621 185 GVSDAIPVQEA 195
Cdd:cd07198  154 GLSNNLPVAEL 164
DUF6363 pfam19890
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ...
 232-305 3.35e-25

Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. This domain is found at the C-terminal of patatin-like proteins from bacteria. There is a conserved tyrosine residue and a conserved FxxxPP sequence motif.


Pssm-ID: 466223 [Multi-domain]  Cd Length: 75  Bit Score: 96.83  E-value: 3.35e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496061621  232 LQPFLNLVQHHETSYRAIQSFIEKPPGKLRIFEIYPPKPLHSMALGSRIPALREDYKTGRLCGRYFLATVGKLL 305
Cdd:pfam19890   1 YPKLVDALLKRYESYNETLDFIENPEKEGKAFVIRPEKPLKSSRLESDPEKLEADYELGYEDGRRFLEELKEFL 74
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 26-210 7.90e-22

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 93.04  E-value: 7.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  26 ALVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPvRFVRGGNLID 105
Cdd:COG1752    8 GLVLSGGGARGAAHIGVLKALEEAGI-PPDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDL-SLPRRLLRLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 106 LDWLVDSTASQMPLAmDNAERLFAAG------KAFYMCACrgdDYTPG---YFSpnRQNWLDLIRASSAIPGFYRTgVVL 176
Cdd:COG1752   86 LGLSPGGLLDGDPLR-RLLERLLGDRdfedlpIPLAVVAT---DLETGrevVFD--SGPLADAVRASAAIPGVFPP-VEI 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 496061621 177 DGVNYLDGGVSDAIPVQEAAKQGAKTLVVIRTVP 210
Cdd:COG1752  159 DGRLYVDGGVVNNLPVDPARALGADRVIAVDLNP 192
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 27-195 5.49e-21

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: 89.21  E-value: 5.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621   27 LVCEGGGQRGIFTAGVLDEFMRAqFNPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDP------VRFVRG 100
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLirkralSLLALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  101 GNLIDLDWLVDSTASQMPLA--------MDNAERLFAAGKAFYMCACRGDDYTPGYFSPNRQNW--------LDLIRASS 164
Cdd:pfam01734  80 RGLIGEGGLFDGDALRELLRkllgdltlEELAARLSLLLVVALRALLTVISTALGTRARILLPDdldddedlADAVLASS 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 496061621  165 AIPGFYRtGVVLDGVNYLDGGVSDAIPVQEA 195
Cdd:pfam01734 160 ALPGVFP-PVRLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 27-210 8.11e-15

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: 72.71  E-value: 8.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFMRAqFNPFELFYGTSAGAQNLSAYLCNQPGYGRKVIMRYT--TRREFFdpvrfVRGGnli 104
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEA-GIEPDIISGTSIGAINGALIAGGDPEAVERLEKLWRelSREDVF-----LRGL--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 105 dLDWLVDstasqmplaMDNAERLFAAGKAFYMCAcrgDDYTPG---YFS--PNRQNwLDLIRASSAIPGFYRtGVVLDGV 179
Cdd:cd07209   72 -LDRALD---------FDTLRLLAILFAGLVIVA---VNVLTGepvYFDdiPDGIL-PEHLLASAALPPFFP-PVEIDGR 136

                        170       180       190
                 ....*....|....*....|....*....|.
gi 496061621 180 NYLDGGVSDAIPVQEAAKQGAKTLVVIRTVP 210
Cdd:cd07209  137 YYWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 26-211 3.25e-09

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: 56.59  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  26 ALVCEGGGQRGIFTAGVLDEFMRAQFNPFElFYGTSAGAQNLSAYLCNQPGYGRKVIMRYTTRREFFDPVRFVRGGNLID 105
Cdd:cd07210    2 ALVLSSGFFGFYAHLGFLAALLEMGLEPSA-ISGTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFWDPPLRGGLLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 106 LD---------WLVDS-TASQMPLAM---DNAER---LFAAGkafymcacrgddytpgyfspnrqNWLDLIRASSAIPGF 169
Cdd:cd07210   81 GDrfaallrehLPPDRfEELRIPLAVsvvDLTSRetlLLSEG-----------------------DLAEAVAASCAVPPL 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 496061621 170 YRTgVVLDGVNYLDGGVSDAIPVQEAAKQGaKTLVVIRTVPS 211
Cdd:cd07210  138 FQP-VEIGGRPFVDGGVADRLPFDALRPEI-ERILYHHVAPR 177
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 26-204 5.45e-09

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: 54.86  E-value: 5.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  26 ALVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQnLSAYLC--NQPGYGRKVIMRYTTRREFFDPVRFVRGGnL 103
Cdd:cd07205    2 GLALSGGGARGLAHIGVLKALEEAGI-PIDIVSGTSAGAI-VGALYAagYSPEEIEERAKLRSTDLKALSDLTIPTAG-L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 104 IDLDWLVDSTASQMPlaMDNAERLFaagKAFYMCACrgdDYTPG---YFSpnRQNWLDLIRASSAIPGFYrTGVVLDGVN 180
Cdd:cd07205   79 LRGDKFLELLDEYFG--DRDIEDLW---IPFFIVAT---DLTSGklvVFR--SGSLVRAVRASMSIPGIF-PPVKIDGQL 147

