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Conserved domains on  [gi|1859677021|sp|D3ZRC4|]
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RecName: Full=Calcium-independent phospholipase A2-gamma; AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 gamma; Short=iPLA2-gamma; AltName: Full=Patatin-like phospholipase domain-containing protein 8

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 ...
429-735 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: 568.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 429 DPVKGRGIRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 508
Cdd:cd07211     1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 509 TQNV-IVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGqTPKAFVFRNYGHFPGTNSHY 587
Cdd:cd07211    81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 588 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTT-T 666
Cdd:cd07211   160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRLETgG 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859677021 667 YTSLKTKLSNVISSATDTEEVHIMLDGLLPADTYFRFNPVICENIPLDESRNEKLDQLQLEGMKYLERN 735
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 ...
429-735 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: 568.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 429 DPVKGRGIRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 508
Cdd:cd07211     1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 509 TQNV-IVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGqTPKAFVFRNYGHFPGTNSHY 587
Cdd:cd07211    81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 588 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTT-T 666
Cdd:cd07211   160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRLETgG 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859677021 667 YTSLKTKLSNVISSATDTEEVHIMLDGLLPADTYFRFNPVICENIPLDESRNEKLDQLQLEGMKYLERN 735
Cdd:cd07211   240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
436-732 2.75e-55

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 192.04  E-value: 2.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 436 IRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:COG3621     7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 516 TVKM-SWSHAFYDSHTWEKILKDKVGSALMIEtARDPLCpkVAAVStIVNRgqtpKAFVFRNYGHFPGTNSHylggcqYK 594
Cdd:COG3621    86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGD-LKTPVL--IPSYD-LDNG----KPVFFKSPHAKFDRDRD------FL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 595 MWQAIRASSAAPGYFAEYALGND-----LHQDGGLLLNNPSALALHECKcIWPDTPLE--CIVSLGTGryesdvRNTTTY 667
Cdd:COG3621   152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEAL-KLLGPDLDdiLVLSLGTG------TAPRSI 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859677021 668 TSLKTK----------LSNVISSATdTEEVHIMLDGLLPaDTYFRFNPVICENIPLDESrNEKLDQLQLEGMKYL 732
Cdd:COG3621   225 PYKKVKnwgalgwllpLIDILMDAQ-SDAVDYQLRQLLG-DRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
437-722 8.76e-29

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 117.60  E-value: 8.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 437 RILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 516 TVKMSWSHAFYDSHTWEKILKDKVGSALmIETARDPLCpkVAAVStiVNRGQtPKAFVFRNYGHFpgTNSHylggcQYKM 595
Cdd:NF041079   80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVL--IPAVN--YTTGK-PQVFKTPHHPDF--TRDH-----KLKL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 596 WQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIwPDTPLE--CIVSLGTGryesdvrnTTTYT---SL 670
Cdd:NF041079  147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSL 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859677021 671 KTKLS--------NVISSATDTEE--VHIMLDGLLPaDTYFRfnpvICENIPLDESRNEKLD 722
Cdd:NF041079  218 KRKRGfldwgggkRLFELTMSAQEqlVDFMLQHILG-DRYLR----IDDVPTNEQAKDLGLD 274
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
439-629 1.34e-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: 110.39  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGVVALQTLRKLVELTQKpihqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVF---TQNV 512
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIrkrALSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 513 IVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGQTPKAFVFRNYGHFPGTNSHYLggcq 592
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1859677021 593 ykmWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNP 629
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 ...
429-735 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: 568.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 429 DPVKGRGIRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 508
Cdd:cd07211     1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 509 TQNV-IVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGqTPKAFVFRNYGHFPGTNSHY 587
Cdd:cd07211    81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACVSTQVNRT-PLKPYVFRNYNHPPGTRSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 588 LGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTT-T 666
Cdd:cd07211   160 LGSCKHKLWEAIRASSAAPGYFEEFKLGNNLHQDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRLETgG 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859677021 667 YTSLKTKLSNVISSATDTEEVHIMLDGLLPADTYFRFNPVICENIPLDESRNEKLDQLQLEGMKYLERN 735
Cdd:cd07211   240 YTSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
438-733 4.28e-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: 195.63  E-value: 4.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 438 ILAIDGGGTRGVVALQTLRKLVELTQKP--IHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFTqNVIVG 515
Cdd:cd07199     1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP-RVLVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 516 TVKMSwshafydshtwekilkdkvgsalmietardplcpkvaavstivnrgqTPKAFVFRNYGHFPGTnshylGGCQYKM 595
Cdd:cd07199    80 AYDLS-----------------------------------------------TGKPVVFSNYDAEEPD-----DDDDFKL 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 596 WQAIRASSAAPGYFAEYALGND----LHQDGGLLLNNPSALALHECKCIWPDTP-LECIVSLGTGRYESDVRNTTTYT-- 668
Cdd:cd07199   108 WDVARATSAAPTYFPPAVIESGgdegAFVDGGVAANNPALLALAEALRLLAPDKdDILVLSLGTGTSPSSSSSKKASRwg 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1859677021 669 ---SLKTKLSNVISSATDTE--EVHIMLDGLLPADTYFRFNPVICENIPLDESRNEK-LDQLQLEGMKYLE 733
Cdd:cd07199   188 glgWGRPLLDILMDAQSDGVdqWLDLLFGSLDSKDNYLRINPPLPGPIPALDDASEAnLLALDSAAFELIE 258
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
436-732 2.75e-55

