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Conserved domains on  [gi|48525351|ref|NP_056538|]
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calcium-independent phospholipase A2-gamma isoform 1 [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 ...
 435-741 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 48525351 435 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 514
Cdd:cd07211   1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 515 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGiTPKAFVFRNYGHFPGINSHY 593
Cdd:cd07211  81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 594 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVT 672
Cdd:cd07211 160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48525351 673 YTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 741
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 ...
 435-741 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 48525351 435 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 514
Cdd:cd07211   1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 515 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGiTPKAFVFRNYGHFPGINSHY 593
Cdd:cd07211  81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 594 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVT 672
Cdd:cd07211 160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48525351 673 YTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 741
Cdd:cd07211 240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 442-738 2.25e-54

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: 2.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 442 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:COG3621   7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 522 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARNptcpkVAAVSTIVNRGitpKAFVFRNYGHFPGINSHylggcqYK 600
Cdd:COG3621  86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTP-----VLIPSYDLDNG---KPVFFKSPHAKFDRDRD------FL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 601 MWQAIRASSAAPGYFAEYALGND-----LHQDGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVT 672
Cdd:COG3621 152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVK 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48525351 673 YTSLKTKLSNVINSATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 738
Cdd:COG3621 231 NWGALGWLLPLIDILMDaqSDAVDYQLRQLL-GDRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
443-728 3.90e-27

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 112.59  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351  443 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351  522 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTCpkVAAVStivnrGITPKAFVFRnYGHFPGINSHYlggcQYKM 601
Cdd:NF041079  80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVL--IPAVN-----YTTGKPQVFK-TPHHPDFTRDH----KLKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351  602 WQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SL 676
Cdd:NF041079 147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSL 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48525351  677 KTKLS--------NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 728
Cdd:NF041079 218 KRKRGfldwgggkRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 445-635 9.46e-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: 9.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351   445 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 518
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351   519 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGITPKAFVFRNYGHFPGINSHYLggcq 598
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 48525351   599 ykmWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNP 635
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 ...
 435-741 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 48525351 435 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 514
Cdd:cd07211   1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 515 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGiTPKAFVFRNYGHFPGINSHY 593
Cdd:cd07211  81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 594 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVT 672
Cdd:cd07211 160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGG 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48525351 673 YTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 741
Cdd:cd07211 240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 444-739 5.54e-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: 5.54e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 444 ILSIDGGGTRGVVALQTLRKLVELTQKP--VHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFSqNVIVG 521
Cdd:cd07199   1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP-RVLVT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 522 TVKMSwshafydsqtwenilkdrmgsalmietarnptcpkvaavstivnrgiTPKAFVFRNYGHfpginSHYLGGCQYKM 601
Cdd:cd07199  80 AYDLS-----------------------------------------------TGKPVVFSNYDA-----EEPDDDDDFKL 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 602 WQAIRASSAAPGYFAEYALGND----LHQDGGLLLNNPSALAMHECKCLWP-DVPLECIVSLGTGRYESDVRNTVTYT-- 674
Cdd:cd07199 108 WDVARATSAAPTYFPPAVIESGgdegAFVDGGVAANNPALLALAEALRLLApDKDDILVLSLGTGTSPSSSSSKKASRwg 187

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48525351 675 ---SLKTKLSNVINSATDTE--EVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEK-LDQLQLEGLKYIE 739
Cdd:cd07199 188 glgWGRPLLDILMDAQSDGVdqWLDLLFGSLDSKDNYLRINPPLPGPIPALDDASEAnLLALDSAAFELIE 258
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 442-738 2.25e-54

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: 2.25e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 442 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:COG3621   7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 522 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARNptcpkVAAVSTIVNRGitpKAFVFRNYGHFPGINSHylggcqYK 600
Cdd:COG3621  86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTP-----VLIPSYDLDNG---KPVFFKSPHAKFDRDRD------FL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 601 MWQAIRASSAAPGYFAEYALGND-----LHQDGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVT 672
Cdd:COG3621 152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVK 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48525351 673 YTSLKTKLSNVINSATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 738
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 ...
 442-738 6.06e-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: 6.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 442 IRILSIDGGGTRGVVALQTLRKLVELTQ---------KPvHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSD 512
Cdd:cd07216   1 LNLLSLDGGGVRGLSSLLILKEIMERIDpkegldeppKP-CDYFDLIGGTSTGGLIAIMLGRLRMTVDECIDAYTRLAKK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 513 VFSQ---NVIVGtvkMSWSHAFYDSQTWENILK---DRMG---SALMIEtaRNPTCPKVAAVSTIVNRgiTPKAFVFRNY 583
Cdd:cd07216  80 IFSRkrlRLIIG---DLRTGARFDSKKLAEAIKvilKELGndeDDLLDE--GEEDGCKVFVCATDKDV--TGKAVRLRSY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 584 GHfPGINSHYLggcQYKMWQAIRASSAAPGYFAEYALGNDLHQ--DGGLLLNNPSALAMHECKCLWPDV--PLECIVSLG 659
Cdd:cd07216 153 PS-KDEPSLYK---NATIWEAARATSAAPTFFDPVKIGPGGRTfvDGGLGANNPIREVWSEAVSLWEGLarLVGCLVSIG 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 660 TG--RYESDVRNTVtYTSLKTKLsnvINSATDTEEVHIM----LDGLLPPDTYFRFN-PVMCENIPLDEsrNEKLDQLQL 732
Cdd:cd07216 229 TGtpSIKSLGRSAE-GAGLLKGL---KDLVTDTEAEAKRfsaeHSELDEEGRYFRFNvPHGLEDVGLDE--YEKMEEIVS 302


