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Conserved domains on  [gi|1419145599|ref|XP_025485518|]
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hypothetical protein BO82DRAFT_437453 [Aspergillus uvarum CBS 121591]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 27818)

patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 109-182 1.77e-22

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.


The actual alignment was detected with superfamily member cd07199:

Pssm-ID: 416256 [Multi-domain]  Cd Length: 258  Bit Score: 93.94  E-value: 1.77e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEHLGPKCGVADVIDLTVGPSAGGLISMGLIAMDWPVSTCSEVFDRLAQRIFR 182
Cdd:cd07199     1 ILSLDGGGIRGIIPAEILAELEKRLGKPSRIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP 74
 
Name Accession Description Interval E-value
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 109-182 1.77e-22

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: 93.94  E-value: 1.77e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEHLGPKCGVADVIDLTVGPSAGGLISMGLIAMDWPVSTCSEVFDRLAQRIFR 182
Cdd:cd07199     1 ILSLDGGGIRGIIPAEILAELEKRLGKPSRIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP 74
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 110-279 8.80e-07

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: 48.37  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 110 LAIDGGGVRGGIPLEFLlliqEHLGPKCGVADVIdltVGPSAGGLISMGLIAMDWPVSTCSEVFDRLAQRIFRERRQPAL 189
Cdd:pfam01734   1 LVLSGGGARGAYHLGVL----KALGEAGIRFDVI---SGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 190 NRalqlvlgrgsfleiIPKWVSWIMRDSCYDAAIFDATLQEVFGRTRRAFQPLGQGSPLHSYSKSKFAAIATSIGKDTKS 269
Cdd:pfam01734  74 SL--------------LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARI 139

                         170
                  ....*....|
gi 1419145599 270 FVFGNFNPVE 279
Cdd:pfam01734 140 LLPDDLDDDE 149
 
Name Accession Description Interval E-value
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 109-182 1.77e-22

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: 93.94  E-value: 1.77e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEHLGPKCGVADVIDLTVGPSAGGLISMGLIAMDWPVSTCSEVFDRLAQRIFR 182
Cdd:cd07199     1 ILSLDGGGIRGIIPAEILAELEKRLGKPSRIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP 74
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 109-278 4.28e-13

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: 68.44  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEHLG-PKCGVADVIdltVGPSAGGLISMGLIAMDWPVSTCSEVFDRLAQRIFrerrqp 187
Cdd:cd07211    10 ILSIDGGGTRGVVALEILRKIEKLTGkPIHELFDYI---CGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF------ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 188 alNRALQLVlgrGSFleiipkWVSWimRDSCYDAAIFDATLQEVFGRTRRAFQPLGQGSPlhsysksKFAAIATSIGKDT 267
Cdd:cd07211    81 --SQNTYIS---GTS------RLVL--SHAYYDTETWEKILKEMMGSDELIDTSADPNCP-------KVACVSTQVNRTP 140

                         170
                  ....*....|..
gi 1419145599 268 -KSFVFGNFNPV 278
Cdd:cd07211   141 lKPYVFRNYNHP 152
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 109-280 4.54e-11

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: 62.32  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 109 ILAIDGGGVRGgipLEFLLLIQE---HLGPKCGVA------DVIDLTVGPSAGGLIS--MGLIAMDwpVSTCSEVFDRLA 177
Cdd:cd07216     3 LLSLDGGGVRG---LSSLLILKEimeRIDPKEGLDeppkpcDYFDLIGGTSTGGLIAimLGRLRMT--VDECIDAYTRLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 178 QRIFRERR---------------QPALNRALQLVLGRGSFLEIIPKWvsWIMRDSCydAAIFDATLQEVFGRTR--RAFQ 240
Cdd:cd07216    78 KKIFSRKRlrliigdlrtgarfdSKKLAEAIKVILKELGNDEDDLLD--EGEEDGC--KVFVCATDKDVTGKAVrlRSYP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1419145599 241 PlGQGSPLhsYSKSKF--AAIATS----------IGKDTKSFV---FGNFNPVEW 280
Cdd:cd07216   154 S-KDEPSL--YKNATIweAARATSaaptffdpvkIGPGGRTFVdggLGANNPIRE 205
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 109-236 2.26e-08

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: 54.33  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEHL-----GPKCGVADVIDLTVGPSAGGLIsmgliamdwpvsTCSEVFDRLAQRIFRE 183
Cdd:cd07215     2 ILSIDGGGIRGIIPATILVSVEEKLqkktgNPEARLADYFDLVAGTSTGGIL------------TCLYLCPNESGRPKFS 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1419145599 184 RRQpalnrALQLVLGRGSFLEIIPKWVSWIMR----DSCYDAAIFDATLQEVFGRTR 236
Cdd:cd07215    70 AKE-----ALNFYLERGNYIFKKKIWNKIKSRggflNEKYSHKPLEEVLLEYFGDTK 121
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 108-163 3.23e-07

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: 50.90  E-value: 3.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 108 SILAIDGGGVRGGIP---LEFL-LLIQEHLGPKCGVADVIDLTVGPSAGGLISMGLIAMD 163
Cdd:cd07214     5 TVLSIDGGGIRGIIPatiLEFLeGKLQELDGPDARIADYFDVIAGTSTGGLITAMLTAPN 64
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 110-279 8.80e-07

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: 48.37  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 110 LAIDGGGVRGGIPLEFLlliqEHLGPKCGVADVIdltVGPSAGGLISMGLIAMDWPVSTCSEVFDRLAQRIFRERRQPAL 189
Cdd:pfam01734   1 LVLSGGGARGAYHLGVL----KALGEAGIRFDVI---SGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 190 NRalqlvlgrgsfleiIPKWVSWIMRDSCYDAAIFDATLQEVFGRTRRAFQPLGQGSPLHSYSKSKFAAIATSIGKDTKS 269
Cdd:pfam01734  74 SL--------------LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARI 139

                         170
                  ....*....|
gi 1419145599 270 FVFGNFNPVE 279
Cdd:pfam01734 140 LLPDDLDDDE 149
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 109-181 1.55e-06

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes 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: 49.03  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 109 ILAIDGGGVRGGIPLEFLL----LIQEHL-GPKCGVADVIDLTVGPSAGGLISMGLIA-------MDWPVSTCSEVFDR- 175
Cdd:cd07217     3 ILALDGGGIRGLLSVEILGriekDLRTHLdDPEFRLGDYFDFVGGTSTGSIIAACIALgmsvtdlLSFYTLNGVNMFDKa 82


                  ....*..
gi 1419145599 176 -LAQRIF 181
Cdd:cd07217    83 wLAQRLF 89
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 109-185 1.84e-05

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: 45.40  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEHLGPKCgvADVIDLTVGPSAGGLISMGLiAMDWPVSTCSEVFDRLAQRIFRERR 185
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPI--RELFDWIAGTSTGGILALAL-LHGKSLREARRLYLRMKDRVFDGSR 74
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 109-195 2.33e-04

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: 41.89  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419145599 109 ILAIDGGGVRGGIPLEFLLLIQEhLGPkcGVADVIDLTVGPSAGGLISMGLiAMDWPVSTCSEVFDRLAQRIFRERRQPA 188
Cdd:cd07213     4 ILSLDGGGVKGIVQLVLLKRLAE-EFP--SFLDQIDLFAGTSAGSLIALGL-ALGYSPRQVLKLYEEVGLKVFSKSSAGG 79


                  ....*..
gi 1419145599 189 LNRALQL 195
Cdd:cd07213    80 GAGNNQY 86
 
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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