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 192.04  E-value: 2.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 436 IRILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:COG3621     7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 516 TVKM-SWSHAFYDSHTWEKILKDKVGSALMIEtARDPLCpkVAAVStIVNRgqtpKAFVFRNYGHFPGTNSHylggcqYK 594
Cdd:COG3621    86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGD-LKTPVL--IPSYD-LDNG----KPVFFKSPHAKFDRDRD------FL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 595 MWQAIRASSAAPGYFAEYALGND-----LHQDGGLLLNNPSALALHECKcIWPDTPLE--CIVSLGTGryesdvRNTTTY 667
Cdd:COG3621   152 LVDVARATSAAPTYFPPAQIKNLtgegyALIDGGVFANNPALCALAEAL-KLLGPDLDdiLVLSLGTG------TAPRSI 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859677021 668 TSLKTK----------LSNVISSATdTEEVHIMLDGLLPaDTYFRFNPVICENIPLDESrNEKLDQLQLEGMKYL 732
Cdd:COG3621   225 PYKKVKnwgalgwllpLIDILMDAQ-SDAVDYQLRQLLG-DRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
436-732 1.43e-46

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: 168.25  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 436 IRILAIDGGGTRGVVALQTLRKLVELTQ---------KPiHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSD 506
Cdd:cd07216     1 LNLLSLDGGGVRGLSSLLILKEIMERIDpkegldeppKP-CDYFDLIGGTSTGGLIAIMLGRLRMTVDECIDAYTRLAKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 507 VFTQ---NVIVGtvkMSWSHAFYDSHTWEKILKDKVG------SALMIEtaRDPLCPKVAAVSTivNRGQTPKAFVFRNY 577
Cdd:cd07216    80 IFSRkrlRLIIG---DLRTGARFDSKKLAEAIKVILKelgndeDDLLDE--GEEDGCKVFVCAT--DKDVTGKAVRLRSY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 578 GHFPGTNSHYlggcQYKMWQAIRASSAAPGYFAEYALGNDLHQ--DGGLLLNNPSALALHECKCIWPD--TPLECIVSLG 653
Cdd:cd07216   153 PSKDEPSLYK----NATIWEAARATSAAPTFFDPVKIGPGGRTfvDGGLGANNPIREVWSEAVSLWEGlaRLVGCLVSIG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 654 TG-RYESDVRNTTTYTSLKTKLsnvISSATDTEEVHIM----LDGLLPADTYFRFN-PVICENIPLDEsrNEKLDQLQLE 727
Cdd:cd07216   229 TGtPSIKSLGRSAEGAGLLKGL---KDLVTDTEAEAKRfsaeHSELDEEGRYFRFNvPHGLEDVGLDE--YEKMEEIVSL 303

