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Conserved domains on  [gi|568980279|ref|XP_006516237|]
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calcium-independent phospholipase A2-gamma isoform X1 [Mus musculus]

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 ...
 429-685 1.61e-168

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: 484.45  E-value: 1.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 429 DPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 508
Cdd:cd07211    1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 509 TQNV-IVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGqTPKAFVFRNYGHFPGTNSHY 587
Cdd:cd07211   81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 588 LGGCQYKMWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVR-NTST 666
Cdd:cd07211  160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                        250
                 ....*....|....*....
gi 568980279 667 YTSLKTKLSNVISSATDTE 685
Cdd:cd07211  240 YTSLKTKLLNLIDSATDTE 258
 
Name Accession Description Interval E-value
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 429-685 1.61e-168

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: 484.45  E-value: 1.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 429 DPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 508
Cdd:cd07211    1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 509 TQNV-IVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGqTPKAFVFRNYGHFPGTNSHY 587
Cdd:cd07211   81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 588 LGGCQYKMWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVR-NTST 666
Cdd:cd07211  160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                        250
                 ....*....|....*....
gi 568980279 667 YTSLKTKLSNVISSATDTE 685
Cdd:cd07211  240 YTSLKTKLLNLIDSATDTE 258
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 436-659 2.46e-47

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 168.93  E-value: 2.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 436 IRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:COG3621    7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 516 TVKM-SWSHAFYDSNTWEKILKDRIGSALMIEtarnpACPKVAAISTIVNRGqtpKAFVFRNYGHFPGTNSHylggcqYK 594
Cdd:COG3621   86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGD-----LKTPVLIPSYDLDNG---KPVFFKSPHAKFDRDRD------FL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980279 595 MWQAIRASSAAPGYFAEYALGSD-----LHQDGGLLLNNPSALALHECKcIWPDTPLE--CIVSLGTGRYES 659
Cdd:COG3621  152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEAL-KLLGPDLDdiLVLSLGTGTAPR 222
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 439-629 2.52e-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: 109.24  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279  439 LTIDGGGTRGVVALQTLRKLVELTQKpihqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVF---TQNV 512
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIrkrALSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279  513 IVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGQTPKAFVFRNYGHFPGTNSHYLggcq 592
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568980279  593 ykmWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNP 629
Cdd:pfam01734 152 ---ADAVLASSALPGVFPPVRLDGELYVDGGLVDNVP 185
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
437-676 3.52e-27

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 112.59  E-value: 3.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 437 RILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 516 TVKMSWSHAFYDSNTWEKILKDRIGSALmIETARNPACPKVAAISTivnrGQtPKAFVFRNYGHFpgTNSHylggcQYKM 595
Cdd:NF041079  80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVLIPAVNYTT----GK-PQVFKTPHHPDF--TRDH-----KLKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 596 WQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIwPDTPLE--CIVSLGTGryesdvrnTSTYTsLKTK 673
Cdd:NF041079 147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFT-VRPS 216


                 ...
gi 568980279 674 LSN 676
Cdd:NF041079 217 LKR 219
 
Name Accession Description Interval E-value
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 429-685 1.61e-168

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: 484.45  E-value: 1.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 429 DPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 508
Cdd:cd07211    1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 509 TQNV-IVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGqTPKAFVFRNYGHFPGTNSHY 587
Cdd:cd07211   81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 588 LGGCQYKMWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVR-NTST 666
Cdd:cd07211  160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                        250
                 ....*....|....*....
gi 568980279 667 YTSLKTKLSNVISSATDTE 685
Cdd:cd07211  240 YTSLKTKLLNLIDSATDTE 258
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 438-685 1.08e-48

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: 171.36  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 438 ILTIDGGGTRGVVALQTLRKLVELTQKP--IHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFTqNVIVg 515
Cdd:cd07199    1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP-RVLV- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 516 TVkmswshafYDSNTWekilkdrigsalmietarnpacpkvaaistivnrgqtpKAFVFRNYGHFPGTnshylGGCQYKM 595
Cdd:cd07199   79 TA--------YDLSTG--------------------------------------KPVVFSNYDAEEPD-----DDDDFKL 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 596 WQAIRASSAAPGYFAEYALGSD----LHQDGGLLLNNPSALALHECKCIWPDTP-LECIVSLGTGRYESDVRNTSTYT-- 668
Cdd:cd07199  108 WDVARATSAAPTYFPPAVIESGgdegAFVDGGVAANNPALLALAEALRLLAPDKdDILVLSLGTGTSPSSSSSKKASRwg 187

                        250       260
                 ....*....|....*....|
gi 568980279 669 ---SLKTKLSNVISSATDTE 685
Cdd:cd07199  188 glgWGRPLLDILMDAQSDGV 207
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 436-659 2.46e-47

