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Conserved domains on  [gi|365192579|ref|NP_001242939|]
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calcium-independent phospholipase A2-gamma isoform 3 [Homo sapiens]

Protein Classification

Pat_PNPLA8 domain-containing protein( domain architecture ID 10163386)

Pat_PNPLA8 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 335-641 0e+00

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: 579.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 335 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 414
Cdd:cd07211    1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 415 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGiTPKAFVFRNYGHFPGINSHY 493
Cdd:cd07211   81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 494 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVT 572
Cdd:cd07211  160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 365192579 573 YTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 641
Cdd:cd07211  240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
 
Name Accession Description Interval E-value
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 335-641 0e+00

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: 579.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 335 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 414
Cdd:cd07211    1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 415 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGiTPKAFVFRNYGHFPGINSHY 493
Cdd:cd07211   81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 494 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVT 572
Cdd:cd07211  160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 365192579 573 YTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 641
Cdd:cd07211  240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 342-638 6.84e-55

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 189.73  E-value: 6.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 342 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 421
Cdd:COG3621    7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 422 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARNptcpkVAAVSTIVNRGitpKAFVFRNYGHFPGINSHylggcqYK 500
Cdd:COG3621   86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTP-----VLIPSYDLDNG---KPVFFKSPHAKFDRDRD------FL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 501 MWQAIRASSAAPGYFAEYALGND-----LHQDGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVT 572
Cdd:COG3621  152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVK 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365192579 573 YTSLKTKLSNVINSATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 638
Cdd:COG3621  231 NWGALGWLLPLIDILMDaqSDAVDYQLRQLL-GDRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
343-628 2.83e-27

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 112.98  E-value: 2.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 343 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 421
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 422 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTCpkVAAVStivnrGITPKAFVFRnYGHFPGINSHYlggcQYKM 501
Cdd:NF041079  80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVL--IPAVN-----YTTGKPQVFK-TPHHPDFTRDH----KLKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 502 WQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SL 576
Cdd:NF041079 147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSL 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 365192579 577 KTKLS--------NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 628
Cdd:NF041079 218 KRKRGfldwgggkRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 345-535 7.90e-27

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 108.08  E-value: 7.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579  345 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 418
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579  419 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGITPKAFVFRNYGHFPGINSHYLggcq 498
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 365192579  499 ykmWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNP 535
Cdd:pfam01734 152 ---ADAVLASSALPGVFPPVRLDGELYVDGGLVDNVP 185
 
Name Accession Description Interval E-value
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 335-641 0e+00

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: 579.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 335 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 414
Cdd:cd07211    1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 415 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGiTPKAFVFRNYGHFPGINSHY 493
Cdd:cd07211   81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 494 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVT 572
Cdd:cd07211  160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 365192579 573 YTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 641
Cdd:cd07211  240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 344-639 1.55e-57

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: 195.24  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 344 ILSIDGGGTRGVVALQTLRKLVELTQKP--VHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFSqNVIVG 421
Cdd:cd07199    1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP-RVLVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 422 TVKMSwshafydsqtwenilkdrmgsalmietarnptcpkvaavstivnrgiTPKAFVFRNYGHfpginSHYLGGCQYKM 501
Cdd:cd07199   80 AYDLS-----------------------------------------------TGKPVVFSNYDA-----EEPDDDDDFKL 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 502 WQAIRASSAAPGYFAEYALGND----LHQDGGLLLNNPSALAMHECKCLWP-DVPLECIVSLGTGRYESDVRNTVTYT-- 574
Cdd:cd07199  108 WDVARATSAAPTYFPPAVIESGgdegAFVDGGVAANNPALLALAEALRLLApDKDDILVLSLGTGTSPSSSSSKKASRwg 187

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 365192579 575 ---SLKTKLSNVINSATDTE--EVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEK-LDQLQLEGLKYIE 639
Cdd:cd07199  188 glgWGRPLLDILMDAQSDGVdqWLDLLFGSLDSKDNYLRINPPLPGPIPALDDASEAnLLALDSAAFELIE 258
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 342-638 6.84e-55

