NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1834424867|gb|QJD30868|]
View 

patatin family protein [Methylococcus geothermalis]

Protein Classification

patatin-like phospholipase family protein( domain architecture ID 11448329)

patatin-like phospholipase family protein may catalyze the hydrolysis of lipids/phospholipids

CATH:  3.40.1090.10
EC:  3.1.1.-
Gene Ontology:  GO:0052689
PubMed:  11080672
SCOP:  3001121

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 15-341 3.28e-23

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 99.21  E-value: 3.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  15 KLGLALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDglkpssqayvvivqEIE 94
Cdd:COG1752     6 KIGLVLSGGGARG-AAHIGVLKALEEAGI--PPDVIAGTSAGAIVGALYAA-------GYSAD--------------ELE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  95 REFVKGVQNNLRMRALSDPLKNARMMLSDD-YSRSDRMAELYEEYFyrkiwhemesddqGSIRLKDIKITpagykvpfnv 173
Cdd:COG1752    62 ELWRSLDRRDLFDLSLPRRLLRLDLGLSPGgLLDGDPLRRLLERLL-------------GDRDFEDLPIP---------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 174 reynkeetiykvpiLAINATILNTGESWLFtasyigSSGDkednsalpysklrfgdaalppkvrakldtinLADAVAASA 253
Cdd:COG1752   119 --------------LAVVATDLETGREVVF------DSGP-------------------------------LADAVRASA 147

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 254 CVPVLLSPFAIHDLYqedgkevvveLVDGGVYDNQGLETLFREECTHIICSDASGQLqsDRTPNssASSVGARSNEILMK 333
Cdd:COG1752   148 AIPGVFPPVEIDGRL----------YVDGGVVNNLPVDPARALGADRVIAVDLNPPL--RKLPS--LLDILGRALEIMFN 213


                  ....*...
gi 1834424867 334 RVREETLD 341
Cdd:COG1752   214 SILRRELA 221
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 15-341 3.28e-23

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 99.21  E-value: 3.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  15 KLGLALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDglkpssqayvvivqEIE 94
Cdd:COG1752     6 KIGLVLSGGGARG-AAHIGVLKALEEAGI--PPDVIAGTSAGAIVGALYAA-------GYSAD--------------ELE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  95 REFVKGVQNNLRMRALSDPLKNARMMLSDD-YSRSDRMAELYEEYFyrkiwhemesddqGSIRLKDIKITpagykvpfnv 173
Cdd:COG1752    62 ELWRSLDRRDLFDLSLPRRLLRLDLGLSPGgLLDGDPLRRLLERLL-------------GDRDFEDLPIP---------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 174 reynkeetiykvpiLAINATILNTGESWLFtasyigSSGDkednsalpysklrfgdaalppkvrakldtinLADAVAASA 253
Cdd:COG1752   119 --------------LAVVATDLETGREVVF------DSGP-------------------------------LADAVRASA 147

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 254 CVPVLLSPFAIHDLYqedgkevvveLVDGGVYDNQGLETLFREECTHIICSDASGQLqsDRTPNssASSVGARSNEILMK 333
Cdd:COG1752   148 AIPGVFPPVEIDGRL----------YVDGGVVNNLPVDPARALGADRVIAVDLNPPL--RKLPS--LLDILGRALEIMFN 213


                  ....*...
gi 1834424867 334 RVREETLD 341
Cdd:COG1752   214 SILRRELA 221
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 16-305 8.00e-12

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: 64.10  E-value: 8.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  16 LGLALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDglkpssqayvvivqEIER 95
Cdd:cd07205     1 IGLALSGGGARG-LAHIGVLKALEEAGI--PIDIVSGTSAGAIVGALYAA-------GYSPE--------------EIEE 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  96 EFVKgvqNNLRMRALSD---PLKNarmmlsddYSRSDRMAELYEEYFyrkiwhemesddqGSIRLKDIKItpagykvPFn 172
Cdd:cd07205    57 RAKL---RSTDLKALSDltiPTAG--------LLRGDKFLELLDEYF-------------GDRDIEDLWI-------PF- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 173 vreynkeetiykvpilAINATILNTGESWLFTasyigsSGDkednsalpysklrfgdaalppkvrakldtinLADAVAAS 252
Cdd:cd07205   105 ----------------FIVATDLTSGKLVVFR------SGS-------------------------------LVRAVRAS 131

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1834424867 253 ACVPVLLSPFAIhdlyqeDGKevvvELVDGGVYDNQGLETLFREECTHIICSD 305
Cdd:cd07205   132 MSIPGIFPPVKI------DGQ----LLVDGGVLNNLPVDVLRELGADIIIAVD 174
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 18-287 6.92e-10