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 168.93  E-value: 2.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 436 IRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:COG3621    7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 516 TVKM-SWSHAFYDSNTWEKILKDRIGSALMIEtarnpACPKVAAISTIVNRGqtpKAFVFRNYGHFPGTNSHylggcqYK 594
Cdd:COG3621   86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGD-----LKTPVLIPSYDLDNG---KPVFFKSPHAKFDRDRD------FL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980279 595 MWQAIRASSAAPGYFAEYALGSD-----LHQDGGLLLNNPSALALHECKcIWPDTPLE--CIVSLGTGRYES 659
Cdd:COG3621  152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEAL-KLLGPDLDdiLVLSLGTGTAPR 222
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 436-685 2.21e-40

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: 150.15  E-value: 2.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 436 IRILTIDGGGTRGVVALQTLRKLVELTQ---------KPiHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSD 506
Cdd:cd07216    1 LNLLSLDGGGVRGLSSLLILKEIMERIDpkegldeppKP-CDYFDLIGGTSTGGLIAIMLGRLRMTVDECIDAYTRLAKK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 507 VFTQ---NVIVGtvkMSWSHAFYDSNTWEKILKDRIG------SALMIEtaRNPACPKVAAISTivNRGQTPKAFVFRNY 577
Cdd:cd07216   80 IFSRkrlRLIIG---DLRTGARFDSKKLAEAIKVILKelgndeDDLLDE--GEEDGCKVFVCAT--DKDVTGKAVRLRSY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 578 GHFPGTNSHYlggcQYKMWQAIRASSAAPGYFAEYALGSDLHQ--DGGLLLNNPSALALHECKCIWPD--TPLECIVSLG 653
Cdd:cd07216  153 PSKDEPSLYK----NATIWEAARATSAAPTFFDPVKIGPGGRTfvDGGLGANNPIREVWSEAVSLWEGlaRLVGCLVSIG 228

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568980279 654 TG--RYESDVRNTStYTSLKTKLsnvISSATDTE 685
Cdd:cd07216  229 TGtpSIKSLGRSAE-GAGLLKGL---KDLVTDTE 258
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 439-629 2.52e-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: 109.24  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279  439 LTIDGGGTRGVVALQTLRKLVELTQKpihqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVF---TQNV 512
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIrkrALSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279  513 IVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGQTPKAFVFRNYGHFPGTNSHYLggcq 592
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568980279  593 ykmWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNP 629
Cdd:pfam01734 152 ---ADAVLASSALPGVFPPVRLDGELYVDGGLVDNVP 185
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
437-676 3.52e-27

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 112.59  E-value: 3.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 437 RILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 516 TVKMSWSHAFYDSNTWEKILKDRIGSALmIETARNPACPKVAAISTivnrGQtPKAFVFRNYGHFpgTNSHylggcQYKM 595
Cdd:NF041079  80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVLIPAVNYTT----GK-PQVFKTPHHPDF--TRDH-----KLKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 596 WQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIwPDTPLE--CIVSLGTGryesdvrnTSTYTsLKTK 673
Cdd:NF041079 147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFT-VRPS 216


                 ...
gi 568980279 674 LSN 676
Cdd:NF041079 217 LKR 219
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 438-686 9.07e-27

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: 111.27  E-value: 9.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 438 ILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAfmLGLFH-MPLDECEELYRKLGSDVFtqnviVGT 516
Cdd:cd07212    1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILA--LALLHgKSLREARRLYLRMKDRVF-----DGS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 517 VKmswshafYDSNTWEKILKDRIGSALMIETARNpacPKVAAISTIVNRgQTPKAFVFRNYG------HFPGTNSH--YL 588
Cdd:cd07212   74 RP-------YNSEPLEEFLKREFGEDTKMTDVKY---PRLMVTGVLADR-QPVQLHLFRNYDppedveEPEKNANFlpPT 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 589 GGCQYKMWQAIRASSAAPGYFAeyALGSDLhqDGGLLLNNPSALAL---HECKCIW-------PDTPLECIVSLGTGRYE 658
Cdd:cd07212  143 DPAEQLLWRAARSSGAAPTYFR--PMGRFL--DGGLIANNPTLDAMteiHEYNKTLkskgrknKVKKIGCVVSLGTGIIP 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568980279 659 S------DVRNTSTYTSLKTKLSN-------VISSATDTEG 686
Cdd:cd07212  219 QtpvntvDVFRPSNPWELAKTVFGaknlgkmVVDQCTASDG 259
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 437-655 2.75e-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: 86.78  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 437 RILTIDGGGTRGVVALQTLRKLVELTQK----PIHQL---FDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFT 509
Cdd:cd07217    2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIAL-GMSVTDLLSFYTLNGVNMFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 510 QNVIVGTVKMSWSHAFYDSNTWEKIL----------KDRIGSALMIETaRNPACPKVAAIStivnrgQTPKAFVFRNYGH 579
Cdd:cd07217   81 KAWLAQRLFLNKLYNQYDPTNLGKKLntvfpettlgDDTLRTLLMIVT-RNATTGSPWPVC------NNPEAKYNDSDRS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 580 FPgtNSHylggcqYKMWQAIRASSAAPGYFA----EYALGSD-LHQDGGL-LLNNPSALALHECKCI-----WP---DTP 645
Cdd:cd07217  154 DC--NLD------LPLWQLVRASTAAPTFFPpevvSIAPGTAfVFVDGGVtTYNNPAFQAFLMATAKpyklnWEvgaDNL 225

                        250
                 ....*....|
gi 568980279 646 LecIVSLGTG 655
Cdd:cd07217  226 L--LVSVGTG 233
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 437-657 3.01e-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: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 85.80  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 437 RILTIDGGGTRGVVALQTLRKLVELTQKPIHQLfDYICGVSTGAILAFMLGLFhMPLDECEELYRKLGSDVFtQNVIVGT 516
Cdd:cd07213    3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQI-DLFAGTSAGSLIALGLALG-YSPRQVLKLYEEVGLKVF-SKSSAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 517 VKMSWShafYDSNTWEKILKDRIGSALMIETARNPACpkVAAI---STIVNRGQTPKAFVFRNyghFPGTNSHylggcQY 593
Cdd:cd07213   80 GAGNNQ---YFAAGFLKAFAEVFFGDLTLGDLKRKVL--VPSFqldSGKDDPNRRWKPKLFHN---FPGEPDL-----DE 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980279 594 KMWQAIRASSAAPGYFAEYalgsDLHQDGGLLLNNPSALAL-HECKCIWPDTPLECIV--SLGTGRY 657
Cdd:cd07213  147 LLVDVCLRSSAAPTYFPSY----QGYVDGGVFANNPSLCAIaQAIGEEGLNIDLKDIVvlSLGTGRP 209
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 437-673 5.98e-18

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: 85.54  E-value: 5.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 437 RILTIDGGGTRGVVALQTLR----KLVELTQKP---IHQLFDYICGVSTGAIL-AFML-----GLFHMPLDECEELYRKL 503
Cdd:cd07215    1 RILSIDGGGIRGIIPATILVsveeKLQKKTGNPearLADYFDLVAGTSTGGILtCLYLcpnesGRPKFSAKEALNFYLER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 504 GSDVFTQNvIVGTVKMSW--SHAFYDSNTWEKILKDRIGSALMIETaRNPACpkvaAISTIVNRGqtpKAFVFRNygHFP 581
Cdd:cd07215   81 GNYIFKKK-IWNKIKSRGgfLNEKYSHKPLEEVLLEYFGDTKLSEL-LKPCL----ITSYDIERR---SPHFFKS--HTA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 582 GTNSHYlggcQYKMWQAIRASSAAPGYFAEYALGSDLHQ-----DGGLLLNNPSALALHECKCIWPDTPlEC-------I 649
Cdd:cd07215  150 IKNEQR----DFYVRDVARATSAAPTYFEPARIHSLTGEkytliDGGVFANNPTLCAYAEARKLKFEQP-GKptakdmiI 224

                        250       260
                 ....*....|....*....|....
gi 568980279 650 VSLGTGryesdvRNTSTYTSLKTK 673
Cdd:cd07215  225 LSLGTG------KNKKSYTYEKVK 242
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 443-637 5.69e-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: 5.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 443 GGGTRGVVALQTLRKLVELtqkPIHqlFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLG-SDVFTQNVIVGTVKMSW 521
Cdd:COG1752   13 GGGARGAAHIGVLKALEEA---GIP--PDVIAGTSAGAIVGALYAA-GYSADELEELWRSLDrRDLFDLSLPRRLLRLDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 522 SH---AFYDSNTWEKILKDRIGSALmIETARnpacPKVAAISTIVNRGqtpKAFVFRnyghfpgtnshylggcQYKMWQA 598
Cdd:COG1752   87 GLspgGLLDGDPLRRLLERLLGDRD-FEDLP----IPLAVVATDLETG---REVVFD----------------SGPLADA 142

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568980279 599 IRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHEC 637
Cdd:COG1752  143 VRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALG 181
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 433-655 4.18e-10