                ....*.
gi 48525351 733 EGLKYI 738
Cdd:cd07216 303 LTREYL 308
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 444-741 3.00e-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: 3.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 444 ILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGLFH-MPLDECEELYRKLGSDVFsqnviVGT 522
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILA--LALLHgKSLREARRLYLRMKDRVF-----DGS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 523 VKmswshafYDSQTWENILKDRMGSALMIETARNPTcpkvAAVSTIVNRGITPKAFVFRNYGhfPGINSHylgGCQYK-- 600
Cdd:cd07212  74 RP-------YNSEPLEEFLKREFGEDTKMTDVKYPR----LMVTGVLADRQPVQLHLFRNYD--PPEDVE---EPEKNan 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 601 -----------MWQAIRASSAAPGYFAeyALGNDLhqDGGLLLNNPSALAM---HECKCLW-------PDVPLECIVSLG 659
Cdd:cd07212 138 flpptdpaeqlLWRAARSSGAAPTYFR--PMGRFL--DGGLIANNPTLDAMteiHEYNKTLkskgrknKVKKIGCVVSLG 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 660 TGRYESDVRNTV----------TYTSLKT--KLSN-VINSATDTEEVHI--------MLDglLPpdtYFRFNPVMCENIP 718
Cdd:cd07212 214 TGIIPQTPVNTVdvfrpsnpweLAKTVFGakNLGKmVVDQCTASDGAPVdrarawceSIG--IP---YFRFSPPLSKDIM 288

                       330       340
                ....*....|....*....|...
gi 48525351 719 LDESRNEKLDQLQLEGLKYIERN 741
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 ...
 443-752 9.62e-29

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: 117.89  E-value: 9.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 443 RILSIDGGGTRGVVALQTLR----KLVELTQKPVHQL---FDYICGVSTGAIL-AFML-----GLFHMPLDECEELYRKL 509
Cdd:cd07215   1 RILSIDGGGIRGIIPATILVsveeKLQKKTGNPEARLadyFDLVAGTSTGGILtCLYLcpnesGRPKFSAKEALNFYLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 510 GSDVFSQNvIVGTVKMSW--SHAFYDSQTWENILKDRMGSALMIETaRNPTCpkvaavstIVNRGITPKAFVFRNyGHFP 587
Cdd:cd07215  81 GNYIFKKK-IWNKIKSRGgfLNEKYSHKPLEEVLLEYFGDTKLSEL-LKPCL--------ITSYDIERRSPHFFK-SHTA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 588 GINSHYlggcQYKMWQAIRASSAAPGYFAEYALGNDLHQ-----DGGLLLNNPSALAMHECKCLWPDVPlEC-------I 655
Cdd:cd07215 150 IKNEQR----DFYVRDVARATSAAPTYFEPARIHSLTGEkytliDGGVFANNPTLCAYAEARKLKFEQP-GKptakdmiI 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 656 VSLGTGryesdvRNTVTYTSLKTK-----------LSNVINSATDTEEVHI--MLDGLLPPDTYFRFNPVMCENIP-LDE 721
Cdd:cd07215 225 LSLGTG------KNKKSYTYEKVKdwgllgwakplIDIMMDGASQTVDYQLkqIFDAEGDQQQYLRIQPELEDADPeMDD 298

                       330       340       350
                ....*....|....*....|....*....|.
gi 48525351 722 SRNEKLDQLQLEGLKYIERNEQKMKKVAKIL 752
Cdd:cd07215 299 ASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
443-728 3.90e-27