                  ....*
gi 1859677021 728 GMKYL 732
Cdd:cd07216   304 TREYL 308
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
438-735 5.72e-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: 129.76  E-value: 5.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 438 ILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAfmLGLFH-MPLDECEELYRKLGSDVFtqnviVGT 516
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILA--LALLHgKSLREARRLYLRMKDRVF-----DGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 517 VKmswshafYDSHTWEKILKDKVGS-ALMIETARdplcPKVAAVSTIVNRgQTPKAFVFRNYG------HFPGTNSH--Y 587
Cdd:cd07212    74 RP-------YNSEPLEEFLKREFGEdTKMTDVKY----PRLMVTGVLADR-QPVQLHLFRNYDppedveEPEKNANFlpP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 588 LGGCQYKMWQAIRASSAAPGYFAeyALGNDLhqDGGLLLNNPSALAL---HECKCIW-------PDTPLECIVSLGTGRY 657
Cdd:cd07212   142 TDPAEQLLWRAARSSGAAPTYFR--PMGRFL--DGGLIANNPTLDAMteiHEYNKTLkskgrknKVKKIGCVVSLGTGII 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 658 ES------DV-RNTTTYTSLKTKL--SN----VISSATDTEEVHI--------MLDglLPadtYFRFNPVICENIPLDES 716
Cdd:cd07212   218 PQtpvntvDVfRPSNPWELAKTVFgaKNlgkmVVDQCTASDGAPVdrarawceSIG--IP---YFRFSPPLSKDIMLDET 292
                         330
                  ....*....|....*....
gi 1859677021 717 RNEKLDQLQLEGMKYLERN 735
Cdd:cd07212   293 DDEDLVNMLWDTEVYIYTH 311
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
437-722 8.76e-29

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 117.60  E-value: 8.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 437 RILAIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFTQNVIVG 515
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 516 TVKMSWSHAFYDSHTWEKILKDKVGSALmIETARDPLCpkVAAVStiVNRGQtPKAFVFRNYGHFpgTNSHylggcQYKM 595
Cdd:NF041079   80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVL--IPAVN--YTTGK-PQVFKTPHHPDF--TRDH-----KLKL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 596 WQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHECKCIwPDTPLE--CIVSLGTGryesdvrnTTTYT---SL 670
Cdd:NF041079  147 VDVALATSAAPTYFPLHEFDNEQFVDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSL 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859677021 671 KTKLS--------NVISSATDTEE--VHIMLDGLLPaDTYFRfnpvICENIPLDESRNEKLD 722
Cdd:NF041079  218 KRKRGfldwgggkRLFELTMSAQEqlVDFMLQHILG-DRYLR----IDDVPTNEQAKDLGLD 274
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
439-629 1.34e-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: 110.39  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGVVALQTLRKLVELTQKpihqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVF---TQNV 512
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIrkrALSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 513 IVGTVKMSWSHAFYDSHTWEKILKDKVGSALMIETARDPLCPKVAAVSTIVNRGQTPKAFVFRNYGHFPGTNSHYLggcq 592
Cdd:pfam01734  76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDL---- 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1859677021 593 ykmWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNP 629
Cdd:pfam01734 152 ---ADAVLASSALPGVFPPVRLDGELYVDGGLVDNVP 185
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
437-746 3.11e-26

