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Conserved domains on  [gi|505445427|ref|WP_015632529|]
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MULTISPECIES: patatin-like phospholipase family protein [Gammaproteobacteria]

Protein Classification

patatin-like phospholipase family protein( domain architecture ID 11466507)

patatin-like phospholipase family protein may act as a phospholipase that catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 2-328 2.00e-72

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


:

Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 227.48  E-value: 2.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   2 NPFRVLCLDGGGMRGVYQATYLQTFSQRLsqtgfkQSDPGSAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIF 81
Cdd:COG3621    5 KPFRILSLDGGGIRGLIPARILAELEERL------GKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  82 PRQRLRALpfvgKYVRGLCSGLASGDfALRKVLKDTFGEETIGKVYERrgigLAITTLDLNRHSSTVFKTPHMARlnGRD 161
Cdd:COG3621   79 PKSRWRKL----LSLRGLFGPKYDSE-GLEKVLKEYFGDTTLGDLKTP----VLIPSYDLDNGKPVFFKSPHAKF--DRD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 162 NDRLLVDVCMATSAAPILRSIARLEEPgsGGAIVDYIDGGLWANNPGAVGMIEAHEILQCrgeTERPVHLFMLGTLpvQG 241
Cdd:COG3621  148 RDFLLVDVARATSAAPTYFPPAQIKNL--TGEGYALIDGGVFANNPALCALAEALKLLGP---DLDDILVLSLGTG--TA 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 242 GEELASSSMLHRGALGWsaGLKAITASMNAQAVACDYMARKIAelrgnGSFAYRMPAqcpsgELHKYLENMDDAR-PRVL 320
Cdd:COG3621  221 PRSIPYKKVKNWGALGW--LLPLIDILMDAQSDAVDYQLRQLL-----GDRYYRLDP-----ELPEEIALDDNAEnIEAL 288


                 ....*...
gi 505445427 321 NALARQAV 328
Cdd:COG3621  289 LAAAEKLI 296
 
Name Accession Description Interval E-value
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 2-328 2.00e-72

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 227.48  E-value: 2.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   2 NPFRVLCLDGGGMRGVYQATYLQTFSQRLsqtgfkQSDPGSAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIF 81
Cdd:COG3621    5 KPFRILSLDGGGIRGLIPARILAELEERL------GKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  82 PRQRLRALpfvgKYVRGLCSGLASGDfALRKVLKDTFGEETIGKVYERrgigLAITTLDLNRHSSTVFKTPHMARlnGRD 161
Cdd:COG3621   79 PKSRWRKL----LSLRGLFGPKYDSE-GLEKVLKEYFGDTTLGDLKTP----VLIPSYDLDNGKPVFFKSPHAKF--DRD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 162 NDRLLVDVCMATSAAPILRSIARLEEPgsGGAIVDYIDGGLWANNPGAVGMIEAHEILQCrgeTERPVHLFMLGTLpvQG 241
Cdd:COG3621  148 RDFLLVDVARATSAAPTYFPPAQIKNL--TGEGYALIDGGVFANNPALCALAEALKLLGP---DLDDILVLSLGTG--TA 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 242 GEELASSSMLHRGALGWsaGLKAITASMNAQAVACDYMARKIAelrgnGSFAYRMPAqcpsgELHKYLENMDDAR-PRVL 320
Cdd:COG3621  221 PRSIPYKKVKNWGALGW--LLPLIDILMDAQSDAVDYQLRQLL-----GDRYYRLDP-----ELPEEIALDDNAEnIEAL 288


                 ....*...
gi 505445427 321 NALARQAV 328
Cdd:COG3621  289 LAAAEKLI 296
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
4-331 1.50e-65