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 189.73  E-value: 6.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 342 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 421
Cdd:COG3621    7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 422 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARNptcpkVAAVSTIVNRGitpKAFVFRNYGHFPGINSHylggcqYK 500
Cdd:COG3621   86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTP-----VLIPSYDLDNG---KPVFFKSPHAKFDRDRD------FL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 501 MWQAIRASSAAPGYFAEYALGND-----LHQDGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVT 572
Cdd:COG3621  152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVK 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365192579 573 YTSLKTKLSNVINSATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 638
Cdd:COG3621  231 NWGALGWLLPLIDILMDaqSDAVDYQLRQLL-GDRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 342-638 2.30e-49

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: 175.18  E-value: 2.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 342 IRILSIDGGGTRGVVALQTLRKLVELTQ---------KPvHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSD 412
Cdd:cd07216    1 LNLLSLDGGGVRGLSSLLILKEIMERIDpkegldeppKP-CDYFDLIGGTSTGGLIAIMLGRLRMTVDECIDAYTRLAKK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 413 VFSQ---NVIVGtvkMSWSHAFYDSQTWENILK---DRMG---SALMIEtaRNPTCPKVAAVSTIVNRgiTPKAFVFRNY 483
Cdd:cd07216   80 IFSRkrlRLIIG---DLRTGARFDSKKLAEAIKvilKELGndeDDLLDE--GEEDGCKVFVCATDKDV--TGKAVRLRSY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 484 GHfPGINSHYLggcQYKMWQAIRASSAAPGYFAEYALGNDLHQ--DGGLLLNNPSALAMHECKCLWPDV--PLECIVSLG 559
Cdd:cd07216  153 PS-KDEPSLYK---NATIWEAARATSAAPTFFDPVKIGPGGRTfvDGGLGANNPIREVWSEAVSLWEGLarLVGCLVSIG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 560 TG--RYESDVRNTVtYTSLKTKLsnvINSATDTEEVHIM----LDGLLPPDTYFRFN-PVMCENIPLDEsrNEKLDQLQL 632
Cdd:cd07216  229 TGtpSIKSLGRSAE-GAGLLKGL---KDLVTDTEAEAKRfsaeHSELDEEGRYFRFNvPHGLEDVGLDE--YEKMEEIVS 302


                 ....*.
gi 365192579 633 EGLKYI 638
Cdd:cd07216  303 LTREYL 308
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 344-641 2.14e-33

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: 130.53  E-value: 2.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 344 ILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGLFH-MPLDECEELYRKLGSDVFsqnviVGT 422
Cdd:cd07212    1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILA--LALLHgKSLREARRLYLRMKDRVF-----DGS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 423 VKmswshafYDSQTWENILKDRMGSALMIETARNPTcpkvAAVSTIVNRGITPKAFVFRNYGhfPGINSHylgGCQYK-- 500
Cdd:cd07212   74 RP-------YNSEPLEEFLKREFGEDTKMTDVKYPR----LMVTGVLADRQPVQLHLFRNYD--PPEDVE---EPEKNan 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 501 -----------MWQAIRASSAAPGYFAeyALGNDLhqDGGLLLNNPSALAM---HECKCLW-------PDVPLECIVSLG 559
Cdd:cd07212  138 flpptdpaeqlLWRAARSSGAAPTYFR--PMGRFL--DGGLIANNPTLDAMteiHEYNKTLkskgrknKVKKIGCVVSLG 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 560 TGRYESDVRNTV----------TYTSLKT--KLSN-VINSATDTEEVHI--------MLDglLPpdtYFRFNPVMCENIP 618
Cdd:cd07212  214 TGIIPQTPVNTVdvfrpsnpweLAKTVFGakNLGKmVVDQCTASDGAPVdrarawceSIG--IP---YFRFSPPLSKDIM 288