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 112.59  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351  443 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351  522 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTCpkVAAVStivnrGITPKAFVFRnYGHFPGINSHYlggcQYKM 601
Cdd:NF041079  80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVL--IPAVN-----YTTGKPQVFK-TPHHPDFTRDH----KLKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351  602 WQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SL 676
Cdd:NF041079 147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSL 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48525351  677 KTKLS--------NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 728
Cdd:NF041079 218 KRKRGfldwgggkRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 445-635 9.46e-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: 9.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351   445 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 518
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351   519 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGITPKAFVFRNYGHFPGINSHYLggcq 598
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 48525351   599 ykmWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNP 635
Cdd:pfam01734 152 ---ADAVLASSALPGVFPPVRLDGELYVDGGLVDNVP 185
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 443-731 2.37e-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: 2.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 443 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLfDYICGVSTGAILAFMLGLFhMPLDECEELYRKLGSDVFSqNVIVGT 522
Cdd:cd07213   3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQI-DLFAGTSAGSLIALGLALG-YSPRQVLKLYEEVGLKVFS-KSSAGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 523 VKMSwshafyDSQTWENILKDRMGSALmiETARNPTCPKVAAVSTIV--------NRGITPKafVFRNyghFPGINSHyl 594
Cdd:cd07213  80 GAGN------NQYFAAGFLKAFAEVFF--GDLTLGDLKRKVLVPSFQldsgkddpNRRWKPK--LFHN---FPGEPDL-- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 595 ggcQYKMWQAIRASSAAPGYFAEYalgnDLHQDGGLLLNNPSALAM-HECKCLWPDVPLECIV--SLGTGR----YESDV 667
Cdd:cd07213 145 ---DELLVDVCLRSSAAPTYFPSY----QGYVDGGVFANNPSLCAIaQAIGEEGLNIDLKDIVvlSLGTGRppsyLDGAN 217

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48525351 668 RNT----VTYTSLKTKLSNVINSATDTEEVHIMLDgllppDTYFRFNPVMCENIPLDESRN-EKLDQLQ 731
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 ...
 443-661 1.22e-17

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: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 443 RILSIDGGGTRGVVALQTLRKLVELTQK----PVHQL---FDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFS 515
Cdd:cd07217   2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIAL-GMSVTDLLSFYTLNGVNMFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 516 QNVIVGTVKMSWSHAFYDSQTWENIL----------KDRMGSALMIETaRNPTCPKVAAVSTivnrgiTPKAFVFRNYGH 585
Cdd:cd07217  81 KAWLAQRLFLNKLYNQYDPTNLGKKLntvfpettlgDDTLRTLLMIVT-RNATTGSPWPVCN------NPEAKYNDSDRS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 586 FPgiNSHylggcqYKMWQAIRASSAAPGYF----------AEYALgndlhQDGGL-LLNNPS--ALAMHECKCL---WP- 648
Cdd:cd07217 154 DC--NLD------LPLWQLVRASTAAPTFFppevvsiapgTAFVF-----VDGGVtTYNNPAfqAFLMATAKPYklnWEv 220

                       250
                ....*....|....*
gi 48525351 649 --DVPLecIVSLGTG 661
Cdd:cd07217 221 gaDNLL--LVSVGTG 233
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 449-643 5.40e-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: 5.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 449 GGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLfHMPLDECEELYRKLG-SDVFSQNVIVGTVKMSW 527
Cdd:COG1752  13 GGGARGAAHIGVLKALEEAGIPP-----DVIAGTSAGAIVGALYAA-GYSADELEELWRSLDrRDLFDLSLPRRLLRLDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 528 SH---AFYDSQTWENILKDRMGSALmIETARnptcPKVAAVSTIVNRGitpKAFVFRnyghfpginshylggcQYKMWQA 604
Cdd:COG1752  87 GLspgGLLDGDPLRRLLERLLGDRD-FEDLP----IPLAVVATDLETG---REVVFD----------------SGPLADA 142

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 48525351 605 IRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHEC 643
Cdd:COG1752 143 VRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALG 181
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 449-645 2.10e-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: 2.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 449 GGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGlFHMPLDECEELYRKLGSDVFSQNVI-VGTVKMSW 527
Cdd:cd07205   7 GGGARGLAHIGVLKALEEAGIPI-----DIVSGTSAGAIVGALYA-AGYSPEEIEERAKLRSTDLKALSDLtIPTAGLLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 528 SHAFydsqtweNILKDRMGSALMIETARNPtcpkVAAVSTIVNRGitpKAFVFRNyghfpginshylgGCqykMWQAIRA 607
Cdd:cd07205  81 GDKF-------LELLDEYFGDRDIEDLWIP----FFIVATDLTSG---KLVVFRS-------------GS---LVRAVRA 130