                        170       180
                 ....*....|....*....|....
gi 496061621 181 YLDGGVSDAIPVQEAAKQGAKTLV 204
Cdd:cd07205  148 LVDGGVLNNLPVDVLRELGADIII 171
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 27-192 1.45e-07

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: 51.13  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQnLSAYLCNqpGYG----RKVIMRYTTRRE-------FFDPV 95
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGI-LKKRVAGTSAGAI-TAALLAL--GYSaadiKDILKETDFAKLldspvglLFLLP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  96 RFVRGGNLID----LDWLVDSTASQMPLAMDNAERLFAAGKAFYMCACRGDDYTPG---YFSPNRQNWLDL---IRASSA 165
Cdd:cd07207   78 SLFKEGGLYKgdalEEWLRELLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGalvVFSAETTPDMPVakaVRASMS 157

                        170       180
                 ....*....|....*....|....*..
gi 496061621 166 IPGFYRTGVVLDGVNYLDGGVSDAIPV 192
Cdd:cd07207  158 IPFVFKPVRLAKGDVYVDGGVLDNYPV 184
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 27-186 8.70e-05

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


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 43.47  E-value: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFMRAQFNP------FELFYGTSAGAqnLSAYLCNQPGYGRKVIMR-YTTR-REFFDPVrfv 98
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKRLGKPsriadlFDLIAGTSTGG--IIALGLALGRYSAEELVElYEELgRKIFPRV--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  99 rggnLIdldwlvdsTASQMPlamDNAERLFAAGKAfyMCACRGDDYTPgyfspnrqnWlDLIRASSAIPGF---YRTGVV 175
Cdd:cd07199   77 ----LV--------TAYDLS---TGKPVVFSNYDA--EEPDDDDDFKL---------W-DVARATSAAPTYfppAVIESG 129

                        170
                 ....*....|.
gi 496061621 176 LDGVNYLDGGV 186
Cdd:cd07199  130 GDEGAFVDGGV 140
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 31-186 4.79e-04

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 41.43  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  31 GGGQRGIFTAGVLDEFMRAQFNP----FELFYGTSAGAQNLSAYLCnqpGY-GRKVIMRYTTR-REFFDPVRFVRggnLI 104
Cdd:COG3621   14 GGGIRGLIPARILAELEERLGKPlaeyFDLIAGTSTGGIIALGLAA---GYsAEEILDLYEEEgKEIFPKSRWRK---LL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 105 DLDWLVDSTASQMPLAmDNAERLF------AAGKAFYMCACRGDDYTPGYFS----PNRQNW----LDLIRASSAIPGFY 170
Cdd:COG3621   88 SLRGLFGPKYDSEGLE-KVLKEYFgdttlgDLKTPVLIPSYDLDNGKPVFFKsphaKFDRDRdfllVDVARATSAAPTYF 166

                        170       180
                 ....*....|....*....|
gi 496061621 171 R----TGVVLDGVNYLDGGV 186
Cdd:COG3621  167 PpaqiKNLTGEGYALIDGGV 186
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 27-191 8.70e-04

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: 39.32  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  27 LVCEGGGQRGIFTAGVLDEFM-RAQFNPFELFYGTSAGAQnLSAYLCNqPGYGRKVIMR--YTTRREFFDPVRFVRggnL 103
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAeRGLLDCVTYLAGTSGGAW-VAATLYP-PSSSLDNKPRqsLEEALSGKLWVSFTP---V 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621 104 IDLDWLVDSTASQMplamdnaERLFAAGkaFYMCacrgddYTPGYFS--PNRQNWLDLIRASSaipgfyrtgvvlDGVNY 181
Cdd:cd01819   76 TAGENVLVSRFVSK-------EELIRAL--FASG------SWPSYFGliPPAELYTSKSNLKE------------KGVRL 128

                        170
                 ....*....|
gi 496061621 182 LDGGVSDAIP 191
Cdd:cd01819  129 VDGGVSNNLP 138
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 26-201 2.41e-03

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: 38.41  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  26 ALVCEGGGQRGIFTAGVLDEFMRAQFnPFELFYGTSAGAQNLSAYLCnqpgyGRKV-------IMRYTTRREFFDPVR-- 96
Cdd:cd07228    2 GLALGSGGARGWAHIGVLRALEEEGI-EIDIIAGSSIGALVGALYAA-----GHLDaleewvrSLSQRDVLRLLDLSAsr 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496061621  97 --FVRGGNLIDL--DWLVDSTASQMPlamdnaerlfaagKAFYMCACrgdDYTPG---YFspNRQNWLDLIRASSAIPGF 169
Cdd:cd07228   76 sgLLKGEKVLEYlrEIMGGVTIEELP-------------IPFAAVAT---DLQTGkevWF--REGSLIDAIRASISIPGI 137

                        170       180       190
                 ....*....|....*....|....*....|..
gi 496061621 170 YRTgVVLDGVNYLDGGVSDAIPVQEAAKQGAK 201
Cdd:cd07228  138 FAP-VEHNGRLLVDGGVVNPIPVSVARALGAD 168
 
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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