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 210.43  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   4 FRVLCLDGGGMRGVYQATYLQTFSQrlsQTGFKQSDpgsAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIFPR 83
Cdd:NF041079   1 FQILSLSGGGYRGLYTASVLAELEE---QFGRPIAD---HFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  84 QRLRalpfvGKYVRGLCSGLASGDfALRKVLKDTFGEETIGKVYERrgigLAITTLDLNRHSSTVFKTPHMARLNgRDND 163
Cdd:NF041079  75 RKWP-----RRLLGLLKKPKYSSE-PLREVLEEIFGDKTIGDLKHR----VLIPAVNYTTGKPQVFKTPHHPDFT-RDHK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 164 RLLVDVCMATSAAPILRSIARLEEPgsggaivDYIDGGLWANNPGAVGMIEAHEILqcrGETERPVHLFMLGTLPVQGGE 243
Cdd:NF041079 144 LKLVDVALATSAAPTYFPLHEFDNE-------QFVDGGLVANNPGLLGLHEALHFL---GVPYDDVRILSIGTLSSKFTV 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 244 ElaSSSMLHRGALGWSAGLKAITASMNAQAVACDYMARKIaelrgNGSFAYRMPAQcPSGELHKYLE--NMDDARPRVLN 321
Cdd:NF041079 214 R--PSLKRKRGFLDWGGGKRLFELTMSAQEQLVDFMLQHI-----LGDRYLRIDDV-PTNEQAKDLGldNASEAALETLL 285

                        330
                 ....*....|
gi 505445427 322 ALARQAVSDV 331
Cdd:NF041079 286 GRAKQAAQRA 295
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 6-323 6.08e-47

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: 160.19  E-value: 6.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   6 VLCLDGGGMRGVYQATYLQTFSQRLsqtgFKQSDPGSAFDLLVGTSTGGIVACALASGIH-LEKVLELYQTYGKDIFPRq 84
Cdd:cd07199    1 ILSLDGGGIRGIIPAEILAELEKRL----GKPSRIADLFDLIAGTSTGGIIALGLALGRYsAEELVELYEELGRKIFPR- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  85 rlralpfvgkyvrglcsglasgdfalrkvlkdtfgeetigkvyerrgigLAITTLDLNRHSSTVFKTPHmARLNGRDNDR 164
Cdd:cd07199   76 -------------------------------------------------VLVTAYDLSTGKPVVFSNYD-AEEPDDDDDF 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 165 LLVDVCMATSAAPILRSIARLEEPGSGGAivdYIDGGLWANNPGAVGMIEAheiLQCRGETERPVHLFMLGTlpvqGGEE 244
Cdd:cd07199  106 KLWDVARATSAAPTYFPPAVIESGGDEGA---FVDGGVAANNPALLALAEA---LRLLAPDKDDILVLSLGT----GTSP 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505445427 245 LASSSMLHRGALGWSAGLKAITASMNAQAVACDYMARKIAELRGNGSFAYRMPAQCPSGELHkylenMDDARPRVLNAL 323
Cdd:cd07199  176 SSSSSKKASRWGGLGWGRPLLDILMDAQSDGVDQWLDLLFGSLDSKDNYLRINPPLPGPIPA-----LDDASEANLLAL 249
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 7-207 1.25e-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: 91.13  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427    7 LCLDGGGMRGVYQATYLQtfsqRLSQTGFKqsdpgsaFDLLVGTSTGGIVACALASGI----HLEKVLELYQTYGKDIFP 82
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLK----ALGEAGIR-------FDVISGTSAGAINAALLALGRdpeeIEDLLLELDLNLFLSLIR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   83 RQRLRALPFVGKYVRGlcSGLASGDfALRKVLKDTFGEETIGKVYERRGIGLAITTLDLNRHSSTVFKTPHMARLNG-RD 161
Cdd:pfam01734  70 KRALSLLALLRGLIGE--GGLFDGD-ALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDdLD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 505445427  162 NDRLLVDVCMATSAAPILRSIARLEEPGsggaivdYIDGGLWANNP 207
Cdd:pfam01734 147 DDEDLADAVLASSALPGVFPPVRLDGEL-------YVDGGLVDNVP 185
 
Name Accession Description Interval E-value
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 2-328 2.00e-72