                        330       340
                 ....*....|....*....|...
gi 365192579 619 LDESRNEKLDQLQLEGLKYIERN 641
Cdd:cd07212  289 LDETDDEDLVNMLWDTEVYIYTH 311
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 343-652 1.66e-28

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: 116.74  E-value: 1.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 343 RILSIDGGGTRGVVALQTLR----KLVELTQKPVHQL---FDYICGVSTGAIL-AFML-----GLFHMPLDECEELYRKL 409
Cdd:cd07215    1 RILSIDGGGIRGIIPATILVsveeKLQKKTGNPEARLadyFDLVAGTSTGGILtCLYLcpnesGRPKFSAKEALNFYLER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 410 GSDVFSQNvIVGTVKMSW--SHAFYDSQTWENILKDRMGSALMIETARnPTCpkvaavstIVNRGITPKAFVFRNyGHFP 487
Cdd:cd07215   81 GNYIFKKK-IWNKIKSRGgfLNEKYSHKPLEEVLLEYFGDTKLSELLK-PCL--------ITSYDIERRSPHFFK-SHTA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 488 GINSHYlggcQYKMWQAIRASSAAPGYFAEYALGNDLHQ-----DGGLLLNNPSALAMHECKCLWPDVPlEC-------I 555
Cdd:cd07215  150 IKNEQR----DFYVRDVARATSAAPTYFEPARIHSLTGEkytliDGGVFANNPTLCAYAEARKLKFEQP-GKptakdmiI 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 556 VSLGTGryesdvRNTVTYTSLKTK-----------LSNVINSATDTEEVHI--MLDGLLPPDTYFRFNPVMCENIP-LDE 621
Cdd:cd07215  225 LSLGTG------KNKKSYTYEKVKdwgllgwakplIDIMMDGASQTVDYQLkqIFDAEGDQQQYLRIQPELEDADPeMDD 298

                        330       340       350
                 ....*....|....*....|....*....|.
gi 365192579 622 SRNEKLDQLQLEGLKYIERNEQKMKKVAKIL 652
Cdd:cd07215  299 ASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
343-628 2.83e-27

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 112.98  E-value: 2.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 343 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 421
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 422 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTCpkVAAVStivnrGITPKAFVFRnYGHFPGINSHYlggcQYKM 501
Cdd:NF041079  80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVL--IPAVN-----YTTGKPQVFK-TPHHPDFTRDH----KLKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 502 WQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SL 576
Cdd:NF041079 147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSL 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 365192579 577 KTKLS--------NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 628
Cdd:NF041079 218 KRKRGfldwgggkRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 345-535 7.90e-27

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 108.08  E-value: 7.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579  345 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 418
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579  419 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGITPKAFVFRNYGHFPGINSHYLggcq 498
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 365192579  499 ykmWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNP 535
Cdd:pfam01734 152 ---ADAVLASSALPGVFPPVRLDGELYVDGGLVDNVP 185
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 343-631 1.95e-22

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: 98.13  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 343 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLfDYICGVSTGAILAFMLGLFhMPLDECEELYRKLGSDVFSqNVIVGT 422
Cdd:cd07213    3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQI-DLFAGTSAGSLIALGLALG-YSPRQVLKLYEEVGLKVFS-KSSAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 423 VKMSwshafyDSQTWENILKDRMGSALmiETARNPTCPKVAAVSTIV--------NRGITPKafVFRNyghFPGINSHyl 494
Cdd:cd07213   80 GAGN------NQYFAAGFLKAFAEVFF--GDLTLGDLKRKVLVPSFQldsgkddpNRRWKPK--LFHN---FPGEPDL-- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 495 ggcQYKMWQAIRASSAAPGYFAEYalgnDLHQDGGLLLNNPSALAM-HECKCLWPDVPLECIV--SLGTGR----YESDV 567
Cdd:cd07213  145 ---DELLVDVCLRSSAAPTYFPSY----QGYVDGGVFANNPSLCAIaQAIGEEGLNIDLKDIVvlSLGTGRppsyLDGAN 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 365192579 568 RNT----VTYTSLKTKLSNVINSATDTEEVHIMLDgllppDTYFRFNPVMCENIPLDESRN-EKLDQLQ 631
Cdd:cd07213  218 GYGdwglLQWLPDLLDLFMDAGVDAADFQCRQLLG-----ERYFRLDPVLPANIDLDDNKQiEELVEIA 281
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 343-561 9.99e-18