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: 110.19  E-value: 3.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 437 RILAIDGGGTRGVVALQTLR----KLVELTQKP---IHQLFDYICGVSTGAIL-AFML-----GLFHMPLDECEELYRKL 503
Cdd:cd07215     1 RILSIDGGGIRGIIPATILVsveeKLQKKTGNPearLADYFDLVAGTSTGGILtCLYLcpnesGRPKFSAKEALNFYLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 504 GSDVFTQNvIVGTVKMSW--SHAFYDSHTWEKILKDKVGSALMIETARDPLcpkvaAVSTIVNRGqtpKAFVFRNygHFP 581
Cdd:cd07215    81 GNYIFKKK-IWNKIKSRGgfLNEKYSHKPLEEVLLEYFGDTKLSELLKPCL-----ITSYDIERR---SPHFFKS--HTA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 582 GTNSHYlggcQYKMWQAIRASSAAPGYFAEYALGNDLHQ-----DGGLLLNNPSALALHECKCIWPDTPlEC-------I 649
Cdd:cd07215   150 IKNEQR----DFYVRDVARATSAAPTYFEPARIHSLTGEkytliDGGVFANNPTLCAYAEARKLKFEQP-GKptakdmiI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 650 VSLGTGR----YE-SDVRNTTTYTSLKTKLSNVISSATDTEEVHI--MLDGLLPADTYFRFNPVICENIP-LDESRNEKL 721
Cdd:cd07215   225 LSLGTGKnkksYTyEKVKDWGLLGWAKPLIDIMMDGASQTVDYQLkqIFDAEGDQQQYLRIQPELEDADPeMDDASPENL 304
                         330       340
                  ....*....|....*....|....*
gi 1859677021 722 DQLQLEGMKYLERNDEKMKKLAKIL 746
Cdd:cd07215   305 EKLREVGQALAEDHKDQLDEIVDRL 329
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
437-725 6.07e-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: 96.59  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 437 RILAIDGGGTRGVVALQTLRKLVELTQKPIHQLfDYICGVSTGAILAFMLGLFhMPLDECEELYRKLGSDVFtQNVIVGT 516
Cdd:cd07213     3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQI-DLFAGTSAGSLIALGLALG-YSPRQVLKLYEEVGLKVF-SKSSAGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 517 VKMSWShafYDSHTWEKILKDKVGSALMIETARDPLCpkVAAV---STIVNRGQTPKAFVFRNyghFPGTNSHylggcQY 593
Cdd:cd07213    80 GAGNNQ---YFAAGFLKAFAEVFFGDLTLGDLKRKVL--VPSFqldSGKDDPNRRWKPKLFHN---FPGEPDL-----DE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 594 KMWQAIRASSAAPGYFAEYalgnDLHQDGGLLLNNPSALAL-HECKCIWPDTPLECIV--SLGTGRYESDVRNTTTYT-- 668
Cdd:cd07213   147 LLVDVCLRSSAAPTYFPSY----QGYVDGGVFANNPSLCAIaQAIGEEGLNIDLKDIVvlSLGTGRPPSYLDGANGYGdw 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1859677021 669 -SLK-----TKLSNVISSATDTEEVHIMLdgllpADTYFRFNPVICENIPLDESRN-EKLDQLQ 725
Cdd:cd07213   223 gLLQwlpdlLDLFMDAGVDAADFQCRQLL-----GERYFRLDPVLPANIDLDDNKQiEELVEIA 281
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
437-655 1.17e-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: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 437 RILAIDGGGTRGVVALQTLRKLVELTQK----PIHQL---FDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFT 509
Cdd:cd07217     2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIAL-GMSVTDLLSFYTLNGVNMFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 510 QNVIVGTVKMSWSHAFYDSHTWEKIL----------KDKVGSALMIETARD------PLCpkvaavstivnrgQTPKAFV 573
Cdd:cd07217    81 KAWLAQRLFLNKLYNQYDPTNLGKKLntvfpettlgDDTLRTLLMIVTRNAttgspwPVC-------------NNPEAKY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 574 FRNYGHFPgtNSHylggcqYKMWQAIRASSAAPGYF----------AEYALgndlhQDGGL-LLNNPSALALHECKCI-- 640
Cdd:cd07217   148 NDSDRSDC--NLD------LPLWQLVRASTAAPTFFppevvsiapgTAFVF-----VDGGVtTYNNPAFQAFLMATAKpy 214
                         250       260
                  ....*....|....*....|.
gi 1859677021 641 ---WP---DTPLecIVSLGTG 655
Cdd:cd07217   215 klnWEvgaDNLL--LVSVGTG 233
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
439-637 3.31e-15