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 227.48  E-value: 2.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   2 NPFRVLCLDGGGMRGVYQATYLQTFSQRLsqtgfkQSDPGSAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIF 81
Cdd:COG3621    5 KPFRILSLDGGGIRGLIPARILAELEERL------GKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  82 PRQRLRALpfvgKYVRGLCSGLASGDfALRKVLKDTFGEETIGKVYERrgigLAITTLDLNRHSSTVFKTPHMARlnGRD 161
Cdd:COG3621   79 PKSRWRKL----LSLRGLFGPKYDSE-GLEKVLKEYFGDTTLGDLKTP----VLIPSYDLDNGKPVFFKSPHAKF--DRD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 162 NDRLLVDVCMATSAAPILRSIARLEEPgsGGAIVDYIDGGLWANNPGAVGMIEAHEILQCrgeTERPVHLFMLGTLpvQG 241
Cdd:COG3621  148 RDFLLVDVARATSAAPTYFPPAQIKNL--TGEGYALIDGGVFANNPALCALAEALKLLGP---DLDDILVLSLGTG--TA 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 242 GEELASSSMLHRGALGWsaGLKAITASMNAQAVACDYMARKIAelrgnGSFAYRMPAqcpsgELHKYLENMDDAR-PRVL 320
Cdd:COG3621  221 PRSIPYKKVKNWGALGW--LLPLIDILMDAQSDAVDYQLRQLL-----GDRYYRLDP-----ELPEEIALDDNAEnIEAL 288


                 ....*...
gi 505445427 321 NALARQAV 328
Cdd:COG3621  289 LAAAEKLI 296
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
4-331 1.50e-65

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 210.43  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   4 FRVLCLDGGGMRGVYQATYLQTFSQrlsQTGFKQSDpgsAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIFPR 83
Cdd:NF041079   1 FQILSLSGGGYRGLYTASVLAELEE---QFGRPIAD---HFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  84 QRLRalpfvGKYVRGLCSGLASGDfALRKVLKDTFGEETIGKVYERrgigLAITTLDLNRHSSTVFKTPHMARLNgRDND 163
Cdd:NF041079  75 RKWP-----RRLLGLLKKPKYSSE-PLREVLEEIFGDKTIGDLKHR----VLIPAVNYTTGKPQVFKTPHHPDFT-RDHK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 164 RLLVDVCMATSAAPILRSIARLEEPgsggaivDYIDGGLWANNPGAVGMIEAHEILqcrGETERPVHLFMLGTLPVQGGE 243
Cdd:NF041079 144 LKLVDVALATSAAPTYFPLHEFDNE-------QFVDGGLVANNPGLLGLHEALHFL---GVPYDDVRILSIGTLSSKFTV 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 244 ElaSSSMLHRGALGWSAGLKAITASMNAQAVACDYMARKIaelrgNGSFAYRMPAQcPSGELHKYLE--NMDDARPRVLN 321
Cdd:NF041079 214 R--PSLKRKRGFLDWGGGKRLFELTMSAQEQLVDFMLQHI-----LGDRYLRIDDV-PTNEQAKDLGldNASEAALETLL 285

                        330
                 ....*....|
gi 505445427 322 ALARQAVSDV 331
Cdd:NF041079 286 GRAKQAAQRA 295
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 6-323 6.08e-47