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: 85.24  E-value: 9.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 343 RILSIDGGGTRGVVALQTLRKLVELTQK----PVHQL---FDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFS 415
Cdd:cd07217    2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIAL-GMSVTDLLSFYTLNGVNMFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 416 QNVIVGTVKMSWSHAFYDSQTWENIL----------KDRMGSALMIETaRNPTCPKVAAVSTivnrgiTPKAFVFRNYGH 485
Cdd:cd07217   81 KAWLAQRLFLNKLYNQYDPTNLGKKLntvfpettlgDDTLRTLLMIVT-RNATTGSPWPVCN------NPEAKYNDSDRS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 486 FPgiNSHylggcqYKMWQAIRASSAAPGYF----------AEYALgndlhQDGGL-LLNNPS--ALAMHECKCL---WP- 548
Cdd:cd07217  154 DC--NLD------LPLWQLVRASTAAPTFFppevvsiapgTAFVF-----VDGGVtTYNNPAfqAFLMATAKPYklnWEv 220

                        250
                 ....*....|....*
gi 365192579 549 --DVPLecIVSLGTG 561
Cdd:cd07217  221 gaDNLL--LVSVGTG 233
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 349-543 4.51e-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: 4.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 349 GGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLfHMPLDECEELYRKLG-SDVFSQNVIVGTVKMSW 427
Cdd:COG1752   13 GGGARGAAHIGVLKALEEAGIPP-----DVIAGTSAGAIVGALYAA-GYSADELEELWRSLDrRDLFDLSLPRRLLRLDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 428 SH---AFYDSQTWENILKDRMGSALmIETARnptcPKVAAVSTIVNRGitpKAFVFRnyghfpginshylggcQYKMWQA 504
Cdd:COG1752   87 GLspgGLLDGDPLRRLLERLLGDRD-FEDLP----IPLAVVATDLETG---REVVFD----------------SGPLADA 142

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 365192579 505 IRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHEC 543
Cdd:COG1752  143 VRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALG 181
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 349-545 1.79e-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: 57.56  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 349 GGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGlFHMPLDECEELYRKLGSDVFSQNVI-VGTVKMSW 427
Cdd:cd07205    7 GGGARGLAHIGVLKALEEAGIPI-----DIVSGTSAGAIVGALYA-AGYSPEEIEERAKLRSTDLKALSDLtIPTAGLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 428 SHAFydsqtweNILKDRMGSALMIETARNPtcpkVAAVSTIVNRGitpKAFVFRNyghfpginshylgGCqykMWQAIRA 507
Cdd:cd07205   81 GDKF-------LELLDEYFGDRDIEDLWIP----FFIVATDLTSG---KLVVFRS-------------GS---LVRAVRA 130

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 365192579 508 SSAAPGYFAEYALGNDLHQDGGLLLNNPsALAMHECKC 545
Cdd:cd07205  131 SMSIPGIFPPVKIDGQLLVDGGVLNNLP-VDVLRELGA 167
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 339-561 6.60e-09

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: 58.22  E-value: 6.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 339 GRGIRILSIDGGGTRGVVA---LQTLR-KLVELTQKPVH--QLFDYICGVSTGAILAFMLGL---FHMPLDECEEL---Y 406
Cdd:cd07214    1 GKFITVLSIDGGGIRGIIPatiLEFLEgKLQELDGPDARiaDYFDVIAGTSTGGLITAMLTApneNKRPLFAAKDIvqfY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 407 RKLGSDVFSQN--VIVGTVKMSWSHAF--YDSQTWENILKDRMGSALMIETARNptcpkvAAVSTIVNRGITPKAFVFRN 482
Cdd:cd07214   81 LENGPKIFPQStgQFEDDRKKLRSLLGpkYDGVYLHDLLNELLGDTRLSDTLTN------VVIPTFDIKLLQPVIFSSSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 483 YGHFPGINSHYLGGCqykmwqaiRASSAAPGYFAEYAL-----GNDLHQ----DGGLLLNNPSALAMHE--------CKC 545
Cdd:cd07214  155 AKNDKLTNARLADVC--------ISTSAAPTYFPAHYFttedsNGDIREfnlvDGGVAANNPTLLAISEvtkeiikdNPF 226