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 76.48  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGVVALQTLRKLVELtqkPIHqlFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLG-SDVFTQNVIVGTV 517
Cdd:COG1752     9 LVLSGGGARGAAHIGVLKALEEA---GIP--PDVIAGTSAGAIVGALYAA-GYSADELEELWRSLDrRDLFDLSLPRRLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 518 KMSWSH---AFYDSHTWEKILKDKVGSALMietarDPLCPKVAAVSTIVNRGqtpKAFVFRnyghfpgtnshylggcQYK 594
Cdd:COG1752    83 RLDLGLspgGLLDGDPLRRLLERLLGDRDF-----EDLPIPLAVVATDLETG---REVVFD----------------SGP 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1859677021 595 MWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALHEC 637
Cdd:COG1752   139 LADAVRASAAIPGVFPPVEIDGRLYVDGGVVNNLPVDPARALG 181
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
433-655 2.68e-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: 62.84  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 433 GRGIRILAIDGGGTRGVVALQTLRKLVELTQK------PIHQLFDYICGVSTGAILAFMLGL---FHMPLDECEEL---Y 500
Cdd:cd07214     1 GKFITVLSIDGGGIRGIIPATILEFLEGKLQEldgpdaRIADYFDVIAGTSTGGLITAMLTApneNKRPLFAAKDIvqfY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 501 RKLGSDVFTQN--VIVGTVKMSWSHAF--YDSHTWEKILKDKVGSALMietaRDPLCPKVaaVSTIVNRGQTPKAFVFRN 576
Cdd:cd07214    81 LENGPKIFPQStgQFEDDRKKLRSLLGpkYDGVYLHDLLNELLGDTRL----SDTLTNVV--IPTFDIKLLQPVIFSSSK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 577 YGHFPGTNSHYLGGCqykmwqaiRASSAAPGYFAEYAL-----GNDLHQ----DGGLLLNNPSALALHE--------CKC 639
Cdd:cd07214   155 AKNDKLTNARLADVC--------ISTSAAPTYFPAHYFttedsNGDIREfnlvDGGVAANNPTLLAISEvtkeiikdNPF 226
                         250       260
                  ....*....|....*....|
gi 1859677021 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; ...
439-633 3.00e-10

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: 59.87  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGVVALQTLRKLVELTQKPihqlfDYICGVSTGAILAFMLGlFHMPLDECEELYRKLGSDVFTQNVI-VGTV 517
Cdd:cd07205     3 LALSGGGARGLAHIGVLKALEEAGIPI-----DIVSGTSAGAIVGALYA-AGYSPEEIEERAKLRSTDLKALSDLtIPTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 518 KMSwSHAFYDSHTWEkILKDKvgsalMIETARDPLcpkvAAVSTIVNRGQTpkaFVFRNyghfpgtnshylgGCqykMWQ 597
Cdd:cd07205    77 GLL-RGDKFLELLDE-YFGDR-----DIEDLWIPF----FIVATDLTSGKL---VVFRS-------------GS---LVR 126
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1859677021 598 AIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALA 633
Cdd:cd07205   127 AVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVDVL 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 4.63e-08

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 53.82  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGVV---ALQtlrklvELTQKPIhqLFDYICGVSTGAILAFMLGL---------FHMPLDECEELYRKLGSD 506
Cdd:cd07207     2 LVFEGGGAKGIAyigALK------ALEEAGI--LKKRVAGTSAGAITAALLALgysaadikdILKETDFAKLLDSPVGLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 507 VFTQNVIVGtvkMSWS--HAFYDshtW-EKILKDKVGSALMIETARDPLCP---KVAAVSTIVNRGqtpKAFVFrnYG-H 579
Cdd:cd07207    74 FLLPSLFKE---GGLYkgDALEE---WlRELLKEKTGNSFATSLLRDLDDDlgkDLKVVATDLTTG---ALVVF--SAeT 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1859677021 580 FPgtnshylggcQYKMWQAIRASSAAPGYFA--EYALGnDLHQDGGLLLNNP 629
Cdd:cd07207   143 TP----------DMPVAKAVRASMSIPFVFKpvRLAKG-DVYVDGGVLDNYP 183
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
439-635 7.80e-08

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 53.45  E-value: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGvvALQ--TLRKLVELTQKPihqlfDYICGVSTGAILAFMLGLF-HMPLDECEELYRKLG-SDVFTQnviv 514
Cdd:cd07209     1 LVLSGGGALG--AYQagVLKALAEAGIEP-----DIISGTSIGAINGALIAGGdPEAVERLEKLWRELSrEDVFLR---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 515 gtvkmswshAFYDSHTWEKILKDkvgsalmietaRDPLCPKVAAVSTIVNRGQtpkafvfrnyghfpgtnSHYLGGC-QY 593
Cdd:cd07209    70 ---------GLLDRALDFDTLRL-----------LAILFAGLVIVAVNVLTGE-----------------PVYFDDIpDG 112
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1859677021 594 KMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALALH 635
Cdd:cd07209   113 ILPEHLLASAALPPFFPPVEIDGRYYWDGGVVDNTPLSPAID 154
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
439-634 2.24e-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: 45.73  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRGVVALQTLRKLVElTQKPIhqlfDYICGVSTGAILAFMLGLFHmpLDECEELYRKLgsdvfTQNVIVGTVK 518
Cdd:cd07228     3 LALGSGGARGWAHIGVLRALEE-EGIEI----DIIAGSSIGALVGALYAAGH--LDALEEWVRSL-----SQRDVLRLLD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 519 MSWSHA-FYDSHTWEKILKDKVGsALMIETARDPLCpkvaAVSTIVNRGqtpKAFVFRNyghfpgtnshylgGCqykMWQ 597
Cdd:cd07228    71 LSASRSgLLKGEKVLEYLREIMG-GVTIEELPIPFA----AVATDLQTG---KEVWFRE-------------GS---LID 126
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1859677021 598 AIRASSAAPGYFAEYALGNDLHQDGGLLlnNPSALAL 634
Cdd:cd07228   127 AIRASISIPGIFAPVEHNGRLLVDGGVV--NPIPVSV 161
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
439-629 3.15e-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: 45.02  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 439 LAIDGGGTRG---VVALQTLRKlveltqkpiHQ-LFDYICGVSTGAILAFMLgLFHMPLDECE--ELYRKLGSDVFTQNV 512
Cdd:cd07198     1 LVLSGGGALGiyhVGVAKALRE---------RGpLIDIIAGTSAGAIVAALL-ASGRDLEEALllLLRLSREVRLRFDGA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859677021 513 IVGTVKMSwshafydSHTWEKILKDKVGSAlmIETARDPLCPKVAAVSTIVNRgqtpkafvfrnyghfpgtnSHYLGGCQ 592
Cdd:cd07198    71 FPPTGRLL-------GILRQPLLSALPDDA--HEDASGKLFISLTRLTDGENV-------------------LVSDTSKG 122
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1859677021 593 YkMWQAIRASSAAPGYFA--EYALGNDLHQDGGLLLNNP 629
Cdd:cd07198   123 E-LWSAVRASSSIPGYFGpvPLSFRGRRYGDGGLSNNLP 160
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
439-483 7.68e-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: 40.86  E-value: 7.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1859677021 439 LAIDGGGTRGVVALQTLRKLVELTqkpIHQLFDYICGVSTGAILA 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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