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: 160.19  E-value: 6.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   6 VLCLDGGGMRGVYQATYLQTFSQRLsqtgFKQSDPGSAFDLLVGTSTGGIVACALASGIH-LEKVLELYQTYGKDIFPRq 84
Cdd:cd07199    1 ILSLDGGGIRGIIPAEILAELEKRL----GKPSRIADLFDLIAGTSTGGIIALGLALGRYsAEELVELYEELGRKIFPR- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  85 rlralpfvgkyvrglcsglasgdfalrkvlkdtfgeetigkvyerrgigLAITTLDLNRHSSTVFKTPHmARLNGRDNDR 164
Cdd:cd07199   76 -------------------------------------------------VLVTAYDLSTGKPVVFSNYD-AEEPDDDDDF 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 165 LLVDVCMATSAAPILRSIARLEEPGSGGAivdYIDGGLWANNPGAVGMIEAheiLQCRGETERPVHLFMLGTlpvqGGEE 244
Cdd:cd07199  106 KLWDVARATSAAPTYFPPAVIESGGDEGA---FVDGGVAANNPALLALAEA---LRLLAPDKDDILVLSLGT----GTSP 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505445427 245 LASSSMLHRGALGWSAGLKAITASMNAQAVACDYMARKIAELRGNGSFAYRMPAQCPSGELHkylenMDDARPRVLNAL 323
Cdd:cd07199  176 SSSSSKKASRWGGLGWGRPLLDILMDAQSDGVDQWLDLLFGSLDSKDNYLRINPPLPGPIPA-----LDDASEANLLAL 249
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 5-327 4.49e-31

Patatin-like phospholipase of bacteria; 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: 132854 [Multi-domain]  Cd Length: 329  Bit Score: 120.20  E-value: 4.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   5 RVLCLDGGGMRGVYQATYLQTFSQRLSQ-TGFKQSDPGSAFDLLVGTSTGGIVACAL----ASGIH---LEKVLELYQTY 76
Cdd:cd07215    1 RILSIDGGGIRGIIPATILVSVEEKLQKkTGNPEARLADYFDLVAGTSTGGILTCLYlcpnESGRPkfsAKEALNFYLER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  77 GKDIFPRQRLRALpfvgkyvrGLCSGLASGDFA---LRKVLKDTFGEETIGKVYERrgigLAITTLDLNRhSSTVFKTPH 153
Cdd:cd07215   81 GNYIFKKKIWNKI--------KSRGGFLNEKYShkpLEEVLLEYFGDTKLSELLKP----CLITSYDIER-RSPHFFKSH 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 154 MARlNGRDNDRLLVDVCMATSAAPILRSIARLEepGSGGAIVDYIDGGLWANNPGAVGMIEAHEILQCRGE--TERPVHL 231
Cdd:cd07215  148 TAI-KNEQRDFYVRDVARATSAAPTYFEPARIH--SLTGEKYTLIDGGVFANNPTLCAYAEARKLKFEQPGkpTAKDMII 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 232 FMLGTLPVQGGEELASSSmlHRGALGWSAGLKAITASMNAQAVacDYMARKIAELRGNGSFAYRMPAQcpsgELHKYLEn 311
Cdd:cd07215  225 LSLGTGKNKKSYTYEKVK--DWGLLGWAKPLIDIMMDGASQTV--DYQLKQIFDAEGDQQQYLRIQPE----LEDADPE- 295

                        330
                 ....*....|....*.
gi 505445427 312 MDDARPRVLNALARQA 327
Cdd:cd07215  296 MDDASPENLEKLREVG 311
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 3-212 2.95e-24

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


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 100.44  E-value: 2.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   3 PFRVLCLDGGGMRGVYQATYLQtfsqRLSQTGFKQSDpgsAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIFP 82
Cdd:cd07213    1 KYRILSLDGGGVKGIVQLVLLK----RLAEEFPSFLD---QIDLFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  83 RQRLRALPFVGKYvrglcsglaSGDFALRKVLKDTFGEETIGKVYERrgigLAITTLDL-------NRHS-STVFKTphm 154
Cdd:cd07213   74 KSSAGGGAGNNQY---------FAAGFLKAFAEVFFGDLTLGDLKRK----VLVPSFQLdsgkddpNRRWkPKLFHN--- 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 155 arLNGR-DNDRLLVDVCMATSAAPILRsiarleepgsggAIVD-YIDGGLWANNPGAVGM 212
Cdd:cd07213  138 --FPGEpDLDELLVDVCLRSSAAPTYF------------PSYQgYVDGGVFANNPSLCAI 183
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 7-207 1.25e-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: 91.13  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427    7 LCLDGGGMRGVYQATYLQtfsqRLSQTGFKqsdpgsaFDLLVGTSTGGIVACALASGI----HLEKVLELYQTYGKDIFP 82
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLK----ALGEAGIR-------FDVISGTSAGAINAALLALGRdpeeIEDLLLELDLNLFLSLIR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   83 RQRLRALPFVGKYVRGlcSGLASGDfALRKVLKDTFGEETIGKVYERRGIGLAITTLDLNRHSSTVFKTPHMARLNG-RD 161
Cdd:pfam01734  70 KRALSLLALLRGLIGE--GGLFDGD-ALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDdLD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 505445427  162 NDRLLVDVCMATSAAPILRSIARLEEPGsggaivdYIDGGLWANNP 207
Cdd:pfam01734 147 DDEDLADAVLASSALPGVFPPVRLDGEL-------YVDGGLVDNVP 185
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 5-231 2.75e-19

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


Pssm-ID: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 87.55  E-value: 2.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   5 RVLCLDGGGMRGVYQATYLQTFSQRLSQTGfkqSDP----GSAFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDI 80
Cdd:cd07217    2 KILALDGGGIRGLLSVEILGRIEKDLRTHL---DDPefrlGDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  81 FPRQRLRALPFVGKYVRglcsglASGDFALRKVLKDTFGEETIGKVYERrgIGLAITTLDLNRHSSTVFKTPHMARLNGR 160
Cdd:cd07217   79 FDKAWLAQRLFLNKLYN------QYDPTNLGKKLNTVFPETTLGDDTLR--TLLMIVTRNATTGSPWPVCNNPEAKYNDS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505445427 161 DN-----DRLLVDVCMATSAAPILRSIARLeEPGSGGAIVdYIDGGLWA-NNPGAVGMIEAheilqcrgeTERPVHL 231
Cdd:cd07217  151 DRsdcnlDLPLWQLVRASTAAPTFFPPEVV-SIAPGTAFV-FVDGGVTTyNNPAFQAFLMA---------TAKPYKL 216
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 5-221 2.60e-18

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: 84.23  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   5 RVLCLDGGGMRGVyqATyLQTFSQRLSQTGFKQSDpgsAFDLLVGTSTGGIVACALA-SGIHLEKVLELYQTYGKDIFPR 83
Cdd:cd07211    9 RILSIDGGGTRGV--VA-LEILRKIEKLTGKPIHE---LFDYICGVSTGAILAFLLGlKKMSLDECEELYRKLGKDVFSQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  84 QrlraLPFVGKyVRGLCSGLASGDFALRKVLKDTFGEETIGKVYERRG---IGLAITTLDLNRHSSTVFKT-PHMARLNG 159
Cdd:cd07211   83 N----TYISGT-SRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNcpkVACVSTQVNRTPLKPYVFRNyNHPPGTRS 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 160 R---DNDRLLVDVCMATSAAPilrsiARLEEPGSGGAIvdYIDGGLWANNPGAVGMIEA-----HEILQC 221
Cdd:cd07211  158 HylgSCKHKLWEAIRASSAAP-----GYFEEFKLGNNL--HQDGGLLANNPTALALHEAkllwpDTPIQC 220
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 4-295 1.61e-16

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


Pssm-ID: 132855 [Multi-domain]  Cd Length: 309  Bit Score: 79.27  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   4 FRVLCLDGGGMRGVYQATYLQTFSQRLSQTGFKQSDPGSA--FDLLVGTSTGGIVAcalasgIHL-------EKVLELYQ 74
Cdd:cd07216    1 LNLLSLDGGGVRGLSSLLILKEIMERIDPKEGLDEPPKPCdyFDLIGGTSTGGLIA------IMLgrlrmtvDECIDAYT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  75 TYGKDIFpRQRLRALPFVGKYVRGLCSGLASGDfALRKVLKDTfGEETI---GKVYERRGIGLAITTLDLNRHSSTVFKT 151
Cdd:cd07216   75 RLAKKIF-SRKRLRLIIGDLRTGARFDSKKLAE-AIKVILKEL-GNDEDdllDEGEEDGCKVFVCATDKDVTGKAVRLRS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427 152 -PHMARLNGRDNDRlLVDVCMATSAAPilrsiaRLEEP---GSGGaiVDYIDGGLWANNPGAVGMIEAHEILqcrGETER 227
Cdd:cd07216  152 yPSKDEPSLYKNAT-IWEAARATSAAP------TFFDPvkiGPGG--RTFVDGGLGANNPIREVWSEAVSLW---EGLAR 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505445427 228 PVHLFM-LGTlpvqGgeeLASSSMLHRGALGWSAGLKAITASMNAQAVACDyMARKIAELRGNGSfAYR 295
Cdd:cd07216  220 LVGCLVsIGT----G---TPSIKSLGRSAEGAGLLKGLKDLVTDTEAEAKR-FSAEHSELDEEGR-YFR 279
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 6-217 2.88e-15

Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 75.45  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   6 VLCLDGGGMRGVYQATYLQTFSQRLSQTGFKQsdpgsaFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIFPRQR 85
Cdd:cd07212    1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIREL------FDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  86 lralpfvgKYVRGLcsglasgdfaLRKVLKDTFGEETigKVYERRGIGLAITTLDLNRH----------------SSTVF 149
Cdd:cd07212   75 --------PYNSEP----------LEEFLKREFGEDT--KMTDVKYPRLMVTGVLADRQpvqlhlfrnydppedvEEPEK 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505445427 150 KTPHMARLNgrDNDRLLVDVCMATSAAPIL-RSIARleepgsggaivdYIDGGLWANNPGAVGMIEAHE 217
Cdd:cd07212  135 NANFLPPTD--PAEQLLWRAARSSGAAPTYfRPMGR------------FLDGGLIANNPTLDAMTEIHE 189
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 6-215 9.29e-15

Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum cardiophyllum. 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). Patatin-like phospholipase are included in this group. Members of this family have also been found in vertebrates.


Pssm-ID: 132853 [Multi-domain]  Cd Length: 349  Bit Score: 74.40  E-value: 9.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   6 VLCLDGGGMRGVYQATYLQTFSQRLSQTGFKQSDPGSAFDLLVGTSTGGIVACALASG-------IHLEKVLELYQTYGK 78
Cdd:cd07214    6 VLSIDGGGIRGIIPATILEFLEGKLQELDGPDARIADYFDVIAGTSTGGLITAMLTAPnenkrplFAAKDIVQFYLENGP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  79 DIFPRQR------------LRALPFVGKYVRGLCSGLasgdfalrkvLKDTFGEETIGKVyerrgiglAITTLDLNRHSS 146
Cdd:cd07214   86 KIFPQSTgqfeddrkklrsLLGPKYDGVYLHDLLNEL----------LGDTRLSDTLTNV--------VIPTFDIKLLQP 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505445427 147 TVFKTpHMARLNGRDNDRLLvDVCMATSAAPILRSIARLEEPGSGGAIVDY--IDGGLWANNPGAVGMIEA 215
Cdd:cd07214  148 VIFSS-SKAKNDKLTNARLA-DVCISTSAAPTYFPAHYFTTEDSNGDIREFnlVDGGVAANNPTLLAISEV 216
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-207 1.58e-14