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: 62.07  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 433 GRGIRILTIDGGGTRGVVALQTLRKLVELTQK------PIHQLFDYICGVSTGAILAFMLGL---FHMPLDECEEL---Y 500
Cdd:cd07214    1 GKFITVLSIDGGGIRGIIPATILEFLEGKLQEldgpdaRIADYFDVIAGTSTGGLITAMLTApneNKRPLFAAKDIvqfY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 501 RKLGSDVFTQN--VIVGTVKMSWSHAF--YDSNTWEKILKDRIGSALMIETARNpacpkvAAISTIVNRGQTPKAFVFRN 576
Cdd:cd07214   81 LENGPKIFPQStgQFEDDRKKLRSLLGpkYDGVYLHDLLNELLGDTRLSDTLTN------VVIPTFDIKLLQPVIFSSSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 577 YGHFPGTNSHYLGGCqykmwqaiRASSAAPGYFAEYAL-----GSDLHQ----DGGLLLNNPSALALHE--------CKC 639
Cdd:cd07214  155 AKNDKLTNARLADVC--------ISTSAAPTYFPAHYFttedsNGDIREfnlvDGGVAANNPTLLAISEvtkeiikdNPF 226

                        250       260
                 ....*....|....*....|
gi 568980279 640 IWPDTPLE----CIVSLGTG 655
Cdd:cd07214  227 FASIKPLDykklLVLSLGTG 246
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 443-633 1.97e-08

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 54.47  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 443 GGGTRGVVALQTLRKLVELTQKPihqlfDYICGVSTGAILAFMLGlFHMPLDECEELYRKLGSDVFTQNVI-VGTVKMSW 521
Cdd:cd07205    7 GGGARGLAHIGVLKALEEAGIPI-----DIVSGTSAGAIVGALYA-AGYSPEEIEERAKLRSTDLKALSDLtIPTAGLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 522 SHAFYDSNtwEKILKDRigsalMIETARNPacpkVAAISTIVNRGQTpkaFVFRNyghfpgtnshylgGCqykMWQAIRA 601
Cdd:cd07205   81 GDKFLELL--DEYFGDR-----DIEDLWIP----FFIVATDLTSGKL---VVFRS-------------GS---LVRAVRA 130

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568980279 602 SSAAPGYFAEYALGSDLHQDGGLLLNNPSALA 633
Cdd:cd07205  131 SMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVL 162
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 439-629 3.34e-06

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: 48.04  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 439 LTIDGGGTRGVV---ALQtlrklvELTQKPIhqLFDYICGVSTGAILAFMLGL---------FHMPLDECEELYRKLGSD 506
Cdd:cd07207    2 LVFEGGGAKGIAyigALK------ALEEAGI--LKKRVAGTSAGAITAALLALgysaadikdILKETDFAKLLDSPVGLL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 507 VFTQNVIVGtvkMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACP---KVAAISTIVNRGqtpKAFVFrnYG-HFPg 582
Cdd:cd07207   74 FLLPSLFKE---GGLYKGDALEEWLRELLKEKTGNSFATSLLRDLDDDlgkDLKVVATDLTTG---ALVVF--SAeTTP- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568980279 583 tnshylggcQYKMWQAIRASSAAPGYFA--EYALGsDLHQDGGLLLNNP 629
Cdd:cd07207  145 ---------DMPVAKAVRASMSIPFVFKpvRLAKG-DVYVDGGVLDNYP 183
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 439-634 1.65e-03

Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 39.95  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 439 LTIDGGGTRGVVALQTLRKLVElTQKPIhqlfDYICGVSTGAILAFMLGLFHmpLDECEELYRKLgsdvfTQNVIVGTVK 518
Cdd:cd07228    3 LALGSGGARGWAHIGVLRALEE-EGIEI----DIIAGSSIGALVGALYAAGH--LDALEEWVRSL-----SQRDVLRLLD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980279 519 MSWSHA-FYDSNTWEKILKDRIGsALMIETARNPacpkVAAISTIVNRGqtpKAFVFRNyghfpgtnshylgGCqykMWQ 597
Cdd:cd07228   71 LSASRSgLLKGEKVLEYLREIMG-GVTIEELPIP----FAAVATDLQTG---KEVWFRE-------------GS---LID 126

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568980279 598 AIRASSAAPGYFAEYALGSDLHQDGGLLlnNPSALAL 634
Cdd:cd07228  127 AIRASISIPGIFAPVEHNGRLLVDGGVV--NPIPVSV 161
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 439-483 2.12e-03

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


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 39.32  E-value: 2.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568980279 439 LTIDGGGTRGVVALQTLRKLVELTqkpIHQLFDYICGVSTGAILA 483
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERG---LLDCVTYLAGTSGGAWVA 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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