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 48525351 608 SSAAPGYFAEYALGNDLHQDGGLLLNNPsALAMHECKC 645
Cdd:cd07205 131 SMSIPGIFPPVKIDGQLLVDGGVLNNLP-VDVLRELGA 167
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 439-661 6.04e-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: 58.60  E-value: 6.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 439 GRGIRILSIDGGGTRGVVA---LQTLR-KLVELTQKPVH--QLFDYICGVSTGAILAFMLGL---FHMPLDECEEL---Y 506
Cdd:cd07214   1 GKFITVLSIDGGGIRGIIPatiLEFLEgKLQELDGPDARiaDYFDVIAGTSTGGLITAMLTApneNKRPLFAAKDIvqfY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 507 RKLGSDVFSQN--VIVGTVKMSWSHAF--YDSQTWENILKDRMGSALMIETARNptcpkvAAVSTIVNRGITPKAFVFRN 582
Cdd:cd07214  81 LENGPKIFPQStgQFEDDRKKLRSLLGpkYDGVYLHDLLNELLGDTRLSDTLTN------VVIPTFDIKLLQPVIFSSSK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 583 YGHFPGINSHYLGGCqykmwqaiRASSAAPGYFAEYAL-----GNDLHQ----DGGLLLNNPSALAMHE--------CKC 645
Cdd:cd07214 155 AKNDKLTNARLADVC--------ISTSAAPTYFPAHYFttedsNGDIREfnlvDGGVAANNPTLLAISEvtkeiikdNPF 226

                       250       260
                ....*....|....*....|
gi 48525351 646 LWPDVPLE----CIVSLGTG 661
Cdd:cd07214 227 FASIKPLDykklLVLSLGTG 246
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 449-641 1.61e-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: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 449 GGGTRGvvALQ--TLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLF-HMPLDECEELYRKLG-SDVFSQNVIVgtvk 524
Cdd:cd07209   5 GGGALG--AYQagVLKALAEAGIEP-----DIISGTSIGAINGALIAGGdPEAVERLEKLWRELSrEDVFLRGLLD---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 525 mswshafydsqtwENILKDRMGSALMIEtarnptcPKVAAVSTIVNrgiTPKAFVFRNYGHFPGInshylggcqykmwQA 604
Cdd:cd07209  74 -------------RALDFDTLRLLAILF-------AGLVIVAVNVL---TGEPVYFDDIPDGILP-------------EH 117

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 48525351 605 IRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMH 641
Cdd:cd07209 118 LLASAALPPFFPPVEIDGRYYWDGGVVDNTPLSPAID 154
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 445-635 1.03e-05

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: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 445 LSIDGGGTRG---VVALQTLRKlveltqkpvHQ-LFDYICGVSTGAILAFMLgLFHMPLDECE--ELYRKLGSDVFSQNV 518
Cdd:cd07198   1 LVLSGGGALGiyhVGVAKALRE---------RGpLIDIIAGTSAGAIVAALL-ASGRDLEEALllLLRLSREVRLRFDGA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 519 IVGTVKMSwshafydsqtweNILKDRMGSALM---IETARNPTCPKVAAVSTIVNrgitpkafvfrnyghfpGINSHYLG 595
Cdd:cd07198  71 FPPTGRLL------------GILRQPLLSALPddaHEDASGKLFISLTRLTDGEN-----------------VLVSDTSK 121

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 48525351 596 GCqykMWQAIRASSAAPGYFA--EYALGNDLHQDGGLLLNNP 635
Cdd:cd07198 122 GE---LWSAVRASSSIPGYFGpvPLSFRGRRYGDGGLSNNLP 160
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 445-650 8.52e-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: 8.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 445 LSIDGGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLFHmpLDECEELYRKLgsdvfSQNVIVGTVK 524
Cdd:cd07228   3 LALGSGGARGWAHIGVLRALEEEGIEI-----DIIAGSSIGALVGALYAAGH--LDALEEWVRSL-----SQRDVLRLLD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48525351 525 MSWSHA-FYDSQTWENILKDRMGsALMIETARNPtcpkVAAVSTIVNRGitpKAFVFRNyghfpginshylgGCqykMWQ 603
Cdd:cd07228  71 LSASRSgLLKGEKVLEYLREIMG-GVTIEELPIP----FAAVATDLQTG---KEVWFRE-------------GS---LID 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 48525351 604 AIRASSAAPGYFAEYALGNDLHQDGGLLlnNPsaLAMHECKCLWPDV 650
Cdd:cd07228 127 AIRASISIPGIFAPVEHNGRLLVDGGVV--NP--IPVSVARALGADI 169
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 445-489 5.61e-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: 5.61e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 48525351 445 LSIDGGGTRGVVALQTLRKLVELTQkpvHQLFDYICGVSTGAILA 489
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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