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 72.63  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   1 MNPFRVLCLDGGGMRGVYQATYLQtfsqRLSQTGFKqsdpgsaFDLLVGTSTGGIVACALASGIHLEKVLELYQTYG-KD 79
Cdd:COG1752    3 ARPKIGLVLSGGGARGAAHIGVLK----ALEEAGIP-------PDVIAGTSAGAIVGALYAAGYSADELEELWRSLDrRD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  80 IFPRQRLRALPFVGKYVRGlcSGLASGDfALRKVLKDTFGEETIgkvyERRGIGLAITTLDLNRHSSTVFktphmarlng 159
Cdd:COG1752   72 LFDLSLPRRLLRLDLGLSP--GGLLDGD-PLRRLLERLLGDRDF----EDLPIPLAVVATDLETGREVVF---------- 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505445427 160 rdNDRLLVDVCMATSAAPILRSIARLeepgsGGAIvdYIDGGLWANNP 207
Cdd:COG1752  135 --DSGPLADAVRASAAIPGVFPPVEI-----DGRL--YVDGGVVNNLP 173
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 7-202 3.42e-09

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: 56.85  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   7 LCLDGGGMRGVYQATYLQTFSQrlsqTGFkqsdpgSAFDLLVGTSTGGIVACALASGihlekvlelyqtygkdifprQRL 86
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLE----AGI------RPFDLVIGVSAGALNAASYLSG--------------------QRG 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  87 RALPFVGKYVRGL----------CSGLASGDFALRKVLK--DTFGEETigkvYERRGIGLAITTLDLNRHSSTVFKTPhm 154
Cdd:cd07208   51 RALRINTKYATDPrylglrsllrTGNLFDLDFLYDELPDglDPFDFEA----FAASPARFYVVATDADTGEAVYFDKP-- 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 505445427 155 arlngrDNDRLLVDVCMATSAAPIL-RSIARLEEPgsggaivdYIDGGL 202
Cdd:cd07208  125 ------DILDDLLDALRASSALPGLfPPVRIDGEP--------YVDGGL 159
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
1-202 5.94e-09

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 56.33  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   1 MNPFRV-LCLDGGGMRGVYQATYLQTFSQRlsqtgfkqsdpGSAFDLLVGTSTGGIVACALASGIHlEKVLELYQTYGKD 79
Cdd:COG4667    1 SNMMKTaLVLEGGGMRGIFTAGVLDALLEE-----------GIPFDLVIGVSAGALNGASYLSRQP-GRARRVITDYATD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  80 ifpRQRLRALPFV--GKYVrGLcsglasgDFALRKVLK--DTFGEETigkvYERRGIGLAITTLDLNRHsSTVFKTPHma 155
Cdd:COG4667   69 ---PRFFSLRNFLrgGNLF-DL-------DFLYDEIPNelLPFDFET----FKASPREFYVVATNADTG-EAEYFSKK-- 130

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505445427 156 rlngrDNDRLLVDVCMATSAAPILRSIARLeepgsGGaiVDYIDGGL 202
Cdd:COG4667  131 -----DDDYDLLDALRASSALPLLYPPVEI-----DG--KRYLDGGV 165
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 7-230 3.44e-08

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: 53.45  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   7 LCLDGGGMRGVYQATYLQTFSQRlsqtgfkqsdpGSAFDLLVGTSTGGIVACALASGihlekvlelyqtygkDIFPRQRL 86
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEA-----------GIEPDIISGTSIGAINGALIAGG---------------DPEAVERL 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  87 RALpfvgkyvrglCSGLASGDFALRKVLKDTFGEETIGKvYERRGIGLAITTLDLNrhsstvfkTPHMARLNgRDNDRLL 166
Cdd:cd07209   55 EKL----------WRELSREDVFLRGLLDRALDFDTLRL-LAILFAGLVIVAVNVL--------TGEPVYFD-DIPDGIL 114

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505445427 167 VDVCMATSAAP-ILRSIARLEEPgsggaivdYIDGGLWANNP--GAVGMIeAHEILQCRGETERPVH 230
Cdd:cd07209  115 PEHLLASAALPpFFPPVEIDGRY--------YWDGGVVDNTPlsPAIDLG-ADEIIVVSLSDKGRDD 172
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 7-207 7.51e-08