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: 58.77  E-value: 6.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  18 LALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDGlkpssqayvvIVQEIEREF 97
Cdd:pfam01734   1 LVLSGGGARG-AYHLGVLKALGEAGI--RFDVISGTSAGAINAALLAL-------GRDPEE----------IEDLLLELD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  98 VKGVQNNLRMRALSDPLKNARMMLSDDYSRSDRMAELYEEYFYRKiwhemesddqgsirlkdikitpagyKVPFNVREYN 177
Cdd:pfam01734  61 LNLFLSLIRKRALSLLALLRGLIGEGGLFDGDALRELLRKLLGDL-------------------------TLEELAARLS 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 178 KEETIYKVPILAINATILNTGESWLFTASyigssgdkednsalpysklrfgdaalppkvraKLDTINLADAVAASACVPV 257
Cdd:pfam01734 116 LLLVVALRALLTVISTALGTRARILLPDD--------------------------------LDDDEDLADAVLASSALPG 163

                         250       260       270
                  ....*....|....*....|....*....|
gi 1834424867 258 LLSPFAIhdlyqeDGKevvvELVDGGVYDN 287
Cdd:pfam01734 164 VFPPVRL------DGE----LYVDGGLVDN 183
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 15-341 3.28e-23

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 99.21  E-value: 3.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  15 KLGLALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDglkpssqayvvivqEIE 94
Cdd:COG1752     6 KIGLVLSGGGARG-AAHIGVLKALEEAGI--PPDVIAGTSAGAIVGALYAA-------GYSAD--------------ELE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  95 REFVKGVQNNLRMRALSDPLKNARMMLSDD-YSRSDRMAELYEEYFyrkiwhemesddqGSIRLKDIKITpagykvpfnv 173
Cdd:COG1752    62 ELWRSLDRRDLFDLSLPRRLLRLDLGLSPGgLLDGDPLRRLLERLL-------------GDRDFEDLPIP---------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 174 reynkeetiykvpiLAINATILNTGESWLFtasyigSSGDkednsalpysklrfgdaalppkvrakldtinLADAVAASA 253
Cdd:COG1752   119 --------------LAVVATDLETGREVVF------DSGP-------------------------------LADAVRASA 147

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 254 CVPVLLSPFAIHDLYqedgkevvveLVDGGVYDNQGLETLFREECTHIICSDASGQLqsDRTPNssASSVGARSNEILMK 333
Cdd:COG1752   148 AIPGVFPPVEIDGRL----------YVDGGVVNNLPVDPARALGADRVIAVDLNPPL--RKLPS--LLDILGRALEIMFN 213


                  ....*...
gi 1834424867 334 RVREETLD 341
Cdd:COG1752   214 SILRRELA 221
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 16-305 8.00e-12

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: 64.10  E-value: 8.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  16 LGLALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDglkpssqayvvivqEIER 95
Cdd:cd07205     1 IGLALSGGGARG-LAHIGVLKALEEAGI--PIDIVSGTSAGAIVGALYAA-------GYSPE--------------EIEE 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  96 EFVKgvqNNLRMRALSD---PLKNarmmlsddYSRSDRMAELYEEYFyrkiwhemesddqGSIRLKDIKItpagykvPFn 172
Cdd:cd07205    57 RAKL---RSTDLKALSDltiPTAG--------LLRGDKFLELLDEYF-------------GDRDIEDLWI-------PF- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 173 vreynkeetiykvpilAINATILNTGESWLFTasyigsSGDkednsalpysklrfgdaalppkvrakldtinLADAVAAS 252
Cdd:cd07205   105 ----------------FIVATDLTSGKLVVFR------SGS-------------------------------LVRAVRAS 131

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1834424867 253 ACVPVLLSPFAIhdlyqeDGKevvvELVDGGVYDNQGLETLFREECTHIICSD 305
Cdd:cd07205   132 MSIPGIFPPVKI------DGQ----LLVDGGVLNNLPVDVLRELGADIIIAVD 174
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 18-287 6.92e-10

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: 58.77  E-value: 6.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  18 LALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALYYLkvkqlleGRRPDGlkpssqayvvIVQEIEREF 97
Cdd:pfam01734   1 LVLSGGGARG-AYHLGVLKALGEAGI--RFDVISGTSAGAINAALLAL-------GRDPEE----------IEDLLLELD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  98 VKGVQNNLRMRALSDPLKNARMMLSDDYSRSDRMAELYEEYFYRKiwhemesddqgsirlkdikitpagyKVPFNVREYN 177
Cdd:pfam01734  61 LNLFLSLIRKRALSLLALLRGLIGEGGLFDGDALRELLRKLLGDL-------------------------TLEELAARLS 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867 178 KEETIYKVPILAINATILNTGESWLFTASyigssgdkednsalpysklrfgdaalppkvraKLDTINLADAVAASACVPV 257
Cdd:pfam01734 116 LLLVVALRALLTVISTALGTRARILLPDD--------------------------------LDDDEDLADAVLASSALPG 163