                        250       260
                 ....*....|....*....|
gi 365192579 546 LWPDVPLE----CIVSLGTG 561
Cdd:cd07214  227 FASIKPLDykklLVLSLGTG 246
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 349-541 1.36e-06

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: 49.60  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 349 GGGTRGvvALQ--TLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLF-HMPLDECEELYRKLG-SDVFSQNVIVgtvk 424
Cdd:cd07209    5 GGGALG--AYQagVLKALAEAGIEP-----DIISGTSIGAINGALIAGGdPEAVERLEKLWRELSrEDVFLRGLLD---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 425 mswshafydsqtwENILKDRMGSALMIEtarnptcPKVAAVSTIVNrgiTPKAFVFRNYGHFPGInshylggcqykmwQA 504
Cdd:cd07209   74 -------------RALDFDTLRLLAILF-------AGLVIVAVNVL---TGEPVYFDDIPDGILP-------------EH 117

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 365192579 505 IRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMH 541
Cdd:cd07209  118 LLASAALPPFFPPVEIDGRYYWDGGVVDNTPLSPAID 154
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 345-535 8.83e-06

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: 46.57  E-value: 8.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 345 LSIDGGGTRG---VVALQTLRKlveltqkpvHQ-LFDYICGVSTGAILAFMLgLFHMPLDECE--ELYRKLGSDVFSQNV 418
Cdd:cd07198    1 LVLSGGGALGiyhVGVAKALRE---------RGpLIDIIAGTSAGAIVAALL-ASGRDLEEALllLLRLSREVRLRFDGA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 419 IVGTVKMSwshafydsqtweNILKDRMGSALM---IETARNPTCPKVAAVSTIVNrgitpkafvfrnyghfpGINSHYLG 495
Cdd:cd07198   71 FPPTGRLL------------GILRQPLLSALPddaHEDASGKLFISLTRLTDGEN-----------------VLVSDTSK 121

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 365192579 496 GCqykMWQAIRASSAAPGYFA--EYALGNDLHQDGGLLLNNP 535
Cdd:cd07198  122 GE---LWSAVRASSSIPGYFGpvPLSFRGRRYGDGGLSNNLP 160
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 345-550 7.27e-05

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: 43.80  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 345 LSIDGGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLFHmpLDECEELYRKLgsdvfSQNVIVGTVK 424
Cdd:cd07228    3 LALGSGGARGWAHIGVLRALEEEGIEI-----DIIAGSSIGALVGALYAAGH--LDALEEWVRSL-----SQRDVLRLLD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365192579 425 MSWSHA-FYDSQTWENILKDRMGsALMIETARNPtcpkVAAVSTIVNRGitpKAFVFRNyghfpginshylgGCqykMWQ 503
Cdd:cd07228   71 LSASRSgLLKGEKVLEYLREIMG-GVTIEELPIP----FAAVATDLQTG---KEVWFRE-------------GS---LID 126

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 365192579 504 AIRASSAAPGYFAEYALGNDLHQDGGLLlnNPsaLAMHECKCLWPDV 550
Cdd:cd07228  127 AIRASISIPGIFAPVEHNGRLLVDGGVV--NP--IPVSVARALGADI 169
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 345-389 4.81e-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: 41.25  E-value: 4.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 365192579 345 LSIDGGGTRGVVALQTLRKLVELTQkpvHQLFDYICGVSTGAILA 389
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGL---LDCVTYLAGTSGGAWVA 42
 
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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