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: 51.90  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   7 LCLDGGGMR-----GVYQAtylqtfsqrLSQTGFKQSDpgsafdlLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIF 81
Cdd:cd07207    2 LVFEGGGAKgiayiGALKA---------LEEAGILKKR-------VAGTSAGAITAALLALGYSAADIKDILKETDFAKL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  82 ---PRQRLRALPFVGKYvrglcSGLASGDFA-------LRKVLKDTFGEETIGKVYERRGIGLAITTLDLNRHSSTVF-- 149
Cdd:cd07207   66 ldsPVGLLFLLPSLFKE-----GGLYKGDALeewlrelLKEKTGNSFATSLLRDLDDDLGKDLKVVATDLTTGALVVFsa 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505445427 150 -KTPHMArlngrdndrlLVDVCMATSAAPIL---RSIARLEEpgsggaivdYIDGGLWANNP 207
Cdd:cd07207  141 eTTPDMP----------VAKAVRASMSIPFVfkpVRLAKGDV---------YVDGGVLDNYP 183
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 7-207 2.41e-07

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: 50.03  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   7 LCLDGGGMRGVYQATYLQTFSQRlsqtgfkqsdpGSAFDLLVGTSTGGIVACALASGIhlekvlELYQTYGKDIfPRQRL 86
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRER-----------GPLIDIIAGTSAGAIVAALLASGR------DLEEALLLLL-RLSRE 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  87 RALPFVGKYVRGlcsglasgdFALRKVLKDTFGEETIGKVYERRGIGLAIttldlnrhSSTVFKTPHMaRLNGRDNDRLL 166
Cdd:cd07198   63 VRLRFDGAFPPT---------GRLLGILRQPLLSALPDDAHEDASGKLFI--------SLTRLTDGEN-VLVSDTSKGEL 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 505445427 167 VDVCMATSAAPIlrsIARLEEPGSGGaiVDYIDGGLWANNP 207
Cdd:cd07198  125 WSAVRASSSIPG---YFGPVPLSFRG--RRYGDGGLSNNLP 160
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 6-217 4.89e-07

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: 50.04  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   6 VLCLDGGGMRGVYQATYLQTfsqrLSQTGFKQSDpgsafdlLVGTSTGGIVACALASGIHLEKVLELyqtygkdIFPRQR 85
Cdd:cd07210    2 ALVLSSGFFGFYAHLGFLAA----LLEMGLEPSA-------ISGTSAGALVGGLFASGISPDEMAEL-------LLSLER 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  86 LRALPFVGkyvRGLCSGLASGDfALRKVLKDTFGEETIgkvyERRGIGLAITTLDLNRHSSTVFktphmarlngrdNDRL 165
Cdd:cd07210   64 KDFWMFWD---PPLRGGLLSGD-RFAALLREHLPPDRF----EELRIPLAVSVVDLTSRETLLL------------SEGD 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505445427 166 LVDVCMATSAAPILRSIARLEEpgsggaiVDYIDGGLwANNPGAVGMIEAHE 217
Cdd:cd07210  124 LAEAVAASCAVPPLFQPVEIGG-------RPFVDGGV-ADRLPFDALRPEIE 167
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 7-210 2.41e-06

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: 47.16  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427   7 LCLDGGGMRGVYQATYLQTFSQRlsqtGFKqsdpgsaFDLLVGTSTGGIVACALASGIHLEKVLELYQTYGKDIFPRQRL 86
Cdd:cd07205    3 LALSGGGARGLAHIGVLKALEEA----GIP-------IDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505445427  87 RaLPFVGkYVRGlcsglasgdFALRKVLKDTFGEETIgkvyERRGIGLAITTLDLNRHSSTVFKtphmarlNGrdndrLL 166
Cdd:cd07205   72 T-IPTAG-LLRG---------DKFLELLDEYFGDRDI----EDLWIPFFIVATDLTSGKLVVFR-------SG-----SL 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 505445427 167 VDVCMATSAAPILrsIARLEEPGSggaivDYIDGGLWANNPGAV 210
Cdd:cd07205  125 VRAVRASMSIPGI--FPPVKIDGQ-----LLVDGGVLNNLPVDV 161
 
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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