                         250       260       270
                  ....*....|....*....|....*....|
gi 1834424867 258 LLSPFAIhdlyqeDGKevvvELVDGGVYDN 287
Cdd:pfam01734 164 VFPPVRL------DGE----LYVDGGLVDN 183
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 18-64 1.51e-09

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: 57.04  E-value: 1.51e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1834424867  18 LALSGGGFRAsLFHIGVLARLAELDLLRQVEVLSTVSGGSIVGALYY 64
Cdd:cd01819     1 LSFSGGGFRG-MYHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY 46
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 18-62 3.75e-05

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 46.05  E-value: 3.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1834424867  18 LALSGGGFRAsLFHIGVLARLAELDLLRQveVLSTVSGGSIVGAL 62
Cdd:cd07206    72 LMLSGGASLG-LFHLGVVKALWEQDLLPR--VISGSSAGAIVAAL 113
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 18-63 5.82e-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: 43.87  E-value: 5.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1834424867  18 LALSGGGFRAsLFHIGVLARLAELDLLrqVEVLSTVSGGSIVGALY 63
Cdd:cd07198     1 LVLSGGGALG-IYHVGVAKALRERGPL--IDIIAGTSAGAIVAALL 43
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 18-61 4.46e-04

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


Pssm-ID: 132868  Cd Length: 421  Bit Score: 42.98  E-value: 4.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1834424867  18 LALSGGG-FraSLFHIGVLARLAELDLLRQveVLSTVSGGSIVGA 61
Cdd:cd07230    76 LLLSGGGtF--GMFHIGVLKALFEANLLPR--IISGSSAGSIVAA 116
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 18-110 1.21e-03

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: 41.12  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834424867  18 LALSGGGFRaSLFHIGVLARLAEL--DLLRQVEVLSTVSGGSIVG---ALYY--LKVKQLLEGRRPDGLKPSSQAYVV-I 89
Cdd:cd07213     5 LSLDGGGVK-GIVQLVLLKRLAEEfpSFLDQIDLFAGTSAGSLIAlglALGYspRQVLKLYEEVGLKVFSKSSAGGGAgN 83

                          90       100
                  ....*....|....*....|....*
gi 1834424867  90 VQEIEREFVKGVQN----NLRMRAL 110
Cdd:cd07213    84 NQYFAAGFLKAFAEvffgDLTLGDL 108
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 17-62 1.43e-03

Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. 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 been found also in vertebrates.


Pssm-ID: 132870  Cd Length: 407  Bit Score: 41.10  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1834424867  17 GLALSGGGFRAsLFHIGVLARLAELDLLRQveVLSTVSGGSIVGAL 62
Cdd:cd07232    69 ALCLSGGAAFA-YYHFGVVKALLDADLLPN--VISGTSGGSLVAAL 111
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 16-63 1.55e-03

Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. 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: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 40.41  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1834424867  16 LGLALSGGGFRAsLFHIGVLARLAELDLlrQVEVLSTVSGGSIVGALY 63
Cdd:cd07210     1 FALVLSSGFFGF-YAHLGFLAALLEMGL--EPSAISGTSAGALVGGLF 45
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
 16-63 3.60e-03

Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; 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. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 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). Calcium is required for cPLA2 to bind with membranes or phospholipids. Group IV cPLA2 includes six intercellular enzymes: cPLA2alpha, cPLA2beta, cPLA2gamma, cPLA2delta, cPLA2epsilon, and cPLA2zeta.


Pssm-ID: 132835 [Multi-domain]  Cd Length: 438  Bit Score: 39.92  E-value: 3.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1834424867  16 LGLALSGGGFRASLFHIGVLARLAELDLLRQVEVLSTVSGGS-IVGALY 63
Cdd:cd00147    44 IAILGSGGGYRAMTGGAGALKALDEGGLLDCVTYLSGLSGSTwLMASLY 92
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 17-63 5.97e-03

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


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 38.02  E-value: 5.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1834424867  17 GLALSGGGFRAsLFHIGVLARLAEldllRQVEVlSTVSG---GSIVGALY 63
Cdd:cd07228     2 GLALGSGGARG-WAHIGVLRALEE----EGIEI-DIIAGssiGALVGALY 45
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH